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Database: PDB
Entry: 2IUL
LinkDB: 2IUL
Original site: 2IUL 
HEADER    HYDROLASE                               06-JUN-06   2IUL              
TITLE     HUMAN TACE G13 MUTANT                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 68-658;                                           
COMPND   5 SYNONYM: HUMAN TESTIS ACE G13 MUTANT, TESTIS-SPECIFIC                
COMPND   6  ISOFORM, ACE-T, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE             
COMPND   7  II;                                                                 
COMPND   8 EC: 3.4.15.1, 3.2.1.-;                                               
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 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_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY CELLS             
KEYWDS    HYDROLASE, PHOSPHORYLATION, CARBOXYPEPTIDASE,                         
KEYWDS   2 METAL-BINDING, TRANSMEMBRANE, METALLOPROTEASE, PEPTIDYL              
KEYWDS   3 DIPEPTIDASE, ALTERNATIVE SPLICING, TYPE-I                            
KEYWDS   4 MEMBRANE-ANCHORED PROTEIN, GLYCOSIDASE, POLYMORPHISM,                
KEYWDS   5 GLYCOPROTEIN, AC, ZINC, MUTANT, MEMBRANE, CHLORIDE,                  
KEYWDS   6 PROTEASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.WATERMEYER,B.T.SEWELL,R.NATESH,H.R.CORRADI,K.R.ACHARYA,           
AUTHOR   2 E.D.STURROCK                                                         
REVDAT   2   24-FEB-09 2IUL    1       VERSN                                    
REVDAT   1   25-OCT-06 2IUL    0                                                
JRNL        AUTH   J.M.WATERMEYER,B.T.SEWELL,S.L.SCHWAGER,R.NATESH,             
JRNL        AUTH 2 H.R.CORRADI,K.R.ACHARYA,E.D.STURROCK                         
JRNL        TITL   STRUCTURE OF TESTIS ACE GLYCOSYLATION MUTANTS AND            
JRNL        TITL 2 EVIDENCE FOR CONSERVED DOMAIN MOVEMENT.                      
JRNL        REF    BIOCHEMISTRY                  V.  45 12654 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17042482                                                     
JRNL        DOI    10.1021/BI061146Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 40225                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1297                            
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) : 2.02                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2172                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4779                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 85                                      
REMARK   3   SOLVENT ATOMS            : 335                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.10000                                              
REMARK   3    B22 (A**2) : -0.26000                                             
REMARK   3    B33 (A**2) : 0.16000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.192         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.163         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.374         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4972 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6780 ; 1.198 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   589 ; 5.178 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   243 ;35.326 ;24.115       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   790 ;14.138 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;20.780 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   727 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3823 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2389 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3411 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   316 ; 0.125 ; 0.200       
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):    56 ; 0.201 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.114 ; 0.200       
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):  3024 ; 0.603 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4722 ; 0.972 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2286 ; 1.465 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2054 ; 2.249 ; 4.500       
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2IUL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  06-JUN-06.                 
REMARK 100 THE PDBE ID CODE IS EBI-29010.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40225                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 12.400                             
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1O8A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 44.06                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH4.7 15%,           
REMARK 280  PEG 4000, 10UM ZINC SULPHATE                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.31650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.23300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.36150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.23300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.31650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.36150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  CONVERTS ANGIOTENSIN I TO ANGIOTENSIN II BY RELEASE OF              
REMARK 400  THE TERMINAL HIS-LEU, THIS RESULTS IN AN INCREASE OF THE            
REMARK 400  VASOCONSTRICTOR ACTIVITY OF ANGIOTENSIN. ALSO ABLE TO INACTIVATE    
REMARK 400  BRADYKININ, A POTENT VASODILATOR. HAS ALSO A GLYCOSIDASE ACTIVITY   
REMARK 400  WHICH RELEASES GPI-ANCHORED PROTEINS FROM THE MEMBRANE BY CLEAVING  
REMARK 400  THE MANNOSE LINKAGE IN THE GPI MOIETY (BY SIMILARITY).              
REMARK 400                                                                      
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 121 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 186 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 368 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 617 TO GLN                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A    37                                                      
REMARK 465     VAL A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A   436                                                      
REMARK 465     ASN A   624                                                      
REMARK 465     SER A   625                                                      
REMARK 465     ALA A   626                                                      
REMARK 465     ARG A   627                                                      
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  64    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;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     LYS A  79    CG   CD   CE   NZ                                   
REMARK 480     GLN A  98    CG   CD  OE1  NE2                                   
REMARK 480     GLN A 106    CG   CD  OE1  NE2                                   
REMARK 480     GLN A 108    CB   CG   CD  OE1  NE2                              
REMARK 480     LYS A 113    CE   NZ                                             
REMARK 480     LYS A 117    CD   CE   NZ                                        
REMARK 480     SER A 298    OG                                                  
REMARK 480     GLU A 303    CG   CD  OE1  OE2                                   
REMARK 480     LYS A 307    CG   CD   CE   NZ                                   
REMARK 480     LYS A 363    CE   NZ                                             
REMARK 480     LYS A 425    CE   NZ                                             
REMARK 480     LYS A 613    CE   NZ                                             
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 113   CD    LYS A 113   CE     -0.263                       
REMARK 500    LYS A 117   CG    LYS A 117   CD      0.229                       
REMARK 500    SER A 298   CB    SER A 298   OG      0.170                       
REMARK 500    LYS A 425   CD    LYS A 425   CE      0.253                       
REMARK 500    LYS A 613   CD    LYS A 613   CE     -0.187                       
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    LYS A 113   CD  -  CE  -  NZ  ANGL. DEV. =  39.5 DEGREES          
REMARK 500    LYS A 113   CG  -  CD  -  CE  ANGL. DEV. =  28.2 DEGREES          
REMARK 500    LYS A 613   CG  -  CD  -  CE  ANGL. DEV. = -24.7 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 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  72       74.51   -166.61                                   
REMARK 500    GLU A 123     -129.59     50.28                                   
REMARK 500    ASP A 300       98.32    -66.58                                   
REMARK 500    LYS A 363      -39.04   -134.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 CYS A  152     HIS A  153                  145.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
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 A1634  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACT A1627   OXT                                                    
REMARK 620 2 HIS A 383   NE2  99.5                                              
REMARK 620 3 GLU A 411   OE1 152.5  91.0                                        
REMARK 620 4 ACT A1627   O    54.5 117.5  98.2                                  
REMARK 620 5 HIS A 387   NE2  94.8 107.8 106.1 127.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1631                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1633                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1634                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN                              
REMARK 900  CONVERING ENZYME IN COMPLEX WITH LISINOPRIL.                        
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN                              
REMARK 900  CONVERING ENZYME (NATIVE).                                          
REMARK 900 RELATED ID: 1UZE   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG                               
REMARK 900  ENALAPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN                       
REMARK 900   I-CONVERTING ENZYME                                                
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG                               
REMARK 900  CAPTOPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN                       
REMARK 900   I-CONVERTING ENZYME                                                
REMARK 900 RELATED ID: 2IUX   RELATED DB: PDB                                   
REMARK 900  HUMAN TACE MUTANT G1234                                             
DBREF  2IUL A   37   627  UNP    P22966   ACET_HUMAN      68    658             
SEQADV 2IUL GLN A   90  UNP  P22966    ASN   121 ENGINEERED MUTATION            
SEQADV 2IUL GLN A  155  UNP  P22966    ASN   186 ENGINEERED MUTATION            
SEQADV 2IUL GLN A  337  UNP  P22966    ASN   368 ENGINEERED MUTATION            
SEQADV 2IUL GLN A  586  UNP  P22966    ASN   617 ENGINEERED MUTATION            
SEQRES   1 A  591  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU          
SEQRES   2 A  591  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR          
SEQRES   3 A  591  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR          
SEQRES   4 A  591  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE          
SEQRES   5 A  591  ALA GLN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS          
SEQRES   6 A  591  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG          
SEQRES   7 A  591  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU          
SEQRES   8 A  591  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU          
SEQRES   9 A  591  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS          
SEQRES  10 A  591  PRO GLN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR          
SEQRES  11 A  591  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU          
SEQRES  12 A  591  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA          
SEQRES  13 A  591  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN          
SEQRES  14 A  591  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP          
SEQRES  15 A  591  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN          
SEQRES  16 A  591  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR          
SEQRES  17 A  591  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG          
SEQRES  18 A  591  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE          
SEQRES  19 A  591  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP          
SEQRES  20 A  591  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA          
SEQRES  21 A  591  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY          
SEQRES  22 A  591  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE          
SEQRES  23 A  591  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE          
SEQRES  24 A  591  TRP GLN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG          
SEQRES  25 A  591  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN          
SEQRES  26 A  591  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN          
SEQRES  27 A  591  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS          
SEQRES  28 A  591  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA          
SEQRES  29 A  591  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE          
SEQRES  30 A  591  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS          
SEQRES  31 A  591  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER          
SEQRES  32 A  591  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU          
SEQRES  33 A  591  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP          
SEQRES  34 A  591  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS          
SEQRES  35 A  591  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS          
SEQRES  36 A  591  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY          
SEQRES  37 A  591  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER          
SEQRES  38 A  591  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN          
SEQRES  39 A  591  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS          
SEQRES  40 A  591  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS          
SEQRES  41 A  591  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY          
SEQRES  42 A  591  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR          
SEQRES  43 A  591  GLY GLN PRO GLN MET SER ALA SER ALA MET LEU SER TYR          
SEQRES  44 A  591  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU          
SEQRES  45 A  591  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP          
SEQRES  46 A  591  THR PRO ASN SER ALA ARG                                      
HET    NAG  A1624      14                                                       
HET    NAG  A1625      14                                                       
HET    NAG  A1626      14                                                       
HET    FUC  A1631      10                                                       
HET    BMA  A1632      11                                                       
HET    BMA  A1633      11                                                       
HET    ACT  A1627       4                                                       
HET    ACT  A1628       4                                                       
HET     CL  A1629       1                                                       
HET     CL  A1630       1                                                       
HET     ZN  A1634       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETSYN     NAG NAG                                                              
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   3  FUC    C6 H12 O5                                                    
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   4  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   8   ZN    ZN 2+                                                        
FORMUL   9  HOH   *335(H2 O1)                                                   
HELIX    1   1 ASP A   40  THR A   71  1                                  32    
HELIX    2   2 THR A   74  ARG A  100  1                                  27    
HELIX    3   3 ASP A  103  LEU A  107  5                                   5    
HELIX    4   4 ASN A  109  GLN A  120  1                                  12    
HELIX    5   5 LEU A  122  LEU A  127  5                                   6    
HELIX    6   6 PRO A  128  ALA A  149  1                                  22    
HELIX    7   7 PRO A  163  SER A  172  1                                  10    
HELIX    8   8 LYS A  174  ALA A  189  1                                  16    
HELIX    9   9 ALA A  189  GLN A  195  1                                   7    
HELIX   10  10 PHE A  196  ASN A  211  1                                  16    
HELIX   11  11 ASP A  215  SER A  222  1                                   8    
HELIX   12  12 MET A  223  GLU A  225  5                                   3    
HELIX   13  13 SER A  228  LEU A  240  1                                  13    
HELIX   14  14 LEU A  240  GLY A  260  1                                  21    
HELIX   15  15 TRP A  283  ASN A  285  5                                   3    
HELIX   16  16 ILE A  286  VAL A  291  1                                   6    
HELIX   17  17 ASP A  300  GLN A  308  1                                   9    
HELIX   18  18 THR A  311  LEU A  326  1                                  16    
HELIX   19  19 PRO A  332  SER A  339  1                                   8    
HELIX   20  20 ASN A  374  TYR A  394  1                                  21    
HELIX   21  21 PRO A  398  ARG A  402  5                                   5    
HELIX   22  22 ASN A  406  SER A  422  1                                  17    
HELIX   23  23 THR A  423  LEU A  430  1                                   8    
HELIX   24  24 SER A  439  ASP A  473  1                                  35    
HELIX   25  25 ASN A  480  GLY A  494  1                                  15    
HELIX   26  26 PHE A  506  LYS A  511  5                                   6    
HELIX   27  27 TYR A  520  ALA A  541  1                                  22    
HELIX   28  28 PRO A  546  CYS A  550  5                                   5    
HELIX   29  29 SER A  555  LEU A  568  1                                  14    
HELIX   30  30 PRO A  573  GLY A  583  1                                  11    
HELIX   31  31 ALA A  589  HIS A  610  1                                  22    
SHEET    1  AA 2 THR A 150  CYS A 152  0                                        
SHEET    2  AA 2 CYS A 158  GLN A 160 -1  O  LEU A 159   N  VAL A 151           
SHEET    1  AB 2 ILE A 270  PRO A 271  0                                        
SHEET    2  AB 2 LEU A 495  CYS A 496  1  N  CYS A 496   O  ILE A 270           
SHEET    1  AC 2 SER A 355  ASP A 358  0                                        
SHEET    2  AC 2 PHE A 365  LYS A 368 -1  O  ARG A 366   N  TRP A 357           
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.05  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.04  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03  
LINK         ND2 ASN A  72                 C1  NAG A1624     1555   1555  1.48  
LINK         ND2 ASN A 109                 C1  NAG A1625     1555   1555  1.44  
LINK         O4  NAG A1625                 C1  NAG A1626     1555   1555  1.44  
LINK         O6  NAG A1625                 C1  FUC A1631     1555   1555  1.33  
LINK         O4  NAG A1626                 C1  BMA A1632     1555   1555  1.44  
LINK         O   ACT A1627                ZN    ZN A1634     1555   1555  2.04  
LINK         O3  BMA A1632                 C1  BMA A1633     1555   1555  1.45  
LINK        ZN    ZN A1634                 NE2 HIS A 383     1555   1555  2.05  
LINK        ZN    ZN A1634                 OE1 GLU A 411     1555   1555  1.99  
LINK        ZN    ZN A1634                 NE2 HIS A 387     1555   1555  2.05  
LINK        ZN    ZN A1634                 OXT ACT A1627     1555   1555  2.48  
CISPEP   1 GLU A  162    PRO A  163          0        12.18                     
CISPEP   2 GLY A  437    GLY A  438          0         2.24                     
SITE     1 AC1  5 ASN A  72  THR A  74  GLU A  76  ARG A 348                    
SITE     2 AC1  5 HOH A2331                                                     
SITE     1 AC2  4 ASN A 109  ILE A 112  NAG A1626  FUC A1631                    
SITE     1 AC3  2 NAG A1625  BMA A1632                                          
SITE     1 AC4  3 SER A  45  GLU A  49  NAG A1625                               
SITE     1 AC5  3 GLU A  43  NAG A1626  BMA A1633                               
SITE     1 AC6  3 GLU A  43  LYS A  46  BMA A1632                               
SITE     1 AC7  8 ALA A 354  HIS A 383  GLU A 384  HIS A 387                    
SITE     2 AC7  8 GLU A 411  TYR A 523   ZN A1634  HOH A2182                    
SITE     1 AC8  7 GLN A 281  LYS A 511  HIS A 513  TYR A 520                    
SITE     2 AC8  7 TYR A 523  HOH A2333  HOH A2334                               
SITE     1 AC9  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 BC1  4 TYR A 224  PRO A 407  PRO A 519  ARG A 522                    
SITE     1 BC2  4 HIS A 383  HIS A 387  GLU A 411  ACT A1627                    
CRYST1   56.633   84.723  134.466  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017658  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011803  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007437        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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