GenomeNet

Database: PDB
Entry: 4BZS
LinkDB: 4BZS
Original site: 4BZS 
HEADER    HYDROLASE                               29-JUL-13   4BZS              
TITLE     HUMAN ANGIOTENISN CONVERTING ENZYME N-DOMAIN IN COMPLEX WITH K-26     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N DOMAIN, RESIDUES 30-657;                                 
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143,     
COMPND   6 ANGIOTENSIN-CONVERTING ENZYME, SOLUBLE FORM;                         
COMPND   7 EC: 3.2.1.-, 3.4.15.1;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS                             
KEYWDS    HYDROLASE, ZINC METALLOPEPTIDASE, ANTIHYPERTENSIVE AGENT              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.J.KRAMER,A.MOHD,S.L.U.SCHWAGER,G.MASUYER,K.R.ACHARYA,E.D.STURROCK,  
AUTHOR   2 B.O.BACHMANN                                                         
REVDAT   3   07-FEB-18 4BZS    1       AUTHOR REMARK                            
REVDAT   2   18-JUN-14 4BZS    1       JRNL                                     
REVDAT   1   26-FEB-14 4BZS    0                                                
JRNL        AUTH   G.J.KRAMER,A.MOHD,S.L.U.SCHWAGER,G.MASUYER,K.R.ACHARYA,      
JRNL        AUTH 2 E.D.STURROCK,B.O.BACHMANN                                    
JRNL        TITL   INTERKINGDOM PHARMACOLOGY OF ANGIOTENSIN-I CONVERTING ENZYME 
JRNL        TITL 2 INHIBITOR PHOSPHONATES PRODUCED BY ACTINOMYCETES             
JRNL        REF    ACS MED.CHEM.LETT.            V.   5   346 2014              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   24900839                                                     
JRNL        DOI    10.1021/ML4004588                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 72571                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3841                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4131                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.4080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9941                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 345                                     
REMARK   3   SOLVENT ATOMS            : 161                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.65000                                              
REMARK   3    B22 (A**2) : -0.38000                                             
REMARK   3    B33 (A**2) : 1.08000                                              
REMARK   3    B12 (A**2) : 2.04000                                              
REMARK   3    B13 (A**2) : 1.95000                                              
REMARK   3    B23 (A**2) : -1.36000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.307         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.238         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.192         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.674         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10605 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9635 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14446 ; 0.914 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22070 ; 0.748 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1220 ; 4.922 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   528 ;34.530 ;23.826       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1593 ;13.735 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;15.393 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1515 ; 0.054 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11940 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2620 ; 0.001 ; 0.020       
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  : NULL                                       
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 4BZS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290057845.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-AUG-10                          
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) : 1.282                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90926                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.0                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
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     (%) : 71.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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 3NXQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS A9 (0.06M DIVALENTS, 0.1M       
REMARK 280  TRIS/BICINE PH 8.5, 30% PEG550MME/PEG20K) SILVER BULLET G3          
REMARK 280  SOLUTION (HAMPTON RESEARCH) ADDITIVE. 1:1:1 PROTEIN:RESERVOIR:      
REMARK 280  ADDITIVE                                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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     LEU A   613                                                      
REMARK 465     VAL A   614                                                      
REMARK 465     THR A   615                                                      
REMARK 465     ASP A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     ALA A   618                                                      
REMARK 465     GLU A   619                                                      
REMARK 465     ALA A   620                                                      
REMARK 465     SER A   621                                                      
REMARK 465     LYS A   622                                                      
REMARK 465     PHE A   623                                                      
REMARK 465     VAL A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     GLU A   626                                                      
REMARK 465     TYR A   627                                                      
REMARK 465     ASP A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     ASP B   612                                                      
REMARK 465     LEU B   613                                                      
REMARK 465     VAL B   614                                                      
REMARK 465     THR B   615                                                      
REMARK 465     ASP B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     ALA B   618                                                      
REMARK 465     GLU B   619                                                      
REMARK 465     ALA B   620                                                      
REMARK 465     SER B   621                                                      
REMARK 465     LYS B   622                                                      
REMARK 465     PHE B   623                                                      
REMARK 465     VAL B   624                                                      
REMARK 465     GLU B   625                                                      
REMARK 465     GLU B   626                                                      
REMARK 465     TYR B   627                                                      
REMARK 465     ASP B   628                                                      
REMARK 465     LEU B   629                                                      
REMARK 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     GLU A 403    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 609    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 403    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 412    CG   OD1  OD2                                       
REMARK 470     GLU B 609    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE A   92   CD1                                                 
REMARK 480     LYS A  126   CD   CE   NZ                                        
REMARK 480     ILE B   92   CD1                                                 
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   OE1  GLU B   522     C3   BMA B   807              1.43            
REMARK 500   OE1  GLU B   522     O3   BMA B   807              1.85            
REMARK 500   NE2  GLN A   598     O    HOH A  2064              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A 126   CG    LYS A 126   CD     -0.219                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  45       80.71   -166.26                                   
REMARK 500    GLN A  81      -22.51     88.84                                   
REMARK 500    THR A 133       78.34    -69.54                                   
REMARK 500    ALA A 134      -64.41   -130.45                                   
REMARK 500    ASN A 203       59.08     36.55                                   
REMARK 500    PRO A 272     -178.67    -68.77                                   
REMARK 500    ASP A 273      -23.86     78.76                                   
REMARK 500    LYS A 341      -54.36   -155.60                                   
REMARK 500    ASN B  45       78.08   -166.51                                   
REMARK 500    LEU B  75      -60.92    -93.20                                   
REMARK 500    TYR B  76       47.48   -101.97                                   
REMARK 500    GLN B  81       -9.11     99.22                                   
REMARK 500    THR B 135      130.35     69.69                                   
REMARK 500    ASN B 203       54.58     38.62                                   
REMARK 500    LYS B 341      -53.50   -133.56                                   
REMARK 500    GLU B 609     -164.23    -77.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 9X6 CORRESPONDS TO THIODIGLYCOLIC ACID PRESENT IN THE SILVER         
REMARK 600   BULLET G3 SOLUTION (HAMPTON RESEARCH)                              
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     PE4 A  703                                                       
REMARK 610     PG4 B 1611                                                       
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 361   NE2                                                    
REMARK 620 2 K26 A1001   OAG  87.2                                              
REMARK 620 3 K26 A1001   OAK 119.2  63.0                                        
REMARK 620 4 HIS A 365   NE2 100.6  78.7 120.9                                  
REMARK 620 5 GLU A 389   OE1 111.2 155.2  92.8 112.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 K26 B1001   PBK                                                    
REMARK 620 2 HIS B 361   NE2  99.8                                              
REMARK 620 3 K26 B1001   OAK  34.6 108.9                                        
REMARK 620 4 GLU B 389   OE1 138.3  86.5 104.4                                  
REMARK 620 5 K26 B1001   OAG  34.5  91.4  68.9 171.9                            
REMARK 620 6 HIS B 365   NE2 121.5 103.0 142.6  96.4  91.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K26 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 1611                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K26 B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9X6 A 1613                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9X6 B 1612                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG A    
REMARK 800  803 through NAG A 804 bound to ASN A 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG A    
REMARK 800  805 through BMA A 807 bound to ASN A 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG A    
REMARK 800  801 through FUC A 802 bound to ASN A 480                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG B    
REMARK 800  803 through NAG B 804 bound to ASN B 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG B    
REMARK 800  805 through BMA B 807 bound to ASN B 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG B    
REMARK 800  801 through FUC B 802 bound to ASN B 480                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BZR   RELATED DB: PDB                                   
REMARK 900 HUMAN TESTIS ANGIOTENSIN CONVERTING ENZYME IN COMPLEX WITH K-26      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ENGINEERED GLYCOSYLATION MUTANT                                      
DBREF  4BZS A    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  4BZS B    1   628  UNP    P12821   ACE_HUMAN       30    657             
SEQADV 4BZS LEU A  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4BZS LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 4BZS LEU B  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4BZS LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQRES   1 A  629  LEU ASP PRO GLY LEU GLN PRO GLY ASN PHE SER ALA ASP          
SEQRES   2 A  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR ASN SER          
SEQRES   3 A  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 A  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 A  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 A  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 A  629  ILE TRP GLN ASN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 A  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 A  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER ASN          
SEQRES  10 A  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 A  629  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 A  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 A  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 A  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 A  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 A  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 A  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 A  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 A  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 A  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 A  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 A  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 A  629  GLY TRP ASN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 A  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 A  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 A  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 A  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 A  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 A  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 A  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 A  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 A  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 A  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 A  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 A  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 A  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 A  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 A  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 A  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 A  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 A  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 A  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU GLN ALA          
SEQRES  43 A  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 A  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 A  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 A  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 A  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 A  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 A  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 B  629  LEU ASP PRO GLY LEU GLN PRO GLY ASN PHE SER ALA ASP          
SEQRES   2 B  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR ASN SER          
SEQRES   3 B  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 B  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 B  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 B  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 B  629  ILE TRP GLN ASN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 B  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 B  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER ASN          
SEQRES  10 B  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 B  629  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 B  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 B  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 B  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 B  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 B  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 B  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 B  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 B  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 B  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 B  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 B  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 B  629  GLY TRP ASN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 B  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 B  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 B  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 B  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 B  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 B  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 B  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 B  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 B  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 B  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 B  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 B  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 B  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 B  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 B  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 B  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 B  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 B  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 B  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU GLN ALA          
SEQRES  43 B  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 B  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 B  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 B  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 B  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 B  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 B  629  GLU GLU TYR ASP LEU                                          
MODRES 4BZS ASN A   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4BZS ASN A  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4BZS ASN A  480  ASN  GLYCOSYLATION SITE                                 
MODRES 4BZS ASN B   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4BZS ASN B  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4BZS ASN B  480  ASN  GLYCOSYLATION SITE                                 
HET     ZN  A 701       1                                                       
HET     CL  A 702       1                                                       
HET    PE4  A 703      13                                                       
HET    P6G  A 704      19                                                       
HET    PEG  A 705       7                                                       
HET    NAG  A 801      14                                                       
HET    FUC  A 802      10                                                       
HET    NAG  A 803      14                                                       
HET    NAG  A 804      14                                                       
HET    NAG  A 805      14                                                       
HET    NAG  A 806      14                                                       
HET    BMA  A 807      11                                                       
HET    K26  A1001      37                                                       
HET    9X6  A1613       9                                                       
HET     ZN  B 701       1                                                       
HET     CL  B 702       1                                                       
HET    PEG  B 703       7                                                       
HET    PEG  B 704       7                                                       
HET    PEG  B 705       7                                                       
HET    NAG  B 801      14                                                       
HET    FUC  B 802      10                                                       
HET    NAG  B 803      14                                                       
HET    NAG  B 804      14                                                       
HET    NAG  B 805      14                                                       
HET    NAG  B 806      14                                                       
HET    BMA  B 807      11                                                       
HET    K26  B1001      37                                                       
HET    PG4  B1611       7                                                       
HET    9X6  B1612       9                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-              
HETNAM   2 PE4  ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL                                 
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     K26 N-ACETYL-L-ILE-L-TYR-(R)-1-AMINO-2-(4-HYDROXYPHENYL)             
HETNAM   2 K26  ETHYLPHOSPHONIC ACID                                            
HETNAM     9X6 THIODIGLYCOLIC ACID                                              
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000                                      
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
HETSYN     9X6 2-(2-HYDROXY-2-OXOETHYLSULFANYL)ETHANOIC ACID                    
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   5  PE4    C16 H34 O8                                                   
FORMUL   6  P6G    C12 H26 O7                                                   
FORMUL   7  PEG    4(C4 H10 O3)                                                 
FORMUL   8  NAG    10(C8 H15 N O6)                                              
FORMUL   8  FUC    2(C6 H12 O5)                                                 
FORMUL  10  BMA    2(C6 H12 O6)                                                 
FORMUL  11  K26    2(C25 H34 N3 O8 P)                                           
FORMUL  12  9X6    2(C4 H6 O4 S)                                                
FORMUL  22  PG4    C8 H18 O5                                                    
FORMUL  24  HOH   *161(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 ASP A   85  THR A   97  1                                  13    
HELIX    5   5 LEU A   98  LEU A  103  5                                   6    
HELIX    6   6 PRO A  104  ALA A  125  1                                  22    
HELIX    7   7 PRO A  141  SER A  150  1                                  10    
HELIX    8   8 SER A  152  GLN A  188  1                                  37    
HELIX    9   9 ASP A  193  SER A  200  1                                   8    
HELIX   10  10 TRP A  201  ASN A  203  5                                   3    
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 ASN 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  ILE A  408  1                                  25    
HELIX   20  20 ASP A  417  ILE A  433  1                                  17    
HELIX   21  21 PHE A  435  SER A  451  1                                  17    
HELIX   22  22 PRO A  455  SER A  457  5                                   3    
HELIX   23  23 ARG A  458  GLY A  472  1                                  15    
HELIX   24  24 PHE A  484  LYS A  489  5                                   6    
HELIX   25  25 TYR A  498  ALA A  519  1                                  22    
HELIX   26  26 PRO A  524  CYS A  528  5                                   5    
HELIX   27  27 SER A  533  GLY A  547  1                                  15    
HELIX   28  28 PRO A  551  GLY A  561  1                                  11    
HELIX   29  29 ALA A  567  ASN A  588  1                                  22    
HELIX   30  30 ASP B    2  GLN B    6  5                                   5    
HELIX   31  31 ASP B   13  THR B   44  1                                  32    
HELIX   32  32 THR B   47  TYR B   76  1                                  30    
HELIX   33  33 ASP B   85  ARG B   96  1                                  12    
HELIX   34  34 LEU B   98  LEU B  103  5                                   6    
HELIX   35  35 PRO B  104  ALA B  125  1                                  22    
HELIX   36  36 PRO B  141  SER B  150  1                                  10    
HELIX   37  37 SER B  152  GLN B  188  1                                  37    
HELIX   38  38 ASP B  193  SER B  200  1                                   8    
HELIX   39  39 TRP B  201  ASN B  203  5                                   3    
HELIX   40  40 THR B  206  GLY B  238  1                                  33    
HELIX   41  41 TRP B  261  ASN B  263  5                                   3    
HELIX   42  42 ILE B  264  VAL B  269  1                                   6    
HELIX   43  43 VAL B  279  GLY B  287  1                                   9    
HELIX   44  44 ASN B  289  LEU B  304  1                                  16    
HELIX   45  45 PRO B  310  SER B  317  1                                   8    
HELIX   46  46 THR B  352  LYS B  373  1                                  22    
HELIX   47  47 PRO B  376  ARG B  380  5                                   5    
HELIX   48  48 ASN B  384  THR B  401  1                                  18    
HELIX   49  49 THR B  401  ILE B  408  1                                   8    
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  GLY B  520  1                                  23    
HELIX   56  56 PRO B  524  CYS B  528  5                                   5    
HELIX   57  57 SER B  533  GLY B  547  1                                  15    
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 ILE A 248  PRO A 249  0                                        
SHEET    2  AA 2 ILE A 473  CYS A 474  1  N  CYS A 474   O  ILE A 248           
SHEET    1  AB 2 SER A 333  ASP A 336  0                                        
SHEET    2  AB 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335           
SHEET    1  BA 2 VAL B 127  CYS B 128  0                                        
SHEET    2  BA 2 CYS B 136  TRP B 137 -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  2.04  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.05  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.04  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.05  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.03  
LINK         ND2 ASN A  45                 C1  NAG A 803     1555   1555  1.44  
LINK         ND2 ASN A 416                 C1  NAG A 805     1555   1555  1.45  
LINK         ND2 ASN A 480                 C1  NAG A 801     1555   1555  1.46  
LINK        ZN    ZN A 701                 NE2 HIS A 361     1555   1555  2.22  
LINK        ZN    ZN A 701                 OAG K26 A1001     1555   1555  2.53  
LINK        ZN    ZN A 701                 OAK K26 A1001     1555   1555  2.13  
LINK        ZN    ZN A 701                 NE2 HIS A 365     1555   1555  2.20  
LINK        ZN    ZN A 701                 OE1 GLU A 389     1555   1555  1.92  
LINK         O6  NAG A 801                 C1  FUC A 802     1555   1555  1.44  
LINK         O4  NAG A 803                 C1  NAG A 804     1555   1555  1.44  
LINK         O4  NAG A 805                 C1  NAG A 806     1555   1555  1.44  
LINK         O4  NAG A 806                 C1  BMA A 807     1555   1555  1.44  
LINK         ND2 ASN B  45                 C1  NAG B 803     1555   1555  1.46  
LINK         ND2 ASN B 416                 C1  NAG B 805     1555   1555  1.45  
LINK         ND2 ASN B 480                 C1  NAG B 801     1555   1555  1.45  
LINK        ZN    ZN B 701                 PBK K26 B1001     1555   1555  2.57  
LINK        ZN    ZN B 701                 NE2 HIS B 361     1555   1555  2.40  
LINK        ZN    ZN B 701                 OAK K26 B1001     1555   1555  2.00  
LINK        ZN    ZN B 701                 OE1 GLU B 389     1555   1555  2.08  
LINK        ZN    ZN B 701                 OAG K26 B1001     1555   1555  2.34  
LINK        ZN    ZN B 701                 NE2 HIS B 365     1555   1555  2.12  
LINK         O6  NAG B 801                 C1  FUC B 802     1555   1555  1.44  
LINK         O4  NAG B 803                 C1  NAG B 804     1555   1555  1.44  
LINK         O4  NAG B 805                 C1  NAG B 806     1555   1555  1.44  
LINK         O4  NAG B 806                 C1  BMA B 807     1555   1555  1.45  
CISPEP   1 ASP A  140    PRO A  141          0         1.83                     
CISPEP   2 TYR A  607    PRO A  608          0        -4.94                     
CISPEP   3 ASP B  140    PRO B  141          0         1.21                     
CISPEP   4 TYR B  607    PRO B  608          0        -2.72                     
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  K26 A1001                    
SITE     1 AC2  3 TYR A 202  PRO A 497  ARG A 500                               
SITE     1 AC3  9 GLN A 286  GLY A 287  TRP A 288  HIS A 292                    
SITE     2 AC3  9 P6G A 704  GLN B 286  GLY B 287  TRP B 288                    
SITE     3 AC3  9 HIS B 292                                                     
SITE     1 AC4  6 ARG A 295  ILE A 408  PE4 A 703  ARG B 295                    
SITE     2 AC4  6 GLU B 299  ILE B 408                                          
SITE     1 AC5  2 SER A  39  K26 A1001                                          
SITE     1 AC6 19 SER A 333  ALA A 334  TRP A 335  ASP A 336                    
SITE     2 AC6 19 TYR A 338  HIS A 361  GLU A 362  HIS A 365                    
SITE     3 AC6 19 TYR A 369  HIS A 388  GLU A 389  PHE A 490                    
SITE     4 AC6 19 TYR A 501   ZN A 701  PEG A 705  HOH A2038                    
SITE     5 AC6 19 HOH A2042  HOH A2044  HOH A2059                               
SITE     1 AC7  4 HIS B 361  HIS B 365  GLU B 389  K26 B1001                    
SITE     1 AC8  3 TYR B 202  PRO B 497  ARG B 500                               
SITE     1 AC9  3 ARG B 381  ARG B 500  K26 B1001                               
SITE     1 BC1  3 SER B  39  K26 B1001  HOH B2078                               
SITE     1 BC2  2 ARG B  96  GLY B 190                                          
SITE     1 BC3  5 ARG A 453  TYR A 465  HOH A2049  ARG B 453                    
SITE     2 BC3  5 TYR B 465                                                     
SITE     1 BC4 19 ALA B 332  SER B 333  ALA B 334  TRP B 335                    
SITE     2 BC4 19 ASP B 336  TYR B 338  HIS B 361  GLU B 362                    
SITE     3 BC4 19 HIS B 365  TYR B 369  HIS B 388  GLU B 389                    
SITE     4 BC4 19 PHE B 490  TYR B 501   ZN B 701  PEG B 703                    
SITE     5 BC4 19 PEG B 704  HOH B2062  HOH B2064                               
SITE     1 BC5  7 GLN A 259  LYS A 489  HIS A 491  TYR A 498                    
SITE     2 BC5  7 TYR A 501  HOH A2038  HOH A2042                               
SITE     1 BC6  3 LYS B 489  HIS B 491  TYR B 498                               
SITE     1 BC7  5 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 BC7  5 ARG A 326                                                     
SITE     1 BC8  3 ASN A 416  PRO A 524  GLN A 527                               
SITE     1 BC9  7 THR A 478  ASN A 480  THR A 482  HIS A 483                    
SITE     2 BC9  7 HOH A2065  ARG B 245  GLU B 596                               
SITE     1 CC1  5 ASN B  45  THR B  47  GLU B  49  ASN B  50                    
SITE     2 CC1  5 ARG B 326                                                     
SITE     1 CC2  4 ASN B 416  GLU B 522  PRO B 524  GLN B 527                    
SITE     1 CC3  5 ARG A 245  GLU A 596  ASN B 480  THR B 482                    
SITE     2 CC3  5 HOH B2096                                                     
CRYST1   73.005   77.320   82.070  88.69  64.53  75.29 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      0.013698 -0.003596 -0.006914        0.00000                         
SCALE2      0.000000  0.013372  0.001329        0.00000                         
SCALE3      0.000000  0.000000  0.013563        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system