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Database: PDB
Entry: 4CA6
LinkDB: 4CA6
Original site: 4CA6 
HEADER    HYDROLASE                               07-OCT-13   4CA6              
TITLE     HUMAN ANGIOTENSIN CONVERTING ENZYME N-DOMAIN IN COMPLEX WITH A        
TITLE    2 PHOSPHINIC TRIPEPTIDE FI                                             
CAVEAT     4CA6    NAG A 1616 HAS WRONG CHIRALITY AT ATOM C1                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME N-DOMAIN;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 30-639;                                           
COMPND   5 EC: 3.4.15.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO                                     
KEYWDS    HYDROLASE, ZINC METALLOPEPTIDASE, INHIBITOR BINDING                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MASUYER,M.AKIF,B.CZARNY,F.BEAU,S.L.U.SCHWAGER,E.D.STURROCK,         
AUTHOR   2 R.E.ISAAC,V.DIVE,K.R.ACHARYA                                         
REVDAT   3   21-NOV-18 4CA6    1       CAVEAT JRNL   REMARK LINK                
REVDAT   2   12-FEB-14 4CA6    1       JRNL                                     
REVDAT   1   11-DEC-13 4CA6    0                                                
JRNL        AUTH   G.MASUYER,M.AKIF,B.CZARNY,F.BEAU,S.L.SCHWAGER,E.D.STURROCK,  
JRNL        AUTH 2 R.E.ISAAC,V.DIVE,K.R.ACHARYA                                 
JRNL        TITL   CRYSTAL STRUCTURES OF HIGHLY SPECIFIC PHOSPHINIC TRIPEPTIDE  
JRNL        TITL 2 ENANTIOMERS IN COMPLEX WITH THE ANGIOTENSIN-I CONVERTING     
JRNL        TITL 3 ENZYME.                                                      
JRNL        REF    FEBS J.                       V. 281   943 2014              
JRNL        REFN                   ISSN 1742-4658                               
JRNL        PMID   24289879                                                     
JRNL        DOI    10.1111/FEBS.12660                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 109477                         
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 + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5779                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.91                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.96                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7074                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 372                          
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9917                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 369                                     
REMARK   3   SOLVENT ATOMS            : 594                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : 0.40000                                              
REMARK   3    B12 (A**2) : 2.04000                                              
REMARK   3    B13 (A**2) : 0.63000                                              
REMARK   3    B23 (A**2) : -0.37000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.150         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.139         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.102         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.980         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10638 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14483 ; 1.350 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1218 ; 5.313 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   532 ;35.672 ;23.759       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1609 ;14.334 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    66 ;15.572 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1514 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8266 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    30        A  1626                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6929 -15.2834 -18.5488              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0237 T22:   0.0852                                     
REMARK   3      T33:   0.0280 T12:  -0.0133                                     
REMARK   3      T13:   0.0128 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3117 L22:   0.4220                                     
REMARK   3      L33:   0.0230 L12:  -0.1010                                     
REMARK   3      L13:  -0.0735 L23:   0.0472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0493 S12:  -0.0082 S13:  -0.0234                       
REMARK   3      S21:  -0.0572 S22:  -0.0415 S23:   0.0023                       
REMARK   3      S31:  -0.0204 S32:  -0.0004 S33:  -0.0078                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    30        B  1624                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9989  14.6284  18.6528              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0271 T22:   0.0520                                     
REMARK   3      T33:   0.0432 T12:  -0.0353                                     
REMARK   3      T13:   0.0174 T23:  -0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0823 L22:   0.4502                                     
REMARK   3      L33:   0.7934 L12:  -0.1871                                     
REMARK   3      L13:  -0.0931 L23:   0.3276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0093 S12:   0.0083 S13:  -0.0116                       
REMARK   3      S21:  -0.0109 S22:  -0.0335 S23:   0.0211                       
REMARK   3      S31:   0.0013 S32:  -0.0526 S33:   0.0242                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4CA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290058645.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : 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 PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 115256                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.910                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: PDB ENTRY 2XYD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.06 M DIVALENT CATIONS, 0.1 M           
REMARK 280  TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 132    CG   CD   CE   NZ                                   
REMARK 470     GLN B  70    CD   OE1  NE2                                       
REMARK 470     PRO B 130    CG   CD                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   416     O5   NAG A  1616              1.46            
REMARK 500   CG   ASN A   416     C1   NAG A  1616              1.64            
REMARK 500   OD1  ASN A   416     C1   NAG A  1616              1.68            
REMARK 500   O    HOH B  2129     O    HOH B  2130              2.07            
REMARK 500   OE2  GLU B   262     O    HOH B  2129              2.11            
REMARK 500   OG   SER B   260     OE1  GLU B   262              2.15            
REMARK 500   OD1  ASN A   416     C2   NAG A  1616              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 130   N   -  CA  -  CB  ANGL. DEV. =   7.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  45       77.47   -171.23                                   
REMARK 500    ASN A 203       52.67     35.73                                   
REMARK 500    ARG A 340       16.92     57.26                                   
REMARK 500    LYS A 341      -41.51   -132.70                                   
REMARK 500    ARG A 413      124.61    -33.27                                   
REMARK 500    ASN A 416       48.75    -87.09                                   
REMARK 500    ASN B  45       78.58   -174.03                                   
REMARK 500    ALA B 134     -137.21    -98.98                                   
REMARK 500    ASN B 203       54.70     33.31                                   
REMARK 500    ASP B 324     -172.43    -66.90                                   
REMARK 500    GLN B 575      -54.46    -26.98                                   
REMARK 500    ASP B 605      -75.63    -35.86                                   
REMARK 500    ASN B 606       50.81   -114.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 5,6-DIHYDRO-BENZO[H]CINNOLIN-3-YLAMINE (3EF): CORRESPOND TO          
REMARK 600  ENANTIOMER OF COMPOUND 3ES IN PDB 2XYD                              
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 A 1625                                                       
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 A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 3EF A1630   OAD                                                    
REMARK 620 2 3EF A1630   OAG  64.6                                              
REMARK 620 3 GLU A 389   OE1 101.7 166.2                                        
REMARK 620 4 HIS A 365   NE2 136.4  88.4 101.7                                  
REMARK 620 5 HIS A 361   NE2 108.5  95.0  91.1 107.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 3EF B1630   PBY                                                    
REMARK 620 2 3EF B1630   OAG  33.1                                              
REMARK 620 3 3EF B1630   OAD  33.6  66.6                                        
REMARK 620 4 GLU B 389   OE1 133.7 166.7 100.5                                  
REMARK 620 5 HIS B 365   NE2 114.2  87.7 140.3 101.4                            
REMARK 620 6 HIS B 361   NE2 105.2  95.2 106.3  91.7 105.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: N-{(2S)-3-[(S)-[(1R)-1-{[(BENZYLOXY)CARBONYL]AMINO}-  
REMARK 630 2-PHENYLETHYL](HYDROXY)PHOSPHORYL]-2-[(3-PHENYL-1,2-OXAZOL-5-YL)     
REMARK 630 METHYL]PROPANOYL}-L-TYROSINE                                         
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     3EF A  1630                                                      
REMARK 630     3EF B  1630                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    PHQ PPH 1JK TYR                                          
REMARK 630 DETAILS: NULL                                                        
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 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1622                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1624                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 1625                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1626                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1621                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B 1622                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1623                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1624                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3EF A 1630                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3EF B 1630                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1616 through FUC A1619 bound to ASN A 416                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues FUC      
REMARK 800  A1611 through NAG A1612 bound to ASN A 480                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B1614 through NAG B1615 bound to ASN B 45                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues FUC      
REMARK 800  B1611 through NAG B1612 bound to ASN B 480                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1614 through NAG A1615                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B1616 through BMA B1618                                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CA5   RELATED DB: PDB                                   
REMARK 900 HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH A PHOSPHINIC     
REMARK 900 TRIPEPTIDE FI                                                        
REMARK 900 RELATED ID: 4CA7   RELATED DB: PDB                                   
REMARK 900 DROSOPHILA ANGIOTENSIN CONVERTING ENZYME (ANCE) IN COMPLEX WITH A    
REMARK 900 PHOSPHINIC TRIPEPTIDE FI                                             
REMARK 900 RELATED ID: 4CA8   RELATED DB: PDB                                   
REMARK 900 DROSOPHILA ANGIOTENSIN CONVERTING ENZYME (ANCE) IN COMPLEX WITH A    
REMARK 900 PHOSPHINIC TRIPEPTIDE FII                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FINAL CONSTRUCT IS UNDERGLYCOSYALTED MUTANT AND CONTAINS             
REMARK 999 TWO MISMATCH MUTATIONS, P576L AND Q545R                              
DBREF  4CA6 A    1   610  UNP    P12821   ACE_HUMAN       30    639             
DBREF  4CA6 B    1   610  UNP    P12821   ACE_HUMAN       30    639             
SEQADV 4CA6 GLN A    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 4CA6 GLN A   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 4CA6 GLN A   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 4CA6 GLN A  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 4CA6 GLN A  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 4CA6 ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4CA6 LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 4CA6 GLN B    9  UNP  P12821    ASN    38 CONFLICT                       
SEQADV 4CA6 GLN B   25  UNP  P12821    ASN    54 CONFLICT                       
SEQADV 4CA6 GLN B   82  UNP  P12821    ASN   111 CONFLICT                       
SEQADV 4CA6 GLN B  117  UNP  P12821    ASN   146 CONFLICT                       
SEQADV 4CA6 GLN B  289  UNP  P12821    ASN   318 CONFLICT                       
SEQADV 4CA6 ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4CA6 LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQRES   1 A  610  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 A  610  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 A  610  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 A  610  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 A  610  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 A  610  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 A  610  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 A  610  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 A  610  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 A  610  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 A  610  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 A  610  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 A  610  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 A  610  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 A  610  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 A  610  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 A  610  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 A  610  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 A  610  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 A  610  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 A  610  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 A  610  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 A  610  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 A  610  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 A  610  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 A  610  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 A  610  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 A  610  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 A  610  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 A  610  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 A  610  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 A  610  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 A  610  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 A  610  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 A  610  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 A  610  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 A  610  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 A  610  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 A  610  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 A  610  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 A  610  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 A  610  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 A  610  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 A  610  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 A  610  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 A  610  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 A  610  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY              
SEQRES   1 B  610  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 B  610  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 B  610  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 B  610  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 B  610  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 B  610  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 B  610  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 B  610  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 B  610  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 B  610  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 B  610  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 B  610  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 B  610  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 B  610  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 B  610  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 B  610  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 B  610  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 B  610  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 B  610  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 B  610  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 B  610  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 B  610  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 B  610  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 B  610  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 B  610  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 B  610  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 B  610  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 B  610  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 B  610  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 B  610  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 B  610  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 B  610  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 B  610  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 B  610  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 B  610  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 B  610  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 B  610  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 B  610  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 B  610  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 B  610  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 B  610  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 B  610  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 B  610  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 B  610  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 B  610  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 B  610  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 B  610  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY              
MODRES 4CA6 ASN A   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4CA6 ASN A  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4CA6 ASN A  480  ASN  GLYCOSYLATION SITE                                 
MODRES 4CA6 ASN B   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4CA6 ASN B  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4CA6 ASN B  480  ASN  GLYCOSYLATION SITE                                 
HET     ZN  A1001       1                                                       
HET     CL  A1002       1                                                       
HET    FUC  A1611      10                                                       
HET    NAG  A1612      14                                                       
HET    NAG  A1614      14                                                       
HET    NAG  A1615      14                                                       
HET    NAG  A1616      14                                                       
HET    NAG  A1617      14                                                       
HET    BMA  A1618      11                                                       
HET    FUC  A1619      10                                                       
HET    PEG  A1622       7                                                       
HET    PEG  A1624       7                                                       
HET    PG4  A1625      10                                                       
HET    PEG  A1626       7                                                       
HET    3EF  A1630      51                                                       
HET     ZN  B1001       1                                                       
HET     CL  B1003       1                                                       
HET    FUC  B1611      10                                                       
HET    NAG  B1612      14                                                       
HET    NAG  B1614      14                                                       
HET    NAG  B1615      14                                                       
HET    NAG  B1616      14                                                       
HET    NAG  B1617      14                                                       
HET    BMA  B1618      11                                                       
HET    PEG  B1621       7                                                       
HET    P6G  B1622      19                                                       
HET    PEG  B1623       7                                                       
HET    PEG  B1624       7                                                       
HET    3EF  B1630      51                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     3EF N-{(2S)-3-[(S)-[(1R)-1-{[(BENZYLOXY)CARBONYL]AMINO}-2-           
HETNAM   2 3EF  PHENYLETHYL](HYDROXY)PHOSPHORYL]-2-[(3-PHENYL-1,2-              
HETNAM   3 3EF  OXAZOL-5-YL)METHYL]PROPANOYL}-L-TYROSINE                        
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   5  FUC    3(C6 H12 O5)                                                 
FORMUL   5  NAG    10(C8 H15 N O6)                                              
FORMUL   7  BMA    2(C6 H12 O6)                                                 
FORMUL   8  PEG    6(C4 H10 O3)                                                 
FORMUL  10  PG4    C8 H18 O5                                                    
FORMUL  12  3EF    2(C38 H38 N3 O9 P)                                           
FORMUL  19  P6G    C12 H26 O7                                                   
FORMUL  23  HOH   *594(H2 O)                                                    
HELIX    1   1 ASP A    2  GLN A    6  5                                   5    
HELIX    2   2 ASP A   13  THR A   44  1                                  32    
HELIX    3   3 THR A   47  GLU A   77  1                                  31    
HELIX    4   4 ILE A   79  PHE A   83  5                                   5    
HELIX    5   5 ASP A   85  ARG A   96  1                                  12    
HELIX    6   6 LEU A   98  LEU A  103  5                                   6    
HELIX    7   7 PRO A  104  ALA A  125  1                                  22    
HELIX    8   8 PRO A  141  SER A  150  1                                  10    
HELIX    9   9 SER A  152  ASP A  189  1                                  38    
HELIX   10  10 ASP A  193  TRP A  201  1                                   9    
HELIX   11  11 THR A  206  GLY A  238  1                                  33    
HELIX   12  12 TRP A  261  ASN A  263  5                                   3    
HELIX   13  13 ILE A  264  VAL A  269  1                                   6    
HELIX   14  14 VAL A  279  GLY A  287  1                                   9    
HELIX   15  15 GLN A  289  LEU A  304  1                                  16    
HELIX   16  16 PRO A  310  SER A  317  1                                   8    
HELIX   17  17 THR A  352  LYS A  373  1                                  22    
HELIX   18  18 PRO A  376  ARG A  380  5                                   5    
HELIX   19  19 ASN A  384  SER A  400  1                                  17    
HELIX   20  20 THR A  401  ILE A  408  1                                   8    
HELIX   21  21 ASP A  417  ILE A  433  1                                  17    
HELIX   22  22 ALA A  434  SER A  451  1                                  18    
HELIX   23  23 PRO A  455  SER A  457  5                                   3    
HELIX   24  24 ARG A  458  GLY A  472  1                                  15    
HELIX   25  25 PHE A  484  LYS A  489  5                                   6    
HELIX   26  26 TYR A  498  ALA A  519  1                                  22    
HELIX   27  27 PRO A  524  CYS A  528  5                                   5    
HELIX   28  28 SER A  533  GLY A  547  1                                  15    
HELIX   29  29 PRO A  551  GLY A  561  1                                  11    
HELIX   30  30 ALA A  567  ASN A  588  1                                  22    
HELIX   31  31 ASP B    2  GLN B    6  5                                   5    
HELIX   32  32 ASP B   13  THR B   44  1                                  32    
HELIX   33  33 THR B   47  GLU B   77  1                                  31    
HELIX   34  34 ILE B   79  PHE B   83  5                                   5    
HELIX   35  35 ASP B   85  ARG B   96  1                                  12    
HELIX   36  36 LEU B   98  LEU B  103  5                                   6    
HELIX   37  37 PRO B  104  ALA B  125  1                                  22    
HELIX   38  38 PRO B  141  SER B  150  1                                  10    
HELIX   39  39 SER B  152  GLN B  188  1                                  37    
HELIX   40  40 ASP B  193  TRP B  201  1                                   9    
HELIX   41  41 THR B  206  GLY B  238  1                                  33    
HELIX   42  42 TRP B  261  ASN B  263  5                                   3    
HELIX   43  43 ILE B  264  VAL B  269  1                                   6    
HELIX   44  44 VAL B  279  GLY B  287  1                                   9    
HELIX   45  45 GLN B  289  LEU B  304  1                                  16    
HELIX   46  46 PRO B  310  SER B  317  1                                   8    
HELIX   47  47 THR B  352  LYS B  373  1                                  22    
HELIX   48  48 PRO B  376  ARG B  380  5                                   5    
HELIX   49  49 ASN B  384  ILE B  408  1                                  25    
HELIX   50  50 ASP B  417  ILE B  433  1                                  17    
HELIX   51  51 PHE B  435  SER B  451  1                                  17    
HELIX   52  52 PRO B  455  SER B  457  5                                   3    
HELIX   53  53 ARG B  458  GLY B  472  1                                  15    
HELIX   54  54 PHE B  484  LYS B  489  5                                   6    
HELIX   55  55 TYR B  498  ALA B  519  1                                  22    
HELIX   56  56 PRO B  524  CYS B  528  5                                   5    
HELIX   57  57 SER B  533  ALA B  546  1                                  14    
HELIX   58  58 PRO B  551  GLY B  561  1                                  11    
HELIX   59  59 ALA B  567  ASN B  588  1                                  22    
SHEET    1  AA 2 LYS A 126  CYS A 128  0                                        
SHEET    2  AA 2 CYS A 136  SER A 138 -1  O  TRP A 137   N  VAL A 127           
SHEET    1  AB 2 ILE A 248  PRO A 249  0                                        
SHEET    2  AB 2 ILE A 473  CYS A 474  1  N  CYS A 474   O  ILE A 248           
SHEET    1  AC 2 SER A 333  ASP A 336  0                                        
SHEET    2  AC 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335           
SHEET    1  BA 2 LYS B 126  VAL B 127  0                                        
SHEET    2  BA 2 TRP B 137  SER B 138 -1  O  TRP B 137   N  VAL B 127           
SHEET    1  BB 2 ILE B 248  PRO B 249  0                                        
SHEET    2  BB 2 ILE B 473  CYS B 474  1  N  CYS B 474   O  ILE B 248           
SHEET    1  BC 2 SER B 333  ASP B 336  0                                        
SHEET    2  BC 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.05  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.08  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.06  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.09  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.02  
LINK         ND2 ASN A  45                 C1  NAG A1614     1555   1555  1.44  
LINK         ND2 ASN A 416                 C1  NAG A1616     1555   1555  1.32  
LINK         ND2 ASN A 480                 C1  NAG A1612     1555   1555  1.45  
LINK        ZN    ZN A1001                 OAD 3EF A1630     1555   1555  2.12  
LINK        ZN    ZN A1001                 OAG 3EF A1630     1555   1555  2.54  
LINK        ZN    ZN A1001                 OE1 GLU A 389     1555   1555  2.03  
LINK        ZN    ZN A1001                 NE2 HIS A 365     1555   1555  2.05  
LINK        ZN    ZN A1001                 NE2 HIS A 361     1555   1555  2.01  
LINK         C1  FUC A1611                 O6  NAG A1612     1555   1555  1.44  
LINK         O4  NAG A1614                 C1  NAG A1615     1555   1555  1.45  
LINK         O6  NAG A1616                 C1  FUC A1619     1555   1555  1.45  
LINK         O4  NAG A1616                 C1  NAG A1617     1555   1555  1.45  
LINK         O4  NAG A1617                 C1  BMA A1618     1555   1555  1.45  
LINK         ND2 ASN B  45                 C1  NAG B1614     1555   1555  1.44  
LINK         ND2 ASN B 416                 C1  NAG B1616     1555   1555  1.44  
LINK         ND2 ASN B 480                 C1  NAG B1612     1555   1555  1.44  
LINK        ZN    ZN B1001                 PBY 3EF B1630     1555   1555  2.70  
LINK        ZN    ZN B1001                 OAG 3EF B1630     1555   1555  2.39  
LINK        ZN    ZN B1001                 OAD 3EF B1630     1555   1555  2.24  
LINK        ZN    ZN B1001                 OE1 GLU B 389     1555   1555  1.91  
LINK        ZN    ZN B1001                 NE2 HIS B 365     1555   1555  1.98  
LINK        ZN    ZN B1001                 NE2 HIS B 361     1555   1555  1.99  
LINK         C1  FUC B1611                 O6  NAG B1612     1555   1555  1.44  
LINK         O4  NAG B1614                 C1  NAG B1615     1555   1555  1.45  
LINK         O4  NAG B1616                 C1  NAG B1617     1555   1555  1.45  
LINK         O4  NAG B1617                 C1  BMA B1618     1555   1555  1.45  
CISPEP   1 ASP A  140    PRO A  141          0         9.06                     
CISPEP   2 TYR A  607    PRO A  608          0         2.66                     
CISPEP   3 ASP B  140    PRO B  141          0        11.82                     
CISPEP   4 TYR B  607    PRO B  608          0         6.27                     
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  3EF A1630                    
SITE     1 AC2  4 TYR A 202  PRO A 497  ARG A 500  HOH A2120                    
SITE     1 AC3  4 ALA A 334  TRP A 335  3EF A1630  HOH A2340                    
SITE     1 AC4  2 ARG A  96  GLY A 190                                          
SITE     1 AC5  8 TYR A 465  HOH A2256  HOH A2341  HOH A2342                    
SITE     2 AC5  8 HOH A2343  ARG B 453  TYR B 465  LEU B 466                    
SITE     1 AC6  9 PHE A 228  ARG A 231  ALA A 232  ARG A 235                    
SITE     2 AC6  9 VAL A 268  VAL A 269  ASN A 588  HOH A2157                    
SITE     3 AC6  9 HOH A2344                                                     
SITE     1 AC7  4 HIS B 361  HIS B 365  GLU B 389  3EF B1630                    
SITE     1 AC8  4 TYR B 202  PRO B 497  ARG B 500  HOH B2096                    
SITE     1 AC9  1 ARG B 295                                                     
SITE     1 BC1  7 GLN A 286  GLY A 287  TRP A 288  HIS A 292                    
SITE     2 BC1  7 GLN B 286  TRP B 288  HIS B 292                               
SITE     1 BC2  5 TRP B 335  3EF B1630  HOH B2014  HOH B2249                    
SITE     2 BC2  5 HOH B2250                                                     
SITE     1 BC3  2 PHE B  33  ARG B 344                                          
SITE     1 BC4 27 GLN A 259  HIS A 331  ALA A 332  SER A 333                    
SITE     2 BC4 27 ALA A 334  SER A 357  THR A 358  HIS A 361                    
SITE     3 BC4 27 GLU A 362  HIS A 365  TYR A 369  HIS A 388                    
SITE     4 BC4 27 GLU A 389  ASP A 393  GLU A 431  LYS A 489                    
SITE     5 BC4 27 PHE A 490  HIS A 491  THR A 496  TYR A 498                    
SITE     6 BC4 27 TYR A 501  PHE A 505   ZN A1001  PEG A1622                    
SITE     7 BC4 27 HOH A2237  HOH A2253  HOH A2284                               
SITE     1 BC5 28 GLN B 259  HIS B 331  ALA B 332  SER B 333                    
SITE     2 BC5 28 ALA B 334  SER B 357  THR B 358  HIS B 361                    
SITE     3 BC5 28 GLU B 362  HIS B 365  TYR B 369  HIS B 388                    
SITE     4 BC5 28 GLU B 389  ASP B 393  GLU B 431  PHE B 435                    
SITE     5 BC5 28 LYS B 489  PHE B 490  HIS B 491  THR B 496                    
SITE     6 BC5 28 TYR B 498  TYR B 501  PHE B 505   ZN B1001                    
SITE     7 BC5 28 PEG B1623  HOH B2191  HOH B2198  HOH B2214                    
SITE     1 BC6  5 PHE A  10  GLU A 403  ASN A 416  PRO A 524                    
SITE     2 BC6  5 GLN A 527                                                     
SITE     1 BC7  5 THR A 478  ASN A 480  THR A 482  ARG B 245                    
SITE     2 BC7  5 GLU B 596                                                     
SITE     1 BC8  4 ASN B  45  THR B  47  GLU B  49  ASN B  50                    
SITE     1 BC9  6 ARG A 245  GLU A 596  THR B 478  ASN B 480                    
SITE     2 BC9  6 THR B 482  HOH B2247                                          
SITE     1 CC1  4 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     1 CC2  5 GLU B 403  ASN B 416  GLU B 522  PRO B 524                    
SITE     2 CC2  5 GLN B 527                                                     
CRYST1   72.925   76.643   82.545  88.62  64.22  75.58 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013713 -0.003526 -0.006996        0.00000                         
SCALE2      0.000000  0.013472  0.001307        0.00000                         
SCALE3      0.000000  0.000000  0.013517        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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