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Database: PDB
Entry: 3BKK
LinkDB: 3BKK
Original site: 3BKK 
HEADER    HYDROLASE                               07-DEC-07   3BKK              
TITLE     TESIS ACE CO-CRYSTAL STRUCTURE WITH KETONE ACE INHIBITOR KAF          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PEPTIDASE M2 2 DOMAIN;                                     
COMPND   5 SYNONYM: DIPEPTIDYL CARBOXYPEPTIDASE I,KININASE II,CD143 ANTIGEN;    
COMPND   6 EC: 3.4.15.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACE, DCP, DCP1;                                                
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PLEN-TACEDELTA36-G13                      
KEYWDS    ENZYME-INHIBITOR COMPLEX, GEM-DIOL, DOMAIN-SELECTIVE,                 
KEYWDS   2 CARBOXYPEPTIDASE, GLYCOPROTEIN, HYDROLASE, MEMBRANE, METAL-BINDING,  
KEYWDS   3 METALLOPROTEASE, PHOSPHOPROTEIN, PROTEASE, SECRETED, TRANSMEMBRANE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.WATERMEYER,W.L.KROGER,H.G.O'NEILL,B.T.SEWELL,E.D.STURROCK         
REVDAT   5   25-OCT-17 3BKK    1       SOURCE REMARK                            
REVDAT   4   13-JUL-11 3BKK    1       VERSN                                    
REVDAT   3   24-FEB-09 3BKK    1       VERSN                                    
REVDAT   2   23-SEP-08 3BKK    1       AUTHOR                                   
REVDAT   1   10-JUN-08 3BKK    0                                                
JRNL        AUTH   J.M.WATERMEYER,W.L.KROGER,H.G.O'NEILL,B.T.SEWELL,            
JRNL        AUTH 2 E.D.STURROCK                                                 
JRNL        TITL   PROBING THE BASIS OF DOMAIN-DEPENDENT INHIBITION USING NOVEL 
JRNL        TITL 2 KETONE INHIBITORS OF ANGIOTENSIN-CONVERTING ENZYME           
JRNL        REF    BIOCHEMISTRY                  V.  47  5942 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18457420                                                     
JRNL        DOI    10.1021/BI8002605                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 49749.781                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 31875                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1464                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.17                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2461                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 173                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4777                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 106                                     
REMARK   3   SOLVENT ATOMS            : 229                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.65000                                              
REMARK   3    B22 (A**2) : -1.92000                                             
REMARK   3    B33 (A**2) : -1.73000                                             
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.20                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.051                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.450                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.190 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.920 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.350 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.060 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 36.45                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  5  : N86.PAR_JEAN.TXT                               
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  5   : N86.TOP_JEAN.TXT                               
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3BKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045634.                                   
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, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36183                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45500                            
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 ENTRY 2IUL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PEG 4000, ZNSO4, PH      
REMARK 280  4.7, TEMPERATURE 289K, VAPOR DIFFUSION, HANGING DROP                
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       30.19150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.75300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.53500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.75300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.19150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.53500            
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     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       73.98   -168.82                                   
REMARK 500    ASN A 105       47.31    -65.92                                   
REMARK 500    GLN A 106       17.41   -165.63                                   
REMARK 500    GLU A 123     -128.89     46.21                                   
REMARK 500    GLU A 225       51.24     32.56                                   
REMARK 500    MET A 299       36.33   -141.18                                   
REMARK 500    LYS A 363      -30.87   -132.77                                   
REMARK 500    PHE A 512      -59.92    -27.24                                   
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 HIS A 383   NE2                                                    
REMARK 620 2 HIS A 387   NE2 104.5                                              
REMARK 620 3 GLU A 411   OE1  92.7 103.4                                        
REMARK 620 4 KAF A 704   OAE 111.0 135.2 101.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 691                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 845                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KAF A 704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2IUL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1UZE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2IUX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3BKL   RELATED DB: PDB                                   
DBREF  3BKK A   37   627  UNP    P12821   ACE_HUMAN      642   1232             
SEQADV 3BKK GLY A   64  UNP  P12821    GLU   669 ENGINEERED                     
SEQADV 3BKK GLN A   90  UNP  P12821    ASN   695 ENGINEERED                     
SEQADV 3BKK GLN A  155  UNP  P12821    ASN   760 ENGINEERED                     
SEQADV 3BKK GLN A  337  UNP  P12821    ASN   942 ENGINEERED                     
SEQADV 3BKK 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 3BKK ASN A   72  ASN  GLYCOSYLATION SITE                                 
MODRES 3BKK ASN A  109  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 691      14                                                       
HET    NAG  A 693      14                                                       
HET    NAG  A 694      14                                                       
HET    FUC  A 845      10                                                       
HET    NAG  A 902      15                                                       
HET     ZN  A 701       1                                                       
HET     CL  A 702       1                                                       
HET     CL  A 703       1                                                       
HET    KAF  A 704      36                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     KAF N-{(5S)-4,4-DIHYDROXY-6-PHENYL-5-[(PHENYLCARBONYL)               
HETNAM   2 KAF  AMINO]HEXANOYL}-L-PHENYLALANINE                                 
FORMUL   2  NAG    4(C8 H15 N O6)                                               
FORMUL   3  FUC    C6 H12 O5                                                    
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   8  KAF    C28 H30 N2 O6                                                
FORMUL   9  HOH   *229(H2 O)                                                    
HELIX    1   1 VAL A   38  THR A   71  1                                  34    
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  ALA A  189  1                                  16    
HELIX    8   8 ALA A  189  GLN A  195  1                                   7    
HELIX    9   9 PHE A  196  ASN A  211  1                                  16    
HELIX   10  10 ASP A  215  SER A  222  1                                   8    
HELIX   11  11 MET A  223  GLU A  225  5                                   3    
HELIX   12  12 SER A  228  LEU A  240  1                                  13    
HELIX   13  13 LEU A  240  GLY A  260  1                                  21    
HELIX   14  14 TRP A  283  ASN A  285  5                                   3    
HELIX   15  15 ILE A  286  VAL A  291  1                                   6    
HELIX   16  16 THR A  301  GLN A  308  1                                   8    
HELIX   17  17 THR A  311  LEU A  326  1                                  16    
HELIX   18  18 PRO A  332  SER A  339  1                                   8    
HELIX   19  19 ASN A  374  TYR A  394  1                                  21    
HELIX   20  20 PRO A  398  ARG A  402  5                                   5    
HELIX   21  21 ASN A  406  SER A  422  1                                  17    
HELIX   22  22 THR A  423  LEU A  430  1                                   8    
HELIX   23  23 SER A  439  ILE A  455  1                                  17    
HELIX   24  24 ALA A  456  ASP A  473  1                                  18    
HELIX   25  25 THR A  477  GLU A  479  5                                   3    
HELIX   26  26 ASN A  480  GLY A  494  1                                  15    
HELIX   27  27 PHE A  506  LYS A  511  5                                   6    
HELIX   28  28 TYR A  520  ALA A  541  1                                  22    
HELIX   29  29 PRO A  546  CYS A  550  5                                   5    
HELIX   30  30 SER A  555  LYS A  567  1                                  13    
HELIX   31  31 PRO A  573  GLY A  583  1                                  11    
HELIX   32  32 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  2.04  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03  
LINK         ND2 ASN A  72                 C1  NAG A 691     1555   1555  1.45  
LINK         ND2 ASN A 109                 C1  NAG A 693     1555   1555  1.45  
LINK         NE2 HIS A 383                ZN    ZN A 701     1555   1555  2.14  
LINK         NE2 HIS A 387                ZN    ZN A 701     1555   1555  2.11  
LINK         OE1 GLU A 411                ZN    ZN A 701     1555   1555  2.10  
LINK         O4  NAG A 693                 C1  NAG A 694     1555   1555  1.39  
LINK         O6  NAG A 693                 C1  FUC A 845     1555   1555  1.40  
LINK        ZN    ZN A 701                 OAE KAF A 704     1555   1555  2.07  
CISPEP   1 GLU A  162    PRO A  163          0         0.94                     
SITE     1 AC1  4 ASN A  72  THR A  74  GLU A  76  ARG A 348                    
SITE     1 AC2  1 ASN A 109                                                     
SITE     1 AC3  1 THR A 111                                                     
SITE     1 AC4  2 SER A  45  GLU A  49                                          
SITE     1 AC5  6 ASP A  52  GLN A  56  ASP A 396  LEU A 397                    
SITE     2 AC5  6 PRO A 398  ARG A 402                                          
SITE     1 AC6  3 HIS A 383  HIS A 387  GLU A 411                               
SITE     1 AC7  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC8  5 TYR A 224  PRO A 407  PRO A 519  ILE A 521                    
SITE     2 AC8  5 ARG A 522                                                     
SITE     1 AC9 20 GLN A 281  HIS A 353  ALA A 354  SER A 355                    
SITE     2 AC9 20 ALA A 356  HIS A 383  GLU A 384  HIS A 387                    
SITE     3 AC9 20 PHE A 391  GLU A 411  PHE A 457  LYS A 511                    
SITE     4 AC9 20 PHE A 512  HIS A 513  TYR A 520  TYR A 523                    
SITE     5 AC9 20 HOH A1009  HOH A1081  HOH A1175  HOH A1199                    
CRYST1   60.383   85.070  135.506  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      0.016561  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011755  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007380        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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