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Database: PDB
Entry: 1C3O
LinkDB: 1C3O
Original site: 1C3O 
HEADER    LIGASE                                  28-JUL-99   1C3O              
TITLE     CRYSTAL STRUCTURE OF THE CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT
TITLE    2 MUTANT C269S WITH BOUND GLUTAMINE                                    
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;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: BACTERIA;                                         
SOURCE   5 EXPRESSION_SYSTEM_COMMON: EUBACTERIA;                                
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 2;                                          
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 EXPRESSION_SYSTEM: BACTERIA;                                         
SOURCE  11 EXPRESSION_SYSTEM_COMMON: EUBACTERIA;                                
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 2                                           
KEYWDS    AMIDOTRANSFERASE, MICHAELIS COMPLEX, ATP-GRASP, LIGASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN                             
REVDAT   6   14-MAR-18 1C3O    1       SEQADV                                   
REVDAT   5   13-JUL-11 1C3O    1       VERSN                                    
REVDAT   4   24-FEB-09 1C3O    1       VERSN                                    
REVDAT   3   26-SEP-01 1C3O    1       SHEET                                    
REVDAT   2   05-MAY-00 1C3O    1       DBREF                                    
REVDAT   1   10-DEC-99 1C3O    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.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT 5E                                               
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 476527                         
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 49936                           
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1890                 
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) : 476527                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 44220                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 453                                     
REMARK   3   SOLVENT ATOMS            : 3666                                    
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) : 0.006 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.190 ; 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 1C3O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009423.                                   
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          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 476527                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28200                            
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   (%): 62.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, MANGANESE CHLORIDE,            
REMARK 280  TETRAETHYLAMMONIUM CHLORIDE, POTASSIUM CHLORIDE, BERYLLIUM          
REMARK 280  FLUORIDE, ADENOSINE 5'-DIPHOSPHATE,L-ORNITHINE, L-GLUTAMINE,        
REMARK 280  HEPPS, PH 7.4, BATCH, TEMPERATURE 278K                              
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       76.25000            
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       82.20000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      166.30000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       82.20000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 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   NE2  GLN C   812     O    HOH C  4684              2.06            
REMARK 500   O    HOH G  3580     O    HOH G  3644              2.14            
REMARK 500   OE1  GLU C   154     O    HOH C  4246              2.15            
REMARK 500   O    HOH E  4720     O    HOH E  4721              2.15            
REMARK 500   O    HOH C  4394     O    HOH C  4627              2.15            
REMARK 500   O    HOH C  4598     O    HOH C  4600              2.16            
REMARK 500   OD2  ASP C   133     O    HOH C  4117              2.17            
REMARK 500   O    HOH C  4578     O    HOH C  4579              2.18            
REMARK 500   OD2  ASP E    62     O    HOH E  4634              2.18            
REMARK 500   O    HOH A  4083     O    HOH A  4175              2.19            
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  39   CD    GLU A  39   OE2     0.068                       
REMARK 500    GLU A  72   CD    GLU A  72   OE2     0.067                       
REMARK 500    GLU A  81   CD    GLU A  81   OE2     0.069                       
REMARK 500    GLU A 109   CD    GLU A 109   OE2     0.097                       
REMARK 500    GLU A 110   CD    GLU A 110   OE2     0.085                       
REMARK 500    GLU A 153   CD    GLU A 153   OE2     0.074                       
REMARK 500    GLU A 186   CD    GLU A 186   OE2     0.094                       
REMARK 500    GLU A 190   CD    GLU A 190   OE2     0.066                       
REMARK 500    GLU A 208   CD    GLU A 208   OE2     0.067                       
REMARK 500    GLU A 217   CD    GLU A 217   OE2     0.080                       
REMARK 500    GLU A 299   CD    GLU A 299   OE2     0.067                       
REMARK 500    GLU A 365   CD    GLU A 365   OE2     0.069                       
REMARK 500    GLU A 478   CD    GLU A 478   OE2     0.069                       
REMARK 500    GLU A 512   CD    GLU A 512   OE2     0.077                       
REMARK 500    GLU A 535   CD    GLU A 535   OE2     0.073                       
REMARK 500    GLU A 560   CD    GLU A 560   OE2     0.071                       
REMARK 500    GLU A 591   CD    GLU A 591   OE2     0.077                       
REMARK 500    GLU A 604   CD    GLU A 604   OE2     0.079                       
REMARK 500    GLU A 624   CD    GLU A 624   OE1    -0.068                       
REMARK 500    GLU A 624   CD    GLU A 624   OE2     0.068                       
REMARK 500    GLU A 633   CD    GLU A 633   OE2     0.071                       
REMARK 500    GLU A 655   CD    GLU A 655   OE2     0.076                       
REMARK 500    GLU A 676   CD    GLU A 676   OE2     0.071                       
REMARK 500    GLU A 683   CD    GLU A 683   OE2     0.077                       
REMARK 500    GLU A 699   CD    GLU A 699   OE2     0.077                       
REMARK 500    GLU A 703   CD    GLU A 703   OE2     0.077                       
REMARK 500    GLU A 707   CD    GLU A 707   OE2     0.071                       
REMARK 500    GLU A 726   CD    GLU A 726   OE2     0.068                       
REMARK 500    GLU A 836   CD    GLU A 836   OE2     0.075                       
REMARK 500    GLU A 882   CD    GLU A 882   OE2     0.069                       
REMARK 500    GLU A 910   CD    GLU A 910   OE2     0.068                       
REMARK 500    GLU A 955   CD    GLU A 955   OE2     0.076                       
REMARK 500    GLU A1009   CD    GLU A1009   OE2     0.096                       
REMARK 500    GLU A1024   CD    GLU A1024   OE2     0.072                       
REMARK 500    GLU A1067   CD    GLU A1067   OE2     0.075                       
REMARK 500    GLU B  70   CD    GLU B  70   OE2     0.067                       
REMARK 500    GLU B 145   CD    GLU B 145   OE2     0.072                       
REMARK 500    GLU B 161   CD    GLU B 161   OE2     0.069                       
REMARK 500    GLU B 166   CD    GLU B 166   OE2     0.086                       
REMARK 500    GLU B 183   CD    GLU B 183   OE2     0.070                       
REMARK 500    GLU B 187   CD    GLU B 187   OE2     0.072                       
REMARK 500    GLU B 226   CD    GLU B 226   OE2     0.067                       
REMARK 500    GLU B 260   CD    GLU B 260   OE2     0.070                       
REMARK 500    GLU B 301   CD    GLU B 301   OE2     0.066                       
REMARK 500    GLU B 318   CD    GLU B 318   OE2     0.066                       
REMARK 500    GLU B 372   CD    GLU B 372   OE2     0.084                       
REMARK 500    GLU C  25   CD    GLU C  25   OE2     0.071                       
REMARK 500    GLU C  59   CD    GLU C  59   OE2     0.072                       
REMARK 500    GLU C 103   CD    GLU C 103   OE2     0.076                       
REMARK 500    GLU C 110   CD    GLU C 110   OE1    -0.115                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     188 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  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A  38   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A  38   NE  -  CZ  -  NH1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 185   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ASP A 197   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ASP A 226   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP A 246   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    MET A 300   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP A 333   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 333   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A 338   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 343   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 372   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP A 410   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 416   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 416   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A 459   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 490   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 499   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 509   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 514   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 514   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A 528   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP A 539   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 539   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ASP A 558   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 559   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG A 615   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 625   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 670   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG A 677   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 677   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    PRO A 716   N   -  CA  -  CB  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 736   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASP A 763   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 763   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 807   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     354 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     -150.95   -109.94                                   
REMARK 500    ASN A  48      116.14   -162.06                                   
REMARK 500    ALA A  52       31.67    -87.26                                   
REMARK 500    ARG A 303     -176.81   -179.08                                   
REMARK 500    ASP A 353       44.53   -105.55                                   
REMARK 500    THR A 375     -156.15   -141.99                                   
REMARK 500    ASP A 530       -1.54   -148.69                                   
REMARK 500    THR A 531       -7.64     72.57                                   
REMARK 500    ALA A 541       72.98   -116.54                                   
REMARK 500    GLU A 548     -157.37   -131.66                                   
REMARK 500    ASN A 554       58.34     39.75                                   
REMARK 500    ASP A 558      -89.94    -57.08                                   
REMARK 500    CYS A 601       23.01   -140.62                                   
REMARK 500    ILE A 698      -71.78    -46.69                                   
REMARK 500    ASP A 758       55.27     32.72                                   
REMARK 500    THR A 800      -13.57   -143.22                                   
REMARK 500    GLN A 821       33.36     72.86                                   
REMARK 500    ASN A 936       30.73     78.33                                   
REMARK 500    HIS A 975      -79.27    -25.15                                   
REMARK 500    SER B 239      177.18    -58.98                                   
REMARK 500    SER B 269     -100.62     53.12                                   
REMARK 500    ASN B 311       78.30   -171.40                                   
REMARK 500    ALA B 356     -123.81     43.75                                   
REMARK 500    SER B 357       70.76     57.26                                   
REMARK 500    PRO C   2     -157.51    -82.99                                   
REMARK 500    ALA C  23     -149.39   -110.53                                   
REMARK 500    ASN C  48      119.48   -161.66                                   
REMARK 500    ALA C  52       38.74    -85.96                                   
REMARK 500    ALA C 239     -178.84    -66.32                                   
REMARK 500    PRO C 302       43.25    -74.04                                   
REMARK 500    ASP C 338      -70.47    -41.18                                   
REMARK 500    THR C 340       40.58   -102.49                                   
REMARK 500    ASP C 353       41.74   -109.22                                   
REMARK 500    ASN C 363       37.89   -148.25                                   
REMARK 500    THR C 375     -159.82   -142.54                                   
REMARK 500    ASP C 459      130.10    -39.67                                   
REMARK 500    THR C 531       -7.76     70.56                                   
REMARK 500    ALA C 541       70.66   -115.13                                   
REMARK 500    GLU C 548     -156.72   -129.53                                   
REMARK 500    CYS C 601       28.99   -141.97                                   
REMARK 500    ILE C 698      -70.90    -51.90                                   
REMARK 500    GLN C 739      -83.69    -56.70                                   
REMARK 500    ALA C 798      150.05    -49.20                                   
REMARK 500    THR C 800      -33.28   -133.21                                   
REMARK 500    GLN C 821       47.62     74.15                                   
REMARK 500    PRO C 844       45.14    -71.48                                   
REMARK 500    SER C 873      152.54    -45.04                                   
REMARK 500    GLU C 951      -71.30    -30.12                                   
REMARK 500    HIS C 975      -72.78    -36.21                                   
REMARK 500    LYS C 993     -178.97    -59.51                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     129 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A4021   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  84   O                                                      
REMARK 620 2 THR A 114   OG1  75.0                                              
REMARK 620 3 HOH A4111   O   123.5  83.8                                        
REMARK 620 4 GLY A 112   O    73.4 101.1 163.1                                  
REMARK 620 5 HOH A4113   O   106.7 172.3  89.2  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4004   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 127   OE1                                                    
REMARK 620 2 GLU A 299   OE1 133.0                                              
REMARK 620 3 MET A 300   O    96.4  94.1                                        
REMARK 620 4 ALA A 126   O    88.7 137.7  85.6                                  
REMARK 620 5 HOH A4090   O    66.3 103.7 160.9  85.7                            
REMARK 620 6 HOH A4092   O    68.7  67.5 123.9 143.5  59.3                      
REMARK 620 7 HOH A4093   O   136.6  89.3  66.6  51.9 119.7 154.1                
REMARK 620 8 ASN A 301   OD1  83.6  54.6  77.2 160.2 107.6  48.4 126.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4003   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 215   OE2                                                    
REMARK 620 2 ASP A 238   O   122.5                                              
REMARK 620 3 ILE A 242   O    88.9 138.3                                        
REMARK 620 4 SER A 247   OG  140.0  95.4  66.7                                  
REMARK 620 5 ALA A 239   O    88.7  70.0  85.7 118.7                            
REMARK 620 6 ASN A 236   OD1  85.0  90.5 121.5  82.0 151.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A4002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 285   OE1                                                    
REMARK 620 2 GLU A 299   OE2  80.5                                              
REMARK 620 3 ADP A4000   O1B 173.3 102.2                                        
REMARK 620 4 PO4 A4006   O3   90.9  88.7  95.2                                  
REMARK 620 5 ADP A4000   O1A  89.6  86.5  84.5 175.1                            
REMARK 620 6 HOH A4089   O    80.6 161.0  96.6  91.9  93.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4020   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 285   OE1                                                    
REMARK 620 2 PO4 A4006   O3   63.1                                              
REMARK 620 3 HOH A4098   O   145.5  87.6                                        
REMARK 620 4  MN A4002  MN    33.2  33.3 120.9                                  
REMARK 620 5 HOH A4089   O    48.2  55.8 129.4  32.9                            
REMARK 620 6 ASN A 283   OD1  81.9  98.9  85.5 101.1 129.5                      
REMARK 620 7 THR A 244   OG1  93.9  96.0 107.6  84.7  52.2 160.6                
REMARK 620 8 HOH A4097   O   137.5  98.4  60.1 112.7  89.4 140.5  47.8          
REMARK 620 9 GLU A 217   OE1 115.4 178.0  94.2 144.8 122.2  82.1  82.7  81.8    
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 A4001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 299   CD                                                     
REMARK 620 2 GLU A 299   OE1  26.8                                              
REMARK 620 3 GLU A 299   OE2  30.1  56.9                                        
REMARK 620 4 ASN A 301   OD1  87.1  87.3  87.7                                  
REMARK 620 5 ADP A4000   O3B  82.4  80.4  86.3 167.7                            
REMARK 620 6 HOH A4092   O   121.8  95.1 151.7  87.1  93.1                      
REMARK 620 7 PO4 A4006   O1  120.8 146.7  91.3  81.2 109.7 115.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4010   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 761   OE2                                                    
REMARK 620 2 HIS A 781   ND1  79.2                                              
REMARK 620 3 GLU A 783   O   129.3  90.6                                        
REMARK 620 4 GLN A 784   O    95.0 143.7  65.4                                  
REMARK 620 5 VAL A 787   O    76.1 125.2 141.8  86.8                            
REMARK 620 6 SER A 792   OG  126.4  79.8  99.5 128.6  77.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A4008  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 829   OE1                                                    
REMARK 620 2 GLU A 841   OE2  89.1                                              
REMARK 620 3 ADP A4007   O2A  92.4  88.9                                        
REMARK 620 4 HOH A4557   O    89.2 173.3  84.7                                  
REMARK 620 5 ADP A4007   O3B 170.9  93.2  78.9  87.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4009   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 841   OE2                                                    
REMARK 620 2 ADP A4007   O2B  90.1                                              
REMARK 620 3 ADP A4007   O3B  60.8  48.5                                        
REMARK 620 4 GLU A 841   OE1  42.9  83.9  87.3                                  
REMARK 620 5 ASN A 843   OD1  70.1 156.9 123.6  73.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B4019   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  16   O                                                      
REMARK 620 2 ASP B 112   O    99.4                                              
REMARK 620 3 HOH B4082   O    88.6  93.4                                        
REMARK 620 4 HOH B4083   O    73.0 158.7 106.1                                  
REMARK 620 5 HOH A4546   O   123.8  80.2 147.5  87.6                            
REMARK 620 6 HOH A4548   O   149.9 104.3  71.7  90.4  79.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4043   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 114   OG1                                                    
REMARK 620 2 THR C 114   N    54.5                                              
REMARK 620 3 GLY C 112   O   110.7  66.5                                        
REMARK 620 4 HOH C4134   O    83.1 118.6 163.2                                  
REMARK 620 5 ASP C  84   O    86.1  45.0  74.9  97.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4027   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 127   OE1                                                    
REMARK 620 2 GLU C 299   OE1 134.5                                              
REMARK 620 3 MET C 300   O    97.1  93.8                                        
REMARK 620 4 HOH C4709   O    96.4 101.0 142.7                                  
REMARK 620 5 ALA C 126   O    87.0 138.1  84.7  61.6                            
REMARK 620 6 HOH C4111   O    61.9 104.0 158.6  45.3  89.7                      
REMARK 620 7 HOH C4113   O    68.6  69.7 127.0  90.3 140.8  52.1                
REMARK 620 8 HOH C4114   O   137.9  86.9  67.8  79.0  53.8 124.2 152.0          
REMARK 620 9 ASN C 301   OD1  87.9  53.5  73.7 141.4 156.9 107.5  55.7 121.6    
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 C4044   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 143   OG1                                                    
REMARK 620 2 ALA C 144   O    76.6                                              
REMARK 620 3 HOH C4221   O    72.8  64.0                                        
REMARK 620 4 THR C 143   O    68.2  69.4 124.4                                  
REMARK 620 5 HOH C4241   O   129.5  84.2  56.9 144.3                            
REMARK 620 6 HOH C4226   O    83.2 132.4 146.8  63.1 139.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4026   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 215   OE2                                                    
REMARK 620 2 ASN C 236   OD1  83.7                                              
REMARK 620 3 ASP C 238   O   123.9  95.6                                        
REMARK 620 4 ALA C 239   O    89.7 151.4  65.4                                  
REMARK 620 5 ILE C 242   O    78.4 117.9 142.7  87.6                            
REMARK 620 6 SER C 247   OG  134.4  81.0 100.3 121.8  71.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4042   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 285   OE1                                                    
REMARK 620 2 PO4 C4028   O3   64.0                                              
REMARK 620 3 GLU C 217   OE1 117.9 170.4                                        
REMARK 620 4 ASN C 283   OD1  80.5 101.7  88.0                                  
REMARK 620 5  MN C4025  MN    33.2  34.3 143.4 101.7                            
REMARK 620 6 HOH C4119   O   148.0  87.0  93.1  93.5 121.0                      
REMARK 620 7 THR C 244   OG1  93.5  87.3  83.1 165.5  79.2  98.5                
REMARK 620 8 HOH C4110   O    51.3  53.5 119.3 131.0  32.6 121.9  47.0          
REMARK 620 9 HOH C4118   O   135.9  96.3  75.8 143.6 110.8  55.9  44.3  85.0    
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 C4025  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 285   OE1                                                    
REMARK 620 2 GLU C 299   OE2  79.2                                              
REMARK 620 3 ADP C4023   O1A  98.0  86.9                                        
REMARK 620 4 HOH C4110   O    90.5 169.7  96.1                                  
REMARK 620 5 PO4 C4028   O3   89.5  84.1 166.9  94.5                            
REMARK 620 6 ADP C4023   O1B 178.2 100.6  83.8  89.6  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C4024  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 299   CD                                                     
REMARK 620 2 GLU C 299   OE1  27.5                                              
REMARK 620 3 GLU C 299   OE2  29.6  57.0                                        
REMARK 620 4 ASN C 301   OD1  78.6  77.4  79.7                                  
REMARK 620 5 ADP C4023   O3B  94.7  94.5  96.9 171.8                            
REMARK 620 6 PO4 C4028   O1  122.3 148.8  92.9  89.9  97.9                      
REMARK 620 7 HOH C4113   O   123.6  96.1 152.9  91.9  87.7 112.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4032   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 761   OE2                                                    
REMARK 620 2 HIS C 781   ND1  78.1                                              
REMARK 620 3 GLU C 783   O   125.9  94.8                                        
REMARK 620 4 VAL C 787   O    79.7 126.1 137.2                                  
REMARK 620 5 SER C 792   OG  126.1  84.2 105.9  70.8                            
REMARK 620 6 GLN C 784   O    87.8 146.4  69.0  79.9 127.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C4030  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 829   CD                                                     
REMARK 620 2 GLN C 829   OE1  20.9                                              
REMARK 620 3 GLU C 841   OE2  99.1  92.6                                        
REMARK 620 4 ADP C4029   O3B 167.1 169.2  89.7                                  
REMARK 620 5 ADP C4029   O2A 105.9  86.4  91.9  83.0                            
REMARK 620 6 HOH C4570   O    88.6 108.6  91.2  81.8 164.5                      
REMARK 620 7 HOH C4571   O    89.6  92.9 168.1  83.0  77.9  97.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D4041   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  16   O                                                      
REMARK 620 2 ASP D 112   O    88.6                                              
REMARK 620 3 HOH D1505   O    76.8  85.3                                        
REMARK 620 4 HOH C4561   O    79.6 149.5 118.5                                  
REMARK 620 5 HOH C4558   O   116.7  85.6 163.5  75.1                            
REMARK 620 6 ARG C 490   NH1 141.0 127.9  91.5  73.7  83.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4065   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  84   O                                                      
REMARK 620 2 THR E 114   OG1  78.1                                              
REMARK 620 3 HOH E4169   O    94.0 164.9                                        
REMARK 620 4 HOH E4166   O    88.3  91.6  75.2                                  
REMARK 620 5 HOH E4167   O   130.8  77.9 116.5 134.5                            
REMARK 620 6 GLY E 112   O    78.7 102.1  88.8 158.6  65.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4049   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 127   OE1                                                    
REMARK 620 2 GLU E 299   OE1 133.5                                              
REMARK 620 3 MET E 300   O    94.7  87.0                                        
REMARK 620 4 HOH E4145   O   142.3  83.1  75.9                                  
REMARK 620 5 ALA E 126   O    87.9 138.6  87.3  55.8                            
REMARK 620 6 ASN E 301   OD1  80.4  56.1  71.5 127.9 154.6                      
REMARK 620 7 HOH E4144   O    72.5  65.6 117.0 144.3 149.3  45.8                
REMARK 620 8 HOH E4142   O    72.5 106.4 165.6 110.2  85.9 111.5  66.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4066   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E 143   OG1                                                    
REMARK 620 2 HOH E4263   O    76.5                                              
REMARK 620 3 ALA E 144   O    73.0 126.7                                        
REMARK 620 4 THR E 143   O    59.6  63.0  64.0                                  
REMARK 620 5 HOH E4280   O   120.8 161.6  68.5 129.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4048   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 215   OE2                                                    
REMARK 620 2 ASN E 236   OD1  81.1                                              
REMARK 620 3 ASP E 238   O   128.2  93.2                                        
REMARK 620 4 ILE E 242   O    82.4 119.0 140.3                                  
REMARK 620 5 SER E 247   OG  136.2  81.6  92.6  71.7                            
REMARK 620 6 ALA E 239   O    93.7 155.1  70.9  84.0 117.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4064   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 217   OE1                                                    
REMARK 620 2 GLN E 285   OE1 117.3                                              
REMARK 620 3 PO4 E4050   O3  172.7  66.5                                        
REMARK 620 4 HOH E4149   O    75.4 141.9  97.8                                  
REMARK 620 5 HOH E4150   O    89.2 149.5  89.1  55.6                            
REMARK 620 6 THR E 244   OG1  86.4  93.1  87.1  50.1 104.1                      
REMARK 620 7 ASN E 283   OD1  83.5  86.4 103.2 131.7  81.6 168.4                
REMARK 620 8  MN E4047  MN   147.0  36.6  33.6 113.6 122.6  78.0 107.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E4047  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 285   OE1                                                    
REMARK 620 2 GLU E 299   OE2  80.3                                              
REMARK 620 3 ADP E4045   O1B 175.1 100.2                                        
REMARK 620 4 HOH E4141   O    87.8 165.6  92.4                                  
REMARK 620 5 PO4 E4050   O3   91.6  88.8  83.6  99.5                            
REMARK 620 6 ADP E4045   O1A  94.7  78.6  90.1  94.6 164.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E4046  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 299   CD                                                     
REMARK 620 2 GLU E 299   OE1  27.6                                              
REMARK 620 3 GLU E 299   OE2  29.9  57.5                                        
REMARK 620 4 ASN E 301   OD1  91.9  86.0  95.3                                  
REMARK 620 5 ADP E4045   O3B  92.2  93.9  92.4 170.9                            
REMARK 620 6 HOH E4144   O   119.9  92.4 149.8  79.9  91.0                      
REMARK 620 7 PO4 E4050   O1  128.7 152.9  99.7  81.6 102.1 108.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4054   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 761   OE2                                                    
REMARK 620 2 HIS E 781   ND1  81.5                                              
REMARK 620 3 GLU E 783   O   124.0  94.8                                        
REMARK 620 4 GLN E 784   O    88.5 147.9  66.0                                  
REMARK 620 5 VAL E 787   O    77.1 119.2 143.5  87.5                            
REMARK 620 6 SER E 792   OG  132.1  80.5 101.5 126.9  73.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E4052  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 829   OE1                                                    
REMARK 620 2 GLU E 841   OE2  82.5                                              
REMARK 620 3 ADP E4051   O2A  97.6  91.1                                        
REMARK 620 4 HOH E4614   O    95.5 173.8  83.2                                  
REMARK 620 5 ADP E4051   O3B 166.3  84.8  87.6  97.7                            
REMARK 620 6 HOH E4615   O    78.7  84.7 174.7 100.8  95.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4053   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 841   OE2                                                    
REMARK 620 2 HOH E4154   O    96.0                                              
REMARK 620 3 ADP E4051   O2B  89.4  49.7                                        
REMARK 620 4 ADP E4051   O3B  56.9  91.2  48.3                                  
REMARK 620 5 ASN E 843   OD1  68.2 113.9 151.9 121.6                            
REMARK 620 6 GLU E 841   OE1  44.9  58.6  83.4  84.4  68.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K F4063   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  16   O                                                      
REMARK 620 2 ASP F 112   O    86.9                                              
REMARK 620 3 HOH F2481   O    83.3  90.8                                        
REMARK 620 4 HOH E4605   O   112.9  83.8 162.4                                  
REMARK 620 5 HOH F2482   O    80.9 153.7 110.7  79.8                            
REMARK 620 6 HOH E4607   O   146.8 123.0  82.5  86.5  76.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4088   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY G 112   O                                                      
REMARK 620 2 HOH G2968   O    76.1                                              
REMARK 620 3 THR G 114   OG1 105.9  94.5                                        
REMARK 620 4 HOH G2966   O   157.9  82.0  72.5                                  
REMARK 620 5 HOH G2970   O    82.1  88.0 172.0 100.4                            
REMARK 620 6 ASP G  84   O    74.6 149.8  86.4 126.5  95.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4072   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 127   OE1                                                    
REMARK 620 2 GLU G 299   OE1 130.4                                              
REMARK 620 3 MET G 300   O    95.1  95.3                                        
REMARK 620 4 HOH G2947   O    64.5  73.0 132.3                                  
REMARK 620 5 ALA G 126   O    88.0 141.6  78.8 137.4                            
REMARK 620 6 HOH G2948   O   141.6  87.2  70.5 149.9  54.9                      
REMARK 620 7 HOH G2945   O    69.1 102.7 161.2  50.8  90.2 115.4                
REMARK 620 8  MN G4069  MN    95.0  35.6 105.6  41.4 174.4 122.8  86.4          
REMARK 620 9 ASN G 301   OD1  83.3  52.3  77.4  58.6 153.8 125.0 109.4  31.7    
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 G4089   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G 143   O                                                      
REMARK 620 2 HOH G3058   O    69.9                                              
REMARK 620 3 HOH G3052   O   123.3 143.6                                        
REMARK 620 4 ALA G 144   O    63.3 131.0  64.0                                  
REMARK 620 5 THR G 143   OG1  70.0  74.9  78.9  76.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4071   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 215   OE2                                                    
REMARK 620 2 ASP G 238   O   121.9                                              
REMARK 620 3 ALA G 239   O    93.7  67.4                                        
REMARK 620 4 ILE G 242   O    85.8 140.4  84.6                                  
REMARK 620 5 SER G 247   OG  139.2  95.1 118.0  73.3                            
REMARK 620 6 ASN G 236   OD1  76.1  95.9 152.2 119.5  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4087   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 217   OE1                                                    
REMARK 620 2 ASN G 283   OD1  88.5                                              
REMARK 620 3 GLN G 285   OE1 122.1  88.7                                        
REMARK 620 4 HOH G2953   O    94.2  97.4 143.4                                  
REMARK 620 5 PO4 G4073   O3  161.1 110.4  59.9  84.4                            
REMARK 620 6 HOH G2952   O    77.5 146.9 124.2  54.8  86.4                      
REMARK 620 7 THR G 244   OG1  80.5 162.6  85.9  96.9  81.0  43.0                
REMARK 620 8 ASN G 283   ND2  57.3  37.5 121.9  79.8 140.1 112.6 137.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G4070  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 285   OE1                                                    
REMARK 620 2 GLU G 299   OE2  79.7                                              
REMARK 620 3 PO4 G4073   O3   88.9  93.7                                        
REMARK 620 4 HOH G2944   O    89.1 168.3  89.6                                  
REMARK 620 5 ADP G4068   O1A 104.7  84.3 165.6  95.2                            
REMARK 620 6 ADP G4068   O1B 171.8 101.7  83.0  89.9  83.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G4069  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 299   CD                                                     
REMARK 620 2 GLU G 299   OE1  26.5                                              
REMARK 620 3 GLU G 299   OE2  28.6  54.9                                        
REMARK 620 4 ASN G 301   OD1  85.6  87.5  88.4                                  
REMARK 620 5 HOH G2947   O   119.9  93.4 148.4  90.6                            
REMARK 620 6 PO4 G4073   O1  119.2 145.7  91.1  86.2 120.4                      
REMARK 620 7 ADP G4068   O3B  87.6  84.7  87.4 172.3  89.6 100.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4077   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 761   OE2                                                    
REMARK 620 2 HIS G 781   ND1  77.4                                              
REMARK 620 3 GLU G 783   O   134.2  96.8                                        
REMARK 620 4 GLN G 784   O    93.3 146.2  66.5                                  
REMARK 620 5 VAL G 787   O    83.1 122.6 133.0  87.7                            
REMARK 620 6 SER G 792   OG  124.5  80.4  98.4 129.3  67.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G4075  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 829   OE1                                                    
REMARK 620 2 GLU G 841   OE2  72.6                                              
REMARK 620 3 ADP G4074   O3B 151.9  79.2                                        
REMARK 620 4 ADP G4074   O2A  87.2  80.8  88.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4076   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 841   OE1                                                    
REMARK 620 2 ADP G4074   O3B  85.4                                              
REMARK 620 3 ADP G4074   O2B  92.7  49.6                                        
REMARK 620 4 ASN G 843   OD1  64.3 110.5 152.5                                  
REMARK 620 5 GLU G 841   OE2  43.0  53.9  90.5  62.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K H4086   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 112   O                                                      
REMARK 620 2 HOH H3435   O    89.3                                              
REMARK 620 3 HOH H3432   O    85.8 166.7                                        
REMARK 620 4 HIS H  16   O    80.6  82.9 108.4                                  
REMARK 620 5 HOH G3434   O   128.9  81.8  91.6 146.3                            
REMARK 620 6 HOH H3661   O   149.6 102.1  88.3  73.1  81.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4022   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A4203   O                                                      
REMARK 620 2 THR A 143   OG1  61.1                                              
REMARK 620 3 ALA A 144   O    58.0  72.1                                        
REMARK 620 4 HOH A4600   O    77.0  68.1 130.3                                  
REMARK 620 5 THR A 143   O   106.7  63.8  61.8 120.3                            
REMARK 620 6 HOH A4209   O   126.5  69.3 123.7  66.6  64.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4031   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C4029   O2B                                                    
REMARK 620 2 HOH C4123   O    63.6                                              
REMARK 620 3 GLU C 841   OE1  89.2  55.6                                        
REMARK 620 4 GLU C 841   OE2  92.6  95.9  44.1                                  
REMARK 620 5 ASN C 843   OD1 156.8 110.0  70.3  65.2                            
REMARK 620 6 ADP C4029   O3B  47.6  98.9  83.7  56.6 116.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4004                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4009                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4010                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4016                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4017                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4018                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 4019                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4020                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4021                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4022                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4024                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4025                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4026                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4027                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4066                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4069                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4031                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4070                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4032                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4071                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4037                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4072                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4038                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4075                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4039                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4076                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4040                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4077                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 4041                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4082                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4042                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4083                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4043                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4084                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4044                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 4085                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4046                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 4086                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4047                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4087                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4048                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4088                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4049                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4089                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4052                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4053                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4054                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4059                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4060                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4061                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 4062                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 4063                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4064                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4065                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 4050                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 4067                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 4073                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 4028                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 4033                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN D 4034                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN C 4035                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 4036                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 4045                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 4051                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 4055                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN F 4056                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN E 4057                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 4058                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 4068                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 4074                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 4078                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN H 4079                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN G 4080                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 4081                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN B 4012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN A 4013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 4014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 4023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 4029                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CS0   RELATED DB: PDB                                   
DBREF  1C3O A    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C3O C    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C3O E    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C3O G    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C3O B    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1C3O D    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1C3O F    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1C3O H    1   382  UNP    P00907   CARA_ECOLI       1    382             
SEQADV 1C3O SER B  269  UNP  P00907    CYS   269 ENGINEERED MUTATION            
SEQADV 1C3O SER D  269  UNP  P00907    CYS   269 ENGINEERED MUTATION            
SEQADV 1C3O SER F  269  UNP  P00907    CYS   269 ENGINEERED MUTATION            
SEQADV 1C3O SER H  269  UNP  P00907    CYS   269 ENGINEERED MUTATION            
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 SER 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 SER 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 SER 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 SER 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                                          
HET     MN  A4001       1                                                       
HET     MN  A4002       1                                                       
HET      K  A4003       1                                                       
HET      K  A4004       1                                                       
HET     MN  A4008       1                                                       
HET      K  A4009       1                                                       
HET      K  A4010       1                                                       
HET     CL  A4015       1                                                       
HET     CL  A4016       1                                                       
HET     CL  A4017       1                                                       
HET      K  A4020       1                                                       
HET      K  A4021       1                                                       
HET      K  A4022       1                                                       
HET    PO4  A4006       5                                                       
HET    ADP  A4000      27                                                       
HET    ADP  A4007      27                                                       
HET    ORN  A4011       9                                                       
HET    GLN  A4013      10                                                       
HET    NET  A4014       9                                                       
HET     CL  B4018       1                                                       
HET      K  B4019       1                                                       
HET    GLN  B4012      10                                                       
HET     MN  C4024       1                                                       
HET     MN  C4025       1                                                       
HET      K  C4026       1                                                       
HET      K  C4027       1                                                       
HET     MN  C4030       1                                                       
HET      K  C4031       1                                                       
HET      K  C4032       1                                                       
HET     CL  C4037       1                                                       
HET     CL  C4038       1                                                       
HET     CL  C4039       1                                                       
HET      K  C4042       1                                                       
HET      K  C4043       1                                                       
HET      K  C4044       1                                                       
HET    PO4  C4028       5                                                       
HET    ORN  C4033       9                                                       
HET    GLN  C4035      10                                                       
HET    NET  C4036       9                                                       
HET    ADP  C4023      27                                                       
HET    ADP  C4029      27                                                       
HET     CL  D4040       1                                                       
HET      K  D4041       1                                                       
HET    GLN  D4034      10                                                       
HET      K  E4066       1                                                       
HET     MN  E4046       1                                                       
HET     MN  E4047       1                                                       
HET      K  E4048       1                                                       
HET      K  E4049       1                                                       
HET     MN  E4052       1                                                       
HET      K  E4053       1                                                       
HET      K  E4054       1                                                       
HET     CL  E4059       1                                                       
HET     CL  E4060       1                                                       
HET     CL  E4061       1                                                       
HET      K  E4064       1                                                       
HET      K  E4065       1                                                       
HET    PO4  E4050       5                                                       
HET    PO4  E4067       5                                                       
HET    ADP  E4045      27                                                       
HET    ADP  E4051      27                                                       
HET    ORN  E4055       9                                                       
HET    GLN  E4057      10                                                       
HET    NET  E4058       9                                                       
HET     CL  F4062       1                                                       
HET      K  F4063       1                                                       
HET    GLN  F4056      10                                                       
HET     MN  G4069       1                                                       
HET     MN  G4070       1                                                       
HET      K  G4071       1                                                       
HET      K  G4072       1                                                       
HET     MN  G4075       1                                                       
HET      K  G4076       1                                                       
HET      K  G4077       1                                                       
HET     CL  G4082       1                                                       
HET     CL  G4083       1                                                       
HET     CL  G4084       1                                                       
HET      K  G4087       1                                                       
HET      K  G4088       1                                                       
HET      K  G4089       1                                                       
HET    PO4  G4073       5                                                       
HET    ADP  G4068      27                                                       
HET    ADP  G4074      27                                                       
HET    ORN  G4078       9                                                       
HET    GLN  G4080      10                                                       
HET    NET  G4081       9                                                       
HET     CL  H4085       1                                                       
HET      K  H4086       1                                                       
HET    GLN  H4079      10                                                       
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     GLN GLUTAMINE                                                        
HETNAM     NET TETRAETHYLAMMONIUM ION                                           
FORMUL   9   MN    12(MN 2+)                                                    
FORMUL  11    K    32(K 1+)                                                     
FORMUL  16   CL    16(CL 1-)                                                    
FORMUL  22  PO4    5(O4 P 3-)                                                   
FORMUL  23  ADP    8(C10 H15 N5 O10 P2)                                         
FORMUL  25  ORN    4(C5 H12 N2 O2)                                              
FORMUL  26  GLN    8(C5 H10 N2 O3)                                              
FORMUL  27  NET    4(C8 H20 N 1+)                                               
FORMUL  98  HOH   *3666(H2 O)                                                   
HELIX    1   1 CYS A   24  GLU A   40  1                                  17    
HELIX    2   2 ASP A   57  ALA A   61  5                                   5    
HELIX    3   3 HIS A   70  ARG A   82  1                                  13    
HELIX    4   4 GLY A   91  GLN A  105  1                                  15    
HELIX    5   5 GLY A  106  GLY A  112  1                                   7    
HELIX    6   6 THR A  119  ASP A  128  1                                  10    
HELIX    7   7 ASP A  128  ILE A  139  1                                  12    
HELIX    8   8 THR A  151  GLY A  163  1                                  13    
HELIX    9   9 ASN A  184  SER A  199  1                                  16    
HELIX   10  10 HIS A  243  SER A  247  5                                   5    
HELIX   11  11 THR A  257  GLY A  276  1                                  20    
HELIX   12  12 SER A  305  GLY A  316  1                                  12    
HELIX   13  13 PRO A  318  VAL A  328  1                                  11    
HELIX   14  14 ASN A  337  GLY A  341  5                                   5    
HELIX   15  15 ASN A  363  PHE A  367  5                                   5    
HELIX   16  16 THR A  390  LEU A  402  1                                  13    
HELIX   17  17 GLU A  419  ASP A  430  1                                  12    
HELIX   18  18 ASP A  434  GLY A  446  1                                  13    
HELIX   19  19 SER A  448  ASN A  457  1                                  10    
HELIX   20  20 ASP A  459  GLY A  480  1                                  22    
HELIX   21  21 ILE A  481  LEU A  484  5                                   4    
HELIX   22  22 ASN A  485  LYS A  495  1                                  11    
HELIX   23  23 ALA A  498  GLY A  507  1                                  10    
HELIX   24  24 ARG A  509  ASP A  521  1                                  13    
HELIX   25  25 GLY A  575  ASP A  592  1                                  18    
HELIX   26  26 ASP A  609  SER A  613  5                                   5    
HELIX   27  27 THR A  622  LYS A  634  1                                  13    
HELIX   28  28 GLY A  644  ALA A  657  1                                  14    
HELIX   29  29 SER A  665  ASP A  674  1                                  10    
HELIX   30  30 ASP A  674  LEU A  685  1                                  12    
HELIX   31  31 ALA A  697  GLY A  709  1                                  13    
HELIX   32  32 ASP A  730  ALA A  741  1                                  12    
HELIX   33  33 HIS A  788  SER A  792  5                                   5    
HELIX   34  34 SER A  802  GLN A  821  1                                  20    
HELIX   35  35 THR A  849  GLY A  858  1                                  10    
HELIX   36  36 PRO A  860  GLY A  871  1                                  12    
HELIX   37  37 SER A  873  GLY A  878  1                                   6    
HELIX   38  38 PRO A  896  PHE A  900  5                                   5    
HELIX   39  39 THR A  923  SER A  935  1                                  13    
HELIX   40  40 ARG A  950  LYS A  954  5                                   5    
HELIX   41  41 ARG A  956  GLY A  968  1                                  13    
HELIX   42  42 HIS A  975  ALA A  984  1                                  10    
HELIX   43  43 HIS A 1000  ASN A 1007  1                                   8    
HELIX   44  44 GLY A 1019  TYR A 1036  1                                  18    
HELIX   45  45 THR A 1043  ASN A 1055  1                                  13    
HELIX   46  46 SER A 1064  GLN A 1071  1                                   8    
HELIX   47  47 GLY B   38  THR B   44  1                                   7    
HELIX   48  48 ASP B   45  TYR B   48  5                                   4    
HELIX   49  49 ASN B   66  GLU B   70  5                                   5    
HELIX   50  50 ASP B   97  ASN B  106  1                                  10    
HELIX   51  51 ASP B  114  GLY B  126  1                                  13    
HELIX   52  52 ASP B  139  PHE B  150  1                                  12    
HELIX   53  53 LEU B  158  THR B  163  1                                   6    
HELIX   54  54 LYS B  186  LEU B  190  5                                   5    
HELIX   55  55 LYS B  202  ARG B  212  1                                  11    
HELIX   56  56 SER B  224  LYS B  230  1                                   7    
HELIX   57  57 CYS B  248  LEU B  259  1                                  12    
HELIX   58  58 SER B  269  SER B  279  1                                  11    
HELIX   59  59 GLU B  318  LEU B  321  5                                   4    
HELIX   60  60 ALA B  364  THR B  380  1                                  17    
HELIX   61  61 CYS C   24  GLU C   40  1                                  17    
HELIX   62  62 THR C   53  ASP C   57  5                                   5    
HELIX   63  63 ASP C   57  ALA C   61  5                                   5    
HELIX   64  64 HIS C   70  ARG C   82  1                                  13    
HELIX   65  65 GLY C   91  GLN C  105  1                                  15    
HELIX   66  66 GLY C  106  GLY C  112  1                                   7    
HELIX   67  67 THR C  119  ASP C  128  1                                  10    
HELIX   68  68 ASP C  128  ILE C  139  1                                  12    
HELIX   69  69 THR C  151  GLY C  163  1                                  13    
HELIX   70  70 ASN C  184  SER C  199  1                                  16    
HELIX   71  71 HIS C  243  SER C  247  5                                   5    
HELIX   72  72 THR C  257  GLY C  276  1                                  20    
HELIX   73  73 SER C  305  GLY C  316  1                                  12    
HELIX   74  74 PRO C  318  VAL C  328  1                                  11    
HELIX   75  75 THR C  331  LEU C  335  5                                   5    
HELIX   76  76 ASN C  337  GLY C  341  5                                   5    
HELIX   77  77 ASN C  363  PHE C  367  5                                   5    
HELIX   78  78 THR C  390  LEU C  402  1                                  13    
HELIX   79  79 GLU C  419  ASP C  430  1                                  12    
HELIX   80  80 ASP C  434  ALA C  445  1                                  12    
HELIX   81  81 SER C  448  ASN C  457  1                                  10    
HELIX   82  82 ASP C  459  GLY C  480  1                                  22    
HELIX   83  83 ILE C  481  GLY C  483  5                                   3    
HELIX   84  84 ASN C  485  LYS C  495  1                                  11    
HELIX   85  85 ALA C  498  GLY C  507  1                                  10    
HELIX   86  86 ARG C  509  ASP C  521  1                                  13    
HELIX   87  87 GLY C  575  ASP C  592  1                                  18    
HELIX   88  88 ASP C  609  SER C  613  5                                   5    
HELIX   89  89 THR C  622  LYS C  634  1                                  13    
HELIX   90  90 GLY C  644  LYS C  649  1                                   6    
HELIX   91  91 LEU C  650  ALA C  657  1                                   8    
HELIX   92  92 SER C  665  ASP C  674  1                                  10    
HELIX   93  93 ASP C  674  LEU C  685  1                                  12    
HELIX   94  94 ALA C  697  GLY C  709  1                                  13    
HELIX   95  95 ASP C  730  ALA C  741  1                                  12    
HELIX   96  96 HIS C  788  SER C  792  5                                   5    
HELIX   97  97 SER C  802  LEU C  820  1                                  19    
HELIX   98  98 THR C  849  GLY C  858  1                                  10    
HELIX   99  99 PRO C  860  ALA C  870  1                                  11    
HELIX  100 100 SER C  873  GLY C  878  1                                   6    
HELIX  101 101 PRO C  896  PHE C  900  5                                   5    
HELIX  102 102 THR C  923  SER C  935  1                                  13    
HELIX  103 103 ARG C  950  LYS C  954  5                                   5    
HELIX  104 104 GLU C  955  GLU C  955  5                                   1    
HELIX  105 105 ARG C  956  GLN C  967  1                                  12    
HELIX  106 106 THR C  974  GLU C  983  1                                  10    
HELIX  107 107 HIS C 1000  ASN C 1007  1                                   8    
HELIX  108 108 GLY C 1019  LYS C 1037  1                                  19    
HELIX  109 109 THR C 1043  LEU C 1054  1                                  12    
HELIX  110 110 SER C 1064  GLN C 1071  1                                   8    
HELIX  111 111 GLY D   38  THR D   44  1                                   7    
HELIX  112 112 ASP D   45  TYR D   48  5                                   4    
HELIX  113 113 ASN D   66  GLU D   70  5                                   5    
HELIX  114 114 ASP D   97  HIS D  105  1                                   9    
HELIX  115 115 ASP D  114  GLY D  126  1                                  13    
HELIX  116 116 ASP D  139  PHE D  150  1                                  12    
HELIX  117 117 LEU D  158  THR D  163  1                                   6    
HELIX  118 118 LYS D  186  LEU D  190  5                                   5    
HELIX  119 119 LYS D  202  ARG D  212  1                                  11    
HELIX  120 120 SER D  224  LYS D  230  1                                   7    
HELIX  121 121 CYS D  248  LEU D  259  1                                  12    
HELIX  122 122 SER D  269  SER D  279  1                                  11    
HELIX  123 123 GLU D  318  LEU D  321  5                                   4    
HELIX  124 124 ALA D  364  THR D  380  1                                  17    
HELIX  125 125 CYS E   24  GLU E   40  1                                  17    
HELIX  126 126 THR E   53  ASP E   57  5                                   5    
HELIX  127 127 ASP E   57  ALA E   61  5                                   5    
HELIX  128 128 HIS E   70  ARG E   82  1                                  13    
HELIX  129 129 GLY E   91  GLN E  105  1                                  15    
HELIX  130 130 GLY E  106  PHE E  111  1                                   6    
HELIX  131 131 THR E  119  ASP E  128  1                                  10    
HELIX  132 132 ASP E  128  GLY E  140  1                                  13    
HELIX  133 133 THR E  151  GLY E  163  1                                  13    
HELIX  134 134 ASN E  184  SER E  199  1                                  16    
HELIX  135 135 HIS E  243  SER E  247  5                                   5    
HELIX  136 136 THR E  257  GLY E  276  1                                  20    
HELIX  137 137 SER E  305  GLY E  316  1                                  12    
HELIX  138 138 PRO E  318  VAL E  328  1                                  11    
HELIX  139 139 ASN E  337  GLY E  341  5                                   5    
HELIX  140 140 ASN E  363  PHE E  367  5                                   5    
HELIX  141 141 THR E  390  LEU E  402  1                                  13    
HELIX  142 142 GLU E  419  ASP E  430  1                                  12    
HELIX  143 143 ASP E  434  ALA E  445  1                                  12    
HELIX  144 144 SER E  448  ASN E  457  1                                  10    
HELIX  145 145 ASP E  459  GLY E  480  1                                  22    
HELIX  146 146 ILE E  481  LEU E  484  5                                   4    
HELIX  147 147 ASN E  485  ARG E  494  1                                  10    
HELIX  148 148 ALA E  498  GLY E  507  1                                  10    
HELIX  149 149 ARG E  509  ASP E  521  1                                  13    
HELIX  150 150 GLY E  575  GLY E  593  1                                  19    
HELIX  151 151 THR E  605  ASP E  609  5                                   5    
HELIX  152 152 ASP E  609  SER E  613  5                                   5    
HELIX  153 153 THR E  622  LYS E  634  1                                  13    
HELIX  154 154 GLY E  644  LEU E  650  1                                   7    
HELIX  155 155 LEU E  650  ALA E  657  1                                   8    
HELIX  156 156 SER E  665  ASP E  674  1                                  10    
HELIX  157 157 ASP E  674  LYS E  686  1                                  13    
HELIX  158 158 ALA E  697  GLY E  709  1                                  13    
HELIX  159 159 ASP E  730  ALA E  741  1                                  12    
HELIX  160 160 HIS E  788  SER E  792  5                                   5    
HELIX  161 161 SER E  802  GLN E  821  1                                  20    
HELIX  162 162 THR E  849  GLY E  858  1                                  10    
HELIX  163 163 PRO E  860  GLY E  871  1                                  12    
HELIX  164 164 SER E  873  GLY E  878  1                                   6    
HELIX  165 165 PRO E  896  PHE E  900  5                                   5    
HELIX  166 166 THR E  923  SER E  935  1                                  13    
HELIX  167 167 ARG E  956  GLN E  967  1                                  12    
HELIX  168 168 THR E  974  GLU E  983  1                                  10    
HELIX  169 169 LYS E  993  GLY E  997  5                                   5    
HELIX  170 170 HIS E 1000  ASN E 1007  1                                   8    
HELIX  171 171 GLY E 1019  TYR E 1036  1                                  18    
HELIX  172 172 THR E 1043  LEU E 1054  1                                  12    
HELIX  173 173 SER E 1064  GLN E 1071  1                                   8    
HELIX  174 174 GLY F   38  THR F   44  1                                   7    
HELIX  175 175 ASP F   45  TYR F   48  5                                   4    
HELIX  176 176 ASN F   66  GLU F   70  5                                   5    
HELIX  177 177 ASP F   97  HIS F  105  1                                   9    
HELIX  178 178 ASP F  114  GLY F  126  1                                  13    
HELIX  179 179 ASP F  139  PHE F  150  1                                  12    
HELIX  180 180 LEU F  158  THR F  163  1                                   6    
HELIX  181 181 LYS F  186  LEU F  190  5                                   5    
HELIX  182 182 LYS F  202  ARG F  212  1                                  11    
HELIX  183 183 SER F  224  LYS F  230  1                                   7    
HELIX  184 184 CYS F  248  LEU F  259  1                                  12    
HELIX  185 185 SER F  269  SER F  279  1                                  11    
HELIX  186 186 GLU F  318  LEU F  321  5                                   4    
HELIX  187 187 PRO F  365  THR F  380  1                                  16    
HELIX  188 188 CYS G   24  GLU G   40  1                                  17    
HELIX  189 189 THR G   53  ASP G   57  5                                   5    
HELIX  190 190 ASP G   57  ALA G   61  5                                   5    
HELIX  191 191 HIS G   70  ARG G   82  1                                  13    
HELIX  192 192 GLY G   91  GLN G  105  1                                  15    
HELIX  193 193 GLY G  106  PHE G  111  1                                   6    
HELIX  194 194 THR G  119  ASP G  128  1                                  10    
HELIX  195 195 ASP G  128  ILE G  139  1                                  12    
HELIX  196 196 THR G  151  GLY G  163  1                                  13    
HELIX  197 197 ASN G  184  SER G  199  1                                  16    
HELIX  198 198 HIS G  243  SER G  247  5                                   5    
HELIX  199 199 THR G  257  GLY G  276  1                                  20    
HELIX  200 200 SER G  305  GLY G  316  1                                  12    
HELIX  201 201 PRO G  318  VAL G  328  1                                  11    
HELIX  202 202 THR G  331  LEU G  335  5                                   5    
HELIX  203 203 ASN G  337  GLY G  341  5                                   5    
HELIX  204 204 ASN G  363  PHE G  367  5                                   5    
HELIX  205 205 THR G  390  LEU G  402  1                                  13    
HELIX  206 206 GLU G  419  ASP G  430  1                                  12    
HELIX  207 207 ASP G  434  ALA G  445  1                                  12    
HELIX  208 208 SER G  448  ASN G  457  1                                  10    
HELIX  209 209 ASP G  459  GLY G  480  1                                  22    
HELIX  210 210 ILE G  481  LEU G  484  5                                   4    
HELIX  211 211 ASN G  485  LYS G  495  1                                  11    
HELIX  212 212 ALA G  498  GLY G  507  1                                  10    
HELIX  213 213 ARG G  509  TYR G  520  1                                  12    
HELIX  214 214 GLY G  575  GLY G  593  1                                  19    
HELIX  215 215 ASP G  609  SER G  613  5                                   5    
HELIX  216 216 THR G  622  LYS G  634  1                                  13    
HELIX  217 217 GLY G  644  LYS G  649  1                                   6    
HELIX  218 218 LEU G  650  ALA G  657  1                                   8    
HELIX  219 219 SER G  665  ASP G  674  1                                  10    
HELIX  220 220 ASP G  674  LYS G  686  1                                  13    
HELIX  221 221 ALA G  697  GLY G  709  1                                  13    
HELIX  222 222 ASP G  730  ALA G  741  1                                  12    
HELIX  223 223 HIS G  788  SER G  792  5                                   5    
HELIX  224 224 SER G  802  LEU G  820  1                                  19    
HELIX  225 225 THR G  849  GLY G  858  1                                  10    
HELIX  226 226 PRO G  860  ALA G  870  1                                  11    
HELIX  227 227 SER G  873  GLY G  878  1                                   6    
HELIX  228 228 LEU G  895  PHE G  900  5                                   6    
HELIX  229 229 THR G  923  SER G  935  1                                  13    
HELIX  230 230 ARG G  950  GLN G  967  1                                  18    
HELIX  231 231 HIS G  975  GLU G  983  1                                   9    
HELIX  232 232 HIS G 1000  ASN G 1007  1                                   8    
HELIX  233 233 GLY G 1019  LYS G 1037  1                                  19    
HELIX  234 234 THR G 1043  ALA G 1053  1                                  11    
HELIX  235 235 LEU G 1054  ALA G 1056  5                                   3    
HELIX  236 236 SER G 1064  GLN G 1071  1                                   8    
HELIX  237 237 GLY H   38  THR H   44  1                                   7    
HELIX  238 238 ASP H   45  TYR H   48  5                                   4    
HELIX  239 239 ASN H   66  GLU H   70  5                                   5    
HELIX  240 240 ASP H   97  HIS H  105  1                                   9    
HELIX  241 241 ASP H  114  GLY H  126  1                                  13    
HELIX  242 242 ASP H  139  PHE H  150  1                                  12    
HELIX  243 243 LEU H  158  THR H  163  1                                   6    
HELIX  244 244 LYS H  202  ASP H  211  1                                  10    
HELIX  245 245 SER H  224  MET H  231  1                                   8    
HELIX  246 246 CYS H  248  LEU H  259  1                                  12    
HELIX  247 247 SER H  269  SER H  279  1                                  11    
HELIX  248 248 GLU H  318  LEU H  321  5                                   4    
HELIX  249 249 PRO H  360  ALA H  363  5                                   4    
HELIX  250 250 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  N  LEU A 204   O  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  O  VAL A 250   N  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 6 VAL A 525  ARG A 528  0                                        
SHEET    2   D 6 TYR A 542  THR A 546 -1  O  TYR A 544   N  LYS A 527           
SHEET    3   D 6 ARG A 615  PHE A 618  1  O  LEU A 616   N  MET A 543           
SHEET    4   D 6 GLU A 595  ASN A 600  1  O  THR A 596   N  ARG A 615           
SHEET    5   D 6 LYS A 561  LEU A 565  1  O  ILE A 562   N  ILE A 597           
SHEET    6   D 6 GLY A 637  ILE A 639  1  O  GLY A 637   N  MET A 563           
SHEET    1   E 2 ASN A 692  THR A 694  0                                        
SHEET    2   E 2 LEU A 751  ASP A 753 -1  N  LEU A 752   O  ALA A 693           
SHEET    1   F 2 LEU A 712  VAL A 714  0                                        
SHEET    2   F 2 GLU A 726  VAL A 728 -1  O  GLU A 726   N  VAL A 714           
SHEET    1   G 7 VAL A 837  ASN A 843  0                                        
SHEET    2   G 7 GLY A 824  VAL A 832 -1  O  ASN A 827   N  ASN A 843           
SHEET    3   G 7 VAL A 760  CYS A 768 -1  N  VAL A 760   O  VAL A 832           
SHEET    4   G 7 VAL A 773  GLN A 784 -1  O  LEU A 774   N  ILE A 767           
SHEET    5   G 7 CYS A 794  LEU A 796 -1  N  SER A 795   O  GLU A 780           
SHEET    6   G 7 TYR A 888  VAL A 894 -1  O  SER A 889   N  LEU A 796           
SHEET    7   G 7 GLY A 915  GLY A 921 -1  O  GLY A 915   N  VAL A 894           
SHEET    1   H 5 ARG A 989  VAL A 991  0                                        
SHEET    2   H 5 PHE A 969  THR A 974  1  O  LEU A 971   N  ARG A 989           
SHEET    3   H 5 GLY A 943  SER A 948  1  O  GLY A 943   N  GLU A 970           
SHEET    4   H 5 TYR A1012  ASN A1015  1  O  TYR A1012   N  LEU A 946           
SHEET    5   H 5 TYR A1040  ASP A1041  1  O  ASP A1041   N  ASN A1015           
SHEET    1   I 8 SER B   4  LEU B   9  0                                        
SHEET    2   I 8 GLN B  14  ALA B  19 -1  N  PHE B  15   O  LEU B   7           
SHEET    3   I 8 VAL B 108  ALA B 111 -1  N  ALA B 111   O  ARG B  18           
SHEET    4   I 8 GLY B  79  VAL B  81  1  O  LEU B  80   N  ILE B 110           
SHEET    5   I 8 GLN B  51  LEU B  55  1  O  GLN B  51   N  GLY B  79           
SHEET    6   I 8 GLY B  24  ASN B  33  1  O  GLU B  29   N  ILE B  52           
SHEET    7   I 8 GLN B 128  ALA B 134 -1  O  GLN B 128   N  VAL B  30           
SHEET    8   I 8 SER B   4  LEU B   9 -1  O  LEU B   6   N  ILE B 133           
SHEET    1   J10 TYR B 168  TRP B 170  0                                        
SHEET    2   J10 CYS B 214  PRO B 220 -1  N  LEU B 216   O  TRP B 170           
SHEET    3   J10 PHE B 192  ASP B 198  1  O  PHE B 192   N  ARG B 215           
SHEET    4   J10 GLY B 235  LEU B 238  1  O  GLY B 235   N  VAL B 195           
SHEET    5   J10 VAL B 265  ILE B 268  1  O  PHE B 266   N  LEU B 238           
SHEET    6   J10 ALA B 347  PHE B 350  1  N  PHE B 348   O  VAL B 265           
SHEET    7   J10 LEU B 337  ARG B 342 -1  O  ILE B 340   N  SER B 349           
SHEET    8   J10 LEU B 325  SER B 331 -1  N  ARG B 326   O  HIS B 341           
SHEET    9   J10 THR B 283  ASP B 299 -1  N  LYS B 298   O  LYS B 330           
SHEET   10   J10 VAL B 304  VAL B 316 -1  O  VAL B 304   N  ASP B 299           
SHEET    1   K 5 ALA C  63  TYR C  65  0                                        
SHEET    2   K 5 ARG C  43  VAL C  47  1  O  VAL C  44   N  ALA C  63           
SHEET    3   K 5 SER C   9  LEU C  13  1  N  ILE C  10   O  ARG C  43           
SHEET    4   K 5 ALA C  85  LEU C  87  1  O  ALA C  85   N  LEU C  11           
SHEET    5   K 5 THR C 114  MET C 115  1  O  THR C 114   N  VAL C  86           
SHEET    1   L 4 SER C 146  ALA C 149  0                                        
SHEET    2   L 4 LEU C 204  GLU C 208 -1  N  LEU C 204   O  ALA C 149           
SHEET    3   L 4 CYS C 166  PRO C 170 -1  N  ILE C 167   O  ASP C 207           
SHEET    4   L 4 GLY C 180  ALA C 182 -1  O  GLY C 180   N  ILE C 168           
SHEET    1   M 7 LEU C 295  ASN C 301  0                                        
SHEET    2   M 7 GLY C 280  VAL C 288 -1  O  ASN C 283   N  ASN C 301           
SHEET    3   M 7 LYS C 214  ARG C 222 -1  N  LYS C 214   O  VAL C 288           
SHEET    4   M 7 CYS C 228  ASN C 236 -1  N  ILE C 229   O  VAL C 221           
SHEET    5   M 7 THR C 249  ALA C 251 -1  O  VAL C 250   N  GLU C 235           
SHEET    6   M 7 VAL C 355  ARG C 361 -1  N  VAL C 356   O  ALA C 251           
SHEET    7   M 7 GLY C 382  GLY C 388 -1  O  GLY C 382   N  ARG C 361           
SHEET    1   N 6 VAL C 525  ARG C 528  0                                        
SHEET    2   N 6 TYR C 542  THR C 546 -1  O  TYR C 544   N  LYS C 527           
SHEET    3   N 6 ARG C 615  TYR C 617  1  O  LEU C 616   N  MET C 543           
SHEET    4   N 6 GLU C 595  VAL C 599  1  O  THR C 596   N  ARG C 615           
SHEET    5   N 6 LYS C 561  LEU C 565  1  O  ILE C 562   N  ILE C 597           
SHEET    6   N 6 GLY C 637  ILE C 639  1  O  GLY C 637   N  MET C 563           
SHEET    1   O 4 ASN C 692  THR C 694  0                                        
SHEET    2   O 4 LEU C 751  HIS C 754 -1  N  LEU C 752   O  ALA C 693           
SHEET    3   O 4 LEU C 712  ARG C 715 -1  N  VAL C 713   O  ASP C 753           
SHEET    4   O 4 GLU C 726  VAL C 728 -1  O  GLU C 726   N  VAL C 714           
SHEET    1   P 7 GLU C 836  ASN C 843  0                                        
SHEET    2   P 7 GLY C 824  LYS C 833 -1  O  ASN C 827   N  ASN C 843           
SHEET    3   P 7 VAL C 760  CYS C 768 -1  O  VAL C 760   N  VAL C 832           
SHEET    4   P 7 VAL C 773  HIS C 781 -1  N  LEU C 774   O  ILE C 767           
SHEET    5   P 7 CYS C 794  LEU C 796 -1  N  SER C 795   O  GLU C 780           
SHEET    6   P 7 TYR C 888  VAL C 894 -1  O  SER C 889   N  LEU C 796           
SHEET    7   P 7 GLY C 915  GLY C 921 -1  O  GLY C 915   N  VAL C 894           
SHEET    1   Q 5 ARG C 989  LEU C 990  0                                        
SHEET    2   Q 5 GLU C 970  ALA C 973  1  O  LEU C 971   N  ARG C 989           
SHEET    3   Q 5 ARG C 944  SER C 948  1  N  ALA C 945   O  GLU C 970           
SHEET    4   Q 5 TYR C1012  ASN C1015  1  O  TYR C1012   N  LEU C 946           
SHEET    5   Q 5 TYR C1040  ASP C1041  1  N  ASP C1041   O  ILE C1013           
SHEET    1   R 8 SER D   4  LEU D   9  0                                        
SHEET    2   R 8 GLN D  14  ALA D  19 -1  N  PHE D  15   O  LEU D   7           
SHEET    3   R 8 VAL D 108  ALA D 111 -1  N  ALA D 111   O  ARG D  18           
SHEET    4   R 8 GLY D  79  VAL D  81  1  O  LEU D  80   N  ILE D 110           
SHEET    5   R 8 GLN D  51  LEU D  55  1  O  GLN D  51   N  GLY D  79           
SHEET    6   R 8 GLY D  24  ASN D  33  1  O  GLU D  29   N  ILE D  52           
SHEET    7   R 8 GLN D 128  ALA D 134 -1  O  GLN D 128   N  VAL D  30           
SHEET    8   R 8 SER D   4  LEU D   9 -1  O  LEU D   6   N  ILE D 133           
SHEET    1   S10 TYR D 168  TRP D 170  0                                        
SHEET    2   S10 CYS D 214  PRO D 220 -1  N  LEU D 216   O  TRP D 170           
SHEET    3   S10 PHE D 192  ASP D 198  1  O  PHE D 192   N  ARG D 215           
SHEET    4   S10 GLY D 235  LEU D 238  1  O  GLY D 235   N  VAL D 195           
SHEET    5   S10 VAL D 265  ILE D 268  1  O  PHE D 266   N  LEU D 238           
SHEET    6   S10 ALA D 347  PHE D 350  1  N  PHE D 348   O  VAL D 265           
SHEET    7   S10 LEU D 337  ARG D 342 -1  O  ILE D 340   N  SER D 349           
SHEET    8   S10 LEU D 325  SER D 331 -1  N  ARG D 326   O  HIS D 341           
SHEET    9   S10 THR D 283  ASP D 299 -1  N  LYS D 298   O  LYS D 330           
SHEET   10   S10 VAL D 304  VAL D 316 -1  O  VAL D 304   N  ASP D 299           
SHEET    1   T 5 ALA E  63  TYR E  65  0                                        
SHEET    2   T 5 ARG E  43  VAL E  47  1  O  VAL E  44   N  ALA E  63           
SHEET    3   T 5 SER E   9  LEU E  13  1  N  ILE E  10   O  ARG E  43           
SHEET    4   T 5 ALA E  85  LEU E  87  1  O  ALA E  85   N  LEU E  11           
SHEET    5   T 5 THR E 114  MET E 115  1  O  THR E 114   N  VAL E  86           
SHEET    1   U 4 SER E 146  ALA E 149  0                                        
SHEET    2   U 4 LEU E 204  GLU E 208 -1  N  LEU E 204   O  ALA E 149           
SHEET    3   U 4 CYS E 166  PRO E 170 -1  N  ILE E 167   O  ASP E 207           
SHEET    4   U 4 GLY E 180  ALA E 182 -1  O  GLY E 180   N  ILE E 168           
SHEET    1   V 7 LEU E 295  ASN E 301  0                                        
SHEET    2   V 7 GLY E 280  VAL E 288 -1  O  ASN E 283   N  ASN E 301           
SHEET    3   V 7 LYS E 214  ARG E 222 -1  O  LYS E 214   N  VAL E 288           
SHEET    4   V 7 CYS E 228  ASN E 236 -1  N  ILE E 229   O  VAL E 221           
SHEET    5   V 7 THR E 249  ALA E 251 -1  N  VAL E 250   O  GLU E 235           
SHEET    6   V 7 VAL E 355  ARG E 361 -1  N  VAL E 356   O  ALA E 251           
SHEET    7   V 7 GLY E 382  GLY E 388 -1  O  GLY E 382   N  ARG E 361           
SHEET    1   W 6 VAL E 525  ARG E 528  0                                        
SHEET    2   W 6 TYR E 542  THR E 546 -1  O  TYR E 544   N  LYS E 527           
SHEET    3   W 6 ARG E 615  PHE E 618  1  O  LEU E 616   N  MET E 543           
SHEET    4   W 6 GLU E 595  ASN E 600  1  O  THR E 596   N  ARG E 615           
SHEET    5   W 6 LYS E 561  LEU E 565  1  O  ILE E 562   N  ILE E 597           
SHEET    6   W 6 GLY E 637  ILE E 639  1  O  GLY E 637   N  MET E 563           
SHEET    1   X 4 ASN E 692  THR E 694  0                                        
SHEET    2   X 4 LEU E 751  HIS E 754 -1  N  LEU E 752   O  ALA E 693           
SHEET    3   X 4 LEU E 712  ARG E 715 -1  N  VAL E 713   O  ASP E 753           
SHEET    4   X 4 GLU E 726  VAL E 728 -1  O  GLU E 726   N  VAL E 714           
SHEET    1   Y 7 GLU E 836  ASN E 843  0                                        
SHEET    2   Y 7 GLY E 824  LYS E 833 -1  O  ASN E 827   N  ASN E 843           
SHEET    3   Y 7 VAL E 760  CYS E 768 -1  N  VAL E 760   O  VAL E 832           
SHEET    4   Y 7 VAL E 773  HIS E 781 -1  N  LEU E 774   O  ILE E 767           
SHEET    5   Y 7 CYS E 794  LEU E 796 -1  N  SER E 795   O  GLU E 780           
SHEET    6   Y 7 TYR E 888  VAL E 894 -1  O  SER E 889   N  LEU E 796           
SHEET    7   Y 7 GLY E 915  GLY E 921 -1  O  GLY E 915   N  VAL E 894           
SHEET    1   Z 5 ARG E 989  LEU E 990  0                                        
SHEET    2   Z 5 GLU E 970  ALA E 973  1  O  LEU E 971   N  ARG E 989           
SHEET    3   Z 5 ARG E 944  SER E 948  1  N  ALA E 945   O  GLU E 970           
SHEET    4   Z 5 TYR E1012  ASN E1015  1  O  TYR E1012   N  LEU E 946           
SHEET    5   Z 5 HIS E1039  ASP E1041  1  O  HIS E1039   N  ILE E1013           
SHEET    1  AA 8 SER F   4  LEU F   9  0                                        
SHEET    2  AA 8 GLN F  14  ALA F  19 -1  N  PHE F  15   O  LEU F   7           
SHEET    3  AA 8 VAL F 108  ALA F 111 -1  O  ALA F 111   N  ARG F  18           
SHEET    4  AA 8 GLY F  79  VAL F  81  1  O  LEU F  80   N  ILE F 110           
SHEET    5  AA 8 GLN F  51  LEU F  55  1  O  GLN F  51   N  GLY F  79           
SHEET    6  AA 8 GLY F  24  ASN F  33  1  O  GLU F  29   N  ILE F  52           
SHEET    7  AA 8 GLN F 128  ALA F 134 -1  O  GLN F 128   N  VAL F  30           
SHEET    8  AA 8 SER F   4  LEU F   9 -1  O  LEU F   6   N  ILE F 133           
SHEET    1  AB10 TYR F 168  TRP F 170  0                                        
SHEET    2  AB10 CYS F 214  PRO F 220 -1  N  LEU F 216   O  TRP F 170           
SHEET    3  AB10 PHE F 192  ASP F 198  1  O  PHE F 192   N  ARG F 215           
SHEET    4  AB10 GLY F 235  LEU F 238  1  O  GLY F 235   N  VAL F 195           
SHEET    5  AB10 VAL F 265  ILE F 268  1  N  PHE F 266   O  ILE F 236           
SHEET    6  AB10 ALA F 347  PHE F 350  1  N  PHE F 348   O  VAL F 265           
SHEET    7  AB10 LEU F 337  ARG F 342 -1  O  ILE F 340   N  SER F 349           
SHEET    8  AB10 LEU F 325  SER F 331 -1  N  ARG F 326   O  HIS F 341           
SHEET    9  AB10 THR F 283  ASP F 299 -1  N  LYS F 298   O  LYS F 330           
SHEET   10  AB10 VAL F 304  VAL F 316 -1  O  VAL F 304   N  ASP F 299           
SHEET    1  AC 5 ALA G  63  TYR G  65  0                                        
SHEET    2  AC 5 ARG G  43  VAL G  47  1  O  VAL G  44   N  ALA G  63           
SHEET    3  AC 5 SER G   9  LEU G  13  1  N  ILE G  10   O  ARG G  43           
SHEET    4  AC 5 ALA G  85  LEU G  87  1  O  ALA G  85   N  LEU G  11           
SHEET    5  AC 5 THR G 114  MET G 115  1  O  THR G 114   N  VAL G  86           
SHEET    1  AD 4 SER G 146  ALA G 149  0                                        
SHEET    2  AD 4 LEU G 204  GLU G 208 -1  N  LEU G 204   O  ALA G 149           
SHEET    3  AD 4 CYS G 166  PRO G 170 -1  O  ILE G 167   N  ASP G 207           
SHEET    4  AD 4 GLY G 180  ALA G 182 -1  O  GLY G 180   N  ILE G 168           
SHEET    1  AE 7 LEU G 295  ASN G 301  0                                        
SHEET    2  AE 7 GLY G 280  VAL G 288 -1  O  ASN G 283   N  ASN G 301           
SHEET    3  AE 7 LYS G 214  ARG G 222 -1  N  LYS G 214   O  VAL G 288           
SHEET    4  AE 7 CYS G 228  ASN G 236 -1  O  ILE G 229   N  VAL G 221           
SHEET    5  AE 7 THR G 249  ALA G 251 -1  O  VAL G 250   N  GLU G 235           
SHEET    6  AE 7 VAL G 355  ARG G 361 -1  N  VAL G 356   O  ALA G 251           
SHEET    7  AE 7 GLY G 382  GLY G 388 -1  O  GLY G 382   N  ARG G 361           
SHEET    1  AF 6 VAL G 525  ARG G 528  0                                        
SHEET    2  AF 6 TYR G 542  THR G 546 -1  N  TYR G 544   O  LYS G 527           
SHEET    3  AF 6 ARG G 615  TYR G 617  1  O  LEU G 616   N  MET G 543           
SHEET    4  AF 6 GLU G 595  VAL G 599  1  O  THR G 596   N  ARG G 615           
SHEET    5  AF 6 LYS G 561  LEU G 565  1  N  ILE G 562   O  GLU G 595           
SHEET    6  AF 6 GLY G 637  ILE G 639  1  O  GLY G 637   N  MET G 563           
SHEET    1  AG 4 ASN G 692  THR G 694  0                                        
SHEET    2  AG 4 LEU G 751  HIS G 754 -1  N  LEU G 752   O  ALA G 693           
SHEET    3  AG 4 LEU G 712  ARG G 715 -1  N  VAL G 713   O  ASP G 753           
SHEET    4  AG 4 GLU G 726  VAL G 728 -1  O  GLU G 726   N  VAL G 714           
SHEET    1  AH 7 GLU G 836  ASN G 843  0                                        
SHEET    2  AH 7 GLY G 824  LYS G 833 -1  O  ASN G 827   N  ASN G 843           
SHEET    3  AH 7 VAL G 760  CYS G 768 -1  O  VAL G 760   N  VAL G 832           
SHEET    4  AH 7 VAL G 773  HIS G 781 -1  N  LEU G 774   O  ILE G 767           
SHEET    5  AH 7 CYS G 794  LEU G 796 -1  O  SER G 795   N  GLU G 780           
SHEET    6  AH 7 TYR G 888  VAL G 894 -1  N  SER G 889   O  LEU G 796           
SHEET    7  AH 7 GLY G 915  GLY G 921 -1  O  GLY G 915   N  VAL G 894           
SHEET    1  AI 5 ARG G 989  VAL G 991  0                                        
SHEET    2  AI 5 GLU G 970  THR G 974  1  O  LEU G 971   N  ARG G 989           
SHEET    3  AI 5 ARG G 944  SER G 948  1  N  ALA G 945   O  GLU G 970           
SHEET    4  AI 5 TYR G1012  ASN G1015  1  O  TYR G1012   N  LEU G 946           
SHEET    5  AI 5 HIS G1039  ASP G1041  1  O  HIS G1039   N  ILE G1013           
SHEET    1  AJ 8 SER H   4  LEU H   9  0                                        
SHEET    2  AJ 8 GLN H  14  ALA H  19 -1  O  PHE H  15   N  LEU H   7           
SHEET    3  AJ 8 VAL H 108  ALA H 111 -1  N  ALA H 111   O  ARG H  18           
SHEET    4  AJ 8 GLY H  79  VAL H  81  1  O  LEU H  80   N  ILE H 110           
SHEET    5  AJ 8 GLN H  51  LEU H  55  1  O  GLN H  51   N  GLY H  79           
SHEET    6  AJ 8 GLY H  24  ASN H  33  1  O  GLU H  29   N  ILE H  52           
SHEET    7  AJ 8 GLN H 128  ALA H 134 -1  O  GLN H 128   N  VAL H  30           
SHEET    8  AJ 8 SER H   4  LEU H   9 -1  O  LEU H   6   N  ILE H 133           
SHEET    1  AK10 TYR H 168  TRP H 170  0                                        
SHEET    2  AK10 CYS H 214  PRO H 220 -1  N  LEU H 216   O  TRP H 170           
SHEET    3  AK10 PHE H 192  ASP H 198  1  O  PHE H 192   N  ARG H 215           
SHEET    4  AK10 GLY H 235  LEU H 238  1  O  GLY H 235   N  VAL H 195           
SHEET    5  AK10 VAL H 265  ILE H 268  1  O  PHE H 266   N  LEU H 238           
SHEET    6  AK10 ALA H 347  PHE H 350  1  N  PHE H 348   O  VAL H 265           
SHEET    7  AK10 LEU H 337  ARG H 342 -1  N  ILE H 340   O  SER H 349           
SHEET    8  AK10 LEU H 325  SER H 331 -1  N  ARG H 326   O  HIS H 341           
SHEET    9  AK10 THR H 283  ASP H 299 -1  N  LYS H 298   O  LYS H 330           
SHEET   10  AK10 VAL H 304  VAL H 316 -1  O  VAL H 304   N  ASP H 299           
LINK         O   ASP A  84                 K     K A4021     1555   1555  2.83  
LINK         OG1 THR A 114                 K     K A4021     1555   1555  2.84  
LINK         OE1 GLU A 127                 K     K A4004     1555   1555  2.93  
LINK         OE2 GLU A 215                 K     K A4003     1555   1555  2.73  
LINK         O   ASP A 238                 K     K A4003     1555   1555  2.83  
LINK         O   ILE A 242                 K     K A4003     1555   1555  2.59  
LINK         OG  SER A 247                 K     K A4003     1555   1555  2.65  
LINK         OE1 GLN A 285                MN    MN A4002     1555   1555  2.02  
LINK         OE1 GLN A 285                 K     K A4020     1555   1555  2.86  
LINK         CD  GLU A 299                MN    MN A4001     1555   1555  2.63  
LINK         OE1 GLU A 299                MN    MN A4001     1555   1555  2.33  
LINK         OE1 GLU A 299                 K     K A4004     1555   1555  2.75  
LINK         OE2 GLU A 299                MN    MN A4001     1555   1555  2.30  
LINK         OE2 GLU A 299                MN    MN A4002     1555   1555  2.22  
LINK         O   MET A 300                 K     K A4004     1555   1555  2.64  
LINK         OD1 ASN A 301                MN    MN A4001     1555   1555  1.86  
LINK         OE2 GLU A 761                 K     K A4010     1555   1555  2.72  
LINK         ND1 HIS A 781                 K     K A4010     1555   1555  2.78  
LINK         O   GLU A 783                 K     K A4010     1555   1555  2.82  
LINK         O   GLN A 784                 K     K A4010     1555   1555  2.73  
LINK         O   VAL A 787                 K     K A4010     1555   1555  2.59  
LINK         OG  SER A 792                 K     K A4010     1555   1555  2.84  
LINK         OE1 GLN A 829                MN    MN A4008     1555   1555  2.22  
LINK         OE2 GLU A 841                MN    MN A4008     1555   1555  2.23  
LINK         OE2 GLU A 841                 K     K A4009     1555   1555  2.75  
LINK         O   HIS B  16                 K     K B4019     1555   1555  2.58  
LINK         O   ASP B 112                 K     K B4019     1555   1555  2.74  
LINK         OG1 THR C 114                 K     K C4043     1555   1555  2.82  
LINK         OE1 GLU C 127                 K     K C4027     1555   1555  2.84  
LINK         OG1 THR C 143                 K     K C4044     1555   1555  2.85  
LINK         O   ALA C 144                 K     K C4044     1555   1555  2.92  
LINK         OE2 GLU C 215                 K     K C4026     1555   1555  2.69  
LINK         OD1 ASN C 236                 K     K C4026     1555   1555  2.89  
LINK         O   ASP C 238                 K     K C4026     1555   1555  2.62  
LINK         O   ALA C 239                 K     K C4026     1555   1555  2.92  
LINK         O   ILE C 242                 K     K C4026     1555   1555  2.75  
LINK         OG  SER C 247                 K     K C4026     1555   1555  2.65  
LINK         OE1 GLN C 285                 K     K C4042     1555   1555  2.64  
LINK         OE1 GLN C 285                MN    MN C4025     1555   1555  2.01  
LINK         CD  GLU C 299                MN    MN C4024     1555   1555  2.61  
LINK         OE1 GLU C 299                 K     K C4027     1555   1555  2.58  
LINK         OE1 GLU C 299                MN    MN C4024     1555   1555  2.29  
LINK         OE2 GLU C 299                MN    MN C4025     1555   1555  2.37  
LINK         OE2 GLU C 299                MN    MN C4024     1555   1555  2.27  
LINK         O   MET C 300                 K     K C4027     1555   1555  2.69  
LINK         OD1 ASN C 301                MN    MN C4024     1555   1555  2.06  
LINK         OE2 GLU C 761                 K     K C4032     1555   1555  2.70  
LINK         ND1 HIS C 781                 K     K C4032     1555   1555  2.84  
LINK         O   GLU C 783                 K     K C4032     1555   1555  2.76  
LINK         O   VAL C 787                 K     K C4032     1555   1555  2.63  
LINK         OG  SER C 792                 K     K C4032     1555   1555  2.87  
LINK         CD  GLN C 829                MN    MN C4030     1555   1555  2.88  
LINK         OE1 GLN C 829                MN    MN C4030     1555   1555  1.97  
LINK         OE2 GLU C 841                MN    MN C4030     1555   1555  2.09  
LINK         O   HIS D  16                 K     K D4041     1555   1555  2.72  
LINK         O   ASP D 112                 K     K D4041     1555   1555  2.78  
LINK         O   ASP E  84                 K     K E4065     1555   1555  2.73  
LINK         OG1 THR E 114                 K     K E4065     1555   1555  2.75  
LINK         OE1 GLU E 127                 K     K E4049     1555   1555  2.79  
LINK         OG1 THR E 143                 K     K E4066     1555   1555  2.89  
LINK         OE2 GLU E 215                 K     K E4048     1555   1555  2.49  
LINK         OE1 GLU E 217                 K     K E4064     1555   1555  2.79  
LINK         OD1 ASN E 236                 K     K E4048     1555   1555  2.69  
LINK         O   ASP E 238                 K     K E4048     1555   1555  2.80  
LINK         O   ILE E 242                 K     K E4048     1555   1555  2.66  
LINK         OG  SER E 247                 K     K E4048     1555   1555  2.78  
LINK         OE1 GLN E 285                 K     K E4064     1555   1555  2.62  
LINK         OE1 GLN E 285                MN    MN E4047     1555   1555  2.19  
LINK         CD  GLU E 299                MN    MN E4046     1555   1555  2.60  
LINK         OE1 GLU E 299                 K     K E4049     1555   1555  2.63  
LINK         OE1 GLU E 299                MN    MN E4046     1555   1555  2.34  
LINK         OE2 GLU E 299                MN    MN E4047     1555   1555  2.27  
LINK         OE2 GLU E 299                MN    MN E4046     1555   1555  2.25  
LINK         O   MET E 300                 K     K E4049     1555   1555  2.66  
LINK         OD1 ASN E 301                MN    MN E4046     1555   1555  2.16  
LINK         OE2 GLU E 761                 K     K E4054     1555   1555  2.69  
LINK         ND1 HIS E 781                 K     K E4054     1555   1555  2.84  
LINK         O   GLU E 783                 K     K E4054     1555   1555  2.86  
LINK         O   GLN E 784                 K     K E4054     1555   1555  2.77  
LINK         O   VAL E 787                 K     K E4054     1555   1555  2.48  
LINK         OG  SER E 792                 K     K E4054     1555   1555  2.76  
LINK         OE1 GLN E 829                MN    MN E4052     1555   1555  2.05  
LINK         OE2 GLU E 841                MN    MN E4052     1555   1555  2.10  
LINK         OE2 GLU E 841                 K     K E4053     1555   1555  2.91  
LINK         O   HIS F  16                 K     K F4063     1555   1555  2.77  
LINK         O   ASP F 112                 K     K F4063     1555   1555  2.85  
LINK         O   GLY G 112                 K     K G4088     1555   1555  2.80  
LINK         OE1 GLU G 127                 K     K G4072     1555   1555  2.83  
LINK         O   THR G 143                 K     K G4089     1555   1555  2.92  
LINK         OE2 GLU G 215                 K     K G4071     1555   1555  2.17  
LINK         OE1 GLU G 217                 K     K G4087     1555   1555  2.93  
LINK         O   ASP G 238                 K     K G4071     1555   1555  2.79  
LINK         O   ALA G 239                 K     K G4071     1555   1555  2.66  
LINK         O   ILE G 242                 K     K G4071     1555   1555  2.65  
LINK         OG  SER G 247                 K     K G4071     1555   1555  2.81  
LINK         OD1 ASN G 283                 K     K G4087     1555   1555  2.90  
LINK         OE1 GLN G 285                 K     K G4087     1555   1555  2.62  
LINK         OE1 GLN G 285                MN    MN G4070     1555   1555  1.95  
LINK         CD  GLU G 299                MN    MN G4069     1555   1555  2.68  
LINK         OE1 GLU G 299                 K     K G4072     1555   1555  2.84  
LINK         OE1 GLU G 299                MN    MN G4069     1555   1555  2.17  
LINK         OE2 GLU G 299                MN    MN G4070     1555   1555  2.02  
LINK         OE2 GLU G 299                MN    MN G4069     1555   1555  2.55  
LINK         O   MET G 300                 K     K G4072     1555   1555  2.93  
LINK         OD1 ASN G 301                MN    MN G4069     1555   1555  1.99  
LINK         OE2 GLU G 761                 K     K G4077     1555   1555  2.58  
LINK         ND1 HIS G 781                 K     K G4077     1555   1555  2.79  
LINK         O   GLU G 783                 K     K G4077     1555   1555  2.78  
LINK         O   GLN G 784                 K     K G4077     1555   1555  2.67  
LINK         O   VAL G 787                 K     K G4077     1555   1555  2.70  
LINK         OG  SER G 792                 K     K G4077     1555   1555  2.70  
LINK         OE1 GLN G 829                MN    MN G4075     1555   1555  2.45  
LINK         OE1 GLU G 841                 K     K G4076     1555   1555  2.84  
LINK         OE2 GLU G 841                MN    MN G4075     1555   1555  2.15  
LINK         O   ASP H 112                 K     K H4086     1555   1555  2.67  
LINK        MN    MN A4001                 O3B ADP A4000     1555   1555  2.09  
LINK        MN    MN A4001                 O   HOH A4092     1555   1555  2.04  
LINK        MN    MN A4001                 O1  PO4 A4006     1555   1555  2.08  
LINK        MN    MN A4002                 O1B ADP A4000     1555   1555  2.02  
LINK        MN    MN A4002                 O3  PO4 A4006     1555   1555  2.06  
LINK        MN    MN A4002                 O1A ADP A4000     1555   1555  2.07  
LINK        MN    MN A4002                 O   HOH A4089     1555   1555  2.03  
LINK        MN    MN A4008                 O2A ADP A4007     1555   1555  2.11  
LINK        MN    MN A4008                 O   HOH A4557     1555   1555  2.43  
LINK        MN    MN A4008                 O3B ADP A4007     1555   1555  1.98  
LINK         K     K A4009                 O2B ADP A4007     1555   1555  2.57  
LINK         K     K B4019                 O   HOH B4082     1555   1555  2.88  
LINK         K     K B4019                 O   HOH B4083     1555   1555  2.80  
LINK         K     K A4020                 O3  PO4 A4006     1555   1555  2.69  
LINK         K     K A4020                 O   HOH A4098     1555   1555  2.84  
LINK         K     K A4021                 O   HOH A4111     1555   1555  2.68  
LINK         K     K A4022                 O   HOH A4203     1555   1555  2.61  
LINK        MN    MN C4024                 O3B ADP C4023     1555   1555  2.08  
LINK        MN    MN C4024                 O1  PO4 C4028     1555   1555  2.16  
LINK        MN    MN C4024                 O   HOH C4113     1555   1555  2.11  
LINK        MN    MN C4025                 O1A ADP C4023     1555   1555  2.09  
LINK        MN    MN C4025                 O   HOH C4110     1555   1555  2.04  
LINK        MN    MN C4025                 O3  PO4 C4028     1555   1555  2.05  
LINK        MN    MN C4025                 O1B ADP C4023     1555   1555  2.27  
LINK         K     K C4027                 O   HOH C4709     1555   1555  2.61  
LINK        MN    MN C4030                 O3B ADP C4029     1555   1555  2.13  
LINK        MN    MN C4030                 O2A ADP C4029     1555   1555  2.24  
LINK        MN    MN C4030                 O   HOH C4570     1555   1555  2.45  
LINK        MN    MN C4030                 O   HOH C4571     1555   1555  2.18  
LINK        MN    MN G4069                 O   HOH G2947     1555   1555  2.46  
LINK        MN    MN G4069                 O1  PO4 G4073     1555   1555  2.02  
LINK        MN    MN G4069                 O3B ADP G4068     1555   1555  2.20  
LINK         K     K C4031                 O2B ADP C4029     1555   1555  2.72  
LINK         K     K C4031                 O   HOH C4123     1555   1555  2.79  
LINK        MN    MN G4070                 O3  PO4 G4073     1555   1555  2.04  
LINK        MN    MN G4070                 O   HOH G2944     1555   1555  2.05  
LINK        MN    MN G4070                 O1A ADP G4068     1555   1555  2.01  
LINK        MN    MN G4070                 O1B ADP G4068     1555   1555  2.23  
LINK         K     K G4072                 O   HOH G2947     1555   1555  2.83  
LINK        MN    MN G4075                 O3B ADP G4074     1555   1555  2.21  
LINK        MN    MN G4075                 O2A ADP G4074     1555   1555  2.19  
LINK         K     K G4076                 O3B ADP G4074     1555   1555  2.88  
LINK         K     K D4041                 O   HOH D1505     1555   1555  2.64  
LINK         K     K C4042                 O3  PO4 C4028     1555   1555  2.76  
LINK         K     K C4044                 O   HOH C4221     1555   1555  2.54  
LINK        MN    MN E4046                 O3B ADP E4045     1555   1555  2.12  
LINK        MN    MN E4046                 O   HOH E4144     1555   1555  1.99  
LINK        MN    MN E4046                 O1  PO4 E4050     1555   1555  2.04  
LINK         K     K H4086                 O   HOH H3435     1555   1555  2.89  
LINK        MN    MN E4047                 O1B ADP E4045     1555   1555  2.26  
LINK        MN    MN E4047                 O   HOH E4141     1555   1555  2.38  
LINK        MN    MN E4047                 O3  PO4 E4050     1555   1555  2.02  
LINK        MN    MN E4047                 O1A ADP E4045     1555   1555  2.10  
LINK         K     K G4087                 O   HOH G2953     1555   1555  2.86  
LINK         K     K G4088                 O   HOH G2968     1555   1555  2.79  
LINK         K     K E4049                 O   HOH E4145     1555   1555  2.64  
LINK         K     K G4089                 O   HOH G3058     1555   1555  2.70  
LINK        MN    MN E4052                 O2A ADP E4051     1555   1555  2.15  
LINK        MN    MN E4052                 O   HOH E4614     1555   1555  2.22  
LINK        MN    MN E4052                 O3B ADP E4051     1555   1555  2.17  
LINK        MN    MN E4052                 O   HOH E4615     1555   1555  2.62  
LINK         K     K E4053                 O   HOH E4154     1555   1555  2.54  
LINK         K     K E4053                 O2B ADP E4051     1555   1555  2.87  
LINK         K     K F4063                 O   HOH F2481     1555   1555  2.45  
LINK         K     K F4063                 O   HOH E4605     1555   1555  2.67  
LINK         K     K F4063                 O   HOH F2482     1555   1555  2.79  
LINK         K     K E4064                 O3  PO4 E4050     1555   1555  2.87  
LINK         K     K E4065                 O   HOH E4169     1555   1555  2.75  
LINK         K     K A4003                 O   ALA A 239     1555   1555  2.99  
LINK         K     K A4003                 OD1 ASN A 236     1555   1555  2.98  
LINK         K     K A4004                 O   ALA A 126     1555   1555  3.24  
LINK         K     K A4004                 O   HOH A4090     1555   1555  3.43  
LINK         K     K A4004                 O   HOH A4092     1555   1555  3.05  
LINK         K     K A4004                 O   HOH A4093     1555   1555  3.07  
LINK         K     K A4004                 OD1 ASN A 301     1555   1555  3.45  
LINK         K     K A4009                 O3B ADP A4007     1555   1555  3.24  
LINK         K     K A4009                 OE1 GLU A 841     1555   1555  3.22  
LINK         K     K A4009                 OD1 ASN A 843     1555   1555  2.93  
LINK         K     K A4020                MN    MN A4002     1555   1555  3.68  
LINK         K     K A4020                 O   HOH A4089     1555   1555  3.43  
LINK         K     K A4020                 OD1 ASN A 283     1555   1555  3.20  
LINK         K     K A4020                 OG1 THR A 244     1555   1555  3.00  
LINK         K     K A4020                 O   HOH A4097     1555   1555  3.27  
LINK         K     K A4020                 OE1 GLU A 217     1555   1555  2.95  
LINK         K     K A4021                 O   GLY A 112     1555   1555  3.00  
LINK         K     K A4021                 O   HOH A4113     1555   1555  2.98  
LINK         K     K A4022                 OG1 THR A 143     1555   1555  3.11  
LINK         K     K A4022                 O   ALA A 144     1555   1555  3.15  
LINK         K     K A4022                 O   HOH A4600     1555   1555  3.36  
LINK         K     K A4022                 O   THR A 143     1555   1555  3.24  
LINK         K     K A4022                 O   HOH A4209     1555   1555  3.56  
LINK         K     K B4019                 O   HOH A4546     1555   1555  3.18  
LINK         K     K B4019                 O   HOH A4548     1555   1555  3.26  
LINK         K     K C4027                 O   ALA C 126     1555   1555  3.43  
LINK         K     K C4027                 O   HOH C4111     1555   1555  3.54  
LINK         K     K C4027                 O   HOH C4113     1555   1555  3.11  
LINK         K     K C4027                 O   HOH C4114     1555   1555  2.94  
LINK         K     K C4027                 OD1 ASN C 301     1555   1555  3.30  
LINK         K     K C4027                MN    MN C4024     1555   1555  3.68  
LINK         K     K C4031                 OE1 GLU C 841     1555   1555  2.97  
LINK         K     K C4031                 OE2 GLU C 841     1555   1555  2.96  
LINK         K     K C4031                 OD1 ASN C 843     1555   1555  3.17  
LINK         K     K C4031                 O3B ADP C4029     1555   1555  3.29  
LINK         K     K C4032                 O   GLN C 784     1555   1555  3.06  
LINK         K     K C4042                 OE1 GLU C 217     1555   1555  3.12  
LINK         K     K C4042                 OD1 ASN C 283     1555   1555  3.30  
LINK         K     K C4042                MN    MN C4025     1555   1555  3.61  
LINK         K     K C4042                 O   HOH C4119     1555   1555  2.94  
LINK         K     K C4042                 OG1 THR C 244     1555   1555  3.41  
LINK         K     K C4042                 O   HOH C4110     1555   1555  3.67  
LINK         K     K C4042                 O   HOH C4118     1555   1555  3.57  
LINK         K     K C4043                 N   THR C 114     1555   1555  3.72  
LINK         K     K C4043                 O   GLY C 112     1555   1555  3.05  
LINK         K     K C4043                 O   HOH C4134     1555   1555  3.06  
LINK         K     K C4043                 O   ASP C  84     1555   1555  3.03  
LINK         K     K C4044                 O   THR C 143     1555   1555  3.00  
LINK         K     K C4044                 O   HOH C4241     1555   1555  3.69  
LINK         K     K C4044                 O   HOH C4226     1555   1555  3.08  
LINK         K     K D4041                 O   HOH C4561     1555   1555  3.31  
LINK         K     K D4041                 O   HOH C4558     1555   1555  3.04  
LINK         K     K D4041                 NH1AARG C 490     1555   1555  3.61  
LINK         K     K E4048                 O   ALA E 239     1555   1555  2.95  
LINK         K     K E4049                 O   ALA E 126     1555   1555  3.27  
LINK         K     K E4049                 OD1 ASN E 301     1555   1555  3.64  
LINK         K     K E4049                 O   HOH E4144     1555   1555  3.11  
LINK         K     K E4049                 O   HOH E4142     1555   1555  3.34  
LINK         K     K E4053                 O3B ADP E4051     1555   1555  3.12  
LINK         K     K E4053                 OD1 ASN E 843     1555   1555  3.08  
LINK         K     K E4053                 OE1 GLU E 841     1555   1555  2.93  
LINK         K     K E4064                 O   HOH E4149     1555   1555  3.45  
LINK         K     K E4064                 O   HOH E4150     1555   1555  2.99  
LINK         K     K E4064                 OG1 THR E 244     1555   1555  3.31  
LINK         K     K E4064                 OD1 ASN E 283     1555   1555  3.02  
LINK         K     K E4064                MN    MN E4047     1555   1555  3.63  
LINK         K     K E4065                 O   HOH E4166     1555   1555  3.05  
LINK         K     K E4065                 O   HOH E4167     1555   1555  3.38  
LINK         K     K E4065                 O   GLY E 112     1555   1555  2.93  
LINK         K     K E4066                 O   HOH E4263     1555   1555  3.09  
LINK         K     K E4066                 O   ALA E 144     1555   1555  2.98  
LINK         K     K E4066                 O   THR E 143     1555   1555  3.16  
LINK         K     K E4066                 O   HOH E4280     1555   1555  3.18  
LINK         K     K F4063                 O   HOH E4607     1555   1555  3.60  
LINK         K     K G4071                 OD1 ASN G 236     1555   1555  2.95  
LINK         K     K G4072                 O   ALA G 126     1555   1555  3.11  
LINK         K     K G4072                 O   HOH G2948     1555   1555  3.09  
LINK         K     K G4072                 O   HOH G2945     1555   1555  3.29  
LINK         K     K G4072                MN    MN G4069     1555   1555  3.71  
LINK         K     K G4072                 OD1 ASN G 301     1555   1555  3.54  
LINK         K     K G4076                 O2B ADP G4074     1555   1555  3.03  
LINK         K     K G4076                 OD1 ASN G 843     1555   1555  3.32  
LINK         K     K G4076                 OE2 GLU G 841     1555   1555  3.21  
LINK         K     K G4087                 O3  PO4 G4073     1555   1555  2.95  
LINK         K     K G4087                 O   HOH G2952     1555   1555  3.53  
LINK         K     K G4087                 OG1 THR G 244     1555   1555  3.61  
LINK         K     K G4087                 ND2 ASN G 283     1555   1555  3.65  
LINK         K     K G4088                 OG1 THR G 114     1555   1555  3.33  
LINK         K     K G4088                 O   HOH G2966     1555   1555  3.54  
LINK         K     K G4088                 O   HOH G2970     1555   1555  3.01  
LINK         K     K G4088                 O   ASP G  84     1555   1555  2.98  
LINK         K     K G4089                 O   HOH G3052     1555   1555  3.02  
LINK         K     K G4089                 O   ALA G 144     1555   1555  3.21  
LINK         K     K G4089                 OG1 THR G 143     1555   1555  2.99  
LINK         K     K H4086                 O   HOH H3432     1555   1555  3.00  
LINK         K     K H4086                 O   HIS H  16     1555   1555  3.11  
LINK         K     K H4086                 O   HOH G3434     1555   1555  3.34  
LINK         K     K H4086                 O   HOH H3661     1555   1555  3.20  
CISPEP   1 PHE A  164    PRO A  165          0        -0.82                     
CISPEP   2 ALA A  251    PRO A  252          0        -0.34                     
CISPEP   3 TYR A  710    PRO A  711          0         0.12                     
CISPEP   4 LEU A  796    PRO A  797          0         3.64                     
CISPEP   5 ARG A  998    PRO A  999          0        -2.56                     
CISPEP   6 SER B  357    PRO B  358          0         3.02                     
CISPEP   7 PHE C  164    PRO C  165          0        -2.33                     
CISPEP   8 ALA C  251    PRO C  252          0         2.02                     
CISPEP   9 TYR C  710    PRO C  711          0         3.72                     
CISPEP  10 LEU C  796    PRO C  797          0         2.73                     
CISPEP  11 ARG C  998    PRO C  999          0        -6.68                     
CISPEP  12 SER D  357    PRO D  358          0         4.51                     
CISPEP  13 PHE E  164    PRO E  165          0         0.24                     
CISPEP  14 ALA E  251    PRO E  252          0        -2.32                     
CISPEP  15 TYR E  710    PRO E  711          0         3.32                     
CISPEP  16 LEU E  796    PRO E  797          0         3.30                     
CISPEP  17 ARG E  998    PRO E  999          0        -2.51                     
CISPEP  18 SER F  357    PRO F  358          0         3.22                     
CISPEP  19 PHE G  164    PRO G  165          0         0.12                     
CISPEP  20 ALA G  251    PRO G  252          0        -0.31                     
CISPEP  21 TYR G  710    PRO G  711          0         1.76                     
CISPEP  22 LEU G  796    PRO G  797          0         2.76                     
CISPEP  23 ARG G  998    PRO G  999          0         2.87                     
CISPEP  24 SER H  357    PRO H  358          0         2.64                     
SITE     1 AC1  6 GLU A 299  ASN A 301  ADP A4000   MN A4002                    
SITE     2 AC1  6 PO4 A4006  HOH A4092                                          
SITE     1 AC2  7 GLN A 285  GLU A 299  ADP A4000   MN A4001                    
SITE     2 AC2  7 PO4 A4006    K A4020  HOH A4089                               
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  7 ALA A 126  GLU A 127  GLU A 299  MET A 300                    
SITE     2 AC4  7 ASN A 301  HOH A4092  HOH A4093                               
SITE     1 AC5  4 GLN A 829  GLU A 841  ADP A4007  HOH A4557                    
SITE     1 AC6  3 GLU A 841  ASN A 843  ADP A4007                               
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 A4028                    
SITE     2 AC8  5 HOH A4031                                                     
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  2 ASP B 114  HOH B4081                                          
SITE     1 BC3  4 HIS B  16  ASP B 112  HOH B4082  HOH B4083                    
SITE     1 BC4  7 GLU A 217  THR A 244  ASN A 283  GLN A 285                    
SITE     2 BC4  7  MN A4002  PO4 A4006  HOH A4098                               
SITE     1 BC5  5 ASP A  84  GLY A 112  THR A 114  HOH A4111                    
SITE     2 BC5  5 HOH A4113                                                     
SITE     1 BC6  3 THR A 143  ALA A 144  HOH A4203                               
SITE     1 BC7  6 GLU C 299  ASN C 301  ADP C4023    K C4027                    
SITE     2 BC7  6 PO4 C4028  HOH C4113                                          
SITE     1 BC8  6 GLN C 285  GLU C 299  ADP C4023  PO4 C4028                    
SITE     2 BC8  6   K C4042  HOH C4110                                          
SITE     1 BC9  6 GLU C 215  ASN C 236  ASP C 238  ALA C 239                    
SITE     2 BC9  6 ILE C 242  SER C 247                                          
SITE     1 CC1  8 ALA C 126  GLU C 127  GLU C 299  MET C 300                    
SITE     2 CC1  8 ASN C 301   MN C4024  HOH C4114  HOH C4709                    
SITE     1 CC2  3 THR E 143  ALA E 144  HOH E4263                               
SITE     1 CC3  5 GLN C 829  GLU C 841  ADP C4029  HOH C4570                    
SITE     2 CC3  5 HOH C4571                                                     
SITE     1 CC4  6 GLU G 299  ASN G 301  HOH G2947  ADP G4068                    
SITE     2 CC4  6  MN G4070  PO4 G4073                                          
SITE     1 CC5  4 GLU C 841  ASN C 843  ADP C4029  HOH C4123                    
SITE     1 CC6  6 GLN G 285  GLU G 299  HOH G2944  ADP G4068                    
SITE     2 CC6  6  MN G4069  PO4 G4073                                          
SITE     1 CC7  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784                    
SITE     2 CC7  6 VAL C 787  SER C 792                                          
SITE     1 CC8  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239                    
SITE     2 CC8  6 ILE G 242  SER G 247                                          
SITE     1 CC9  3 THR C 173  MET C 174  HOH C4050                               
SITE     1 DC1  7 ALA G 126  GLU G 127  GLU G 299  MET G 300                    
SITE     2 DC1  7 ASN G 301  HOH G2947  HOH G2948                               
SITE     1 DC2  3 ASN C 289  ASN C 292  ARG C 294                               
SITE     1 DC3  3 GLN G 829  GLU G 841  ADP G4074                               
SITE     1 DC4  4 ASN C 371  PHE C 900  PRO C 901  GLY C 902                    
SITE     1 DC5  3 GLU G 841  ASN G 843  ADP G4074                               
SITE     1 DC6  3 GLU C 549  ASP D 114  HOH D1501                               
SITE     1 DC7  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784                    
SITE     2 DC7  6 VAL G 787  SER G 792                                          
SITE     1 DC8  5 ARG C 490  HOH C4558  HIS D  16  ASP D 112                    
SITE     2 DC8  5 HOH D1505                                                     
SITE     1 DC9  4 GLN G  93  THR G 173  MET G 174  HOH G2879                    
SITE     1 EC1  7 GLU C 217  THR C 244  ASN C 283  GLN C 285                    
SITE     2 EC1  7  MN C4025  PO4 C4028  HOH C4119                               
SITE     1 EC2  3 ASN G 289  ASN G 292  ARG G 294                               
SITE     1 EC3  4 ASP C  84  GLY C 112  THR C 114  HOH C4134                    
SITE     1 EC4  3 ASN G 371  PRO G 901  GLY G 902                               
SITE     1 EC5  4 THR C 143  ALA C 144  HOH C4221  HOH C4226                    
SITE     1 EC6  2 PHE H  15  ASP H 114                                          
SITE     1 EC7  6 GLU E 299  ASN E 301  ADP E4045   MN E4047                    
SITE     2 EC7  6 PO4 E4050  HOH E4144                                          
SITE     1 EC8  4 HIS H  16  ASP H 112  HOH H3432  HOH H3435                    
SITE     1 EC9  7 GLN E 285  GLU E 299  ADP E4045   MN E4046                    
SITE     2 EC9  7 PO4 E4050    K E4064  HOH E4141                               
SITE     1 FC1  6 GLU G 217  THR G 244  ASN G 283  GLN G 285                    
SITE     2 FC1  6 HOH G2953  PO4 G4073                                          
SITE     1 FC2  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239                    
SITE     2 FC2  6 ILE E 242  SER E 247                                          
SITE     1 FC3  5 ASP G  84  GLY G 112  THR G 114  HOH G2968                    
SITE     2 FC3  5 HOH G2970                                                     
SITE     1 FC4  6 ALA E 126  GLU E 127  GLU E 299  MET E 300                    
SITE     2 FC4  6 ASN E 301  HOH E4145                                          
SITE     1 FC5  4 THR G 143  ALA G 144  HOH G3052  HOH G3058                    
SITE     1 FC6  5 GLN E 829  GLU E 841  ADP E4051  HOH E4614                    
SITE     2 FC6  5 HOH E4615                                                     
SITE     1 FC7  4 GLU E 841  ASN E 843  ADP E4051  HOH E4154                    
SITE     1 FC8  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784                    
SITE     2 FC8  6 VAL E 787  SER E 792                                          
SITE     1 FC9  5 GLN E  93  THR E 173  MET E 174  HOH E4080                    
SITE     2 FC9  5 HOH E4083                                                     
SITE     1 GC1  3 ASN E 289  ASN E 292  ARG E 294                               
SITE     1 GC2  4 ASN E 371  PHE E 900  PRO E 901  GLY E 902                    
SITE     1 GC3  5 GLU E 549  HOH E4605  PHE F  15  ASP F 114                    
SITE     2 GC3  5 HOH F2477                                                     
SITE     1 GC4  5 HOH E4605  HIS F  16  ASP F 112  HOH F2481                    
SITE     2 GC4  5 HOH F2482                                                     
SITE     1 GC5  7 GLU E 217  THR E 244  ASN E 283  GLN E 285                    
SITE     2 GC5  7  MN E4047  PO4 E4050  HOH E4150                               
SITE     1 GC6  5 ASP E  84  GLY E 112  THR E 114  HOH E4166                    
SITE     2 GC6  5 HOH E4169                                                     
SITE     1 GC7 13 MET E 174  GLY E 175  HIS E 243  GLN E 285                    
SITE     2 GC7 13 GLU E 299  ASN E 301  ARG E 303  ARG E 306                    
SITE     3 GC7 13 ADP E4045   MN E4046   MN E4047    K E4064                    
SITE     4 GC7 13 HOH E4150                                                     
SITE     1 GC8  1 GLU E 560                                                     
SITE     1 GC9 14 MET G 174  GLY G 175  HIS G 243  GLN G 285                    
SITE     2 GC9 14 GLU G 299  ASN G 301  ARG G 303  ARG G 306                    
SITE     3 GC9 14 HOH G2944  HOH G2953  ADP G4068   MN G4069                    
SITE     4 GC9 14  MN G4070    K G4087                                          
SITE     1 HC1 14 MET A 174  GLY A 175  HIS A 243  GLN A 285                    
SITE     2 HC1 14 GLU A 299  ASN A 301  ARG A 303  ARG A 306                    
SITE     3 HC1 14 ADP A4000   MN A4001   MN A4002    K A4020                    
SITE     4 HC1 14 HOH A4089  HOH A4098                                          
SITE     1 HC2 15 MET C 174  GLY C 175  HIS C 243  GLN C 285                    
SITE     2 HC2 15 GLU C 299  ASN C 301  ARG C 303  ARG C 306                    
SITE     3 HC2 15 ADP C4023   MN C4024   MN C4025    K C4042                    
SITE     4 HC2 15 HOH C4110  HOH C4119  HOH C4120                               
SITE     1 HC3 10 GLU C 783  ASP C 791  GLU C 892  LEU C 907                    
SITE     2 HC3 10 TYR C1040  ASP C1041  THR C1042  HOH C4075                    
SITE     3 HC3 10 HOH C4077  HOH C4105                                          
SITE     1 HC4 13 SER D  47  ASN D 240  GLY D 241  GLY D 243                    
SITE     2 HC4 13 SER D 269  LEU D 270  GLN D 273  ASN D 311                    
SITE     3 HC4 13 HIS D 312  GLY D 313  PHE D 314  HIS D 353                    
SITE     4 HC4 13 HOH D 995                                                     
SITE     1 HC5 11 ARG C 528  ALA C 537  THR C 538  GLU C 552                    
SITE     2 HC5 11 ASN C 554  HOH C4450  HOH C4451  HOH C4456                    
SITE     3 HC5 11 HOH C4566  ARG D 120  ARG D 123                               
SITE     1 HC6  4 GLN C  22  THR C  94  ASN C  97  ASN C 936                    
SITE     1 HC7 27 ARG E 129  ILE E 167  ARG E 169  THR E 173                    
SITE     2 HC7 27 MET E 174  GLY E 175  GLY E 176  GLU E 208                    
SITE     3 HC7 27 LEU E 210  ILE E 211  GLU E 215  MET E 240                    
SITE     4 HC7 27 GLY E 241  ILE E 242  HIS E 243  THR E 244                    
SITE     5 HC7 27 GLN E 285  ILE E 298  GLU E 299  THR E 376                    
SITE     6 HC7 27  MN E4046   MN E4047  PO4 E4050  HOH E4137                    
SITE     7 HC7 27 HOH E4141  HOH E4144  HOH E4613                               
SITE     1 HC8 20 PRO E 690  ARG E 715  MET E 725  HIS E 754                    
SITE     2 HC8 20 PHE E 755  LEU E 756  GLU E 761  ALA E 785                    
SITE     3 HC8 20 GLY E 786  VAL E 787  HIS E 788  SER E 789                    
SITE     4 HC8 20 GLN E 829  GLU E 841   MN E4052    K E4053                    
SITE     5 HC8 20 HOH E4153  HOH E4154  HOH E4156  HOH E4614                    
SITE     1 HC9 10 GLU E 783  ASP E 791  GLU E 892  LEU E 907                    
SITE     2 HC9 10 TYR E1040  ASP E1041  THR E1042  HOH E4105                    
SITE     3 HC9 10 HOH E4136  HOH E4616                                          
SITE     1 IC1 13 SER F  47  ASN F 240  GLY F 241  PRO F 242                    
SITE     2 IC1 13 GLY F 243  SER F 269  LEU F 270  GLN F 273                    
SITE     3 IC1 13 ASN F 311  HIS F 312  GLY F 313  PHE F 314                    
SITE     4 IC1 13 HOH F1956                                                     
SITE     1 IC2 11 ARG E 528  ALA E 537  THR E 538  GLU E 552                    
SITE     2 IC2 11 ASN E 554  HOH E4492  HOH E4493  HOH E4720                    
SITE     3 IC2 11 HOH E4721  ARG F 120  ARG F 123                               
SITE     1 IC3  3 GLN E  22  THR E  94  ASN E 936                               
SITE     1 IC4 24 ARG G 129  ILE G 167  ARG G 169  THR G 173                    
SITE     2 IC4 24 MET G 174  GLY G 175  GLY G 176  GLU G 208                    
SITE     3 IC4 24 LEU G 210  ILE G 211  GLU G 215  MET G 240                    
SITE     4 IC4 24 GLY G 241  ILE G 242  HIS G 243  THR G 244                    
SITE     5 IC4 24 GLN G 285  GLU G 299  HOH G2940  HOH G2944                    
SITE     6 IC4 24 HOH G3549   MN G4069   MN G4070  PO4 G4073                    
SITE     1 IC5 15 ARG G 715  MET G 725  HIS G 754  PHE G 755                    
SITE     2 IC5 15 LEU G 756  GLU G 761  ALA G 785  GLY G 786                    
SITE     3 IC5 15 VAL G 787  HIS G 788  SER G 789  GLN G 829                    
SITE     4 IC5 15 GLU G 841   MN G4075    K G4076                               
SITE     1 IC6 10 GLU G 783  ASP G 791  GLU G 892  VAL G 893                    
SITE     2 IC6 10 LEU G 907  TYR G1040  ASP G1041  THR G1042                    
SITE     3 IC6 10 HOH G2901  HOH G2932                                          
SITE     1 IC7 26 ARG A 129  ILE A 167  ARG A 169  MET A 174                    
SITE     2 IC7 26 GLY A 175  GLY A 176  GLU A 208  LEU A 210                    
SITE     3 IC7 26 ILE A 211  GLU A 215  MET A 240  GLY A 241                    
SITE     4 IC7 26 ILE A 242  HIS A 243  THR A 244  GLN A 285                    
SITE     5 IC7 26 ILE A 298  GLU A 299  THR A 376   MN A4001                    
SITE     6 IC7 26  MN A4002  PO4 A4006  HOH A4085  HOH A4089                    
SITE     7 IC7 26 HOH A4092  HOH A4556                                          
SITE     1 IC8 15 SER H  47  ASN H 240  GLY H 241  PRO H 242                    
SITE     2 IC8 15 GLY H 243  SER H 269  LEU H 270  GLN H 273                    
SITE     3 IC8 15 ASN H 311  HIS H 312  GLY H 313  PHE H 314                    
SITE     4 IC8 15 HIS H 353  HOH H2934  HOH H2938                               
SITE     1 IC9  8 ARG G 528  ALA G 537  THR G 538  GLU G 552                    
SITE     2 IC9  8 ASN G 554  HOH G3308  ARG H 120  ARG H 123                    
SITE     1 JC1 18 PRO A 690  ARG A 715  MET A 725  HIS A 754                    
SITE     2 JC1 18 PHE A 755  LEU A 756  GLU A 761  ALA A 785                    
SITE     3 JC1 18 GLY A 786  VAL A 787  HIS A 788  SER A 789                    
SITE     4 JC1 18 GLN A 829  GLU A 841   MN A4008    K A4009                    
SITE     5 JC1 18 HOH A4103  HOH A4557                                          
SITE     1 JC2  3 VAL G  19  THR G  94  ASN G  97                               
SITE     1 JC3 10 GLU A 783  ASP A 791  GLU A 892  LEU A 895                    
SITE     2 JC3 10 LEU A 907  TYR A1040  ASP A1041  THR A1042                    
SITE     3 JC3 10 HOH A4053  HOH A4084                                          
SITE     1 JC4 15 SER B  47  ASN B 240  GLY B 241  PRO B 242                    
SITE     2 JC4 15 GLY B 243  SER B 269  LEU B 270  GLN B 273                    
SITE     3 JC4 15 ASN B 311  HIS B 312  GLY B 313  PHE B 314                    
SITE     4 JC4 15 HIS B 353  HOH B4021  HOH B4025                               
SITE     1 JC5 10 ARG A 528  ALA A 537  THR A 538  GLU A 552                    
SITE     2 JC5 10 ASN A 554  HOH A4436  HOH A4437  HOH A4561                    
SITE     3 JC5 10 ARG B 120  ARG B 123                                          
SITE     1 JC6  3 GLN A  22  THR A  94  ASN A 936                               
SITE     1 JC7 27 ARG C 129  ILE C 167  ARG C 169  THR C 173                    
SITE     2 JC7 27 MET C 174  GLY C 175  GLY C 176  GLU C 208                    
SITE     3 JC7 27 LEU C 210  ILE C 211  GLU C 215  MET C 240                    
SITE     4 JC7 27 GLY C 241  ILE C 242  HIS C 243  THR C 244                    
SITE     5 JC7 27 GLN C 285  ILE C 298  GLU C 299  THR C 376                    
SITE     6 JC7 27  MN C4024   MN C4025  PO4 C4028  HOH C4106                    
SITE     7 JC7 27 HOH C4110  HOH C4113  HOH C4567                               
SITE     1 JC8 20 PRO C 690  ARG C 715  MET C 725  HIS C 754                    
SITE     2 JC8 20 PHE C 755  LEU C 756  GLU C 761  ALA C 785                    
SITE     3 JC8 20 GLY C 786  VAL C 787  HIS C 788  SER C 789                    
SITE     4 JC8 20 GLN C 829  GLU C 841   MN C4030    K C4031                    
SITE     5 JC8 20 HOH C4122  HOH C4123  HOH C4570  HOH C4571                    
CRYST1  152.500  164.400  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      0.006557  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006083  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003007        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system