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Database: PDB
Entry: 1T36
LinkDB: 1T36
Original site: 1T36 
HEADER    LIGASE                                  24-APR-04   1T36              
TITLE     CRYSTAL STRUCTURE OF E. COLI CARBAMOYL PHOSPHATE SYNTHETASE SMALL     
TITLE    2 SUBUNIT MUTANT C248D COMPLEXED WITH URIDINE 5'-MONOPHOSPHATE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBAMOYL-PHOSPHATE SYNTHASE LARGE CHAIN;                  
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: CARBAMOYL-PHOSPHATE SYNTHETASE AMMONIA CHAIN;               
COMPND   5 EC: 6.3.5.5;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN;                  
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 SYNONYM: CARBAMOYL-PHOSPHATE SYNTHETASE GLUTAMINE CHAIN;             
COMPND  11 EC: 6.3.5.5;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: CARB, PYRA, B0033;                                             
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 562;                                                 
SOURCE  13 GENE: CARA, PYRA, B0032, Z0037, ECS0035;                             
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PET15                                     
KEYWDS    CHANNELING, PYRIMIDINE BIOSYNTHESIS, ARGININE BIOSYNTHESIS, LIGASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN                             
REVDAT   3   13-JUL-11 1T36    1       VERSN                                    
REVDAT   2   24-FEB-09 1T36    1       VERSN                                    
REVDAT   1   21-SEP-04 1T36    0                                                
JRNL        AUTH   J.B.THODEN,X.HUANG,J.KIM,F.M.RAUSHEL,H.M.HOLDEN              
JRNL        TITL   LONG-RANGE ALLOSTERIC TRANSITIONS IN CARBAMOYL PHOSPHATE     
JRNL        TITL 2 SYNTHETASE.                                                  
JRNL        REF    PROTEIN SCI.                  V.  13  2398 2004              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   15322282                                                     
JRNL        DOI    10.1110/PS.04822704                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 433843                         
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDON                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 42551                           
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
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) : 433843                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 44228                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 458                                     
REMARK   3   SOLVENT ATOMS            : 3907                                    
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) : 2.430 ; 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 1T36 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022253.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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) : 0.65                               
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          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 433843                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.20300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: TNT                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1JDB                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TETRAMETHYLAMMONIUM            
REMARK 280  CHLORIDE, POTASSIUM CHLORIDE, MANGANESE CHLORIDE, ORNITHINE, ADP,   
REMARK 280  HEPES, PH 7.4, BATCH, TEMPERATURE 277K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       76.25000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      166.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       82.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      166.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       82.45000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: HETERO-OCTAMER COMPRISING CHAINS                             
REMARK 300 A,B,C,D,E,F,G,H.   THESE CHAINS,                                     
REMARK 300 AS DEPOSITED, REPRESENT THE BIOLOGICAL                               
REMARK 300 ASSEBMLY                                                             
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   717                                                      
REMARK 465     TYR A   718                                                      
REMARK 465     VAL A   719                                                      
REMARK 465     LEU A   720                                                      
REMARK 465     GLY A   721                                                      
REMARK 465     GLY A   722                                                      
REMARK 465     ARG A   723                                                      
REMARK 465     VAL A   742                                                      
REMARK 465     SER A   743                                                      
REMARK 465     VAL A   744                                                      
REMARK 465     SER A   745                                                      
REMARK 465     ASN A   746                                                      
REMARK 465     ASP A   747                                                      
REMARK 465     ALA A   748                                                      
REMARK 465     PRO A   749                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   381                                                      
REMARK 465     LYS B   382                                                      
REMARK 465     SER C   717                                                      
REMARK 465     TYR C   718                                                      
REMARK 465     VAL C   719                                                      
REMARK 465     LEU C   720                                                      
REMARK 465     GLY C   721                                                      
REMARK 465     GLY C   722                                                      
REMARK 465     ARG C   723                                                      
REMARK 465     VAL C   742                                                      
REMARK 465     SER C   743                                                      
REMARK 465     VAL C   744                                                      
REMARK 465     SER C   745                                                      
REMARK 465     ASN C   746                                                      
REMARK 465     ASP C   747                                                      
REMARK 465     ALA C   748                                                      
REMARK 465     PRO C   749                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D   381                                                      
REMARK 465     LYS D   382                                                      
REMARK 465     SER E   717                                                      
REMARK 465     TYR E   718                                                      
REMARK 465     VAL E   719                                                      
REMARK 465     LEU E   720                                                      
REMARK 465     GLY E   721                                                      
REMARK 465     GLY E   722                                                      
REMARK 465     ARG E   723                                                      
REMARK 465     VAL E   742                                                      
REMARK 465     SER E   743                                                      
REMARK 465     VAL E   744                                                      
REMARK 465     SER E   745                                                      
REMARK 465     ASN E   746                                                      
REMARK 465     ASP E   747                                                      
REMARK 465     ALA E   748                                                      
REMARK 465     PRO E   749                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F   381                                                      
REMARK 465     LYS F   382                                                      
REMARK 465     SER G   717                                                      
REMARK 465     TYR G   718                                                      
REMARK 465     VAL G   719                                                      
REMARK 465     LEU G   720                                                      
REMARK 465     GLY G   721                                                      
REMARK 465     GLY G   722                                                      
REMARK 465     ARG G   723                                                      
REMARK 465     VAL G   742                                                      
REMARK 465     SER G   743                                                      
REMARK 465     VAL G   744                                                      
REMARK 465     SER G   745                                                      
REMARK 465     ASN G   746                                                      
REMARK 465     ASP G   747                                                      
REMARK 465     ALA G   748                                                      
REMARK 465     PRO G   749                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ALA H   381                                                      
REMARK 465     LYS H   382                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A 716    CG   CD                                             
REMARK 470     PRO C 716    CG   CD                                             
REMARK 470     PRO E 716    CG   CD                                             
REMARK 470     PRO G 716    CG   CD                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH E  1221     O    HOH F  1026              2.09            
REMARK 500   O    HOH A  1734     O    HOH A  1735              2.12            
REMARK 500   O    HOH A  1435     O    HOH A  1436              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1848     O    HOH C  1912     4555     2.14            
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  72   CD    GLU A  72   OE2     0.072                       
REMARK 500    GLU A 109   CD    GLU A 109   OE2     0.087                       
REMARK 500    GLU A 110   CD    GLU A 110   OE2     0.067                       
REMARK 500    GLU A 153   CD    GLU A 153   OE2     0.070                       
REMARK 500    GLU A 186   CD    GLU A 186   OE2     0.076                       
REMARK 500    GLU A 203   CD    GLU A 203   OE2     0.073                       
REMARK 500    GLU A 217   CD    GLU A 217   OE2     0.082                       
REMARK 500    GLU A 219   CD    GLU A 219   OE2     0.070                       
REMARK 500    GLU A 334   CD    GLU A 334   OE2     0.070                       
REMARK 500    GLU A 365   CD    GLU A 365   OE2     0.071                       
REMARK 500    GLU A 467   CD    GLU A 467   OE2     0.073                       
REMARK 500    GLU A 473   CD    GLU A 473   OE2     0.076                       
REMARK 500    GLU A 478   CD    GLU A 478   OE2     0.080                       
REMARK 500    GLU A 510   CD    GLU A 510   OE2     0.067                       
REMARK 500    GLU A 512   CD    GLU A 512   OE2     0.074                       
REMARK 500    GLU A 577   CD    GLU A 577   OE2     0.070                       
REMARK 500    GLU A 591   CD    GLU A 591   OE2     0.076                       
REMARK 500    GLU A 624   CD    GLU A 624   OE2     0.066                       
REMARK 500    GLU A 633   CD    GLU A 633   OE2     0.069                       
REMARK 500    GLU A 676   CD    GLU A 676   OE2     0.078                       
REMARK 500    GLU A 683   CD    GLU A 683   OE2     0.074                       
REMARK 500    GLU A 699   CD    GLU A 699   OE2     0.084                       
REMARK 500    GLU A 703   CD    GLU A 703   OE2     0.067                       
REMARK 500    GLU A 707   CD    GLU A 707   OE2     0.081                       
REMARK 500    GLU A 726   CD    GLU A 726   OE2     0.075                       
REMARK 500    GLU A 771   CD    GLU A 771   OE2     0.070                       
REMARK 500    GLU A 780   CD    GLU A 780   OE2     0.073                       
REMARK 500    GLU A 783   CD    GLU A 783   OE2     0.072                       
REMARK 500    GLU A 804   CD    GLU A 804   OE2     0.070                       
REMARK 500    GLU A 876   CD    GLU A 876   OE2     0.072                       
REMARK 500    GLU A 910   CD    GLU A 910   OE2     0.078                       
REMARK 500    GLU A 951   CD    GLU A 951   OE2     0.077                       
REMARK 500    GLU A 955   CD    GLU A 955   OE2     0.083                       
REMARK 500    GLU A 970   CD    GLU A 970   OE2     0.068                       
REMARK 500    GLU A 983   CD    GLU A 983   OE2     0.070                       
REMARK 500    GLU A1009   CD    GLU A1009   OE2     0.084                       
REMARK 500    GLU B 145   CD    GLU B 145   OE2     0.073                       
REMARK 500    GLU B 161   CD    GLU B 161   OE2     0.067                       
REMARK 500    GLU B 166   CD    GLU B 166   OE2     0.083                       
REMARK 500    GLU B 183   CD    GLU B 183   OE2     0.088                       
REMARK 500    GLU B 226   CD    GLU B 226   OE2     0.081                       
REMARK 500    GLU B 260   CD    GLU B 260   OE2     0.074                       
REMARK 500    GLU B 301   CD    GLU B 301   OE2     0.071                       
REMARK 500    GLU B 372   CD    GLU B 372   OE2     0.075                       
REMARK 500    GLU B 375   CD    GLU B 375   OE2     0.069                       
REMARK 500    GLU C  39   CD    GLU C  39   OE2     0.078                       
REMARK 500    GLU C  72   CD    GLU C  72   OE2     0.070                       
REMARK 500    GLU C 109   CD    GLU C 109   OE2     0.078                       
REMARK 500    GLU C 110   CD    GLU C 110   OE2     0.069                       
REMARK 500    GLU C 127   CD    GLU C 127   OE2     0.078                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     194 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A   6   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    TYR A  42   CB  -  CG  -  CD2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    TYR A  42   CB  -  CG  -  CD1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A  43   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ASP A  57   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A  82   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 130   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ASP A 161   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG A 169   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    PHE A 237   CB  -  CG  -  CD1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ASP A 246   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    TYR A 261   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ALA A 287   N   -  CA  -  CB  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 294   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 294   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP A 333   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A 343   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 373   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 400   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 400   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP A 416   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP A 416   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 441   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 459   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 460   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 460   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP A 487   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ARG A 490   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    TYR A 520   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ASP A 521   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 558   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 558   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP A 579   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP A 579   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASP A 609   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP A 609   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     407 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     -169.63    -79.47                                   
REMARK 500    ALA A  23     -149.44   -110.17                                   
REMARK 500    ALA A  52       34.59    -87.20                                   
REMARK 500    ARG A 303     -175.30   -176.04                                   
REMARK 500    ASP A 353       44.96   -108.52                                   
REMARK 500    ASN A 363       35.13   -146.68                                   
REMARK 500    THR A 375     -155.92   -144.09                                   
REMARK 500    THR A 531      -13.35     73.44                                   
REMARK 500    ASP A 558      -78.94    -52.88                                   
REMARK 500    THR A 664      126.62    -30.45                                   
REMARK 500    ARG A 736      -59.17    -29.98                                   
REMARK 500    GLN A 739      -70.11    -51.67                                   
REMARK 500    ASP A 758       54.57     38.65                                   
REMARK 500    HIS A 788      140.44    -38.83                                   
REMARK 500    ARG A1020      -54.55    -27.20                                   
REMARK 500    ASP B  11       -7.21    -53.69                                   
REMARK 500    GLU B  96      129.74   -174.35                                   
REMARK 500    ASN B 154       85.74    -36.07                                   
REMARK 500    ASP B 188       -5.56    -52.56                                   
REMARK 500    ASN B 232       68.24     66.47                                   
REMARK 500    CYS B 269     -106.71     63.91                                   
REMARK 500    ALA B 278       -6.79    -56.25                                   
REMARK 500    ASN B 311       82.90   -165.37                                   
REMARK 500    PRO B 346       42.15    -94.64                                   
REMARK 500    ALA B 356     -133.51     42.84                                   
REMARK 500    SER B 357       70.24     59.43                                   
REMARK 500    PRO C   2     -163.82    -79.45                                   
REMARK 500    ALA C  23     -156.30   -108.00                                   
REMARK 500    ALA C  52       44.88    -83.61                                   
REMARK 500    ALA C 239     -173.29    -67.32                                   
REMARK 500    ASN C 292       10.44   -154.83                                   
REMARK 500    PRO C 302       43.80    -72.50                                   
REMARK 500    ASN C 363       35.59   -149.78                                   
REMARK 500    ALA C 368      -55.97    -23.95                                   
REMARK 500    THR C 531       -4.93     75.74                                   
REMARK 500    ALA C 541       78.33   -112.18                                   
REMARK 500    GLU C 548     -156.30   -133.41                                   
REMARK 500    GLU C 549      -61.32    -99.23                                   
REMARK 500    THR C 664      125.68    -37.87                                   
REMARK 500    ASP C 758       46.16     38.62                                   
REMARK 500    ASN C 835       18.40     49.63                                   
REMARK 500    HIS C 975      -70.77    -34.18                                   
REMARK 500    ASP D  11        1.65    -64.30                                   
REMARK 500    ARG D  50       -6.64     71.48                                   
REMARK 500    ASN D 154       51.79    -31.31                                   
REMARK 500    THR D 171       33.47   -146.57                                   
REMARK 500    ASP D 188        5.24    -69.98                                   
REMARK 500    LEU D 229      -35.58    -39.54                                   
REMARK 500    ASN D 232       62.48     62.15                                   
REMARK 500    CYS D 269     -110.57     65.31                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     127 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ALA A  23        23.5      L          L   OUTSIDE RANGE           
REMARK 500    MET A  55        23.1      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 118        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 339        20.5      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 368        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 435        24.1      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 512        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 625        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 651        23.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 726        23.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 804        24.4      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 811        23.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 949        23.9      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 975        22.6      L          L   OUTSIDE RANGE           
REMARK 500    ASN A1007        24.3      L          L   OUTSIDE RANGE           
REMARK 500    SER B   4        23.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP B  11        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ALA B 127        23.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 154         4.3      L          L   EXPECTING SP3           
REMARK 500    PHE B 192        23.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP B 249        17.8      L          L   OUTSIDE RANGE           
REMARK 500    MET B 306        24.4      L          L   OUTSIDE RANGE           
REMARK 500    THR B 328        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ALA C  23        23.5      L          L   OUTSIDE RANGE           
REMARK 500    MET C  55        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 139        23.3      L          L   OUTSIDE RANGE           
REMARK 500    THR C 143        24.3      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 339        17.6      L          L   OUTSIDE RANGE           
REMARK 500    ARG C 400        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG C 435        23.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 625        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ALA C 651        21.3      L          L   OUTSIDE RANGE           
REMARK 500    GLU C 673        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 730        21.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 861        21.3      L          L   OUTSIDE RANGE           
REMARK 500    ASP C1057        23.5      L          L   OUTSIDE RANGE           
REMARK 500    ILE C1072        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN D 154         1.4      L          L   EXPECTING SP3           
REMARK 500    ASN D 204        24.3      L          L   OUTSIDE RANGE           
REMARK 500    ASP D 249        17.8      L          L   OUTSIDE RANGE           
REMARK 500    THR D 328        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ALA E  23        21.7      L          L   OUTSIDE RANGE           
REMARK 500    PHE E  26        24.8      L          L   OUTSIDE RANGE           
REMARK 500    MET E  55        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE E 139        23.0      L          L   OUTSIDE RANGE           
REMARK 500    ALA E 149        23.1      L          L   OUTSIDE RANGE           
REMARK 500    PHE E 172        24.3      L          L   OUTSIDE RANGE           
REMARK 500    ILE E 339        17.3      L          L   OUTSIDE RANGE           
REMARK 500    ALA E 368        20.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG E 435        24.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      82 CHIRALITY DEVIATIONS.                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1224        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1225        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH A1243        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A1410        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A1479        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A1628        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A1632        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH A1643        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A1679        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A1711        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A1728        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH A1731        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH A1743        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A1744        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH A1770        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH A1779        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A1785        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A1909        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A1914        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A1923        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A1931        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH A1934        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH B3910        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH B3967        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH B3993        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH C1213        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH C1223        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH C1234        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH C1401        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH C1429        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH C1629        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH C1639        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH C1646        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH C1654        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH C1655        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH C1720        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH C1735        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH C1736        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH C1744        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH C1787        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH C1804        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH C1871        DISTANCE =  7.89 ANGSTROMS                       
REMARK 525    HOH C1872        DISTANCE =  8.61 ANGSTROMS                       
REMARK 525    HOH C1884        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH C1893        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH C1898        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH C1909        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH D2044        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH D2620        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH D2833        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH D2857        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH D2884        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH D2953        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH D2954        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH E1208        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH E1220        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH E1341        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH E1429        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH E1676        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH E1720        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH E1745        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH E1757        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH E1780        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH E1869        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH E1870        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH E1872        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH E1909        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH E1924        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH F1263        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH F1803        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH F1889        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH F1890        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH F1891        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH F1895        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH F1907        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH F1912        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH G1213        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH G1386        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH G1525        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH G1584        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH G1601        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH G1605        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH G1610        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH G1620        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH G1712        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH G1728        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH G1732        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH G1746        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH G1766        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH G1767        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH G1777        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH G1787        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH G1794        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH H 387        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH H 394        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH H 498        DISTANCE =  7.40 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1077   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 127   OE1                                                    
REMARK 620 2 GLU A 299   OE1 129.8                                              
REMARK 620 3 MET A 300   O    98.4  94.6                                        
REMARK 620 4 HOH A1607   O    99.6 102.2 138.1                                  
REMARK 620 5 HOH A1193   O   142.0  87.8  69.1  73.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1082   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 143   O                                                      
REMARK 620 2 THR A 143   OG1  67.1                                              
REMARK 620 3 HOH A1203   O   137.6  84.8                                        
REMARK 620 4 HOH A1202   O   121.7  73.7  75.6                                  
REMARK 620 5 HOH A1204   O    68.2  79.6  76.3 142.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1076   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 215   OE2                                                    
REMARK 620 2 ASN A 236   OD1  86.1                                              
REMARK 620 3 ASP A 238   O   122.6  89.5                                        
REMARK 620 4 ALA A 239   O    88.5 151.6  70.1                                  
REMARK 620 5 ILE A 242   O    84.3 119.4 143.2  87.7                            
REMARK 620 6 SER A 247   OG  139.6  77.5  94.3 122.2  72.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1075  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 285   OE1                                                    
REMARK 620 2 GLU A 299   OE2  77.8                                              
REMARK 620 3 PO4 A1078   O3   90.1  83.7                                        
REMARK 620 4 ADP A1087   O1B 175.9  98.5  87.9                                  
REMARK 620 5 ADP A1087   O1A  94.6  90.1 171.3  87.1                            
REMARK 620 6 HOH A1605   O    87.1 164.7  98.9  96.7  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1074  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 299   OE1                                                    
REMARK 620 2 GLU A 299   OE2  58.0                                              
REMARK 620 3 ASN A 301   OD1  85.6  90.1                                        
REMARK 620 4 ADP A1087   O3B  83.5  92.1 165.6                                  
REMARK 620 5 HOH A1191   O    98.9 156.4  82.5  89.8                            
REMARK 620 6 PO4 A1078   O1  149.7  92.8  86.4 107.7 109.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1080   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 761   OE2                                                    
REMARK 620 2 HIS A 781   ND1  77.9                                              
REMARK 620 3 GLU A 783   O   134.8  92.2                                        
REMARK 620 4 GLN A 784   O    97.3 149.3  69.6                                  
REMARK 620 5 VAL A 787   O    78.6 122.9 138.7  84.8                            
REMARK 620 6 SER A 792   OG  127.1  82.7  94.2 121.8  71.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1079  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 829   OE1                                                    
REMARK 620 2 GLU A 841   OE2  95.3                                              
REMARK 620 3 ADP A1088   O2A  91.4  95.2                                        
REMARK 620 4 HOH A1903   O    91.5 173.1  83.2                                  
REMARK 620 5 ADP A1088   O3B 178.6  85.4  87.3  87.7                            
REMARK 620 6 HOH A1608   O    95.9  92.7 168.7  88.0  85.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 383   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  16   O                                                      
REMARK 620 2 ASP B 112   O    94.7                                              
REMARK 620 3 HOH A1457   O   140.1 124.3                                        
REMARK 620 4 HOH B3605   O    96.2  86.4  79.6                                  
REMARK 620 5 HOH A1456   O   117.2  84.3  78.8 145.9                            
REMARK 620 6 HOH B3394   O    75.0 153.9  72.5 118.1  79.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1077   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 127   OE1                                                    
REMARK 620 2 GLU C 299   OE1 130.6                                              
REMARK 620 3 MET C 300   O    97.8  93.4                                        
REMARK 620 4 HOH C1193   O   143.9  84.6  68.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1082   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 143   OG1                                                    
REMARK 620 2 ALA C 144   O    71.2                                              
REMARK 620 3 HOH C1201   O    63.4  59.8                                        
REMARK 620 4 HOH C1202   O    80.6 119.5  59.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1076   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 215   OE2                                                    
REMARK 620 2 ASN C 236   OD1  85.2                                              
REMARK 620 3 ASP C 238   O   125.7  95.9                                        
REMARK 620 4 ALA C 239   O    89.0 154.7  67.9                                  
REMARK 620 5 ILE C 242   O    81.1 116.9 140.4  86.3                            
REMARK 620 6 SER C 247   OG  135.5  76.7  96.6 122.8  72.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1075  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 285   OE1                                                    
REMARK 620 2 GLU C 299   OE2  74.7                                              
REMARK 620 3 ADP C1089   O1A 103.8  94.9                                        
REMARK 620 4 HOH C1587   O    93.4 167.7  84.9                                  
REMARK 620 5 PO4 C1078   O3   85.1  79.3 167.9 103.0                            
REMARK 620 6 ADP C1089   O1B 166.8  99.1  88.3  93.1  82.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1074  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 299   OE1                                                    
REMARK 620 2 GLU C 299   OE2  59.2                                              
REMARK 620 3 ASN C 301   OD1  87.8  85.6                                        
REMARK 620 4 ADP C1089   O3B  88.4 100.9 169.4                                  
REMARK 620 5 HOH C1191   O   105.2 161.8  84.4  87.0                            
REMARK 620 6 PO4 C1078   O1  155.9  97.5  84.0 103.2  96.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1080   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 761   OE2                                                    
REMARK 620 2 HIS C 781   ND1  78.6                                              
REMARK 620 3 GLU C 783   O   126.6  93.1                                        
REMARK 620 4 GLN C 784   O    90.9 148.2  69.0                                  
REMARK 620 5 VAL C 787   O    78.4 126.3 138.8  79.6                            
REMARK 620 6 SER C 792   OG  131.2  88.8 100.7 119.6  71.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1079  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 829   OE1                                                    
REMARK 620 2 GLU C 841   OE2  96.4                                              
REMARK 620 3 ADP C1090   O3B 169.8  88.0                                        
REMARK 620 4 ADP C1090   O2A  84.3 105.8  85.7                                  
REMARK 620 5 HOH C1589   O    76.6 170.7  99.8  79.8                            
REMARK 620 6 HOH C1590   O   109.1  86.2  80.3 161.3  90.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D 383   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  16   O                                                      
REMARK 620 2 ASP D 112   O    90.4                                              
REMARK 620 3 HOH D2536   O    91.0  88.8                                        
REMARK 620 4 HOH D2331   O    71.4 154.8 108.4                                  
REMARK 620 5 HOH C1451   O   115.3  83.9 152.6  88.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E1081   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  84   O                                                      
REMARK 620 2 GLY E 112   O    80.1                                              
REMARK 620 3 THR E 114   OG1  77.9 105.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E1077   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 127   OE1                                                    
REMARK 620 2 GLU E 299   OE1 130.7                                              
REMARK 620 3 MET E 300   O    97.3  83.9                                        
REMARK 620 4 HOH E1195   O   142.3  85.5  73.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E1083   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E 143   OG1                                                    
REMARK 620 2 ALA E 144   O    71.9                                              
REMARK 620 3 HOH E1202   O    79.8  69.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E1076   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 215   OE2                                                    
REMARK 620 2 ASN E 236   OD1  84.4                                              
REMARK 620 3 ASP E 238   O   128.7  93.1                                        
REMARK 620 4 ALA E 239   O    92.1 157.6  72.0                                  
REMARK 620 5 ILE E 242   O    78.6 115.5 143.6  85.2                            
REMARK 620 6 SER E 247   OG  133.9  74.4  93.4 121.9  74.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E1075  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 285   OE1                                                    
REMARK 620 2 GLU E 299   OE2  79.3                                              
REMARK 620 3 ADP E1089   O1B 171.6  92.9                                        
REMARK 620 4 HOH E1597   O    88.9 164.3  99.3                                  
REMARK 620 5 ADP E1089   O1A  88.9  78.6  92.5  91.0                            
REMARK 620 6 PO4 E1078   O3   91.3  91.4  85.9  99.3 169.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E1074  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 299   OE1                                                    
REMARK 620 2 GLU E 299   OE2  56.0                                              
REMARK 620 3 ASN E 301   OD1  82.9  97.1                                        
REMARK 620 4 ADP E1089   O3B  92.4  85.2 172.4                                  
REMARK 620 5 HOH E1193   O    97.3 152.9  82.8  91.9                            
REMARK 620 6 PO4 E1078   O1  142.6  91.9  82.8 104.4 114.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E1080   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 761   OE2                                                    
REMARK 620 2 HIS E 781   ND1  80.1                                              
REMARK 620 3 GLU E 783   O   128.5  94.2                                        
REMARK 620 4 GLN E 784   O    91.2 149.6  68.6                                  
REMARK 620 5 VAL E 787   O    76.4 121.7 141.2  83.6                            
REMARK 620 6 SER E 792   OG  129.0  84.2 100.6 122.5  71.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E1079  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 829   OE1                                                    
REMARK 620 2 GLU E 841   OE2  82.9                                              
REMARK 620 3 ADP E1090   O2A  90.1  95.1                                        
REMARK 620 4 HOH E1602   O    90.9 173.2  87.6                                  
REMARK 620 5 ADP E1090   O3B 171.9  90.3  86.1  96.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K F 383   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  16   O                                                      
REMARK 620 2 ASP F 112   O    91.8                                              
REMARK 620 3 HOH E1447   O   111.9  82.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G1081   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY G 112   O                                                      
REMARK 620 2 THR G 114   OG1 105.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G1083   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G 143   O                                                      
REMARK 620 2 THR G 143   OG1  64.7                                              
REMARK 620 3 HOH G1199   O    66.5  73.0                                        
REMARK 620 4 HOH G1198   O   123.7  72.6 132.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G1076   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN G 236   OD1                                                    
REMARK 620 2 ASP G 238   O    93.1                                              
REMARK 620 3 ALA G 239   O   156.1  71.7                                        
REMARK 620 4 ILE G 242   O   119.9 139.7  82.1                                  
REMARK 620 5 SER G 247   OG   81.1  98.9 118.7  67.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G1075  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 285   OE1                                                    
REMARK 620 2 GLU G 299   OE2  86.9                                              
REMARK 620 3 PO4 G1078   O3   81.6  90.9                                        
REMARK 620 4 HOH G1549   O    87.0 169.7  96.4                                  
REMARK 620 5 ADP G1089   O1A 102.0  83.4 173.1  89.8                            
REMARK 620 6 ADP G1089   O1B 172.3  96.7  91.6  90.3  85.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G1077   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 299   OE1                                                    
REMARK 620 2 MET G 300   O    96.6                                              
REMARK 620 3 HOH G1190   O    71.7 129.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G1074  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 299   OE1                                                    
REMARK 620 2 GLU G 299   OE2  56.5                                              
REMARK 620 3 ASN G 301   OD1  88.3  95.5                                        
REMARK 620 4 HOH G1190   O    92.8 148.8  88.5                                  
REMARK 620 5 PO4 G1078   O1  144.2  88.7  86.8 122.5                            
REMARK 620 6 ADP G1089   O3B  83.9  84.2 171.0  87.2 102.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G1080   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 761   OE2                                                    
REMARK 620 2 HIS G 781   ND1  77.3                                              
REMARK 620 3 GLU G 783   O   134.0 102.6                                        
REMARK 620 4 GLN G 784   O    96.4 152.5  62.5                                  
REMARK 620 5 VAL G 787   O    78.7 121.1 131.9  82.8                            
REMARK 620 6 SER G 792   OG  124.1  82.1 101.0 121.9  68.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G1079  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 829   OE1                                                    
REMARK 620 2 GLU G 841   OE2  73.4                                              
REMARK 620 3 ADP G1090   O3B 160.1  86.7                                        
REMARK 620 4 HOH G1551   O   101.7  89.4  79.0                                  
REMARK 620 5 HOH G1550   O    98.9 172.3 101.0  91.6                            
REMARK 620 6 ADP G1090   O2A  88.1  91.1  91.0 169.9  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K H 383   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH G1422   O                                                      
REMARK 620 2 HOH G1423   O    91.7                                              
REMARK 620 N                    1                                               
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 1074                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1075                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1076                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1077                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1078                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1079                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1080                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1081                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1082                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1083                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1084                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1085                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1086                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 383                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1074                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1075                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1076                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1077                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1078                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1079                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1080                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1081                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1082                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1083                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1084                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1085                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1086                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 383                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 384                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1087                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 1088                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1074                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1075                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 1076                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 1077                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 1078                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1079                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 1080                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 1081                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1082                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 1083                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1084                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1085                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1086                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1087                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 383                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 384                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1088                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 1074                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 1075                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 1076                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 1077                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 1078                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 1079                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 1080                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 1081                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 1082                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 1083                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 1084                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 1085                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 1086                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 1087                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 383                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 384                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 1088                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 385                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1087                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1088                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 1089                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 1090                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U A 1091                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 1089                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 1090                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 1091                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 1092                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U C 1093                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 1089                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 1090                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 1091                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 1092                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U E 1093                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 1089                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 1090                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 1091                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 1092                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U G 1093                  
DBREF  1T36 A    1  1073  UNP    P00968   CARB_ECOLI       0   1072             
DBREF  1T36 C    1  1073  UNP    P00968   CARB_ECOLI       0   1072             
DBREF  1T36 E    1  1073  UNP    P00968   CARB_ECOLI       0   1072             
DBREF  1T36 G    1  1073  UNP    P00968   CARB_ECOLI       0   1072             
DBREF  1T36 B    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1T36 D    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1T36 F    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1T36 H    1   382  UNP    P00907   CARA_ECOLI       1    382             
SEQADV 1T36 ASP B  248  UNP  P00907    CYS   248 ENGINEERED                     
SEQADV 1T36 ASP D  248  UNP  P00907    CYS   248 ENGINEERED                     
SEQADV 1T36 ASP F  248  UNP  P00907    CYS   248 ENGINEERED                     
SEQADV 1T36 ASP H  248  UNP  P00907    CYS   248 ENGINEERED                     
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  ASP ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 B  382  THR ASP ILE PRO VAL PHE GLY ILE CYS 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  ASP ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 D  382  THR ASP ILE PRO VAL PHE GLY ILE CYS 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  ASP ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 F  382  THR ASP ILE PRO VAL PHE GLY ILE CYS 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  ASP ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 H  382  THR ASP ILE PRO VAL PHE GLY ILE CYS 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  A1074       1                                                       
HET     MN  A1075       1                                                       
HET      K  A1076       1                                                       
HET      K  A1077       1                                                       
HET    PO4  A1078       5                                                       
HET     MN  A1079       1                                                       
HET      K  A1080       1                                                       
HET     CL  A1081       1                                                       
HET      K  A1082       1                                                       
HET     CL  A1083       1                                                       
HET     CL  A1084       1                                                       
HET     CL  A1085       1                                                       
HET     CL  A1086       1                                                       
HET      K  B 383       1                                                       
HET     MN  C1074       1                                                       
HET     MN  C1075       1                                                       
HET      K  C1076       1                                                       
HET      K  C1077       1                                                       
HET    PO4  C1078       5                                                       
HET     MN  C1079       1                                                       
HET      K  C1080       1                                                       
HET     CL  C1081       1                                                       
HET      K  C1082       1                                                       
HET     CL  C1083       1                                                       
HET     CL  C1084       1                                                       
HET     CL  C1085       1                                                       
HET     CL  C1086       1                                                       
HET      K  D 383       1                                                       
HET     CL  D 384       1                                                       
HET     CL  C1087       1                                                       
HET    PO4  C1088       5                                                       
HET     MN  E1074       1                                                       
HET     MN  E1075       1                                                       
HET      K  E1076       1                                                       
HET      K  E1077       1                                                       
HET    PO4  E1078       5                                                       
HET     MN  E1079       1                                                       
HET      K  E1080       1                                                       
HET      K  E1081       1                                                       
HET     CL  E1082       1                                                       
HET      K  E1083       1                                                       
HET     CL  E1084       1                                                       
HET     CL  E1085       1                                                       
HET     CL  E1086       1                                                       
HET     CL  E1087       1                                                       
HET      K  F 383       1                                                       
HET     CL  F 384       1                                                       
HET     CL  E1088       1                                                       
HET     MN  G1074       1                                                       
HET     MN  G1075       1                                                       
HET      K  G1076       1                                                       
HET      K  G1077       1                                                       
HET    PO4  G1078       5                                                       
HET     MN  G1079       1                                                       
HET      K  G1080       1                                                       
HET      K  G1081       1                                                       
HET     CL  G1082       1                                                       
HET      K  G1083       1                                                       
HET     CL  G1084       1                                                       
HET     CL  G1085       1                                                       
HET     CL  G1086       1                                                       
HET     CL  G1087       1                                                       
HET      K  H 383       1                                                       
HET     CL  H 384       1                                                       
HET     CL  G1088       1                                                       
HET     CL  H 385       1                                                       
HET    ADP  A1087      27                                                       
HET    ADP  A1088      27                                                       
HET    ORN  A1089       9                                                       
HET    NET  A1090       9                                                       
HET      U  A1091      21                                                       
HET    ADP  C1089      27                                                       
HET    ADP  C1090      27                                                       
HET    ORN  C1091       9                                                       
HET    NET  C1092       9                                                       
HET      U  C1093      21                                                       
HET    ADP  E1089      27                                                       
HET    ADP  E1090      27                                                       
HET    ORN  E1091       9                                                       
HET    NET  E1092       9                                                       
HET      U  E1093      21                                                       
HET    ADP  G1089      27                                                       
HET    ADP  G1090      27                                                       
HET    ORN  G1091       9                                                       
HET    NET  G1092       9                                                       
HET      U  G1093      21                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM       K POTASSIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     ORN L-ORNITHINE                                                      
HETNAM     NET TETRAETHYLAMMONIUM ION                                           
HETNAM       U URIDINE-5'-MONOPHOSPHATE                                         
FORMUL   9   MN    12(MN 2+)                                                    
FORMUL  11    K    22(K 1+)                                                     
FORMUL  13  PO4    5(O4 P 3-)                                                   
FORMUL  16   CL    27(CL 1-)                                                    
FORMUL  75  ADP    8(C10 H15 N5 O10 P2)                                         
FORMUL  77  ORN    4(C5 H12 N2 O2)                                              
FORMUL  78  NET    4(C8 H20 N 1+)                                               
FORMUL  79    U    4(C9 H13 N2 O9 P)                                            
FORMUL  95  HOH   *3907(H2 O)                                                   
HELIX    1   1 CYS A   24  GLU A   40  1                                  17    
HELIX    2   2 THR A   53  ALA A   61  5                                   9    
HELIX    3   3 HIS A   70  ARG A   82  1                                  13    
HELIX    4   4 GLY A   91  GLN A  105  1                                  15    
HELIX    5   5 GLY A  106  GLY A  112  1                                   7    
HELIX    6   6 THR A  119  ASP A  128  1                                  10    
HELIX    7   7 ASP A  128  ILE A  139  1                                  12    
HELIX    8   8 THR A  151  GLY A  163  1                                  13    
HELIX    9   9 ASN A  184  SER A  199  1                                  16    
HELIX   10  10 HIS A  243  SER A  247  5                                   5    
HELIX   11  11 THR A  257  GLY A  276  1                                  20    
HELIX   12  12 SER A  305  GLY A  316  1                                  12    
HELIX   13  13 PRO A  318  ALA A  327  1                                  10    
HELIX   14  14 THR A  331  LEU A  335  5                                   5    
HELIX   15  15 ASN A  363  PHE A  367  5                                   5    
HELIX   16  16 THR A  390  LEU A  402  1                                  13    
HELIX   17  17 GLU A  419  ASP A  430  1                                  12    
HELIX   18  18 ASP A  434  ALA A  445  1                                  12    
HELIX   19  19 SER A  448  ASN A  457  1                                  10    
HELIX   20  20 ASP A  459  GLY A  480  1                                  22    
HELIX   21  21 ILE A  481  LEU A  484  5                                   4    
HELIX   22  22 ASN A  485  LYS A  495  1                                  11    
HELIX   23  23 ALA A  498  GLY A  507  1                                  10    
HELIX   24  24 ARG A  509  ASP A  521  1                                  13    
HELIX   25  25 GLY A  575  ASP A  592  1                                  18    
HELIX   26  26 THR A  605  SER A  613  5                                   9    
HELIX   27  27 THR A  622  LYS A  634  1                                  13    
HELIX   28  28 GLY A  644  LYS A  649  1                                   6    
HELIX   29  29 LEU A  650  ALA A  657  1                                   8    
HELIX   30  30 SER A  665  ASP A  674  1                                  10    
HELIX   31  31 ASP A  674  LYS A  686  1                                  13    
HELIX   32  32 ALA A  697  GLY A  709  1                                  13    
HELIX   33  33 ASP A  730  ALA A  741  1                                  12    
HELIX   34  34 HIS A  788  SER A  792  5                                   5    
HELIX   35  35 SER A  802  GLN A  821  1                                  20    
HELIX   36  36 THR A  849  GLY A  858  1                                  10    
HELIX   37  37 PRO A  860  GLY A  871  1                                  12    
HELIX   38  38 SER A  873  GLY A  878  1                                   6    
HELIX   39  39 LEU A  895  PHE A  900  5                                   6    
HELIX   40  40 THR A  923  SER A  935  1                                  13    
HELIX   41  41 ARG A  950  GLY A  968  1                                  19    
HELIX   42  42 THR A  974  ALA A  984  1                                  11    
HELIX   43  43 HIS A 1000  ASN A 1007  1                                   8    
HELIX   44  44 GLY A 1019  TYR A 1036  1                                  18    
HELIX   45  45 THR A 1043  LEU A 1054  1                                  12    
HELIX   46  46 SER A 1064  GLN A 1071  1                                   8    
HELIX   47  47 GLY B   38  THR B   44  1                                   7    
HELIX   48  48 ASP B   45  SER B   49  5                                   5    
HELIX   49  49 ASN B   66  GLU B   70  5                                   5    
HELIX   50  50 ASP B   97  ASN B  106  1                                  10    
HELIX   51  51 ASP B  114  GLY B  126  1                                  13    
HELIX   52  52 ASP B  139  PHE B  150  1                                  12    
HELIX   53  53 LEU B  158  THR B  163  1                                   6    
HELIX   54  54 LYS B  186  LEU B  190  5                                   5    
HELIX   55  55 LYS B  202  ASP B  211  1                                  10    
HELIX   56  56 SER B  224  LYS B  230  1                                   7    
HELIX   57  57 ASP B  249  LEU B  259  1                                  11    
HELIX   58  58 CYS B  269  ALA B  278  1                                  10    
HELIX   59  59 GLU B  318  LEU B  321  5                                   4    
HELIX   60  60 ALA B  364  ARG B  378  1                                  15    
HELIX   61  61 CYS C   24  GLU C   40  1                                  17    
HELIX   62  62 THR C   53  ALA C   61  5                                   9    
HELIX   63  63 HIS C   70  ARG C   82  1                                  13    
HELIX   64  64 GLY C   91  GLN C  105  1                                  15    
HELIX   65  65 GLY C  106  PHE C  111  1                                   6    
HELIX   66  66 THR C  119  ASP C  128  1                                  10    
HELIX   67  67 ASP C  128  ILE C  139  1                                  12    
HELIX   68  68 THR C  151  GLY C  163  1                                  13    
HELIX   69  69 ASN C  184  SER C  199  1                                  16    
HELIX   70  70 HIS C  243  SER C  247  5                                   5    
HELIX   71  71 THR C  257  GLY C  276  1                                  20    
HELIX   72  72 SER C  305  GLY C  316  1                                  12    
HELIX   73  73 PRO C  318  VAL C  328  1                                  11    
HELIX   74  74 THR C  331  LEU C  335  5                                   5    
HELIX   75  75 ASN C  337  GLY C  341  5                                   5    
HELIX   76  76 ASN C  363  PHE C  367  5                                   5    
HELIX   77  77 THR C  390  LEU C  402  1                                  13    
HELIX   78  78 GLU C  419  ASP C  430  1                                  12    
HELIX   79  79 ASP C  434  ALA C  445  1                                  12    
HELIX   80  80 SER C  448  ASN C  457  1                                  10    
HELIX   81  81 ASP C  459  GLY C  480  1                                  22    
HELIX   82  82 ILE C  481  LEU C  484  5                                   4    
HELIX   83  83 ASN C  485  LYS C  495  1                                  11    
HELIX   84  84 ALA C  498  GLY C  507  1                                  10    
HELIX   85  85 ARG C  509  ASP C  521  1                                  13    
HELIX   86  86 GLY C  575  ASP C  592  1                                  18    
HELIX   87  87 THR C  605  SER C  613  5                                   9    
HELIX   88  88 THR C  622  LYS C  634  1                                  13    
HELIX   89  89 GLY C  644  LYS C  649  1                                   6    
HELIX   90  90 LEU C  650  ALA C  657  1                                   8    
HELIX   91  91 SER C  665  ASP C  674  1                                  10    
HELIX   92  92 ASP C  674  LYS C  686  1                                  13    
HELIX   93  93 ALA C  697  GLY C  709  1                                  13    
HELIX   94  94 ASP C  730  ALA C  741  1                                  12    
HELIX   95  95 HIS C  788  SER C  792  5                                   5    
HELIX   96  96 SER C  802  GLN C  821  1                                  20    
HELIX   97  97 THR C  849  GLY C  858  1                                  10    
HELIX   98  98 PRO C  860  GLY C  871  1                                  12    
HELIX   99  99 SER C  873  GLY C  878  1                                   6    
HELIX  100 100 PRO C  896  PHE C  900  5                                   5    
HELIX  101 101 THR C  923  SER C  935  1                                  13    
HELIX  102 102 ARG C  950  LYS C  954  5                                   5    
HELIX  103 103 GLU C  955  GLU C  955  5                                   1    
HELIX  104 104 ARG C  956  GLN C  967  1                                  12    
HELIX  105 105 THR C  974  GLU C  983  1                                  10    
HELIX  106 106 LYS C  993  GLY C  997  5                                   5    
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  GLN C 1071  1                                   8    
HELIX  111 111 GLY D   38  THR D   44  1                                   7    
HELIX  112 112 ASP D   45  SER D   49  5                                   5    
HELIX  113 113 ASN D   66  GLU D   70  5                                   5    
HELIX  114 114 ASP D   97  ASN D  106  1                                  10    
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 ASP D  249  LEU D  259  1                                  11    
HELIX  122 122 CYS D  269  ALA D  278  1                                  10    
HELIX  123 123 ALA D  364  ARG D  378  1                                  15    
HELIX  124 124 CYS E   24  GLU E   40  1                                  17    
HELIX  125 125 THR E   53  ALA E   61  5                                   9    
HELIX  126 126 HIS E   70  ARG E   82  1                                  13    
HELIX  127 127 GLY E   91  GLN E  105  1                                  15    
HELIX  128 128 GLY E  106  PHE E  111  1                                   6    
HELIX  129 129 THR E  119  ASP E  128  1                                  10    
HELIX  130 130 ASP E  128  ILE E  139  1                                  12    
HELIX  131 131 THR E  151  GLY E  163  1                                  13    
HELIX  132 132 ASN E  184  SER E  199  1                                  16    
HELIX  133 133 HIS E  243  SER E  247  5                                   5    
HELIX  134 134 THR E  257  GLY E  276  1                                  20    
HELIX  135 135 SER E  305  GLY E  316  1                                  12    
HELIX  136 136 PRO E  318  ALA E  327  1                                  10    
HELIX  137 137 ASN E  363  PHE E  367  5                                   5    
HELIX  138 138 THR E  390  LEU E  402  1                                  13    
HELIX  139 139 GLU E  419  ASP E  430  1                                  12    
HELIX  140 140 ASP E  434  ALA E  445  1                                  12    
HELIX  141 141 SER E  448  ASN E  457  1                                  10    
HELIX  142 142 ASP E  459  GLY E  480  1                                  22    
HELIX  143 143 ILE E  481  LEU E  484  5                                   4    
HELIX  144 144 ASN E  485  LYS E  495  1                                  11    
HELIX  145 145 ALA E  498  ALA E  506  1                                   9    
HELIX  146 146 ARG E  509  TYR E  520  1                                  12    
HELIX  147 147 GLY E  575  ASP E  592  1                                  18    
HELIX  148 148 THR E  605  SER E  613  5                                   9    
HELIX  149 149 THR E  622  LYS E  634  1                                  13    
HELIX  150 150 GLY E  644  LYS E  649  1                                   6    
HELIX  151 151 LEU E  650  ALA E  657  1                                   8    
HELIX  152 152 SER E  665  ASP E  674  1                                  10    
HELIX  153 153 ASP E  674  LYS E  686  1                                  13    
HELIX  154 154 ALA E  697  GLY E  709  1                                  13    
HELIX  155 155 ASP E  730  ALA E  741  1                                  12    
HELIX  156 156 HIS E  788  SER E  792  5                                   5    
HELIX  157 157 SER E  802  GLN E  821  1                                  20    
HELIX  158 158 THR E  849  GLY E  858  1                                  10    
HELIX  159 159 PRO E  860  GLY E  871  1                                  12    
HELIX  160 160 SER E  873  GLY E  878  1                                   6    
HELIX  161 161 PRO E  896  PHE E  900  5                                   5    
HELIX  162 162 THR E  923  SER E  935  1                                  13    
HELIX  163 163 ARG E  956  GLN E  967  1                                  12    
HELIX  164 164 HIS E  975  ALA E  984  1                                  10    
HELIX  165 165 LYS E  993  GLY E  997  5                                   5    
HELIX  166 166 HIS E 1000  ASN E 1007  1                                   8    
HELIX  167 167 GLY E 1019  SER E 1026  1                                   8    
HELIX  168 168 SER E 1026  TYR E 1036  1                                  11    
HELIX  169 169 THR E 1043  LEU E 1054  1                                  12    
HELIX  170 170 SER E 1064  GLN E 1071  1                                   8    
HELIX  171 171 GLY F   38  THR F   44  1                                   7    
HELIX  172 172 ASP F   45  SER F   49  5                                   5    
HELIX  173 173 ASN F   66  GLU F   70  5                                   5    
HELIX  174 174 ASP F   97  HIS F  105  1                                   9    
HELIX  175 175 ASP F  114  GLY F  126  1                                  13    
HELIX  176 176 ASP F  139  PHE F  150  1                                  12    
HELIX  177 177 ASP F  157  THR F  163  1                                   7    
HELIX  178 178 LYS F  186  LEU F  190  5                                   5    
HELIX  179 179 LYS F  202  ARG F  212  1                                  11    
HELIX  180 180 SER F  224  LYS F  230  1                                   7    
HELIX  181 181 ASP F  249  THR F  261  1                                  13    
HELIX  182 182 CYS F  269  SER F  279  1                                  11    
HELIX  183 183 ALA F  364  THR F  380  1                                  17    
HELIX  184 184 CYS G   24  GLU G   40  1                                  17    
HELIX  185 185 THR G   53  ALA G   61  5                                   9    
HELIX  186 186 HIS G   70  ARG G   82  1                                  13    
HELIX  187 187 GLY G   91  GLN G  105  1                                  15    
HELIX  188 188 GLY G  106  PHE G  111  1                                   6    
HELIX  189 189 THR G  119  ASP G  128  1                                  10    
HELIX  190 190 ASP G  128  ILE G  139  1                                  12    
HELIX  191 191 THR G  151  GLY G  163  1                                  13    
HELIX  192 192 ASN G  184  SER G  199  1                                  16    
HELIX  193 193 HIS G  243  SER G  247  5                                   5    
HELIX  194 194 THR G  257  GLY G  276  1                                  20    
HELIX  195 195 SER G  305  GLY G  316  1                                  12    
HELIX  196 196 PRO G  318  VAL G  328  1                                  11    
HELIX  197 197 THR G  331  LEU G  335  5                                   5    
HELIX  198 198 ASN G  337  GLY G  341  5                                   5    
HELIX  199 199 ASN G  363  PHE G  367  5                                   5    
HELIX  200 200 THR G  390  GLY G  401  1                                  12    
HELIX  201 201 GLU G  419  ASP G  430  1                                  12    
HELIX  202 202 ASP G  434  ALA G  445  1                                  12    
HELIX  203 203 SER G  448  ASN G  457  1                                  10    
HELIX  204 204 ASP G  459  GLY G  480  1                                  22    
HELIX  205 205 ILE G  481  LEU G  484  5                                   4    
HELIX  206 206 ASN G  485  LYS G  495  1                                  11    
HELIX  207 207 ALA G  498  GLY G  507  1                                  10    
HELIX  208 208 ARG G  509  ASP G  521  1                                  13    
HELIX  209 209 GLY G  575  GLY G  593  1                                  19    
HELIX  210 210 ASP G  609  SER G  613  5                                   5    
HELIX  211 211 THR G  622  LYS G  634  1                                  13    
HELIX  212 212 GLY G  644  LYS G  649  1                                   6    
HELIX  213 213 LEU G  650  ALA G  657  1                                   8    
HELIX  214 214 SER G  665  ASP G  674  1                                  10    
HELIX  215 215 ASP G  674  LYS G  686  1                                  13    
HELIX  216 216 ALA G  697  GLY G  709  1                                  13    
HELIX  217 217 ASP G  730  ALA G  741  1                                  12    
HELIX  218 218 HIS G  788  SER G  792  5                                   5    
HELIX  219 219 SER G  802  LEU G  820  1                                  19    
HELIX  220 220 THR G  849  GLY G  858  1                                  10    
HELIX  221 221 PRO G  860  GLY G  871  1                                  12    
HELIX  222 222 SER G  873  GLY G  878  1                                   6    
HELIX  223 223 LEU G  895  PHE G  900  5                                   6    
HELIX  224 224 THR G  923  SER G  935  1                                  13    
HELIX  225 225 ARG G  950  GLN G  967  1                                  18    
HELIX  226 226 HIS G  975  ALA G  984  1                                  10    
HELIX  227 227 LYS G  993  GLY G  997  5                                   5    
HELIX  228 228 HIS G 1000  ASN G 1007  1                                   8    
HELIX  229 229 GLY G 1019  TYR G 1036  1                                  18    
HELIX  230 230 THR G 1043  ASN G 1055  1                                  13    
HELIX  231 231 SER G 1064  GLN G 1071  1                                   8    
HELIX  232 232 GLY H   38  THR H   44  1                                   7    
HELIX  233 233 ASP H   45  SER H   49  5                                   5    
HELIX  234 234 ASN H   66  GLU H   70  5                                   5    
HELIX  235 235 ASP H   97  HIS H  105  1                                   9    
HELIX  236 236 ASP H  114  GLY H  126  1                                  13    
HELIX  237 237 ASP H  139  ALA H  149  1                                  11    
HELIX  238 238 LEU H  158  THR H  163  1                                   6    
HELIX  239 239 LYS H  186  LEU H  190  5                                   5    
HELIX  240 240 LYS H  202  ARG H  212  1                                  11    
HELIX  241 241 SER H  224  LYS H  230  1                                   7    
HELIX  242 242 ASP H  249  LEU H  259  1                                  11    
HELIX  243 243 CYS H  269  SER H  279  1                                  11    
HELIX  244 244 PRO H  360  ALA H  364  5                                   5    
HELIX  245 245 PRO H  365  LYS H  379  1                                  15    
SHEET    1   A 5 ALA A  63  TYR A  65  0                                        
SHEET    2   A 5 ARG A  43  VAL A  47  1  N  LEU A  46   O  ALA A  63           
SHEET    3   A 5 SER A   9  LEU A  13  1  N  ILE A  10   O  ILE A  45           
SHEET    4   A 5 ALA A  85  LEU A  87  1  O  LEU A  87   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  ASP A 207 -1  O  LEU A 204   N  ALA A 149           
SHEET    3   B 4 CYS A 166  PRO A 170 -1  N  ARG A 169   O  LEU A 205           
SHEET    4   B 4 GLY A 180  ALA A 182 -1  O  ALA A 182   N  CYS A 166           
SHEET    1   C 7 LEU A 295  ASN A 301  0                                        
SHEET    2   C 7 GLY A 280  VAL A 288 -1  N  GLN A 285   O  GLU A 299           
SHEET    3   C 7 LYS A 214  ARG A 222 -1  N  VAL A 220   O  SER A 282           
SHEET    4   C 7 CYS A 228  ASN A 236 -1  O  VAL A 231   N  GLU A 219           
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  O  VAL A 356   N  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  THR A 546   N  VAL A 525           
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  N  MET A 598   O  ARG A 615           
SHEET    5   D 6 LYS A 561  LEU A 565  1  N  ILE A 562   O  GLU A 595           
SHEET    6   D 6 GLY A 637  ILE A 639  1  O  ILE A 639   N  MET A 563           
SHEET    1   E 4 ASN A 692  THR A 694  0                                        
SHEET    2   E 4 LEU A 751  HIS A 754 -1  O  LEU A 752   N  ALA A 693           
SHEET    3   E 4 LEU A 712  VAL A 714 -1  N  VAL A 713   O  ASP A 753           
SHEET    4   E 4 GLU A 726  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  N  GLN A 829   O  ILE A 840           
SHEET    3   F 7 VAL A 760  CYS A 768 -1  N  VAL A 760   O  VAL A 832           
SHEET    4   F 7 VAL A 773  GLN A 784 -1  O  LEU A 774   N  ILE A 767           
SHEET    5   F 7 CYS A 794  LEU A 796 -1  O  SER A 795   N  GLU A 780           
SHEET    6   F 7 TYR A 888  VAL A 894 -1  O  LYS A 891   N  CYS A 794           
SHEET    7   F 7 GLY A 915  GLY A 921 -1  O  GLY A 919   N  VAL A 890           
SHEET    1   G 5 ARG A 989  LEU A 990  0                                        
SHEET    2   G 5 GLU A 970  ALA A 973  1  N  LEU A 971   O  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  ASP A1041   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  O  PHE B  15   N  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  N  LEU B  80   O  ILE B 110           
SHEET    5   H 8 GLN B  51  LEU B  55  1  N  VAL B  53   O  VAL B  81           
SHEET    6   H 8 GLY B  24  ASN B  33  1  N  GLU B  29   O  ILE B  52           
SHEET    7   H 8 GLN B 128  ALA B 134 -1  O  GLN B 128   N  VAL B  30           
SHEET    8   H 8 SER B   4  LEU B   9 -1  N  LEU B   6   O  ILE B 133           
SHEET    1   I10 TYR B 168  TRP B 170  0                                        
SHEET    2   I10 LEU B 216  PRO B 220 -1  O  ILE B 218   N  TYR B 168           
SHEET    3   I10 VAL B 194  ASP B 198  1  N  ASP B 198   O  VAL B 219           
SHEET    4   I10 GLY B 235  LEU B 238  1  O  PHE B 237   N  VAL B 195           
SHEET    5   I10 VAL B 265  ILE B 268  1  O  ILE B 268   N  LEU B 238           
SHEET    6   I10 ALA B 347  PHE B 350  1  O  PHE B 348   N  VAL B 265           
SHEET    7   I10 LEU B 337  ARG B 342 -1  N  ARG B 342   O  ALA B 347           
SHEET    8   I10 LEU B 325  SER B 331 -1  N  HIS B 329   O  GLN B 338           
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  GLY B 313   N  MET B 286           
SHEET    1   J 5 ALA C  63  TYR C  65  0                                        
SHEET    2   J 5 ARG C  43  VAL C  47  1  N  LEU C  46   O  TYR C  65           
SHEET    3   J 5 SER C   9  LEU C  13  1  N  ILE C  10   O  ILE C  45           
SHEET    4   J 5 ALA C  85  LEU C  87  1  O  LEU C  87   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  O  ILE C 206   N  GLY C 147           
SHEET    3   K 4 CYS C 166  PRO C 170 -1  N  ARG C 169   O  LEU C 205           
SHEET    4   K 4 GLY C 180  ALA C 182 -1  O  ALA C 182   N  CYS C 166           
SHEET    1   L 7 LEU C 295  ASN C 301  0                                        
SHEET    2   L 7 GLY C 280  VAL C 288 -1  N  GLN C 285   O  ILE C 298           
SHEET    3   L 7 LYS C 214  ARG C 222 -1  N  VAL C 220   O  SER C 282           
SHEET    4   L 7 CYS C 228  ASN C 236 -1  O  ASN C 236   N  GLU C 215           
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  O  LYS C 358   N  THR C 249           
SHEET    7   L 7 GLY C 382  GLY C 388 -1  O  GLY C 388   N  VAL C 355           
SHEET    1   M 6 VAL C 525  ARG C 528  0                                        
SHEET    2   M 6 ALA C 541  THR C 546 -1  O  THR C 546   N  VAL C 525           
SHEET    3   M 6 ARG C 615  TYR C 617  1  O  LEU C 616   N  MET C 543           
SHEET    4   M 6 GLU C 595  VAL C 599  1  N  MET C 598   O  TYR C 617           
SHEET    5   M 6 LYS C 561  LEU C 565  1  N  VAL C 564   O  ILE C 597           
SHEET    6   M 6 GLY C 637  ILE C 639  1  O  ILE C 639   N  MET C 563           
SHEET    1   N 4 ASN C 692  THR C 694  0                                        
SHEET    2   N 4 LEU C 751  HIS C 754 -1  O  LEU C 752   N  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  VAL C 728   N  LEU C 712           
SHEET    1   O 7 GLU C 836  ASN C 843  0                                        
SHEET    2   O 7 GLY C 824  LYS C 833 -1  N  ASN C 827   O  ASN C 843           
SHEET    3   O 7 VAL C 760  CYS C 768 -1  N  VAL C 764   O  VAL C 828           
SHEET    4   O 7 VAL C 773  GLN C 784 -1  O  MET C 779   N  ASP C 763           
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  O  SER C 889   N  LEU C 796           
SHEET    7   O 7 GLY C 915  GLY C 921 -1  O  GLY C 921   N  TYR C 888           
SHEET    1   P 5 ARG C 989  LEU C 990  0                                        
SHEET    2   P 5 GLU C 970  ALA C 973  1  N  LEU C 971   O  ARG C 989           
SHEET    3   P 5 ARG C 944  SER C 948  1  N  ALA C 945   O  ASP C 972           
SHEET    4   P 5 TYR C1012  ASN C1015  1  O  ILE C1014   N  SER C 948           
SHEET    5   P 5 HIS C1039  ASP C1041  1  O  ASP C1041   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  O  PHE D  15   N  LEU D   7           
SHEET    3   Q 8 VAL D 108  ALA D 111 -1  O  ALA D 111   N  ARG D  18           
SHEET    4   Q 8 GLY D  79  VAL D  81  1  N  LEU D  80   O  ILE D 110           
SHEET    5   Q 8 GLN D  51  LEU D  55  1  N  VAL D  53   O  VAL D  81           
SHEET    6   Q 8 GLY D  24  ASN D  33  1  N  GLU D  29   O  ILE D  52           
SHEET    7   Q 8 GLN D 128  ALA D 134 -1  O  ALA D 134   N  GLY D  24           
SHEET    8   Q 8 SER D   4  LEU D   9 -1  N  LEU D   6   O  ILE D 133           
SHEET    1   R10 TYR D 168  TRP D 170  0                                        
SHEET    2   R10 CYS D 214  PRO D 220 -1  O  ILE D 218   N  TYR D 168           
SHEET    3   R10 PHE D 192  ASP D 198  1  N  PHE D 192   O  ARG D 215           
SHEET    4   R10 GLY D 235  LEU D 238  1  O  PHE D 237   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  O  PHE D 350   N  GLY D 267           
SHEET    7   R10 LEU D 337  ARG D 342 -1  N  ILE D 340   O  SER D 349           
SHEET    8   R10 LEU D 325  SER D 331 -1  N  HIS D 329   O  GLN D 338           
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  GLY D 313   N  MET D 286           
SHEET    1   S 5 ALA E  63  TYR E  65  0                                        
SHEET    2   S 5 ARG E  43  VAL E  47  1  N  LEU E  46   O  TYR E  65           
SHEET    3   S 5 SER E   9  LEU E  13  1  N  ILE E  12   O  ILE E  45           
SHEET    4   S 5 ALA E  85  LEU E  87  1  O  LEU E  87   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  O  ILE E 206   N  GLY E 147           
SHEET    3   T 4 CYS E 166  PRO E 170 -1  N  ARG E 169   O  LEU E 205           
SHEET    4   T 4 GLY E 180  ALA E 182 -1  O  ALA E 182   N  CYS E 166           
SHEET    1   U 7 LEU E 295  ASN E 301  0                                        
SHEET    2   U 7 GLY E 280  VAL E 288 -1  N  ALA E 287   O  ILE E 296           
SHEET    3   U 7 LYS E 214  ARG E 222 -1  N  VAL E 220   O  SER E 282           
SHEET    4   U 7 CYS E 228  ASN E 236 -1  O  ILE E 229   N  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  O  LYS E 358   N  THR E 249           
SHEET    7   U 7 GLY E 382  GLY E 388 -1  O  GLY E 388   N  VAL E 355           
SHEET    1   V 6 VAL E 525  ARG E 528  0                                        
SHEET    2   V 6 TYR E 542  THR E 546 -1  O  THR E 546   N  VAL E 525           
SHEET    3   V 6 ARG E 615  PHE E 618  1  O  PHE E 618   N  MET E 543           
SHEET    4   V 6 GLU E 595  ASN E 600  1  N  MET E 598   O  TYR E 617           
SHEET    5   V 6 LYS E 561  LEU E 565  1  N  VAL E 564   O  ILE E 597           
SHEET    6   V 6 GLY E 637  ILE E 639  1  O  ILE E 639   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  O  LEU E 752   N  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  VAL E 728   N  LEU E 712           
SHEET    1   X 7 GLU E 836  ASN E 843  0                                        
SHEET    2   X 7 GLY E 824  LYS E 833 -1  N  ASN E 827   O  ASN E 843           
SHEET    3   X 7 VAL E 760  CYS E 768 -1  N  VAL E 762   O  PHE E 830           
SHEET    4   X 7 VAL E 773  GLN E 784 -1  O  LEU E 774   N  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 919   N  VAL E 890           
SHEET    1   Y 5 ARG E 989  VAL E 991  0                                        
SHEET    2   Y 5 GLU E 970  THR E 974  1  N  LEU E 971   O  ARG E 989           
SHEET    3   Y 5 ARG E 944  SER E 948  1  N  LEU E 947   O  ASP E 972           
SHEET    4   Y 5 TYR E1012  ASN E1015  1  O  ILE E1014   N  LEU E 946           
SHEET    5   Y 5 TYR E1040  ASP E1041  1  O  ASP E1041   N  ASN E1015           
SHEET    1   Z 8 SER F   4  LEU F   9  0                                        
SHEET    2   Z 8 GLN F  14  ALA F  19 -1  O  PHE F  15   N  LEU F   7           
SHEET    3   Z 8 VAL F 108  ALA F 111 -1  O  ALA F 111   N  ARG F  18           
SHEET    4   Z 8 GLY F  79  VAL F  81  1  N  LEU F  80   O  ILE F 110           
SHEET    5   Z 8 GLN F  51  LEU F  55  1  N  VAL F  53   O  VAL F  81           
SHEET    6   Z 8 GLY F  24  ASN F  33  1  N  GLU F  29   O  ILE F  52           
SHEET    7   Z 8 GLN F 128  ALA F 134 -1  O  ALA F 134   N  GLY F  24           
SHEET    8   Z 8 SER F   4  LEU F   9 -1  N  VAL F   8   O  CYS F 131           
SHEET    1  AA10 TYR F 168  TRP F 170  0                                        
SHEET    2  AA10 CYS F 214  VAL F 219 -1  O  ILE F 218   N  TYR F 168           
SHEET    3  AA10 PHE F 192  TYR F 197  1  N  ALA F 196   O  THR F 217           
SHEET    4  AA10 GLY F 235  LEU F 238  1  O  PHE F 237   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  O  PHE F 350   N  GLY F 267           
SHEET    7  AA10 LEU F 337  ARG F 342 -1  N  ARG F 342   O  ALA F 347           
SHEET    8  AA10 LEU F 325  SER F 331 -1  N  HIS F 329   O  GLN F 338           
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  GLY F 313   N  MET F 286           
SHEET    1  AB 5 ALA G  63  TYR G  65  0                                        
SHEET    2  AB 5 ARG G  43  VAL G  47  1  N  LEU G  46   O  TYR G  65           
SHEET    3  AB 5 SER G   9  LEU G  13  1  N  ILE G  12   O  ILE G  45           
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  N  ARG G 169   O  LEU G 205           
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  ALA G 287   O  ILE G 296           
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  O  CYS G 232   N  GLU G 219           
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  VAL G 384   N  ILE G 359           
SHEET    1  AE 6 VAL G 525  ARG G 528  0                                        
SHEET    2  AE 6 TYR G 542  THR G 546 -1  O  THR G 546   N  VAL G 525           
SHEET    3  AE 6 ARG G 615  TYR G 617  1  O  LEU G 616   N  MET G 543           
SHEET    4  AE 6 GLU G 595  VAL G 599  1  N  MET G 598   O  TYR G 617           
SHEET    5  AE 6 LYS G 561  LEU G 565  1  N  ILE G 562   O  GLU G 595           
SHEET    6  AE 6 GLY G 637  ILE G 639  1  O  ILE G 639   N  MET G 563           
SHEET    1  AF 4 ASN G 692  THR G 694  0                                        
SHEET    2  AF 4 LEU G 751  HIS G 754 -1  O  LEU G 752   N  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  VAL G 728   N  LEU G 712           
SHEET    1  AG 7 GLU G 836  ASN G 843  0                                        
SHEET    2  AG 7 ARG G 823  LYS G 833 -1  N  ASN G 827   O  ASN G 843           
SHEET    3  AG 7 VAL G 760  ASP G 769 -1  N  VAL G 762   O  PHE G 830           
SHEET    4  AG 7 VAL G 773  HIS G 781 -1  O  LEU G 774   N  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 919   N  VAL G 890           
SHEET    1  AH 5 ARG G 989  VAL G 991  0                                        
SHEET    2  AH 5 PHE G 969  THR G 974  1  N  LEU G 971   O  ARG G 989           
SHEET    3  AH 5 GLY G 943  SER G 948  1  N  ALA G 945   O  GLU G 970           
SHEET    4  AH 5 TYR G1012  ASN G1015  1  O  ILE G1014   N  LEU G 946           
SHEET    5  AH 5 HIS G1039  ASP G1041  1  O  ASP G1041   N  ASN G1015           
SHEET    1  AI 8 SER H   4  LEU H   9  0                                        
SHEET    2  AI 8 GLN H  14  ALA H  19 -1  O  PHE H  15   N  LEU H   7           
SHEET    3  AI 8 VAL H 108  ALA H 111 -1  O  ALA H 111   N  ARG H  18           
SHEET    4  AI 8 GLY H  79  VAL H  81  1  N  LEU H  80   O  ILE H 110           
SHEET    5  AI 8 GLN H  51  LEU H  55  1  N  VAL H  53   O  VAL H  81           
SHEET    6  AI 8 GLY H  24  ASN H  33  1  N  GLU H  29   O  ILE H  52           
SHEET    7  AI 8 GLN H 128  ALA H 134 -1  O  GLY H 130   N  GLY H  28           
SHEET    8  AI 8 SER H   4  LEU H   9 -1  N  LEU H   6   O  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  N  VAL H 194   O  ARG H 215           
SHEET    4  AJ10 GLY H 235  LEU H 238  1  O  PHE H 237   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  O  PHE H 348   N  GLY H 267           
SHEET    7  AJ10 LEU H 337  ARG H 342 -1  N  ARG H 342   O  ALA H 347           
SHEET    8  AJ10 LEU H 325  SER H 331 -1  N  HIS H 329   O  GLN H 338           
SHEET    9  AJ10 THR H 283  ASP H 299 -1  N  LYS H 298   O  LYS H 330           
SHEET   10  AJ10 VAL H 305  VAL H 316 -1  O  ALA H 315   N  VAL H 284           
LINK         OE1 GLU A 127                 K     K A1077     1555   1555  2.77  
LINK         O   THR A 143                 K     K A1082     1555   1555  2.84  
LINK         OG1 THR A 143                 K     K A1082     1555   1555  2.61  
LINK         OE2 GLU A 215                 K     K A1076     1555   1555  2.72  
LINK         OD1 ASN A 236                 K     K A1076     1555   1555  2.89  
LINK         O   ASP A 238                 K     K A1076     1555   1555  2.78  
LINK         O   ALA A 239                 K     K A1076     1555   1555  2.77  
LINK         O   ILE A 242                 K     K A1076     1555   1555  2.52  
LINK         OG  SER A 247                 K     K A1076     1555   1555  2.75  
LINK         OE1 GLN A 285                MN    MN A1075     1555   1555  1.99  
LINK         OE1 GLU A 299                MN    MN A1074     1555   1555  2.16  
LINK         OE1 GLU A 299                 K     K A1077     1555   1555  2.82  
LINK         OE2 GLU A 299                MN    MN A1074     1555   1555  2.32  
LINK         OE2 GLU A 299                MN    MN A1075     1555   1555  2.27  
LINK         O   MET A 300                 K     K A1077     1555   1555  2.62  
LINK         OD1 ASN A 301                MN    MN A1074     1555   1555  2.01  
LINK         OE2 GLU A 761                 K     K A1080     1555   1555  2.64  
LINK         ND1 HIS A 781                 K     K A1080     1555   1555  2.68  
LINK         O   GLU A 783                 K     K A1080     1555   1555  2.90  
LINK         O   GLN A 784                 K     K A1080     1555   1555  2.83  
LINK         O   VAL A 787                 K     K A1080     1555   1555  2.61  
LINK         OG  SER A 792                 K     K A1080     1555   1555  2.76  
LINK         OE1 GLN A 829                MN    MN A1079     1555   1555  2.12  
LINK         OE2 GLU A 841                MN    MN A1079     1555   1555  2.33  
LINK         O   HIS B  16                 K     K B 383     1555   1555  2.75  
LINK         O   ASP B 112                 K     K B 383     1555   1555  2.69  
LINK         OE1 GLU C 127                 K     K C1077     1555   1555  2.69  
LINK         OG1 THR C 143                 K     K C1082     1555   1555  2.98  
LINK         O   ALA C 144                 K     K C1082     1555   1555  2.95  
LINK         OE2 GLU C 215                 K     K C1076     1555   1555  2.62  
LINK         OD1 ASN C 236                 K     K C1076     1555   1555  2.88  
LINK         O   ASP C 238                 K     K C1076     1555   1555  2.64  
LINK         O   ALA C 239                 K     K C1076     1555   1555  2.74  
LINK         O   ILE C 242                 K     K C1076     1555   1555  2.68  
LINK         OG  SER C 247                 K     K C1076     1555   1555  2.77  
LINK         OE1 GLN C 285                MN    MN C1075     1555   1555  2.28  
LINK         OE1 GLU C 299                 K     K C1077     1555   1555  2.81  
LINK         OE1 GLU C 299                MN    MN C1074     1555   1555  2.22  
LINK         OE2 GLU C 299                MN    MN C1075     1555   1555  2.30  
LINK         OE2 GLU C 299                MN    MN C1074     1555   1555  2.22  
LINK         O   MET C 300                 K     K C1077     1555   1555  2.79  
LINK         OD1 ASN C 301                MN    MN C1074     1555   1555  2.13  
LINK         OE2 GLU C 761                 K     K C1080     1555   1555  2.78  
LINK         ND1 HIS C 781                 K     K C1080     1555   1555  2.71  
LINK         O   GLU C 783                 K     K C1080     1555   1555  2.82  
LINK         O   GLN C 784                 K     K C1080     1555   1555  2.98  
LINK         O   VAL C 787                 K     K C1080     1555   1555  2.59  
LINK         OG  SER C 792                 K     K C1080     1555   1555  2.74  
LINK         OE1 GLN C 829                MN    MN C1079     1555   1555  2.23  
LINK         OE2 GLU C 841                MN    MN C1079     1555   1555  2.14  
LINK         O   HIS D  16                 K     K D 383     1555   1555  2.60  
LINK         O   ASP D 112                 K     K D 383     1555   1555  2.72  
LINK         O   ASP E  84                 K     K E1081     1555   1555  2.75  
LINK         O   GLY E 112                 K     K E1081     1555   1555  2.83  
LINK         OG1 THR E 114                 K     K E1081     1555   1555  2.59  
LINK         OE1 GLU E 127                 K     K E1077     1555   1555  2.73  
LINK         OG1 THR E 143                 K     K E1083     1555   1555  2.97  
LINK         O   ALA E 144                 K     K E1083     1555   1555  2.83  
LINK         OE2 GLU E 215                 K     K E1076     1555   1555  2.47  
LINK         OD1 ASN E 236                 K     K E1076     1555   1555  2.91  
LINK         O   ASP E 238                 K     K E1076     1555   1555  2.60  
LINK         O   ALA E 239                 K     K E1076     1555   1555  2.81  
LINK         O   ILE E 242                 K     K E1076     1555   1555  2.72  
LINK         OG  SER E 247                 K     K E1076     1555   1555  2.74  
LINK         OE1 GLN E 285                MN    MN E1075     1555   1555  2.19  
LINK         OE1 GLU E 299                MN    MN E1074     1555   1555  2.37  
LINK         OE1 GLU E 299                 K     K E1077     1555   1555  2.74  
LINK         OE2 GLU E 299                MN    MN E1074     1555   1555  2.31  
LINK         OE2 GLU E 299                MN    MN E1075     1555   1555  2.21  
LINK         O   MET E 300                 K     K E1077     1555   1555  2.69  
LINK         OD1 ASN E 301                MN    MN E1074     1555   1555  2.27  
LINK         OE2 GLU E 761                 K     K E1080     1555   1555  2.61  
LINK         ND1 HIS E 781                 K     K E1080     1555   1555  2.76  
LINK         O   GLU E 783                 K     K E1080     1555   1555  2.77  
LINK         O   GLN E 784                 K     K E1080     1555   1555  2.74  
LINK         O   VAL E 787                 K     K E1080     1555   1555  2.57  
LINK         OG  SER E 792                 K     K E1080     1555   1555  2.76  
LINK         OE1 GLN E 829                MN    MN E1079     1555   1555  2.07  
LINK         OE2 GLU E 841                MN    MN E1079     1555   1555  2.16  
LINK         O   HIS F  16                 K     K F 383     1555   1555  2.80  
LINK         O   ASP F 112                 K     K F 383     1555   1555  2.93  
LINK         O   GLY G 112                 K     K G1081     1555   1555  2.74  
LINK         OG1 THR G 114                 K     K G1081     1555   1555  2.96  
LINK         O   THR G 143                 K     K G1083     1555   1555  2.93  
LINK         OG1 THR G 143                 K     K G1083     1555   1555  2.71  
LINK         OD1 ASN G 236                 K     K G1076     1555   1555  2.84  
LINK         O   ASP G 238                 K     K G1076     1555   1555  2.87  
LINK         O   ALA G 239                 K     K G1076     1555   1555  2.70  
LINK         O   ILE G 242                 K     K G1076     1555   1555  2.59  
LINK         OG  SER G 247                 K     K G1076     1555   1555  2.90  
LINK         OE1 GLN G 285                MN    MN G1075     1555   1555  2.18  
LINK         OE1 GLU G 299                 K     K G1077     1555   1555  2.77  
LINK         OE1 GLU G 299                MN    MN G1074     1555   1555  2.27  
LINK         OE2 GLU G 299                MN    MN G1075     1555   1555  2.04  
LINK         OE2 GLU G 299                MN    MN G1074     1555   1555  2.40  
LINK         O   MET G 300                 K     K G1077     1555   1555  2.86  
LINK         OD1 ASN G 301                MN    MN G1074     1555   1555  2.03  
LINK         OE2 GLU G 761                 K     K G1080     1555   1555  2.72  
LINK         ND1 HIS G 781                 K     K G1080     1555   1555  2.73  
LINK         O   GLU G 783                 K     K G1080     1555   1555  2.81  
LINK         O   GLN G 784                 K     K G1080     1555   1555  2.78  
LINK         O   VAL G 787                 K     K G1080     1555   1555  2.84  
LINK         OG  SER G 792                 K     K G1080     1555   1555  2.72  
LINK         OE1 GLN G 829                MN    MN G1079     1555   1555  2.13  
LINK         OE2 GLU G 841                MN    MN G1079     1555   1555  2.26  
LINK        MN    MN A1074                 O3B ADP A1087     1555   1555  2.07  
LINK        MN    MN A1074                 O   HOH A1191     1555   1555  2.12  
LINK        MN    MN A1074                 O1  PO4 A1078     1555   1555  2.20  
LINK        MN    MN A1075                 O3  PO4 A1078     1555   1555  2.18  
LINK        MN    MN A1075                 O1B ADP A1087     1555   1555  2.13  
LINK        MN    MN A1075                 O1A ADP A1087     1555   1555  2.07  
LINK        MN    MN A1075                 O   HOH A1605     1555   1555  2.28  
LINK         K     K A1077                 O   HOH A1607     1555   1555  2.42  
LINK         K     K A1077                 O   HOH A1193     1555   1555  2.94  
LINK        MN    MN A1079                 O2A ADP A1088     1555   1555  2.08  
LINK        MN    MN A1079                 O   HOH A1903     1555   1555  2.41  
LINK        MN    MN A1079                 O3B ADP A1088     1555   1555  2.02  
LINK        MN    MN A1079                 O   HOH A1608     1555   1555  2.18  
LINK         K     K A1082                 O   HOH A1203     1555   1555  2.79  
LINK         K     K A1082                 O   HOH A1202     1555   1555  2.39  
LINK         K     K A1082                 O   HOH A1204     1555   1555  2.90  
LINK         K     K B 383                 O   HOH A1457     1555   1555  2.85  
LINK         K     K B 383                 O   HOH B3605     1555   1555  2.69  
LINK         K     K B 383                 O   HOH A1456     1555   1555  2.92  
LINK         K     K B 383                 O   HOH B3394     1555   1555  2.99  
LINK        MN    MN C1074                 O3B ADP C1089     1555   1555  2.04  
LINK        MN    MN C1074                 O   HOH C1191     1555   1555  1.96  
LINK        MN    MN C1074                 O1  PO4 C1078     1555   1555  2.18  
LINK        MN    MN C1075                 O1A ADP C1089     1555   1555  2.10  
LINK        MN    MN C1075                 O   HOH C1587     1555   1555  2.24  
LINK        MN    MN C1075                 O3  PO4 C1078     1555   1555  2.06  
LINK        MN    MN C1075                 O1B ADP C1089     1555   1555  2.25  
LINK         K     K C1077                 O   HOH C1193     1555   1555  2.85  
LINK        MN    MN C1079                 O3B ADP C1090     1555   1555  1.91  
LINK        MN    MN C1079                 O2A ADP C1090     1555   1555  2.06  
LINK        MN    MN C1079                 O   HOH C1589     1555   1555  2.24  
LINK        MN    MN C1079                 O   HOH C1590     1555   1555  2.35  
LINK         K     K C1082                 O   HOH C1201     1555   1555  2.55  
LINK         K     K C1082                 O   HOH C1202     1555   1555  2.88  
LINK         K     K D 383                 O   HOH D2536     1555   1555  2.52  
LINK         K     K D 383                 O   HOH D2331     1555   1555  2.76  
LINK         K     K D 383                 O   HOH C1451     1555   1555  2.70  
LINK        MN    MN E1074                 O3B ADP E1089     1555   1555  2.20  
LINK        MN    MN E1074                 O   HOH E1193     1555   1555  2.01  
LINK        MN    MN E1074                 O1  PO4 E1078     1555   1555  2.13  
LINK        MN    MN E1075                 O1B ADP E1089     1555   1555  2.08  
LINK        MN    MN E1075                 O   HOH E1597     1555   1555  2.18  
LINK        MN    MN E1075                 O1A ADP E1089     1555   1555  2.09  
LINK        MN    MN E1075                 O3  PO4 E1078     1555   1555  2.16  
LINK         K     K E1077                 O   HOH E1195     1555   1555  2.83  
LINK        MN    MN E1079                 O2A ADP E1090     1555   1555  2.04  
LINK        MN    MN E1079                 O   HOH E1602     1555   1555  2.38  
LINK        MN    MN E1079                 O3B ADP E1090     1555   1555  2.03  
LINK         K     K E1083                 O   HOH E1202     1555   1555  2.64  
LINK         K     K F 383                 O   HOH E1447     1555   1555  2.93  
LINK        MN    MN G1074                 O   HOH G1190     1555   1555  2.39  
LINK        MN    MN G1074                 O1  PO4 G1078     1555   1555  1.94  
LINK        MN    MN G1074                 O3B ADP G1089     1555   1555  2.22  
LINK        MN    MN G1075                 O3  PO4 G1078     1555   1555  2.14  
LINK        MN    MN G1075                 O   HOH G1549     1555   1555  1.97  
LINK        MN    MN G1075                 O1A ADP G1089     1555   1555  2.12  
LINK        MN    MN G1075                 O1B ADP G1089     1555   1555  2.07  
LINK         K     K G1077                 O   HOH G1190     1555   1555  2.99  
LINK        MN    MN G1079                 O3B ADP G1090     1555   1555  2.07  
LINK        MN    MN G1079                 O   HOH G1551     1555   1555  2.01  
LINK        MN    MN G1079                 O   HOH G1550     1555   1555  2.29  
LINK        MN    MN G1079                 O2A ADP G1090     1555   1555  2.17  
LINK         K     K G1083                 O   HOH G1199     1555   1555  2.72  
LINK         K     K G1083                 O   HOH G1198     1555   1555  2.56  
LINK         K     K H 383                 O   HOH G1422     1555   1555  2.99  
LINK         K     K H 383                 O   HOH G1423     1555   1555  2.97  
CISPEP   1 PHE A  164    PRO A  165          0        -1.29                     
CISPEP   2 ALA A  251    PRO A  252          0        -2.49                     
CISPEP   3 TYR A  710    PRO A  711          0         0.36                     
CISPEP   4 LEU A  796    PRO A  797          0         4.08                     
CISPEP   5 ARG A  998    PRO A  999          0        -1.01                     
CISPEP   6 SER B  357    PRO B  358          0         3.86                     
CISPEP   7 PHE C  164    PRO C  165          0        -2.36                     
CISPEP   8 ALA C  251    PRO C  252          0         1.54                     
CISPEP   9 TYR C  710    PRO C  711          0         2.28                     
CISPEP  10 LEU C  796    PRO C  797          0         3.86                     
CISPEP  11 ARG C  998    PRO C  999          0        -4.52                     
CISPEP  12 SER D  357    PRO D  358          0         4.57                     
CISPEP  13 PHE E  164    PRO E  165          0         1.15                     
CISPEP  14 ALA E  251    PRO E  252          0        -0.40                     
CISPEP  15 TYR E  710    PRO E  711          0         1.32                     
CISPEP  16 LEU E  796    PRO E  797          0        -0.41                     
CISPEP  17 ARG E  998    PRO E  999          0        -7.70                     
CISPEP  18 SER F  357    PRO F  358          0         3.78                     
CISPEP  19 PHE G  164    PRO G  165          0         2.71                     
CISPEP  20 ALA G  251    PRO G  252          0         4.41                     
CISPEP  21 TYR G  710    PRO G  711          0         1.28                     
CISPEP  22 LEU G  796    PRO G  797          0         0.55                     
CISPEP  23 ARG G  998    PRO G  999          0         0.79                     
CISPEP  24 SER H  357    PRO H  358          0         3.19                     
SITE     1 AC1  5 GLU A 299  ASN A 301  PO4 A1078  ADP A1087                    
SITE     2 AC1  5 HOH A1191                                                     
SITE     1 AC2  5 GLN A 285  GLU A 299  PO4 A1078  ADP A1087                    
SITE     2 AC2  5 HOH A1605                                                     
SITE     1 AC3  6 GLU A 215  ASN A 236  ASP A 238  ALA A 239                    
SITE     2 AC3  6 ILE A 242  SER A 247                                          
SITE     1 AC4  7 ALA A 126  GLU A 127  GLU A 299  MET A 300                    
SITE     2 AC4  7 ASN A 301  HOH A1193  HOH A1607                               
SITE     1 AC5 14 MET A 174  GLY A 175  HIS A 243  GLN A 285                    
SITE     2 AC5 14 GLU A 299  ASN A 301  ARG A 303  ARG A 306                    
SITE     3 AC5 14  MN A1074   MN A1075  ADP A1087  HOH A1130                    
SITE     4 AC5 14 HOH A1305  HOH A1306                                          
SITE     1 AC6  5 GLN A 829  GLU A 841  ADP A1088  HOH A1608                    
SITE     2 AC6  5 HOH A1903                                                     
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  2 GLN A  93  MET A 174                                          
SITE     1 AC9  5 THR A 143  ALA A 144  HOH A1202  HOH A1203                    
SITE     2 AC9  5 HOH A1204                                                     
SITE     1 BC1  2 TRP A  71  HOH A1622                                          
SITE     1 BC2  3 ASN A 289  ASN A 292  ARG A 294                               
SITE     1 BC3  5 ALA A 370  ASN A 371  PHE A 900  PRO A 901                    
SITE     2 BC3  5 GLY A 902                                                     
SITE     1 BC4  3 LYS A 475  ASN A 485  PHE A 488                               
SITE     1 BC5  6 HOH A1456  HOH A1457  HIS B  16  ASP B 112                    
SITE     2 BC5  6 HOH B3394  HOH B3605                                          
SITE     1 BC6  6 GLU C 299  ASN C 301   MN C1075  PO4 C1078                    
SITE     2 BC6  6 ADP C1089  HOH C1191                                          
SITE     1 BC7  6 GLN C 285  GLU C 299   MN C1074  PO4 C1078                    
SITE     2 BC7  6 ADP C1089  HOH C1587                                          
SITE     1 BC8  6 GLU C 215  ASN C 236  ASP C 238  ALA C 239                    
SITE     2 BC8  6 ILE C 242  SER C 247                                          
SITE     1 BC9  6 ALA C 126  GLU C 127  GLU C 299  MET C 300                    
SITE     2 BC9  6 ASN C 301  HOH C1193                                          
SITE     1 CC1 13 MET C 174  GLY C 175  HIS C 243  GLN C 285                    
SITE     2 CC1 13 GLU C 299  ASN C 301  ARG C 303  ARG C 306                    
SITE     3 CC1 13  MN C1074   MN C1075  ADP C1089  HOH C1191                    
SITE     4 CC1 13 HOH C1301                                                     
SITE     1 CC2  5 GLN C 829  GLU C 841  ADP C1090  HOH C1589                    
SITE     2 CC2  5 HOH C1590                                                     
SITE     1 CC3  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784                    
SITE     2 CC3  6 VAL C 787  SER C 792                                          
SITE     1 CC4  3 THR C 173  MET C 174  HOH C1127                               
SITE     1 CC5  4 THR C 143  ALA C 144  HOH C1201  HOH C1202                    
SITE     1 CC6  1 TRP C  71                                                     
SITE     1 CC7  3 ASN C 289  ASN C 292  ARG C 294                               
SITE     1 CC8  5 ALA C 370  ASN C 371  PHE C 900  PRO C 901                    
SITE     2 CC8  5 GLY C 902                                                     
SITE     1 CC9  3 LYS C 475  ASN C 485  HOH C1607                               
SITE     1 DC1  5 HOH C1451  HIS D  16  ASP D 112  HOH D2331                    
SITE     2 DC1  5 HOH D2536                                                     
SITE     1 DC2  4 GLU C 549  PHE D  15  ASP D 114  HOH D2330                    
SITE     1 DC3  4 PHE C 578  ARG C 845  ALA C 847  ARG C 848                    
SITE     1 DC4  2 GLU C 560  ASP C 592                                          
SITE     1 DC5  5 GLU E 299  ASN E 301  PO4 E1078  ADP E1089                    
SITE     2 DC5  5 HOH E1193                                                     
SITE     1 DC6  5 GLN E 285  GLU E 299  PO4 E1078  ADP E1089                    
SITE     2 DC6  5 HOH E1597                                                     
SITE     1 DC7  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239                    
SITE     2 DC7  6 ILE E 242  SER E 247                                          
SITE     1 DC8  7 ALA E 126  GLU E 127  GLU E 299  MET E 300                    
SITE     2 DC8  7 ASN E 301  HOH E1193  HOH E1195                               
SITE     1 DC9 13 MET E 174  GLY E 175  HIS E 243  GLN E 285                    
SITE     2 DC9 13 GLU E 299  ASN E 301  ARG E 303  ARG E 306                    
SITE     3 DC9 13  MN E1074   MN E1075  ADP E1089  HOH E1129                    
SITE     4 DC9 13 HOH E1303                                                     
SITE     1 EC1  5 GLN E 829  GLU E 841  ADP E1090  HOH E1601                    
SITE     2 EC1  5 HOH E1602                                                     
SITE     1 EC2  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784                    
SITE     2 EC2  6 VAL E 787  SER E 792                                          
SITE     1 EC3  5 ASP E  84  GLY E 112  THR E 114  HOH E1095                    
SITE     2 EC3  5 HOH E1605                                                     
SITE     1 EC4  2 THR E 173  MET E 174                                          
SITE     1 EC5  4 THR E 143  ALA E 144  HOH E1202  HOH E1203                    
SITE     1 EC6  1 TRP E  71                                                     
SITE     1 EC7  3 ASN E 289  ASN E 292  ARG E 294                               
SITE     1 EC8  5 ALA E 370  ASN E 371  PHE E 900  PRO E 901                    
SITE     2 EC8  5 GLY E 902                                                     
SITE     1 EC9  3 LYS E 475  ASN E 485  HOH E1614                               
SITE     1 FC1  4 HOH E1447  HIS F  16  ASP F 112  HOH F1308                    
SITE     1 FC2  5 GLU E 549  HOH E1447  PHE F  15  ASP F 114                    
SITE     2 FC2  5 HOH F1307                                                     
SITE     1 FC3  2 ALA E 847  ARG E 848                                          
SITE     1 FC4  7 MET G 174  GLU G 299  ASN G 301   MN G1075                    
SITE     2 FC4  7 PO4 G1078  ADP G1089  HOH G1190                               
SITE     1 FC5  6 GLN G 285  GLU G 299   MN G1074  PO4 G1078                    
SITE     2 FC5  6 ADP G1089  HOH G1549                                          
SITE     1 FC6  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239                    
SITE     2 FC6  6 ILE G 242  SER G 247                                          
SITE     1 FC7  7 ALA G 126  GLU G 127  GLU G 299  MET G 300                    
SITE     2 FC7  7 ASN G 301  HOH G1190  HOH G1191                               
SITE     1 FC8 14 MET G 174  GLY G 175  HIS G 243  GLN G 285                    
SITE     2 FC8 14 GLU G 299  ASN G 301  ARG G 303  ARG G 306                    
SITE     3 FC8 14  MN G1074   MN G1075  ADP G1089  HOH G1130                    
SITE     4 FC8 14 HOH G1289  HOH G1549                                          
SITE     1 FC9  5 GLN G 829  GLU G 841  ADP G1090  HOH G1550                    
SITE     2 FC9  5 HOH G1551                                                     
SITE     1 GC1  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784                    
SITE     2 GC1  6 VAL G 787  SER G 792                                          
SITE     1 GC2  3 ASP G  84  GLY G 112  THR G 114                               
SITE     1 GC3  5 GLN G  93  THR G 173  MET G 174  NET G1092                    
SITE     2 GC3  5 HOH G1122                                                     
SITE     1 GC4  4 THR G 143  ALA G 144  HOH G1198  HOH G1199                    
SITE     1 GC5  1 TRP G  71                                                     
SITE     1 GC6  3 ASN G 289  ASN G 292  ARG G 294                               
SITE     1 GC7  5 ASN G 371  PHE G 900  PRO G 901  GLY G 902                    
SITE     2 GC7  5 HOH G1246                                                     
SITE     1 GC8  4 LYS G 475  ASN G 485  PHE G 488  HOH G1419                    
SITE     1 GC9  4 HOH G1422  HOH G1423  HIS H  16  ASP H 112                    
SITE     1 HC1  2 PHE H  15  ASP H 114                                          
SITE     1 HC2  3 ARG G 845  ALA G 847  ARG G 848                               
SITE     1 HC3  3 TRP H 170  THR H 171  GLN H 172                               
SITE     1 HC4 28 ARG A 129  ILE A 167  ARG A 169  THR A 173                    
SITE     2 HC4 28 MET A 174  GLY A 175  GLY A 176  ASP A 207                    
SITE     3 HC4 28 GLU A 208  LEU A 210  ILE A 211  GLU A 215                    
SITE     4 HC4 28 MET A 240  GLY A 241  ILE A 242  HIS A 243                    
SITE     5 HC4 28 THR A 244  GLN A 285  ILE A 298  GLU A 299                    
SITE     6 HC4 28 THR A 376   MN A1074   MN A1075  PO4 A1078                    
SITE     7 HC4 28 HOH A1191  HOH A1231  HOH A1244  HOH A1605                    
SITE     1 HC5 22 PRO A 690  ARG A 715  MET A 725  HIS A 754                    
SITE     2 HC5 22 PHE A 755  LEU A 756  GLU A 761  ALA A 785                    
SITE     3 HC5 22 GLY A 786  VAL A 787  HIS A 788  SER A 789                    
SITE     4 HC5 22 GLN A 829  GLU A 841  PRO A 909   MN A1079                    
SITE     5 HC5 22 HOH A1499  HOH A1522  HOH A1526  HOH A1608                    
SITE     6 HC5 22 HOH A1609  HOH A1903                                          
SITE     1 HC6 10 GLU A 783  ASP A 791  ALA A 793  GLU A 892                    
SITE     2 HC6 10 LEU A 907  TYR A1040  ASP A1041  THR A1042                    
SITE     3 HC6 10 HOH A1538  HOH A1564                                          
SITE     1 HC7  3 THR A  94  ASN A  97  ASN A 936                               
SITE     1 HC8 14 SER A 948  VAL A 949  LYS A 954  THR A 974                    
SITE     2 HC8 14 GLY A 976  THR A 977  LYS A 993  ASN A1015                    
SITE     3 HC8 14 THR A1016  THR A1017  ASP A1025  SER A1026                    
SITE     4 HC8 14 ILE A1029  HOH A1590                                          
SITE     1 HC9 28 ARG C 129  ILE C 167  ARG C 169  THR C 173                    
SITE     2 HC9 28 MET C 174  GLY C 175  GLY C 176  GLU C 208                    
SITE     3 HC9 28 SER C 209  LEU C 210  ILE C 211  GLU C 215                    
SITE     4 HC9 28 MET C 240  GLY C 241  ILE C 242  HIS C 243                    
SITE     5 HC9 28 THR C 244  GLN C 285  ILE C 298  GLU C 299                    
SITE     6 HC9 28 THR C 376   MN C1074   MN C1075  PO4 C1078                    
SITE     7 HC9 28 HOH C1191  HOH C1229  HOH C1244  HOH C1587                    
SITE     1 IC1 18 ARG C 715  MET C 725  HIS C 754  PHE C 755                    
SITE     2 IC1 18 LEU C 756  GLU C 761  ALA C 785  GLY C 786                    
SITE     3 IC1 18 VAL C 787  HIS C 788  SER C 789  GLN C 829                    
SITE     4 IC1 18 GLU C 841   MN C1079  HOH C1515  HOH C1516                    
SITE     5 IC1 18 HOH C1589  HOH C1590                                          
SITE     1 IC2  9 GLU C 783  ASP C 791  GLU C 892  LEU C 907                    
SITE     2 IC2  9 TYR C1040  ASP C1041  THR C1042  HOH C1530                    
SITE     3 IC2  9 HOH C1548                                                     
SITE     1 IC3  2 THR C  94  ASN C  97                                          
SITE     1 IC4 15 SER C 948  VAL C 949  LYS C 954  THR C 974                    
SITE     2 IC4 15 GLY C 976  THR C 977  LYS C 993  ASN C1015                    
SITE     3 IC4 15 THR C1016  THR C1017  ALA C1022  SER C1026                    
SITE     4 IC4 15 ILE C1029  HOH C1576  HOH C1846                               
SITE     1 IC5 26 ARG E 129  ILE E 167  ARG E 169  MET E 174                    
SITE     2 IC5 26 GLY E 175  GLY E 176  GLU E 208  LEU E 210                    
SITE     3 IC5 26 ILE E 211  GLU E 215  MET E 240  GLY E 241                    
SITE     4 IC5 26 ILE E 242  HIS E 243  THR E 244  GLN E 285                    
SITE     5 IC5 26 ILE E 298  GLU E 299  THR E 376   MN E1074                    
SITE     6 IC5 26  MN E1075  PO4 E1078  HOH E1193  HOH E1227                    
SITE     7 IC5 26 HOH E1244  HOH E1597                                          
SITE     1 IC6 22 PRO E 690  ARG E 715  MET E 725  HIS E 754                    
SITE     2 IC6 22 PHE E 755  LEU E 756  GLU E 761  ALA E 785                    
SITE     3 IC6 22 GLY E 786  VAL E 787  HIS E 788  SER E 789                    
SITE     4 IC6 22 GLN E 829  GLU E 841   MN E1079  HOH E1520                    
SITE     5 IC6 22 HOH E1521  HOH E1525  HOH E1598  HOH E1599                    
SITE     6 IC6 22 HOH E1600  HOH E1602                                          
SITE     1 IC7 10 GLU E 783  ASP E 791  GLU E 892  LEU E 907                    
SITE     2 IC7 10 TYR E1040  ASP E1041  THR E1042  HOH E1537                    
SITE     3 IC7 10 HOH E1560  HOH E1570                                          
SITE     1 IC8  3 GLN E  22  GLN E  93  THR E  94                               
SITE     1 IC9 17 SER E 948  VAL E 949  ARG E 950  LYS E 954                    
SITE     2 IC9 17 THR E 974  GLY E 976  THR E 977  LYS E 993                    
SITE     3 IC9 17 ASN E1015  THR E1016  THR E1017  ASP E1025                    
SITE     4 IC9 17 SER E1026  ILE E1029  HOH E1585  HOH E1839                    
SITE     5 IC9 17 HOH E1847                                                     
SITE     1 JC1 27 ARG G 129  ILE G 167  ARG G 169  THR G 173                    
SITE     2 JC1 27 MET G 174  GLY G 175  GLY G 176  GLU G 208                    
SITE     3 JC1 27 LEU G 210  ILE G 211  GLU G 215  MET G 240                    
SITE     4 JC1 27 GLY G 241  ILE G 242  HIS G 243  THR G 244                    
SITE     5 JC1 27 GLN G 285  ILE G 298  GLU G 299  THR G 376                    
SITE     6 JC1 27  MN G1074   MN G1075  PO4 G1078  HOH G1222                    
SITE     7 JC1 27 HOH G1237  HOH G1548  HOH G1549                               
SITE     1 JC2 17 ARG G 715  HIS G 754  PHE G 755  LEU G 756                    
SITE     2 JC2 17 GLU G 761  ALA G 785  GLY G 786  VAL G 787                    
SITE     3 JC2 17 HIS G 788  SER G 789  GLN G 829  GLU G 841                    
SITE     4 JC2 17  MN G1079  HOH G1474  HOH G1478  HOH G1550                    
SITE     5 JC2 17 HOH G1551                                                     
SITE     1 JC3 10 GLU G 783  ASP G 791  GLU G 892  LEU G 907                    
SITE     2 JC3 10 TYR G1040  ASP G1041  THR G1042  HOH G1488                    
SITE     3 JC3 10 HOH G1511  HOH G1554                                          
SITE     1 JC4  4 GLN G  22  THR G  94  ASN G  97   CL G1082                    
SITE     1 JC5 15 SER G 948  VAL G 949  LYS G 954  THR G 974                    
SITE     2 JC5 15 GLY G 976  THR G 977  LYS G 993  ASN G1015                    
SITE     3 JC5 15 THR G1016  THR G1017  ALA G1022  ASP G1025                    
SITE     4 JC5 15 SER G1026  ILE G1029  HOH G1537                               
CRYST1  152.500  164.900  333.100  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006557  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006064  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003002        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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