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Database: PDB
Entry: 6F9R
LinkDB: 6F9R
Original site: 6F9R 
HEADER    HYDROLASE                               15-DEC-17   6F9R              
TITLE     CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN IN
TITLE    2 COMPLEX WITH SAMPATRILAT-ASP.                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A, B;                                                         
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_TAXID: 10029                                       
KEYWDS    ANGIOTENSIN-1 CONVERTING ENZYME, ACE INHIBITOR, SAMPATRILAT-ASP,      
KEYWDS   2 SAMPATRILAT, HYDROLASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.E.COZIER,K.R.ACHARYA                                                
REVDAT   3   02-MAY-18 6F9R    1       JRNL                                     
REVDAT   2   21-MAR-18 6F9R    1       JRNL                                     
REVDAT   1   07-MAR-18 6F9R    0                                                
JRNL        AUTH   G.E.COZIER,S.L.SCHWAGER,R.K.SHARMA,K.CHIBALE,E.D.STURROCK,   
JRNL        AUTH 2 K.R.ACHARYA                                                  
JRNL        TITL   CRYSTAL STRUCTURES OF SAMPATRILAT AND SAMPATRILAT-ASP IN     
JRNL        TITL 2 COMPLEX WITH HUMAN ACE - A MOLECULAR BASIS FOR DOMAIN        
JRNL        TITL 3 SELECTIVITY.                                                 
JRNL        REF    FEBS J.                       V. 285  1477 2018              
JRNL        REFN                   ISSN 1742-4658                               
JRNL        PMID   29476645                                                     
JRNL        DOI    10.1111/FEBS.14421                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 130790                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2591                            
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 44.3998 -  4.9344    1.00     6819   139  0.1722 0.2017        
REMARK   3     2  4.9344 -  3.9174    0.99     6806   138  0.1510 0.1748        
REMARK   3     3  3.9174 -  3.4224    0.99     6829   123  0.1687 0.1735        
REMARK   3     4  3.4224 -  3.1096    0.99     6788   147  0.1869 0.2041        
REMARK   3     5  3.1096 -  2.8867    0.99     6777   134  0.1967 0.2370        
REMARK   3     6  2.8867 -  2.7166    0.99     6774   148  0.2039 0.2266        
REMARK   3     7  2.7166 -  2.5805    0.99     6723   137  0.2053 0.2735        
REMARK   3     8  2.5805 -  2.4682    0.99     6786   144  0.2041 0.2586        
REMARK   3     9  2.4682 -  2.3732    0.99     6764   127  0.2167 0.2961        
REMARK   3    10  2.3732 -  2.2913    0.99     6748   131  0.2278 0.2737        
REMARK   3    11  2.2913 -  2.2197    0.98     6736   129  0.2311 0.2730        
REMARK   3    12  2.2197 -  2.1562    0.98     6781   135  0.2400 0.2840        
REMARK   3    13  2.1562 -  2.0995    0.98     6712   133  0.2447 0.2762        
REMARK   3    14  2.0995 -  2.0482    0.98     6714   143  0.2496 0.2739        
REMARK   3    15  2.0482 -  2.0017    0.98     6712   138  0.2604 0.2754        
REMARK   3    16  2.0017 -  1.9591    0.98     6668   143  0.2676 0.2655        
REMARK   3    17  1.9591 -  1.9199    0.98     6655   150  0.2796 0.3211        
REMARK   3    18  1.9199 -  1.8837    0.98     6706   129  0.2851 0.2883        
REMARK   3    19  1.8837 -  1.8500    0.97     6701   123  0.3015 0.2773        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.480           
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      :  0.006          11068                                  
REMARK   3   ANGLE     :  0.802          15093                                  
REMARK   3   CHIRALITY :  0.044           1587                                  
REMARK   3   PLANARITY :  0.006           1942                                  
REMARK   3   DIHEDRAL  : 14.078           6455                                  
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 6F9R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007991.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-17                          
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                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7500                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DIALS                              
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 131017                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : NULL                               
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) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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   (%): 55.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS/BICINE PH 8.5, 0.06 M         
REMARK 280  DIVALENT CATIONS, 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                                                    
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 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     PRO A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     ASP A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     VAL A   614                                                      
REMARK 465     THR A   615                                                      
REMARK 465     ASP A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     ALA A   618                                                      
REMARK 465     GLU A   619                                                      
REMARK 465     ALA A   620                                                      
REMARK 465     SER A   621                                                      
REMARK 465     LYS A   622                                                      
REMARK 465     PHE A   623                                                      
REMARK 465     VAL A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     GLU A   626                                                      
REMARK 465     TYR A   627                                                      
REMARK 465     ASP A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     GLU B   609                                                      
REMARK 465     GLY B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     ASP B   612                                                      
REMARK 465     LEU B   613                                                      
REMARK 465     VAL B   614                                                      
REMARK 465     THR B   615                                                      
REMARK 465     ASP B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     ALA B   618                                                      
REMARK 465     GLU B   619                                                      
REMARK 465     ALA B   620                                                      
REMARK 465     SER B   621                                                      
REMARK 465     LYS B   622                                                      
REMARK 465     PHE B   623                                                      
REMARK 465     VAL B   624                                                      
REMARK 465     GLU B   625                                                      
REMARK 465     GLU B   626                                                      
REMARK 465     TYR B   627                                                      
REMARK 465     ASP B   628                                                      
REMARK 465     LEU B   629                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  HD21  ASN B    45     O    HOH B   820              1.60            
REMARK 500   OG1  THR A   282     O    HOH A   801              1.95            
REMARK 500   OE2  GLU A   518     O    HOH A   802              2.15            
REMARK 500   O    HOH B   831     O    HOH B  1018              2.15            
REMARK 500   OE2  GLU A    55     O    HOH A   803              2.18            
REMARK 500   OE1  GLU B   184     O    HOH B   801              2.18            
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       80.84   -175.33                                   
REMARK 500    GLU A 522      -24.42   -142.88                                   
REMARK 500    ASN B  45       83.07   -173.69                                   
REMARK 500    ILE B  79       17.11   -143.72                                   
REMARK 500    SER B 204      116.49   -161.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 714  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 262   OE2                                                    
REMARK 620 2 ASN A 263   OD1 109.2                                              
REMARK 620 3 ASP A 354   OD2  97.7  85.3                                        
REMARK 620 4 HOH A 823   O    83.1 101.4 172.6                                  
REMARK 620 5 HOH A1085   O   169.5  80.5  87.1  91.0                            
REMARK 620 6 HOH A1067   O    82.9 162.2  80.1  92.7  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 709  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 361   NE2                                                    
REMARK 620 2 HIS A 365   NE2 104.7                                              
REMARK 620 3 GLU A 389   OE1  96.5 107.9                                        
REMARK 620 4 D0W A 710   O38 114.7 129.5  98.1                                  
REMARK 620 5 D0W A 710   O37  96.5  88.3 155.9  57.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 715  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 262   OE1                                                    
REMARK 620 2 GLU B 262   OE2  49.4                                              
REMARK 620 3 ASP B 354   OD2  97.0  75.5                                        
REMARK 620 4 HOH B1056   O    82.8 115.7  70.3                                  
REMARK 620 5 HOH B1059   O    75.3 114.9 152.3  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 716  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 262   OE2                                                    
REMARK 620 2 GLU B 262   OE2  87.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 710  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 361   NE2                                                    
REMARK 620 2 HIS B 365   NE2 103.2                                              
REMARK 620 3 GLU B 389   OE1  88.4 100.8                                        
REMARK 620 4 D0W B 711   O37  99.9  93.7 161.2                                  
REMARK 620 5 D0W B 711   O38 115.8 133.7 103.9  57.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D0W A 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 711                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 714                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 715                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 710                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D0W B 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 712                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 715                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 716                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 717                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE8 B 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  707 through NAG A 708 bound to ASN A 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  703 through BMA A 706 bound to ASN A 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  701 through FUC A 702 bound to ASN A 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  701 through NAG B 702 bound to ASN B 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  703 through FUC B 706 bound to ASN B 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  707 through NAG B 709 bound to ASN B 480                            
DBREF  6F9R A    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  6F9R B    1   628  UNP    P12821   ACE_HUMAN       30    657             
SEQADV 6F9R GLN A    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6F9R GLN A   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6F9R GLN A   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6F9R GLN A  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6F9R GLN A  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6F9R ARG A  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6F9R LEU A  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6F9R LEU A  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 6F9R GLN B    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 6F9R GLN B   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 6F9R GLN B   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 6F9R GLN B  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 6F9R GLN B  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 6F9R ARG B  545  UNP  P12821    GLN   574 CONFLICT                       
SEQADV 6F9R LEU B  576  UNP  P12821    PRO   605 CONFLICT                       
SEQADV 6F9R LEU B  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  ASN 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  ASN 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                                          
HET    NAG  A 701      26                                                       
HET    FUC  A 702      20                                                       
HET    NAG  A 703      25                                                       
HET    NAG  A 704      26                                                       
HET    FUC  A 705      20                                                       
HET    BMA  A 706      21                                                       
HET    NAG  A 707      26                                                       
HET    NAG  A 708      27                                                       
HET     ZN  A 709       1                                                       
HET    D0W  A 710      68                                                       
HET     CL  A 711       1                                                       
HET    PEG  A 712      17                                                       
HET    PG4  A 713      31                                                       
HET     MG  A 714       1                                                       
HET    EDO  A 715      10                                                       
HET    ACT  A 716       7                                                       
HET    ACT  A 717       7                                                       
HET    NAG  B 701      27                                                       
HET    NAG  B 702      28                                                       
HET    NAG  B 703      25                                                       
HET    NAG  B 704      26                                                       
HET    BMA  B 705      21                                                       
HET    FUC  B 706      20                                                       
HET    NAG  B 707      25                                                       
HET    FUC  B 708      20                                                       
HET    NAG  B 709      27                                                       
HET     ZN  B 710       1                                                       
HET    D0W  B 711      68                                                       
HET     CL  B 712       1                                                       
HET    PEG  B 713      17                                                       
HET    PEG  B 714      17                                                       
HET     MG  B 715       1                                                       
HET     MG  B 716       1                                                       
HET    EDO  B 717      10                                                       
HET    EDO  B 718      10                                                       
HET    EDO  B 719      10                                                       
HET    EDO  B 720      10                                                       
HET    PE8  B 721      59                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     D0W SAMPATRILAT-ASP                                                  
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM     PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  NAG    11(C8 H15 N O6)                                              
FORMUL   3  FUC    4(C6 H12 O5)                                                 
FORMUL   4  BMA    2(C6 H12 O6)                                                 
FORMUL   6   ZN    2(ZN 2+)                                                     
FORMUL   7  D0W    2(C25 H33 N3 O10)                                            
FORMUL   8   CL    2(CL 1-)                                                     
FORMUL   9  PEG    3(C4 H10 O3)                                                 
FORMUL  10  PG4    C8 H18 O5                                                    
FORMUL  11   MG    3(MG 2+)                                                     
FORMUL  12  EDO    5(C2 H6 O2)                                                  
FORMUL  13  ACT    2(C2 H3 O2 1-)                                               
FORMUL  29  PE8    C16 H34 O9                                                   
FORMUL  30  HOH   *739(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  TYR A  372  1                                  21    
HELIX   18 AB9 PRO A  376  ARG A  380  5                                   5    
HELIX   19 AC1 ASN A  384  SER A  400  1                                  17    
HELIX   20 AC2 THR A  401  ILE A  408  1                                   8    
HELIX   21 AC3 ASP A  417  ILE A  433  1                                  17    
HELIX   22 AC4 ALA A  434  SER A  451  1                                  18    
HELIX   23 AC5 PRO A  455  SER A  457  5                                   3    
HELIX   24 AC6 ARG A  458  GLY A  472  1                                  15    
HELIX   25 AC7 PHE A  484  LYS A  489  5                                   6    
HELIX   26 AC8 TYR A  498  ALA A  519  1                                  22    
HELIX   27 AC9 PRO A  524  CYS A  528  5                                   5    
HELIX   28 AD1 SER A  533  GLY A  547  1                                  15    
HELIX   29 AD2 PRO A  551  GLY A  561  1                                  11    
HELIX   30 AD3 ALA A  567  ASN A  588  1                                  22    
HELIX   31 AD4 ASP B    2  GLN B    6  5                                   5    
HELIX   32 AD5 ASP B   13  THR B   44  1                                  32    
HELIX   33 AD6 THR B   47  GLU B   77  1                                  31    
HELIX   34 AD7 ILE B   79  PHE B   83  5                                   5    
HELIX   35 AD8 ASP B   85  ARG B   96  1                                  12    
HELIX   36 AD9 LEU B   98  LEU B  103  5                                   6    
HELIX   37 AE1 PRO B  104  ALA B  125  1                                  22    
HELIX   38 AE2 PRO B  141  SER B  150  1                                  10    
HELIX   39 AE3 SER B  152  GLN B  188  1                                  37    
HELIX   40 AE4 ASP B  193  TRP B  201  1                                   9    
HELIX   41 AE5 THR B  206  GLY B  238  1                                  33    
HELIX   42 AE6 TRP B  261  ASN B  263  5                                   3    
HELIX   43 AE7 ILE B  264  VAL B  269  1                                   6    
HELIX   44 AE8 VAL B  279  GLY B  287  1                                   9    
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  GLY B  452  1                                  19    
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    
SHEET    1 AA1 2 VAL A 127  CYS A 128  0                                        
SHEET    2 AA1 2 CYS A 136  TRP A 137 -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 LYS B 126  CYS B 128  0                                        
SHEET    2 AA4 2 CYS B 136  SER B 138 -1  O  TRP B 137   N  VAL B 127           
SHEET    1 AA5 2 ILE B 248  PRO B 249  0                                        
SHEET    2 AA5 2 ILE B 473  CYS B 474  1  O  CYS B 474   N  ILE B 248           
SHEET    1 AA6 2 SER B 333  ASP B 336  0                                        
SHEET    2 AA6 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.04  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.06  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.04  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.06  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.05  
LINK         ND2 ASN A  45                 C1  NAG A 707     1555   1555  1.44  
LINK         OE2 GLU A 262                MG    MG A 714     1555   1555  2.32  
LINK         OD1 ASN A 263                MG    MG A 714     1555   1555  2.48  
LINK         OD2 ASP A 354                MG    MG A 714     1555   1555  2.77  
LINK         NE2 HIS A 361                ZN    ZN A 709     1555   1555  1.95  
LINK         NE2 HIS A 365                ZN    ZN A 709     1555   1555  1.96  
LINK         OE1 GLU A 389                ZN    ZN A 709     1555   1555  1.83  
LINK         ND2 ASN A 416                 C1  NAG A 703     1555   1555  1.44  
LINK         ND2 ASN A 480                 C1  NAG A 701     1555   1555  1.43  
LINK         ND2 ASN B  45                 C1  NAG B 701     1555   1555  1.44  
LINK         OE1AGLU B 262                MG    MG B 715     1555   1555  2.71  
LINK         OE2AGLU B 262                MG    MG B 715     1555   1555  2.51  
LINK         OE2AGLU B 262                MG    MG B 716     1555   1555  2.60  
LINK         OE2BGLU B 262                MG    MG B 716     1555   1555  2.78  
LINK         OD2 ASP B 354                MG    MG B 715     1555   1555  2.54  
LINK         NE2 HIS B 361                ZN    ZN B 710     1555   1555  2.11  
LINK         NE2 HIS B 365                ZN    ZN B 710     1555   1555  1.98  
LINK         OE1 GLU B 389                ZN    ZN B 710     1555   1555  1.95  
LINK         ND2 ASN B 416                 C1  NAG B 703     1555   1555  1.43  
LINK         ND2 ASN B 480                 C1  NAG B 707     1555   1555  1.44  
LINK         O6  NAG A 701                 C1  FUC A 702     1555   1555  1.46  
LINK         O4  NAG A 703                 C1  NAG A 704     1555   1555  1.43  
LINK         O6  NAG A 703                 C1  FUC A 705     1555   1555  1.45  
LINK         O4  NAG A 704                 C1  BMA A 706     1555   1555  1.45  
LINK         O4  NAG A 707                 C1  NAG A 708     1555   1555  1.44  
LINK        ZN    ZN A 709                 O38 D0W A 710     1555   1555  2.01  
LINK        ZN    ZN A 709                 O37 D0W A 710     1555   1555  2.38  
LINK        MG    MG A 714                 O   HOH A 823     1555   1555  2.25  
LINK        MG    MG A 714                 O   HOH A1085     1555   1555  2.68  
LINK        MG    MG A 714                 O   HOH A1067     1555   1555  2.37  
LINK         O4  NAG B 701                 C1  NAG B 702     1555   1555  1.44  
LINK         O4  NAG B 703                 C1  NAG B 704     1555   1555  1.44  
LINK         O6  NAG B 703                 C1  FUC B 706     1555   1555  1.45  
LINK         O4  NAG B 704                 C1  BMA B 705     1555   1555  1.44  
LINK         O4  NAG B 707                 C1  NAG B 709     1555   1555  1.44  
LINK         O6  NAG B 707                 C1  FUC B 708     1555   1555  1.44  
LINK        ZN    ZN B 710                 O37 D0W B 711     1555   1555  2.54  
LINK        ZN    ZN B 710                 O38 D0W B 711     1555   1555  1.86  
LINK        MG    MG B 715                 O   HOH B1056     1555   1555  2.50  
LINK        MG    MG B 715                 O   HOH B1059     1555   1555  2.28  
CISPEP   1 ASP A  140    PRO A  141          0         8.41                     
CISPEP   2 TYR A  607    PRO A  608          0        -0.54                     
CISPEP   3 ASP B  140    PRO B  141          0         7.51                     
CISPEP   4 TYR B  607    PRO B  608          0        -5.91                     
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  D0W A 710                    
SITE     1 AC2 21 GLN A 259  HIS A 331  ALA A 332  SER A 333                    
SITE     2 AC2 21 ALA A 334  THR A 358  HIS A 361  GLU A 362                    
SITE     3 AC2 21 HIS A 365  TYR A 369  GLU A 389  ASP A 393                    
SITE     4 AC2 21 LYS A 489  HIS A 491  TYR A 498  TYR A 501                    
SITE     5 AC2 21  ZN A 709  HOH A 813  HOH A 919  HOH A 951                    
SITE     6 AC2 21 HOH A 985                                                     
SITE     1 AC3  4 TYR A 202  PRO A 497  ARG A 500  HOH A1028                    
SITE     1 AC4  5 TYR A  24  LEU A  32  TYR A 338  VAL A 377                    
SITE     2 AC4  5 ARG A 381                                                     
SITE     1 AC5 12 ARG A 453  TYR A 465  HOH A 814  HOH A 819                    
SITE     2 AC5 12 HOH A 870  GLY B 448  THR B 454  ASP B 462                    
SITE     3 AC5 12 TYR B 465  HOH B 829  HOH B 879  HOH B1017                    
SITE     1 AC6  6 GLU A 262  ASN A 263  ASP A 354  HOH A 823                    
SITE     2 AC6  6 HOH A1067  HOH A1085                                          
SITE     1 AC7  2 GLU A 513  ASP A 566                                          
SITE     1 AC8  1 LYS A 187                                                     
SITE     1 AC9  4 ARG A 199  GLU A 208  HOH A 846  HOH A 871                    
SITE     1 AD1  4 HIS B 361  HIS B 365  GLU B 389  D0W B 711                    
SITE     1 AD2 22 GLN B 259  HIS B 331  ALA B 332  SER B 333                    
SITE     2 AD2 22 ALA B 334  THR B 358  HIS B 361  GLU B 362                    
SITE     3 AD2 22 HIS B 365  TYR B 369  GLU B 389  ASP B 393                    
SITE     4 AD2 22 LYS B 489  HIS B 491  TYR B 498  TYR B 501                    
SITE     5 AD2 22 PHE B 505   ZN B 710  HOH B 869  HOH B 986                    
SITE     6 AD2 22 HOH B1054  HOH B1088                                          
SITE     1 AD3  3 TYR B 202  PRO B 497  ARG B 500                               
SITE     1 AD4  1 ARG B 295                                                     
SITE     1 AD5  7 PHE B 228  ARG B 231  VAL B 268  VAL B 269                    
SITE     2 AD5  7 ASN B 588  HOH B 915  HOH B1082                               
SITE     1 AD6  5 GLU B 262  ASN B 263  ASP B 354  HOH B1056                    
SITE     2 AD6  5 HOH B1059                                                     
SITE     1 AD7  3 GLU B 262  ASN B 263  ASP B 354                               
SITE     1 AD8  3 TRP B 201  ARG B 381  HOH B1042                               
SITE     1 AD9  3 ARG B  96  GLY B 190  PHE B 191                               
SITE     1 AE1  5 ILE B  46  THR B  47  ALA B  48  ARG B 120                    
SITE     2 AE1  5 HOH B 990                                                     
SITE     1 AE2  3 LEU B 284  GLY B 287  TRP B 288                               
SITE     1 AE3 11 GLN A 286  TRP A 288  HIS A 292  ARG A 295                    
SITE     2 AE3 11 VAL A 296  GLN B 286  GLY B 287  TRP B 288                    
SITE     3 AE3 11 HIS B 292  VAL B 296  GLU B 299                               
SITE     1 AE4  5 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 AE4  5 ARG A 326                                                     
SITE     1 AE5  6 ASN A 416  ASP A 417  THR A 418  GLU A 522                    
SITE     2 AE5  6 PRO A 524  GLN A 527                                          
SITE     1 AE6  8 THR A 478  ASN A 480  THR A 482  HIS A 483                    
SITE     2 AE6  8 HOH A 835  HOH A 884  ARG B 245  GLU B 596                    
SITE     1 AE7  3 ASN B  45  THR B  47  ASN B  50                               
SITE     1 AE8  8 PHE B  10  GLU B 403  ASN B 416  GLU B 522                    
SITE     2 AE8  8 PRO B 524  GLN B 527  HOH B 846  HOH B1036                    
SITE     1 AE9  6 ARG A 245  GLU A 596  THR B 478  ASN B 480                    
SITE     2 AE9  6 THR B 482  HOH B1001                                          
CRYST1   72.591   76.966   82.637  88.43  64.40  75.32 P 1           2          
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      0.013776 -0.003609 -0.006972        0.00000                         
SCALE2      0.000000  0.013431  0.001271        0.00000                         
SCALE3      0.000000  0.000000  0.013478        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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