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Database: PDB
Entry: 2OC2
LinkDB: 2OC2
Original site: 2OC2 
HEADER    HYDROLASE                               20-DEC-06   2OC2              
TITLE     STRUCTURE OF TESTIS ACE WITH RXPA380                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PEPTIDASE M2 2 (RESIDUES 631-1232);                        
COMPND   5 SYNONYM: DIPEPTIDYL CARBOXYPEPTIDASE I; KININASE II; CD143 ANTIGEN;  
COMPND   6 EC: 3.4.15.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACE, DCP, DCP1;                                                
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: CHO-K1;                                    
SOURCE  10 EXPRESSION_SYSTEM_CELL: HAMPSTER OVARY CELLS;                        
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PEE-ACEDELTA36NJ                          
KEYWDS    ENZYME-INHIBITOR COMPLEX, HYDROLASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.R.CORRADI,C.S.ANTHONY,S.L.SCHWAGER,P.REDELINGHUYS,D.GEORGIADIS,     
AUTHOR   2 V.DIVE,K.R.ACHARYA,E.D.STURROCK                                      
REVDAT   4   11-APR-12 2OC2    1       REMARK VERSN                             
REVDAT   3   22-SEP-10 2OC2    1       AUTHOR JRNL                              
REVDAT   2   24-FEB-09 2OC2    1       VERSN                                    
REVDAT   1   22-MAY-07 2OC2    0                                                
JRNL        AUTH   C.S.ANTHONY,H.R.CORRADI,S.L.SCHWAGER,P.REDELINGHUYS,         
JRNL        AUTH 2 D.GEORGIADIS,V.DIVE,K.R.ACHARYA,E.D.STURROCK                 
JRNL        TITL   THE N DOMAIN OF HUMAN ANGIOTENSIN-I CONVERTING ENZYME: THE   
JRNL        TITL 2 ROLE OF N-GLYCOSYLATION AND THE CRYSTAL STRUCTURE IN COMPLEX 
JRNL        TITL 3 WITH AN N DOMAIN SPECIFIC PHOSPHINIC INHIBITOR RXP407.       
JRNL        REF    J.BIOL.CHEM.                  V.  46  5473 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20826823                                                     
JRNL        DOI    10.1074/JBC.M110.167866                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
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) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 72.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 22492                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 926                             
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1258                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 43                           
REMARK   3   BIN FREE R VALUE                    : 0.4190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4751                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 107                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.842         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.317         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.195         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.760         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4920 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6701 ; 1.207 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   583 ; 5.344 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   242 ;36.012 ;24.132       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   789 ;15.972 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;19.926 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   699 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3833 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2465 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3344 ; 0.297 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   212 ; 0.137 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.071 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    51 ; 0.210 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.159 ; 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):  2999 ; 0.403 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4703 ; 0.695 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2253 ; 0.907 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1997 ; 1.392 ; 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2OC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB040947.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 4.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8073                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22494                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 72.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.530                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHASES KNOWN                 
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: TESTIS ACE                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13.5% PEG 4000, 0.12M NA MALONATE,       
REMARK 280  90MM NA ACETATE PH 4.7, 9UM ZN ACETATE , VAPOR DIFFUSION, HANGING   
REMARK 280  DROP, TEMPERATURE 289K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.25700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.74150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.38150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.74150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.25700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.38150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A    37                                                      
REMARK 465     VAL A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A   436                                                      
REMARK 465     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; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   79   CG   CD   CE   NZ                                   
REMARK 480     GLN A   98   CG   CD   OE1  NE2                                  
REMARK 480     ASN A  105   CG   OD1  ND2                                       
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     GLU A  303   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  307   CG   CD   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    GLN A  98   CB    GLN A  98   CG     -0.456                       
REMARK 500    ASN A 105   CB    ASN A 105   CG      0.277                       
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    GLN A  98   CA  -  CB  -  CG  ANGL. DEV. =  18.9 DEGREES          
REMARK 500    GLN A 108   CB  -  CA  -  C   ANGL. DEV. = -19.3 DEGREES          
REMARK 500    GLN A 108   N   -  CA  -  CB  ANGL. DEV. =  36.8 DEGREES          
REMARK 500    GLN A 108   CA  -  CB  -  CG  ANGL. DEV. =  31.1 DEGREES          
REMARK 500    LYS A 113   CG  -  CD  -  CE  ANGL. DEV. =  46.0 DEGREES          
REMARK 500    LYS A 113   CD  -  CE  -  NZ  ANGL. DEV. =  25.8 DEGREES          
REMARK 500    GLU A 303   CA  -  CB  -  CG  ANGL. DEV. =  20.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  72       75.95   -169.24                                   
REMARK 500    GLU A 123     -126.19     39.91                                   
REMARK 500    ASN A 155       -9.99    -57.97                                   
REMARK 500    ASP A 300       93.37    -66.30                                   
REMARK 500    ASP A 346       24.53    -77.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLN A 108        12.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 RX3 A 680   O3                                                     
REMARK 620 2 HIS A 387   NE2 133.3                                              
REMARK 620 3 RX3 A 680   O4   68.2  84.4                                        
REMARK 620 4 GLU A 411   OE1  92.6 103.0 158.2                                  
REMARK 620 5 HIS A 383   NE2 113.6 109.4 104.0  92.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: N-({(1S,2R)-2-[(S)-[(1R)-1-{[(BENZYLOXY)CARBONYL]     
REMARK 630 AMINO}-2-PHENYLETHYL](HYDROXY)PHOSPHORYL]CYCLOPENTYL}CARBONYL)-L-    
REMARK 630 TRYPTOPHAN                                                           
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     RX3 A   680                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    PHQ PPH IQ0 TRP                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RX3 A 680                 
DBREF  2OC2 A   37   627  UNP    P12821   ACE_HUMAN      642   1232             
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 ASN 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 ASN 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 ASN 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 ASN 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     ZN  A 701       1                                                       
HET     CL  A 703       1                                                       
HET     CL  A 704       1                                                       
HET    RX3  A 680      44                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     RX3 N-({(1S,2R)-2-[(S)-[(1R)-1-{[(BENZYLOXY)                         
HETNAM   2 RX3  CARBONYL]AMINO}-2-PHENYLETHYL](HYDROXY)                         
HETNAM   3 RX3  PHOSPHORYL]CYCLOPENTYL}CARBONYL)-L-TRYPTOPHAN                   
HETSYN     RX3 RXPA380                                                          
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  RX3    C33 H36 N3 O7 P                                              
FORMUL   6  HOH   *107(H2 O)                                                    
HELIX    1   1 ASP A   40  THR A   71  1                                  32    
HELIX    2   2 THR A   74  ARG A  100  1                                  27    
HELIX    3   3 LYS A  101  PHE A  102  5                                   2    
HELIX    4   4 ASP A  103  LEU A  107  5                                   5    
HELIX    5   5 ASN A  109  ASP A  121  1                                  13    
HELIX    6   6 LEU A  122  LEU A  127  5                                   6    
HELIX    7   7 PRO A  128  ALA A  149  1                                  22    
HELIX    8   8 PRO A  163  SER A  172  1                                  10    
HELIX    9   9 LYS A  174  LEU A  194  1                                  21    
HELIX   10  10 PHE A  196  LEU A  210  1                                  15    
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  GLY A  569  1                                  15    
HELIX   30  30 PRO A  573  GLY A  583  1                                  11    
HELIX   31  31 ALA A  589  GLY A  611  1                                  23    
SHEET    1   A 2 VAL A 151  CYS A 152  0                                        
SHEET    2   A 2 CYS A 158  LEU A 159 -1  O  LEU A 159   N  VAL A 151           
SHEET    1   B 2 ILE A 270  PRO A 271  0                                        
SHEET    2   B 2 LEU A 495  CYS A 496  1  O  CYS A 496   N  ILE A 270           
SHEET    1   C 2 SER A 355  ASP A 358  0                                        
SHEET    2   C 2 PHE A 365  LYS A 368 -1  O  ARG A 366   N  TRP A 357           
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.03  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.04  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.02  
LINK         O3  RX3 A 680                ZN    ZN A 701     1555   1555  1.97  
LINK        ZN    ZN A 701                 NE2 HIS A 387     1555   1555  2.01  
LINK        ZN    ZN A 701                 O4  RX3 A 680     1555   1555  2.46  
LINK        ZN    ZN A 701                 OE1 GLU A 411     1555   1555  1.91  
LINK        ZN    ZN A 701                 NE2 HIS A 383     1555   1555  2.00  
CISPEP   1 GLU A  162    PRO A  163          0         2.39                     
SITE     1 AC1  4 HIS A 383  HIS A 387  GLU A 411  RX3 A 680                    
SITE     1 AC2  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC3  4 TYR A 224  PRO A 519  ARG A 522  HOH A 763                    
SITE     1 AC4 21 GLN A 281  HIS A 353  ALA A 354  SER A 355                    
SITE     2 AC4 21 ALA A 356  HIS A 383  GLU A 384  HIS A 387                    
SITE     3 AC4 21 PHE A 391  HIS A 410  GLU A 411  ASP A 415                    
SITE     4 AC4 21 PHE A 457  LYS A 511  PHE A 512  HIS A 513                    
SITE     5 AC4 21 VAL A 518  TYR A 520  TYR A 523   ZN A 701                    
SITE     6 AC4 21 HOH A 786                                                     
CRYST1   56.514   84.763  133.483  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      0.017695  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011798  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007492        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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