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Database: PDB
Entry: 2C6N
LinkDB: 2C6N
Original site: 2C6N 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           10-NOV-05   2C6N              
TITLE     STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN  
TITLE    2 WITH LISINOPRIL                                                      
CAVEAT     2C6N    ILE B 530 HAS WRONG CHIRALITY AT ATOM CB NAG B 696 HAS WRONG 
CAVEAT   2 2C6N    CHIRALITY AT ATOM C2 NAG B 693 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 2C6N    C1 CHIRALITY ERROR AT THE CB CENTER OF ILE 530 B             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM;            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N DOMAIN, RESIDUES 38-649;                                 
COMPND   5 SYNONYM: SOMATIC ANGIOTENSIN-I CONVERTING ENZYME N DOMAIN, DIPEPTIDYL
COMPND   6 CARBOXYPEPTIDASE I, KININASE II, CD143 ANTIGEN;                      
COMPND   7 EC: 3.4.15.1;                                                        
COMPND   8 ENGINEERED: 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: CHO-K1;                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PEE14                                      
KEYWDS    HYDROLASE, ANGIOTENSIN-I CONVERTING ENZYME, N DOMAIN, ZINC            
KEYWDS   2 METALLOPEPTIDASE, METALLOPROTEASE, ANGIOTENSIN, LISINOPRIL,          
KEYWDS   3 CARBOXYPEPTIDASE, GLYCOPROTEIN, METAL-BINDING, PHOSPHORYLATION,      
KEYWDS   4 PROTEASE, TRANSMEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.R.CORRADI,S.L.U.SCHWAGER,A.NICHINDA,E.D.STURROCK,K.R.ACHARYA        
REVDAT   6   25-JUL-18 2C6N    1       CAVEAT COMPND SOURCE JRNL                
REVDAT   6 2                   1       REMARK HET    HETNAM FORMUL              
REVDAT   6 3                   1       LINK   ATOM                              
REVDAT   5   15-APR-15 2C6N    1       SOURCE JRNL   REMARK                     
REVDAT   4   13-JUL-11 2C6N    1       VERSN                                    
REVDAT   3   24-FEB-09 2C6N    1       VERSN                                    
REVDAT   2   22-MAR-06 2C6N    1       SOURCE JRNL                              
REVDAT   1   15-MAR-06 2C6N    0                                                
JRNL        AUTH   H.R.CORRADI,S.L.SCHWAGER,A.T.NCHINDA,E.D.STURROCK,           
JRNL        AUTH 2 K.R.ACHARYA                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE N DOMAIN OF HUMAN SOMATIC           
JRNL        TITL 2 ANGIOTENSIN I-CONVERTING ENZYME PROVIDES A STRUCTURAL BASIS  
JRNL        TITL 3 FOR DOMAIN-SPECIFIC INHIBITOR DESIGN.                        
JRNL        REF    J. MOL. BIOL.                 V. 357   964 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16476442                                                     
JRNL        DOI    10.1016/J.JMB.2006.01.048                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2443102.530                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 35238                          
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 SET) : 0.294                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 903                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5119                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3750                       
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 130                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9412                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 190                                     
REMARK   3   SOLVENT ATOMS            : 19                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.50                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.61                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.54                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.950                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 39.17                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2C6N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-NOV-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290026323.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.90                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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 CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36858                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: 1O8A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULPHATE, 0.1M SODIUM       
REMARK 280  ACETATE, PH 4.9, 10UM ZINC SULPHATE, 18% POLYETHYLENE GLYCOL        
REMARK 280  4000, PH 4.90                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.50000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.50000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      105.45000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      105.45000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.50000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      105.45000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.50000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.65000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      105.45000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU B     1                                                      
REMARK 465     ASN B   276                                                      
REMARK 465     ASP B   612                                                      
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     LEU A   1    CG   CD1  CD2                                       
REMARK 470     GLN A  18    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  22    CG   CD   OE1  NE2                                  
REMARK 470     SER A  23    OG                                                  
REMARK 470     TYR A  24    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A  26    OG                                                  
REMARK 470     GLN A  30    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  49    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  56    CG   CD   OE1  OE2                                  
REMARK 470     LEU A  60    CG   CD1  CD2                                       
REMARK 470     GLN A  70    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  71    CG   CD   CE   NZ                                   
REMARK 470     GLU A  74    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  79    CG1  CG2  CD1                                       
REMARK 470     TRP A  80    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  80    CZ3  CH2                                            
REMARK 470     GLN A  81    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  88    CG   CD1  CD2                                       
REMARK 470     ARG A  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  98    CG   CD1  CD2                                       
REMARK 470     LEU A 105    CG   CD1  CD2                                       
REMARK 470     ASN A 131    CG   OD1  ND2                                       
REMARK 470     LYS A 132    CG   CD   CE   NZ                                   
REMARK 470     THR A 133    OG1  CG2                                            
REMARK 470     THR A 135    OG1  CG2                                            
REMARK 470     GLN A 188    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 203    CG   OD1  ND2                                       
REMARK 470     ARG A 240    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 273    CG   OD1  OD2                                       
REMARK 470     ASN A 276    CG   OD1  ND2                                       
REMARK 470     ASP A 278    CG   OD1  OD2                                       
REMARK 470     THR A 280    OG1  CG2                                            
REMARK 470     SER A 281    OG                                                  
REMARK 470     GLN A 285    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 289    CG   OD1  ND2                                       
REMARK 470     THR A 291    OG1  CG2                                            
REMARK 470     HIS A 292    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A 296    CG1  CG2                                            
REMARK 470     SER A 303    OG                                                  
REMARK 470     GLU A 305    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 315    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 321    CG   CD   CE   NZ                                   
REMARK 470     ASP A 324    CG   OD1  OD2                                       
REMARK 470     GLU A 327    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 340    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 341    CG   CD   CE   NZ                                   
REMARK 470     ARG A 344    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 353    CG   SD   CE                                        
REMARK 470     SER A 357    OG                                                  
REMARK 470     LEU A 375    CG   CD1  CD2                                       
REMARK 470     VAL A 377    CG1  CG2                                            
REMARK 470     ARG A 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 403    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 407    CG   CD   CE   NZ                                   
REMARK 470     LEU A 410    CG   CD1  CD2                                       
REMARK 470     ASP A 412    CG   OD1  OD2                                       
REMARK 470     ARG A 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 414    CG1  CG2                                            
REMARK 470     THR A 415    OG1  CG2                                            
REMARK 470     ASN A 416    CG   OD1  ND2                                       
REMARK 470     LEU A 515    CG   CD1  CD2                                       
REMARK 470     LYS A 542    CG   CD   CE   NZ                                   
REMARK 470     GLN A 545    CG   CD   OE1  NE2                                  
REMARK 470     SER A 548    OG                                                  
REMARK 470     GLN A 568    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 609    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 611    CG1  CG2  CD1                                       
REMARK 470     ASP A 612    CG   OD1  OD2                                       
REMARK 470     ASP B   2    CG   OD1  OD2                                       
REMARK 470     GLN B   6    CG   CD   OE1  NE2                                  
REMARK 470     ASN B   9    CG   OD1  ND2                                       
REMARK 470     SER B  11    OG                                                  
REMARK 470     ASP B  13    CG   OD1  OD2                                       
REMARK 470     GLU B  14    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  18    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  19    CG   CD1  CD2                                       
REMARK 470     GLN B  22    CG   CD   OE1  NE2                                  
REMARK 470     SER B  23    OG                                                  
REMARK 470     TYR B  24    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B  26    OG                                                  
REMARK 470     GLN B  34    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  52    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  56    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  70    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  71    CG   CD   CE   NZ                                   
REMARK 470     LYS B  73    CG   CD   CE   NZ                                   
REMARK 470     GLU B  74    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  79    CG1  CG2  CD1                                       
REMARK 470     GLN B  81    CG   CD   OE1  NE2                                  
REMARK 470     PHE B  83    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B  84    OG1  CG2                                            
REMARK 470     LEU B  88    CG   CD1  CD2                                       
REMARK 470     ARG B  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 105    CG   CD1  CD2                                       
REMARK 470     LYS B 126    CG   CD   CE   NZ                                   
REMARK 470     LYS B 132    CG   CD   CE   NZ                                   
REMARK 470     THR B 133    OG1  CG2                                            
REMARK 470     THR B 135    OG1  CG2                                            
REMARK 470     GLU B 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     SER B 200    OG                                                  
REMARK 470     ASN B 203    CG   OD1  ND2                                       
REMARK 470     SER B 204    OG                                                  
REMARK 470     GLU B 262    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 269    CG1  CG2                                            
REMARK 470     LYS B 274    CG   CD   CE   NZ                                   
REMARK 470     LEU B 277    CG   CD1  CD2                                       
REMARK 470     LEU B 284    CG   CD1  CD2                                       
REMARK 470     GLN B 285    CG   CD   OE1  NE2                                  
REMARK 470     HIS B 292    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B 295    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 299    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 306    CG   CD1  CD2                                       
REMARK 470     GLU B 312    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 315    CG   CD   OE1  OE2                                  
REMARK 470     SER B 317    OG                                                  
REMARK 470     SER B 333    OG                                                  
REMARK 470     LYS B 341    CG   CD   CE   NZ                                   
REMARK 470     ARG B 344    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 345    CG1  CG2  CD1                                       
REMARK 470     ARG B 350    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 353    CG   SD   CE                                        
REMARK 470     ASP B 354    CG   OD1  OD2                                       
REMARK 470     GLN B 355    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 356    CG   CD1  CD2                                       
REMARK 470     ASP B 374    CG   OD1  OD2                                       
REMARK 470     LEU B 375    CG   CD1  CD2                                       
REMARK 470     VAL B 377    CG1  CG2                                            
REMARK 470     ARG B 380    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER B 400    OG                                                  
REMARK 470     GLU B 403    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 405    CG   CD1  CD2                                       
REMARK 470     LEU B 410    CG   CD1  CD2                                       
REMARK 470     ASP B 412    CG   OD1  OD2                                       
REMARK 470     ARG B 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 444    CG   CD   OE1  NE2                                  
REMARK 470     SER B 451    OG                                                  
REMARK 470     GLU B 513    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 515    CG   CD1  CD2                                       
REMARK 470     GLU B 522    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 530    CD1                                                 
REMARK 470     SER B 533    OG                                                  
REMARK 470     LYS B 535    CG   CD   CE   NZ                                   
REMARK 470     LYS B 539    CG   CD   CE   NZ                                   
REMARK 470     SER B 548    OG                                                  
REMARK 470     ARG B 550    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 553    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 555    CG1  CG2                                            
REMARK 470     LEU B 562    CG   CD1  CD2                                       
REMARK 470     GLN B 568    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 609    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 611    CG1  CG2  CD1                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE A   46   CD1                                                 
REMARK 480     ILE A   92   CD1                                                 
REMARK 480     LYS A  126   CE   NZ                                             
REMARK 480     LYS A  274   CD   CE   NZ                                        
REMARK 480     GLU B   66   CD   OE1  OE2                                       
REMARK 480     LEU B   98   CD1  CD2                                            
REMARK 480     ILE B  408   CD1                                                 
REMARK 480     LYS B  427   CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY A    16     OH   TYR A    76              1.99            
REMARK 500   O    GLY B     4     N    GLN B     6              2.03            
REMARK 500   ND2  ASN B   480     O5   NAG B   691              2.06            
REMARK 500   OD1  ASN A   480     C1   NAG A   691              2.07            
REMARK 500   O    LEU B   129     N    ASN B   131              2.08            
REMARK 500   NH1  ARG B   235     O    HOH B  2004              2.10            
REMARK 500   O    THR B   280     N    MET B   283              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 381   CB    ARG A 381   CG      0.221                       
REMARK 500    ARG A 381   CG    ARG A 381   CD      0.151                       
REMARK 500    ASN B  25   CB    ASN B  25   CG     -0.147                       
REMARK 500    ARG B 541   CB    ARG B 541   CG      0.167                       
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    GLU A  63   C   -  N   -  CA  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    LEU A 174   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    THR A 280   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    THR A 349   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    VAL A 351   N   -  CA  -  CB  ANGL. DEV. = -17.1 DEGREES          
REMARK 500    ARG A 380   N   -  CA  -  C   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    ARG A 380   CA  -  C   -  N   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ARG A 381   CB  -  CA  -  C   ANGL. DEV. =  12.7 DEGREES          
REMARK 500    PRO A 402   C   -  N   -  CA  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    GLY A 523   N   -  CA  -  C   ANGL. DEV. = -20.9 DEGREES          
REMARK 500    PRO A 524   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 550   CA  -  CB  -  CG  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    PRO A 551   C   -  N   -  CA  ANGL. DEV. =  10.8 DEGREES          
REMARK 500    PRO B   3   N   -  CA  -  C   ANGL. DEV. =  20.9 DEGREES          
REMARK 500    LEU B   5   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    TYR B  76   N   -  CA  -  C   ANGL. DEV. =  22.2 DEGREES          
REMARK 500    PRO B  78   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO B  78   C   -  N   -  CD  ANGL. DEV. = -27.3 DEGREES          
REMARK 500    GLU B 305   N   -  CA  -  C   ANGL. DEV. =  26.5 DEGREES          
REMARK 500    PRO B 308   C   -  N   -  CD  ANGL. DEV. = -31.9 DEGREES          
REMARK 500    ARG B 350   C   -  N   -  CA  ANGL. DEV. = -18.7 DEGREES          
REMARK 500    LEU B 441   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ARG B 541   C   -  N   -  CA  ANGL. DEV. = -16.9 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    PRO A   7      -91.50    -39.22                                   
REMARK 500    ARG A  53      -70.15    -59.48                                   
REMARK 500    LEU A  75       -4.48   -140.27                                   
REMARK 500    GLN A  81       -0.81     94.18                                   
REMARK 500    GLN A  87        3.61    -59.57                                   
REMARK 500    ALA A 101       -1.17    -53.44                                   
REMARK 500    PRO A 104      152.45    -50.00                                   
REMARK 500    TYR A 111      -73.34    -45.25                                   
REMARK 500    PRO A 130      -71.05    -65.98                                   
REMARK 500    LYS A 132      104.85    -58.65                                   
REMARK 500    THR A 133       71.21    -64.59                                   
REMARK 500    ASP A 189       20.73    -79.55                                   
REMARK 500    PHE A 191      176.15    -58.01                                   
REMARK 500    ALA A 250      -13.77    -47.89                                   
REMARK 500    MET A 256      -35.87    -37.85                                   
REMARK 500    GLU A 262        1.19    -55.16                                   
REMARK 500    VAL A 269      118.27    -38.77                                   
REMARK 500    PRO A 272     -164.05    -76.04                                   
REMARK 500    LEU A 277       41.17    -81.82                                   
REMARK 500    GLU A 298      -73.29    -60.36                                   
REMARK 500    GLU A 299      -27.67    -35.98                                   
REMARK 500    LEU A 304       47.49    -78.17                                   
REMARK 500    PRO A 322      165.70    -42.24                                   
REMARK 500    ASP A 324        0.21    -67.85                                   
REMARK 500    ARG A 326       91.87    -63.44                                   
REMARK 500    GLU A 327      114.36    -34.18                                   
REMARK 500    ARG A 340       10.66     50.78                                   
REMARK 500    GLN A 347      143.13   -172.67                                   
REMARK 500    VAL A 351       53.94     36.43                                   
REMARK 500    ASP A 374       42.60    -75.53                                   
REMARK 500    PRO A 376     -158.48    -65.62                                   
REMARK 500    ARG A 380      -16.91   -141.39                                   
REMARK 500    ILE A 391      -49.73    -29.23                                   
REMARK 500    ASN A 416       45.53    -82.90                                   
REMARK 500    ASP A 417     -166.90   -105.55                                   
REMARK 500    ARG A 458       25.58   -141.79                                   
REMARK 500    GLU A 481       36.96    -87.42                                   
REMARK 500    PHE A 484       74.19   -150.83                                   
REMARK 500    PHE A 490      -38.40    -31.48                                   
REMARK 500    VAL A 495       68.55     36.31                                   
REMARK 500    ILE A 499       -0.52    -53.13                                   
REMARK 500    ILE A 530       28.39    -74.24                                   
REMARK 500    ARG A 532       18.07     49.24                                   
REMARK 500    GLN A 545        3.65    -65.18                                   
REMARK 500    GLU A 596       54.23    -90.60                                   
REMARK 500    GLN A 598      -11.92     82.60                                   
REMARK 500    PRO A 604     -156.85    -55.72                                   
REMARK 500    ASN A 606       97.47   -160.89                                   
REMARK 500    PRO B   3     -130.31     -0.42                                   
REMARK 500    LEU B   5       70.50    -64.65                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      92 RAMACHANDRAN OUTLIERS.                        
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 PHE B   83     THR B   84                  149.98                    
REMARK 500 ASP B   85     PRO B   86                  114.34                    
REMARK 500 PRO B   86     GLN B   87                   87.10                    
REMARK 500 ASP B  140     PRO B  141                   34.38                    
REMARK 500 GLU B  609     GLY B  610                  148.15                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  76         0.08    SIDE CHAIN                              
REMARK 500    TYR B 215         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A 380        -10.00                                           
REMARK 500    ARG B 541         11.74                                           
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 HIS A 365   NE2                                                    
REMARK 620 2 LPR A 705   O3  116.7                                              
REMARK 620 3 GLU A 389   OE1 103.0  95.6                                        
REMARK 620 4 LPR A 705   O2  101.2  50.2 144.7                                  
REMARK 620 5 HIS A 361   NE2 108.7 118.4 112.8  82.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 365   NE2                                                    
REMARK 620 2 GLU B 389   OE1  83.4                                              
REMARK 620 3 LPR B 705   O2   94.4 153.7                                        
REMARK 620 4 LPR B 705   O3  126.5  94.1  66.1                                  
REMARK 620 5 HIS B 361   NE2 106.8 122.6  83.2 118.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: OLIGOPEPTIDE ENZYME INHIBITOR                         
REMARK 630 MOLECULE NAME: [N2-[(S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-PROLINE  
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     LPR A   705                                                      
REMARK 630     LPR B   705                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    CLT LYS PRO                                              
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 NAG A 691                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 696                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 691                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 696                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LPR A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LPR B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A2433                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A2434                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C6F   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN 
DBREF  2C6N A    1   612  UNP    Q59GY8   ACE_HUMAN       38    649             
DBREF  2C6N B    1   612  UNP    Q59GY8   ACE_HUMAN       38    649             
SEQRES   1 A  612  LEU ASP PRO GLY LEU GLN PRO GLY ASN PHE SER ALA ASP          
SEQRES   2 A  612  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR ASN SER          
SEQRES   3 A  612  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 A  612  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 A  612  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 A  612  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 A  612  ILE TRP GLN ASN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 A  612  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 A  612  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER ASN          
SEQRES  10 A  612  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 A  612  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 A  612  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 A  612  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 A  612  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 A  612  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 A  612  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 A  612  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 A  612  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 A  612  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 A  612  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 A  612  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 A  612  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 A  612  GLY TRP ASN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 A  612  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 A  612  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 A  612  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 A  612  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 A  612  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 A  612  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 A  612  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 A  612  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 A  612  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 A  612  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 A  612  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 A  612  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 A  612  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 A  612  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 A  612  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 A  612  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 A  612  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 A  612  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 A  612  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU GLN ALA          
SEQRES  43 A  612  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 A  612  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 A  612  TYR PHE GLN PRO VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 A  612  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 A  612  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 A  612  ASP                                                          
SEQRES   1 B  612  LEU ASP PRO GLY LEU GLN PRO GLY ASN PHE SER ALA ASP          
SEQRES   2 B  612  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR ASN SER          
SEQRES   3 B  612  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 B  612  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 B  612  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 B  612  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 B  612  ILE TRP GLN ASN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 B  612  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 B  612  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER ASN          
SEQRES  10 B  612  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 B  612  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 B  612  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 B  612  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 B  612  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 B  612  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 B  612  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 B  612  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 B  612  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 B  612  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 B  612  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 B  612  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 B  612  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 B  612  GLY TRP ASN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 B  612  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 B  612  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 B  612  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 B  612  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 B  612  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 B  612  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 B  612  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 B  612  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 B  612  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 B  612  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 B  612  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 B  612  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 B  612  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 B  612  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 B  612  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 B  612  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 B  612  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 B  612  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 B  612  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU GLN ALA          
SEQRES  43 B  612  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 B  612  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 B  612  TYR PHE GLN PRO VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 B  612  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 B  612  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 B  612  ASP                                                          
MODRES 2C6N ASN A   25  ASN  GLYCOSYLATION SITE                                 
MODRES 2C6N ASN A  117  ASN  GLYCOSYLATION SITE                                 
MODRES 2C6N ASN A  480  ASN  GLYCOSYLATION SITE                                 
MODRES 2C6N ASN B   25  ASN  GLYCOSYLATION SITE                                 
MODRES 2C6N ASN B  117  ASN  GLYCOSYLATION SITE                                 
MODRES 2C6N ASN B  480  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 691      14                                                       
HET    NAG  A 696      14                                                       
HET    NAG  A 693      14                                                       
HET    NAG  A 695      14                                                       
HET     ZN  A 701       1                                                       
HET     CL  A 703       1                                                       
HET    LPR  A 705      29                                                       
HET    GOL  A2433       6                                                       
HET    GOL  A2434       6                                                       
HET    NAG  B 691      14                                                       
HET    NAG  B 696      14                                                       
HET    NAG  B 693      14                                                       
HET    NAG  B 695      14                                                       
HET     ZN  B 701       1                                                       
HET     CL  B 702       1                                                       
HET    LPR  B 705      29                                                       
HET    ACT  B 710       4                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     LPR [N2-[(S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-PROLINE             
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETSYN     LPR LISINOPRIL                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    8(C8 H15 N O6)                                               
FORMUL   6   ZN    2(ZN 2+)                                                     
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL   8  LPR    2(C21 H31 N3 O5)                                             
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  17  ACT    C2 H3 O2 1-                                                  
FORMUL  18  HOH   *19(H2 O)                                                     
HELIX    1   1 ASP A    2  GLN A    6  5                                   5    
HELIX    2   2 ASP A   13  ALA A   15  5                                   3    
HELIX    3   3 GLY A   16  ASN A   45  1                                  30    
HELIX    4   4 THR A   47  GLU A   77  1                                  31    
HELIX    5   5 ASP A   85  ARG A   96  1                                  12    
HELIX    6   6 PRO A  104  ALA A  125  1                                  22    
HELIX    7   7 PRO A  141  SER A  150  1                                  10    
HELIX    8   8 SER A  152  LYS A  187  1                                  36    
HELIX    9   9 ASP A  193  ARG A  199  1                                   7    
HELIX   10  10 THR A  206  GLY A  238  1                                  33    
HELIX   11  11 ILE A  264  VAL A  269  1                                   6    
HELIX   12  12 SER A  281  GLY A  287  1                                   7    
HELIX   13  13 ASN A  289  LEU A  304  1                                  16    
HELIX   14  14 PRO A  310  GLY A  316  1                                   7    
HELIX   15  15 THR A  352  LYS A  373  1                                  22    
HELIX   16  16 ASN A  384  ILE A  408  1                                  25    
HELIX   17  17 ASP A  417  ILE A  433  1                                  17    
HELIX   18  18 ALA A  434  SER A  451  1                                  18    
HELIX   19  19 PRO A  455  SER A  457  5                                   3    
HELIX   20  20 ARG A  458  GLY A  472  1                                  15    
HELIX   21  21 ASP A  485  LYS A  489  5                                   5    
HELIX   22  22 TYR A  498  GLY A  520  1                                  23    
HELIX   23  23 PRO A  524  CYS A  528  5                                   5    
HELIX   24  24 SER A  533  GLN A  545  1                                  13    
HELIX   25  25 PRO A  551  GLY A  561  1                                  11    
HELIX   26  26 ALA A  567  ASN A  588  1                                  22    
HELIX   27  27 GLU B   14  ASN B   45  1                                  32    
HELIX   28  28 ALA B   48  GLU B   77  1                                  30    
HELIX   29  29 GLN B   87  ARG B   96  1                                  10    
HELIX   30  30 LEU B   98  LEU B  103  5                                   6    
HELIX   31  31 PRO B  104  SER B  123  1                                  20    
HELIX   32  32 PRO B  141  SER B  150  1                                  10    
HELIX   33  33 SER B  152  ILE B  169  1                                  18    
HELIX   34  34 LEU B  171  GLN B  188  1                                  18    
HELIX   35  35 ASP B  193  SER B  200  1                                   8    
HELIX   36  36 TRP B  201  ASN B  203  5                                   3    
HELIX   37  37 THR B  206  GLY B  238  1                                  33    
HELIX   38  38 TRP B  261  VAL B  268  5                                   8    
HELIX   39  39 MET B  283  GLY B  287  5                                   5    
HELIX   40  40 ASN B  289  LEU B  304  1                                  16    
HELIX   41  41 PRO B  310  GLY B  316  1                                   7    
HELIX   42  42 THR B  352  TYR B  372  1                                  21    
HELIX   43  43 PRO B  376  ARG B  380  5                                   5    
HELIX   44  44 ASN B  384  THR B  401  1                                  18    
HELIX   45  45 THR B  401  ILE B  408  1                                   8    
HELIX   46  46 THR B  418  ILE B  433  1                                  16    
HELIX   47  47 ALA B  434  SER B  451  1                                  18    
HELIX   48  48 PRO B  455  TYR B  459  5                                   5    
HELIX   49  49 ASN B  460  TYR B  470  1                                  11    
HELIX   50  50 PHE B  484  LYS B  489  5                                   6    
HELIX   51  51 TYR B  498  ALA B  519  1                                  22    
HELIX   52  52 PRO B  524  CYS B  528  5                                   5    
HELIX   53  53 SER B  533  GLN B  545  1                                  13    
HELIX   54  54 PRO B  551  VAL B  560  1                                  10    
HELIX   55  55 ALA B  567  ASN B  588  1                                  22    
SHEET    1  AA 2 LYS A 126  VAL A 127  0                                        
SHEET    2  AA 2 TRP A 137  SER A 138 -1  O  TRP A 137   N  VAL A 127           
SHEET    1  AB 2 ILE A 248  PRO A 249  0                                        
SHEET    2  AB 2 ILE A 473  CYS A 474  1  N  CYS A 474   O  ILE A 248           
SHEET    1  AC 2 SER A 333  ASP A 336  0                                        
SHEET    2  AC 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335           
SHEET    1  BA 2 LYS B 126  CYS B 128  0                                        
SHEET    2  BA 2 CYS B 136  SER B 138 -1  O  TRP B 137   N  VAL B 127           
SHEET    1  BB 2 ILE B 248  PRO B 249  0                                        
SHEET    2  BB 2 ILE B 473  CYS B 474  1  N  CYS B 474   O  ILE B 248           
SHEET    1  BC 2 SER B 333  ASP B 336  0                                        
SHEET    2  BC 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.58  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.03  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  1.81  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.05  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.03  
LINK         ND2 ASN A  25                 C1  NAG A 693     1555   1555  1.49  
LINK         ND2 ASN A  25                 O5  NAG A 693     1555   1555  1.70  
LINK         ND2 ASN A 117                 C1  NAG A 695     1555   1555  1.47  
LINK         CG  ASN A 480                 C1  NAG A 691     1555   1555  1.97  
LINK         ND2 ASN A 480                 C1  NAG A 691     1555   1555  1.45  
LINK         O4  NAG A 691                 C1  NAG A 696     1555   1555  1.46  
LINK        ZN    ZN A 701                 NE2 HIS A 365     1555   1555  2.17  
LINK        ZN    ZN A 701                 O3  LPR A 705     1555   1555  2.53  
LINK        ZN    ZN A 701                 OE1 GLU A 389     1555   1555  1.79  
LINK        ZN    ZN A 701                 O2  LPR A 705     1555   1555  2.60  
LINK        ZN    ZN A 701                 NE2 HIS A 361     1555   1555  2.05  
LINK         ND2 ASN B  25                 O5  NAG B 693     1555   1555  1.76  
LINK         ND2 ASN B  25                 C1  NAG B 693     1555   1555  1.45  
LINK         ND2 ASN B 117                 C1  NAG B 695     1555   1555  1.43  
LINK         ND2 ASN B 480                 C1  NAG B 691     1555   1555  1.46  
LINK         O4  NAG B 691                 C1  NAG B 696     1555   1555  1.41  
LINK        ZN    ZN B 701                 NE2 HIS B 365     1555   1555  2.19  
LINK        ZN    ZN B 701                 OE1 GLU B 389     1555   1555  1.75  
LINK        ZN    ZN B 701                 O2  LPR B 705     1555   1555  2.01  
LINK        ZN    ZN B 701                 O3  LPR B 705     1555   1555  2.01  
LINK        ZN    ZN B 701                 NE2 HIS B 361     1555   1555  1.96  
CISPEP   1 ASP A  140    PRO A  141          0         9.89                     
CISPEP   2 TYR A  607    PRO A  608          0        10.76                     
CISPEP   3 ASP B    2    PRO B    3          0       -10.95                     
CISPEP   4 TYR B  607    PRO B  608          0        10.96                     
SITE     1 AC1  4 ASN A 480  THR A 482  HIS A 483  NAG A 696                    
SITE     1 AC2  1 NAG A 691                                                     
SITE     1 AC3  2 ASN A  25  GLU A  29                                          
SITE     1 AC4  5 GLN A 110  ALA A 113  LEU A 114  ASN A 117                    
SITE     2 AC4  5 ARG A 120                                                     
SITE     1 AC5  3 ASN B 480  THR B 482  NAG B 696                               
SITE     1 AC6  1 NAG B 691                                                     
SITE     1 AC7  6 GLN B  22  ASN B  25  SER B  26  GLU B  29                    
SITE     2 AC7  6 ARG B 340  PRO B 376                                          
SITE     1 AC8  3 ALA B 113  ASN B 117  ARG B 120                               
SITE     1 AC9  4 HIS A 361  HIS A 365  GLU A 389  LPR A 705                    
SITE     1 BC1  3 TYR A 202  PRO A 497  ARG A 500                               
SITE     1 BC2  4 HIS B 361  HIS B 365  GLU B 389  LPR B 705                    
SITE     1 BC3  4 TYR B 202  PRO B 385  PRO B 497  ARG B 500                    
SITE     1 BC4  3 ARG A 453  ASP A 462  TYR A 465                               
SITE     1 BC5 13 GLN A 259  HIS A 331  ALA A 332  HIS A 361                    
SITE     2 BC5 13 GLU A 362  HIS A 365  GLU A 389  LYS A 489                    
SITE     3 BC5 13 HIS A 491  THR A 496  TYR A 498  TYR A 501                    
SITE     4 BC5 13  ZN A 701                                                     
SITE     1 BC6 13 GLN B 259  HIS B 331  ALA B 332  HIS B 361                    
SITE     2 BC6 13 GLU B 362  HIS B 365  GLU B 389  LYS B 489                    
SITE     3 BC6 13 HIS B 491  THR B 496  TYR B 498  TYR B 501                    
SITE     4 BC6 13  ZN B 701                                                     
SITE     1 BC7  5 GLN A 586  LEU B 223  LYS B 469  GLY B 593                    
SITE     2 BC7  5 TRP B 594                                                     
SITE     1 BC8  5 GLU A 219  LEU A 223  LYS A 469  GLY A 593                    
SITE     2 BC8  5 TRP A 594                                                     
CRYST1  101.300  210.900  171.000  90.00  90.00  90.00 C 2 2 21     16          
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      0.009872  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004742  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005848        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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