GenomeNet

Database: PDB
Entry: 3L3N
LinkDB: 3L3N
Original site: 3L3N 
HEADER    HYDROLASE                               17-DEC-09   3L3N              
TITLE     TESTIS ACE CO-CRYSTAL STRUCTURE WITH NOVEL INHIBITOR LISW             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PEPTIDASE M2 2, RESIDUES 642-1232;                         
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II,            
COMPND   6 ANGIOTENSIN-CONVERTING ENZYME, SOLUBLE FORM;                         
COMPND   7 EC: 3.4.15.1, 3.2.1.-;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACE, DCP, DCP1;                                                
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: CHO-K1;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PLEN                                      
KEYWDS    ENZYME-INHIBITOR COMPLEX, ANGIOTENSIN-CONVERTING ENZYME (ACE)         
KEYWDS   2 INHIBITORS, TESTIS, CARBOXYPEPTIDASE, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.WATERMEYER,W.L.KROGER,H.G.O'NEIL,B.T.SEWELL,E.D.STURROCK          
REVDAT   3   01-NOV-17 3L3N    1       REMARK                                   
REVDAT   2   09-JUN-10 3L3N    1       JRNL                                     
REVDAT   1   28-APR-10 3L3N    0                                                
JRNL        AUTH   J.M.WATERMEYER,W.L.KROGER,H.G.O'NEILL,B.T.SEWELL,            
JRNL        AUTH 2 E.D.STURROCK                                                 
JRNL        TITL   CHARACTERIZATION OF DOMAIN-SELECTIVE INHIBITOR BINDING IN    
JRNL        TITL 2 ANGIOTENSIN-CONVERTING ENZYME USING A NOVEL DERIVATIVE OF    
JRNL        TITL 3 LISINOPRIL.                                                  
JRNL        REF    BIOCHEM.J.                    V. 428    67 2010              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   20233165                                                     
JRNL        DOI    10.1042/BJ20100056                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 25108                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : SAME SET USED AS FOR PDB ID     
REMARK   3                                      1O8A                            
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1294                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3680                       
REMARK   3   BIN FREE R VALUE                    : 0.3330                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4689                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 77                                      
REMARK   3   SOLVENT ATOMS            : 176                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.61500                                              
REMARK   3    B22 (A**2) : -1.73500                                             
REMARK   3    B33 (A**2) : 0.12000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 32.26                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:CARBOHYDRATE.PARAM                  
REMARK   3  PARAMETER FILE  5  : PRES.PAR                                       
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3L3N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000056791.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26578                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR 2.5                                              
REMARK 200 STARTING MODEL: PDB ID 1O8A                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PEG 4000, ZNSO4, PH      
REMARK 280  4.7, 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       28.19150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.97900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.39450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.97900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.19150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.39450            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     GLU A   436                                                      
REMARK 465     GLY A   437                                                      
REMARK 465     GLY A   438                                                      
REMARK 465     GLN A   618                                                      
REMARK 465     TYR A   619                                                      
REMARK 465     ASN A   620                                                      
REMARK 465     TRP A   621                                                      
REMARK 465     THR A   622                                                      
REMARK 465     PRO A   623                                                      
REMARK 465     ASN A   624                                                      
REMARK 465     SER A   625                                                      
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       73.21   -168.30                                   
REMARK 500    ILE A  73       99.03    -67.57                                   
REMARK 500    GLU A 123     -132.75     54.71                                   
REMARK 500    GLN A 155       16.08     54.67                                   
REMARK 500    LYS A 363      -38.54   -132.62                                   
REMARK 500    ASP A 453      -64.47    -96.16                                   
REMARK 500    PHE A 506       75.98   -150.38                                   
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 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 411   OE1                                                    
REMARK 620 2 HIS A 387   NE2 108.1                                              
REMARK 620 3 HIS A 383   NE2  96.0 111.0                                        
REMARK 620 4 LSW A   1   O    93.3 121.2 120.5                                  
REMARK 620 5 LSW A   1   OXT 149.1  95.3  94.0  56.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 845                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LSW A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1UZE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2IUL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3BKK   RELATED DB: PDB                                   
DBREF  3L3N A   37   627  UNP    P12821   ACE_HUMAN      642   1232             
SEQADV 3L3N GLY A   64  UNP  P12821    GLU   669 ENGINEERED                     
SEQADV 3L3N GLN A   90  UNP  P12821    ASN   695 ENGINEERED                     
SEQADV 3L3N GLN A  155  UNP  P12821    ASN   760 ENGINEERED                     
SEQADV 3L3N GLN A  337  UNP  P12821    ASN   942 ENGINEERED                     
SEQADV 3L3N GLN A  586  UNP  P12821    ASN  1191 ENGINEERED                     
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                                      
MODRES 3L3N ASN A  109  ASN  GLYCOSYLATION SITE                                 
HET     ZN  A 701       1                                                       
HET     CL  A 702       1                                                       
HET     CL  A 703       1                                                       
HET    NAG  A 693      14                                                       
HET    NAG  A 694      14                                                       
HET    FUC  A 845      10                                                       
HET    LSW  A   1      36                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     LSW N~2~-[(1S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-                  
HETNAM   2 LSW  TRYPTOPHAN                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL   6  LSW    C27 H34 N4 O5                                                
FORMUL   7  HOH   *176(H2 O)                                                    
HELIX    1   1 ASP A   40  THR A   71  1                                  32    
HELIX    2   2 THR A   74  ARG A  100  1                                  27    
HELIX    3   3 ASN A  109  GLN A  120  1                                  12    
HELIX    4   4 LEU A  122  LEU A  127  5                                   6    
HELIX    5   5 PRO A  128  ALA A  149  1                                  22    
HELIX    6   6 PRO A  163  SER A  172  1                                  10    
HELIX    7   7 LYS A  174  GLN A  195  1                                  22    
HELIX    8   8 PHE A  196  ASN A  211  1                                  16    
HELIX    9   9 ASP A  215  SER A  222  1                                   8    
HELIX   10  10 MET A  223  GLU A  225  5                                   3    
HELIX   11  11 SER A  228  LEU A  240  1                                  13    
HELIX   12  12 LEU A  240  GLY A  260  1                                  21    
HELIX   13  13 TRP A  283  ASN A  285  5                                   3    
HELIX   14  14 ILE A  286  VAL A  291  1                                   6    
HELIX   15  15 ASP A  300  GLN A  308  1                                   9    
HELIX   16  16 THR A  311  LEU A  326  1                                  16    
HELIX   17  17 PRO A  332  SER A  339  1                                   8    
HELIX   18  18 ASN A  374  TYR A  394  1                                  21    
HELIX   19  19 PRO A  398  ARG A  402  5                                   5    
HELIX   20  20 ASN A  406  SER A  422  1                                  17    
HELIX   21  21 THR A  423  LEU A  430  1                                   8    
HELIX   22  22 SER A  439  ILE A  455  1                                  17    
HELIX   23  23 ALA A  456  ASP A  473  1                                  18    
HELIX   24  24 ASN A  480  GLY A  494  1                                  15    
HELIX   25  25 PHE A  506  LYS A  511  5                                   6    
HELIX   26  26 TYR A  520  ALA A  541  1                                  22    
HELIX   27  27 PRO A  546  CYS A  550  5                                   5    
HELIX   28  28 SER A  555  LEU A  568  1                                  14    
HELIX   29  29 PRO A  573  GLY A  583  1                                  11    
HELIX   30  30 ALA A  589  HIS A  610  1                                  22    
SHEET    1   A 2 THR A 150  CYS A 152  0                                        
SHEET    2   A 2 CYS A 158  GLN A 160 -1  O  LEU A 159   N  VAL A 151           
SHEET    1   B 2 ILE A 270  PRO A 271  0                                        
SHEET    2   B 2 LEU A 495  CYS A 496  1  O  CYS A 496   N  ILE A 270           
SHEET    1   C 2 SER A 355  ASP A 358  0                                        
SHEET    2   C 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  2.04  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.02  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03  
LINK         O4  NAG A 693                 C1  NAG A 694     1555   1555  1.37  
LINK         O6  NAG A 693                 C1  FUC A 845     1555   1555  1.40  
LINK         ND2 ASN A 109                 C1  NAG A 693     1555   1555  1.46  
LINK         OE1 GLU A 411                ZN    ZN A 701     1555   1555  1.92  
LINK         NE2 HIS A 387                ZN    ZN A 701     1555   1555  2.09  
LINK         NE2 HIS A 383                ZN    ZN A 701     1555   1555  2.11  
LINK        ZN    ZN A 701                 O   LSW A   1     1555   1555  2.22  
LINK        ZN    ZN A 701                 OXT LSW A   1     1555   1555  2.38  
CISPEP   1 GLU A  162    PRO A  163          0         0.29                     
SITE     1 AC1  4 LSW A   1  HIS A 383  HIS A 387  GLU A 411                    
SITE     1 AC2  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC3  5 TYR A 224  PRO A 519  ILE A 521  ARG A 522                    
SITE     2 AC3  5 HOH A1001                                                     
SITE     1 AC4  3 ASN A 109  NAG A 694  FUC A 845                               
SITE     1 AC5  1 NAG A 693                                                     
SITE     1 AC6  3 SER A  45  GLU A  49  NAG A 693                               
SITE     1 AC7 18 GLN A 281  HIS A 353  ALA A 354  VAL A 380                    
SITE     2 AC7 18 HIS A 383  GLU A 384  HIS A 387  GLU A 411                    
SITE     3 AC7 18 ASP A 415  LYS A 511  PHE A 512  HIS A 513                    
SITE     4 AC7 18 TYR A 520  TYR A 523  PHE A 527   ZN A 701                    
SITE     5 AC7 18 HOH A1159  HOH A1177                                          
CRYST1   56.383   84.789  133.958  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      0.017736  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011794  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007465        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system