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Database: PDB
Entry: 6EN5
LinkDB: 6EN5
Original site: 6EN5 
HEADER    HYDROLASE                               04-OCT-17   6EN5              
TITLE     CRYSTAL STRUCTURE A 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   2   24-JAN-18 6EN5    1       JRNL                                     
REVDAT   1   20-DEC-17 6EN5    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.    1.75 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 330572                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3192                            
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 79.5634 -  4.9764    0.98    14398   141  0.1630 0.1828        
REMARK   3     2  4.9764 -  3.9499    0.99    14430   147  0.1321 0.1437        
REMARK   3     3  3.9499 -  3.4506    0.98    14452   116  0.1500 0.1527        
REMARK   3     4  3.4506 -  3.1351    0.98    14398   139  0.1671 0.1894        
REMARK   3     5  3.1351 -  2.9104    0.98    14434   145  0.1706 0.1963        
REMARK   3     6  2.9104 -  2.7388    0.98    14365   141  0.1661 0.2076        
REMARK   3     7  2.7388 -  2.6016    0.98    14349   146  0.1601 0.1632        
REMARK   3     8  2.6016 -  2.4884    0.98    14337   150  0.1597 0.2221        
REMARK   3     9  2.4884 -  2.3926    0.97    14217   166  0.1575 0.1728        
REMARK   3    10  2.3926 -  2.3100    0.97    14215   129  0.1617 0.1993        
REMARK   3    11  2.3100 -  2.2378    0.97    14245   131  0.1659 0.2289        
REMARK   3    12  2.2378 -  2.1738    0.97    14207   137  0.1767 0.2129        
REMARK   3    13  2.1738 -  2.1166    0.97    14143   135  0.1858 0.2352        
REMARK   3    14  2.1166 -  2.0649    0.96    14192   119  0.1953 0.2022        
REMARK   3    15  2.0649 -  2.0180    0.97    14172   145  0.2098 0.2348        
REMARK   3    16  2.0180 -  1.9750    0.97    14175   132  0.2259 0.2893        
REMARK   3    17  1.9750 -  1.9355    0.96    14162   125  0.2329 0.2678        
REMARK   3    18  1.9355 -  1.8990    0.96    14067   152  0.2390 0.2693        
REMARK   3    19  1.8990 -  1.8651    0.96    14110   135  0.2474 0.2683        
REMARK   3    20  1.8651 -  1.8335    0.96    14098   137  0.2545 0.2876        
REMARK   3    21  1.8335 -  1.8039    0.96    14051   144  0.2758 0.3037        
REMARK   3    22  1.8039 -  1.7761    0.96    14118   143  0.2892 0.3231        
REMARK   3    23  1.7761 -  1.7500    0.96    14045   137  0.3181 0.3419        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.900           
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      :  0.009          21776                                  
REMARK   3   ANGLE     :  0.948          29646                                  
REMARK   3   CHIRALITY :  0.050           3117                                  
REMARK   3   PLANARITY :  0.006           3800                                  
REMARK   3   DIHEDRAL  : 20.857           8104                                  
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 6EN5 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_1200006799.                                   
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   : 330946                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 102.110                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
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   (%): 59.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
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     GLN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     ALA B   134                                                      
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     GLN D   131                                                      
REMARK 465     LYS D   132                                                      
REMARK 465     THR D   133                                                      
REMARK 465     ALA D   618                                                      
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   OE2  GLU B   554     O    HOH B   801              2.17            
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       77.51   -168.75                                   
REMARK 500    ARG A 326      142.11    -37.29                                   
REMARK 500    LYS A 341      -44.00   -133.43                                   
REMARK 500    GLU A 609       92.82    -64.62                                   
REMARK 500    ASN B  45       79.20   -169.00                                   
REMARK 500    ASN B 203       57.67     38.21                                   
REMARK 500    ARG B 326      141.68    -37.96                                   
REMARK 500    LYS B 341      -45.60   -130.32                                   
REMARK 500    GLU B 609     -179.86    -67.41                                   
REMARK 500    ASN C  45       78.20   -168.39                                   
REMARK 500    ARG C 326      141.48    -37.10                                   
REMARK 500    ASN D  45       79.65   -169.51                                   
REMARK 500    ASN D 203       56.47     38.14                                   
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 A1384        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH D1480        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH D1481        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH D1482        DISTANCE =  6.64 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 704  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 262   OE2                                                    
REMARK 620 2 ASN A 263   OD1 105.4                                              
REMARK 620 3 ASP A 354   OD2  98.6  89.3                                        
REMARK 620 4 HOH A 919   O    82.7  98.6 171.4                                  
REMARK 620 5 HOH A1231   O    86.1 168.2  86.2  85.4                            
REMARK 620 6 HOH A1274   O   170.4  77.8  90.4  87.9  91.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 361   NE2                                                    
REMARK 620 2 HIS A 365   NE2 109.1                                              
REMARK 620 3 GLU A 389   OE1  92.2 104.8                                        
REMARK 620 4 BJ2 A 702   O06 115.8 126.2 101.6                                  
REMARK 620 5 BJ2 A 702   O07  90.7  94.9 157.9  57.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 704  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 262   OE1                                                    
REMARK 620 2 ASN B 263   OD1 107.9                                              
REMARK 620 3 ASP B 354   OD2 102.8  86.8                                        
REMARK 620 4 HOH B 870   O    84.9  92.7 172.1                                  
REMARK 620 5 HOH B1201   O    81.8 169.1  86.1  93.2                            
REMARK 620 6 HOH B1267   O   167.2  77.5  88.9  83.3  94.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 361   NE2                                                    
REMARK 620 2 HIS B 365   NE2 109.1                                              
REMARK 620 3 GLU B 389   OE1  93.5 103.6                                        
REMARK 620 4 BJ2 B 702   O07  90.8  94.1 159.2                                  
REMARK 620 5 BJ2 B 702   O06 114.3 126.5 103.4  56.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 704  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 262   OE2                                                    
REMARK 620 2 ASN C 263   OD1 106.8                                              
REMARK 620 3 ASP C 354   OD2  99.4  92.3                                        
REMARK 620 4 HOH C 860   O    83.5  96.7 169.3                                  
REMARK 620 5 HOH C1086   O    78.1 174.4  84.2  86.4                            
REMARK 620 6 HOH C1232   O   168.3  78.3  90.8  85.5  97.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 361   NE2                                                    
REMARK 620 2 HIS C 365   NE2 110.3                                              
REMARK 620 3 GLU C 389   OE1  92.4 110.8                                        
REMARK 620 4 BJ2 C 702   O06 118.7 121.3  97.9                                  
REMARK 620 5 BJ2 C 702   O07  90.3  93.3 153.1  57.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 704  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 262   OE1                                                    
REMARK 620 2 ASN D 263   OD1 100.4                                              
REMARK 620 3 ASP D 354   OD2  98.1  87.0                                        
REMARK 620 4 HOH D1303   O    91.1 166.9  85.0                                  
REMARK 620 5 HOH D1312   O   168.8  78.4  92.9  91.6                            
REMARK 620 6 HOH D 908   O    80.5  95.6 177.2  92.6  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 361   NE2                                                    
REMARK 620 2 HIS D 365   NE2 108.6                                              
REMARK 620 3 GLU D 389   OE1  92.3 108.1                                        
REMARK 620 4 BJ2 D 702   O06 115.2 125.1 101.7                                  
REMARK 620 5 BJ2 D 702   O07  90.3  91.9 157.8  57.6                            
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 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 704                  
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 PEG 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 EDO A 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 722                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 723                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 724                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 725                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 A 726                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 722                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 723                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 724                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 725                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 726                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 C 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 722                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 723                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 C 724                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BJ2 D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 722                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 723                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XPE D 724                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  705 through NAG A 706 bound to ASN A 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues BMA A    
REMARK 800  707 through NAG A 710 bound to ASN A 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  711 through FUC A 713 bound to ASN A 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  705 through NAG B 706 bound to ASN B 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B    
REMARK 800  707 through BMA B 710 bound to ASN B 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  711 through FUC B 713 bound to ASN B 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  705 through NAG C 706 bound to ASN C 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  707 through BMA C 709 bound to ASN C 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC C    
REMARK 800  710 through NAG C 712 bound to ASN C 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  705 through BMA D 707 bound to ASN D 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC D    
REMARK 800  708 through MAN D 713 bound to ASN D 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  714 through FUC D 716 bound to ASN D 480                            
DBREF  6EN5 A    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  6EN5 B    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  6EN5 C    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  6EN5 D    1   628  UNP    P12821   ACE_HUMAN       30    657             
SEQADV 6EN5 GLN A    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN5 GLN A   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN5 GLN A   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN5 GLN A  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN5 GLN A  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN5 GLN A  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN5 ARG A  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN5 LEU A  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN5 LEU A  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 6EN5 GLN B    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN5 GLN B   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN5 GLN B   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN5 GLN B  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN5 GLN B  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN5 GLN B  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN5 ARG B  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN5 LEU B  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN5 LEU B  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 6EN5 GLN C    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN5 GLN C   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN5 GLN C   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN5 GLN C  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN5 GLN C  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN5 GLN C  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN5 ARG C  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN5 LEU C  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN5 LEU C  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 6EN5 GLN D    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6EN5 GLN D   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6EN5 GLN D   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6EN5 GLN D  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6EN5 GLN D  131  UNP  P12821    ASN   160 CONFLICT                       
SEQADV 6EN5 GLN D  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6EN5 ARG D  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6EN5 LEU D  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6EN5 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     ZN  A 701       1                                                       
HET    BJ2  A 702      55                                                       
HET     CL  A 703       1                                                       
HET     MG  A 704       1                                                       
HET    NAG  A 705      27                                                       
HET    NAG  A 706      28                                                       
HET    BMA  A 707      22                                                       
HET    FUC  A 708      20                                                       
HET    NAG  A 709      26                                                       
HET    NAG  A 710      27                                                       
HET    NAG  A 711      26                                                       
HET    NAG  A 712      28                                                       
HET    FUC  A 713      20                                                       
HET    PEG  A 714      17                                                       
HET    PEG  A 715      17                                                       
HET    PEG  A 716      17                                                       
HET    EDO  A 717      10                                                       
HET    EDO  A 718      10                                                       
HET    EDO  A 719      10                                                       
HET    EDO  A 720      10                                                       
HET    EDO  A 721      10                                                       
HET    EDO  A 722      10                                                       
HET    EDO  A 723      10                                                       
HET    ACT  A 724       7                                                       
HET    ACT  A 725       7                                                       
HET    PE3  A 726     101                                                       
HET     ZN  B 701       1                                                       
HET    BJ2  B 702      55                                                       
HET     CL  B 703       1                                                       
HET     MG  B 704       1                                                       
HET    NAG  B 705      27                                                       
HET    NAG  B 706      27                                                       
HET    FUC  B 707      21                                                       
HET    NAG  B 708      26                                                       
HET    NAG  B 709      27                                                       
HET    BMA  B 710      21                                                       
HET    NAG  B 711      26                                                       
HET    NAG  B 712      27                                                       
HET    FUC  B 713      20                                                       
HET    PEG  B 714      17                                                       
HET    PEG  B 715      17                                                       
HET    PEG  B 716      17                                                       
HET    PEG  B 717      17                                                       
HET    PEG  B 718      17                                                       
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    ACT  B 724       7                                                       
HET    PGE  B 725      24                                                       
HET    PG4  B 726      31                                                       
HET     ZN  C 701       1                                                       
HET    BJ2  C 702      55                                                       
HET     CL  C 703       1                                                       
HET     MG  C 704       1                                                       
HET    NAG  C 705      27                                                       
HET    NAG  C 706      27                                                       
HET    NAG  C 707      27                                                       
HET    NAG  C 708      27                                                       
HET    BMA  C 709      21                                                       
HET    FUC  C 710      21                                                       
HET    NAG  C 711      26                                                       
HET    NAG  C 712      27                                                       
HET    PEG  C 713      17                                                       
HET    PEG  C 714      17                                                       
HET    EDO  C 715      10                                                       
HET    EDO  C 716      10                                                       
HET    EDO  C 717      10                                                       
HET    EDO  C 718      10                                                       
HET    EDO  C 719      10                                                       
HET    EDO  C 720      10                                                       
HET    EDO  C 721      10                                                       
HET    EDO  C 722      10                                                       
HET    ACT  C 723       7                                                       
HET    PG4  C 724      62                                                       
HET     ZN  D 701       1                                                       
HET    BJ2  D 702      55                                                       
HET     CL  D 703       1                                                       
HET     MG  D 704       1                                                       
HET    NAG  D 705      27                                                       
HET    NAG  D 706      27                                                       
HET    BMA  D 707      21                                                       
HET    FUC  D 708      21                                                       
HET    NAG  D 709      26                                                       
HET    NAG  D 710      27                                                       
HET    BMA  D 711      19                                                       
HET    MAN  D 712      21                                                       
HET    MAN  D 713      21                                                       
HET    NAG  D 714      26                                                       
HET    NAG  D 715      27                                                       
HET    FUC  D 716      19                                                       
HET    PEG  D 717      17                                                       
HET    PEG  D 718      17                                                       
HET    EDO  D 719      10                                                       
HET    EDO  D 720      10                                                       
HET    EDO  D 721      10                                                       
HET    ACT  D 722       7                                                       
HET    ACT  D 723       7                                                       
HET    XPE  D 724      73                                                       
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     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM     PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-                             
HETNAM   2 PE3  TRIDECAOXAHENTETRACONTANE-1,41-DIOL                             
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     XPE 3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL              
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     PE3 POLYETHYLENE GLYCOL                                              
HETSYN     XPE DECAETHYLENE GLYCOL                                              
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  BJ2    4(C18 H28 N4 O8)                                             
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL   8   MG    4(MG 2+)                                                     
FORMUL   9  NAG    24(C8 H15 N O6)                                              
FORMUL  10  BMA    5(C6 H12 O6)                                                 
FORMUL  10  FUC    7(C6 H12 O5)                                                 
FORMUL  12  PEG    12(C4 H10 O3)                                                
FORMUL  15  EDO    23(C2 H6 O2)                                                 
FORMUL  22  ACT    6(C2 H3 O2 1-)                                               
FORMUL  24  PE3    C28 H58 O15                                                  
FORMUL  43  PGE    C6 H14 O4                                                    
FORMUL  44  PG4    2(C8 H18 O5)                                                 
FORMUL  69  MAN    2(C6 H12 O6)                                                 
FORMUL  78  XPE    C20 H42 O11                                                  
FORMUL  79  HOH   *2393(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  GLN A  286  1                                   8    
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  ALA A  546  1                                  14    
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  TYR B  372  1                                  21    
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  THR C  401  1                                  18    
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  GLY D  547  1                                  15    
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 PRO D  608  VAL D  614  5                                   7    
SHEET    1 AA1 2 LYS A 126  VAL A 127  0                                        
SHEET    2 AA1 2 TRP A 137  SER A 138 -1  O  TRP A 137   N  VAL A 127           
SHEET    1 AA2 2 ILE A 248  PRO A 249  0                                        
SHEET    2 AA2 2 ILE A 473  CYS A 474  1  O  CYS A 474   N  ILE A 248           
SHEET    1 AA3 2 SER A 333  ASP A 336  0                                        
SHEET    2 AA3 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335           
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 VAL C 127  CYS C 128  0                                        
SHEET    2 AA6 2 CYS C 136  TRP C 137 -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  ARG C 344   N  TRP C 335           
SHEET    1 AA9 2 LYS D 126  CYS D 128  0                                        
SHEET    2 AA9 2 CYS D 136  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  LYS D 346   N  SER D 333           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.04  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.07  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.05  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.05  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.05  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.04  
SSBOND   7 CYS C  128    CYS C  136                          1555   1555  2.05  
SSBOND   8 CYS C  330    CYS C  348                          1555   1555  2.08  
SSBOND   9 CYS C  516    CYS C  528                          1555   1555  2.05  
SSBOND  10 CYS D  128    CYS D  136                          1555   1555  2.06  
SSBOND  11 CYS D  330    CYS D  348                          1555   1555  2.06  
SSBOND  12 CYS D  516    CYS D  528                          1555   1555  2.05  
LINK         ND2 ASN A  45                 C1  NAG A 705     1555   1555  1.43  
LINK         OE2 GLU A 262                MG    MG A 704     1555   1555  2.33  
LINK         OD1 ASN A 263                MG    MG A 704     1555   1555  2.67  
LINK         OD2 ASP A 354                MG    MG A 704     1555   1555  2.45  
LINK         NE2 HIS A 361                ZN    ZN A 701     1555   1555  2.10  
LINK         NE2 HIS A 365                ZN    ZN A 701     1555   1555  2.08  
LINK         OE1 GLU A 389                ZN    ZN A 701     1555   1555  1.90  
LINK         ND2 ASN A 416                 C1  NAG A 709     1555   1555  1.45  
LINK         ND2 ASN A 480                 C1  NAG A 711     1555   1555  1.46  
LINK         ND2 ASN B  45                 C1  NAG B 705     1555   1555  1.43  
LINK         OE1 GLU B 262                MG    MG B 704     1555   1555  2.42  
LINK         OD1 ASN B 263                MG    MG B 704     1555   1555  2.76  
LINK         OD2 ASP B 354                MG    MG B 704     1555   1555  2.46  
LINK         NE2 HIS B 361                ZN    ZN B 701     1555   1555  2.10  
LINK         NE2 HIS B 365                ZN    ZN B 701     1555   1555  2.05  
LINK         OE1 GLU B 389                ZN    ZN B 701     1555   1555  1.93  
LINK         ND2 ASN B 416                 C1  NAG B 708     1555   1555  1.45  
LINK         ND2 ASN B 480                 C1  NAG B 711     1555   1555  1.45  
LINK         ND2 ASN C  45                 C1  NAG C 705     1555   1555  1.43  
LINK         OE2 GLU C 262                MG    MG C 704     1555   1555  2.38  
LINK         OD1 ASN C 263                MG    MG C 704     1555   1555  2.64  
LINK         OD2 ASP C 354                MG    MG C 704     1555   1555  2.42  
LINK         NE2 HIS C 361                ZN    ZN C 701     1555   1555  2.07  
LINK         NE2 HIS C 365                ZN    ZN C 701     1555   1555  2.07  
LINK         OE1 GLU C 389                ZN    ZN C 701     1555   1555  2.00  
LINK         ND2 ASN C 416                 C1  NAG C 707     1555   1555  1.44  
LINK         ND2 ASN C 480                 C1  NAG C 711     1555   1555  1.45  
LINK         ND2 ASN D  45                 C1  NAG D 705     1555   1555  1.43  
LINK         OE1 GLU D 262                MG    MG D 704     1555   1555  2.38  
LINK         OD1 ASN D 263                MG    MG D 704     1555   1555  2.47  
LINK         OD2 ASP D 354                MG    MG D 704     1555   1555  2.49  
LINK         NE2 HIS D 361                ZN    ZN D 701     1555   1555  2.10  
LINK         NE2 HIS D 365                ZN    ZN D 701     1555   1555  2.02  
LINK         OE1 GLU D 389                ZN    ZN D 701     1555   1555  2.00  
LINK         ND2 ASN D 416                 C1  NAG D 709     1555   1555  1.46  
LINK         ND2 ASN D 480                 C1  NAG D 714     1555   1555  1.46  
LINK        ZN    ZN A 701                 O06 BJ2 A 702     1555   1555  2.02  
LINK        ZN    ZN A 701                 O07 BJ2 A 702     1555   1555  2.50  
LINK        MG    MG A 704                 O   HOH A 919     1555   1555  2.35  
LINK        MG    MG A 704                 O   HOH A1231     1555   1555  2.23  
LINK        MG    MG A 704                 O   HOH A1274     1555   1555  2.91  
LINK         O4  NAG A 705                 C1  NAG A 706     1555   1555  1.44  
LINK         C1  BMA A 707                 O4  NAG A 710     1555   1555  1.44  
LINK         C1  FUC A 708                 O6  NAG A 709     1555   1555  1.45  
LINK         O4  NAG A 709                 C1  NAG A 710     1555   1555  1.44  
LINK         O4  NAG A 711                 C1  NAG A 712     1555   1555  1.45  
LINK         O6  NAG A 711                 C1  FUC A 713     1555   1555  1.46  
LINK        ZN    ZN B 701                 O07 BJ2 B 702     1555   1555  2.49  
LINK        ZN    ZN B 701                 O06 BJ2 B 702     1555   1555  2.00  
LINK        MG    MG B 704                 O   HOH B 870     1555   1555  2.23  
LINK        MG    MG B 704                 O   HOH B1201     1555   1555  2.25  
LINK        MG    MG B 704                 O   HOH B1267     1555   1555  2.81  
LINK         O4  NAG B 705                 C1  NAG B 706     1555   1555  1.44  
LINK         C1  FUC B 707                 O6  NAG B 708     1555   1555  1.44  
LINK         O4  NAG B 708                 C1  NAG B 709     1555   1555  1.44  
LINK         O4  NAG B 709                 C1  BMA B 710     1555   1555  1.44  
LINK         O4  NAG B 711                 C1  NAG B 712     1555   1555  1.45  
LINK         O6  NAG B 711                 C1  FUC B 713     1555   1555  1.44  
LINK        ZN    ZN C 701                 O06 BJ2 C 702     1555   1555  2.06  
LINK        ZN    ZN C 701                 O07 BJ2 C 702     1555   1555  2.45  
LINK        MG    MG C 704                 O   HOH C 860     1555   1555  2.32  
LINK        MG    MG C 704                 O   HOH C1086     1555   1555  2.20  
LINK        MG    MG C 704                 O   HOH C1232     1555   1555  2.75  
LINK         O4  NAG C 705                 C1  NAG C 706     1555   1555  1.45  
LINK         O4  NAG C 707                 C1  NAG C 708     1555   1555  1.44  
LINK         O4  NAG C 708                 C1  BMA C 709     1555   1555  1.44  
LINK         C1  FUC C 710                 O6  NAG C 711     1555   1555  1.45  
LINK         O4  NAG C 711                 C1  NAG C 712     1555   1555  1.45  
LINK        ZN    ZN D 701                 O06 BJ2 D 702     1555   1555  2.07  
LINK        ZN    ZN D 701                 O07 BJ2 D 702     1555   1555  2.44  
LINK        MG    MG D 704                 O   HOH D1303     1555   1555  2.27  
LINK        MG    MG D 704                 O   HOH D1312     1555   1555  2.66  
LINK        MG    MG D 704                 O   HOH D 908     1555   1555  2.39  
LINK         O4  NAG D 705                 C1  NAG D 706     1555   1555  1.44  
LINK         O4  NAG D 706                 C1  BMA D 707     1555   1555  1.45  
LINK         C1  FUC D 708                 O6  NAG D 709     1555   1555  1.45  
LINK         O4  NAG D 709                 C1  NAG D 710     1555   1555  1.44  
LINK         O4  NAG D 710                 C1  BMA D 711     1555   1555  1.45  
LINK         O3  BMA D 711                 C1  MAN D 713     1555   1555  1.45  
LINK         O6  BMA D 711                 C1  MAN D 712     1555   1555  1.44  
LINK         O4  NAG D 714                 C1  NAG D 715     1555   1555  1.44  
LINK         O6  NAG D 714                 C1  FUC D 716     1555   1555  1.45  
CISPEP   1 ASP A  140    PRO A  141          0         8.50                     
CISPEP   2 TYR A  607    PRO A  608          0         1.57                     
CISPEP   3 ASP B  140    PRO B  141          0         8.38                     
CISPEP   4 TYR B  607    PRO B  608          0         2.85                     
CISPEP   5 ASP C  140    PRO C  141          0         8.90                     
CISPEP   6 TYR C  607    PRO C  608          0         4.28                     
CISPEP   7 ASP D  140    PRO D  141          0         8.87                     
CISPEP   8 TYR D  607    PRO D  608          0        -0.51                     
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  BJ2 A 702                    
SITE     1 AC2 24 GLN A 259  HIS A 331  ALA A 332  SER A 333                    
SITE     2 AC2 24 ALA A 334  HIS A 361  GLU A 362  HIS A 365                    
SITE     3 AC2 24 TYR A 369  GLU A 389  LYS A 489  PHE A 490                    
SITE     4 AC2 24 HIS A 491  TYR A 498  TYR A 501   ZN A 701                    
SITE     5 AC2 24 PEG A 714  EDO A 723  HOH A 810  HOH A 982                    
SITE     6 AC2 24 HOH A 988  HOH A1009  HOH A1014  HOH A1022                    
SITE     1 AC3  3 TYR A 202  ARG A 500  HOH A1173                               
SITE     1 AC4  6 GLU A 262  ASN A 263  ASP A 354  HOH A 919                    
SITE     2 AC4  6 HOH A1231  HOH A1274                                          
SITE     1 AC5  3 TRP A 335  BJ2 A 702  HOH A 842                               
SITE     1 AC6  7 PHE A  33  ALA A  37  TRP A  40  ASP A 342                    
SITE     2 AC6  7 ARG A 344  HOH A1083  HOH A1197                               
SITE     1 AC7  8 ALA A 196  ARG A 199  SER A 204  PRO A 205                    
SITE     2 AC7  8 PHE A 207  HOH A 805  HOH A 827  HOH A 922                    
SITE     1 AC8  8 ARG A 295  GLU A 298  PRO A 308  MET A 309                    
SITE     2 AC8  8 TRP A 314  HOH A1225  HOH A1322  HOH B 903                    
SITE     1 AC9  3 LEU A  32  VAL A 377  ARG A 381                               
SITE     1 AD1  6 PRO A 524  HIS A 526  LEU A 576  NAG A 710                    
SITE     2 AD1  6 HOH A 855  HOH A1141                                          
SITE     1 AD2  3 VAL A 477  THR A 478  FUC A 713                               
SITE     1 AD3  4 SER A 281  LEU A 284  GLN A 285  HOH A1087                    
SITE     1 AD4  2 ASP A 189  PHE A 191                                          
SITE     1 AD5  7 ARG A 381  ARG A 500  BJ2 A 702  HOH A 810                    
SITE     2 AD5  7 HOH A 864  HOH A1009  HOH A1119                               
SITE     1 AD6  4 ARG A 199  GLU A 208  TRP A 447  HOH A 898                    
SITE     1 AD7  5 GLU A 513  GLN A 568  PRO A 569  HOH A 809                    
SITE     2 AD7  5 HOH A 951                                                     
SITE     1 AD8 16 GLN A 286  GLY A 287  TRP A 288  THR A 291                    
SITE     2 AD8 16 HIS A 292  ARG A 295  VAL A 296  GLU A 299                    
SITE     3 AD8 16 ILE A 408  HOH A1261  GLN B 286  GLY B 287                    
SITE     4 AD8 16 HIS B 292  VAL B 296  GLU B 299  ILE B 408                    
SITE     1 AD9  4 HIS B 361  HIS B 365  GLU B 389  BJ2 B 702                    
SITE     1 AE1 23 GLN B 259  HIS B 331  ALA B 332  SER B 333                    
SITE     2 AE1 23 ALA B 334  HIS B 361  GLU B 362  HIS B 365                    
SITE     3 AE1 23 TYR B 369  GLU B 389  LYS B 489  HIS B 491                    
SITE     4 AE1 23 TYR B 498  TYR B 501   ZN B 701  EDO B 719                    
SITE     5 AE1 23 HOH B 842  HOH B 940  HOH B 950  HOH B 979                    
SITE     6 AE1 23 HOH B1055  HOH B1082  HOH B1135                               
SITE     1 AE2  2 TYR B 202  ARG B 500                                          
SITE     1 AE3  6 GLU B 262  ASN B 263  ASP B 354  HOH B 870                    
SITE     2 AE3  6 HOH B1201  HOH B1267                                          
SITE     1 AE4  3 ARG B  96  GLY B 190  PHE B 191                               
SITE     1 AE5  6 PHE B 271  GLU B 419  TRP B 580  GLN B 584                    
SITE     2 AE5  6 HOH B 828  HOH B1151                                          
SITE     1 AE6  6 PHE B  33  ALA B  37  ASP B 342  ARG B 344                    
SITE     2 AE6  6 HOH B 826  HOH B1150                                          
SITE     1 AE7  2 PG4 B 726  HOH B 836                                          
SITE     1 AE8  2 ARG B 235  PG4 B 726                                          
SITE     1 AE9  3 TRP B 335  BJ2 B 702  HOH B1080                               
SITE     1 AF1  3 THR B 534  ALA B 538  HOH B 827                               
SITE     1 AF2  3 ARG B 120  PRO B 170  HOH B1049                               
SITE     1 AF3  2 ARG B 231  LEU B 244                                          
SITE     1 AF4  5 ARG B 199  GLU B 208  TRP B 447  HOH B 994                    
SITE     2 AF4  5 HOH B1043                                                     
SITE     1 AF5  7 TYR A 465  HOH A 880  TYR B 465  HOH B 803                    
SITE     2 AF5  7 HOH B 818  HOH B 904  HOH B 953                               
SITE     1 AF6 10 PHE B 228  ARG B 231  ARG B 235  VAL B 268                    
SITE     2 AF6 10 VAL B 269  ASN B 588  PEG B 717  PEG B 718                    
SITE     3 AF6 10 HOH B 960  HOH B1195                                          
SITE     1 AF7  4 HIS C 361  HIS C 365  GLU C 389  BJ2 C 702                    
SITE     1 AF8 24 GLN C 259  HIS C 331  ALA C 332  SER C 333                    
SITE     2 AF8 24 ALA C 334  HIS C 361  GLU C 362  HIS C 365                    
SITE     3 AF8 24 TYR C 369  GLU C 389  LYS C 489  PHE C 490                    
SITE     4 AF8 24 HIS C 491  TYR C 498  TYR C 501   ZN C 701                    
SITE     5 AF8 24 PEG C 713  HOH C 903  HOH C 994  HOH C1013                    
SITE     6 AF8 24 HOH C1080  HOH C1122  HOH C1163  HOH C1177                    
SITE     1 AF9  2 TYR C 202  ARG C 500                                          
SITE     1 AG1  6 GLU C 262  ASN C 263  ASP C 354  HOH C 860                    
SITE     2 AG1  6 HOH C1086  HOH C1232                                          
SITE     1 AG2  3 TRP C 335  BJ2 C 702  HOH C1295                               
SITE     1 AG3  5 THR C  47  ALA C  48  ARG C 120  THR C 124                    
SITE     2 AG3  5 HOH C 984                                                     
SITE     1 AG4  3 ASP C 189  GLY C 190  PHE C 191                               
SITE     1 AG5  4 GLU C 212  TYR C 440  HOH C 996  ARG D 453                    
SITE     1 AG6  3 GLU C 513  ASP C 566  GLN C 568                               
SITE     1 AG7  3 ASN C 102  GLN C 188  HOH C 878                               
SITE     1 AG8  3 VAL C 477  THR C 478  FUC C 710                               
SITE     1 AG9  2 ASP C 342  ARG C 344                                          
SITE     1 AH1  6 ALA C 519  ARG C 532  SER C 533  THR C 534                    
SITE     2 AH1  6 LYS C 535  HOH C 857                                          
SITE     1 AH2  4 ARG C 199  GLU C 208  TRP C 447  HOH C 973                    
SITE     1 AH3 16 ASP C 462  TYR C 465  LEU C 466  HOH C 803                    
SITE     2 AH3 16 HOH C 841  HOH C 847  HOH C 867  HOH C 870                    
SITE     3 AH3 16 HOH C1140  GLN D 444  GLY D 448  ARG D 453                    
SITE     4 AH3 16 THR D 454  ASP D 462  TYR D 465  HOH D1201                    
SITE     1 AH4  4 HIS D 361  HIS D 365  GLU D 389  BJ2 D 702                    
SITE     1 AH5 23 GLN D 259  HIS D 331  ALA D 332  SER D 333                    
SITE     2 AH5 23 ALA D 334  HIS D 361  GLU D 362  HIS D 365                    
SITE     3 AH5 23 TYR D 369  GLU D 389  LYS D 489  HIS D 491                    
SITE     4 AH5 23 TYR D 498  TYR D 501   ZN D 701  PEG D 717                    
SITE     5 AH5 23 HOH D 872  HOH D 963  HOH D 969  HOH D1057                    
SITE     6 AH5 23 HOH D1131  HOH D1202  HOH D1239                               
SITE     1 AH6  2 TYR D 202  ARG D 500                                          
SITE     1 AH7  6 GLU D 262  ASN D 263  ASP D 354  HOH D 908                    
SITE     2 AH7  6 HOH D1303  HOH D1312                                          
SITE     1 AH8  3 TRP D 335  BJ2 D 702  HOH D1258                               
SITE     1 AH9  1 PHE D 191                                                     
SITE     1 AI1  4 GLU D 305  SER D 307  GLN D 371  ARG D 541                    
SITE     1 AI2  3 TRP D 201  ARG D 381  HOH D1215                               
SITE     1 AI3  5 GLN A  22  ARG D 235  ARG D 236  TYR D 237                    
SITE     2 AI3  5 HOH D 808                                                     
SITE     1 AI4  2 ARG D 199  GLU D 208                                          
SITE     1 AI5  6 LYS A 542  HOH A 869  ASP D 612  LEU D 613                    
SITE     2 AI5  6 HOH D1083  HOH D1087                                          
SITE     1 AI6  8 GLN C 286  HIS C 292  GLN D 286  GLY D 287                    
SITE     2 AI6  8 TRP D 288  HIS D 292  HOH D 829  HOH D1256                    
SITE     1 AI7  5 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 AI7  5 ARG A 326                                                     
SITE     1 AI8 10 ASN A 416  THR A 418  ASP A 421  GLU A 522                    
SITE     2 AI8 10 GLY A 523  PRO A 524  GLN A 527  EDO A 719                    
SITE     3 AI8 10 HOH A 816  HOH A 855                                          
SITE     1 AI9  7 THR A 478  ASN A 480  THR A 482  EDO A 720                    
SITE     2 AI9  7 HOH A 882  ARG B 245  GLU B 596                               
SITE     1 AJ1  4 ASN B  45  THR B  47  ASN B  50  ARG B 326                    
SITE     1 AJ2  7 GLN B   9  ASN B 416  GLU B 522  PRO B 524                    
SITE     2 AJ2  7 GLN B 527  HOH B 877  HOH B1185                               
SITE     1 AJ3  6 ARG A 245  GLU A 596  ASN B 480  THR B 482                    
SITE     2 AJ3  6 HOH B 847  HOH B1199                                          
SITE     1 AJ4  6 ASN C  45  THR C  47  GLU C  49  ASN C  50                    
SITE     2 AJ4  6 ARG C 326  HOH C 833                                          
SITE     1 AJ5  4 ASN C 416  GLU C 522  PRO C 524  GLN C 527                    
SITE     1 AJ6  8 THR C 478  ASN C 480  THR C 482  HIS C 483                    
SITE     2 AJ6  8 EDO C 720  HOH C 933  ARG D 245  GLU D 596                    
SITE     1 AJ7  6 ASN D  45  THR D  47  GLU D  49  ASN D  50                    
SITE     2 AJ7  6 HOH D 931  HOH D1241                                          
SITE     1 AJ8  8 GLN D   9  ASN D 416  GLU D 522  GLY D 523                    
SITE     2 AJ8  8 PRO D 524  GLN D 527  HOH D 966  HOH D1155                    
SITE     1 AJ9  8 ARG C 245  GLU C 596  THR D 478  ASN D 480                    
SITE     2 AJ9  8 THR D 482  HOH D 946  HOH D 975  HOH D1112                    
CRYST1   74.167  103.447  115.446  84.86  85.49  81.99 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      0.013483 -0.001898 -0.000915        0.00000                         
SCALE2      0.000000  0.009762 -0.000779        0.00000                         
SCALE3      0.000000  0.000000  0.008717        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system