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Database: PDB
Entry: 1C30
LinkDB: 1C30
Original site: 1C30 
HEADER    LIGASE                                  24-JUL-99   1C30              
TITLE     CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT    
TITLE    2 MUTATION C269S                                                       
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, ATP-GRASP, SUBSTRATE CHANNELING, LIGASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN                             
REVDAT   6   14-MAR-18 1C30    1       SEQADV                                   
REVDAT   5   13-JUL-11 1C30    1       VERSN                                    
REVDAT   4   24-FEB-09 1C30    1       VERSN                                    
REVDAT   3   01-APR-03 1C30    1       JRNL                                     
REVDAT   2   26-SEP-01 1C30    1       SHEET                                    
REVDAT   1   10-DEC-99 1C30    0                                                
JRNL        AUTH   J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN                    
JRNL        TITL   THE SMALL SUBUNIT OF CARBAMOYL PHOSPHATE SYNTHETASE:         
JRNL        TITL 2 SNAPSHOTS ALONG THE REACTION PATHWAY.                        
JRNL        REF    BIOCHEMISTRY                  V.  38 16158 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10587438                                                     
JRNL        DOI    10.1021/BI991741J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT 5E                                               
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 546635                         
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) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 54664                           
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) : 546635                 
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          : 376                                     
REMARK   3   SOLVENT ATOMS            : 3987                                    
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.012 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.260 ; 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 1C30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000009393.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-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) : 0.70849                            
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   : 546635                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100                            
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   (%): 62.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASSIUM CHLORIDE,            
REMARK 280  MANGANESE CHLORIDE, TETRAETHYLAMMONIUM CHLORIDE, L-ORNITHINE,       
REMARK 280  ADP, BERYLLIUM FLUORIDE, HEPPS, PH 7.4, BATCH, TEMPERATURE 277.0K   
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       76.30000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      166.35000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       82.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      166.35000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       82.30000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 47500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 47000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   717                                                      
REMARK 465     TYR A   718                                                      
REMARK 465     VAL A   719                                                      
REMARK 465     LEU A   720                                                      
REMARK 465     GLY A   721                                                      
REMARK 465     GLY A   722                                                      
REMARK 465     ARG A   723                                                      
REMARK 465     VAL A   742                                                      
REMARK 465     SER A   743                                                      
REMARK 465     VAL A   744                                                      
REMARK 465     SER A   745                                                      
REMARK 465     ASN A   746                                                      
REMARK 465     ASP A   747                                                      
REMARK 465     ALA A   748                                                      
REMARK 465     PRO A   749                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   381                                                      
REMARK 465     LYS B   382                                                      
REMARK 465     SER C   717                                                      
REMARK 465     TYR C   718                                                      
REMARK 465     VAL C   719                                                      
REMARK 465     LEU C   720                                                      
REMARK 465     GLY C   721                                                      
REMARK 465     GLY C   722                                                      
REMARK 465     ARG C   723                                                      
REMARK 465     VAL C   742                                                      
REMARK 465     SER C   743                                                      
REMARK 465     VAL C   744                                                      
REMARK 465     SER C   745                                                      
REMARK 465     ASN C   746                                                      
REMARK 465     ASP C   747                                                      
REMARK 465     ALA C   748                                                      
REMARK 465     PRO C   749                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D   381                                                      
REMARK 465     LYS D   382                                                      
REMARK 465     SER E   717                                                      
REMARK 465     TYR E   718                                                      
REMARK 465     VAL E   719                                                      
REMARK 465     LEU E   720                                                      
REMARK 465     GLY E   721                                                      
REMARK 465     GLY E   722                                                      
REMARK 465     ARG E   723                                                      
REMARK 465     VAL E   742                                                      
REMARK 465     SER E   743                                                      
REMARK 465     VAL E   744                                                      
REMARK 465     SER E   745                                                      
REMARK 465     ASN E   746                                                      
REMARK 465     ASP E   747                                                      
REMARK 465     ALA E   748                                                      
REMARK 465     PRO E   749                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F   381                                                      
REMARK 465     LYS F   382                                                      
REMARK 465     SER G   717                                                      
REMARK 465     TYR G   718                                                      
REMARK 465     VAL G   719                                                      
REMARK 465     LEU G   720                                                      
REMARK 465     GLY G   721                                                      
REMARK 465     GLY G   722                                                      
REMARK 465     ARG G   723                                                      
REMARK 465     VAL G   742                                                      
REMARK 465     SER G   743                                                      
REMARK 465     VAL G   744                                                      
REMARK 465     SER G   745                                                      
REMARK 465     ASN G   746                                                      
REMARK 465     ASP G   747                                                      
REMARK 465     ALA G   748                                                      
REMARK 465     PRO G   749                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ALA H   381                                                      
REMARK 465     LYS H   382                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A 716    CG   CD                                             
REMARK 470     PRO C 716    CG   CD                                             
REMARK 470     PRO E 716    CG   CD                                             
REMARK 470     PRO G 716    CG   CD                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  4295     O    HOH A  4753              1.89            
REMARK 500   NH1  ARG C   559     O    HOH C  4442              2.09            
REMARK 500   O    HOH A  4246     O    HOH A  4743              2.11            
REMARK 500   O    HOH F  2857     O    HOH F  3122              2.12            
REMARK 500   OE2  GLU C  1009     O    HOH C  4707              2.14            
REMARK 500   O    HOH G  4602     O    HOH G  4721              2.14            
REMARK 500   O    HOH G  4585     O    HOH G  4738              2.16            
REMARK 500   O    HOH G  4708     O    HOH G  4709              2.18            
REMARK 500   O    HOH E  4575     O    HOH E  4832              2.18            
REMARK 500   O    HOH A  4637     O    HOH E  4068              2.18            
REMARK 500   O    ILE G   148     O    HOH G  4640              2.19            
REMARK 500   O    HOH H  3678     O    HOH H  3965              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  25   CD    GLU A  25   OE2     0.070                       
REMARK 500    GLU A  59   CD    GLU A  59   OE2     0.067                       
REMARK 500    GLU A  81   CD    GLU A  81   OE2     0.070                       
REMARK 500    GLU A 109   CD    GLU A 109   OE2     0.072                       
REMARK 500    GLU A 110   CD    GLU A 110   OE2     0.066                       
REMARK 500    GLU A 153   CD    GLU A 153   OE2     0.077                       
REMARK 500    GLU A 217   CD    GLU A 217   OE2     0.077                       
REMARK 500    GLU A 235   CD    GLU A 235   OE2     0.070                       
REMARK 500    GLU A 365   CD    GLU A 365   OE2     0.069                       
REMARK 500    GLU A 427   CD    GLU A 427   OE2     0.068                       
REMARK 500    GLU A 467   CD    GLU A 467   OE2     0.067                       
REMARK 500    GLU A 478   CD    GLU A 478   OE2     0.069                       
REMARK 500    GLU A 510   CD    GLU A 510   OE2     0.070                       
REMARK 500    GLU A 512   CD    GLU A 512   OE2     0.083                       
REMARK 500    GLU A 560   CD    GLU A 560   OE2     0.071                       
REMARK 500    GLU A 591   CD    GLU A 591   OE2     0.072                       
REMARK 500    GLU A 604   CD    GLU A 604   OE2     0.072                       
REMARK 500    GLU A 655   CD    GLU A 655   OE2     0.072                       
REMARK 500    GLU A 676   CD    GLU A 676   OE2     0.067                       
REMARK 500    GLU A 683   CD    GLU A 683   OE2     0.072                       
REMARK 500    GLU A 699   CD    GLU A 699   OE2     0.073                       
REMARK 500    GLU A 703   CD    GLU A 703   OE2     0.076                       
REMARK 500    GLU A 707   CD    GLU A 707   OE2     0.066                       
REMARK 500    GLU A 726   CD    GLU A 726   OE2     0.070                       
REMARK 500    GLU A 771   CD    GLU A 771   OE2     0.067                       
REMARK 500    GLU A 836   CD    GLU A 836   OE2     0.068                       
REMARK 500    TYR A 838   CZ    TYR A 838   CE2     0.099                       
REMARK 500    GLU A 841   CD    GLU A 841   OE2     0.071                       
REMARK 500    GLU A 882   CD    GLU A 882   OE2     0.074                       
REMARK 500    GLU A 910   CD    GLU A 910   OE2     0.070                       
REMARK 500    GLU A 916   CD    GLU A 916   OE2     0.067                       
REMARK 500    GLU A 955   CD    GLU A 955   OE2     0.076                       
REMARK 500    GLU A 970   CD    GLU A 970   OE2     0.070                       
REMARK 500    GLU A 983   CD    GLU A 983   OE2     0.069                       
REMARK 500    GLU A1009   CD    GLU A1009   OE2     0.078                       
REMARK 500    GLU A1024   CD    GLU A1024   OE2     0.067                       
REMARK 500    GLU B  29   CD    GLU B  29   OE2     0.070                       
REMARK 500    GLU B  70   CD    GLU B  70   OE2     0.072                       
REMARK 500    GLU B  96   CD    GLU B  96   OE2     0.074                       
REMARK 500    GLU B 145   CD    GLU B 145   OE2     0.073                       
REMARK 500    GLU B 166   CD    GLU B 166   OE2     0.075                       
REMARK 500    GLU B 226   CD    GLU B 226   OE2     0.070                       
REMARK 500    GLU B 318   CD    GLU B 318   OE2     0.068                       
REMARK 500    GLU B 372   CD    GLU B 372   OE2     0.079                       
REMARK 500    GLU C  39   CD    GLU C  39   OE2     0.077                       
REMARK 500    GLU C  40   CD    GLU C  40   OE1    -0.071                       
REMARK 500    GLU C  40   CD    GLU C  40   OE2     0.113                       
REMARK 500    GLU C  59   CD    GLU C  59   OE2     0.087                       
REMARK 500    GLU C  67   CD    GLU C  67   OE1    -0.070                       
REMARK 500    GLU C  67   CD    GLU C  67   OE2     0.077                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     180 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A   6   CB  -  CG  -  OD2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG A  38   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP A  62   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  84   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 133   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP A 197   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 197   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 258   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 265   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 294   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    TYR A 330   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 333   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 333   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 343   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 343   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP A 353   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 353   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A 400   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ASP A 410   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 410   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A 416   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 426   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A 459   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 490   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 490   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG A 514   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 518   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 539   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP A 579   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 579   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A 592   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ASP A 670   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 670   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 671   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 671   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 674   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    PRO A 716   N   -  CA  -  CB  ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ASP A 733   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 736   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     371 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    PRO A   2     -159.34    -85.33                                   
REMARK 500    ALA A  23     -148.71   -110.57                                   
REMARK 500    ALA A  52       34.02    -86.25                                   
REMARK 500    ARG A  82       73.64     44.72                                   
REMARK 500    ASP A 226       10.80     80.51                                   
REMARK 500    ARG A 303     -176.86   -176.16                                   
REMARK 500    ASP A 353       46.12   -109.96                                   
REMARK 500    ASN A 363       38.25   -145.72                                   
REMARK 500    THR A 375     -156.37   -146.60                                   
REMARK 500    THR A 531       -9.87     71.59                                   
REMARK 500    ALA A 541       76.89   -116.52                                   
REMARK 500    ASN A 554       63.83     39.65                                   
REMARK 500    ASP A 558      -82.43    -57.53                                   
REMARK 500    CYS A 601       20.71   -140.52                                   
REMARK 500    THR A 646      -72.16    -49.98                                   
REMARK 500    ALA A 693      128.74    171.61                                   
REMARK 500    MET A 725      132.94   -173.52                                   
REMARK 500    THR A 800      -10.45   -145.57                                   
REMARK 500    ARG A 845     -175.47   -172.20                                   
REMARK 500    HIS A 975      -80.33    -30.40                                   
REMARK 500    GLU B  96      132.38   -170.43                                   
REMARK 500    CYS B 248       48.68    -89.56                                   
REMARK 500    SER B 269     -109.05     52.53                                   
REMARK 500    ASN B 311       77.35   -153.01                                   
REMARK 500    ALA B 356     -122.70     43.33                                   
REMARK 500    PRO C   2     -160.64    -69.81                                   
REMARK 500    ALA C  23     -149.28   -108.63                                   
REMARK 500    ALA C  52       48.02    -96.03                                   
REMARK 500    ALA C 239     -177.66    -66.48                                   
REMARK 500    ASN C 292        7.81   -151.64                                   
REMARK 500    ILE C 298      -61.32    -96.05                                   
REMARK 500    ASP C 338      -70.20    -42.87                                   
REMARK 500    ASN C 363       42.75   -144.71                                   
REMARK 500    ALA C 368      -66.39    -23.76                                   
REMARK 500    THR C 375     -155.16   -147.58                                   
REMARK 500    THR C 531      -13.61     76.13                                   
REMARK 500    ALA C 541       72.47   -107.99                                   
REMARK 500    GLU C 548     -154.16   -134.72                                   
REMARK 500    THR C 696      -50.08   -123.51                                   
REMARK 500    ILE C 698      -78.90    -39.67                                   
REMARK 500    ARG C 736      -62.89    -22.69                                   
REMARK 500    GLN C 739      -72.82    -62.17                                   
REMARK 500    ASP C 758       38.03     34.14                                   
REMARK 500    HIS C 788      140.89    -39.95                                   
REMARK 500    THR C 800      -11.76   -141.57                                   
REMARK 500    ASN C 835       19.57     52.98                                   
REMARK 500    PRO C 844       52.67    -66.37                                   
REMARK 500    SER C 948       89.49   -159.97                                   
REMARK 500    HIS C 975      -73.48    -26.68                                   
REMARK 500    SER D 269     -109.21     61.47                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     117 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     ORN A 4030                                                       
REMARK 610     ORN A 4051                                                       
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 A4018   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  84   O                                                      
REMARK 620 2 GLY A 112   O    75.4                                              
REMARK 620 3 THR A 114   OG1  76.6 109.9                                        
REMARK 620 4 HOH A4158   O   103.2  92.4 156.5                                  
REMARK 620 5 HOH A4156   O   123.1 161.5  77.4  83.6                            
REMARK 620 N                    1     2     3     4                             
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 ASN A 236   OD1  83.8                                              
REMARK 620 3 ASP A 238   O   121.8  92.1                                        
REMARK 620 4 ILE A 242   O    86.0 119.8 140.9                                  
REMARK 620 5 SER A 247   OG  139.5  81.3  96.2  69.7                            
REMARK 620 6 ALA A 239   O    90.0 152.9  68.9  85.9 118.7                      
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  78.3                                              
REMARK 620 3 ADP A4000   O1B 176.5  98.3                                        
REMARK 620 4 PO4 A4005   O3   90.6  86.2  88.5                                  
REMARK 620 5 ADP A4000   O1A  93.0  84.7  87.3 169.3                            
REMARK 620 6 HOH A4136   O    87.1 165.0  96.4  97.5  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4017   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 285   OE1                                                    
REMARK 620 2 HOH A4145   O   137.1                                              
REMARK 620 3 ASN A 283   OD1  73.8  84.0                                        
REMARK 620 4 PO4 A4005   O3   59.6  84.4  89.3                                  
REMARK 620 5 THR A 244   OG1  91.5 111.5 164.0  88.3                            
REMARK 620 6 HOH A4144   O   137.3  61.7 144.7  94.9  51.3                      
REMARK 620 7 GLU A 217   OE1 118.6  99.3  95.3 174.3  86.3  83.2                
REMARK 620 8 ASN A 283   ND2 104.3  75.6  37.7 124.0 147.6 118.4  61.3          
REMARK 620 N                    1     2     3     4     5     6     7           
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  28.0                                              
REMARK 620 3 GLU A 299   OE2  30.4  58.3                                        
REMARK 620 4 ASN A 301   CG   84.3  90.7  78.8                                  
REMARK 620 5 ASN A 301   OD1  93.5  90.4  95.8  20.2                            
REMARK 620 6 ADP A4000   O3B  84.3  81.7  88.7 167.5 167.1                      
REMARK 620 7 HOH A4139   O   124.2  96.4 154.2  97.9  77.8  92.9                
REMARK 620 8 PO4 A4005   O1  123.6 151.4  93.3  79.3  89.1 102.8 111.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4004   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 299   OE1                                                    
REMARK 620 2 MET A 300   O    96.1                                              
REMARK 620 3 ALA A 126   O   140.5  83.0                                        
REMARK 620 4 GLU A 127   OE1 130.7  89.3  88.8                                  
REMARK 620 5 HOH A4137   O   104.2 159.5  83.3  75.3                            
REMARK 620 6 HOH A4139   O    68.2 122.7 143.3  67.8  64.1                      
REMARK 620 7 HOH A4140   O    92.1  66.9  51.2 134.0 114.7 158.1                
REMARK 620 8 ASN A 301   OD1  57.8  77.1 155.0  76.1 111.2  47.3 130.0          
REMARK 620 N                    1     2     3     4     5     6     7           
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 761   OE2                                                    
REMARK 620 2 HIS A 781   ND1  78.4                                              
REMARK 620 3 GLU A 783   O   133.0  94.0                                        
REMARK 620 4 GLN A 784   O    95.8 146.8  66.0                                  
REMARK 620 5 VAL A 787   O    74.1 123.8 139.7  84.4                            
REMARK 620 6 SER A 792   OG  127.2  85.2  97.6 122.1  74.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A4007  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 829   OE1                                                    
REMARK 620 2 GLU A 841   OE2  88.9                                              
REMARK 620 3 ADP A4006   O2A  95.5  90.8                                        
REMARK 620 4 HOH A4580   O    91.9 176.2  92.8                                  
REMARK 620 5 ADP A4006   O3B 177.7  89.4  83.0  90.0                            
REMARK 620 6 HOH A4850   O   108.1  86.4 156.2  89.8  73.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4008   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 841   OE1                                                    
REMARK 620 2 GLU A 841   OE2  48.8                                              
REMARK 620 3 ASN A 843   OD1  78.6  67.6                                        
REMARK 620 4 ADP A4006   O2B  81.7  95.4 159.6                                  
REMARK 620 5 ADP A4006   O3B  88.9  65.2 126.3  47.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B4016   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  16   O                                                      
REMARK 620 2 ASP B 112   O    98.5                                              
REMARK 620 3 HOH A4567   O   114.4  80.7                                        
REMARK 620 4 HOH A4569   O   144.7 114.1  85.3                                  
REMARK 620 5 HOH B4068   O    94.0  89.1 150.9  74.1                            
REMARK 620 6 HOH B4069   O    71.1 155.6  83.8  83.0 113.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4038   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 114   OG1                                                    
REMARK 620 2 THR C 114   N    49.5                                              
REMARK 620 3 GLY C 112   O   110.3  66.7                                        
REMARK 620 4 HOH C4123   O    76.5 117.1 171.4                                  
REMARK 620 5 ASP C  84   O    75.8  44.1  77.0 100.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4024   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 127   OE1                                                    
REMARK 620 2 GLU C 299   OE1 131.4                                              
REMARK 620 3 MET C 300   O    95.6  94.5                                        
REMARK 620 4 HOH C4105   O   140.1  86.8  66.4                                  
REMARK 620 5 HOH C4645   O    95.0 102.3 145.9  85.0                            
REMARK 620 6 ALA C 126   O    89.8 138.7  81.4  53.7  66.4                      
REMARK 620 7 ASN C 301   OD1  79.8  58.1  73.6 123.7 140.3 151.7                
REMARK 620 8  MN C4021  MN    95.2  36.4 104.3 123.0 106.8 171.9  36.1          
REMARK 620 9 HOH C4102   O    62.3 104.4 157.2 126.3  41.5  92.3 105.6  84.5    
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 C4023   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 215   OE2                                                    
REMARK 620 2 ASN C 236   OD1  84.0                                              
REMARK 620 3 ASP C 238   O   122.1  94.9                                        
REMARK 620 4 ALA C 239   O    87.1 149.7  65.8                                  
REMARK 620 5 ILE C 242   O    79.7 119.5 142.2  87.1                            
REMARK 620 6 SER C 247   OG  137.2  82.0  99.3 122.6  72.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C4022  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 285   OE1                                                    
REMARK 620 2 GLU C 299   OE2  77.4                                              
REMARK 620 3 ADP C4020   O1A  98.5  87.8                                        
REMARK 620 4 HOH C4101   O    86.8 160.1  82.6                                  
REMARK 620 5 PO4 C4025   O3   88.8  81.8 165.7 110.2                            
REMARK 620 6 ADP C4020   O1B 172.6  98.3  87.2  98.6  84.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4037   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 285   OE1                                                    
REMARK 620 2 HOH C4110   O   145.0                                              
REMARK 620 3 PO4 C4025   O3   65.4  84.7                                        
REMARK 620 4 GLU C 217   OE1 119.0  92.6 173.3                                  
REMARK 620 5 ASN C 283   OD1  75.0  91.1  95.8  90.3                            
REMARK 620 6 ASN C 283   ND2 108.4  71.2 121.8  62.7  35.9                      
REMARK 620 7 HOH C4109   O   141.9  56.8  98.9  74.6 142.9 109.2                
REMARK 620 8 THR C 244   OG1  98.4 102.4  95.5  79.1 163.1 140.5  46.5          
REMARK 620 9  MN C4022  MN    34.3 121.2  36.7 144.7  98.1 134.0 113.9  83.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C4021  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 299   CD                                                     
REMARK 620 2 GLU C 299   OE1  28.5                                              
REMARK 620 3 GLU C 299   OE2  30.5  59.1                                        
REMARK 620 4 ASN C 301   OD1  87.5  86.9  88.1                                  
REMARK 620 5 ADP C4020   O3B  90.3  89.0  92.4 174.9                            
REMARK 620 6 HOH C4104   O   128.2  99.7 158.4  86.8  90.9                      
REMARK 620 7 PO4 C4025   O1  123.7 151.9  93.2  87.9  97.1 107.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4029   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 761   OE2                                                    
REMARK 620 2 GLU C 783   O   128.7                                              
REMARK 620 3 VAL C 787   O    78.4 142.8                                        
REMARK 620 4 SER C 792   OG  124.7 103.2  68.3                                  
REMARK 620 5 HIS C 781   ND1  73.6  94.7 119.6  85.9                            
REMARK 620 6 GLN C 784   O    92.6  71.3  84.1 124.8 148.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C4027  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 829   OE1                                                    
REMARK 620 2 GLU C 841   OE2  91.7                                              
REMARK 620 3 ADP C4026   O3B 163.0  95.2                                        
REMARK 620 4 HOH C4531   O    83.5 175.2  89.5                                  
REMARK 620 5 ADP C4026   O2A  82.2  91.7  82.1  88.2                            
REMARK 620 6 HOH C4530   O   109.2  95.5  85.5  85.6 166.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D4036   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  16   O                                                      
REMARK 620 2 ASP D 112   O    89.3                                              
REMARK 620 3 HOH D1603   O    74.2 157.3                                        
REMARK 620 4 HOH C4519   O   115.1  85.7  87.4                                  
REMARK 620 5 HOH C4521   O   142.3 127.2  72.6  80.8                            
REMARK 620 6 HOH D1602   O    82.3  84.6 107.9 159.9  91.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4059   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  84   O                                                      
REMARK 620 2 GLY E 112   O    83.1                                              
REMARK 620 3 THR E 114   OG1  75.7 105.0                                        
REMARK 620 4 HOH E4167   O    96.0  95.7 156.4                                  
REMARK 620 5 HOH E4165   O   151.2  79.0  87.3 108.0                            
REMARK 620 6 HOH E4702   O   123.3 152.6  77.7  89.3  73.8                      
REMARK 620 7 HOH E4164   O    88.4 161.8  88.3  69.1 114.5  41.7                
REMARK 620 8 THR E 114   N    48.9  66.8  45.4 140.7 102.9 122.8 118.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4045   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 127   OE1                                                    
REMARK 620 2 GLU E 299   OE1 127.5                                              
REMARK 620 3 MET E 300   O    92.5  88.1                                        
REMARK 620 4 HOH E4144   O   142.3  88.3  75.7                                  
REMARK 620 5 ASN E 301   OD1  77.3  54.7  67.7 127.1                            
REMARK 620 6 HOH E4143   O    64.7  69.5 119.2 151.7  53.0                      
REMARK 620 7 ALA E 126   O    91.5 141.0  90.0  53.7 154.2 141.5                
REMARK 620 8 HOH E4141   O    75.9 100.4 168.2 112.4 110.6  57.7  88.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4044   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 215   OE2                                                    
REMARK 620 2 ASN E 236   OD1  80.1                                              
REMARK 620 3 ASP E 238   O   127.7  95.0                                        
REMARK 620 4 ALA E 239   O    95.9 154.0  67.1                                  
REMARK 620 5 ILE E 242   O    81.5 117.2 141.2  87.2                            
REMARK 620 6 SER E 247   OG  135.2  77.6  92.7 120.1  75.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4058   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 285   OE1                                                    
REMARK 620 2 HOH E4148   O   138.1                                              
REMARK 620 3 HOH E4149   O   142.1  55.1                                        
REMARK 620 4 THR E 244   OG1  93.8  48.8 102.5                                  
REMARK 620 5 PO4 E4046   O3   64.5  88.8  83.9  82.2                            
REMARK 620 6 GLU E 217   OE1 125.8  74.1  90.4  82.6 162.2                      
REMARK 620 7 ASN E 283   OD1  86.4 132.3  79.5 176.1 101.4  94.1                
REMARK 620 8  MN E4043  MN    33.6 109.0 117.6  77.7  33.7 148.5 104.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E4043  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 285   OE1                                                    
REMARK 620 2 GLU E 299   OE2  75.9                                              
REMARK 620 3 ADP E4041   O1B 176.0 101.9                                        
REMARK 620 4 HOH E4140   O    88.1 163.0  94.4                                  
REMARK 620 5 ADP E4041   O1A  92.2  78.9  90.6  96.2                            
REMARK 620 6 PO4 E4046   O3   96.5  93.3  80.2  94.3 166.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E4042  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 299   CD                                                     
REMARK 620 2 GLU E 299   OE1  26.9                                              
REMARK 620 3 GLU E 299   OE2  29.2  56.1                                        
REMARK 620 4 ASN E 301   OD1  84.6  81.1  89.6                                  
REMARK 620 5 ADP E4041   O3B  93.3  93.8  92.0 172.6                            
REMARK 620 6 HOH E4143   O   123.0  96.2 152.3  85.8  89.5                      
REMARK 620 7 PO4 E4046   O1  124.7 149.9  96.3  87.9  99.2 110.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4050   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 761   OE2                                                    
REMARK 620 2 HIS E 781   ND1  76.8                                              
REMARK 620 3 GLU E 783   O   129.4  97.7                                        
REMARK 620 4 VAL E 787   O    75.7 120.1 140.1                                  
REMARK 620 5 SER E 792   OG  124.9  77.8 101.9  76.4                            
REMARK 620 6 GLN E 784   O    96.4 149.0  63.0  86.2 127.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E4048  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 829   OE1                                                    
REMARK 620 2 GLU E 841   OE2  92.1                                              
REMARK 620 3 ADP E4047   O2A  94.2  93.8                                        
REMARK 620 4 HOH E4578   O    86.0 178.0  86.9                                  
REMARK 620 5 ADP E4047   O3B 176.8  91.1  85.5  90.8                            
REMARK 620 6 HOH E4579   O    89.6  94.0 171.2  85.4  90.3                      
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 841   OE2                                                    
REMARK 620 2 HOH E4153   O    99.4                                              
REMARK 620 3 ADP E4047   O3B  57.5  89.2                                        
REMARK 620 4 GLU E 841   OE1  45.6  58.6  79.3                                  
REMARK 620 5 ASN E 843   OD1  68.8 110.0 125.3  70.0                            
REMARK 620 6 ADP E4047   O2B  88.5  47.9  46.0  76.5 146.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K F4057   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  16   O                                                      
REMARK 620 2 ASP F 112   O    92.4                                              
REMARK 620 3 HOH F2544   O    84.6  92.4                                        
REMARK 620 4 HOH F2541   O   114.8  78.1 158.4                                  
REMARK 620 5 HOH E4574   O   145.2 120.5  82.8  85.4                            
REMARK 620 6 HOH F2545   O    77.4 158.0 105.8  88.4  75.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4080   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY G 112   O                                                      
REMARK 620 2 THR G 114   OG1 109.0                                              
REMARK 620 3 HOH G4172   O    81.8 160.8                                        
REMARK 620 4 HOH G4170   O   163.9  73.4 100.6                                  
REMARK 620 5 ASP G  84   O    76.5  81.9  85.6 119.4                            
REMARK 620 6 HOH G4171   O   154.0  77.7  85.8  41.5  79.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4081   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G 143   O                                                      
REMARK 620 2 THR G 143   OG1  68.9                                              
REMARK 620 3 HOH G4246   O   130.4  80.7                                        
REMARK 620 4 HOH G4251   O    66.4  73.1 139.9                                  
REMARK 620 5 ALA G 144   O    69.0  78.0  66.9 133.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4065   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 215   OE2                                                    
REMARK 620 2 ASN G 236   OD1  82.9                                              
REMARK 620 3 ASP G 238   O   124.1  89.9                                        
REMARK 620 4 ALA G 239   O    95.1 151.9  67.9                                  
REMARK 620 5 ILE G 242   O    82.2 123.8 141.4  83.3                            
REMARK 620 6 SER G 247   OG  134.0  79.8  98.3 119.1  73.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4079   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 285   OE1                                                    
REMARK 620 2 PO4 G4067   O3   67.6                                              
REMARK 620 3  MN G4064  MN    32.7  36.1                                        
REMARK 620 4 ASN G 283   OD1  88.5 107.6 105.5                                  
REMARK 620 5 THR G 244   OG1  84.9  80.7  74.7 166.5                            
REMARK 620 6 HOH G4158   O   148.3  81.3 117.2  95.6  96.2                      
REMARK 620 7 ASN G 283   ND2 123.2 136.3 146.0  40.4 137.8  75.8                
REMARK 620 8 GLU G 217   OE1 119.7 159.3 143.5  92.4  80.7  91.6  58.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G4064  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 285   OE1                                                    
REMARK 620 2 GLU G 299   OE2  82.2                                              
REMARK 620 3 PO4 G4067   O3   87.7  88.7                                        
REMARK 620 4 HOH G4149   O    83.6 165.7  88.8                                  
REMARK 620 5 ADP G4062   O1A  99.5  88.0 171.6  96.3                            
REMARK 620 6 ADP G4062   O1B 173.4  95.1  86.2  98.8  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G4063  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 299   CD                                                     
REMARK 620 2 GLU G 299   OE1  28.0                                              
REMARK 620 3 GLU G 299   OE2  30.0  57.9                                        
REMARK 620 4 ASN G 301   OD1  88.7  88.9  90.8                                  
REMARK 620 5 HOH G4152   O   117.5  89.6 147.4  85.3                            
REMARK 620 6 PO4 G4067   O1  119.3 146.8  89.9  83.4 121.6                      
REMARK 620 7 ADP G4062   O3B  90.2  85.2  93.5 169.5  85.9 106.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4066   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 299   OE1                                                    
REMARK 620 2 MET G 300   O    96.2                                              
REMARK 620 3 HOH G4152   O    71.4 134.0                                        
REMARK 620 4 ASN G 301   OD1  57.5  78.8  56.8                                  
REMARK 620 5  MN G4063  MN    36.5 106.6  39.8  33.7                            
REMARK 620 6 ALA G 126   O   139.2  79.7 138.0 154.4 171.9                      
REMARK 620 7 HOH G4153   O    86.7  67.7 149.5 127.7 123.2  53.9                
REMARK 620 8 HOH G4150   O    99.8 162.9  58.4 115.1  90.0  84.2 106.9          
REMARK 620 9 GLU G 127   OE1 130.9  93.5  67.6  77.7  94.8  89.9 140.6  80.7    
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 G4071   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 761   OE2                                                    
REMARK 620 2 HIS G 781   ND1  75.7                                              
REMARK 620 3 GLU G 783   O   135.9 104.3                                        
REMARK 620 4 GLN G 784   O    92.7 149.7  64.8                                  
REMARK 620 5 VAL G 787   O    76.6 119.9 132.0  83.0                            
REMARK 620 6 SER G 792   OG  127.2  87.3  96.5 121.0  69.7                      
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 GLN G 829   OE1                                                    
REMARK 620 2 GLU G 841   OE2  74.5                                              
REMARK 620 3 ADP G4068   O3B 155.1  80.9                                        
REMARK 620 4 ADP G4068   O2A  94.8  75.8  82.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G4070   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 841   OE1                                                    
REMARK 620 2 ADP G4068   O2B  86.0                                              
REMARK 620 3 ADP G4068   O3B  87.1  47.0                                        
REMARK 620 4 ASN G 843   OD1  68.4 153.8 122.9                                  
REMARK 620 5 GLU G 841   OE2  45.4  89.3  58.0  69.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K H4078   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 112   O                                                      
REMARK 620 2 HOH H3632   O    85.6                                              
REMARK 620 3 HIS H  16   O    78.7 106.0                                        
REMARK 620 4 HOH G4531   O   125.6 100.9 145.2                                  
REMARK 620 5 HOH H3805   O   152.1  92.5  75.1  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A4019   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A4244   O                                                      
REMARK 620 2 THR A 143   OG1  66.9                                              
REMARK 620 3 ALA A 144   O    59.1  71.9                                        
REMARK 620 4 HOH A4617   O    83.0  73.6 136.3                                  
REMARK 620 5 THR A 143   O   114.9  67.6  64.1 123.9                            
REMARK 620 6 HOH A4250   O   138.3  81.4 135.8  61.8  73.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4028   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C4026   O2B                                                    
REMARK 620 2 GLU C 841   OE1  77.5                                              
REMARK 620 3 GLU C 841   OE2  88.9  42.6                                        
REMARK 620 4 ASN C 843   OD1 147.5  72.2  60.7                                  
REMARK 620 5 ADP C4026   O3B  47.2  79.2  58.1 114.0                            
REMARK 620 6 HOH C4114   O    54.4  50.0  90.1 110.3  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C4039   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C4203   O                                                      
REMARK 620 2 THR C 143   OG1  64.2                                              
REMARK 620 3 THR C 143   O   117.0  67.1                                        
REMARK 620 4 HOH C4222   O    59.6 123.8 141.4                                  
REMARK 620 5 ALA C 144   O    59.2  70.6  68.7  80.2                            
REMARK 620 6 HOH C4208   O   135.3  79.3  65.3 147.5 131.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E4060   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E4256   O                                                      
REMARK 620 2 ALA E 144   O   131.0                                              
REMARK 620 3 THR E 143   OG1  71.5  74.5                                        
REMARK 620 4 THR E 143   O    68.1  64.9  60.9                                  
REMARK 620 5 HOH E4271   O   152.5  76.4 123.7 138.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 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 4007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4008                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4009                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4012                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4013                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4014                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 4016                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4017                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4018                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4019                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4021                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4022                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4023                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4059                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4024                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4060                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4063                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4028                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4064                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4029                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4065                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4032                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4066                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4033                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4069                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4034                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4070                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4035                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4071                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 4036                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4074                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4037                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4075                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4038                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4076                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4039                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 4077                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4042                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 4078                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4043                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4079                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4044                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4080                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4045                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4081                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4048                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4049                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4050                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4053                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4054                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4055                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 4056                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 4057                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4058                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 4046                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 4061                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 4067                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 4025                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 4040                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 4030                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 4051                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 4072                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 4041                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 4047                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 4052                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 4062                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 4068                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 4073                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 4020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 4026                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 4031                
DBREF  1C30 A    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C30 C    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C30 E    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C30 G    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1C30 B    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1C30 D    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1C30 F    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1C30 H    1   382  UNP    P00907   CARA_ECOLI       1    382             
SEQADV 1C30 SER B  269  UNP  P00907    CYS   269 ENGINEERED MUTATION            
SEQADV 1C30 SER D  269  UNP  P00907    CYS   269 ENGINEERED MUTATION            
SEQADV 1C30 SER F  269  UNP  P00907    CYS   269 ENGINEERED MUTATION            
SEQADV 1C30 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  A4007       1                                                       
HET      K  A4008       1                                                       
HET      K  A4009       1                                                       
HET     CL  A4012       1                                                       
HET     CL  A4013       1                                                       
HET     CL  A4014       1                                                       
HET      K  A4017       1                                                       
HET      K  A4018       1                                                       
HET      K  A4019       1                                                       
HET    PO4  A4005       5                                                       
HET    ORN  A4010       9                                                       
HET    ORN  A4030       8                                                       
HET    ORN  A4051       8                                                       
HET    ORN  A4072       9                                                       
HET    ADP  A4000      27                                                       
HET    ADP  A4006      27                                                       
HET    NET  A4011       9                                                       
HET     CL  B4015       1                                                       
HET      K  B4016       1                                                       
HET     MN  C4021       1                                                       
HET     MN  C4022       1                                                       
HET      K  C4023       1                                                       
HET      K  C4024       1                                                       
HET     MN  C4027       1                                                       
HET      K  C4028       1                                                       
HET      K  C4029       1                                                       
HET     CL  C4032       1                                                       
HET     CL  C4033       1                                                       
HET     CL  C4034       1                                                       
HET      K  C4037       1                                                       
HET      K  C4038       1                                                       
HET      K  C4039       1                                                       
HET    PO4  C4025       5                                                       
HET    PO4  C4040       5                                                       
HET    ADP  C4020      27                                                       
HET    ADP  C4026      27                                                       
HET    NET  C4031       9                                                       
HET     CL  D4035       1                                                       
HET      K  D4036       1                                                       
HET      K  E4059       1                                                       
HET      K  E4060       1                                                       
HET     MN  E4042       1                                                       
HET     MN  E4043       1                                                       
HET      K  E4044       1                                                       
HET      K  E4045       1                                                       
HET     MN  E4048       1                                                       
HET      K  E4049       1                                                       
HET      K  E4050       1                                                       
HET     CL  E4053       1                                                       
HET     CL  E4054       1                                                       
HET     CL  E4055       1                                                       
HET      K  E4058       1                                                       
HET    PO4  E4046       5                                                       
HET    PO4  E4061       5                                                       
HET    ADP  E4041      27                                                       
HET    ADP  E4047      27                                                       
HET    NET  E4052       9                                                       
HET     CL  F4056       1                                                       
HET      K  F4057       1                                                       
HET     MN  G4063       1                                                       
HET     MN  G4064       1                                                       
HET      K  G4065       1                                                       
HET      K  G4066       1                                                       
HET     MN  G4069       1                                                       
HET      K  G4070       1                                                       
HET      K  G4071       1                                                       
HET     CL  G4074       1                                                       
HET     CL  G4075       1                                                       
HET     CL  G4076       1                                                       
HET      K  G4079       1                                                       
HET      K  G4080       1                                                       
HET      K  G4081       1                                                       
HET    PO4  G4067       5                                                       
HET    ADP  G4062      27                                                       
HET    ADP  G4068      27                                                       
HET    NET  G4073       9                                                       
HET     CL  H4077       1                                                       
HET      K  H4078       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM       K POTASSIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ORN L-ORNITHINE                                                      
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
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    6(O4 P 3-)                                                   
FORMUL  23  ORN    4(C5 H12 N2 O2)                                              
FORMUL  27  ADP    8(C10 H15 N5 O10 P2)                                         
FORMUL  29  NET    4(C8 H20 N 1+)                                               
FORMUL  91  HOH   *3987(H2 O)                                                   
HELIX    1   1 CYS A   24  GLU A   40  1                                  17    
HELIX    2   2 THR A   53  ASP A   57  5                                   5    
HELIX    3   3 ASP A   57  ALA A   61  5                                   5    
HELIX    4   4 HIS A   70  ARG A   82  1                                  13    
HELIX    5   5 GLY A   91  GLN A  105  1                                  15    
HELIX    6   6 GLY A  106  PHE A  111  1                                   6    
HELIX    7   7 THR A  119  ASP A  128  1                                  10    
HELIX    8   8 ASP A  128  ILE A  139  1                                  12    
HELIX    9   9 THR A  151  GLY A  163  1                                  13    
HELIX   10  10 ASN A  184  SER A  199  1                                  16    
HELIX   11  11 HIS A  243  SER A  247  5                                   5    
HELIX   12  12 THR A  257  GLY A  276  1                                  20    
HELIX   13  13 SER A  305  GLY A  316  1                                  12    
HELIX   14  14 PRO A  318  ALA A  327  1                                  10    
HELIX   15  15 THR A  331  LEU A  335  5                                   5    
HELIX   16  16 ASN A  337  GLY A  341  5                                   5    
HELIX   17  17 ASN A  363  PHE A  367  5                                   5    
HELIX   18  18 THR A  390  LEU A  402  1                                  13    
HELIX   19  19 GLU A  419  ASP A  430  1                                  12    
HELIX   20  20 ASP A  434  GLY A  446  1                                  13    
HELIX   21  21 SER A  448  ASN A  457  1                                  10    
HELIX   22  22 ASP A  459  GLY A  480  1                                  22    
HELIX   23  23 ILE A  481  LEU A  484  5                                   4    
HELIX   24  24 ASN A  485  LYS A  495  1                                  11    
HELIX   25  25 ALA A  498  GLY A  507  1                                  10    
HELIX   26  26 ARG A  509  TYR A  520  1                                  12    
HELIX   27  27 GLY A  575  ASP A  592  1                                  18    
HELIX   28  28 ASP A  609  SER A  613  5                                   5    
HELIX   29  29 THR A  622  LYS A  634  1                                  13    
HELIX   30  30 GLY A  644  ALA A  657  1                                  14    
HELIX   31  31 SER A  665  ASP A  674  1                                  10    
HELIX   32  32 ASP A  674  LYS A  686  1                                  13    
HELIX   33  33 ALA A  697  GLY A  709  1                                  13    
HELIX   34  34 ASP A  730  ALA A  741  1                                  12    
HELIX   35  35 HIS A  788  SER A  792  5                                   5    
HELIX   36  36 SER A  802  GLN A  821  1                                  20    
HELIX   37  37 THR A  849  GLY A  858  1                                  10    
HELIX   38  38 PRO A  860  GLY A  871  1                                  12    
HELIX   39  39 SER A  873  GLY A  878  1                                   6    
HELIX   40  40 LEU A  895  PHE A  900  5                                   6    
HELIX   41  41 THR A  923  SER A  935  1                                  13    
HELIX   42  42 ARG A  950  GLY A  952  5                                   3    
HELIX   43  43 ASP A  953  GLY A  968  1                                  16    
HELIX   44  44 THR A  974  ALA A  984  1                                  11    
HELIX   45  45 HIS A 1000  ASN A 1007  1                                   8    
HELIX   46  46 GLY A 1019  TYR A 1036  1                                  18    
HELIX   47  47 THR A 1043  LEU A 1054  1                                  12    
HELIX   48  48 SER A 1064  GLN A 1071  1                                   8    
HELIX   49  49 GLY B   38  THR B   44  1                                   7    
HELIX   50  50 ASP B   45  TYR B   48  5                                   4    
HELIX   51  51 ASN B   66  GLU B   70  5                                   5    
HELIX   52  52 ASP B   97  HIS B  105  1                                   9    
HELIX   53  53 ASP B  114  GLY B  126  1                                  13    
HELIX   54  54 ASP B  139  PHE B  150  1                                  12    
HELIX   55  55 LEU B  158  THR B  163  1                                   6    
HELIX   56  56 LYS B  186  LEU B  190  5                                   5    
HELIX   57  57 LYS B  202  ARG B  212  1                                  11    
HELIX   58  58 SER B  224  LYS B  230  1                                   7    
HELIX   59  59 CYS B  248  GLU B  260  1                                  13    
HELIX   60  60 SER B  269  SER B  279  1                                  11    
HELIX   61  61 ALA B  364  LYS B  379  1                                  16    
HELIX   62  62 CYS C   24  GLU C   40  1                                  17    
HELIX   63  63 THR C   53  ASP C   57  5                                   5    
HELIX   64  64 ASP C   57  ALA C   61  5                                   5    
HELIX   65  65 HIS C   70  ARG C   82  1                                  13    
HELIX   66  66 GLY C   91  GLN C  105  1                                  15    
HELIX   67  67 GLY C  106  PHE C  111  1                                   6    
HELIX   68  68 THR C  119  ASP C  128  1                                  10    
HELIX   69  69 ASP C  128  ILE C  139  1                                  12    
HELIX   70  70 THR C  151  GLY C  163  1                                  13    
HELIX   71  71 ASN C  184  SER C  199  1                                  16    
HELIX   72  72 HIS C  243  SER C  247  5                                   5    
HELIX   73  73 THR C  257  GLY C  276  1                                  20    
HELIX   74  74 SER C  305  GLY C  316  1                                  12    
HELIX   75  75 PRO C  318  VAL C  328  1                                  11    
HELIX   76  76 THR C  331  LEU C  335  5                                   5    
HELIX   77  77 ASN C  337  GLY C  341  5                                   5    
HELIX   78  78 ASN C  363  PHE C  367  5                                   5    
HELIX   79  79 THR C  390  GLY C  401  1                                  12    
HELIX   80  80 GLU C  419  ASP C  430  1                                  12    
HELIX   81  81 ASP C  434  ALA C  445  1                                  12    
HELIX   82  82 SER C  448  ASN C  457  1                                  10    
HELIX   83  83 ASP C  459  GLY C  480  1                                  22    
HELIX   84  84 ILE C  481  LEU C  484  5                                   4    
HELIX   85  85 ASN C  485  LYS C  495  1                                  11    
HELIX   86  86 ALA C  498  GLY C  507  1                                  10    
HELIX   87  87 ARG C  509  ASP C  521  1                                  13    
HELIX   88  88 GLY C  575  ASP C  592  1                                  18    
HELIX   89  89 ASP C  609  SER C  613  5                                   5    
HELIX   90  90 THR C  622  LYS C  634  1                                  13    
HELIX   91  91 GLY C  644  LYS C  649  1                                   6    
HELIX   92  92 LEU C  650  ALA C  657  1                                   8    
HELIX   93  93 SER C  665  ASP C  674  1                                  10    
HELIX   94  94 ASP C  674  LEU C  685  1                                  12    
HELIX   95  95 ALA C  697  GLY C  709  1                                  13    
HELIX   96  96 ASP C  730  ALA C  741  1                                  12    
HELIX   97  97 HIS C  788  SER C  792  5                                   5    
HELIX   98  98 SER C  802  GLN C  821  1                                  20    
HELIX   99  99 THR C  849  GLY C  858  1                                  10    
HELIX  100 100 PRO C  860  GLY C  871  1                                  12    
HELIX  101 101 SER C  873  GLY C  878  1                                   6    
HELIX  102 102 LEU C  895  PHE C  900  5                                   6    
HELIX  103 103 THR C  923  SER C  935  1                                  13    
HELIX  104 104 ARG C  950  GLY C  952  5                                   3    
HELIX  105 105 ASP C  953  GLN C  967  1                                  15    
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  TYR C 1036  1                                  18    
HELIX  109 109 THR C 1043  LEU C 1054  1                                  12    
HELIX  110 110 SER C 1064  ALA C 1070  1                                   7    
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 PRO D  365  THR D  380  1                                  16    
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  ILE E  139  1                                  12    
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  LYS E  495  1                                  11    
HELIX  148 148 ALA E  498  GLY E  507  1                                  10    
HELIX  149 149 ARG E  509  TYR E  520  1                                  12    
HELIX  150 150 GLY E  575  ASP E  592  1                                  18    
HELIX  151 151 ASP E  609  SER E  613  5                                   5    
HELIX  152 152 THR E  622  LYS E  634  1                                  13    
HELIX  153 153 GLY E  644  LYS E  649  1                                   6    
HELIX  154 154 LEU E  650  ALA E  657  1                                   8    
HELIX  155 155 SER E  665  ASP E  674  1                                  10    
HELIX  156 156 ASP E  674  LYS E  686  1                                  13    
HELIX  157 157 ALA E  697  GLY E  709  1                                  13    
HELIX  158 158 ASP E  730  ALA E  741  1                                  12    
HELIX  159 159 HIS E  788  SER E  792  5                                   5    
HELIX  160 160 SER E  802  LEU E  820  1                                  19    
HELIX  161 161 THR E  849  GLY E  858  1                                  10    
HELIX  162 162 PRO E  860  ALA E  870  1                                  11    
HELIX  163 163 SER E  873  GLY E  878  1                                   6    
HELIX  164 164 PRO E  896  PHE E  900  5                                   5    
HELIX  165 165 THR E  923  SER E  935  1                                  13    
HELIX  166 166 ARG E  950  LYS E  954  5                                   5    
HELIX  167 167 GLU E  955  GLU E  955  5                                   1    
HELIX  168 168 ARG E  956  GLN E  967  1                                  12    
HELIX  169 169 HIS E  975  ALA E  984  1                                  10    
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  ASP F  211  1                                  10    
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  GLY G  401  1                                  12    
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 ASN G  485  LYS G  495  1                                  11    
HELIX  211 211 ALA G  498  ALA G  506  1                                   9    
HELIX  212 212 ARG G  509  ASP G  521  1                                  13    
HELIX  213 213 GLY G  575  ASP G  592  1                                  18    
HELIX  214 214 THR G  605  ASP G  609  5                                   5    
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  GLU G  955  1                                   6    
HELIX  231 231 ARG G  956  GLN G  967  1                                  12    
HELIX  232 232 HIS G  975  ALA G  984  1                                  10    
HELIX  233 233 HIS G 1000  ASN G 1007  1                                   8    
HELIX  234 234 GLY G 1019  LYS G 1037  1                                  19    
HELIX  235 235 THR G 1043  LEU G 1054  1                                  12    
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  186  LEU H  190  5                                   5    
HELIX  245 245 LYS H  202  ARG H  212  1                                  11    
HELIX  246 246 SER H  224  MET H  231  1                                   8    
HELIX  247 247 CYS H  248  LEU H  259  1                                  12    
HELIX  248 248 SER H  269  SER H  279  1                                  11    
HELIX  249 249 GLU H  318  LEU H  321  5                                   4    
HELIX  250 250 PRO H  360  ALA H  363  5                                   4    
HELIX  251 251 ALA H  364  LYS H  379  1                                  16    
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  O  ILE A 229   N  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  TYR A 617  1  O  LEU A 616   N  MET A 543           
SHEET    4   D 6 GLU A 595  VAL A 599  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 LEU A 712  VAL A 713  0                                        
SHEET    2   E 2 ILE A 727  VAL A 728 -1  O  VAL A 728   N  LEU A 712           
SHEET    1   F 7 GLU A 836  ASN A 843  0                                        
SHEET    2   F 7 GLY A 824  LYS A 833 -1  O  ASN A 827   N  ASN A 843           
SHEET    3   F 7 VAL A 760  CYS A 768 -1  O  VAL A 760   N  VAL A 832           
SHEET    4   F 7 VAL A 773  GLN A 784 -1  N  LEU A 774   O  ILE A 767           
SHEET    5   F 7 CYS A 794  LEU A 796 -1  N  SER A 795   O  GLU A 780           
SHEET    6   F 7 TYR A 888  VAL A 894 -1  O  SER A 889   N  LEU A 796           
SHEET    7   F 7 GLY A 915  GLY A 921 -1  O  GLY A 915   N  VAL A 894           
SHEET    1   G 5 ARG A 989  LEU A 990  0                                        
SHEET    2   G 5 GLU A 970  ALA A 973  1  O  LEU A 971   N  ARG A 989           
SHEET    3   G 5 ARG A 944  SER A 948  1  N  ALA A 945   O  GLU A 970           
SHEET    4   G 5 TYR A1012  ASN A1015  1  O  TYR A1012   N  LEU A 946           
SHEET    5   G 5 HIS A1039  ASP A1041  1  O  HIS A1039   N  ILE A1013           
SHEET    1   H 8 SER B   4  LEU B   9  0                                        
SHEET    2   H 8 GLN B  14  ALA B  19 -1  N  PHE B  15   O  LEU B   7           
SHEET    3   H 8 VAL B 108  ALA B 111 -1  O  ALA B 111   N  ARG B  18           
SHEET    4   H 8 GLY B  79  VAL B  81  1  O  LEU B  80   N  ILE B 110           
SHEET    5   H 8 GLN B  51  LEU B  55  1  O  GLN B  51   N  GLY B  79           
SHEET    6   H 8 GLY B  24  ASN B  33  1  O  GLU B  29   N  ILE B  52           
SHEET    7   H 8 GLN B 128  ALA B 134 -1  O  GLN B 128   N  VAL B  30           
SHEET    8   H 8 SER B   4  LEU B   9 -1  O  LEU B   6   N  ILE B 133           
SHEET    1   I10 TYR B 168  TRP B 170  0                                        
SHEET    2   I10 CYS B 214  PRO B 220 -1  O  LEU B 216   N  TRP B 170           
SHEET    3   I10 PHE B 192  ASP B 198  1  O  PHE B 192   N  ARG B 215           
SHEET    4   I10 GLY B 235  LEU B 238  1  O  GLY B 235   N  VAL B 195           
SHEET    5   I10 VAL B 265  ILE B 268  1  O  PHE B 266   N  LEU B 238           
SHEET    6   I10 ALA B 347  PHE B 350  1  N  PHE B 348   O  VAL B 265           
SHEET    7   I10 LEU B 337  ARG B 342 -1  O  ILE B 340   N  SER B 349           
SHEET    8   I10 LEU B 325  SER B 331 -1  N  ARG B 326   O  HIS B 341           
SHEET    9   I10 THR B 283  ASP B 299 -1  N  LYS B 298   O  LYS B 330           
SHEET   10   I10 VAL B 304  VAL B 316 -1  O  VAL B 304   N  ASP B 299           
SHEET    1   J 5 ALA C  63  TYR C  65  0                                        
SHEET    2   J 5 ARG C  43  VAL C  47  1  O  VAL C  44   N  ALA C  63           
SHEET    3   J 5 SER C   9  LEU C  13  1  O  ILE C  10   N  ILE C  45           
SHEET    4   J 5 ALA C  85  LEU C  87  1  O  ALA C  85   N  LEU C  11           
SHEET    5   J 5 THR C 114  MET C 115  1  O  THR C 114   N  VAL C  86           
SHEET    1   K 4 SER C 146  ALA C 149  0                                        
SHEET    2   K 4 LEU C 204  GLU C 208 -1  N  LEU C 204   O  ALA C 149           
SHEET    3   K 4 CYS C 166  PRO C 170 -1  O  ILE C 167   N  ASP C 207           
SHEET    4   K 4 GLY C 180  ALA C 182 -1  O  GLY C 180   N  ILE C 168           
SHEET    1   L 7 LEU C 295  ASN C 301  0                                        
SHEET    2   L 7 GLY C 280  VAL C 288 -1  O  ASN C 283   N  ASN C 301           
SHEET    3   L 7 LYS C 214  ARG C 222 -1  N  LYS C 214   O  VAL C 288           
SHEET    4   L 7 CYS C 228  ASN C 236 -1  N  ILE C 229   O  VAL C 221           
SHEET    5   L 7 THR C 249  ALA C 251 -1  O  VAL C 250   N  GLU C 235           
SHEET    6   L 7 VAL C 355  ARG C 361 -1  N  VAL C 356   O  ALA C 251           
SHEET    7   L 7 GLY C 382  GLY C 388 -1  O  GLY C 382   N  ARG C 361           
SHEET    1   M 7 VAL C 525  ARG C 528  0                                        
SHEET    2   M 7 ALA C 541  THR C 546 -1  O  TYR C 544   N  LYS C 527           
SHEET    3   M 7 ARG C 615  TYR C 617  1  N  LEU C 616   O  ALA C 541           
SHEET    4   M 7 GLU C 595  VAL C 599  1  O  THR C 596   N  ARG C 615           
SHEET    5   M 7 LYS C 561  LEU C 565  1  N  ILE C 562   O  GLU C 595           
SHEET    6   M 7 GLY C 637  ILE C 639  1  O  GLY C 637   N  MET C 563           
SHEET    7   M 7 VAL C 661  ILE C 662  1  N  ILE C 662   O  VAL C 638           
SHEET    1   N 4 ASN C 692  THR C 694  0                                        
SHEET    2   N 4 LEU C 751  HIS C 754 -1  N  LEU C 752   O  ALA C 693           
SHEET    3   N 4 LEU C 712  ARG C 715 -1  N  VAL C 713   O  ASP C 753           
SHEET    4   N 4 GLU C 726  VAL C 728 -1  O  GLU C 726   N  VAL C 714           
SHEET    1   O 7 GLU C 836  ASN C 843  0                                        
SHEET    2   O 7 GLY C 824  LYS C 833 -1  O  ASN C 827   N  ASN C 843           
SHEET    3   O 7 VAL C 760  CYS C 768 -1  O  VAL C 760   N  VAL C 832           
SHEET    4   O 7 VAL C 773  HIS C 781 -1  N  LEU C 774   O  ILE C 767           
SHEET    5   O 7 CYS C 794  LEU C 796 -1  O  SER C 795   N  GLU C 780           
SHEET    6   O 7 TYR C 888  VAL C 894 -1  N  SER C 889   O  LEU C 796           
SHEET    7   O 7 GLY C 915  GLY C 921 -1  O  GLY C 915   N  VAL C 894           
SHEET    1   P 5 ARG C 989  LEU C 990  0                                        
SHEET    2   P 5 GLU C 970  ALA C 973  1  O  LEU C 971   N  ARG C 989           
SHEET    3   P 5 ARG C 944  SER C 948  1  N  ALA C 945   O  GLU C 970           
SHEET    4   P 5 TYR C1012  ASN C1015  1  O  TYR C1012   N  LEU C 946           
SHEET    5   P 5 HIS C1039  ASP C1041  1  O  HIS C1039   N  ILE C1013           
SHEET    1   Q 8 SER D   4  LEU D   9  0                                        
SHEET    2   Q 8 GLN D  14  ALA D  19 -1  N  PHE D  15   O  LEU D   7           
SHEET    3   Q 8 VAL D 108  ALA D 111 -1  N  ALA D 111   O  ARG D  18           
SHEET    4   Q 8 GLY D  79  VAL D  81  1  O  LEU D  80   N  ILE D 110           
SHEET    5   Q 8 GLN D  51  LEU D  55  1  O  GLN D  51   N  GLY D  79           
SHEET    6   Q 8 GLY D  24  ASN D  33  1  O  GLU D  29   N  ILE D  52           
SHEET    7   Q 8 GLN D 128  ALA D 134 -1  O  GLN D 128   N  VAL D  30           
SHEET    8   Q 8 SER D   4  LEU D   9 -1  O  LEU D   6   N  ILE D 133           
SHEET    1   R10 TYR D 168  TRP D 170  0                                        
SHEET    2   R10 CYS D 214  PRO D 220 -1  O  LEU D 216   N  TRP D 170           
SHEET    3   R10 PHE D 192  ASP D 198  1  O  PHE D 192   N  ARG D 215           
SHEET    4   R10 GLY D 235  LEU D 238  1  O  GLY D 235   N  VAL D 195           
SHEET    5   R10 VAL D 265  ILE D 268  1  O  PHE D 266   N  LEU D 238           
SHEET    6   R10 ALA D 347  PHE D 350  1  N  PHE D 348   O  VAL D 265           
SHEET    7   R10 LEU D 337  ARG D 342 -1  O  ILE D 340   N  SER D 349           
SHEET    8   R10 LEU D 325  SER D 331 -1  N  ARG D 326   O  HIS D 341           
SHEET    9   R10 THR D 283  ASP D 299 -1  N  LYS D 298   O  LYS D 330           
SHEET   10   R10 VAL D 304  VAL D 316 -1  O  VAL D 304   N  ASP D 299           
SHEET    1   S 5 ALA E  63  TYR E  65  0                                        
SHEET    2   S 5 ARG E  43  VAL E  47  1  O  VAL E  44   N  ALA E  63           
SHEET    3   S 5 SER E   9  LEU E  13  1  N  ILE E  10   O  ARG E  43           
SHEET    4   S 5 ALA E  85  LEU E  87  1  O  ALA E  85   N  LEU E  11           
SHEET    5   S 5 THR E 114  MET E 115  1  O  THR E 114   N  VAL E  86           
SHEET    1   T 4 SER E 146  ALA E 149  0                                        
SHEET    2   T 4 LEU E 204  GLU E 208 -1  N  LEU E 204   O  ALA E 149           
SHEET    3   T 4 CYS E 166  PRO E 170 -1  O  ILE E 167   N  ASP E 207           
SHEET    4   T 4 GLY E 180  ALA E 182 -1  O  GLY E 180   N  ILE E 168           
SHEET    1   U 7 LEU E 295  ASN E 301  0                                        
SHEET    2   U 7 GLY E 280  VAL E 288 -1  O  ASN E 283   N  ASN E 301           
SHEET    3   U 7 LYS E 214  ARG E 222 -1  N  LYS E 214   O  VAL E 288           
SHEET    4   U 7 CYS E 228  ASN E 236 -1  N  ILE E 229   O  VAL E 221           
SHEET    5   U 7 THR E 249  ALA E 251 -1  O  VAL E 250   N  GLU E 235           
SHEET    6   U 7 VAL E 355  ARG E 361 -1  N  VAL E 356   O  ALA E 251           
SHEET    7   U 7 GLY E 382  GLY E 388 -1  O  GLY E 382   N  ARG E 361           
SHEET    1   V 6 VAL E 525  ARG E 528  0                                        
SHEET    2   V 6 TYR E 542  THR E 546 -1  O  TYR E 544   N  LYS E 527           
SHEET    3   V 6 ARG E 615  PHE E 618  1  O  LEU E 616   N  MET E 543           
SHEET    4   V 6 GLU E 595  ASN E 600  1  O  THR E 596   N  ARG E 615           
SHEET    5   V 6 LYS E 561  LEU E 565  1  O  ILE E 562   N  ILE E 597           
SHEET    6   V 6 GLY E 637  ILE E 639  1  O  GLY E 637   N  MET E 563           
SHEET    1   W 4 ASN E 692  THR E 694  0                                        
SHEET    2   W 4 LEU E 751  HIS E 754 -1  N  LEU E 752   O  ALA E 693           
SHEET    3   W 4 LEU E 712  ARG E 715 -1  N  VAL E 713   O  ASP E 753           
SHEET    4   W 4 GLU E 726  VAL E 728 -1  O  GLU E 726   N  VAL E 714           
SHEET    1   X 7 GLU E 836  ASN E 843  0                                        
SHEET    2   X 7 GLY E 824  LYS E 833 -1  O  ASN E 827   N  ASN E 843           
SHEET    3   X 7 VAL E 760  CYS E 768 -1  N  VAL E 760   O  VAL E 832           
SHEET    4   X 7 VAL E 773  HIS E 781 -1  N  LEU E 774   O  ILE E 767           
SHEET    5   X 7 CYS E 794  LEU E 796 -1  O  SER E 795   N  GLU E 780           
SHEET    6   X 7 TYR E 888  VAL E 894 -1  O  SER E 889   N  LEU E 796           
SHEET    7   X 7 GLY E 915  GLY E 921 -1  O  GLY E 915   N  VAL E 894           
SHEET    1   Y 5 ARG E 989  VAL E 991  0                                        
SHEET    2   Y 5 PHE E 969  THR E 974  1  O  LEU E 971   N  ARG E 989           
SHEET    3   Y 5 GLY E 943  SER E 948  1  O  GLY E 943   N  GLU E 970           
SHEET    4   Y 5 TYR E1012  ASN E1015  1  O  TYR E1012   N  LEU E 946           
SHEET    5   Y 5 HIS E1039  ASP E1041  1  O  HIS E1039   N  ILE E1013           
SHEET    1   Z 8 SER F   4  LEU F   9  0                                        
SHEET    2   Z 8 GLN F  14  ALA F  19 -1  N  PHE F  15   O  LEU F   7           
SHEET    3   Z 8 ALA F 109  ALA F 111 -1  N  ALA F 111   O  ARG F  18           
SHEET    4   Z 8 GLY F  79  VAL F  81  1  O  LEU F  80   N  ILE F 110           
SHEET    5   Z 8 GLN F  51  LEU F  55  1  O  GLN F  51   N  GLY F  79           
SHEET    6   Z 8 GLY F  24  ASN F  33  1  O  GLU F  29   N  ILE F  52           
SHEET    7   Z 8 GLN F 128  ALA F 134 -1  O  GLN F 128   N  VAL F  30           
SHEET    8   Z 8 SER F   4  LEU F   9 -1  O  LEU F   6   N  ILE F 133           
SHEET    1  AA10 TYR F 168  TRP F 170  0                                        
SHEET    2  AA10 CYS F 214  PRO F 220 -1  N  LEU F 216   O  TRP F 170           
SHEET    3  AA10 PHE F 192  ASP F 198  1  O  PHE F 192   N  ARG F 215           
SHEET    4  AA10 GLY F 235  LEU F 238  1  O  GLY F 235   N  VAL F 195           
SHEET    5  AA10 VAL F 265  ILE F 268  1  O  PHE F 266   N  LEU F 238           
SHEET    6  AA10 ALA F 347  PHE F 350  1  N  PHE F 348   O  VAL F 265           
SHEET    7  AA10 LEU F 337  ARG F 342 -1  O  ILE F 340   N  SER F 349           
SHEET    8  AA10 LEU F 325  SER F 331 -1  N  ARG F 326   O  HIS F 341           
SHEET    9  AA10 THR F 283  ASP F 299 -1  N  LYS F 298   O  LYS F 330           
SHEET   10  AA10 VAL F 304  VAL F 316 -1  O  VAL F 304   N  ASP F 299           
SHEET    1  AB 5 ALA G  63  TYR G  65  0                                        
SHEET    2  AB 5 ARG G  43  VAL G  47  1  O  VAL G  44   N  ALA G  63           
SHEET    3  AB 5 SER G   9  LEU G  13  1  N  ILE G  10   O  ARG G  43           
SHEET    4  AB 5 ALA G  85  LEU G  87  1  O  ALA G  85   N  LEU G  11           
SHEET    5  AB 5 THR G 114  MET G 115  1  O  THR G 114   N  VAL G  86           
SHEET    1  AC 4 SER G 146  ALA G 149  0                                        
SHEET    2  AC 4 LEU G 204  GLU G 208 -1  O  LEU G 204   N  ALA G 149           
SHEET    3  AC 4 CYS G 166  PRO G 170 -1  O  ILE G 167   N  ASP G 207           
SHEET    4  AC 4 GLY G 180  ALA G 182 -1  O  GLY G 180   N  ILE G 168           
SHEET    1  AD 7 LEU G 295  ASN G 301  0                                        
SHEET    2  AD 7 GLY G 280  VAL G 288 -1  N  ASN G 283   O  ASN G 301           
SHEET    3  AD 7 LYS G 214  ARG G 222 -1  N  LYS G 214   O  VAL G 288           
SHEET    4  AD 7 CYS G 228  ASN G 236 -1  N  ILE G 229   O  VAL G 221           
SHEET    5  AD 7 THR G 249  ALA G 251 -1  O  VAL G 250   N  GLU G 235           
SHEET    6  AD 7 VAL G 355  ARG G 361 -1  O  VAL G 356   N  ALA G 251           
SHEET    7  AD 7 GLY G 382  GLY G 388 -1  O  GLY G 382   N  ARG G 361           
SHEET    1  AE 7 VAL G 525  ARG G 528  0                                        
SHEET    2  AE 7 ALA G 541  THR G 546 -1  O  TYR G 544   N  LYS G 527           
SHEET    3  AE 7 ARG G 615  TYR G 617  1  N  LEU G 616   O  ALA G 541           
SHEET    4  AE 7 GLU G 595  VAL G 599  1  O  THR G 596   N  ARG G 615           
SHEET    5  AE 7 LYS G 561  LEU G 565  1  O  ILE G 562   N  ILE G 597           
SHEET    6  AE 7 GLY G 637  ILE G 639  1  O  GLY G 637   N  MET G 563           
SHEET    7  AE 7 VAL G 661  ILE G 662  1  N  ILE G 662   O  VAL G 638           
SHEET    1  AF 4 ASN G 692  THR G 694  0                                        
SHEET    2  AF 4 LEU G 751  HIS G 754 -1  N  LEU G 752   O  ALA G 693           
SHEET    3  AF 4 LEU G 712  ARG G 715 -1  N  VAL G 713   O  ASP G 753           
SHEET    4  AF 4 GLU G 726  VAL G 728 -1  O  GLU G 726   N  VAL G 714           
SHEET    1  AG 7 GLU G 836  ASN G 843  0                                        
SHEET    2  AG 7 GLY G 824  LYS G 833 -1  O  ASN G 827   N  ASN G 843           
SHEET    3  AG 7 VAL G 760  CYS G 768 -1  O  VAL G 760   N  VAL G 832           
SHEET    4  AG 7 VAL G 773  HIS G 781 -1  N  LEU G 774   O  ILE G 767           
SHEET    5  AG 7 CYS G 794  LEU G 796 -1  O  SER G 795   N  GLU G 780           
SHEET    6  AG 7 TYR G 888  VAL G 894 -1  O  SER G 889   N  LEU G 796           
SHEET    7  AG 7 GLY G 915  GLY G 921 -1  O  GLY G 915   N  VAL G 894           
SHEET    1  AH 5 ARG G 989  VAL G 991  0                                        
SHEET    2  AH 5 GLU G 970  THR G 974  1  O  LEU G 971   N  ARG G 989           
SHEET    3  AH 5 ARG G 944  SER G 948  1  N  ALA G 945   O  GLU G 970           
SHEET    4  AH 5 TYR G1012  ASN G1015  1  O  TYR G1012   N  LEU G 946           
SHEET    5  AH 5 HIS G1039  ASP G1041  1  O  HIS G1039   N  ILE G1013           
SHEET    1  AI 8 SER H   4  LEU H   9  0                                        
SHEET    2  AI 8 GLN H  14  ALA H  19 -1  N  PHE H  15   O  LEU H   7           
SHEET    3  AI 8 VAL H 108  ALA H 111 -1  N  ALA H 111   O  ARG H  18           
SHEET    4  AI 8 GLY H  79  VAL H  81  1  O  LEU H  80   N  ILE H 110           
SHEET    5  AI 8 GLN H  51  LEU H  55  1  O  GLN H  51   N  GLY H  79           
SHEET    6  AI 8 GLY H  24  ASN H  33  1  O  GLU H  29   N  ILE H  52           
SHEET    7  AI 8 GLN H 128  ALA H 134 -1  O  GLN H 128   N  VAL H  30           
SHEET    8  AI 8 SER H   4  LEU H   9 -1  O  LEU H   6   N  ILE H 133           
SHEET    1  AJ10 TYR H 168  TRP H 170  0                                        
SHEET    2  AJ10 CYS H 214  VAL H 219 -1  O  LEU H 216   N  TRP H 170           
SHEET    3  AJ10 PHE H 192  TYR H 197  1  O  PHE H 192   N  ARG H 215           
SHEET    4  AJ10 GLY H 235  LEU H 238  1  O  GLY H 235   N  VAL H 195           
SHEET    5  AJ10 VAL H 265  ILE H 268  1  O  PHE H 266   N  LEU H 238           
SHEET    6  AJ10 ALA H 347  PHE H 350  1  N  PHE H 348   O  VAL H 265           
SHEET    7  AJ10 LEU H 337  ARG H 342 -1  N  ILE H 340   O  SER H 349           
SHEET    8  AJ10 LEU H 325  SER H 331 -1  N  ARG H 326   O  HIS H 341           
SHEET    9  AJ10 THR H 283  ASP H 299 -1  N  LYS H 298   O  LYS H 330           
SHEET   10  AJ10 VAL H 304  VAL H 316 -1  O  VAL H 304   N  ASP H 299           
LINK         O   ASP A  84                 K     K A4018     1555   1555  2.88  
LINK         O   GLY A 112                 K     K A4018     1555   1555  2.84  
LINK         OG1 THR A 114                 K     K A4018     1555   1555  2.66  
LINK         OE2 GLU A 215                 K     K A4003     1555   1555  2.71  
LINK         OD1 ASN A 236                 K     K A4003     1555   1555  2.92  
LINK         O   ASP A 238                 K     K A4003     1555   1555  2.76  
LINK         O   ILE A 242                 K     K A4003     1555   1555  2.65  
LINK         OG  SER A 247                 K     K A4003     1555   1555  2.74  
LINK         OE1 GLN A 285                MN    MN A4002     1555   1555  2.06  
LINK         OE1 GLN A 285                 K     K A4017     1555   1555  2.92  
LINK         CD  GLU A 299                MN    MN A4001     1555   1555  2.58  
LINK         OE1 GLU A 299                MN    MN A4001     1555   1555  2.25  
LINK         OE1 GLU A 299                 K     K A4004     1555   1555  2.77  
LINK         OE2 GLU A 299                MN    MN A4001     1555   1555  2.33  
LINK         OE2 GLU A 299                MN    MN A4002     1555   1555  2.22  
LINK         O   MET A 300                 K     K A4004     1555   1555  2.69  
LINK         CG  ASN A 301                MN    MN A4001     1555   1555  2.89  
LINK         OD1 ASN A 301                MN    MN A4001     1555   1555  1.97  
LINK         OE2 GLU A 761                 K     K A4009     1555   1555  2.76  
LINK         ND1 HIS A 781                 K     K A4009     1555   1555  2.84  
LINK         O   GLU A 783                 K     K A4009     1555   1555  2.83  
LINK         O   GLN A 784                 K     K A4009     1555   1555  2.83  
LINK         O   VAL A 787                 K     K A4009     1555   1555  2.63  
LINK         OG  SER A 792                 K     K A4009     1555   1555  2.76  
LINK         OE1 GLN A 829                MN    MN A4007     1555   1555  2.10  
LINK         OE1 GLU A 841                 K     K A4008     1555   1555  2.83  
LINK         OE2 GLU A 841                MN    MN A4007     1555   1555  2.29  
LINK         OE2 GLU A 841                 K     K A4008     1555   1555  2.59  
LINK         OD1 ASN A 843                 K     K A4008     1555   1555  2.88  
LINK         O   HIS B  16                 K     K B4016     1555   1555  2.67  
LINK         O   ASP B 112                 K     K B4016     1555   1555  2.74  
LINK         OG1 THR C 114                 K     K C4038     1555   1555  2.40  
LINK         OE1 GLU C 127                 K     K C4024     1555   1555  2.83  
LINK         OE2 GLU C 215                 K     K C4023     1555   1555  2.83  
LINK         OD1 ASN C 236                 K     K C4023     1555   1555  2.73  
LINK         O   ASP C 238                 K     K C4023     1555   1555  2.70  
LINK         O   ALA C 239                 K     K C4023     1555   1555  2.82  
LINK         O   ILE C 242                 K     K C4023     1555   1555  2.70  
LINK         OG  SER C 247                 K     K C4023     1555   1555  2.73  
LINK         OE1 GLN C 285                MN    MN C4022     1555   1555  1.99  
LINK         OE1 GLN C 285                 K     K C4037     1555   1555  2.48  
LINK         CD  GLU C 299                MN    MN C4021     1555   1555  2.57  
LINK         OE1 GLU C 299                 K     K C4024     1555   1555  2.66  
LINK         OE1 GLU C 299                MN    MN C4021     1555   1555  2.20  
LINK         OE2 GLU C 299                MN    MN C4022     1555   1555  2.27  
LINK         OE2 GLU C 299                MN    MN C4021     1555   1555  2.35  
LINK         O   MET C 300                 K     K C4024     1555   1555  2.77  
LINK         OD1 ASN C 301                MN    MN C4021     1555   1555  2.21  
LINK         OE2 GLU C 761                 K     K C4029     1555   1555  2.76  
LINK         O   GLU C 783                 K     K C4029     1555   1555  2.72  
LINK         O   VAL C 787                 K     K C4029     1555   1555  2.64  
LINK         OG  SER C 792                 K     K C4029     1555   1555  2.77  
LINK         OE1 GLN C 829                MN    MN C4027     1555   1555  2.24  
LINK         OE2 GLU C 841                MN    MN C4027     1555   1555  2.24  
LINK         O   HIS D  16                 K     K D4036     1555   1555  2.68  
LINK         O   ASP D 112                 K     K D4036     1555   1555  2.71  
LINK         O   ASP E  84                 K     K E4059     1555   1555  2.77  
LINK         O   GLY E 112                 K     K E4059     1555   1555  2.70  
LINK         OG1 THR E 114                 K     K E4059     1555   1555  2.64  
LINK         OE1 GLU E 127                 K     K E4045     1555   1555  2.85  
LINK         OE2 GLU E 215                 K     K E4044     1555   1555  2.50  
LINK         OD1 ASN E 236                 K     K E4044     1555   1555  2.74  
LINK         O   ASP E 238                 K     K E4044     1555   1555  2.78  
LINK         O   ALA E 239                 K     K E4044     1555   1555  2.87  
LINK         O   ILE E 242                 K     K E4044     1555   1555  2.67  
LINK         OG  SER E 247                 K     K E4044     1555   1555  2.71  
LINK         OE1 GLN E 285                 K     K E4058     1555   1555  2.72  
LINK         OE1 GLN E 285                MN    MN E4043     1555   1555  2.09  
LINK         CD  GLU E 299                MN    MN E4042     1555   1555  2.65  
LINK         OE1 GLU E 299                 K     K E4045     1555   1555  2.66  
LINK         OE1 GLU E 299                MN    MN E4042     1555   1555  2.30  
LINK         OE2 GLU E 299                MN    MN E4043     1555   1555  2.21  
LINK         OE2 GLU E 299                MN    MN E4042     1555   1555  2.37  
LINK         O   MET E 300                 K     K E4045     1555   1555  2.65  
LINK         OD1 ASN E 301                MN    MN E4042     1555   1555  2.20  
LINK         OE2 GLU E 761                 K     K E4050     1555   1555  2.73  
LINK         ND1 HIS E 781                 K     K E4050     1555   1555  2.85  
LINK         O   GLU E 783                 K     K E4050     1555   1555  2.73  
LINK         O   VAL E 787                 K     K E4050     1555   1555  2.57  
LINK         OG  SER E 792                 K     K E4050     1555   1555  2.63  
LINK         OE1 GLN E 829                MN    MN E4048     1555   1555  2.23  
LINK         OE2 GLU E 841                MN    MN E4048     1555   1555  2.11  
LINK         OE2 GLU E 841                 K     K E4049     1555   1555  2.75  
LINK         O   HIS F  16                 K     K F4057     1555   1555  2.75  
LINK         O   ASP F 112                 K     K F4057     1555   1555  2.76  
LINK         O   GLY G 112                 K     K G4080     1555   1555  2.81  
LINK         OG1 THR G 114                 K     K G4080     1555   1555  2.75  
LINK         O   THR G 143                 K     K G4081     1555   1555  2.86  
LINK         OG1 THR G 143                 K     K G4081     1555   1555  2.88  
LINK         OE2 GLU G 215                 K     K G4065     1555   1555  2.21  
LINK         OD1 ASN G 236                 K     K G4065     1555   1555  2.85  
LINK         O   ASP G 238                 K     K G4065     1555   1555  2.85  
LINK         O   ALA G 239                 K     K G4065     1555   1555  2.80  
LINK         O   ILE G 242                 K     K G4065     1555   1555  2.65  
LINK         OG  SER G 247                 K     K G4065     1555   1555  2.86  
LINK         OE1 GLN G 285                 K     K G4079     1555   1555  2.53  
LINK         OE1 GLN G 285                MN    MN G4064     1555   1555  2.08  
LINK         CD  GLU G 299                MN    MN G4063     1555   1555  2.61  
LINK         OE1 GLU G 299                 K     K G4066     1555   1555  2.70  
LINK         OE1 GLU G 299                MN    MN G4063     1555   1555  2.22  
LINK         OE2 GLU G 299                MN    MN G4064     1555   1555  2.20  
LINK         OE2 GLU G 299                MN    MN G4063     1555   1555  2.35  
LINK         O   MET G 300                 K     K G4066     1555   1555  2.83  
LINK         OD1 ASN G 301                MN    MN G4063     1555   1555  2.08  
LINK         OE2 GLU G 761                 K     K G4071     1555   1555  2.61  
LINK         ND1 HIS G 781                 K     K G4071     1555   1555  2.78  
LINK         O   GLU G 783                 K     K G4071     1555   1555  2.62  
LINK         O   GLN G 784                 K     K G4071     1555   1555  2.76  
LINK         O   VAL G 787                 K     K G4071     1555   1555  2.80  
LINK         OG  SER G 792                 K     K G4071     1555   1555  2.68  
LINK         OE1 GLN G 829                MN    MN G4069     1555   1555  2.31  
LINK         OE1 GLU G 841                 K     K G4070     1555   1555  2.82  
LINK         OE2 GLU G 841                MN    MN G4069     1555   1555  2.25  
LINK         O   ASP H 112                 K     K H4078     1555   1555  2.72  
LINK        MN    MN A4001                 O3B ADP A4000     1555   1555  2.07  
LINK        MN    MN A4001                 O   HOH A4139     1555   1555  2.12  
LINK        MN    MN A4001                 O1  PO4 A4005     1555   1555  2.17  
LINK        MN    MN A4002                 O1B ADP A4000     1555   1555  2.19  
LINK        MN    MN A4002                 O3  PO4 A4005     1555   1555  2.06  
LINK        MN    MN A4002                 O1A ADP A4000     1555   1555  2.05  
LINK        MN    MN A4002                 O   HOH A4136     1555   1555  2.07  
LINK        MN    MN A4007                 O2A ADP A4006     1555   1555  2.09  
LINK        MN    MN A4007                 O   HOH A4580     1555   1555  2.27  
LINK        MN    MN A4007                 O3B ADP A4006     1555   1555  2.19  
LINK        MN    MN A4007                 O   HOH A4850     1555   1555  2.46  
LINK         K     K A4008                 O2B ADP A4006     1555   1555  2.51  
LINK         K     K B4016                 O   HOH A4567     1555   1555  2.82  
LINK         K     K A4017                 O   HOH A4145     1555   1555  2.81  
LINK         K     K A4018                 O   HOH A4158     1555   1555  2.92  
LINK         K     K A4019                 O   HOH A4244     1555   1555  2.69  
LINK        MN    MN C4021                 O3B ADP C4020     1555   1555  2.04  
LINK        MN    MN C4021                 O   HOH C4104     1555   1555  2.20  
LINK        MN    MN C4021                 O1  PO4 C4025     1555   1555  2.19  
LINK        MN    MN C4022                 O1A ADP C4020     1555   1555  2.06  
LINK        MN    MN C4022                 O   HOH C4101     1555   1555  2.16  
LINK        MN    MN C4022                 O3  PO4 C4025     1555   1555  2.08  
LINK        MN    MN C4022                 O1B ADP C4020     1555   1555  2.17  
LINK         K     K E4059                 O   HOH E4167     1555   1555  2.84  
LINK         K     K C4024                 O   HOH C4105     1555   1555  2.80  
LINK         K     K C4024                 O   HOH C4645     1555   1555  2.77  
LINK        MN    MN C4027                 O3B ADP C4026     1555   1555  2.00  
LINK        MN    MN C4027                 O   HOH C4531     1555   1555  2.36  
LINK        MN    MN C4027                 O2A ADP C4026     1555   1555  2.23  
LINK        MN    MN C4027                 O   HOH C4530     1555   1555  2.55  
LINK        MN    MN G4063                 O   HOH G4152     1555   1555  2.37  
LINK        MN    MN G4063                 O1  PO4 G4067     1555   1555  1.97  
LINK        MN    MN G4063                 O3B ADP G4062     1555   1555  2.26  
LINK         K     K C4028                 O2B ADP C4026     1555   1555  2.43  
LINK        MN    MN G4064                 O3  PO4 G4067     1555   1555  2.19  
LINK        MN    MN G4064                 O   HOH G4149     1555   1555  2.24  
LINK        MN    MN G4064                 O1A ADP G4062     1555   1555  2.05  
LINK        MN    MN G4064                 O1B ADP G4062     1555   1555  2.24  
LINK         K     K G4066                 O   HOH G4152     1555   1555  2.84  
LINK        MN    MN G4069                 O3B ADP G4068     1555   1555  2.40  
LINK        MN    MN G4069                 O2A ADP G4068     1555   1555  2.22  
LINK         K     K G4070                 O2B ADP G4068     1555   1555  2.84  
LINK         K     K D4036                 O   HOH D1603     1555   1555  2.85  
LINK         K     K D4036                 O   HOH C4519     1555   1555  2.82  
LINK         K     K C4037                 O   HOH C4110     1555   1555  2.91  
LINK         K     K C4037                 O3  PO4 C4025     1555   1555  2.77  
LINK         K     K C4039                 O   HOH C4203     1555   1555  2.42  
LINK        MN    MN E4042                 O3B ADP E4041     1555   1555  2.02  
LINK        MN    MN E4042                 O   HOH E4143     1555   1555  2.20  
LINK        MN    MN E4042                 O1  PO4 E4046     1555   1555  2.06  
LINK         K     K H4078                 O   HOH H3632     1555   1555  2.86  
LINK        MN    MN E4043                 O1B ADP E4041     1555   1555  2.21  
LINK        MN    MN E4043                 O   HOH E4140     1555   1555  2.25  
LINK        MN    MN E4043                 O1A ADP E4041     1555   1555  2.09  
LINK        MN    MN E4043                 O3  PO4 E4046     1555   1555  2.06  
LINK         K     K G4079                 O3  PO4 G4067     1555   1555  2.77  
LINK         K     K G4080                 O   HOH G4172     1555   1555  2.85  
LINK         K     K E4045                 O   HOH E4144     1555   1555  2.58  
LINK         K     K G4081                 O   HOH G4246     1555   1555  2.51  
LINK        MN    MN E4048                 O2A ADP E4047     1555   1555  2.11  
LINK        MN    MN E4048                 O   HOH E4578     1555   1555  2.26  
LINK        MN    MN E4048                 O3B ADP E4047     1555   1555  2.02  
LINK        MN    MN E4048                 O   HOH E4579     1555   1555  2.41  
LINK         K     K E4049                 O   HOH E4153     1555   1555  2.18  
LINK         K     K F4057                 O   HOH F2544     1555   1555  2.59  
LINK         K     K F4057                 O   HOH F2541     1555   1555  2.83  
LINK         K     K A4003                 O   ALA A 239     1555   1555  2.95  
LINK         K     K A4004                 O   ALA A 126     1555   1555  3.22  
LINK         K     K A4004                 OE1 GLU A 127     1555   1555  3.02  
LINK         K     K A4004                 O   HOH A4137     1555   1555  3.02  
LINK         K     K A4004                 O   HOH A4139     1555   1555  3.02  
LINK         K     K A4004                 O   HOH A4140     1555   1555  3.00  
LINK         K     K A4004                 OD1 ASN A 301     1555   1555  3.34  
LINK         K     K A4008                 O3B ADP A4006     1555   1555  3.19  
LINK         K     K A4017                 OD1 ASN A 283     1555   1555  3.39  
LINK         K     K A4017                 O3  PO4 A4005     1555   1555  2.97  
LINK         K     K A4017                 OG1 THR A 244     1555   1555  3.09  
LINK         K     K A4017                 O   HOH A4144     1555   1555  3.25  
LINK         K     K A4017                 OE1 GLU A 217     1555   1555  2.94  
LINK         K     K A4017                 ND2 ASN A 283     1555   1555  3.62  
LINK         K     K A4018                 O   HOH A4156     1555   1555  3.07  
LINK         K     K A4019                 OG1 THR A 143     1555   1555  3.10  
LINK         K     K A4019                 O   ALA A 144     1555   1555  3.00  
LINK         K     K A4019                 O   HOH A4617     1555   1555  3.16  
LINK         K     K A4019                 O   THR A 143     1555   1555  2.97  
LINK         K     K A4019                 O   HOH A4250     1555   1555  2.95  
LINK         K     K B4016                 O   HOH A4569     1555   1555  3.14  
LINK         K     K B4016                 O   HOH B4068     1555   1555  2.93  
LINK         K     K B4016                 O   HOH B4069     1555   1555  2.94  
LINK         K     K C4024                 O   ALA C 126     1555   1555  3.43  
LINK         K     K C4024                 OD1 ASN C 301     1555   1555  3.42  
LINK         K     K C4024                MN    MN C4021     1555   1555  3.67  
LINK         K     K C4024                 O   HOH C4102     1555   1555  3.44  
LINK         K     K C4024                 O   HOH C4104     1555   1555  3.16  
LINK         K     K C4028                 OE1 GLU C 841     1555   1555  3.12  
LINK         K     K C4028                 OE2 GLU C 841     1555   1555  3.05  
LINK         K     K C4028                 OD1 ASN C 843     1555   1555  3.29  
LINK         K     K C4028                 O3B ADP C4026     1555   1555  3.38  
LINK         K     K C4028                 O   HOH C4114     1555   1555  2.97  
LINK         K     K C4029                 ND1 HIS C 781     1555   1555  3.09  
LINK         K     K C4029                 O   GLN C 784     1555   1555  2.93  
LINK         K     K C4037                 OE1 GLU C 217     1555   1555  3.18  
LINK         K     K C4037                 OD1 ASN C 283     1555   1555  3.66  
LINK         K     K C4037                 ND2 ASN C 283     1555   1555  3.66  
LINK         K     K C4037                 O   HOH C4109     1555   1555  3.49  
LINK         K     K C4037                 OG1 THR C 244     1555   1555  3.30  
LINK         K     K C4037                MN    MN C4022     1555   1555  3.47  
LINK         K     K C4037                 O   HOH C4101     1555   1555  3.71  
LINK         K     K C4038                 N   THR C 114     1555   1555  3.72  
LINK         K     K C4038                 O   GLY C 112     1555   1555  2.94  
LINK         K     K C4038                 O   HOH C4123     1555   1555  3.18  
LINK         K     K C4038                 O   ASP C  84     1555   1555  2.93  
LINK         K     K C4039                 OG1 THR C 143     1555   1555  3.12  
LINK         K     K C4039                 O   THR C 143     1555   1555  2.94  
LINK         K     K C4039                 O   HOH C4222     1555   1555  3.46  
LINK         K     K C4039                 O   ALA C 144     1555   1555  3.02  
LINK         K     K C4039                 O   HOH C4208     1555   1555  2.93  
LINK         K     K D4036                 O   HOH C4521     1555   1555  3.51  
LINK         K     K D4036                 O   HOH D1602     1555   1555  3.07  
LINK         K     K E4045                 OD1 ASN E 301     1555   1555  3.50  
LINK         K     K E4045                 O   HOH E4143     1555   1555  3.17  
LINK         K     K E4045                 O   ALA E 126     1555   1555  3.34  
LINK         K     K E4045                 O   HOH E4141     1555   1555  3.52  
LINK         K     K E4049                 O3B ADP E4047     1555   1555  3.30  
LINK         K     K E4049                 OE1 GLU E 841     1555   1555  3.05  
LINK         K     K E4049                 OD1 ASN E 843     1555   1555  3.05  
LINK         K     K E4049                 O2B ADP E4047     1555   1555  3.06  
LINK         K     K E4050                 O   GLN E 784     1555   1555  2.96  
LINK         K     K E4058                 O   HOH E4148     1555   1555  3.60  
LINK         K     K E4058                 O   HOH E4149     1555   1555  3.12  
LINK         K     K E4058                 OG1 THR E 244     1555   1555  3.46  
LINK         K     K E4058                 O3  PO4 E4046     1555   1555  3.05  
LINK         K     K E4058                 OE1 GLU E 217     1555   1555  2.98  
LINK         K     K E4058                 OD1 ASN E 283     1555   1555  3.14  
LINK         K     K E4058                MN    MN E4043     1555   1555  3.71  
LINK         K     K E4059                 O   HOH E4165     1555   1555  2.99  
LINK         K     K E4059                 O   HOH E4702     1555   1555  3.19  
LINK         K     K E4059                 O   HOH E4164     1555   1555  3.10  
LINK         K     K E4059                 N   THR E 114     1555   1555  3.70  
LINK         K     K E4060                 O   HOH E4256     1555   1555  3.22  
LINK         K     K E4060                 O   ALA E 144     1555   1555  2.95  
LINK         K     K E4060                 OG1 THR E 143     1555   1555  3.08  
LINK         K     K E4060                 O   THR E 143     1555   1555  3.19  
LINK         K     K E4060                 O   HOH E4271     1555   1555  3.19  
LINK         K     K F4057                 O   HOH E4574     1555   1555  3.60  
LINK         K     K F4057                 O   HOH F2545     1555   1555  2.97  
LINK         K     K G4066                 OD1 ASN G 301     1555   1555  3.42  
LINK         K     K G4066                MN    MN G4063     1555   1555  3.70  
LINK         K     K G4066                 O   ALA G 126     1555   1555  3.21  
LINK         K     K G4066                 O   HOH G4153     1555   1555  3.01  
LINK         K     K G4066                 O   HOH G4150     1555   1555  3.05  
LINK         K     K G4066                 OE1 GLU G 127     1555   1555  3.04  
LINK         K     K G4070                 O3B ADP G4068     1555   1555  3.24  
LINK         K     K G4070                 OD1 ASN G 843     1555   1555  3.39  
LINK         K     K G4070                 OE2 GLU G 841     1555   1555  2.97  
LINK         K     K G4079                MN    MN G4064     1555   1555  3.69  
LINK         K     K G4079                 OD1 ASN G 283     1555   1555  3.07  
LINK         K     K G4079                 OG1 THR G 244     1555   1555  3.60  
LINK         K     K G4079                 O   HOH G4158     1555   1555  2.93  
LINK         K     K G4079                 ND2 ASN G 283     1555   1555  3.46  
LINK         K     K G4079                 OE1 GLU G 217     1555   1555  3.11  
LINK         K     K G4080                 O   HOH G4170     1555   1555  3.52  
LINK         K     K G4080                 O   ASP G  84     1555   1555  3.11  
LINK         K     K G4080                 O   HOH G4171     1555   1555  3.55  
LINK         K     K G4081                 O   HOH G4251     1555   1555  2.95  
LINK         K     K G4081                 O   ALA G 144     1555   1555  3.12  
LINK         K     K H4078                 O   HIS H  16     1555   1555  3.18  
LINK         K     K H4078                 O   HOH G4531     1555   1555  3.39  
LINK         K     K H4078                 O   HOH H3805     1555   1555  3.26  
CISPEP   1 PHE A  164    PRO A  165          0        -3.94                     
CISPEP   2 ALA A  251    PRO A  252          0        -2.23                     
CISPEP   3 TYR A  710    PRO A  711          0         2.10                     
CISPEP   4 LEU A  796    PRO A  797          0         4.11                     
CISPEP   5 ARG A  998    PRO A  999          0        -3.92                     
CISPEP   6 SER B  357    PRO B  358          0         2.75                     
CISPEP   7 PHE C  164    PRO C  165          0        -0.70                     
CISPEP   8 ALA C  251    PRO C  252          0        -0.57                     
CISPEP   9 TYR C  710    PRO C  711          0         2.76                     
CISPEP  10 LEU C  796    PRO C  797          0         2.73                     
CISPEP  11 ARG C  998    PRO C  999          0        -6.10                     
CISPEP  12 SER D  357    PRO D  358          0         3.80                     
CISPEP  13 PHE E  164    PRO E  165          0         0.14                     
CISPEP  14 ALA E  251    PRO E  252          0        -1.78                     
CISPEP  15 TYR E  710    PRO E  711          0         0.50                     
CISPEP  16 LEU E  796    PRO E  797          0         1.44                     
CISPEP  17 ARG E  998    PRO E  999          0        -5.25                     
CISPEP  18 SER F  357    PRO F  358          0         2.86                     
CISPEP  19 PHE G  164    PRO G  165          0        -0.27                     
CISPEP  20 ALA G  251    PRO G  252          0        -0.37                     
CISPEP  21 TYR G  710    PRO G  711          0         2.29                     
CISPEP  22 LEU G  796    PRO G  797          0         2.20                     
CISPEP  23 ARG G  998    PRO G  999          0        -0.35                     
CISPEP  24 SER H  357    PRO H  358          0         2.31                     
SITE     1 AC1  5 GLU A 299  ASN A 301  ADP A4000  PO4 A4005                    
SITE     2 AC1  5 HOH A4139                                                     
SITE     1 AC2  5 GLN A 285  GLU A 299  ADP A4000  PO4 A4005                    
SITE     2 AC2  5 HOH A4136                                                     
SITE     1 AC3  6 GLU A 215  ASN A 236  ASP A 238  ALA A 239                    
SITE     2 AC3  6 ILE A 242  SER A 247                                          
SITE     1 AC4  8 ALA A 126  GLU A 127  GLU A 299  MET A 300                    
SITE     2 AC4  8 ASN A 301  HOH A4137  HOH A4139  HOH A4140                    
SITE     1 AC5  5 GLN A 829  GLU A 841  ADP A4006  HOH A4580                    
SITE     2 AC5  5 HOH A4850                                                     
SITE     1 AC6  3 GLU A 841  ASN A 843  ADP A4006                               
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  4 GLN A  93  THR A 173  MET A 174  HOH A4078                    
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 HOH A4567  ASP B 114                                          
SITE     1 BC3  5 HOH A4567  HIS B  16  ASP B 112  HOH B4068                    
SITE     2 BC3  5 HOH B4069                                                     
SITE     1 BC4  6 GLU A 217  THR A 244  ASN A 283  GLN A 285                    
SITE     2 BC4  6 PO4 A4005  HOH A4145                                          
SITE     1 BC5  5 ASP A  84  GLY A 112  THR A 114  HOH A4156                    
SITE     2 BC5  5 HOH A4158                                                     
SITE     1 BC6  4 THR A 143  ALA A 144  HOH A4244  HOH A4250                    
SITE     1 BC7  6 GLU C 299  ASN C 301  ADP C4020    K C4024                    
SITE     2 BC7  6 PO4 C4025  HOH C4104                                          
SITE     1 BC8  6 GLN C 285  GLU C 299  ADP C4020  PO4 C4025                    
SITE     2 BC8  6   K C4037  HOH C4101                                          
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  6 ASP E  84  GLY E 112  THR E 114  HOH E4164                    
SITE     2 CC1  6 HOH E4165  HOH E4167                                          
SITE     1 CC2  8 ALA C 126  GLU C 127  GLU C 299  MET C 300                    
SITE     2 CC2  8 ASN C 301   MN C4021  HOH C4105  HOH C4645                    
SITE     1 CC3  2 THR E 143  ALA E 144                                          
SITE     1 CC4  5 GLN C 829  GLU C 841  ADP C4026  HOH C4530                    
SITE     2 CC4  5 HOH C4531                                                     
SITE     1 CC5  7 GLU G 299  ASN G 301  ADP G4062   MN G4064                    
SITE     2 CC5  7   K G4066  PO4 G4067  HOH G4152                               
SITE     1 CC6  4 GLU C 841  ASN C 843  ADP C4026  HOH C4114                    
SITE     1 CC7  7 GLN G 285  GLU G 299  ADP G4062   MN G4063                    
SITE     2 CC7  7 PO4 G4067    K G4079  HOH G4149                               
SITE     1 CC8  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784                    
SITE     2 CC8  6 VAL C 787  SER C 792                                          
SITE     1 CC9  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239                    
SITE     2 CC9  6 ILE G 242  SER G 247                                          
SITE     1 DC1  2 THR C 173  MET C 174                                          
SITE     1 DC2  9 ALA G 126  GLU G 127  GLU G 299  MET G 300                    
SITE     2 DC2  9 ASN G 301   MN G4063  HOH G4150  HOH G4152                    
SITE     3 DC2  9 HOH G4153                                                     
SITE     1 DC3  3 ASN C 289  ASN C 292  ARG C 294                               
SITE     1 DC4  4 SER G 789  GLN G 829  GLU G 841  ADP G4068                    
SITE     1 DC5  5 ALA C 370  ASN C 371  PHE C 900  PRO C 901                    
SITE     2 DC5  5 GLY C 902                                                     
SITE     1 DC6  3 GLU G 841  ASN G 843  ADP G4068                               
SITE     1 DC7  2 ASP D 114  HOH D1598                                          
SITE     1 DC8  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784                    
SITE     2 DC8  6 VAL G 787  SER G 792                                          
SITE     1 DC9  5 HOH C4519  HIS D  16  ASP D 112  HOH D1602                    
SITE     2 DC9  5 HOH D1603                                                     
SITE     1 EC1  3 THR G 173  MET G 174  HOH G4087                               
SITE     1 EC2  7 GLU C 217  THR C 244  ASN C 283  GLN C 285                    
SITE     2 EC2  7  MN C4022  PO4 C4025  HOH C4110                               
SITE     1 EC3  3 ASN G 289  ASN G 292  ARG G 294                               
SITE     1 EC4  3 ASP C  84  GLY C 112  THR C 114                               
SITE     1 EC5  5 ALA G 370  ASN G 371  PHE G 900  PRO G 901                    
SITE     2 EC5  5 GLY G 902                                                     
SITE     1 EC6  4 THR C 143  ALA C 144  HOH C4203  HOH C4208                    
SITE     1 EC7  2 PHE H  15  ASP H 114                                          
SITE     1 EC8  6 GLU E 299  ASN E 301  ADP E4041   MN E4043                    
SITE     2 EC8  6 PO4 E4046  HOH E4143                                          
SITE     1 EC9  3 HIS H  16  ASP H 112  HOH H3632                               
SITE     1 FC1  6 GLN E 285  GLU E 299  ADP E4041   MN E4042                    
SITE     2 FC1  6 PO4 E4046  HOH E4140                                          
SITE     1 FC2  7 GLU G 217  THR G 244  ASN G 283  GLN G 285                    
SITE     2 FC2  7  MN G4064  PO4 G4067  HOH G4158                               
SITE     1 FC3  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239                    
SITE     2 FC3  6 ILE E 242  SER E 247                                          
SITE     1 FC4  4 ASP G  84  GLY G 112  THR G 114  HOH G4172                    
SITE     1 FC5  6 ALA E 126  GLU E 127  GLU E 299  MET E 300                    
SITE     2 FC5  6 ASN E 301  HOH E4144                                          
SITE     1 FC6  4 THR G 143  ALA G 144  HOH G4246  HOH G4251                    
SITE     1 FC7  5 GLN E 829  GLU E 841  ADP E4047  HOH E4578                    
SITE     2 FC7  5 HOH E4579                                                     
SITE     1 FC8  4 GLU E 841  ASN E 843  ADP E4047  HOH E4153                    
SITE     1 FC9  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784                    
SITE     2 FC9  6 VAL E 787  SER E 792                                          
SITE     1 GC1  3 MET E 174  NET E4052  HOH E4084                               
SITE     1 GC2  2 ASN E 289  ARG E 294                                          
SITE     1 GC3  3 ASN E 371  PRO E 901  GLY E 902                               
SITE     1 GC4  3 GLU E 549  ASP F 114  HOH F2540                               
SITE     1 GC5  5 HIS F  16  ASP F 112  HOH F2541  HOH F2544                    
SITE     2 GC5  5 HOH F2545                                                     
SITE     1 GC6  5 GLU E 217  THR E 244  ASN E 283  GLN E 285                    
SITE     2 GC6  5 PO4 E4046                                                     
SITE     1 GC7 14 MET E 174  GLY E 175  HIS E 243  GLN E 285                    
SITE     2 GC7 14 GLU E 299  ASN E 301  ARG E 303  ARG E 306                    
SITE     3 GC7 14 ADP E4041   MN E4042   MN E4043    K E4058                    
SITE     4 GC7 14 HOH E4149  HOH E4150                                          
SITE     1 GC8  1 GLU E 560                                                     
SITE     1 GC9 15 MET G 174  GLY G 175  HIS G 243  GLN G 285                    
SITE     2 GC9 15 GLU G 299  ASN G 301  ARG G 303  ARG G 306                    
SITE     3 GC9 15 ADP G4062   MN G4063   MN G4064    K G4079                    
SITE     4 GC9 15 HOH G4149  HOH G4158  HOH G4159                               
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 A4017                    
SITE     4 HC1 14 HOH A4145  HOH A4146                                          
SITE     1 HC2 14 MET C 174  GLY C 175  HIS C 243  GLN C 285                    
SITE     2 HC2 14 GLU C 299  ASN C 301  ARG C 303  ARG C 306                    
SITE     3 HC2 14 ADP C4020   MN C4021   MN C4022    K C4037                    
SITE     4 HC2 14 HOH C4110  HOH C4111                                          
SITE     1 HC3  1 ASP C 518                                                     
SITE     1 HC4 10 GLU A 783  ASP A 791  ALA A 793  GLU A 892                    
SITE     2 HC4 10 LEU A 907  TYR A1040  ASP A1041  THR A1042                    
SITE     3 HC4 10 HOH A4102  HOH A4131                                          
SITE     1 HC5 10 HOH A4895  HOH A4896  GLU C 783  ASP C 791                    
SITE     2 HC5 10 ALA C 793  GLU C 892  VAL C 893  TYR C1040                    
SITE     3 HC5 10 ASP C1041  THR C1042                                          
SITE     1 HC6  8 HOH A4898  GLU E 783  ASP E 791  GLU E 892                    
SITE     2 HC6  8 VAL E 893  TYR E1040  ASP E1041  THR E1042                    
SITE     1 HC7  9 HOH A4900  HOH A4901  GLU G 783  ASP G 791                    
SITE     2 HC7  9 GLU G 892  LEU G 907  TYR G1040  ASP G1041                    
SITE     3 HC7  9 THR G1042                                                     
SITE     1 HC8 27 ARG E 129  ILE E 167  ARG E 169  THR E 173                    
SITE     2 HC8 27 MET E 174  GLY E 175  GLY E 176  GLU E 208                    
SITE     3 HC8 27 LEU E 210  ILE E 211  GLU E 215  MET E 240                    
SITE     4 HC8 27 GLY E 241  ILE E 242  HIS E 243  THR E 244                    
SITE     5 HC8 27 GLN E 285  ILE E 298  GLU E 299  THR E 376                    
SITE     6 HC8 27  MN E4042   MN E4043  PO4 E4046  HOH E4136                    
SITE     7 HC8 27 HOH E4140  HOH E4143  HOH E4577                               
SITE     1 HC9 19 PRO E 690  ARG E 715  MET E 725  HIS E 754                    
SITE     2 HC9 19 PHE E 755  LEU E 756  GLU E 761  ALA E 785                    
SITE     3 HC9 19 GLY E 786  VAL E 787  HIS E 788  SER E 789                    
SITE     4 HC9 19 GLN E 829  GLU E 841   MN E4048    K E4049                    
SITE     5 HC9 19 HOH E4152  HOH E4153  HOH E4578                               
SITE     1 IC1  2 THR E  94   CL E4053                                          
SITE     1 IC2 26 ARG G 129  ILE G 167  ARG G 169  THR G 173                    
SITE     2 IC2 26 MET G 174  GLY G 175  GLY G 176  GLU G 208                    
SITE     3 IC2 26 LEU G 210  ILE G 211  GLU G 215  MET G 240                    
SITE     4 IC2 26 GLY G 241  ILE G 242  HIS G 243  THR G 244                    
SITE     5 IC2 26 GLN G 285  ILE G 298  GLU G 299  THR G 376                    
SITE     6 IC2 26  MN G4063   MN G4064  PO4 G4067  HOH G4145                    
SITE     7 IC2 26 HOH G4149  HOH G4540                                          
SITE     1 IC3 16 PRO G 690  ARG G 715  MET G 725  HIS G 754                    
SITE     2 IC3 16 PHE G 755  LEU G 756  GLU G 761  ALA G 785                    
SITE     3 IC3 16 GLY G 786  VAL G 787  HIS G 788  SER G 789                    
SITE     4 IC3 16 GLN G 829  GLU G 841   MN G4069    K G4070                    
SITE     1 IC4  4 GLN G  22  THR G  94  ASN G  97  HOH G4130                    
SITE     1 IC5 27 ARG A 129  ILE A 167  ARG A 169  MET A 174                    
SITE     2 IC5 27 GLY A 175  GLY A 176  ASP A 207  GLU A 208                    
SITE     3 IC5 27 LEU A 210  ILE A 211  GLU A 215  MET A 240                    
SITE     4 IC5 27 GLY A 241  ILE A 242  HIS A 243  THR A 244                    
SITE     5 IC5 27 GLN A 285  ILE A 298  GLU A 299  THR A 376                    
SITE     6 IC5 27  MN A4001   MN A4002  PO4 A4005  HOH A4132                    
SITE     7 IC5 27 HOH A4136  HOH A4139  HOH A4579                               
SITE     1 IC6 20 PRO A 690  ARG A 715  MET A 725  HIS A 754                    
SITE     2 IC6 20 PHE A 755  LEU A 756  GLU A 761  ALA A 785                    
SITE     3 IC6 20 GLY A 786  VAL A 787  HIS A 788  SER A 789                    
SITE     4 IC6 20 GLN A 829  GLU A 841   MN A4007    K A4008                    
SITE     5 IC6 20 HOH A4148  HOH A4150  HOH A4580  HOH A4850                    
SITE     1 IC7  2 GLN A  22  THR A  94                                          
SITE     1 IC8 27 ARG C 129  ILE C 167  ARG C 169  THR C 173                    
SITE     2 IC8 27 MET C 174  GLY C 175  GLY C 176  GLU C 208                    
SITE     3 IC8 27 LEU C 210  ILE C 211  GLU C 215  MET C 240                    
SITE     4 IC8 27 GLY C 241  ILE C 242  HIS C 243  THR C 244                    
SITE     5 IC8 27 GLN C 285  ILE C 298  GLU C 299  THR C 376                    
SITE     6 IC8 27  MN C4021   MN C4022  PO4 C4025  HOH C4097                    
SITE     7 IC8 27 HOH C4101  HOH C4104  HOH C4527                               
SITE     1 IC9 19 PRO C 690  ARG C 715  MET C 725  HIS C 754                    
SITE     2 IC9 19 PHE C 755  LEU C 756  GLU C 761  ALA C 785                    
SITE     3 IC9 19 GLY C 786  VAL C 787  HIS C 788  SER C 789                    
SITE     4 IC9 19 GLN C 829  GLU C 841   MN C4027    K C4028                    
SITE     5 IC9 19 HOH C4113  HOH C4114  HOH C4531                               
SITE     1 JC1  4 GLN C  22  THR C  94  ASN C  97  ASN C 936                    
CRYST1  152.600  164.600  332.700  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      0.006553  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006075  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003006        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system