GenomeNet

Database: PDB
Entry: 6EN6
LinkDB: 6EN6
Original site: 6EN6 
HEADER    HYDROLASE                               04-OCT-17   6EN6              
TITLE     CRYSTAL STRUCTURE B OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN IN
TITLE    2 COMPLEX WITH A DIPROLYL INHIBITOR.                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ACE,DIPEPTIDYL CARBOXYPEPTIDASE I,KININASE II;              
COMPND   5 EC: 3.2.1.-,3.4.15.1;                                                
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACE, DCP, DCP1;                                                
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    ACE INHIBITOR, ANGIOTENSIN-I CONVERTING ENZYME, DIPROLYL INHIBITOR,   
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.E.COZIER,K.R.ACHARYA,S.FIENBERG,K.CHIBALE,E.D.STURROCK              
REVDAT   1   07-MAR-18 6EN6    0                                                
JRNL        AUTH   S.FIENBERG,G.E.COZIER,K.R.ACHARYA,K.CHIBALE,E.D.STURROCK     
JRNL        TITL   THE DESIGN AND DEVELOPMENT OF A POTENT AND SELECTIVE NOVEL   
JRNL        TITL 2 DIPROLYL DERIVATIVE THAT BINDS TO THE N-DOMAIN OF            
JRNL        TITL 3 ANGIOTENSIN-I CONVERTING ENZYME.                             
JRNL        REF    J. MED. CHEM.                 V.  61   344 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29206036                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01478                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 305465                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3040                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 79.7757 -  5.0433    0.98    13877   149  0.1848 0.2100        
REMARK   3     2  5.0433 -  4.0030    0.99    13960   143  0.1442 0.1540        
REMARK   3     3  4.0030 -  3.4970    0.99    13933   137  0.1602 0.1933        
REMARK   3     4  3.4970 -  3.1773    0.98    13947   128  0.1760 0.2018        
REMARK   3     5  3.1773 -  2.9495    0.98    13822   138  0.1839 0.2371        
REMARK   3     6  2.9495 -  2.7756    0.98    13919   159  0.1823 0.2177        
REMARK   3     7  2.7756 -  2.6366    0.98    13763   128  0.1900 0.2539        
REMARK   3     8  2.6366 -  2.5218    0.98    13831   123  0.1875 0.2281        
REMARK   3     9  2.5218 -  2.4247    0.98    13812   159  0.1888 0.2313        
REMARK   3    10  2.4247 -  2.3411    0.97    13747   128  0.1960 0.2298        
REMARK   3    11  2.3411 -  2.2679    0.97    13700   129  0.1993 0.2577        
REMARK   3    12  2.2679 -  2.2030    0.97    13749   138  0.2126 0.2827        
REMARK   3    13  2.2030 -  2.1450    0.97    13691   154  0.2202 0.2594        
REMARK   3    14  2.1450 -  2.0927    0.97    13709   141  0.2179 0.2617        
REMARK   3    15  2.0927 -  2.0451    0.97    13738   147  0.2311 0.2495        
REMARK   3    16  2.0451 -  2.0016    0.97    13629   128  0.2442 0.2653        
REMARK   3    17  2.0016 -  1.9615    0.97    13713   123  0.2662 0.3205        
REMARK   3    18  1.9615 -  1.9245    0.96    13640   134  0.2743 0.2896        
REMARK   3    19  1.9245 -  1.8901    0.96    13521   129  0.2790 0.2980        
REMARK   3    20  1.8901 -  1.8581    0.96    13647   138  0.2903 0.3443        
REMARK   3    21  1.8581 -  1.8281    0.96    13489   141  0.2994 0.2948        
REMARK   3    22  1.8281 -  1.8000    0.96    13588   146  0.3142 0.3329        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.570           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013          21747                                  
REMARK   3   ANGLE     :  1.161          29573                                  
REMARK   3   CHIRALITY :  0.062           3086                                  
REMARK   3   PLANARITY :  0.008           3803                                  
REMARK   3   DIHEDRAL  : 20.314           8076                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EN6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006883.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9282                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 305646                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 101.890                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.13500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3NXQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.06 M DIVALENT CATIONS, 0.1 M           
REMARK 280  TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     GLN A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     THR A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     THR A   135                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     ASP A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     VAL A   614                                                      
REMARK 465     THR A   615                                                      
REMARK 465     ASP A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     ALA A   618                                                      
REMARK 465     GLU A   619                                                      
REMARK 465     ALA A   620                                                      
REMARK 465     SER A   621                                                      
REMARK 465     LYS A   622                                                      
REMARK 465     PHE A   623                                                      
REMARK 465     VAL A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     GLU A   626                                                      
REMARK 465     TYR A   627                                                      
REMARK 465     ASP A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     GLN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     THR B   135                                                      
REMARK 465     ASP B   612                                                      
REMARK 465     LEU B   613                                                      
REMARK 465     VAL B   614                                                      
REMARK 465     THR B   615                                                      
REMARK 465     ASP B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     ALA B   618                                                      
REMARK 465     GLU B   619                                                      
REMARK 465     ALA B   620                                                      
REMARK 465     SER B   621                                                      
REMARK 465     LYS B   622                                                      
REMARK 465     PHE B   623                                                      
REMARK 465     VAL B   624                                                      
REMARK 465     GLU B   625                                                      
REMARK 465     GLU B   626                                                      
REMARK 465     TYR B   627                                                      
REMARK 465     ASP B   628                                                      
REMARK 465     LEU B   629                                                      
REMARK 465     GLN C   131                                                      
REMARK 465     LYS C   132                                                      
REMARK 465     THR C   133                                                      
REMARK 465     ALA C   134                                                      
REMARK 465     ILE C   611                                                      
REMARK 465     ASP C   612                                                      
REMARK 465     LEU C   613                                                      
REMARK 465     VAL C   614                                                      
REMARK 465     THR C   615                                                      
REMARK 465     ASP C   616                                                      
REMARK 465     GLU C   617                                                      
REMARK 465     ALA C   618                                                      
REMARK 465     GLU C   619                                                      
REMARK 465     ALA C   620                                                      
REMARK 465     SER C   621                                                      
REMARK 465     LYS C   622                                                      
REMARK 465     PHE C   623                                                      
REMARK 465     VAL C   624                                                      
REMARK 465     GLU C   625                                                      
REMARK 465     GLU C   626                                                      
REMARK 465     TYR C   627                                                      
REMARK 465     ASP C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     LYS D   132                                                      
REMARK 465     THR D   133                                                      
REMARK 465     ALA D   134                                                      
REMARK 465     THR D   135                                                      
REMARK 465     GLU D   619                                                      
REMARK 465     ALA D   620                                                      
REMARK 465     SER D   621                                                      
REMARK 465     LYS D   622                                                      
REMARK 465     PHE D   623                                                      
REMARK 465     VAL D   624                                                      
REMARK 465     GLU D   625                                                      
REMARK 465     GLU D   626                                                      
REMARK 465     TYR D   627                                                      
REMARK 465     ASP D   628                                                      
REMARK 465     LEU D   629                                                      
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  HD21  ASN A   416     C1   NAG A   703              1.54            
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 B 219   CD    GLU B 219   OE1    -0.086                       
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    ASN A  45       79.07   -167.97                                   
REMARK 500    LYS A 341      -46.69   -130.84                                   
REMARK 500    ASN B  45       83.17   -170.22                                   
REMARK 500    ARG B 340       -0.18     67.47                                   
REMARK 500    ASN C  45       79.82   -170.19                                   
REMARK 500    LYS C 341      -44.71   -130.41                                   
REMARK 500    ASN D  45       83.30   -169.44                                   
REMARK 500    ASN D 203       58.26     33.25                                   
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 A1371        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH A1372        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH B1371        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH C1356        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH D1462        DISTANCE =  6.68 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                              MG A 713  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 262   OE2                                                    
REMARK 620 2 ASN A 263   OD1 101.2                                              
REMARK 620 3 ASP A 354   OD2  98.1  90.8                                        
REMARK 620 4 HOH A 838   O    96.3  88.5 165.5                                  
REMARK 620 5 HOH A1269   O   173.2  77.0  88.5  77.2                            
REMARK 620 6 HOH A1169   O   100.2 155.7  74.9 100.4  83.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 710  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 361   NE2                                                    
REMARK 620 2 HIS A 365   NE2 110.7                                              
REMARK 620 3 GLU A 389   OE1  89.4 104.0                                        
REMARK 620 4 BJ2 A 711   O07 114.2 128.6 100.3                                  
REMARK 620 5 BJ2 A 711   O06  92.6  96.9 156.8  58.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 712  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 262   OE1                                                    
REMARK 620 2 ASN B 263   OD1 102.5                                              
REMARK 620 3 ASP B 354   OD2  95.4  92.4                                        
REMARK 620 4 HOH B 857   O    81.9  97.6 170.0                                  
REMARK 620 5 HOH B 965   O    70.8 173.3  87.6  82.5                            
REMARK 620 6 HOH B1246   O   170.7  82.2  92.4  89.5 104.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 709  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 361   NE2                                                    
REMARK 620 2 HIS B 365   NE2 108.4                                              
REMARK 620 3 GLU B 389   OE1  94.4 107.1                                        
REMARK 620 4 BJ2 B 710   O06  91.4  91.9 157.2                                  
REMARK 620 5 BJ2 B 710   O07 117.1 122.8 102.2  55.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 711  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 262   OE2                                                    
REMARK 620 2 ASP C 354   OD2  97.5                                              
REMARK 620 3 HOH C 828   O    88.8 170.8                                        
REMARK 620 4 HOH C 901   O    75.2  87.2  88.1                                  
REMARK 620 5 HOH C1233   O   173.7  88.8  84.9 105.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 708  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 361   NE2                                                    
REMARK 620 2 HIS C 365   NE2 111.9                                              
REMARK 620 3 GLU C 389   OE1  93.7 104.7                                        
REMARK 620 4 BJ2 C 709   O06  93.9  88.3 161.3                                  
REMARK 620 5 BJ2 C 709   O07 116.8 122.1 101.7  59.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 712  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 262   OE1                                                    
REMARK 620 2 ASP D 354   OD2  92.1                                              
REMARK 620 3 HOH D1290   O   171.8  95.6                                        
REMARK 620 4 HOH D1296   O    91.1  79.5  87.5                                  
REMARK 620 5 HOH D 894   O    80.5 171.0  91.6  95.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 709  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 361   NE2                                                    
REMARK 620 2 HIS D 365   NE2 111.3                                              
REMARK 620 3 GLU D 389   OE2  91.6 109.2                                        
REMARK 620 4 BJ2 D 710   O06  91.0  94.4 153.4                                  
REMARK 620 5 BJ2 D 710   O07 116.3 122.7  99.5  56.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 710                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 A 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 712                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 713                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCN A 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 B 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 711                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 712                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 722                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 723                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 724                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 725                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 726                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 727                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 728                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 729                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2PE B 730                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XPE B 731                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 C 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 710                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 711                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XPE C 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 D 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 711                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 712                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 722                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 723                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 724                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 725                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 726                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 727                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 728                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 729                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 730                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 731                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  701 through NAG A 702 bound to ASN A 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  703 through FUC A 706 bound to ASN A 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  707 through FUC A 709 bound to ASN A 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  701 through NAG B 702 bound to ASN B 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  703 through FUC B 706 bound to ASN B 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  707 through FUC B 708 bound to ASN B 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 701 bound   
REMARK 800  to ASN C 45                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  702 through BMA C 704 bound to ASN C 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  705 through FUC C 707 bound to ASN C 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  701 through NAG D 702 bound to ASN D 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  703 through FUC D 706 bound to ASN D 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  707 through FUC D 708 bound to ASN D 480                            
DBREF  6EN6 A    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  6EN6 B    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  6EN6 C    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  6EN6 D    1   628  UNP    P12821   ACE_HUMAN       30    657             
SEQADV 6EN6 GLN A    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN6 GLN A   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN6 GLN A   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN6 GLN A  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN6 GLN A  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN6 GLN A  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN6 ARG A  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN6 LEU A  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN6 LEU A  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 6EN6 GLN B    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN6 GLN B   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN6 GLN B   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN6 GLN B  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN6 GLN B  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN6 GLN B  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN6 ARG B  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN6 LEU B  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN6 LEU B  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 6EN6 GLN C    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN6 GLN C   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN6 GLN C   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN6 GLN C  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN6 GLN C  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN6 GLN C  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN6 ARG C  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN6 LEU C  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN6 LEU C  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 6EN6 GLN D    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN6 GLN D   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN6 GLN D   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN6 GLN D  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN6 GLN D  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN6 GLN D  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN6 ARG D  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN6 LEU D  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN6 LEU D  629  UNP  P12821              EXPRESSION TAG                 
SEQRES   1 A  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 A  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 A  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 A  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 A  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 A  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 A  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 A  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 A  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 A  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 A  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 A  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 A  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 A  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 A  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 A  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 A  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 A  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 A  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 A  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 A  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 A  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 A  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 A  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 A  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 A  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 A  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 A  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 A  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 A  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 A  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 A  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 A  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 A  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 A  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 A  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 A  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 A  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 A  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 A  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 A  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 A  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 A  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 A  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 A  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 A  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 A  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 A  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 A  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 B  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 B  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 B  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 B  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 B  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 B  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 B  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 B  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 B  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 B  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 B  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 B  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 B  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 B  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 B  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 B  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 B  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 B  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 B  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 B  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 B  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 B  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 B  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 B  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 B  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 B  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 B  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 B  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 B  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 B  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 B  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 B  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 B  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 B  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 B  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 B  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 B  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 B  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 B  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 B  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 B  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 B  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 B  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 B  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 B  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 B  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 B  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 B  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 B  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 C  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 C  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 C  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 C  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 C  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 C  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 C  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 C  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 C  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 C  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 C  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 C  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 C  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 C  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 C  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 C  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 C  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 C  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 C  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 C  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 C  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 C  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 C  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 C  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 C  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 C  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 C  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 C  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 C  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 C  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 C  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 C  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 C  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 C  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 C  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 C  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 C  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 C  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 C  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 C  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 C  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 C  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 C  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 C  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 C  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 C  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 C  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 C  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 C  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 D  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 D  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 D  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 D  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 D  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 D  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 D  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 D  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 D  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 D  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 D  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 D  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 D  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 D  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 D  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 D  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 D  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 D  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 D  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 D  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 D  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 D  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 D  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 D  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 D  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 D  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 D  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 D  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 D  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 D  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 D  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 D  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 D  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 D  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 D  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 D  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 D  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 D  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 D  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 D  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 D  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 D  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 D  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 D  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 D  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 D  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 D  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 D  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 D  629  GLU GLU TYR ASP LEU                                          
HET    NAG  A 701      26                                                       
HET    NAG  A 702      27                                                       
HET    NAG  A 703      25                                                       
HET    NAG  A 704      26                                                       
HET    BMA  A 705      21                                                       
HET    FUC  A 706      20                                                       
HET    NAG  A 707      25                                                       
HET    NAG  A 708      27                                                       
HET    FUC  A 709      20                                                       
HET     ZN  A 710       1                                                       
HET    BJ2  A 711      55                                                       
HET     CL  A 712       1                                                       
HET     MG  A 713       1                                                       
HET    PEG  A 714      17                                                       
HET    PEG  A 715      17                                                       
HET    EDO  A 716      10                                                       
HET    EDO  A 717      10                                                       
HET    ACT  A 718       7                                                       
HET    ACT  A 719       7                                                       
HET    PGE  A 720      24                                                       
HET    BCN  A 721      23                                                       
HET    NAG  B 701      26                                                       
HET    NAG  B 702      27                                                       
HET    NAG  B 703      25                                                       
HET    NAG  B 704      26                                                       
HET    BMA  B 705      21                                                       
HET    FUC  B 706      20                                                       
HET    NAG  B 707      26                                                       
HET    FUC  B 708      20                                                       
HET     ZN  B 709       1                                                       
HET    BJ2  B 710      55                                                       
HET     CL  B 711       1                                                       
HET     MG  B 712       1                                                       
HET    PEG  B 713      17                                                       
HET    PEG  B 714      17                                                       
HET    PEG  B 715      17                                                       
HET    PEG  B 716      17                                                       
HET    EDO  B 717      10                                                       
HET    EDO  B 718      10                                                       
HET    EDO  B 719      10                                                       
HET    EDO  B 720      10                                                       
HET    EDO  B 721      10                                                       
HET    EDO  B 722      10                                                       
HET    EDO  B 723      10                                                       
HET    EDO  B 724      10                                                       
HET    ACT  B 725       7                                                       
HET    ACT  B 726       7                                                       
HET    ACT  B 727       7                                                       
HET    PGE  B 728      24                                                       
HET    PGE  B 729      48                                                       
HET    2PE  B 730      66                                                       
HET    XPE  B 731      73                                                       
HET    NAG  C 701      27                                                       
HET    NAG  C 702      26                                                       
HET    NAG  C 703      26                                                       
HET    BMA  C 704      21                                                       
HET    NAG  C 705      25                                                       
HET    NAG  C 706      27                                                       
HET    FUC  C 707      20                                                       
HET     ZN  C 708       1                                                       
HET    BJ2  C 709      55                                                       
HET     CL  C 710       1                                                       
HET     MG  C 711       1                                                       
HET    PEG  C 712      17                                                       
HET    PEG  C 713      17                                                       
HET    EDO  C 714      10                                                       
HET    EDO  C 715      10                                                       
HET    EDO  C 716      10                                                       
HET    EDO  C 717      10                                                       
HET    ACT  C 718       7                                                       
HET    ACT  C 719       7                                                       
HET    ACT  C 720       7                                                       
HET    XPE  C 721      73                                                       
HET    NAG  D 701      26                                                       
HET    NAG  D 702      27                                                       
HET    NAG  D 703      25                                                       
HET    NAG  D 704      26                                                       
HET    BMA  D 705      21                                                       
HET    FUC  D 706      20                                                       
HET    NAG  D 707      26                                                       
HET    FUC  D 708      20                                                       
HET     ZN  D 709       1                                                       
HET    BJ2  D 710      55                                                       
HET     CL  D 711       1                                                       
HET     MG  D 712       1                                                       
HET    PEG  D 713      17                                                       
HET    PEG  D 714      17                                                       
HET    EDO  D 715      10                                                       
HET    EDO  D 716      10                                                       
HET    EDO  D 717      10                                                       
HET    EDO  D 718      10                                                       
HET    EDO  D 719      10                                                       
HET    EDO  D 720      10                                                       
HET    EDO  D 721      10                                                       
HET    EDO  D 722      10                                                       
HET    EDO  D 723      10                                                       
HET    ACT  D 724       7                                                       
HET    ACT  D 725       7                                                       
HET    ACT  D 726       7                                                       
HET    ACT  D 727       7                                                       
HET    ACT  D 728       7                                                       
HET    PGE  D 729      24                                                       
HET    PGE  D 730      24                                                       
HET    PGE  D 731      24                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     BJ2 (2~{S})-1-[(2~{S})-2-[[(1~{S})-1-[(2~{S})-1-[(2~{S})-2-          
HETNAM   2 BJ2  AZANYL-4-OXIDANYL-4-OXIDANYLIDENE-BUTANOYL]PYRROLIDIN-          
HETNAM   3 BJ2  2-YL]-2-OXIDANYL-2-OXIDANYLIDENE-                               
HETNAM   4 BJ2  ETHYL]AMINO]PROPANOYL]PYRROLIDINE-2-CARBOXYLIC ACID             
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     BCN BICINE                                                           
HETNAM     2PE NONAETHYLENE GLYCOL                                              
HETNAM     XPE 3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL              
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     XPE DECAETHYLENE GLYCOL                                              
FORMUL   5  NAG    21(C8 H15 N O6)                                              
FORMUL   6  BMA    4(C6 H12 O6)                                                 
FORMUL   6  FUC    7(C6 H12 O5)                                                 
FORMUL   8   ZN    4(ZN 2+)                                                     
FORMUL   9  BJ2    4(C18 H28 N4 O8)                                             
FORMUL  10   CL    4(CL 1-)                                                     
FORMUL  11   MG    4(MG 2+)                                                     
FORMUL  12  PEG    10(C4 H10 O3)                                                
FORMUL  14  EDO    23(C2 H6 O2)                                                 
FORMUL  16  ACT    13(C2 H3 O2 1-)                                              
FORMUL  18  PGE    6(C6 H14 O4)                                                 
FORMUL  19  BCN    C6 H13 N O4                                                  
FORMUL  44  2PE    C18 H38 O10                                                  
FORMUL  45  XPE    2(C20 H42 O11)                                               
FORMUL  89  HOH   *2361(H2 O)                                                   
HELIX    1 AA1 ASP A    2  GLN A    6  5                                   5    
HELIX    2 AA2 ASP A   13  THR A   44  1                                  32    
HELIX    3 AA3 THR A   47  GLU A   77  1                                  31    
HELIX    4 AA4 ILE A   79  PHE A   83  5                                   5    
HELIX    5 AA5 ASP A   85  ARG A   96  1                                  12    
HELIX    6 AA6 LEU A   98  LEU A  103  5                                   6    
HELIX    7 AA7 PRO A  104  ALA A  125  1                                  22    
HELIX    8 AA8 PRO A  141  SER A  150  1                                  10    
HELIX    9 AA9 SER A  152  GLN A  188  1                                  37    
HELIX   10 AB1 ASP A  193  TRP A  201  1                                   9    
HELIX   11 AB2 THR A  206  GLY A  238  1                                  33    
HELIX   12 AB3 TRP A  261  ASN A  263  5                                   3    
HELIX   13 AB4 ILE A  264  VAL A  269  1                                   6    
HELIX   14 AB5 VAL A  279  GLY A  287  1                                   9    
HELIX   15 AB6 GLN A  289  LEU A  304  1                                  16    
HELIX   16 AB7 PRO A  310  SER A  317  1                                   8    
HELIX   17 AB8 THR A  352  LYS A  373  1                                  22    
HELIX   18 AB9 PRO A  376  ARG A  380  5                                   5    
HELIX   19 AC1 ASN A  384  SER A  400  1                                  17    
HELIX   20 AC2 THR A  401  ILE A  408  1                                   8    
HELIX   21 AC3 ASP A  417  ILE A  433  1                                  17    
HELIX   22 AC4 ALA A  434  SER A  451  1                                  18    
HELIX   23 AC5 PRO A  455  SER A  457  5                                   3    
HELIX   24 AC6 ARG A  458  GLY A  472  1                                  15    
HELIX   25 AC7 PHE A  484  LYS A  489  5                                   6    
HELIX   26 AC8 TYR A  498  ALA A  519  1                                  22    
HELIX   27 AC9 PRO A  524  CYS A  528  5                                   5    
HELIX   28 AD1 SER A  533  GLY A  547  1                                  15    
HELIX   29 AD2 PRO A  551  GLY A  561  1                                  11    
HELIX   30 AD3 ALA A  567  ASN A  588  1                                  22    
HELIX   31 AD4 ASP B    2  GLN B    6  5                                   5    
HELIX   32 AD5 ASP B   13  THR B   44  1                                  32    
HELIX   33 AD6 THR B   47  GLU B   77  1                                  31    
HELIX   34 AD7 ILE B   79  PHE B   83  5                                   5    
HELIX   35 AD8 ASP B   85  ARG B   96  1                                  12    
HELIX   36 AD9 LEU B   98  LEU B  103  5                                   6    
HELIX   37 AE1 PRO B  104  ALA B  125  1                                  22    
HELIX   38 AE2 PRO B  141  SER B  150  1                                  10    
HELIX   39 AE3 SER B  152  GLN B  188  1                                  37    
HELIX   40 AE4 ASP B  193  TRP B  201  1                                   9    
HELIX   41 AE5 THR B  206  GLY B  238  1                                  33    
HELIX   42 AE6 TRP B  261  ASN B  263  5                                   3    
HELIX   43 AE7 ILE B  264  VAL B  269  1                                   6    
HELIX   44 AE8 VAL B  279  GLN B  286  1                                   8    
HELIX   45 AE9 GLN B  289  LEU B  304  1                                  16    
HELIX   46 AF1 PRO B  310  SER B  317  1                                   8    
HELIX   47 AF2 THR B  352  LYS B  373  1                                  22    
HELIX   48 AF3 PRO B  376  ARG B  380  5                                   5    
HELIX   49 AF4 ASN B  384  SER B  400  1                                  17    
HELIX   50 AF5 THR B  401  ILE B  408  1                                   8    
HELIX   51 AF6 ASP B  417  ILE B  433  1                                  17    
HELIX   52 AF7 ALA B  434  SER B  451  1                                  18    
HELIX   53 AF8 PRO B  455  SER B  457  5                                   3    
HELIX   54 AF9 ARG B  458  GLY B  472  1                                  15    
HELIX   55 AG1 PHE B  484  LYS B  489  5                                   6    
HELIX   56 AG2 TYR B  498  ALA B  519  1                                  22    
HELIX   57 AG3 PRO B  524  CYS B  528  5                                   5    
HELIX   58 AG4 SER B  533  GLY B  547  1                                  15    
HELIX   59 AG5 PRO B  551  GLY B  561  1                                  11    
HELIX   60 AG6 ALA B  567  ASN B  588  1                                  22    
HELIX   61 AG7 ASP C    2  GLN C    6  5                                   5    
HELIX   62 AG8 ASP C   13  THR C   44  1                                  32    
HELIX   63 AG9 THR C   47  GLU C   77  1                                  31    
HELIX   64 AH1 ILE C   79  PHE C   83  5                                   5    
HELIX   65 AH2 ASP C   85  ARG C   96  1                                  12    
HELIX   66 AH3 LEU C   98  LEU C  103  5                                   6    
HELIX   67 AH4 PRO C  104  ALA C  125  1                                  22    
HELIX   68 AH5 PRO C  141  SER C  150  1                                  10    
HELIX   69 AH6 SER C  152  GLN C  188  1                                  37    
HELIX   70 AH7 ASP C  193  TRP C  201  1                                   9    
HELIX   71 AH8 THR C  206  GLY C  238  1                                  33    
HELIX   72 AH9 TRP C  261  ASN C  263  5                                   3    
HELIX   73 AI1 ILE C  264  VAL C  269  1                                   6    
HELIX   74 AI2 VAL C  279  GLN C  286  1                                   8    
HELIX   75 AI3 GLN C  289  LEU C  304  1                                  16    
HELIX   76 AI4 PRO C  310  SER C  317  1                                   8    
HELIX   77 AI5 THR C  352  TYR C  372  1                                  21    
HELIX   78 AI6 PRO C  376  ARG C  380  5                                   5    
HELIX   79 AI7 ASN C  384  SER C  400  1                                  17    
HELIX   80 AI8 THR C  401  ILE C  408  1                                   8    
HELIX   81 AI9 ASP C  417  ILE C  433  1                                  17    
HELIX   82 AJ1 ALA C  434  SER C  451  1                                  18    
HELIX   83 AJ2 PRO C  455  SER C  457  5                                   3    
HELIX   84 AJ3 ARG C  458  GLY C  472  1                                  15    
HELIX   85 AJ4 PHE C  484  LYS C  489  5                                   6    
HELIX   86 AJ5 TYR C  498  ALA C  519  1                                  22    
HELIX   87 AJ6 PRO C  524  CYS C  528  5                                   5    
HELIX   88 AJ7 SER C  533  GLY C  547  1                                  15    
HELIX   89 AJ8 PRO C  551  GLY C  561  1                                  11    
HELIX   90 AJ9 ALA C  567  ASN C  588  1                                  22    
HELIX   91 AK1 ASP D    2  GLN D    6  5                                   5    
HELIX   92 AK2 ASP D   13  THR D   44  1                                  32    
HELIX   93 AK3 THR D   47  GLU D   77  1                                  31    
HELIX   94 AK4 ILE D   79  PHE D   83  5                                   5    
HELIX   95 AK5 ASP D   85  ARG D   96  1                                  12    
HELIX   96 AK6 LEU D   98  LEU D  103  5                                   6    
HELIX   97 AK7 PRO D  104  ALA D  125  1                                  22    
HELIX   98 AK8 PRO D  141  SER D  150  1                                  10    
HELIX   99 AK9 SER D  152  GLN D  188  1                                  37    
HELIX  100 AL1 ASP D  193  TRP D  201  1                                   9    
HELIX  101 AL2 THR D  206  GLY D  238  1                                  33    
HELIX  102 AL3 TRP D  261  ASN D  263  5                                   3    
HELIX  103 AL4 ILE D  264  VAL D  269  1                                   6    
HELIX  104 AL5 VAL D  279  GLN D  286  1                                   8    
HELIX  105 AL6 GLN D  289  LEU D  304  1                                  16    
HELIX  106 AL7 PRO D  310  SER D  317  1                                   8    
HELIX  107 AL8 THR D  352  TYR D  372  1                                  21    
HELIX  108 AL9 PRO D  376  ARG D  380  5                                   5    
HELIX  109 AM1 ASN D  384  SER D  400  1                                  17    
HELIX  110 AM2 THR D  401  ILE D  408  1                                   8    
HELIX  111 AM3 ASP D  417  ILE D  433  1                                  17    
HELIX  112 AM4 ALA D  434  SER D  451  1                                  18    
HELIX  113 AM5 PRO D  455  SER D  457  5                                   3    
HELIX  114 AM6 ARG D  458  GLY D  472  1                                  15    
HELIX  115 AM7 PHE D  484  LYS D  489  5                                   6    
HELIX  116 AM8 TYR D  498  ALA D  519  1                                  22    
HELIX  117 AM9 PRO D  524  CYS D  528  5                                   5    
HELIX  118 AN1 SER D  533  ALA D  546  1                                  14    
HELIX  119 AN2 PRO D  551  GLY D  561  1                                  11    
HELIX  120 AN3 ALA D  567  ASN D  588  1                                  22    
HELIX  121 AN4 GLY D  610  VAL D  614  5                                   5    
SHEET    1 AA1 2 ILE A 248  PRO A 249  0                                        
SHEET    2 AA1 2 ILE A 473  CYS A 474  1  O  CYS A 474   N  ILE A 248           
SHEET    1 AA2 2 SER A 333  ASP A 336  0                                        
SHEET    2 AA2 2 PHE A 343  LYS A 346 -1  O  LYS A 346   N  SER A 333           
SHEET    1 AA3 2 LYS B 126  VAL B 127  0                                        
SHEET    2 AA3 2 TRP B 137  SER B 138 -1  O  TRP B 137   N  VAL B 127           
SHEET    1 AA4 2 ILE B 248  PRO B 249  0                                        
SHEET    2 AA4 2 ILE B 473  CYS B 474  1  O  CYS B 474   N  ILE B 248           
SHEET    1 AA5 2 SER B 333  ASP B 336  0                                        
SHEET    2 AA5 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335           
SHEET    1 AA6 2 LYS C 126  CYS C 128  0                                        
SHEET    2 AA6 2 CYS C 136  SER C 138 -1  O  TRP C 137   N  VAL C 127           
SHEET    1 AA7 2 ILE C 248  PRO C 249  0                                        
SHEET    2 AA7 2 ILE C 473  CYS C 474  1  O  CYS C 474   N  ILE C 248           
SHEET    1 AA8 2 SER C 333  ASP C 336  0                                        
SHEET    2 AA8 2 PHE C 343  LYS C 346 -1  O  LYS C 346   N  SER C 333           
SHEET    1 AA9 2 LYS D 126  VAL D 127  0                                        
SHEET    2 AA9 2 TRP D 137  SER D 138 -1  O  TRP D 137   N  VAL D 127           
SHEET    1 AB1 2 ILE D 248  PRO D 249  0                                        
SHEET    2 AB1 2 ILE D 473  CYS D 474  1  O  CYS D 474   N  ILE D 248           
SHEET    1 AB2 2 SER D 333  ASP D 336  0                                        
SHEET    2 AB2 2 PHE D 343  LYS D 346 -1  O  ARG D 344   N  TRP D 335           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.07  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.07  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.04  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.05  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.07  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.02  
SSBOND   7 CYS C  128    CYS C  136                          1555   1555  2.06  
SSBOND   8 CYS C  330    CYS C  348                          1555   1555  2.05  
SSBOND   9 CYS C  516    CYS C  528                          1555   1555  2.03  
SSBOND  10 CYS D  128    CYS D  136                          1555   1555  2.06  
SSBOND  11 CYS D  330    CYS D  348                          1555   1555  2.09  
SSBOND  12 CYS D  516    CYS D  528                          1555   1555  2.05  
LINK         ND2 ASN A  45                 C1  NAG A 701     1555   1555  1.39  
LINK         OE2 GLU A 262                MG    MG A 713     1555   1555  2.18  
LINK         OD1 ASN A 263                MG    MG A 713     1555   1555  2.66  
LINK         OD2 ASP A 354                MG    MG A 713     1555   1555  2.49  
LINK         NE2 HIS A 361                ZN    ZN A 710     1555   1555  2.15  
LINK         NE2 HIS A 365                ZN    ZN A 710     1555   1555  2.15  
LINK         OE1 GLU A 389                ZN    ZN A 710     1555   1555  1.92  
LINK         ND2 ASN A 416                 C1  NAG A 703     1555   1555  1.43  
LINK         ND2 ASN A 480                 C1  NAG A 707     1555   1555  1.46  
LINK         ND2 ASN B  45                 C1  NAG B 701     1555   1555  1.28  
LINK         OE1 GLU B 262                MG    MG B 712     1555   1555  2.62  
LINK         OD1 ASN B 263                MG    MG B 712     1555   1555  2.59  
LINK         OD2 ASP B 354                MG    MG B 712     1555   1555  2.21  
LINK         NE2 HIS B 361                ZN    ZN B 709     1555   1555  2.16  
LINK         NE2 HIS B 365                ZN    ZN B 709     1555   1555  2.07  
LINK         OE1 GLU B 389                ZN    ZN B 709     1555   1555  1.88  
LINK         ND2 ASN B 416                 C1  NAG B 703     1555   1555  1.51  
LINK         ND2 ASN B 480                 C1  NAG B 707     1555   1555  1.46  
LINK         ND2 ASN C  45                 C1  NAG C 701     1555   1555  1.33  
LINK         OE2 GLU C 262                MG    MG C 711     1555   1555  2.35  
LINK         OD2 ASP C 354                MG    MG C 711     1555   1555  2.47  
LINK         NE2 HIS C 361                ZN    ZN C 708     1555   1555  2.10  
LINK         NE2 HIS C 365                ZN    ZN C 708     1555   1555  2.07  
LINK         OE1 GLU C 389                ZN    ZN C 708     1555   1555  2.02  
LINK         ND2 ASN C 416                 C1  NAG C 702     1555   1555  1.39  
LINK         ND2 ASN C 480                 C1  NAG C 705     1555   1555  1.45  
LINK         ND2 ASN D  45                 C1  NAG D 701     1555   1555  1.30  
LINK         OE1 GLU D 262                MG    MG D 712     1555   1555  2.42  
LINK         OD2 ASP D 354                MG    MG D 712     1555   1555  2.44  
LINK         NE2 HIS D 361                ZN    ZN D 709     1555   1555  2.15  
LINK         NE2 HIS D 365                ZN    ZN D 709     1555   1555  2.06  
LINK         OE2 GLU D 389                ZN    ZN D 709     1555   1555  1.90  
LINK         ND2 ASN D 416                 C1  NAG D 703     1555   1555  1.47  
LINK         ND2 ASN D 480                 C1  NAG D 707     1555   1555  1.45  
LINK         O4  NAG A 701                 C1  NAG A 702     1555   1555  1.44  
LINK         O4  NAG A 703                 C1  NAG A 704     1555   1555  1.44  
LINK         O6  NAG A 703                 C1  FUC A 706     1555   1555  1.46  
LINK         O4  NAG A 704                 C1  BMA A 705     1555   1555  1.44  
LINK         O4  NAG A 707                 C1  NAG A 708     1555   1555  1.45  
LINK         O6  NAG A 707                 C1  FUC A 709     1555   1555  1.44  
LINK        ZN    ZN A 710                 O07 BJ2 A 711     1555   1555  1.98  
LINK        ZN    ZN A 710                 O06 BJ2 A 711     1555   1555  2.44  
LINK        MG    MG A 713                 O   HOH A 838     1555   1555  2.12  
LINK        MG    MG A 713                 O   HOH A1269     1555   1555  2.94  
LINK        MG    MG A 713                 O   HOH A1169     1555   1555  2.48  
LINK         O4  NAG B 701                 C1  NAG B 702     1555   1555  1.44  
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.44  
LINK         O6  NAG B 703                 C1  FUC B 706     1555   1555  1.45  
LINK         O4  NAG B 704                 C1  BMA B 705     1555   1555  1.44  
LINK         O6  NAG B 707                 C1  FUC B 708     1555   1555  1.45  
LINK        ZN    ZN B 709                 O06 BJ2 B 710     1555   1555  2.55  
LINK        ZN    ZN B 709                 O07 BJ2 B 710     1555   1555  1.97  
LINK        MG    MG B 712                 O   HOH B 857     1555   1555  2.43  
LINK        MG    MG B 712                 O   HOH B 965     1555   1555  2.08  
LINK        MG    MG B 712                 O   HOH B1246     1555   1555  2.49  
LINK         O4  NAG C 702                 C1  NAG C 703     1555   1555  1.43  
LINK         O4  NAG C 703                 C1  BMA C 704     1555   1555  1.44  
LINK         O4  NAG C 705                 C1  NAG C 706     1555   1555  1.44  
LINK         O6  NAG C 705                 C1  FUC C 707     1555   1555  1.45  
LINK        ZN    ZN C 708                 O06 BJ2 C 709     1555   1555  2.28  
LINK        ZN    ZN C 708                 O07 BJ2 C 709     1555   1555  2.12  
LINK        MG    MG C 711                 O   HOH C 828     1555   1555  2.32  
LINK        MG    MG C 711                 O   HOH C 901     1555   1555  2.02  
LINK        MG    MG C 711                 O   HOH C1233     1555   1555  2.79  
LINK         O4  NAG D 701                 C1  NAG D 702     1555   1555  1.43  
LINK         O4  NAG D 703                 C1  NAG D 704     1555   1555  1.44  
LINK         O6  NAG D 703                 C1  FUC D 706     1555   1555  1.45  
LINK         O4  NAG D 704                 C1  BMA D 705     1555   1555  1.45  
LINK         O6  NAG D 707                 C1  FUC D 708     1555   1555  1.44  
LINK        ZN    ZN D 709                 O06 BJ2 D 710     1555   1555  2.51  
LINK        ZN    ZN D 709                 O07 BJ2 D 710     1555   1555  2.12  
LINK        MG    MG D 712                 O   HOH D1290     1555   1555  2.44  
LINK        MG    MG D 712                 O   HOH D1296     1555   1555  2.58  
LINK        MG    MG D 712                 O   HOH D 894     1555   1555  2.39  
CISPEP   1 ASP A  140    PRO A  141          0         9.01                     
CISPEP   2 TYR A  607    PRO A  608          0         4.69                     
CISPEP   3 ASP B  140    PRO B  141          0         9.45                     
CISPEP   4 TYR B  607    PRO B  608          0         8.10                     
CISPEP   5 ASP C  140    PRO C  141          0         8.77                     
CISPEP   6 TYR C  607    PRO C  608          0         5.52                     
CISPEP   7 ASP D  140    PRO D  141          0        10.52                     
CISPEP   8 TYR D  607    PRO D  608          0         2.25                     
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  BJ2 A 711                    
SITE     1 AC2 22 GLN A 259  HIS A 331  ALA A 332  SER A 333                    
SITE     2 AC2 22 ALA A 334  HIS A 361  GLU A 362  HIS A 365                    
SITE     3 AC2 22 TYR A 369  GLU A 389  LYS A 489  HIS A 491                    
SITE     4 AC2 22 THR A 496  TYR A 498  TYR A 501   ZN A 710                    
SITE     5 AC2 22 PEG A 714  HOH A 875  HOH A 893  HOH A 942                    
SITE     6 AC2 22 HOH A 948  HOH A1080                                          
SITE     1 AC3  2 TYR A 202  ARG A 500                                          
SITE     1 AC4  6 GLU A 262  ASN A 263  ASP A 354  HOH A 838                    
SITE     2 AC4  6 HOH A1169  HOH A1269                                          
SITE     1 AC5  6 SER A 333  TRP A 335  BJ2 A 711  EDO A 717                    
SITE     2 AC5  6 HOH A 831  HOH A1112                                          
SITE     1 AC6  3 TYR A 338  VAL A 377  HOH A 881                               
SITE     1 AC7  7 ARG A 295  GLU A 298  PRO A 308  MET A 309                    
SITE     2 AC7  7 HOH A1195  HOH A1246  HOH B 842                               
SITE     1 AC8  4 ASN A 494  PEG A 714  HOH A 911  HOH A1193                    
SITE     1 AC9  4 ARG A 199  GLU A 208  TRP A 447  HOH A1001                    
SITE     1 AD1  4 GLU A 513  PRO A 569  HOH A 828  HOH A1045                    
SITE     1 AD2  8 HIS A  42  ILE A  46  THR A  47  ALA A  48                    
SITE     2 AD2  8 ALA A  51  SER A 116  ARG A 120  GLU A 327                    
SITE     1 AD3 10 TYR A 465  HOH A 824  HOH A 835  HOH A1019                    
SITE     2 AD3 10 HOH A1167  GLN B 444  TYR B 465  LEU B 466                    
SITE     3 AD3 10 EDO B 719  HOH B 878                                          
SITE     1 AD4  4 HIS B 361  HIS B 365  GLU B 389  BJ2 B 710                    
SITE     1 AD5 23 GLN B 259  HIS B 331  ALA B 332  SER B 333                    
SITE     2 AD5 23 ALA B 334  HIS B 361  GLU B 362  HIS B 365                    
SITE     3 AD5 23 TYR B 369  GLU B 389  LYS B 489  HIS B 491                    
SITE     4 AD5 23 TYR B 498  TYR B 501   ZN B 709  PEG B 714                    
SITE     5 AD5 23 HOH B 832  HOH B 887  HOH B 902  HOH B 961                    
SITE     6 AD5 23 HOH B 986  HOH B1039  HOH B1112                               
SITE     1 AD6  2 TYR B 202  ARG B 500                                          
SITE     1 AD7  6 GLU B 262  ASN B 263  ASP B 354  HOH B 857                    
SITE     2 AD7  6 HOH B 965  HOH B1246                                          
SITE     1 AD8  3 TYR B  24  LEU B  32  TYR B 338                               
SITE     1 AD9  4 ALA B 334  TRP B 335  BJ2 B 710  HOH B 995                    
SITE     1 AE1  4 TRP B  40  ASP B 342  ARG B 344  HOH B1032                    
SITE     1 AE2  3 ASP B 189  GLY B 190  PHE B 191                               
SITE     1 AE3  3 HOH B 833  HOH B 898  HOH B1129                               
SITE     1 AE4  6 HIS B 164  TRP B 257  TRP B 463  TRP B 464                    
SITE     2 AE4  6 ARG B 467  ASP B 485                                          
SITE     1 AE5  5 GLN A 444  ASP A 462  BCN A 721  TYR B 465                    
SITE     2 AE5  5 HOH B 818                                                     
SITE     1 AE6  4 HOH A1172  GLU B 212  HIS B 213  GLN B 216                    
SITE     1 AE7  3 SER B 204  GLN B 553  ASP B 563                               
SITE     1 AE8  3 ASN B  50  ARG B  53  HOH B 812                               
SITE     1 AE9  2 ARG B 120  THR B 124                                          
SITE     1 AF1  1 HOH B 814                                                     
SITE     1 AF2  5 ARG B 199  GLU B 208  TRP B 447  HOH B 936                    
SITE     2 AF2  5 HOH B1010                                                     
SITE     1 AF3  4 GLU B  55  ALA B 113  GLN B 117  HOH B1344                    
SITE     1 AF4  3 GLU B 513  GLN B 568  PRO B 569                               
SITE     1 AF5  8 ALA B 196  ARG B 199  SER B 204  PRO B 205                    
SITE     2 AF5  8 THR B 206  PHE B 207  GLU B 208  HOH B 834                    
SITE     1 AF6  7 ARG B 231  HIS B 234  ASP B 239  LEU B 244                    
SITE     2 AF6  7 GLY B 589  HOH B 959  HOH B1014                               
SITE     1 AF7  6 PHE B 228  ARG B 231  ARG B 235  VAL B 268                    
SITE     2 AF7  6 HOH B 919  HOH B1221                                          
SITE     1 AF8  8 GLN A 286  TRP A 288  HIS A 292  VAL A 296                    
SITE     2 AF8  8 GLN B 286  GLY B 287  HIS B 292  HOH B1139                    
SITE     1 AF9  4 HIS C 361  HIS C 365  GLU C 389  BJ2 C 709                    
SITE     1 AG1 24 GLN C 259  HIS C 331  ALA C 332  SER C 333                    
SITE     2 AG1 24 ALA C 334  HIS C 361  GLU C 362  HIS C 365                    
SITE     3 AG1 24 TYR C 369  GLU C 389  LYS C 489  PHE C 490                    
SITE     4 AG1 24 HIS C 491  TYR C 498  TYR C 501   ZN C 708                    
SITE     5 AG1 24 PEG C 712  EDO C 714  HOH C 918  HOH C 952                    
SITE     6 AG1 24 HOH C 983  HOH C 985  HOH C1037  HOH C1082                    
SITE     1 AG2  3 TYR C 202  ARG C 500  HOH C1132                               
SITE     1 AG3  6 GLU C 262  ASN C 263  ASP C 354  HOH C 828                    
SITE     2 AG3  6 HOH C 901  HOH C1233                                          
SITE     1 AG4  2 SER C 333  BJ2 C 709                                          
SITE     1 AG5  5 GLY C 287  HIS C 292  XPE C 721  HOH C 925                    
SITE     2 AG5  5 GLN D 286                                                     
SITE     1 AG6  3 THR C 496  ARG C 500  BJ2 C 709                               
SITE     1 AG7  3 ASP C 189  GLY C 190  PHE C 191                               
SITE     1 AG8  5 ASN C 585  GLN C 586  GLU C 590  HOH C1002                    
SITE     2 AG8  5 HOH C1079                                                     
SITE     1 AG9  6 GLY C 448  ARG C 453  THR C 454  HOH C 899                    
SITE     2 AG9  6 HOH C1135  PGE D 729                                          
SITE     1 AH1  4 ARG C 199  GLU C 208  HOH C 899  HOH C 908                    
SITE     1 AH2  3 THR C 478  FUC C 707  HOH C 835                               
SITE     1 AH3  2 GLU C  55  GLN C 117                                          
SITE     1 AH4 11 GLN C 286  TRP C 288  HIS C 292  PEG C 713                    
SITE     2 AH4 11 HOH C 888  HOH C 943  HOH C1057  GLN D 286                    
SITE     3 AH4 11 TRP D 288  HIS D 292  ILE D 408                               
SITE     1 AH5  4 HIS D 361  HIS D 365  GLU D 389  BJ2 D 710                    
SITE     1 AH6 23 GLN D 259  HIS D 331  ALA D 332  SER D 333                    
SITE     2 AH6 23 ALA D 334  HIS D 361  GLU D 362  HIS D 365                    
SITE     3 AH6 23 TYR D 369  GLU D 389  LYS D 489  HIS D 491                    
SITE     4 AH6 23 TYR D 498  TYR D 501   ZN D 709  PEG D 713                    
SITE     5 AH6 23 EDO D 721  HOH D 881  HOH D 896  HOH D1038                    
SITE     6 AH6 23 HOH D1041  HOH D1125  HOH D1237                               
SITE     1 AH7  2 TYR D 202  ARG D 500                                          
SITE     1 AH8  6 GLU D 262  ASN D 263  ASP D 354  HOH D 894                    
SITE     2 AH8  6 HOH D1290  HOH D1296                                          
SITE     1 AH9  2 SER D  39  BJ2 D 710                                          
SITE     1 AI1  2 HIS D 406  HOH D1215                                          
SITE     1 AI2  4 PHE D  33  ASP D 342  ARG D 344  HOH D1028                    
SITE     1 AI3  4 HOH C 900  GLU D 315  HOH D 827  HOH D 857                    
SITE     1 AI4  3 PRO D 308  HOH D 817  HOH D1242                               
SITE     1 AI5  1 ARG D 541                                                     
SITE     1 AI6  1 PHE D 191                                                     
SITE     1 AI7  4 SER D 317  MET D 318  ARG D 326  HOH D1328                    
SITE     1 AI8  4 ARG D 381  ARG D 500  BJ2 D 710  EDO D 722                    
SITE     1 AI9  3 TRP D 201  ARG D 381  EDO D 721                               
SITE     1 AJ1  3 SER C 451  ARG C 453  GLU D 212                               
SITE     1 AJ2  7 LYS A 542  ALA A 546  HOH A 894  GLU D 609                    
SITE     2 AJ2  7 ASP D 612  LEU D 613  ACT D 727                               
SITE     1 AJ3  6 ARG D 199  GLU D 208  TRP D 447  HOH D 815                    
SITE     2 AJ3  6 HOH D 872  HOH D 928                                          
SITE     1 AJ4  4 GLU D 513  GLN D 568  PRO D 569  HOH D 850                    
SITE     1 AJ5  4 ARG A 545  HOH A1282  ASN D 606  ACT D 724                    
SITE     1 AJ6  5 VAL D 477  THR D 478  LEU D 603  FUC D 708                    
SITE     2 AJ6  5 HOH D 923                                                     
SITE     1 AJ7  7 TYR C 465  EDO C 717  GLN D 444  TYR D 465                    
SITE     2 AJ7  7 HOH D 884  HOH D 887  HOH D1018                               
SITE     1 AJ8 13 PHE C 461  GLN C 598  HIS C 600  TRP D 464                    
SITE     2 AJ8 13 THR D 468  TYR D 597  GLN D 598  HIS D 600                    
SITE     3 AJ8 13 HOH D1112  HOH D1169  HOH D1179  HOH D1294                    
SITE     4 AJ8 13 HOH D1323                                                     
SITE     1 AJ9  5 LYS D 321  PRO D 322  HOH D 971  HOH D1090                    
SITE     2 AJ9  5 HOH D1355                                                     
SITE     1 AK1  5 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 AK1  5 ARG A 326                                                     
SITE     1 AK2  8 ASN A 416  ASP A 417  THR A 418  GLU A 522                    
SITE     2 AK2  8 GLY A 523  PRO A 524  GLN A 527  HOH A 927                    
SITE     1 AK3  7 THR A 478  ASN A 480  THR A 482  HIS A 483                    
SITE     2 AK3  7 HOH A1017  ARG B 245  GLU B 596                               
SITE     1 AK4  5 ASN B  45  THR B  47  GLU B  49  ASN B  50                    
SITE     2 AK4  5 ARG B 326                                                     
SITE     1 AK5  7 GLN B   9  GLU B 403  ASN B 416  GLU B 522                    
SITE     2 AK5  7 PRO B 524  GLN B 527  HOH B 888                               
SITE     1 AK6  6 ARG A 245  GLU A 596  THR B 478  ASN B 480                    
SITE     2 AK6  6 THR B 482  HOH B 868                                          
SITE     1 AK7  6 ASN C  45  THR C  47  GLU C  49  ASN C  50                    
SITE     2 AK7  6 ARG C 326  HOH C1087                                          
SITE     1 AK8  4 ASN C 416  GLU C 522  PRO C 524  GLN C 527                    
SITE     1 AK9  8 THR C 478  ASN C 480  THR C 482  HIS C 483                    
SITE     2 AK9  8 ACT C 719  HOH C 826  ARG D 245  GLU D 596                    
SITE     1 AL1  4 ASN D  45  THR D  47  GLU D  49  ASN D  50                    
SITE     1 AL2  8 GLN D   9  PHE D  10  SER D  11  ASN D 416                    
SITE     2 AL2  8 GLU D 522  PRO D 524  GLN D 527  HOH D1144                    
SITE     1 AL3  8 ARG C 245  GLU C 596  THR D 478  ASN D 480                    
SITE     2 AL3  8 THR D 482  HIS D 483  ACT D 728  HOH D 836                    
CRYST1   74.445  103.373  115.646  84.48  85.50  81.61 P 1           4          
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      0.013433 -0.001981 -0.000890        0.00000                         
SCALE2      0.000000  0.009778 -0.000843        0.00000                         
SCALE3      0.000000  0.000000  0.008706        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system