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Database: PDB
Entry: 4C2Q
LinkDB: 4C2Q
Original site: 4C2Q 
HEADER    HYDROLASE                               19-AUG-13   4C2Q              
TITLE     CRYSTAL STRUCTURE OF HUMAN TESTIS ANGIOTENSIN-I CONVERTING            
TITLE    2 ENZYME MUTANT R522K                                                  
CAVEAT     4C2Q    FUC A 1103 PLANAR AT C1                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 68-656;                     
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143,     
COMPND   6  ANGIOTENSIN-CONVERTING ENZYME\,SOLUBLE FORM, ANGIOTENSIN-I          
COMPND   7  CONVERTING ENZYME;                                                  
COMPND   8 EC: 3.2.1.-, 3.4.15.1;                                               
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 ORGAN: TESTIS;                                                       
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHO CELLS;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PGEM11ZF                                  
KEYWDS    HYDROLASE, CHLORIDE ACTIVATION, HYPERTENSION                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MASUYER,C.J.YATES,S.L.U.SCHWAGER,A.MOHD,E.D.STURROCK,K.R.ACHARYA    
REVDAT   2   05-FEB-14 4C2Q    1       JRNL   LINK   HETATM ANISOU              
REVDAT   2 2                           CONECT MASTER                            
REVDAT   1   11-DEC-13 4C2Q    0                                                
JRNL        AUTH   C.J.YATES,G.MASUYER,S.L.U.SCHWAGER,A.MOHD,E.D.STURROCK,      
JRNL        AUTH 2 K.R.ACHARYA                                                  
JRNL        TITL   MOLECULAR AND THERMODYNAMIC MECHANISMS OF THE CHLORIDE       
JRNL        TITL 2 DEPENDENT HUMAN ANGIOTENSIN-I CONVERTING ENZYME (ACE)        
JRNL        REF    J.BIOL.CHEM.                  V. 289  1798 2014              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   24297181                                                     
JRNL        DOI    10.1074/JBC.M113.512335                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 66.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.88                          
REMARK   3   NUMBER OF REFLECTIONS             : 24379                          
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) : 0.19114                         
REMARK   3   R VALUE            (WORKING SET) : 0.18826                         
REMARK   3   FREE R VALUE                     : 0.24510                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1309                            
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) : 2.400                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.462                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1777                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.254                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 95                           
REMARK   3   BIN FREE R VALUE                    : 0.319                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4772                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 109                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.438                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.92                                                
REMARK   3    B22 (A**2) : -2.55                                                
REMARK   3    B33 (A**2) : 3.47                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.482         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.271         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.192         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.095        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4991 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4600 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6789 ; 1.249 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10576 ; 0.839 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   585 ; 5.754 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   246 ;36.645 ;24.309       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   812 ;14.958 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;19.342 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   720 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5611 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1200 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    40        A   625                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.4898   5.2698 -23.7838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0456 T22:   0.0327                                     
REMARK   3      T33:   0.0041 T12:   0.0053                                     
REMARK   3      T13:  -0.0127 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1066 L22:   0.3027                                     
REMARK   3      L33:   0.2998 L12:  -0.0659                                     
REMARK   3      L13:   0.0578 L23:  -0.1836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0294 S12:  -0.0192 S13:   0.0114                       
REMARK   3      S21:   0.0130 S22:   0.0210 S23:   0.0014                       
REMARK   3      S31:  -0.0148 S32:  -0.0193 S33:   0.0084                       
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 4C2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-AUG-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58094.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25732                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.80                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.3                                
REMARK 200  R MERGE                    (I) : 0.13                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.67                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.20                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1O8A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MIB BUFFER PH4.0, 10UM              
REMARK 280  ZINC SULFATE, 5% GLYCEROL, 15% PEG3350                              
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       28.32000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.83000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.52000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.83000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.32000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.52000            
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 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 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       79.56   -162.06                                   
REMARK 500    GLU A 123     -129.98     50.61                                   
REMARK 500    ALA A 296       70.79   -111.59                                   
REMARK 500    ASP A 300       96.38    -69.29                                   
REMARK 500    ARG A 348      126.66    -29.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE4 A 1203                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 383   NE2                                                    
REMARK 620 2 HIS A 387   NE2 110.7                                              
REMARK 620 3 GLU A 411   OE1  94.6 105.0                                        
REMARK 620 4 SO4 A1200   O4  131.7 114.5  89.7                                  
REMARK 620 5 SO4 A1200   S   112.4 111.8 120.9  33.2                            
REMARK 620 6 SO4 A1200   O3  109.8  83.1 149.9  61.0  33.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A1100  THROUGH FUC A1103  BOUND TO ASN A 109           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C2N   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN TESTIS ANGIOTENSIN-I                     
REMARK 900  CONVERTING ENZYME MUTANT E403R                                      
REMARK 900 RELATED ID: 4C2O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN TESTIS ANGIOTENSIN-I                     
REMARK 900  CONVERTING ENZYME MUTANT D465T                                      
REMARK 900 RELATED ID: 4C2P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN TESTIS ANGIOTENSIN-I                     
REMARK 900  CONVERTING ENZYME MUTANT R522K IN COMPLEX WITH CAPTOPRIL            
REMARK 900 RELATED ID: 4C2R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN TESTIS ANGIOTENSIN-I                     
REMARK 900  CONVERTING ENZYME MUTANT R522Q                                      
DBREF  4C2Q A   37   625  UNP    P12821   ACE_HUMAN       68    656             
SEQADV 4C2Q LYS A  522  UNP  P12821    ARG   553 ENGINEERED MUTATION            
SEQRES   1 A  589  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU          
SEQRES   2 A  589  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR          
SEQRES   3 A  589  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR          
SEQRES   4 A  589  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE          
SEQRES   5 A  589  ALA ASN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS          
SEQRES   6 A  589  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG          
SEQRES   7 A  589  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU          
SEQRES   8 A  589  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU          
SEQRES   9 A  589  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS          
SEQRES  10 A  589  PRO ASN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR          
SEQRES  11 A  589  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU          
SEQRES  12 A  589  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA          
SEQRES  13 A  589  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN          
SEQRES  14 A  589  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP          
SEQRES  15 A  589  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN          
SEQRES  16 A  589  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR          
SEQRES  17 A  589  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG          
SEQRES  18 A  589  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE          
SEQRES  19 A  589  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP          
SEQRES  20 A  589  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA          
SEQRES  21 A  589  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY          
SEQRES  22 A  589  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE          
SEQRES  23 A  589  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE          
SEQRES  24 A  589  TRP ASN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG          
SEQRES  25 A  589  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN          
SEQRES  26 A  589  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN          
SEQRES  27 A  589  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS          
SEQRES  28 A  589  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA          
SEQRES  29 A  589  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE          
SEQRES  30 A  589  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS          
SEQRES  31 A  589  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER          
SEQRES  32 A  589  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU          
SEQRES  33 A  589  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP          
SEQRES  34 A  589  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS          
SEQRES  35 A  589  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS          
SEQRES  36 A  589  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY          
SEQRES  37 A  589  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER          
SEQRES  38 A  589  VAL PRO TYR ILE LYS TYR PHE VAL SER PHE ILE ILE GLN          
SEQRES  39 A  589  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS          
SEQRES  40 A  589  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS          
SEQRES  41 A  589  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY          
SEQRES  42 A  589  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR          
SEQRES  43 A  589  GLY GLN PRO ASN MET SER ALA SER ALA MET LEU SER TYR          
SEQRES  44 A  589  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU          
SEQRES  45 A  589  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP          
SEQRES  46 A  589  THR PRO ASN SER                                              
HET     ZN  A1001       1                                                       
HET     CL  A1002       1                                                       
HET    NAG  A1100      14                                                       
HET    NAG  A1101      14                                                       
HET    BMA  A1102      11                                                       
HET    FUC  A1103      10                                                       
HET    SO4  A1200       5                                                       
HET    ACT  A1201       4                                                       
HET    PE4  A1203      16                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-                      
HETNAM   2 PE4  ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     BMA BETA-D-MANNOSE                                                   
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  PE4    C16 H34 O8                                                   
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  FUC    C6 H12 O5                                                    
FORMUL   8   CL    CL 1-                                                        
FORMUL   9  BMA    C6 H12 O6                                                    
FORMUL  10  HOH   *109(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 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  LEU A  194  1                                  21    
HELIX    9   9 PHE A  196  ASN A  211  1                                  16    
HELIX   10  10 ASP A  215  MET A  223  1                                   9    
HELIX   11  11 SER A  228  LEU A  240  1                                  13    
HELIX   12  12 LEU A  240  GLY A  260  1                                  21    
HELIX   13  13 ALA A  261  ILE A  264  5                                   4    
HELIX   14  14 TRP A  283  ASN A  285  5                                   3    
HELIX   15  15 ILE A  286  VAL A  291  1                                   6    
HELIX   16  16 ASP A  300  GLN A  308  1                                   9    
HELIX   17  17 THR A  311  LEU A  326  1                                  16    
HELIX   18  18 PRO A  332  SER A  339  1                                   8    
HELIX   19  19 ASN A  374  TYR A  394  1                                  21    
HELIX   20  20 PRO A  398  ARG A  402  5                                   5    
HELIX   21  21 ASN A  406  SER A  422  1                                  17    
HELIX   22  22 THR A  423  LEU A  430  1                                   8    
HELIX   23  23 SER A  439  ILE A  455  1                                  17    
HELIX   24  24 ALA A  456  ASP A  473  1                                  18    
HELIX   25  25 ASN A  480  TYR A  492  1                                  13    
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  HIS A  610  1                                  22    
SHEET    1  AA 2 VAL A 151  CYS A 152  0                                        
SHEET    2  AA 2 CYS A 158  LEU A 159 -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  2.07  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.04  
LINK         ND2 ASN A 109                 C1  NAG A1100     1555   1555  1.44  
LINK        ZN    ZN A1001                 NE2 HIS A 387     1555   1555  2.18  
LINK        ZN    ZN A1001                 OE1 GLU A 411     1555   1555  1.90  
LINK        ZN    ZN A1001                 O4  SO4 A1200     1555   1555  2.46  
LINK        ZN    ZN A1001                 O3  SO4 A1200     1555   1555  2.39  
LINK        ZN    ZN A1001                 NE2 HIS A 383     1555   1555  2.12  
LINK         O6  NAG A1100                 C1  FUC A1103     1555   1555  1.43  
LINK         O4  NAG A1100                 C1  NAG A1101     1555   1555  1.44  
LINK         O4  NAG A1101                 C1  BMA A1102     1555   1555  1.44  
CISPEP   1 GLU A  162    PRO A  163          0         1.72                     
SITE     1 AC1  4 HIS A 383  HIS A 387  GLU A 411  SO4 A1200                    
SITE     1 AC2  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 AC3 10 HIS A 353  ALA A 354  HIS A 383  GLU A 384                    
SITE     2 AC3 10 HIS A 387  GLU A 411  TYR A 523   ZN A1001                    
SITE     3 AC3 10 HOH A2068  HOH A2069                                          
SITE     1 AC4  6 GLN A 281  HIS A 353  LYS A 511  HIS A 513                    
SITE     2 AC4  6 TYR A 520  HOH A2094                                          
SITE     1 AC5  4 LEU A 375  GLU A 376  LYS A 449  ASP A 453                    
SITE     1 AC6  6 GLU A  43  SER A  45  GLU A  49  LYS A 101                    
SITE     2 AC6  6 ASN A 109  HOH A2109                                          
CRYST1   56.640   85.040  133.660  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      0.017655  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011759  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007482        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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