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Database: PDB
Entry: 6F9U
LinkDB: 6F9U
Original site: 6F9U 
HEADER    HYDROLASE                               15-DEC-17   6F9U              
TITLE     CRYSTAL STRUCTURE OF HUMAN TESTIS ANGIOTENSIN-1 CONVERTING ENZYME IN  
TITLE    2 COMPLEX WITH SAMPATRILAT-ASP.                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
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,          
KEYWDS   2 SAMPATRILAT-ASP, HYDROLASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.E.COZIER,K.R.ACHARYA                                                
REVDAT   3   02-MAY-18 6F9U    1       JRNL                                     
REVDAT   2   21-MAR-18 6F9U    1       JRNL                                     
REVDAT   1   07-MAR-18 6F9U    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.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 72.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 51651                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2599                            
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 72.2246 -  5.0695    1.00     2769   162  0.1708 0.1965        
REMARK   3     2  5.0695 -  4.0239    1.00     2649   140  0.1290 0.1432        
REMARK   3     3  4.0239 -  3.5153    1.00     2615   148  0.1409 0.1783        
REMARK   3     4  3.5153 -  3.1939    1.00     2626   136  0.1591 0.2089        
REMARK   3     5  3.1939 -  2.9649    1.00     2577   138  0.1776 0.2462        
REMARK   3     6  2.9649 -  2.7901    1.00     2588   143  0.1706 0.2057        
REMARK   3     7  2.7901 -  2.6504    1.00     2607   117  0.1653 0.2354        
REMARK   3     8  2.6504 -  2.5350    1.00     2566   137  0.1579 0.1932        
REMARK   3     9  2.5350 -  2.4374    1.00     2539   142  0.1623 0.2200        
REMARK   3    10  2.4374 -  2.3533    1.00     2590   134  0.1592 0.2394        
REMARK   3    11  2.3533 -  2.2797    1.00     2578   125  0.1702 0.2101        
REMARK   3    12  2.2797 -  2.2145    1.00     2548   131  0.1771 0.2335        
REMARK   3    13  2.2145 -  2.1562    1.00     2536   138  0.1792 0.2198        
REMARK   3    14  2.1562 -  2.1036    1.00     2557   141  0.1954 0.2500        
REMARK   3    15  2.1036 -  2.0558    1.00     2557   133  0.2009 0.2579        
REMARK   3    16  2.0558 -  2.0120    1.00     2520   138  0.2194 0.2572        
REMARK   3    17  2.0120 -  1.9718    1.00     2541   151  0.2350 0.2804        
REMARK   3    18  1.9718 -  1.9346    1.00     2541   123  0.2575 0.2953        
REMARK   3    19  1.9346 -  1.9000    1.00     2548   122  0.2703 0.3566        
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) : 20.630           
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      :  0.007           5132                                  
REMARK   3   ANGLE     :  0.848           6971                                  
REMARK   3   CHIRALITY :  0.046            737                                  
REMARK   3   PLANARITY :  0.006            891                                  
REMARK   3   DIHEDRAL  : 15.968           3014                                  
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 6F9U 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_1200007978.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
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   : 51795                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 25.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 21.70                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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: 1O8A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MIB BUFFER PH 4.0, 5% GLYCEROL,    
REMARK 280  15% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.15800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.61650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.93050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.61650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.15800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.93050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 21.0 KCAL/MOL                         
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 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     LEU A    37                                                      
REMARK 465     VAL A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     ALA A   626                                                      
REMARK 465     ARG A   627                                                      
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  72       79.62   -169.27                                   
REMARK 500    GLU A 123     -136.35     56.08                                   
REMARK 500    ALA A 296       74.09   -112.82                                   
REMARK 500    LYS A 363      -26.25   -143.93                                   
REMARK 500    SER A 439      109.39   -164.90                                   
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                              ZN A 707  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 383   NE2                                                    
REMARK 620 2 HIS A 387   NE2 107.3                                              
REMARK 620 3 GLU A 411   OE1  93.8 106.3                                        
REMARK 620 4 D0W A 711   O38  94.1  92.0 156.8                                  
REMARK 620 5 D0W A 711   O37 112.2 129.7 100.9  56.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 707                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 708                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 709                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D0W A 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BO3 A 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 714                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 716                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 718                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 719                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 720                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 721                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 706 bound   
REMARK 800  to ASN A 72                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  701 through MAN A 705 bound to ASN A 109                            
DBREF  6F9U A   37   627  UNP    P12821   ACE_HUMAN      642   1232             
SEQADV 6F9U GLY A   64  UNP  P12821    GLU   669 CONFLICT                       
SEQADV 6F9U GLN A   90  UNP  P12821    ASN   695 CONFLICT                       
SEQADV 6F9U GLN A  155  UNP  P12821    ASN   760 CONFLICT                       
SEQADV 6F9U GLN A  337  UNP  P12821    ASN   942 CONFLICT                       
SEQADV 6F9U GLN A  586  UNP  P12821    ASN  1191 CONFLICT                       
SEQRES   1 A  591  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU          
SEQRES   2 A  591  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR          
SEQRES   3 A  591  ALA GLY ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR          
SEQRES   4 A  591  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE          
SEQRES   5 A  591  ALA GLN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS          
SEQRES   6 A  591  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG          
SEQRES   7 A  591  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU          
SEQRES   8 A  591  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU          
SEQRES   9 A  591  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS          
SEQRES  10 A  591  PRO GLN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR          
SEQRES  11 A  591  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU          
SEQRES  12 A  591  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA          
SEQRES  13 A  591  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN          
SEQRES  14 A  591  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP          
SEQRES  15 A  591  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN          
SEQRES  16 A  591  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR          
SEQRES  17 A  591  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG          
SEQRES  18 A  591  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE          
SEQRES  19 A  591  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP          
SEQRES  20 A  591  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA          
SEQRES  21 A  591  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY          
SEQRES  22 A  591  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE          
SEQRES  23 A  591  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE          
SEQRES  24 A  591  TRP GLN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG          
SEQRES  25 A  591  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN          
SEQRES  26 A  591  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN          
SEQRES  27 A  591  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS          
SEQRES  28 A  591  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA          
SEQRES  29 A  591  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE          
SEQRES  30 A  591  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS          
SEQRES  31 A  591  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER          
SEQRES  32 A  591  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU          
SEQRES  33 A  591  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP          
SEQRES  34 A  591  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS          
SEQRES  35 A  591  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS          
SEQRES  36 A  591  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY          
SEQRES  37 A  591  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER          
SEQRES  38 A  591  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN          
SEQRES  39 A  591  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS          
SEQRES  40 A  591  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS          
SEQRES  41 A  591  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY          
SEQRES  42 A  591  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR          
SEQRES  43 A  591  GLY GLN PRO GLN MET SER ALA SER ALA MET LEU SER TYR          
SEQRES  44 A  591  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU          
SEQRES  45 A  591  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP          
SEQRES  46 A  591  THR PRO ASN SER ALA ARG                                      
HET    NAG  A 701      25                                                       
HET    NAG  A 702      26                                                       
HET    BMA  A 703      20                                                       
HET    FUC  A 704      20                                                       
HET    MAN  A 705      21                                                       
HET    NAG  A 706      27                                                       
HET     ZN  A 707       1                                                       
HET     CL  A 708       1                                                       
HET     CL  A 709       1                                                       
HET    1PE  A 710      38                                                       
HET    D0W  A 711      68                                                       
HET    BO3  A 712       7                                                       
HET    IMD  A 713      10                                                       
HET    IMD  A 714      10                                                       
HET    EDO  A 715      10                                                       
HET    EDO  A 716      10                                                       
HET    EDO  A 717      10                                                       
HET    EDO  A 718      10                                                       
HET    EDO  A 719      10                                                       
HET    EDO  A 720      10                                                       
HET    PEG  A 721      17                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     D0W SAMPATRILAT-ASP                                                  
HETNAM     BO3 BORIC ACID                                                       
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     1PE PEG400                                                           
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   2  BMA    C6 H12 O6                                                    
FORMUL   2  FUC    C6 H12 O5                                                    
FORMUL   2  MAN    C6 H12 O6                                                    
FORMUL   4   ZN    ZN 2+                                                        
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7  1PE    C10 H22 O6                                                   
FORMUL   8  D0W    C25 H33 N3 O10                                               
FORMUL   9  BO3    B H3 O3                                                      
FORMUL  10  IMD    2(C3 H5 N2 1+)                                               
FORMUL  12  EDO    6(C2 H6 O2)                                                  
FORMUL  18  PEG    C4 H10 O3                                                    
FORMUL  19  HOH   *341(H2 O)                                                    
HELIX    1 AA1 ASP A   40  THR A   71  1                                  32    
HELIX    2 AA2 THR A   74  ARG A  100  1                                  27    
HELIX    3 AA3 LYS A  101  PHE A  102  5                                   2    
HELIX    4 AA4 ASP A  103  LEU A  107  5                                   5    
HELIX    5 AA5 ASN A  109  GLN A  120  1                                  12    
HELIX    6 AA6 LEU A  122  LEU A  127  5                                   6    
HELIX    7 AA7 PRO A  128  ALA A  149  1                                  22    
HELIX    8 AA8 PRO A  163  SER A  172  1                                  10    
HELIX    9 AA9 LYS A  174  ALA A  189  1                                  16    
HELIX   10 AB1 ALA A  189  LEU A  194  1                                   6    
HELIX   11 AB2 PHE A  196  ASN A  211  1                                  16    
HELIX   12 AB3 ASP A  215  MET A  223  1                                   9    
HELIX   13 AB4 SER A  228  GLY A  260  1                                  33    
HELIX   14 AB5 TRP A  283  ASN A  285  5                                   3    
HELIX   15 AB6 ILE A  286  VAL A  291  1                                   6    
HELIX   16 AB7 ASP A  300  GLN A  308  1                                   9    
HELIX   17 AB8 THR A  311  LEU A  326  1                                  16    
HELIX   18 AB9 PRO A  332  SER A  339  1                                   8    
HELIX   19 AC1 ASN A  374  TYR A  394  1                                  21    
HELIX   20 AC2 PRO A  398  ARG A  402  5                                   5    
HELIX   21 AC3 ASN A  406  SER A  422  1                                  17    
HELIX   22 AC4 THR A  423  LEU A  430  1                                   8    
HELIX   23 AC5 SER A  439  ILE A  455  1                                  17    
HELIX   24 AC6 ALA A  456  ASP A  473  1                                  18    
HELIX   25 AC7 ASN A  480  GLY A  494  1                                  15    
HELIX   26 AC8 PHE A  506  LYS A  511  5                                   6    
HELIX   27 AC9 TYR A  520  ALA A  541  1                                  22    
HELIX   28 AD1 PRO A  546  CYS A  550  5                                   5    
HELIX   29 AD2 SER A  555  LEU A  568  1                                  14    
HELIX   30 AD3 PRO A  573  GLY A  583  1                                  11    
HELIX   31 AD4 ALA A  589  HIS A  610  1                                  22    
SHEET    1 AA1 2 THR A 150  CYS A 152  0                                        
SHEET    2 AA1 2 CYS A 158  GLN A 160 -1  O  LEU A 159   N  VAL A 151           
SHEET    1 AA2 2 ILE A 270  PRO A 271  0                                        
SHEET    2 AA2 2 LEU A 495  CYS A 496  1  O  CYS A 496   N  ILE A 270           
SHEET    1 AA3 2 SER A 355  ASP A 358  0                                        
SHEET    2 AA3 2 PHE A 365  LYS A 368 -1  O  ARG A 366   N  TRP A 357           
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.05  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.05  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.04  
LINK         ND2 ASN A  72                 C1  NAG A 706     1555   1555  1.43  
LINK         ND2 ASN A 109                 C1  NAG A 701     1555   1555  1.43  
LINK         NE2 HIS A 383                ZN    ZN A 707     1555   1555  2.04  
LINK         NE2 HIS A 387                ZN    ZN A 707     1555   1555  1.98  
LINK         OE1 GLU A 411                ZN    ZN A 707     1555   1555  1.97  
LINK         O4  NAG A 701                 C1  NAG A 702     1555   1555  1.43  
LINK         O6  NAG A 701                 C1  FUC A 704     1555   1555  1.44  
LINK         O4  NAG A 702                 C1  BMA A 703     1555   1555  1.44  
LINK         O6  BMA A 703                 C1  MAN A 705     1555   1555  1.45  
LINK        ZN    ZN A 707                 O38 D0W A 711     1555   1555  2.56  
LINK        ZN    ZN A 707                 O37 D0W A 711     1555   1555  2.07  
CISPEP   1 GLU A  162    PRO A  163          0         2.35                     
SITE     1 AC1  4 HIS A 383  HIS A 387  GLU A 411  D0W A 711                    
SITE     1 AC2  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC3  4 TYR A 224  PRO A 519  ARG A 522  HOH A 999                    
SITE     1 AC4  7 TYR A 287  LEU A 375  LYS A 449  ASP A 453                    
SITE     2 AC4  7 BO3 A 712  HOH A 832  HOH A 835                               
SITE     1 AC5 15 GLN A 281  HIS A 353  ALA A 354  SER A 355                    
SITE     2 AC5 15 ALA A 356  HIS A 383  GLU A 384  HIS A 387                    
SITE     3 AC5 15 GLU A 411  LYS A 511  HIS A 513  TYR A 520                    
SITE     4 AC5 15 TYR A 523   ZN A 707  HOH A 824                               
SITE     1 AC6  8 TYR A 287  SER A 298  LEU A 433  GLU A 436                    
SITE     2 AC6  8 HIS A 442  1PE A 710  HOH A 804  HOH A 844                    
SITE     1 AC7  3 TYR A  62  ASN A  85  ARG A 124                               
SITE     1 AC8  6 GLU A 183  ASP A 187  PRO A 500  ARG A 501                    
SITE     2 AC8  6 THR A 502  ASP A 505                                          
SITE     1 AC9  3 GLY A 615  TRP A 616  HOH A 970                               
SITE     1 AD1  4 SER A 339  MET A 340  LEU A 341  GLU A 342                    
SITE     1 AD2  2 CYS A 152  LYS A 188                                          
SITE     1 AD3  1 ASN A 211                                                     
SITE     1 AD4  2 ASP A 141  THR A 145                                          
SITE     1 AD5  4 ASN A  72  THR A  74  GLU A  76  ARG A 348                    
SITE     1 AD6  8 GLU A  43  SER A  45  VAL A  48  GLU A  49                    
SITE     2 AD6  8 ASN A 109  ASP A 396  HOH A 813  HOH A1075                    
CRYST1   56.316   85.861  133.233  90.00  90.00  90.00 P 21 21 21    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      0.017757  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007506        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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