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Database: PDB
Entry: 1BXR
LinkDB: 1BXR
Original site: 1BXR 
HEADER    AMIDOTRANSFERASE                        08-OCT-98   1BXR              
TITLE     STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED WITH THE ATP    
TITLE    2 ANALOG AMPPNP                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBAMOYL-PHOSPHATE SYNTHASE;                              
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 EC: 6.3.5.5;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CARBAMOYL-PHOSPHATE SYNTHASE;                              
COMPND   8 CHAIN: B, D, F, H;                                                   
COMPND   9 EC: 6.3.5.5;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   8 ORGANISM_TAXID: 562;                                                 
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    AMIDOTRANSFERASE, CARBAMOYL-PHOSPHATE SYNTHASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.THODEN,G.WESENBERG,F.M.RAUSHEL,H.M.HOLDEN                         
REVDAT   3   13-JUL-11 1BXR    1       VERSN                                    
REVDAT   2   24-FEB-09 1BXR    1       VERSN                                    
REVDAT   1   20-APR-99 1BXR    0                                                
JRNL        AUTH   J.B.THODEN,G.WESENBERG,F.M.RAUSHEL,H.M.HOLDEN                
JRNL        TITL   CARBAMOYL PHOSPHATE SYNTHETASE: CLOSURE OF THE B-DOMAIN AS A 
JRNL        TITL 2 RESULT OF NUCLEOTIDE BINDING.                                
JRNL        REF    BIOCHEMISTRY                  V.  38  2347 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10029528                                                     
JRNL        DOI    10.1021/BI982517H                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT V. 5-E                                           
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        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 446040                         
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1950                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1950                 
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) : 446040                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 44652                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 366                                     
REMARK   3   SOLVENT ATOMS            : 3242                                    
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) : 0.010 ; 10.000; 45799           
REMARK   3   BOND ANGLES            (DEGREES) : 2.123 ; 18.000; 61795           
REMARK   3   TORSION ANGLES         (DEGREES) : 18.310; 0.000 ; 27671           
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.007 ; 25.500; 1212            
REMARK   3   GENERAL PLANES               (A) : 0.012 ; 50.000; 6659            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : 0.025 ; NULL  ; 813             
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.90                                                 
REMARK   3   BSOL        : 435.50                                               
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : TNT PROTGEO                                      
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  RESIDUES MODELED IN DUAL CONFORMATIONS: ASP A 757, MET A            
REMARK   3  MET A 772, LYS A 881, ARG A 912, ARG E 104, ASN E 936,              
REMARK   3  GLU E 1009, ARG G 490, AND ASN G 936                                
REMARK   4                                                                      
REMARK   4 1BXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUL-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               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 446040                             
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     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.5000                            
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     (%) : 80.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1A9X                                       
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: PH 7.4                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       75.95000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      166.30000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       82.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      166.30000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       75.95000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       82.25000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 9150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   381                                                      
REMARK 465     LYS B   382                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D   381                                                      
REMARK 465     LYS D   382                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F   381                                                      
REMARK 465     LYS F   382                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ALA H   381                                                      
REMARK 465     LYS H   382                                                      
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 F  2544     O    HOH F  2548              2.09            
REMARK 500   O    HOH C  4348     O    HOH C  4349              2.11            
REMARK 500   O    HOH G  4094     O    HOH G  4095              2.13            
REMARK 500   O    HOH H  3346     O    HOH H  3578              2.13            
REMARK 500   O    HOH A  1507     O    HOH A  1508              2.14            
REMARK 500   OE2  GLU A    39     O    HOH A  1380              2.16            
REMARK 500   O    HOH G  4402     O    HOH G  4424              2.16            
REMARK 500   OD1  ASN C   337     O    HOH C  4485              2.17            
REMARK 500   OE1  GLU G   628     O    HOH G  4185              2.17            
REMARK 500   O    HOH E  3610     O    HOH E  3611              2.19            
REMARK 500   O3'  ANP E  2910     O    HOH E  3414              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  39   CD    GLU A  39   OE1     0.109                       
REMARK 500    GLU A 103   CD    GLU A 103   OE1     0.069                       
REMARK 500    GLU A 110   CD    GLU A 110   OE1     0.075                       
REMARK 500    GLU A 127   CD    GLU A 127   OE1     0.068                       
REMARK 500    GLU A 153   CD    GLU A 153   OE1     0.072                       
REMARK 500    GLU A 186   CD    GLU A 186   OE2     0.070                       
REMARK 500    GLU A 190   CD    GLU A 190   OE1     0.076                       
REMARK 500    GLU A 260   CD    GLU A 260   OE2     0.072                       
REMARK 500    THR A 279   C     THR A 279   O      -0.124                       
REMARK 500    GLU A 419   CD    GLU A 419   OE1     0.089                       
REMARK 500    GLU A 427   CD    GLU A 427   OE2     0.073                       
REMARK 500    GLU A 474   CD    GLU A 474   OE1     0.072                       
REMARK 500    GLU A 478   CD    GLU A 478   OE1     0.066                       
REMARK 500    GLU A 535   CD    GLU A 535   OE1     0.068                       
REMARK 500    GLU A 549   CD    GLU A 549   OE2     0.067                       
REMARK 500    GLU A 560   CD    GLU A 560   OE2     0.066                       
REMARK 500    GLU A 577   CD    GLU A 577   OE1     0.082                       
REMARK 500    GLU A 591   CD    GLU A 591   OE1     0.081                       
REMARK 500    GLU A 628   CD    GLU A 628   OE1     0.074                       
REMARK 500    GLU A 676   CD    GLU A 676   OE2     0.072                       
REMARK 500    GLU A 683   CD    GLU A 683   OE1     0.066                       
REMARK 500    GLU A 699   CD    GLU A 699   OE1     0.067                       
REMARK 500    GLU A 699   CD    GLU A 699   OE2    -0.069                       
REMARK 500    GLU A 731   CD    GLU A 731   OE1     0.070                       
REMARK 500    GLU A 804   CD    GLU A 804   OE1     0.091                       
REMARK 500    GLU A 819   CD    GLU A 819   OE1     0.069                       
REMARK 500    LYS A 833   CE    LYS A 833   NZ     -0.173                       
REMARK 500    GLU A 876   CD    GLU A 876   OE2     0.072                       
REMARK 500    GLU A 910   CD    GLU A 910   OE2     0.082                       
REMARK 500    GLU A 951   CD    GLU A 951   OE1     0.068                       
REMARK 500    GLU A 955   CD    GLU A 955   OE1     0.070                       
REMARK 500    GLU A 983   CD    GLU A 983   OE1     0.075                       
REMARK 500    GLU A 996   CD    GLU A 996   OE2     0.077                       
REMARK 500    GLU A1024   CD    GLU A1024   OE1     0.072                       
REMARK 500    GLU A1060   CD    GLU A1060   OE2     0.067                       
REMARK 500    GLU A1067   CD    GLU A1067   OE1     0.071                       
REMARK 500    GLU B 145   CD    GLU B 145   OE1     0.070                       
REMARK 500    GLU B 166   CD    GLU B 166   OE2     0.069                       
REMARK 500    GLU B 187   CD    GLU B 187   OE1     0.068                       
REMARK 500    GLU B 189   CD    GLU B 189   OE2     0.067                       
REMARK 500    GLU B 260   CD    GLU B 260   OE2     0.070                       
REMARK 500    GLU B 301   CD    GLU B 301   OE1     0.070                       
REMARK 500    GLU B 318   CD    GLU B 318   OE2     0.066                       
REMARK 500    GLU B 372   CD    GLU B 372   OE1     0.069                       
REMARK 500    GLU C  59   CD    GLU C  59   OE1     0.067                       
REMARK 500    GLU C  79   CD    GLU C  79   OE2     0.067                       
REMARK 500    GLU C 103   CD    GLU C 103   OE1     0.066                       
REMARK 500    GLU C 109   CD    GLU C 109   OE2     0.084                       
REMARK 500    GLU C 110   CD    GLU C 110   OE1     0.093                       
REMARK 500    GLU C 110   CD    GLU C 110   OE2    -0.075                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     173 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A   6   CB  -  CG  -  OD1 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A  43   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU A  59   CG  -  CD  -  OE1 ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ASP A  62   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A  62   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ASP A 121   CB  -  CG  -  OD1 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ASP A 133   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 161   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A 207   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 207   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 226   CB  -  CG  -  OD1 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    ASP A 226   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP A 246   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 372   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASP A 410   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 430   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 434   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 434   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 487   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A 490   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 494   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 514   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 514   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP A 518   CB  -  CG  -  OD1 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    ASP A 518   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 521   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP A 521   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 530   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 530   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 539   N   -  CA  -  CB  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ASP A 558   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A 579   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 579   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TYR A 580   N   -  CA  -  CB  ANGL. DEV. = -11.2 DEGREES          
REMARK 500    TYR A 580   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 592   CB  -  CG  -  OD1 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ASP A 592   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 609   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 609   CB  -  CG  -  OD2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    THR A 646   CA  -  CB  -  CG2 ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ASP A 670   CB  -  CG  -  OD1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP A 670   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG A 671   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 675   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG A 677   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 684   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     336 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     -144.19    -88.90                                   
REMARK 500    ASP A   6        0.89    -68.80                                   
REMARK 500    ALA A  23     -153.13   -114.30                                   
REMARK 500    ARG A 145      106.36    -39.75                                   
REMARK 500    SER A 146     -156.87   -128.93                                   
REMARK 500    ASP A 161      -74.59    -95.61                                   
REMARK 500    ASP A 226        1.99     85.16                                   
REMARK 500    GLU A 299     -178.47    178.45                                   
REMARK 500    ARG A 303     -167.02   -173.57                                   
REMARK 500    PRO A 318       76.13    -69.78                                   
REMARK 500    ASP A 353       43.05   -106.80                                   
REMARK 500    ASN A 363       39.18   -141.87                                   
REMARK 500    ALA A 368      -78.35    -38.43                                   
REMARK 500    THR A 375     -152.64   -147.99                                   
REMARK 500    ASP A 416       41.94   -106.09                                   
REMARK 500    ASP A 521       34.67     76.64                                   
REMARK 500    THR A 531      -16.02     69.62                                   
REMARK 500    ALA A 541       77.53   -112.13                                   
REMARK 500    GLU A 548     -154.94   -138.32                                   
REMARK 500    GLU A 549      -73.24    -87.32                                   
REMARK 500    ASN A 554       62.59     37.04                                   
REMARK 500    ALA A 588      -72.67    -56.72                                   
REMARK 500    CYS A 601       27.20   -147.01                                   
REMARK 500    THR A 646      -73.30    -53.71                                   
REMARK 500    PRO A 690     -177.42    -69.53                                   
REMARK 500    ASP A 758       49.83     38.22                                   
REMARK 500    THR A 800      -19.28   -140.07                                   
REMARK 500    PRO A 844       37.11    -67.69                                   
REMARK 500    PRO A 905       45.16    -80.31                                   
REMARK 500    SER A 948       85.07   -151.48                                   
REMARK 500    HIS A 975      -84.85    -29.46                                   
REMARK 500    LYS A 993     -173.73    -63.51                                   
REMARK 500    ARG A 998      135.90   -173.25                                   
REMARK 500    SER A1018      116.12   -164.07                                   
REMARK 500    ASP B 112       33.74     70.30                                   
REMARK 500    PRO B 191      -77.37    -50.61                                   
REMARK 500    VAL B 228      -72.21    -59.37                                   
REMARK 500    LEU B 229      -30.40    -37.43                                   
REMARK 500    ASN B 232       77.54     61.19                                   
REMARK 500    SER B 239     -177.94    -62.20                                   
REMARK 500    ALA B 246      -70.22    -42.61                                   
REMARK 500    CYS B 269      -99.87     67.25                                   
REMARK 500    ASN B 311       91.48   -174.90                                   
REMARK 500    ALA B 319       31.02    -76.52                                   
REMARK 500    THR B 320       14.47   -153.54                                   
REMARK 500    PRO B 346       50.80   -108.32                                   
REMARK 500    ALA B 356     -128.32     48.80                                   
REMARK 500    SER B 357       70.39     58.43                                   
REMARK 500    PRO C   2     -139.44    -94.56                                   
REMARK 500    ALA C  23     -155.11   -100.77                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     167 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY G1008        -12.92                                           
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    CYS A  24        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 129        18.9      L          L   OUTSIDE RANGE           
REMARK 500    CYS A 166        24.9      L          L   OUTSIDE RANGE           
REMARK 500    SER A 209        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 339        16.9      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 420        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 435        21.3      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 481        23.8      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 484        24.5      L          L   OUTSIDE RANGE           
REMARK 500    THR A 612        22.1      L          L   OUTSIDE RANGE           
REMARK 500    THR A 646        22.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 675        24.5      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 738        19.6      L          L   OUTSIDE RANGE           
REMARK 500    SER A 745        22.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 975        21.3      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 996        19.4      L          L   OUTSIDE RANGE           
REMARK 500    SER B   4        24.6      L          L   OUTSIDE RANGE           
REMARK 500    LEU B   6        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP B  69        22.3      L          L   OUTSIDE RANGE           
REMARK 500    ASP B 136        24.0      L          L   OUTSIDE RANGE           
REMARK 500    MET B 156        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR B 336        25.0      L          L   OUTSIDE RANGE           
REMARK 500    LYS C   3        23.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE C  26        19.2      L          L   OUTSIDE RANGE           
REMARK 500    TYR C  28        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 139        22.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 172        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 339        12.2      L          L   OUTSIDE RANGE           
REMARK 500    THR C 596        24.2      L          L   OUTSIDE RANGE           
REMARK 500    THR C 646        19.8      L          L   OUTSIDE RANGE           
REMARK 500    ARG C 675        24.5      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 738        23.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN C 835        24.9      L          L   OUTSIDE RANGE           
REMARK 500    HIS C 975        22.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP D  69        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ALA D 246        22.5      L          L   OUTSIDE RANGE           
REMARK 500    CYS E  24        22.7      L          L   OUTSIDE RANGE           
REMARK 500    THR E  56        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ARG E 129        24.4      L          L   OUTSIDE RANGE           
REMARK 500    THR E 201        21.8      L          L   OUTSIDE RANGE           
REMARK 500    SER E 209        22.2      L          L   OUTSIDE RANGE           
REMARK 500    ILE E 339        18.5      L          L   OUTSIDE RANGE           
REMARK 500    ARG E 435        24.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL E 479        21.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG E 559        18.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG E 675        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ALA E 705        16.4      L          L   OUTSIDE RANGE           
REMARK 500    TYR E 718        24.1      L          L   OUTSIDE RANGE           
REMARK 500    PHE E 738        22.7      L          L   OUTSIDE RANGE           
REMARK 500    ASN E 746        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      89 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 A1131        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A1185        DISTANCE =  7.34 ANGSTROMS                       
REMARK 525    HOH A1403        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A1407        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A1422        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A1456        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A1467        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH A1471        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH A1474        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A1499        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH A1570        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH A1575        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A1577        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A1578        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A1589        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH A1592        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A1628        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A1658        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH A1673        DISTANCE =  8.42 ANGSTROMS                       
REMARK 525    HOH B 995        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH B1136        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH C4082        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH C4086        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH C4305        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH C4306        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH C4309        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH C4316        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH C4369        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH C4402        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH C4422        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH C4457        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH C4474        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH C4476        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH C4483        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH C4490        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH C4503        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH C4504        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH C4505        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH C4506        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH C4507        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH C4585        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH D1211        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH D1333        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH D1570        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH D1579        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH D1761        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH D1850        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH E3084        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH E3088        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH E3306        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH E3312        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH E3339        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH E3366        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH E3381        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH E3453        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH E3455        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH E3458        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH E3469        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH E3485        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH E3489        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH E3490        DISTANCE =  7.76 ANGSTROMS                       
REMARK 525    HOH E3491        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH E3492        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH E3504        DISTANCE =  7.26 ANGSTROMS                       
REMARK 525    HOH E3531        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH E3536        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH E3553        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH E3619        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH F2544        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH F2570        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH F2686        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH F2687        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH F2826        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH G4090        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH G4299        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH G4314        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH G4361        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH G4365        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH G4376        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH H3333        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH H3380        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH H3463        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH H3540        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH H3561        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH H3580        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH H3617        DISTANCE =  6.54 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                              MN A1074  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 299   OE1                                                    
REMARK 620 2 GLU A 299   OE2  56.5                                              
REMARK 620 3 ASN A 301   OD1 111.2  77.9                                        
REMARK 620 4 HOH A1393   O   108.2 148.4  84.2                                  
REMARK 620 5 ANP A1083   O2B  70.7 107.1 174.5  90.4                            
REMARK 620 6 ANP A1083   O3G 145.5 112.4  95.8  95.1  84.4                      
REMARK 620 N                    1     2     3     4     5                       
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 MET A 300   O                                                      
REMARK 620 2 ALA A 126   O   106.6                                              
REMARK 620 3 GLU A 127   OE2  98.5  98.7                                        
REMARK 620 4 ASN A 301   OD1  65.8 163.2  68.9                                  
REMARK 620 5 HOH A1199   O   168.1  64.4  90.9 125.0                            
REMARK 620 6 HOH A1393   O   115.8 130.0  51.3  51.2  75.8                      
REMARK 620 7 GLU A 299   OE1  93.9 133.4 119.5  63.3  87.8  70.0                
REMARK 620 8 HOH A1200   O    71.4  72.2 162.9 116.5  97.8 145.3  75.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1077  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A1084   O2G                                                    
REMARK 620 2 ANP A1084   O2A 153.0                                              
REMARK 620 3 GLN A 829   OE1 111.2  95.0                                        
REMARK 620 4 HOH A1516   O    98.8  86.6  91.8                                  
REMARK 620 5 GLU A 841   OE2  85.7  89.4  86.5 175.5                            
REMARK 620 6 ANP A1084   N3B  61.7  91.8 172.6  91.6  90.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1078  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A1084   O3G                                                    
REMARK 620 2 ANP A1084   O2B  95.9                                              
REMARK 620 3 GLU A 841   OE2 101.6  93.2                                        
REMARK 620 4 ASN A 843   OD1  91.5 170.8  79.9                                  
REMARK 620 5 HOH A1308   O   107.2  90.6 150.4  92.5                            
REMARK 620 6 GLU A 841   OE1 156.7  82.0  55.6  89.0  96.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1901  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP C1900   O3G                                                    
REMARK 620 2 ANP C1900   O2B  86.7                                              
REMARK 620 3 GLU C 299   OE1 152.2  89.9                                        
REMARK 620 4 ASN C 301   OD1  87.3 174.0  94.9                                  
REMARK 620 5 HOH C4295   O   103.7  89.2 103.8  93.0                            
REMARK 620 6 GLU C 299   OE2  96.1  96.0  56.8  83.9 159.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1912  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP C1910   O3G                                                    
REMARK 620 2 ANP C1910   O2B  94.8                                              
REMARK 620 3 GLU C 841   OE1 141.4  74.7                                        
REMARK 620 4 GLU C 841   OE2  98.6 112.6  55.1                                  
REMARK 620 5 ASN C 843   OD1  83.9 177.4 104.9  65.4                            
REMARK 620 6 HOH C4209   O    99.2  92.7 118.0 147.5  89.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1911  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP C1910   O2A                                                    
REMARK 620 2 GLN C 829   OE1 100.7                                              
REMARK 620 3 HOH C4420   O    74.5  79.4                                        
REMARK 620 4 ANP C1910   O2G 136.1 118.7  93.2                                  
REMARK 620 5 ANP C1910   N3B  76.6 169.8  90.4  61.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C3985   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C4027   O                                                      
REMARK 620 2 THR C 143   O   118.7                                              
REMARK 620 3 HOH C4313   O   125.0 104.8                                        
REMARK 620 4 THR C 143   OG1  66.1  67.4 168.9                                  
REMARK 620 5 HOH C4461   O    66.4 136.9 103.5  79.1                            
REMARK 620 6 ALA C 144   O    60.2  71.7 109.7  76.1 126.4                      
REMARK 620 7 HOH C4026   O   133.5  68.4  91.7  78.1  79.0 138.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C3986  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 150   ND1                                                    
REMARK 620 2 GLU C 154   OE1 101.8                                              
REMARK 620 3 GLU C 154   OE2 159.8  59.6                                        
REMARK 620 4 HOH C4314   O   108.6 125.3  90.0                                  
REMARK 620 5 HIS A 680   NE2 100.5  97.4  76.0 119.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E2901  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E2900   O3G                                                    
REMARK 620 2 ANP E2900   O2B  85.6                                              
REMARK 620 3 GLU E 299   OE1 158.9  85.3                                        
REMARK 620 4 GLU E 299   OE2 100.4  86.1  59.9                                  
REMARK 620 5 ASN E 301   OD1  90.1 169.2 101.9 104.4                            
REMARK 620 6 HOH E3292   O   107.9  83.3  89.9 148.8  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E2912  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E2910   O3G                                                    
REMARK 620 2 ANP E2910   O2B 101.1                                              
REMARK 620 3 GLU E 841   OE2 104.7  99.0                                        
REMARK 620 4 HOH E3207   O   100.9  93.6 148.5                                  
REMARK 620 5 ASN E 843   OD1  95.8 154.9  58.4 101.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E2911  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E2910   N3B                                                    
REMARK 620 2 ANP E2910   O2A  86.2                                              
REMARK 620 3 GLN E 829   OE1 167.3 105.7                                        
REMARK 620 4 ANP E2910   O2G  63.0 147.1 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G3901  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP G3900   O3G                                                    
REMARK 620 2 ANP G3900   O2B  93.0                                              
REMARK 620 3 GLU G 299   OE1 163.7  88.0                                        
REMARK 620 4 GLU G 299   OE2 106.1  91.9  57.6                                  
REMARK 620 5 HOH G4292   O    94.1  75.7 101.9 156.9                            
REMARK 620 6 ASN G 301   OD1  91.1 166.7  91.7  99.2  91.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G3912  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP G3910   O3G                                                    
REMARK 620 2 ANP G3910   O2B  95.6                                              
REMARK 620 3 GLU G 841   OE2  97.9  87.1                                        
REMARK 620 4 GLU G 841   OE1 145.6  87.7  48.0                                  
REMARK 620 5 ASN G 843   OD1  89.2 164.7  77.9  80.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G3911  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP G3910   N3B                                                    
REMARK 620 2 ANP G3910   O2A  98.3                                              
REMARK 620 3 GLN G 829   OE1 164.6  93.1                                        
REMARK 620 4 HOH G4408   O   103.8 110.4  81.5                                  
REMARK 620 5 GLU G 841   OE2  95.9  76.3  76.8 157.7                            
REMARK 620 6 ANP G3910   O2G  61.5 153.0 104.2  92.7  87.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1075   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 215   OE1                                                    
REMARK 620 2 ILE A 242   O    89.9                                              
REMARK 620 3 ASP A 238   O   119.7 134.4                                        
REMARK 620 4 ALA A 239   O    86.4  84.2  65.8                                  
REMARK 620 5 SER A 247   OG  142.8  67.4  96.6 118.3                            
REMARK 620 6 ASN A 236   OD1  86.8 123.1  94.3 151.8  82.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1079   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 783   O                                                      
REMARK 620 2 GLN A 784   O    66.9                                              
REMARK 620 3 VAL A 787   O   140.7  85.3                                        
REMARK 620 4 SER A 792   OG   98.5 124.6  74.2                                  
REMARK 620 5 GLU A 761   OE1 128.7  90.6  76.1 130.7                            
REMARK 620 6 HIS A 781   ND1  93.2 144.5 123.9  85.9  79.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 984   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 112   O                                                      
REMARK 620 2 HOH B1010   O    84.7                                              
REMARK 620 3 HIS B  16   O    95.3 122.2                                        
REMARK 620 4 HOH B1009   O   165.5  81.1  89.5                                  
REMARK 620 5 HOH B1063   O    88.3 143.5  94.2 105.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1903   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 215   OE1                                                    
REMARK 620 2 ASP C 238   O   120.9                                              
REMARK 620 3 ALA C 239   O    90.2  67.9                                        
REMARK 620 4 ASN C 236   OD1  83.1  91.2 150.7                                  
REMARK 620 5 ILE C 242   O    84.9 146.5  93.1 114.5                            
REMARK 620 6 SER C 247   OG  134.6  97.1 129.3  71.4  73.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1904   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA C 126   O                                                      
REMARK 620 2 GLU C 127   OE2  91.1                                              
REMARK 620 3 GLU C 299   OE1 140.1 128.5                                        
REMARK 620 4 MET C 300   O    85.7  98.7  90.8                                  
REMARK 620 5 HOH C4100   O    79.0  86.7  97.7 163.9                            
REMARK 620 6 HOH C4101   O    58.4 145.8  83.9  66.4 100.8                      
REMARK 620 7 HOH C4295   O   143.4  66.0  67.0 124.2  71.8 148.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C1913   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C 792   OG                                                     
REMARK 620 2 HIS C 781   ND1  87.8                                              
REMARK 620 3 VAL C 787   O    68.5 123.7                                        
REMARK 620 4 GLU C 761   OE1 125.3  68.4  84.7                                  
REMARK 620 5 GLU C 783   O    99.0  94.2 138.1 129.9                            
REMARK 620 6 GLN C 784   O   123.4 144.1  87.2 100.5  66.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D3984   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D1529   O                                                      
REMARK 620 2 HOH C4183   O   161.8                                              
REMARK 620 3 ASP D 112   O    88.4  85.9                                        
REMARK 620 4 HIS D  16   O    83.1 113.8  86.7                                  
REMARK 620 5 HOH D1219   O   109.5  82.6 152.3  75.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E2903   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 238   O                                                      
REMARK 620 2 ALA E 239   O    65.1                                              
REMARK 620 3 GLU E 215   OE1 121.2  91.4                                        
REMARK 620 4 ASN E 236   OD1  93.0 147.9  79.9                                  
REMARK 620 5 ILE E 242   O   140.8  89.7  87.1 120.3                            
REMARK 620 6 SER E 247   OG   92.3 121.4 141.8  80.5  75.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E2904   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 299   OE1                                                    
REMARK 620 2 HOH E3102   O    82.4                                              
REMARK 620 3 ALA E 126   O   131.8  73.9                                        
REMARK 620 4 HOH E3103   O    78.7  83.1  57.5                                  
REMARK 620 5 MET E 300   O    96.7 157.9  91.0  75.1                            
REMARK 620 6 ASN E 301   OD1  66.6 123.9 158.9 130.1  74.7                      
REMARK 620 7 HOH E3292   O    69.1  61.4 127.8 134.0 138.9  64.2                
REMARK 620 8 GLU E 127   OE2 133.8  96.4  90.8 147.3  99.9  76.8  70.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E2913   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 761   OE1                                                    
REMARK 620 2 GLN E 784   O    87.0                                              
REMARK 620 3 VAL E 787   O    72.5  86.2                                        
REMARK 620 4 GLU E 783   O   129.8  66.0 140.2                                  
REMARK 620 5 HIS E 781   ND1  90.6 151.9 119.7  95.0                            
REMARK 620 6 SER E 792   OG  129.5 118.7  67.4 100.7  83.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E2983   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  84   O                                                      
REMARK 620 2 GLY E 112   O    71.3                                              
REMARK 620 3 THR E 114   OG1  74.2 100.0                                        
REMARK 620 4 HOH E3451   O    97.6  74.7 171.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G3903   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 238   O                                                      
REMARK 620 2 SER G 247   OG   95.4                                              
REMARK 620 3 GLU G 215   OE1 116.6 141.3                                        
REMARK 620 4 ALA G 239   O    66.4 122.7  91.4                                  
REMARK 620 5 ASN G 236   OD1  86.6  80.3  80.6 144.7                            
REMARK 620 6 ILE G 242   O   142.9  70.7  92.3  91.8 122.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G3904   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN G 301   OD1                                                    
REMARK 620 2 HOH G4292   O    62.1                                              
REMARK 620 3 ALA G 126   O   146.6 135.5                                        
REMARK 620 4 HOH G4105   O   127.9 145.0  58.6                                  
REMARK 620 5 MET G 300   O    67.8 129.4  85.9  75.2                            
REMARK 620 6 GLU G 127   OE2  66.8  59.8  96.4 153.0  94.3                      
REMARK 620 7 GLU G 299   OE1  64.5  72.0 140.7  83.2  93.5 122.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G3913   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER G 792   OG                                                     
REMARK 620 2 GLN G 784   O   127.1                                              
REMARK 620 3 GLU G 761   OE1 124.0  97.4                                        
REMARK 620 4 VAL G 787   O    73.7  83.7  80.4                                  
REMARK 620 5 GLU G 783   O    97.3  69.6 132.7 138.4                            
REMARK 620 6 HIS G 781   ND1  80.5 148.7  72.8 122.2  94.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G3988   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH G4389   O                                                      
REMARK 620 2 CYS G 551   O   102.1                                              
REMARK 620 3 HOH G4390   O    81.0 167.8                                        
REMARK 620 4 HOH G4382   O   161.1  93.5  81.6                                  
REMARK 620 5 ASN G 554   OD1  73.7 101.8  67.5  92.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K H3987   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH H3529   O                                                      
REMARK 620 2 ASP H 112   O   102.6                                              
REMARK 620 3 HIS H  16   O    87.4  94.6                                        
REMARK 620 4 HOH G4184   O    75.8 122.0 142.0                                  
REMARK 620 5 HOH H3220   O    60.9 162.0  78.2  63.8                            
REMARK 620 6 HOH G4183   O   148.9  82.2 123.1  75.7 115.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1074                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K 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 MN A 1077                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1078                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1079                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL 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 CL B 982                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1082                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 984                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 1913                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1980                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1981                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1982                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1983                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 3984                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3985                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 3986                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 2901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 2903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 2904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 2911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 2912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 2913                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 2980                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 2981                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 2983                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 3901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 3903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 3904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 3911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 3912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 3913                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 3980                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 3981                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 3982                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 3983                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 3987                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 3988                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 1083                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 1084                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 1085                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 1086                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 1900                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 1910                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 1920                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 1950                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 2900                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP E 2910                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 2920                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 2950                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP G 3900                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP G 3910                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 3920                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 3950                
DBREF  1BXR A    2  1073  UNP    P00968   CARB_ECOLI       1   1072             
DBREF  1BXR B    1   382  UNP    P0A6F1   CARA_ECOLI       1    382             
DBREF  1BXR C    2  1073  UNP    P00968   CARB_ECOLI       1   1072             
DBREF  1BXR D    1   382  UNP    P0A6F1   CARA_ECOLI       1    382             
DBREF  1BXR E    2  1073  UNP    P00968   CARB_ECOLI       1   1072             
DBREF  1BXR F    1   382  UNP    P0A6F1   CARA_ECOLI       1    382             
DBREF  1BXR G    2  1073  UNP    P00968   CARB_ECOLI       1   1072             
DBREF  1BXR H    1   382  UNP    P0A6F1   CARA_ECOLI       1    382             
SEQADV 1BXR GLN B  183  UNP  P0A6F1    GLU   183 CONFLICT                       
SEQADV 1BXR GLN D  183  UNP  P0A6F1    GLU   183 CONFLICT                       
SEQADV 1BXR GLN F  183  UNP  P0A6F1    GLU   183 CONFLICT                       
SEQADV 1BXR GLN H  183  UNP  P0A6F1    GLU   183 CONFLICT                       
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  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 B  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 B  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 B  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 B  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 B  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 B  382  THR ASP ILE PRO VAL PHE GLY ILE 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  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 D  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 D  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 D  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 D  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 D  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 D  382  THR ASP ILE PRO VAL PHE GLY ILE 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  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 F  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 F  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 F  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 F  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 F  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 F  382  THR ASP ILE PRO VAL PHE GLY ILE 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  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 H  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 H  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 H  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 H  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 H  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 H  382  THR ASP ILE PRO VAL PHE GLY ILE 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      K  A1075       1                                                       
HET      K  A1076       1                                                       
HET     MN  A1077       1                                                       
HET     MN  A1078       1                                                       
HET      K  A1079       1                                                       
HET     CL  A1080       1                                                       
HET     CL  A1081       1                                                       
HET     CL  B 982       1                                                       
HET     CL  A1082       1                                                       
HET      K  B 984       1                                                       
HET     MN  C1901       1                                                       
HET      K  C1903       1                                                       
HET      K  C1904       1                                                       
HET     MN  C1911       1                                                       
HET     MN  C1912       1                                                       
HET      K  C1913       1                                                       
HET     CL  C1980       1                                                       
HET     CL  C1981       1                                                       
HET     CL  D1982       1                                                       
HET     CL  C1983       1                                                       
HET      K  D3984       1                                                       
HET      K  C3985       1                                                       
HET     MN  C3986       1                                                       
HET     MN  E2901       1                                                       
HET      K  E2903       1                                                       
HET      K  E2904       1                                                       
HET     MN  E2911       1                                                       
HET     MN  E2912       1                                                       
HET      K  E2913       1                                                       
HET     CL  E2980       1                                                       
HET     CL  E2981       1                                                       
HET      K  E2982       1                                                       
HET      K  E2983       1                                                       
HET     MN  G3901       1                                                       
HET      K  G3903       1                                                       
HET      K  G3904       1                                                       
HET     MN  G3911       1                                                       
HET     MN  G3912       1                                                       
HET      K  G3913       1                                                       
HET     CL  G3980       1                                                       
HET     CL  G3981       1                                                       
HET     CL  G3982       1                                                       
HET     CL  G3983       1                                                       
HET      K  H3987       1                                                       
HET      K  G3988       1                                                       
HET    ANP  A1083      31                                                       
HET    ANP  A1084      31                                                       
HET    ORN  A1085       9                                                       
HET    NET  A1086       9                                                       
HET    ANP  C1900      31                                                       
HET    ANP  C1910      31                                                       
HET    ORN  C1920       9                                                       
HET    NET  C1950       9                                                       
HET    ANP  E2900      31                                                       
HET    ANP  E2910      31                                                       
HET    ORN  E2920       9                                                       
HET    NET  E2950       9                                                       
HET    ANP  G3900      31                                                       
HET    ANP  G3910      31                                                       
HET    ORN  G3920       9                                                       
HET    NET  G3950       9                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM       K POTASSIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     ORN L-ORNITHINE                                                      
HETNAM     NET TETRAETHYLAMMONIUM ION                                           
FORMUL   9   MN    13(MN 2+)                                                    
FORMUL  10    K    19(K 1+)                                                     
FORMUL  15   CL    14(CL 1-)                                                    
FORMUL  55  ANP    8(C10 H17 N6 O12 P3)                                         
FORMUL  57  ORN    4(C5 H12 N2 O2)                                              
FORMUL  58  NET    4(C8 H20 N 1+)                                               
FORMUL  71  HOH   *3242(H2 O)                                                   
HELIX    1   1 GLU A   25  GLU A   40  1                                  16    
HELIX    2   2 TRP A   71  GLU A   81  1                                  11    
HELIX    3   3 GLY A   92  ARG A  104  1                                  13    
HELIX    4   4 VAL A  107  PHE A  111  1                                   5    
HELIX    5   5 ALA A  120  GLU A  127  1                                   8    
HELIX    6   6 ARG A  129  ILE A  139  1                                  11    
HELIX    7   7 MET A  152  VAL A  162  1                                  11    
HELIX    8   8 ARG A  185  LEU A  198  1                                  14    
HELIX    9   9 ASP A  258  ILE A  275  1                                  18    
HELIX   10  10 ARG A  306  THR A  315  1                                  10    
HELIX   11  11 ILE A  319  VAL A  328  1                                  10    
HELIX   12  12 ASP A  338  THR A  340  5                                   3    
HELIX   13  13 PHE A  364  LYS A  366  5                                   3    
HELIX   14  14 GLN A  391  GLY A  401  1                                  11    
HELIX   15  15 ALA A  420  LYS A  429  1                                  10    
HELIX   16  16 ARG A  435  ALA A  445  1                                  11    
HELIX   17  17 VAL A  449  THR A  456  1                                   8    
HELIX   18  18 ARG A  460  GLY A  483  1                                  24    
HELIX   19  19 ALA A  486  LYS A  495  1                                  10    
HELIX   20  20 ASP A  499  LEU A  505  1                                   7    
HELIX   21  21 GLU A  510  TYR A  520  1                                  11    
HELIX   22  22 ILE A  576  GLU A  591  1                                  16    
HELIX   23  23 LEU A  623  GLU A  633  1                                  11    
HELIX   24  24 GLN A  645  ALA A  656  1                                  12    
HELIX   25  25 PRO A  666  GLU A  673  1                                   8    
HELIX   26  26 ARG A  675  ARG A  684  1                                  10    
HELIX   27  27 ILE A  698  ILE A  708  1                                  11    
HELIX   28  28 GLU A  731  VAL A  744  1                                  14    
HELIX   29  29 SER A  789  ASP A  791  5                                   3    
HELIX   30  30 GLN A  803  LEU A  820  1                                  18    
HELIX   31  31 VAL A  850  THR A  857  1                                   8    
HELIX   32  32 LEU A  861  MET A  869  1                                   9    
HELIX   33  33 LEU A  874  GLN A  877  1                                   4    
HELIX   34  34 PHE A  897  LYS A  899  5                                   3    
HELIX   35  35 PHE A  924  GLY A  934  1                                  11    
HELIX   36  36 GLU A  951  LYS A  954  5                                   4    
HELIX   37  37 ARG A  956  GLN A  967  1                                  12    
HELIX   38  38 HIS A  975  ALA A  984  1                                  10    
HELIX   39  39 ILE A 1001  LYS A 1006  1                                   6    
HELIX   40  40 ARG A 1020  GLN A 1035  1                                  16    
HELIX   41  41 LEU A 1044  ASN A 1055  1                                  12    
HELIX   42  42 VAL A 1065  GLN A 1071  1                                   7    
HELIX   43  43 TYR B   39  LEU B   43  1                                   5    
HELIX   44  44 PRO B   46  TYR B   48  5                                   3    
HELIX   45  45 ASP B   67  ASP B   69  5                                   3    
HELIX   46  46 LEU B   98  ARG B  104  1                                   7    
HELIX   47  47 THR B  115  LYS B  125  1                                  11    
HELIX   48  48 ALA B  140  ARG B  148  1                                   9    
HELIX   49  49 ALA B  159  VAL B  162  1                                   4    
HELIX   50  50 GLU B  187  GLU B  189  5                                   3    
HELIX   51  51 ARG B  203  ARG B  212  1                                  10    
HELIX   52  52 ALA B  225  MET B  231  1                                   7    
HELIX   53  53 ASP B  249  PHE B  258  1                                  10    
HELIX   54  54 LEU B  270  LEU B  277  1                                   8    
HELIX   55  55 GLU B  318  THR B  320  5                                   3    
HELIX   56  56 ASP B  362  ARG B  378  5                                  17    
HELIX   57  57 CYS C   24  ARG C   38  5                                  15    
HELIX   58  58 ILE C   54  THR C   56  5                                   3    
HELIX   59  59 PRO C   58  MET C   60  5                                   3    
HELIX   60  60 TRP C   71  GLU C   81  1                                  11    
HELIX   61  61 GLY C   92  ARG C  104  1                                  13    
HELIX   62  62 GLU C  109  PHE C  111  5                                   3    
HELIX   63  63 ALA C  120  GLU C  127  1                                   8    
HELIX   64  64 ARG C  129  LYS C  138  1                                  10    
HELIX   65  65 MET C  152  VAL C  162  1                                  11    
HELIX   66  66 ARG C  185  LEU C  198  1                                  14    
HELIX   67  67 THR C  244  ASP C  246  5                                   3    
HELIX   68  68 ASP C  258  ILE C  275  1                                  18    
HELIX   69  69 ARG C  306  THR C  315  1                                  10    
HELIX   70  70 ILE C  319  VAL C  328  1                                  10    
HELIX   71  71 LEU C  332  GLU C  334  5                                   3    
HELIX   72  72 PHE C  364  LYS C  366  5                                   3    
HELIX   73  73 GLN C  391  GLY C  401  1                                  11    
HELIX   74  74 ALA C  420  LYS C  429  1                                  10    
HELIX   75  75 ARG C  435  ARG C  444  1                                  10    
HELIX   76  76 VAL C  449  THR C  456  1                                   8    
HELIX   77  77 ARG C  460  VAL C  479  1                                  20    
HELIX   78  78 ILE C  481  GLY C  483  5                                   3    
HELIX   79  79 ALA C  486  LYS C  495  1                                  10    
HELIX   80  80 ASP C  499  LEU C  505  1                                   7    
HELIX   81  81 GLU C  510  TYR C  520  1                                  11    
HELIX   82  82 ILE C  576  GLU C  591  1                                  16    
HELIX   83  83 VAL C  606  THR C  608  5                                   3    
HELIX   84  84 LEU C  623  GLU C  633  1                                  11    
HELIX   85  85 GLN C  645  ALA C  657  1                                  13    
HELIX   86  86 PRO C  666  GLU C  673  1                                   8    
HELIX   87  87 ARG C  675  LEU C  685  1                                  11    
HELIX   88  88 ILE C  698  ILE C  708  1                                  11    
HELIX   89  89 ALA C  732  SER C  743  1                                  12    
HELIX   90  90 SER C  789  ASP C  791  5                                   3    
HELIX   91  91 GLN C  803  LEU C  820  1                                  18    
HELIX   92  92 VAL C  850  THR C  857  1                                   8    
HELIX   93  93 LEU C  861  ALA C  870  1                                  10    
HELIX   94  94 LEU C  874  GLN C  877  1                                   4    
HELIX   95  95 PHE C  897  LYS C  899  5                                   3    
HELIX   96  96 PHE C  924  GLY C  934  1                                  11    
HELIX   97  97 GLU C  951  LYS C  954  5                                   4    
HELIX   98  98 ARG C  956  LYS C  966  1                                  11    
HELIX   99  99 HIS C  975  ALA C  984  1                                  10    
HELIX  100 100 ILE C 1001  ASN C 1007  1                                   7    
HELIX  101 101 ARG C 1020  GLN C 1035  1                                  16    
HELIX  102 102 LEU C 1044  ASN C 1055  1                                  12    
HELIX  103 103 VAL C 1065  ALA C 1070  1                                   6    
HELIX  104 104 TYR D   39  LEU D   43  1                                   5    
HELIX  105 105 PRO D   46  TYR D   48  5                                   3    
HELIX  106 106 ASP D   67  ASP D   69  5                                   3    
HELIX  107 107 LEU D   98  ARG D  104  1                                   7    
HELIX  108 108 THR D  115  LYS D  125  1                                  11    
HELIX  109 109 ALA D  140  ALA D  149  1                                  10    
HELIX  110 110 ALA D  159  VAL D  162  1                                   4    
HELIX  111 111 GLU D  187  GLU D  189  5                                   3    
HELIX  112 112 ARG D  203  ASP D  211  1                                   9    
HELIX  113 113 ALA D  225  MET D  231  1                                   7    
HELIX  114 114 ASP D  249  GLU D  260  1                                  12    
HELIX  115 115 CYS D  269  SER D  279  5                                  11    
HELIX  116 116 GLU D  318  THR D  320  5                                   3    
HELIX  117 117 HIS D  361  ARG D  378  5                                  18    
HELIX  118 118 CYS E   24  GLU E   39  5                                  16    
HELIX  119 119 ILE E   54  THR E   56  5                                   3    
HELIX  120 120 PRO E   58  MET E   60  5                                   3    
HELIX  121 121 TRP E   71  GLU E   81  1                                  11    
HELIX  122 122 GLY E   92  ARG E  104  1                                  13    
HELIX  123 123 VAL E  107  PHE E  111  1                                   5    
HELIX  124 124 ALA E  120  GLU E  127  1                                   8    
HELIX  125 125 ARG E  129  ILE E  139  1                                  11    
HELIX  126 126 MET E  152  VAL E  162  1                                  11    
HELIX  127 127 ARG E  185  LEU E  198  1                                  14    
HELIX  128 128 THR E  244  ASP E  246  5                                   3    
HELIX  129 129 ASP E  258  ILE E  275  1                                  18    
HELIX  130 130 ARG E  306  THR E  315  1                                  10    
HELIX  131 131 ILE E  319  VAL E  328  1                                  10    
HELIX  132 132 PHE E  364  LYS E  366  5                                   3    
HELIX  133 133 GLN E  391  GLY E  401  1                                  11    
HELIX  134 134 GLU E  419  LYS E  429  5                                  11    
HELIX  135 135 ARG E  435  ARG E  444  1                                  10    
HELIX  136 136 VAL E  449  THR E  456  1                                   8    
HELIX  137 137 ARG E  460  VAL E  479  1                                  20    
HELIX  138 138 ILE E  481  GLY E  483  5                                   3    
HELIX  139 139 ALA E  486  LYS E  493  1                                   8    
HELIX  140 140 ASP E  499  ALA E  506  1                                   8    
HELIX  141 141 GLU E  510  GLN E  519  1                                  10    
HELIX  142 142 ILE E  576  ASP E  592  1                                  17    
HELIX  143 143 TYR E  610  THR E  612  5                                   3    
HELIX  144 144 LEU E  623  GLU E  633  1                                  11    
HELIX  145 145 GLN E  645  ALA E  656  1                                  12    
HELIX  146 146 PRO E  666  GLU E  673  1                                   8    
HELIX  147 147 ARG E  675  LEU E  685  1                                  11    
HELIX  148 148 ILE E  698  ILE E  708  1                                  11    
HELIX  149 149 GLU E  731  ARG E  735  1                                   5    
HELIX  150 150 PHE E  738  SER E  743  1                                   6    
HELIX  151 151 SER E  789  ASP E  791  5                                   3    
HELIX  152 152 GLN E  803  LEU E  820  1                                  18    
HELIX  153 153 VAL E  850  THR E  857  1                                   8    
HELIX  154 154 LEU E  861  ALA E  870  1                                  10    
HELIX  155 155 LEU E  874  GLN E  877  1                                   4    
HELIX  156 156 PHE E  924  GLY E  934  1                                  11    
HELIX  157 157 GLY E  952  LYS E  954  5                                   3    
HELIX  158 158 VAL E  957  LYS E  966  1                                  10    
HELIX  159 159 HIS E  975  ALA E  984  1                                  10    
HELIX  160 160 ILE E 1001  LYS E 1006  1                                   6    
HELIX  161 161 ARG E 1020  GLN E 1035  1                                  16    
HELIX  162 162 LEU E 1044  ASN E 1055  1                                  12    
HELIX  163 163 VAL E 1065  GLN E 1071  1                                   7    
HELIX  164 164 TYR F   39  LEU F   43  1                                   5    
HELIX  165 165 PRO F   46  TYR F   48  5                                   3    
HELIX  166 166 ASP F   67  ASP F   69  5                                   3    
HELIX  167 167 LEU F   98  ARG F  104  1                                   7    
HELIX  168 168 THR F  115  LYS F  125  1                                  11    
HELIX  169 169 ALA F  140  ALA F  149  1                                  10    
HELIX  170 170 ALA F  159  VAL F  162  1                                   4    
HELIX  171 171 GLU F  187  GLU F  189  5                                   3    
HELIX  172 172 ARG F  203  ARG F  212  1                                  10    
HELIX  173 173 ALA F  225  MET F  231  1                                   7    
HELIX  174 174 ASP F  249  GLU F  260  1                                  12    
HELIX  175 175 LEU F  270  SER F  279  1                                  10    
HELIX  176 176 ALA F  364  ARG F  378  5                                  15    
HELIX  177 177 CYS G   24  GLU G   39  5                                  16    
HELIX  178 178 ILE G   54  THR G   56  5                                   3    
HELIX  179 179 PRO G   58  MET G   60  5                                   3    
HELIX  180 180 TRP G   71  GLU G   81  1                                  11    
HELIX  181 181 GLY G   92  GLN G  105  1                                  14    
HELIX  182 182 VAL G  107  GLU G  110  1                                   4    
HELIX  183 183 ALA G  120  GLU G  127  1                                   8    
HELIX  184 184 ARG G  129  LYS G  138  1                                  10    
HELIX  185 185 MET G  152  ASP G  161  1                                  10    
HELIX  186 186 ARG G  185  LEU G  198  1                                  14    
HELIX  187 187 THR G  244  ASP G  246  5                                   3    
HELIX  188 188 ASP G  258  ILE G  275  1                                  18    
HELIX  189 189 ARG G  306  THR G  315  1                                  10    
HELIX  190 190 ILE G  319  VAL G  328  1                                  10    
HELIX  191 191 ASP G  338  THR G  340  5                                   3    
HELIX  192 192 PHE G  364  LYS G  366  5                                   3    
HELIX  193 193 GLN G  391  LEU G  402  1                                  12    
HELIX  194 194 ALA G  420  LYS G  429  1                                  10    
HELIX  195 195 ARG G  435  ALA G  445  1                                  11    
HELIX  196 196 VAL G  449  THR G  456  1                                   8    
HELIX  197 197 ARG G  460  VAL G  479  1                                  20    
HELIX  198 198 ILE G  481  GLY G  483  5                                   3    
HELIX  199 199 ALA G  486  ARG G  494  1                                   9    
HELIX  200 200 ASP G  499  ALA G  506  1                                   8    
HELIX  201 201 GLU G  510  TYR G  520  1                                  11    
HELIX  202 202 ILE G  576  GLU G  591  1                                  16    
HELIX  203 203 LEU G  623  GLU G  633  1                                  11    
HELIX  204 204 GLN G  645  ALA G  657  1                                  13    
HELIX  205 205 PRO G  666  GLU G  673  1                                   8    
HELIX  206 206 ARG G  675  ARG G  684  1                                  10    
HELIX  207 207 ILE G  698  ILE G  708  1                                  11    
HELIX  208 208 GLU G  731  VAL G  744  1                                  14    
HELIX  209 209 SER G  789  ASP G  791  5                                   3    
HELIX  210 210 GLN G  803  LEU G  820  1                                  18    
HELIX  211 211 VAL G  850  THR G  857  1                                   8    
HELIX  212 212 LEU G  861  ALA G  870  1                                  10    
HELIX  213 213 LEU G  874  GLN G  877  1                                   4    
HELIX  214 214 PRO G  896  LYS G  899  5                                   4    
HELIX  215 215 PHE G  924  GLY G  934  1                                  11    
HELIX  216 216 GLU G  951  LYS G  954  5                                   4    
HELIX  217 217 VAL G  957  LYS G  966  1                                  10    
HELIX  218 218 HIS G  975  ALA G  984  1                                  10    
HELIX  219 219 ILE G 1001  LYS G 1006  1                                   6    
HELIX  220 220 ARG G 1020  GLU G 1024  1                                   5    
HELIX  221 221 ARG G 1027  GLN G 1035  1                                   9    
HELIX  222 222 LEU G 1044  ASN G 1055  1                                  12    
HELIX  223 223 VAL G 1065  ALA G 1070  1                                   6    
HELIX  224 224 TYR H   39  LEU H   43  1                                   5    
HELIX  225 225 PRO H   46  TYR H   48  5                                   3    
HELIX  226 226 ASP H   67  ASP H   69  5                                   3    
HELIX  227 227 LEU H   98  ARG H  104  1                                   7    
HELIX  228 228 THR H  115  LYS H  125  1                                  11    
HELIX  229 229 ALA H  140  ALA H  149  1                                  10    
HELIX  230 230 ALA H  159  VAL H  162  1                                   4    
HELIX  231 231 GLU H  187  GLU H  189  5                                   3    
HELIX  232 232 ARG H  203  ARG H  212  1                                  10    
HELIX  233 233 ALA H  225  MET H  231  1                                   7    
HELIX  234 234 ASP H  249  GLU H  260  1                                  12    
HELIX  235 235 LEU H  270  LEU H  277  1                                   8    
HELIX  236 236 GLU H  318  THR H  320  5                                   3    
HELIX  237 237 HIS H  361  ARG H  378  5                                  18    
SHEET    1   A 5 THR A 114  ILE A 116  0                                        
SHEET    2   A 5 ALA A  85  LEU A  87  1  N  VAL A  86   O  THR A 114           
SHEET    3   A 5 SER A   9  LEU A  13  1  N  LEU A  11   O  ALA A  85           
SHEET    4   A 5 ARG A  43  VAL A  47  1  N  ARG A  43   O  ILE A  10           
SHEET    5   A 5 ALA A  63  TYR A  65  1  N  ALA A  63   O  LEU A  46           
SHEET    1   B 4 SER A 146  ALA A 149  0                                        
SHEET    2   B 4 LEU A 204  ASP A 207 -1  N  ILE A 206   O  GLY A 147           
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  N  ALA A 182   O  CYS A 166           
SHEET    1   C 4 CYS A 228  GLU A 235  0                                        
SHEET    2   C 4 LYS A 214  ARG A 222 -1  N  VAL A 221   O  ILE A 229           
SHEET    3   C 4 GLY A 280  ASN A 289 -1  N  VAL A 288   O  LYS A 214           
SHEET    4   C 4 ARG A 294  ASN A 301 -1  N  ASN A 301   O  ASN A 283           
SHEET    1   D 3 THR A 249  ALA A 251  0                                        
SHEET    2   D 3 VAL A 355  ARG A 361 -1  N  LYS A 358   O  THR A 249           
SHEET    3   D 3 GLY A 382  GLY A 388 -1  N  GLY A 388   O  VAL A 355           
SHEET    1   E 2 VAL A 525  ARG A 528  0                                        
SHEET    2   E 2 MET A 543  THR A 546 -1  N  THR A 546   O  VAL A 525           
SHEET    1   F 4 GLY A 637  ILE A 639  0                                        
SHEET    2   F 4 LYS A 561  LEU A 565  1  N  MET A 563   O  GLY A 637           
SHEET    3   F 4 GLU A 595  ASN A 600  1  N  GLU A 595   O  ILE A 562           
SHEET    4   F 4 ARG A 615  PHE A 618  1  N  ARG A 615   O  MET A 598           
SHEET    1   G 4 ASN A 692  VAL A 695  0                                        
SHEET    2   G 4 VAL A 750  HIS A 754 -1  N  LEU A 752   O  ALA A 693           
SHEET    3   G 4 LEU A 712  ARG A 715 -1  N  ARG A 715   O  LEU A 751           
SHEET    4   G 4 GLU A 726  VAL A 728 -1  N  VAL A 728   O  LEU A 712           
SHEET    1   H 4 VAL A 773  GLU A 780  0                                        
SHEET    2   H 4 VAL A 760  CYS A 768 -1  N  ILE A 767   O  LEU A 774           
SHEET    3   H 4 GLY A 824  LYS A 833 -1  N  VAL A 832   O  VAL A 760           
SHEET    4   H 4 GLU A 836  ASN A 843 -1  N  ASN A 843   O  ASN A 827           
SHEET    1   I 3 CYS A 794  LEU A 796  0                                        
SHEET    2   I 3 TYR A 888  LEU A 895 -1  N  LYS A 891   O  CYS A 794           
SHEET    3   I 3 SER A 913  GLY A 921 -1  N  GLY A 921   O  TYR A 888           
SHEET    1   J 4 GLU A 970  ALA A 973  0                                        
SHEET    2   J 4 ARG A 944  SER A 948  1  N  ALA A 945   O  GLU A 970           
SHEET    3   J 4 TYR A1012  ASN A1015  1  N  TYR A1012   O  LEU A 946           
SHEET    4   J 4 HIS A1039  ASP A1041  1  N  HIS A1039   O  ILE A1013           
SHEET    1   K 6 GLN B  14  ARG B  18  0                                        
SHEET    2   K 6 SER B   4  LEU B   9 -1  N  LEU B   7   O  PHE B  15           
SHEET    3   K 6 GLN B 128  ALA B 134 -1  N  ILE B 133   O  LEU B   6           
SHEET    4   K 6 GLY B  24  ASN B  33 -1  N  VAL B  30   O  GLN B 128           
SHEET    5   K 6 GLN B  51  LEU B  55  1  N  ILE B  52   O  GLU B  29           
SHEET    6   K 6 GLY B  79  VAL B  81  1  N  GLY B  79   O  VAL B  53           
SHEET    1   L10 TYR B 168  TRP B 170  0                                        
SHEET    2   L10 CYS B 214  PRO B 220 -1  N  ILE B 218   O  TYR B 168           
SHEET    3   L10 PHE B 192  ASP B 198  1  N  PHE B 192   O  ARG B 215           
SHEET    4   L10 GLY B 235  LEU B 238  1  N  GLY B 235   O  VAL B 195           
SHEET    5   L10 VAL B 265  ILE B 268  1  N  PHE B 266   O  ILE B 236           
SHEET    6   L10 ALA B 347  PHE B 350  1  N  PHE B 348   O  VAL B 265           
SHEET    7   L10 GLY B 339  ARG B 342 -1  N  ILE B 340   O  SER B 349           
SHEET    8   L10 LEU B 325  SER B 331 -1  N  HIS B 329   O  GLY B 339           
SHEET    9   L10 HIS B 295  ASP B 299 -1  N  LYS B 298   O  LYS B 330           
SHEET   10   L10 VAL B 304  THR B 308 -1  N  THR B 308   O  HIS B 295           
SHEET    1   M 2 LYS B 282  LYS B 285  0                                        
SHEET    2   M 2 PHE B 314  ASP B 317 -1  N  ASP B 317   O  LYS B 282           
SHEET    1   N 2 HIS B 290  GLY B 292  0                                        
SHEET    2   N 2 GLN B 310  HIS B 312 -1  N  HIS B 312   O  HIS B 290           
SHEET    1   O 5 THR C 114  ILE C 116  0                                        
SHEET    2   O 5 ALA C  85  LEU C  87  1  N  VAL C  86   O  THR C 114           
SHEET    3   O 5 SER C   9  LEU C  13  1  N  LEU C  11   O  ALA C  85           
SHEET    4   O 5 ARG C  43  VAL C  47  1  N  ARG C  43   O  ILE C  10           
SHEET    5   O 5 ALA C  63  TYR C  65  1  N  ALA C  63   O  LEU C  46           
SHEET    1   P 4 SER C 146  ALA C 149  0                                        
SHEET    2   P 4 LEU C 204  GLU C 208 -1  N  ILE C 206   O  GLY C 147           
SHEET    3   P 4 CYS C 166  PRO C 170 -1  N  ARG C 169   O  LEU C 205           
SHEET    4   P 4 GLY C 180  ALA C 182 -1  N  ALA C 182   O  CYS C 166           
SHEET    1   Q 4 CYS C 228  GLU C 235  0                                        
SHEET    2   Q 4 LYS C 214  ARG C 222 -1  N  VAL C 221   O  ILE C 229           
SHEET    3   Q 4 GLY C 280  VAL C 288 -1  N  VAL C 288   O  LYS C 214           
SHEET    4   Q 4 LEU C 295  ASN C 301 -1  N  ASN C 301   O  ASN C 283           
SHEET    1   R 3 THR C 249  ALA C 251  0                                        
SHEET    2   R 3 VAL C 355  ARG C 361 -1  N  LYS C 358   O  THR C 249           
SHEET    3   R 3 GLY C 382  GLY C 388 -1  N  GLY C 388   O  VAL C 355           
SHEET    1   S 2 VAL C 525  ARG C 528  0                                        
SHEET    2   S 2 MET C 543  THR C 546 -1  N  THR C 546   O  VAL C 525           
SHEET    1   T 4 GLY C 637  ILE C 639  0                                        
SHEET    2   T 4 LYS C 561  LEU C 565  1  N  MET C 563   O  GLY C 637           
SHEET    3   T 4 GLU C 595  VAL C 599  1  N  GLU C 595   O  ILE C 562           
SHEET    4   T 4 ARG C 615  TYR C 617  1  N  ARG C 615   O  MET C 598           
SHEET    1   U 4 ALA C 693  VAL C 695  0                                        
SHEET    2   U 4 VAL C 750  HIS C 754 -1  N  LEU C 752   O  ALA C 693           
SHEET    3   U 4 LEU C 712  ARG C 715 -1  N  ARG C 715   O  LEU C 751           
SHEET    4   U 4 GLU C 726  VAL C 728 -1  N  VAL C 728   O  LEU C 712           
SHEET    1   V 4 VAL C 773  GLU C 780  0                                        
SHEET    2   V 4 VAL C 760  CYS C 768 -1  N  ILE C 767   O  LEU C 774           
SHEET    3   V 4 GLY C 824  LYS C 833 -1  N  VAL C 832   O  VAL C 760           
SHEET    4   V 4 GLU C 836  ASN C 843 -1  N  ASN C 843   O  ASN C 827           
SHEET    1   W 3 CYS C 794  LEU C 796  0                                        
SHEET    2   W 3 TYR C 888  LEU C 895 -1  N  LYS C 891   O  CYS C 794           
SHEET    3   W 3 SER C 913  GLY C 921 -1  N  GLY C 921   O  TYR C 888           
SHEET    1   X 5 HIS C1039  ASP C1041  0                                        
SHEET    2   X 5 TYR C1012  ASN C1015  1  N  ILE C1013   O  HIS C1039           
SHEET    3   X 5 GLY C 943  SER C 948  1  N  LEU C 946   O  TYR C1012           
SHEET    4   X 5 PHE C 969  THR C 974  1  N  GLU C 970   O  GLY C 943           
SHEET    5   X 5 ARG C 989  VAL C 991  1  N  ARG C 989   O  ALA C 973           
SHEET    1   Y 7 GLN D  14  ARG D  18  0                                        
SHEET    2   Y 7 SER D   4  LEU D   9 -1  N  LEU D   7   O  PHE D  15           
SHEET    3   Y 7 GLN D 128  ALA D 134 -1  N  ILE D 133   O  LEU D   6           
SHEET    4   Y 7 GLY D  24  ASN D  33 -1  N  VAL D  30   O  GLN D 128           
SHEET    5   Y 7 GLN D  51  LEU D  55  1  N  ILE D  52   O  GLU D  29           
SHEET    6   Y 7 GLY D  79  VAL D  81  1  N  GLY D  79   O  VAL D  53           
SHEET    7   Y 7 VAL D 108  ILE D 110  1  N  VAL D 108   O  LEU D  80           
SHEET    1   Z10 TYR D 168  TRP D 170  0                                        
SHEET    2   Z10 CYS D 214  VAL D 219 -1  N  ILE D 218   O  TYR D 168           
SHEET    3   Z10 PHE D 192  TYR D 197  1  N  PHE D 192   O  ARG D 215           
SHEET    4   Z10 GLY D 235  LEU D 238  1  N  GLY D 235   O  VAL D 195           
SHEET    5   Z10 PRO D 264  ILE D 268  1  N  PRO D 264   O  ILE D 236           
SHEET    6   Z10 ALA D 347  PHE D 350  1  N  PHE D 348   O  VAL D 265           
SHEET    7   Z10 GLY D 339  ARG D 342 -1  N  ILE D 340   O  SER D 349           
SHEET    8   Z10 LEU D 325  SER D 331 -1  N  HIS D 329   O  GLY D 339           
SHEET    9   Z10 HIS D 295  ASP D 299 -1  N  LYS D 298   O  LYS D 330           
SHEET   10   Z10 VAL D 304  THR D 308 -1  N  THR D 308   O  HIS D 295           
SHEET    1  AA 2 LYS D 282  LYS D 285  0                                        
SHEET    2  AA 2 PHE D 314  ASP D 317 -1  N  ASP D 317   O  LYS D 282           
SHEET    1  AB 2 HIS D 290  GLY D 292  0                                        
SHEET    2  AB 2 GLN D 310  HIS D 312 -1  N  HIS D 312   O  HIS D 290           
SHEET    1  AC 5 THR E 114  ILE E 116  0                                        
SHEET    2  AC 5 ALA E  85  LEU E  87  1  N  VAL E  86   O  THR E 114           
SHEET    3  AC 5 SER E   9  LEU E  13  1  N  LEU E  11   O  ALA E  85           
SHEET    4  AC 5 ARG E  43  VAL E  47  1  N  ARG E  43   O  ILE E  10           
SHEET    5  AC 5 ALA E  63  TYR E  65  1  N  ALA E  63   O  LEU E  46           
SHEET    1  AD 4 SER E 146  ALA E 149  0                                        
SHEET    2  AD 4 LEU E 204  GLU E 208 -1  N  ILE E 206   O  GLY E 147           
SHEET    3  AD 4 CYS E 166  PRO E 170 -1  N  ARG E 169   O  LEU E 205           
SHEET    4  AD 4 GLY E 180  ALA E 182 -1  N  ALA E 182   O  CYS E 166           
SHEET    1  AE 4 CYS E 228  GLU E 235  0                                        
SHEET    2  AE 4 LYS E 214  ARG E 222 -1  N  VAL E 221   O  ILE E 229           
SHEET    3  AE 4 GLY E 280  VAL E 288 -1  N  VAL E 288   O  LYS E 214           
SHEET    4  AE 4 LEU E 295  ASN E 301 -1  N  ASN E 301   O  ASN E 283           
SHEET    1  AF 3 THR E 249  ALA E 251  0                                        
SHEET    2  AF 3 VAL E 355  ARG E 361 -1  N  LYS E 358   O  THR E 249           
SHEET    3  AF 3 GLY E 382  GLY E 388 -1  N  GLY E 388   O  VAL E 355           
SHEET    1  AG 2 VAL E 525  ARG E 528  0                                        
SHEET    2  AG 2 MET E 543  THR E 546 -1  N  THR E 546   O  VAL E 525           
SHEET    1  AH 4 GLY E 637  ILE E 639  0                                        
SHEET    2  AH 4 LYS E 561  LEU E 565  1  N  MET E 563   O  GLY E 637           
SHEET    3  AH 4 GLU E 595  ASN E 600  1  N  GLU E 595   O  ILE E 562           
SHEET    4  AH 4 ARG E 615  PHE E 618  1  N  ARG E 615   O  MET E 598           
SHEET    1  AI 4 ASN E 692  VAL E 695  0                                        
SHEET    2  AI 4 VAL E 750  HIS E 754 -1  N  LEU E 752   O  ALA E 693           
SHEET    3  AI 4 LEU E 712  ARG E 715 -1  N  ARG E 715   O  LEU E 751           
SHEET    4  AI 4 GLU E 726  VAL E 728 -1  N  VAL E 728   O  LEU E 712           
SHEET    1  AJ 4 VAL E 773  GLU E 780  0                                        
SHEET    2  AJ 4 VAL E 760  CYS E 768 -1  N  ILE E 767   O  LEU E 774           
SHEET    3  AJ 4 GLY E 824  VAL E 832 -1  N  VAL E 832   O  VAL E 760           
SHEET    4  AJ 4 VAL E 837  ASN E 843 -1  N  ASN E 843   O  ASN E 827           
SHEET    1  AK 3 CYS E 794  LEU E 796  0                                        
SHEET    2  AK 3 TYR E 888  LEU E 895 -1  N  LYS E 891   O  CYS E 794           
SHEET    3  AK 3 SER E 913  GLY E 921 -1  N  GLY E 921   O  TYR E 888           
SHEET    1  AL 5 HIS E1039  ASP E1041  0                                        
SHEET    2  AL 5 TYR E1012  ASN E1015  1  N  ILE E1013   O  HIS E1039           
SHEET    3  AL 5 GLY E 943  SER E 948  1  N  LEU E 946   O  TYR E1012           
SHEET    4  AL 5 PHE E 969  THR E 974  1  N  GLU E 970   O  GLY E 943           
SHEET    5  AL 5 ARG E 989  VAL E 991  1  N  ARG E 989   O  ALA E 973           
SHEET    1  AM 7 GLN F  14  ARG F  18  0                                        
SHEET    2  AM 7 SER F   4  LEU F   9 -1  N  LEU F   7   O  PHE F  15           
SHEET    3  AM 7 GLN F 128  ALA F 134 -1  N  ILE F 133   O  LEU F   6           
SHEET    4  AM 7 GLY F  24  ASN F  33 -1  N  VAL F  30   O  GLN F 128           
SHEET    5  AM 7 GLN F  51  LEU F  55  1  N  ILE F  52   O  GLU F  29           
SHEET    6  AM 7 GLY F  79  VAL F  81  1  N  GLY F  79   O  VAL F  53           
SHEET    7  AM 7 VAL F 108  ILE F 110  1  N  VAL F 108   O  LEU F  80           
SHEET    1  AN10 TYR F 168  TRP F 170  0                                        
SHEET    2  AN10 CYS F 214  PRO F 220 -1  N  ILE F 218   O  TYR F 168           
SHEET    3  AN10 PHE F 192  ASP F 198  1  N  PHE F 192   O  ARG F 215           
SHEET    4  AN10 GLY F 235  LEU F 238  1  N  GLY F 235   O  VAL F 195           
SHEET    5  AN10 VAL F 265  ILE F 268  1  N  PHE F 266   O  ILE F 236           
SHEET    6  AN10 ALA F 347  PHE F 350  1  N  PHE F 348   O  VAL F 265           
SHEET    7  AN10 GLY F 339  ARG F 342 -1  N  ILE F 340   O  SER F 349           
SHEET    8  AN10 LEU F 325  SER F 331 -1  N  HIS F 329   O  GLY F 339           
SHEET    9  AN10 HIS F 295  ASP F 299 -1  N  LYS F 298   O  LYS F 330           
SHEET   10  AN10 VAL F 304  THR F 308 -1  N  THR F 308   O  HIS F 295           
SHEET    1  AO 2 LYS F 282  LYS F 285  0                                        
SHEET    2  AO 2 PHE F 314  ASP F 317 -1  N  ASP F 317   O  LYS F 282           
SHEET    1  AP 2 HIS F 290  GLY F 292  0                                        
SHEET    2  AP 2 GLN F 310  HIS F 312 -1  N  HIS F 312   O  HIS F 290           
SHEET    1  AQ 5 THR G 114  ILE G 116  0                                        
SHEET    2  AQ 5 ALA G  85  LEU G  87  1  N  VAL G  86   O  THR G 114           
SHEET    3  AQ 5 SER G   9  LEU G  13  1  N  LEU G  11   O  ALA G  85           
SHEET    4  AQ 5 ARG G  43  VAL G  47  1  N  ARG G  43   O  ILE G  10           
SHEET    5  AQ 5 ALA G  63  TYR G  65  1  N  ALA G  63   O  LEU G  46           
SHEET    1  AR 4 SER G 146  ALA G 149  0                                        
SHEET    2  AR 4 LEU G 204  GLU G 208 -1  N  ILE G 206   O  GLY G 147           
SHEET    3  AR 4 CYS G 166  PRO G 170 -1  N  ARG G 169   O  LEU G 205           
SHEET    4  AR 4 GLY G 180  ALA G 182 -1  N  ALA G 182   O  CYS G 166           
SHEET    1  AS 4 CYS G 228  GLU G 235  0                                        
SHEET    2  AS 4 LYS G 214  ARG G 222 -1  N  VAL G 221   O  ILE G 229           
SHEET    3  AS 4 GLY G 280  ASN G 289 -1  N  VAL G 288   O  LYS G 214           
SHEET    4  AS 4 ARG G 294  ASN G 301 -1  N  ASN G 301   O  ASN G 283           
SHEET    1  AT 3 THR G 249  ALA G 251  0                                        
SHEET    2  AT 3 VAL G 355  ARG G 361 -1  N  LYS G 358   O  THR G 249           
SHEET    3  AT 3 GLY G 382  GLY G 388 -1  N  GLY G 388   O  VAL G 355           
SHEET    1  AU 6 VAL G 525  ARG G 528  0                                        
SHEET    2  AU 6 ALA G 541  THR G 546 -1  N  THR G 546   O  VAL G 525           
SHEET    3  AU 6 ARG G 615  PHE G 618  1  N  LEU G 616   O  ALA G 541           
SHEET    4  AU 6 GLU G 595  ASN G 600  1  N  MET G 598   O  ARG G 615           
SHEET    5  AU 6 LYS G 561  LEU G 565  1  N  ILE G 562   O  GLU G 595           
SHEET    6  AU 6 GLY G 637  ILE G 639  1  N  GLY G 637   O  MET G 563           
SHEET    1  AV 4 ASN G 692  VAL G 695  0                                        
SHEET    2  AV 4 VAL G 750  HIS G 754 -1  N  LEU G 752   O  ALA G 693           
SHEET    3  AV 4 LEU G 712  ARG G 715 -1  N  ARG G 715   O  LEU G 751           
SHEET    4  AV 4 GLU G 726  VAL G 728 -1  N  VAL G 728   O  LEU G 712           
SHEET    1  AW 4 VAL G 773  GLU G 780  0                                        
SHEET    2  AW 4 VAL G 760  CYS G 768 -1  N  ILE G 767   O  LEU G 774           
SHEET    3  AW 4 GLY G 824  LYS G 833 -1  N  VAL G 832   O  VAL G 760           
SHEET    4  AW 4 GLU G 836  ASN G 843 -1  N  ASN G 843   O  ASN G 827           
SHEET    1  AX 3 CYS G 794  LEU G 796  0                                        
SHEET    2  AX 3 TYR G 888  LEU G 895 -1  N  LYS G 891   O  CYS G 794           
SHEET    3  AX 3 SER G 913  GLY G 921 -1  N  GLY G 921   O  TYR G 888           
SHEET    1  AY 5 HIS G1039  ASP G1041  0                                        
SHEET    2  AY 5 TYR G1012  ASN G1015  1  N  ILE G1013   O  HIS G1039           
SHEET    3  AY 5 GLY G 943  SER G 948  1  N  LEU G 946   O  TYR G1012           
SHEET    4  AY 5 PHE G 969  THR G 974  1  N  GLU G 970   O  GLY G 943           
SHEET    5  AY 5 ARG G 989  VAL G 991  1  N  ARG G 989   O  ALA G 973           
SHEET    1  AZ 7 GLN H  14  ARG H  18  0                                        
SHEET    2  AZ 7 SER H   4  LEU H   9 -1  N  LEU H   7   O  PHE H  15           
SHEET    3  AZ 7 GLN H 128  ALA H 134 -1  N  ILE H 133   O  LEU H   6           
SHEET    4  AZ 7 GLY H  24  ASN H  33 -1  N  VAL H  30   O  GLN H 128           
SHEET    5  AZ 7 GLN H  51  LEU H  55  1  N  ILE H  52   O  GLU H  29           
SHEET    6  AZ 7 GLY H  79  VAL H  81  1  N  GLY H  79   O  VAL H  53           
SHEET    7  AZ 7 VAL H 108  ILE H 110  1  N  VAL H 108   O  LEU H  80           
SHEET    1  BA10 TYR H 168  TRP H 170  0                                        
SHEET    2  BA10 CYS H 214  VAL H 219 -1  N  ILE H 218   O  TYR H 168           
SHEET    3  BA10 PHE H 192  TYR H 197  1  N  PHE H 192   O  ARG H 215           
SHEET    4  BA10 GLY H 235  LEU H 238  1  N  GLY H 235   O  VAL H 195           
SHEET    5  BA10 PRO H 264  ILE H 268  1  N  PRO H 264   O  ILE H 236           
SHEET    6  BA10 ALA H 347  PHE H 350  1  N  PHE H 348   O  VAL H 265           
SHEET    7  BA10 GLY H 339  ARG H 342 -1  N  ILE H 340   O  SER H 349           
SHEET    8  BA10 LEU H 325  SER H 331 -1  N  HIS H 329   O  GLY H 339           
SHEET    9  BA10 HIS H 295  ASP H 299 -1  N  LYS H 298   O  LYS H 330           
SHEET   10  BA10 VAL H 304  THR H 308 -1  N  THR H 308   O  HIS H 295           
SHEET    1  BB 2 THR H 283  LYS H 285  0                                        
SHEET    2  BB 2 PHE H 314  VAL H 316 -1  N  ALA H 315   O  VAL H 284           
SHEET    1  BC 2 HIS H 290  GLY H 292  0                                        
SHEET    2  BC 2 GLN H 310  HIS H 312 -1  N  HIS H 312   O  HIS H 290           
LINK        MN    MN A1074                 OE1 GLU A 299     1555   1555  2.38  
LINK        MN    MN A1074                 OE2 GLU A 299     1555   1555  2.34  
LINK        MN    MN A1074                 OD1 ASN A 301     1555   1555  2.06  
LINK        MN    MN A1074                 O   HOH A1393     1555   1555  2.38  
LINK         K     K A1076                 O   MET A 300     1555   1555  2.15  
LINK         O2G ANP A1084                MN    MN A1077     1555   1555  2.40  
LINK         O3G ANP A1084                MN    MN A1078     1555   1555  1.89  
LINK         O2B ANP A1084                MN    MN A1078     1555   1555  2.11  
LINK         O2A ANP A1084                MN    MN A1077     1555   1555  1.90  
LINK        MN    MN A1077                 OE1 GLN A 829     1555   1555  2.16  
LINK        MN    MN A1077                 O   HOH A1516     1555   1555  2.23  
LINK        MN    MN A1078                 OE2 GLU A 841     1555   1555  2.24  
LINK        MN    MN A1078                 OD1 ASN A 843     1555   1555  2.25  
LINK        MN    MN A1078                 O   HOH A1308     1555   1555  2.23  
LINK         O3G ANP C1900                MN    MN C1901     1555   1555  1.93  
LINK         O2B ANP C1900                MN    MN C1901     1555   1555  2.02  
LINK        MN    MN C1901                 OE1 GLU C 299     1555   1555  2.28  
LINK        MN    MN C1901                 OD1 ASN C 301     1555   1555  2.13  
LINK        MN    MN C1901                 O   HOH C4295     1555   1555  2.11  
LINK         O3G ANP C1910                MN    MN C1912     1555   1555  2.06  
LINK         O2B ANP C1910                MN    MN C1912     1555   1555  2.33  
LINK         O2A ANP C1910                MN    MN C1911     1555   1555  1.86  
LINK        MN    MN C1911                 OE1 GLN C 829     1555   1555  2.07  
LINK        MN    MN C1911                 O   HOH C4420     1555   1555  2.28  
LINK         K     K C3985                 O   HOH C4027     1555   1555  2.38  
LINK        MN    MN C3986                 ND1 HIS C 150     1555   1555  2.37  
LINK        MN    MN C3986                 OE1 GLU C 154     1555   1555  2.21  
LINK        MN    MN C3986                 OE2 GLU C 154     1555   1555  2.27  
LINK        MN    MN C3986                 O   HOH C4314     1555   1555  2.32  
LINK         O3G ANP E2900                MN    MN E2901     1555   1555  2.12  
LINK         O2B ANP E2900                MN    MN E2901     1555   1555  2.27  
LINK        MN    MN E2901                 OE1 GLU E 299     1555   1555  2.19  
LINK        MN    MN E2901                 OE2 GLU E 299     1555   1555  2.28  
LINK        MN    MN E2901                 OD1 ASN E 301     1555   1555  2.37  
LINK         O3G ANP E2910                MN    MN E2912     1555   1555  2.13  
LINK         O2B ANP E2910                MN    MN E2912     1555   1555  2.36  
LINK         N3B ANP E2910                MN    MN E2911     1555   1555  2.31  
LINK         O2A ANP E2910                MN    MN E2911     1555   1555  2.16  
LINK        MN    MN E2911                 OE1 GLN E 829     1555   1555  2.19  
LINK        MN    MN E2912                 OE2 GLU E 841     1555   1555  2.27  
LINK        MN    MN E2912                 O   HOH E3207     1555   1555  2.39  
LINK         O3G ANP G3900                MN    MN G3901     1555   1555  1.90  
LINK         O2B ANP G3900                MN    MN G3901     1555   1555  2.20  
LINK        MN    MN G3901                 OE1 GLU G 299     1555   1555  2.31  
LINK        MN    MN G3901                 OE2 GLU G 299     1555   1555  2.35  
LINK         O3G ANP G3910                MN    MN G3912     1555   1555  1.86  
LINK         O2B ANP G3910                MN    MN G3912     1555   1555  2.11  
LINK         N3B ANP G3910                MN    MN G3911     1555   1555  2.38  
LINK         O2A ANP G3910                MN    MN G3911     1555   1555  2.17  
LINK        MN    MN G3911                 OE1 GLN G 829     1555   1555  2.37  
LINK        MN    MN A1074                 O2B ANP A1083     1555   1555  2.40  
LINK        MN    MN A1074                 O3G ANP A1083     1555   1555  2.41  
LINK         K     K A1075                 OE1 GLU A 215     1555   1555  2.85  
LINK         K     K A1075                 O   ILE A 242     1555   1555  2.60  
LINK         K     K A1075                 O   ASP A 238     1555   1555  2.88  
LINK         K     K A1075                 O   ALA A 239     1555   1555  3.08  
LINK         K     K A1075                 OG  SER A 247     1555   1555  2.77  
LINK         K     K A1075                 OD1 ASN A 236     1555   1555  2.65  
LINK         K     K A1076                 O   ALA A 126     1555   1555  3.46  
LINK         K     K A1076                 OE2 GLU A 127     1555   1555  3.17  
LINK         K     K A1076                 OD1 ASN A 301     1555   1555  3.57  
LINK         K     K A1076                 O   HOH A1199     1555   1555  2.45  
LINK         K     K A1076                 O   HOH A1393     1555   1555  3.31  
LINK         K     K A1076                 OE1 GLU A 299     1555   1555  3.41  
LINK         K     K A1076                 O   HOH A1200     1555   1555  2.58  
LINK        MN    MN A1077                 OE2 GLU A 841     1555   1555  2.59  
LINK        MN    MN A1077                 N3B ANP A1084     1555   1555  2.41  
LINK        MN    MN A1078                 OE1 GLU A 841     1555   1555  2.48  
LINK         K     K A1079                 O   GLU A 783     1555   1555  2.92  
LINK         K     K A1079                 O   GLN A 784     1555   1555  2.91  
LINK         K     K A1079                 O   VAL A 787     1555   1555  2.53  
LINK         K     K A1079                 OG  SER A 792     1555   1555  2.60  
LINK         K     K A1079                 OE1 GLU A 761     1555   1555  2.67  
LINK         K     K A1079                 ND1 HIS A 781     1555   1555  2.79  
LINK         K     K B 984                 O   ASP B 112     1555   1555  2.60  
LINK         K     K B 984                 O   HOH B1010     1555   1555  3.06  
LINK         K     K B 984                 O   HIS B  16     1555   1555  2.78  
LINK         K     K B 984                 O   HOH B1009     1555   1555  2.94  
LINK         K     K B 984                 O   HOH B1063     1555   1555  2.81  
LINK        MN    MN C1901                 OE2 GLU C 299     1555   1555  2.46  
LINK         K     K C1903                 OE1 GLU C 215     1555   1555  2.58  
LINK         K     K C1903                 O   ASP C 238     1555   1555  2.55  
LINK         K     K C1903                 O   ALA C 239     1555   1555  2.70  
LINK         K     K C1903                 OD1 ASN C 236     1555   1555  2.98  
LINK         K     K C1903                 O   ILE C 242     1555   1555  2.60  
LINK         K     K C1903                 OG  SER C 247     1555   1555  2.73  
LINK         K     K C1904                 O   ALA C 126     1555   1555  3.06  
LINK         K     K C1904                 OE2 GLU C 127     1555   1555  2.83  
LINK         K     K C1904                 OE1 GLU C 299     1555   1555  2.87  
LINK         K     K C1904                 O   MET C 300     1555   1555  2.80  
LINK         K     K C1904                 O   HOH C4100     1555   1555  2.81  
LINK         K     K C1904                 O   HOH C4101     1555   1555  2.85  
LINK         K     K C1904                 O   HOH C4295     1555   1555  3.35  
LINK        MN    MN C1911                 O2G ANP C1910     1555   1555  2.55  
LINK        MN    MN C1911                 N3B ANP C1910     1555   1555  2.47  
LINK        MN    MN C1912                 OE1 GLU C 841     1555   1555  2.42  
LINK        MN    MN C1912                 OE2 GLU C 841     1555   1555  2.41  
LINK        MN    MN C1912                 OD1 ASN C 843     1555   1555  2.40  
LINK        MN    MN C1912                 O   HOH C4209     1555   1555  2.55  
LINK         K     K C1913                 OG  SER C 792     1555   1555  2.71  
LINK         K     K C1913                 ND1 HIS C 781     1555   1555  2.90  
LINK         K     K C1913                 O   VAL C 787     1555   1555  2.60  
LINK         K     K C1913                 OE1 GLU C 761     1555   1555  2.74  
LINK         K     K C1913                 O   GLU C 783     1555   1555  2.79  
LINK         K     K C1913                 O   GLN C 784     1555   1555  2.86  
LINK         K     K C3985                 O   THR C 143     1555   1555  2.94  
LINK         K     K C3985                 O   HOH C4313     1555   1555  3.26  
LINK         K     K C3985                 OG1 THR C 143     1555   1555  2.83  
LINK         K     K C3985                 O   HOH C4461     1555   1555  3.22  
LINK         K     K C3985                 O   ALA C 144     1555   1555  2.98  
LINK         K     K C3985                 O   HOH C4026     1555   1555  3.21  
LINK         K     K D3984                 O   HOH D1529     1555   1555  2.59  
LINK         K     K D3984                 O   HOH C4183     1555   1555  2.69  
LINK         K     K D3984                 O   ASP D 112     1555   1555  2.75  
LINK         K     K D3984                 O   HIS D  16     1555   1555  2.64  
LINK         K     K D3984                 O   HOH D1219     1555   1555  3.14  
LINK        MN    MN E2901                 O   HOH E3292     1555   1555  2.63  
LINK         K     K E2903                 O   ASP E 238     1555   1555  2.63  
LINK         K     K E2903                 O   ALA E 239     1555   1555  2.85  
LINK         K     K E2903                 OE1 GLU E 215     1555   1555  2.52  
LINK         K     K E2903                 OD1 ASN E 236     1555   1555  2.86  
LINK         K     K E2903                 O   ILE E 242     1555   1555  2.53  
LINK         K     K E2903                 OG  SER E 247     1555   1555  2.60  
LINK         K     K E2904                 OE1 GLU E 299     1555   1555  2.94  
LINK         K     K E2904                 O   HOH E3102     1555   1555  3.02  
LINK         K     K E2904                 O   ALA E 126     1555   1555  3.36  
LINK         K     K E2904                 O   HOH E3103     1555   1555  2.98  
LINK         K     K E2904                 O   MET E 300     1555   1555  2.55  
LINK         K     K E2904                 OD1 ASN E 301     1555   1555  3.47  
LINK         K     K E2904                 O   HOH E3292     1555   1555  3.09  
LINK         K     K E2904                 OE2 GLU E 127     1555   1555  2.56  
LINK        MN    MN E2911                 O2G ANP E2910     1555   1555  2.65  
LINK        MN    MN E2912                 OD1 ASN E 843     1555   1555  2.66  
LINK         K     K E2913                 OE1 GLU E 761     1555   1555  2.94  
LINK         K     K E2913                 O   GLN E 784     1555   1555  2.97  
LINK         K     K E2913                 O   VAL E 787     1555   1555  2.59  
LINK         K     K E2913                 O   GLU E 783     1555   1555  2.89  
LINK         K     K E2913                 ND1 HIS E 781     1555   1555  2.81  
LINK         K     K E2913                 OG  SER E 792     1555   1555  2.76  
LINK         K     K E2982                 O   HOH E3282     1555   1555  3.34  
LINK         K     K E2983                 O   ASP E  84     1555   1555  3.02  
LINK         K     K E2983                 O   GLY E 112     1555   1555  2.89  
LINK         K     K E2983                 OG1 THR E 114     1555   1555  2.42  
LINK         K     K E2983                 O   HOH E3451     1555   1555  2.84  
LINK        MN    MN G3901                 O   HOH G4292     1555   1555  2.61  
LINK        MN    MN G3901                 OD1 ASN G 301     1555   1555  2.56  
LINK         K     K G3903                 O   ASP G 238     1555   1555  2.97  
LINK         K     K G3903                 OG  SER G 247     1555   1555  2.77  
LINK         K     K G3903                 OE1 GLU G 215     1555   1555  2.46  
LINK         K     K G3903                 O   ALA G 239     1555   1555  2.64  
LINK         K     K G3903                 OD1 ASN G 236     1555   1555  2.89  
LINK         K     K G3903                 O   ILE G 242     1555   1555  2.49  
LINK         K     K G3904                 OD1 ASN G 301     1555   1555  3.60  
LINK         K     K G3904                 O   HOH G4292     1555   1555  3.57  
LINK         K     K G3904                 O   ALA G 126     1555   1555  3.22  
LINK         K     K G3904                 O   HOH G4105     1555   1555  2.50  
LINK         K     K G3904                 O   MET G 300     1555   1555  2.93  
LINK         K     K G3904                 OE2 GLU G 127     1555   1555  3.43  
LINK         K     K G3904                 OE1 GLU G 299     1555   1555  2.87  
LINK        MN    MN G3911                 O   HOH G4408     1555   1555  2.69  
LINK        MN    MN G3911                 OE2 GLU G 841     1555   1555  2.70  
LINK        MN    MN G3911                 O2G ANP G3910     1555   1555  2.61  
LINK        MN    MN G3912                 OE2 GLU G 841     1555   1555  2.69  
LINK        MN    MN G3912                 OE1 GLU G 841     1555   1555  2.76  
LINK        MN    MN G3912                 OD1 ASN G 843     1555   1555  2.65  
LINK         K     K G3913                 OG  SER G 792     1555   1555  2.72  
LINK         K     K G3913                 O   GLN G 784     1555   1555  2.86  
LINK         K     K G3913                 OE1 GLU G 761     1555   1555  2.50  
LINK         K     K G3913                 O   VAL G 787     1555   1555  2.62  
LINK         K     K G3913                 O   GLU G 783     1555   1555  2.96  
LINK         K     K G3913                 ND1 HIS G 781     1555   1555  2.75  
LINK         K     K G3988                 O   HOH G4389     1555   1555  3.05  
LINK         K     K G3988                 O   CYS G 551     1555   1555  2.66  
LINK         K     K G3988                 O   HOH G4390     1555   1555  2.62  
LINK         K     K G3988                 O   HOH G4382     1555   1555  3.41  
LINK         K     K G3988                 OD1 ASN G 554     1555   1555  2.67  
LINK         K     K H3987                 O   HOH H3529     1555   1555  2.80  
LINK         K     K H3987                 O   ASP H 112     1555   1555  2.79  
LINK         K     K H3987                 O   HIS H  16     1555   1555  2.69  
LINK         K     K H3987                 O   HOH G4184     1555   1555  3.55  
LINK         K     K H3987                 O   HOH H3220     1555   1555  3.62  
LINK         K     K H3987                 O   HOH G4183     1555   1555  3.37  
LINK        MN    MN C3986                 NE2 HIS A 680     1555   4455  2.03  
CISPEP   1 PHE A  164    PRO A  165          0         2.87                     
CISPEP   2 ALA A  251    PRO A  252          0         1.12                     
CISPEP   3 TYR A  710    PRO A  711          0        -2.05                     
CISPEP   4 LEU A  796    PRO A  797          0         1.36                     
CISPEP   5 ARG A  998    PRO A  999          0        -2.30                     
CISPEP   6 SER B  357    PRO B  358          0         4.79                     
CISPEP   7 PHE C  164    PRO C  165          0        -2.86                     
CISPEP   8 ALA C  251    PRO C  252          0         1.84                     
CISPEP   9 TYR C  710    PRO C  711          0         3.75                     
CISPEP  10 LEU C  796    PRO C  797          0         4.06                     
CISPEP  11 ARG C  998    PRO C  999          0        -4.18                     
CISPEP  12 SER D  357    PRO D  358          0         6.04                     
CISPEP  13 PHE E  164    PRO E  165          0         2.99                     
CISPEP  14 ALA E  251    PRO E  252          0         0.27                     
CISPEP  15 TYR E  710    PRO E  711          0        -0.64                     
CISPEP  16 LEU E  796    PRO E  797          0         4.63                     
CISPEP  17 ARG E  998    PRO E  999          0       -14.47                     
CISPEP  18 SER F  357    PRO F  358          0         4.18                     
CISPEP  19 PHE G  164    PRO G  165          0         2.67                     
CISPEP  20 ALA G  251    PRO G  252          0         1.87                     
CISPEP  21 TYR G  710    PRO G  711          0         1.21                     
CISPEP  22 LEU G  796    PRO G  797          0         2.31                     
CISPEP  23 ARG G  998    PRO G  999          0         5.78                     
CISPEP  24 SER H  357    PRO H  358          0         3.77                     
SITE     1 AC1  4 GLU A 299  ASN A 301  ANP A1083  HOH A1393                    
SITE     1 AC2  6 GLU A 215  ASN A 236  ASP A 238  ALA A 239                    
SITE     2 AC2  6 ILE A 242  SER A 247                                          
SITE     1 AC3  7 ALA A 126  GLU A 127  GLU A 299  MET A 300                    
SITE     2 AC3  7 ASN A 301  HOH A1199  HOH A1200                               
SITE     1 AC4  4 GLN A 829  GLU A 841  ANP A1084  HOH A1516                    
SITE     1 AC5  4 GLU A 841  ASN A 843  ANP A1084  HOH A1308                    
SITE     1 AC6  6 GLU A 761  HIS A 781  GLU A 783  GLN A 784                    
SITE     2 AC6  6 VAL A 787  SER A 792                                          
SITE     1 AC7  5 ASN A 371  PHE A 900  PRO A 901  GLY A 902                    
SITE     2 AC7  5 HOH A1454                                                     
SITE     1 AC8  3 LYS A 475  ASN A 485  HOH A1264                               
SITE     1 AC9  3 GLU A 549  ASP B 114  HOH B1007                               
SITE     1 BC1  3 ASN A 289  ASN A 292  ARG A 294                               
SITE     1 BC2  5 HIS B  16  ASP B 112  HOH B1009  HOH B1010                    
SITE     2 BC2  5 HOH B1063                                                     
SITE     1 BC3  4 GLU C 299  ASN C 301  ANP C1900  HOH C4295                    
SITE     1 BC4  6 GLU C 215  ASN C 236  ASP C 238  ALA C 239                    
SITE     2 BC4  6 ILE C 242  SER C 247                                          
SITE     1 BC5  6 ALA C 126  GLU C 127  GLU C 299  MET C 300                    
SITE     2 BC5  6 HOH C4100  HOH C4101                                          
SITE     1 BC6  4 GLN C 829  GLU C 841  ANP C1910  HOH C4420                    
SITE     1 BC7  4 GLU C 841  ASN C 843  ANP C1910  HOH C4209                    
SITE     1 BC8  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784                    
SITE     2 BC8  6 VAL C 787  SER C 792                                          
SITE     1 BC9  5 MET C 174  NET C1950  HOH C4293  HOH C4447                    
SITE     2 BC9  5 HOH C4450                                                     
SITE     1 CC1  5 ALA C 370  ASN C 371  PHE C 900  PRO C 901                    
SITE     2 CC1  5 GLY C 902                                                     
SITE     1 CC2  5 GLU C 549  HOH C4183  ASP D 114  HOH D1217                    
SITE     2 CC2  5 HOH D1218                                                     
SITE     1 CC3  3 ASN C 289  ASN C 292  ARG C 294                               
SITE     1 CC4  4 HOH C4183  HIS D  16  ASP D 112  HOH D1529                    
SITE     1 CC5  3 THR C 143  ALA C 144  HOH C4027                               
SITE     1 CC6  4 HIS A 680  HIS C 150  GLU C 154  HOH C4314                    
SITE     1 CC7  4 GLU E 299  ASN E 301  ANP E2900  HOH E3292                    
SITE     1 CC8  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239                    
SITE     2 CC8  6 ILE E 242  SER E 247                                          
SITE     1 CC9  8 ALA E 126  GLU E 127  GLU E 299  MET E 300                    
SITE     2 CC9  8 ASN E 301  HOH E3102  HOH E3103  HOH E3292                    
SITE     1 DC1  3 GLN E 829  GLU E 841  ANP E2910                               
SITE     1 DC2  5 VAL E 719  GLU E 841  ASN E 843  ANP E2910                    
SITE     2 DC2  5 HOH E3207                                                     
SITE     1 DC3  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784                    
SITE     2 DC3  6 VAL E 787  SER E 792                                          
SITE     1 DC4  5 ALA E  15  ILE E  18  ALA E  23  PHE E  26                    
SITE     2 DC4  5 HOH E2992                                                     
SITE     1 DC5  1 SER E 854                                                     
SITE     1 DC6  4 ASP E  84  GLY E 112  THR E 114  HOH E3451                    
SITE     1 DC7  4 GLU G 299  ASN G 301  ANP G3900  HOH G4292                    
SITE     1 DC8  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239                    
SITE     2 DC8  6 ILE G 242  SER G 247                                          
SITE     1 DC9  6 ALA G 126  GLU G 127  GLU G 299  MET G 300                    
SITE     2 DC9  6 ASN G 301  HOH G4105                                          
SITE     1 EC1  4 GLN G 829  GLU G 841  ANP G3910  HOH G4408                    
SITE     1 EC2  5 VAL G 719  GLU G 841  ASN G 843  ANP G3910                    
SITE     2 EC2  5 HOH G4209                                                     
SITE     1 EC3  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784                    
SITE     2 EC3  6 VAL G 787  SER G 792                                          
SITE     1 EC4  4 ALA G 370  ASN G 371  PRO G 901  GLY G 902                    
SITE     1 EC5  1 LYS G 475                                                     
SITE     1 EC6  1 LYS G 941                                                     
SITE     1 EC7  2 ASN G 289  ASN G 292                                          
SITE     1 EC8  3 HIS H  16  ASP H 112  HOH H3529                               
SITE     1 EC9  4 CYS G 551  ASN G 554  HOH G4389  HOH G4390                    
SITE     1 FC1 26 ARG A 129  ARG A 169  THR A 173  MET A 174                    
SITE     2 FC1 26 GLY A 175  GLY A 176  ASP A 207  GLU A 208                    
SITE     3 FC1 26 LEU A 210  ILE A 211  GLU A 215  MET A 240                    
SITE     4 FC1 26 GLY A 241  ILE A 242  HIS A 243  THR A 244                    
SITE     5 FC1 26 GLN A 285  GLU A 299  ASN A 301  ARG A 303                    
SITE     6 FC1 26 ARG A 306  THR A 376   MN A1074  HOH A1132                    
SITE     7 FC1 26 HOH A1441  HOH A1557                                          
SITE     1 FC2 28 ARG A 675  ARG A 715  VAL A 719  LEU A 720                    
SITE     2 FC2 28 GLY A 721  GLY A 722  MET A 725  ASP A 753                    
SITE     3 FC2 28 HIS A 754  PHE A 755  LEU A 756  GLU A 761                    
SITE     4 FC2 28 ALA A 785  GLY A 786  VAL A 787  HIS A 788                    
SITE     5 FC2 28 SER A 789  GLN A 829  GLU A 841  ASN A 843                    
SITE     6 FC2 28 ARG A 845  ARG A 848  PRO A 909   MN A1077                    
SITE     7 FC2 28  MN A1078  HOH A1308  HOH A1516  HOH A1730                    
SITE     1 FC3 10 GLU A 783  ASP A 791  ALA A 793  GLU A 892                    
SITE     2 FC3 10 LEU A 907  TYR A1040  ASP A1041  THR A1042                    
SITE     3 FC3 10 HOH A1345  HOH A1362                                          
SITE     1 FC4  4 GLN A  22  GLN A  93  THR A  94  ASN A 936                    
SITE     1 FC5 25 ARG C 129  ILE C 167  ARG C 169  MET C 174                    
SITE     2 FC5 25 GLY C 175  GLY C 176  GLU C 208  SER C 209                    
SITE     3 FC5 25 LEU C 210  ILE C 211  GLU C 215  MET C 240                    
SITE     4 FC5 25 GLY C 241  ILE C 242  HIS C 243  THR C 244                    
SITE     5 FC5 25 GLN C 285  GLU C 299  ASN C 301  ARG C 303                    
SITE     6 FC5 25 ARG C 306  THR C 376   MN C1901  HOH C4031                    
SITE     7 FC5 25 HOH C4295                                                     
SITE     1 FC6 25 ARG C 675  ARG C 715  VAL C 719  LEU C 720                    
SITE     2 FC6 25 GLY C 721  GLY C 722  MET C 725  ASP C 753                    
SITE     3 FC6 25 HIS C 754  PHE C 755  LEU C 756  GLU C 761                    
SITE     4 FC6 25 GLY C 786  VAL C 787  HIS C 788  SER C 789                    
SITE     5 FC6 25 GLN C 829  GLU C 841  ASN C 843  ARG C 845                    
SITE     6 FC6 25 ARG C 848  PRO C 909   MN C1911   MN C1912                    
SITE     7 FC6 25 HOH C4420                                                     
SITE     1 FC7 10 GLU C 783  ASP C 791  GLU C 892  VAL C 893                    
SITE     2 FC7 10 LEU C 907  TYR C1040  ASP C1041  THR C1042                    
SITE     3 FC7 10 HOH C4246  HOH C4263                                          
SITE     1 FC8  5 GLN C  22  THR C  94  ASN C 936   CL C1980                    
SITE     2 FC8  5 HOH C4000                                                     
SITE     1 FC9 24 ARG E 129  ARG E 169  THR E 173  MET E 174                    
SITE     2 FC9 24 GLY E 175  GLY E 176  GLU E 208  LEU E 210                    
SITE     3 FC9 24 ILE E 211  GLU E 215  MET E 240  GLY E 241                    
SITE     4 FC9 24 ILE E 242  HIS E 243  THR E 244  GLN E 285                    
SITE     5 FC9 24 GLU E 299  ASN E 301  ARG E 303  ARG E 306                    
SITE     6 FC9 24 THR E 376   MN E2901  HOH E3033  HOH E3341                    
SITE     1 GC1 25 ARG E 675  ARG E 715  VAL E 719  LEU E 720                    
SITE     2 GC1 25 GLY E 721  GLY E 722  MET E 725  ASP E 753                    
SITE     3 GC1 25 HIS E 754  PHE E 755  LEU E 756  GLU E 761                    
SITE     4 GC1 25 ALA E 785  GLY E 786  VAL E 787  HIS E 788                    
SITE     5 GC1 25 SER E 789  GLN E 829  GLU E 841  ASN E 843                    
SITE     6 GC1 25 ARG E 845  ARG E 848   MN E2911   MN E2912                    
SITE     7 GC1 25 HOH E3414                                                     
SITE     1 GC2  9 GLU E 783  ASP E 791  GLU E 892  LEU E 907                    
SITE     2 GC2  9 TYR E1040  ASP E1041  THR E1042  HOH E3244                    
SITE     3 GC2  9 HOH E3261                                                     
SITE     1 GC3  3 GLN E  22  THR E  94  ASN E 936                               
SITE     1 GC4 26 ARG G 129  ILE G 167  ARG G 169  THR G 173                    
SITE     2 GC4 26 MET G 174  GLY G 175  GLY G 176  GLU G 208                    
SITE     3 GC4 26 LEU G 210  ILE G 211  GLU G 215  MET G 240                    
SITE     4 GC4 26 GLY G 241  ILE G 242  HIS G 243  THR G 244                    
SITE     5 GC4 26 GLN G 285  GLU G 299  ASN G 301  ARG G 303                    
SITE     6 GC4 26 ARG G 306  THR G 376   MN G3901  HOH G4037                    
SITE     7 GC4 26 HOH G4292  HOH G4338                                          
SITE     1 GC5 26 ARG G 675  ARG G 715  VAL G 719  LEU G 720                    
SITE     2 GC5 26 GLY G 721  GLY G 722  MET G 725  ASP G 753                    
SITE     3 GC5 26 HIS G 754  PHE G 755  LEU G 756  GLU G 761                    
SITE     4 GC5 26 ALA G 785  GLY G 786  VAL G 787  HIS G 788                    
SITE     5 GC5 26 SER G 789  GLN G 829  ILE G 840  GLU G 841                    
SITE     6 GC5 26 ASN G 843  ARG G 845  ARG G 848   MN G3911                    
SITE     7 GC5 26  MN G3912  HOH G4408                                          
SITE     1 GC6  8 GLU G 783  ASP G 791  GLU G 892  LEU G 907                    
SITE     2 GC6  8 TYR G1040  ASP G1041  THR G1042  HOH G4245                    
SITE     1 GC7  6 GLN G  22  THR G  94  ASN G  97  ASN G 936                    
SITE     2 GC7  6 HOH G4005  HOH G4270                                          
CRYST1  151.900  164.500  332.600  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006583  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006079  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003007        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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