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Database: PDB
Entry: 4NJQ
LinkDB: 4NJQ
Original site: 4NJQ 
HEADER    HYDROLASE                               11-NOV-13   4NJQ              
TITLE     STRUCTURAL AND KINETIC BASES FOR THE METAL PREFERENCE OF THE M18      
TITLE    2 AMINOPEPTIDASE FROM PSEUDOMONAS AERUGINOSA                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE M18 FAMILY AMINOPEPTIDASE 2;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.4.11.-;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;                
SOURCE   5 GENE: APEB, PA3247;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVFT1S                                    
KEYWDS    METALLOPEPTIDASE, ASPARTYL AMINOPEPTIDASE, COBALT COMPLEX,            
KEYWDS   2 TETRAHEDRAL SHAPE DODECAMERIC STRUCTURE, METAL BINDING, HYDROLASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.D.NGUYEN,R.PANDIAN,D.Y.KIM,S.C.HA,K.H.YUN,K.S.KIM,J.H.KIM,K.K.KIM   
REVDAT   4   17-SEP-14 4NJQ    1       JRNL                                     
REVDAT   3   23-APR-14 4NJQ    1       JRNL                                     
REVDAT   2   09-APR-14 4NJQ    1       JRNL                                     
REVDAT   1   02-APR-14 4NJQ    0                                                
JRNL        AUTH   D.D.NGUYEN,R.PANDIAN,D.KIM,S.C.HA,H.J.YOON,K.S.KIM,K.H.YUN,  
JRNL        AUTH 2 J.H.KIM,K.K.KIM                                              
JRNL        TITL   STRUCTURAL AND KINETIC BASES FOR THE METAL PREFERENCE OF THE 
JRNL        TITL 2 M18 AMINOPEPTIDASE FROM PSEUDOMONAS AERUGINOSA               
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 447   101 2014              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   24704201                                                     
JRNL        DOI    10.1016/J.BBRC.2014.03.109                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.76                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 54605                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2920                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.7697 -  7.4432    0.97     2560   140  0.1697 0.1784        
REMARK   3     2  7.4432 -  5.9129    0.99     2616   153  0.1773 0.2220        
REMARK   3     3  5.9129 -  5.1669    0.99     2615   155  0.1704 0.1987        
REMARK   3     4  5.1669 -  4.6951    0.99     2579   158  0.1477 0.1751        
REMARK   3     5  4.6951 -  4.3589    1.00     2653   129  0.1370 0.2062        
REMARK   3     6  4.3589 -  4.1022    1.00     2658   141  0.1449 0.1951        
REMARK   3     7  4.1022 -  3.8969    1.00     2613   132  0.1505 0.2001        
REMARK   3     8  3.8969 -  3.7273    1.00     2656   154  0.1548 0.2202        
REMARK   3     9  3.7273 -  3.5839    1.00     2603   135  0.1636 0.2338        
REMARK   3    10  3.5839 -  3.4603    1.00     2660   130  0.1766 0.2525        
REMARK   3    11  3.4603 -  3.3522    1.00     2669   117  0.1773 0.2685        
REMARK   3    12  3.3522 -  3.2564    0.99     2625   131  0.1915 0.2653        
REMARK   3    13  3.2564 -  3.1707    0.99     2604   117  0.1853 0.2409        
REMARK   3    14  3.1707 -  3.0933    0.99     2632   141  0.1795 0.2580        
REMARK   3    15  3.0933 -  3.0230    0.98     2560   133  0.1762 0.2525        
REMARK   3    16  3.0230 -  2.9587    0.98     2564   165  0.1753 0.2380        
REMARK   3    17  2.9587 -  2.8995    0.97     2586   146  0.1833 0.2867        
REMARK   3    18  2.8995 -  2.8448    0.97     2521   147  0.1930 0.2779        
REMARK   3    19  2.8448 -  2.7940    0.96     2558   133  0.1946 0.2677        
REMARK   3    20  2.7940 -  2.7467    0.96     2519   132  0.2110 0.3296        
REMARK   3    21  2.7467 -  2.7024    0.96     2540   131  0.2015 0.2690        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.830           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.02000                                              
REMARK   3    B12 (A**2) : -0.01000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          12962                                  
REMARK   3   ANGLE     :  1.211          17588                                  
REMARK   3   CHIRALITY :  0.045           1954                                  
REMARK   3   PLANARITY :  0.005           2348                                  
REMARK   3   DIHEDRAL  : 16.785           4732                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4NJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB083289.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54605                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 50.00                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.2M MAGNESIUM CHLORIDE,     
REMARK 280  0.1MM ZINC CHLORIDE , PH 8.0, MICROBATCH CRYSTALLIZATION,           
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.60250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       38.45297            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      107.43867            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       66.60250            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       38.45297            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      107.43867            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       66.60250            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       38.45297            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      107.43867            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       76.90594            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      214.87733            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       76.90594            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      214.87733            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       76.90594            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      214.87733            
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 85630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 151170 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -474.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C                            
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   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  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     GLY A   268                                                      
REMARK 465     SER A   269                                                      
REMARK 465     CYS A   270                                                      
REMARK 465     SER A   271                                                      
REMARK 465     HIS A   272                                                      
REMARK 465     CYS A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     ALA A   275                                                      
REMARK 465     ASP A   276                                                      
REMARK 465     GLY A   277                                                      
REMARK 465     GLY A   373                                                      
REMARK 465     CYS A   374                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     SER A   376                                                      
REMARK 465     THR A   377                                                      
REMARK 465     ILE A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     PRO A   380                                                      
REMARK 465     ILE A   381                                                      
REMARK 465     THR A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     GLY B   268                                                      
REMARK 465     SER B   269                                                      
REMARK 465     CYS B   270                                                      
REMARK 465     SER B   271                                                      
REMARK 465     HIS B   272                                                      
REMARK 465     CYS B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     ALA B   275                                                      
REMARK 465     ASP B   276                                                      
REMARK 465     GLY B   277                                                      
REMARK 465     GLY B   373                                                      
REMARK 465     CYS B   374                                                      
REMARK 465     GLY B   375                                                      
REMARK 465     SER B   376                                                      
REMARK 465     THR B   377                                                      
REMARK 465     ILE B   378                                                      
REMARK 465     GLY B   379                                                      
REMARK 465     PRO B   380                                                      
REMARK 465     ILE B   381                                                      
REMARK 465     GLY C   268                                                      
REMARK 465     SER C   269                                                      
REMARK 465     CYS C   270                                                      
REMARK 465     SER C   271                                                      
REMARK 465     HIS C   272                                                      
REMARK 465     CYS C   273                                                      
REMARK 465     GLY C   274                                                      
REMARK 465     ALA C   275                                                      
REMARK 465     ASP C   276                                                      
REMARK 465     GLY C   277                                                      
REMARK 465     GLY C   373                                                      
REMARK 465     CYS C   374                                                      
REMARK 465     GLY C   375                                                      
REMARK 465     SER C   376                                                      
REMARK 465     THR C   377                                                      
REMARK 465     ILE C   378                                                      
REMARK 465     GLY C   379                                                      
REMARK 465     PRO C   380                                                      
REMARK 465     ILE C   381                                                      
REMARK 465     THR C   382                                                      
REMARK 465     ALA C   383                                                      
REMARK 465     SER C   384                                                      
REMARK 465     GLY D   268                                                      
REMARK 465     SER D   269                                                      
REMARK 465     CYS D   270                                                      
REMARK 465     SER D   271                                                      
REMARK 465     HIS D   272                                                      
REMARK 465     CYS D   273                                                      
REMARK 465     GLY D   274                                                      
REMARK 465     ALA D   275                                                      
REMARK 465     ASP D   276                                                      
REMARK 465     GLY D   277                                                      
REMARK 465     GLY D   373                                                      
REMARK 465     CYS D   374                                                      
REMARK 465     GLY D   375                                                      
REMARK 465     SER D   376                                                      
REMARK 465     THR D   377                                                      
REMARK 465     ILE D   378                                                      
REMARK 465     GLY D   379                                                      
REMARK 465     PRO D   380                                                      
REMARK 465     ILE D   381                                                      
REMARK 465     THR D   382                                                      
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     ALA A 181    CB                                                  
REMARK 470     ALA B 181    CB                                                  
REMARK 470     ALA C 181    CB                                                  
REMARK 470     PRO D 182    CG   CD                                             
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   OD1  ASP B    84     O    HOH B   622              1.96            
REMARK 500   ND1  HIS B    82     O    HOH B   622              2.07            
REMARK 500   O2   NHE C   504     O    HOH C   610              2.09            
REMARK 500   O    HOH B   605     O    HOH B   613              2.16            
REMARK 500   OE2  GLU C    31     OH   TYR C    53              2.17            
REMARK 500   ND2  ASN D   237     O    HOH D   630              2.17            
REMARK 500   O    ALA D   306     O    HOH D   630              2.18            
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    ALA A   3   C   -  N   -  CA  ANGL. DEV. =  15.2 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    ARG A   2     -166.87     69.52                                   
REMARK 500    ALA A   3      -67.17     86.75                                   
REMARK 500    THR A  46      114.88     59.54                                   
REMARK 500    CYS A  87     -173.33   -170.37                                   
REMARK 500    ASP A 121       94.45    -68.10                                   
REMARK 500    ARG A 144      -50.98     56.34                                   
REMARK 500    ASN A 158       66.09   -161.09                                   
REMARK 500    ALA A 181      -81.55     -8.51                                   
REMARK 500    ALA A 204      124.28     60.58                                   
REMARK 500    LEU A 208      -64.70    -90.03                                   
REMARK 500    PRO A 289       96.00    -60.81                                   
REMARK 500    GLU A 290      164.00    -48.61                                   
REMARK 500    TYR A 316       36.43   -143.77                                   
REMARK 500    THR A 344      126.53    -37.69                                   
REMARK 500    ASP A 371       34.02    -98.70                                   
REMARK 500    ALA A 399       42.15     73.82                                   
REMARK 500    ASN B  93       73.78   -111.22                                   
REMARK 500    SER B 123     -165.85   -120.77                                   
REMARK 500    ARG B 144      -55.62     55.94                                   
REMARK 500    ASN B 158       64.54   -168.23                                   
REMARK 500    ALA B 185      122.97     64.94                                   
REMARK 500    LEU B 208      -68.76    -94.67                                   
REMARK 500    TYR B 316       39.16   -141.92                                   
REMARK 500    ALA B 383      -77.33     64.55                                   
REMARK 500    ARG C   2      -73.87     63.33                                   
REMARK 500    SER C  59       -0.34   -140.99                                   
REMARK 500    CYS C  87     -167.84   -164.92                                   
REMARK 500    SER C 123     -168.23   -120.59                                   
REMARK 500    LEU C 136      101.65     73.89                                   
REMARK 500    ARG C 144      -55.63     59.62                                   
REMARK 500    ALA C 181     -172.94    -62.91                                   
REMARK 500    ALA C 185      122.09     65.64                                   
REMARK 500    LEU C 208      -69.93   -100.66                                   
REMARK 500    ASP C 254       58.83   -146.37                                   
REMARK 500    PRO C 289     -105.93    -57.45                                   
REMARK 500    GLU C 290     -169.87    -62.09                                   
REMARK 500    TYR C 316       42.40   -140.74                                   
REMARK 500    HIS C 324       57.71   -140.62                                   
REMARK 500    ASN D  57       17.10     58.48                                   
REMARK 500    SER D  59       -1.33   -147.36                                   
REMARK 500    ASN D  93       77.62   -109.74                                   
REMARK 500    ASN D 133       55.86     20.19                                   
REMARK 500    ARG D 144      -59.33     56.11                                   
REMARK 500    ALA D 160       39.33    -92.79                                   
REMARK 500    LEU D 180     -116.52   -113.59                                   
REMARK 500    ALA D 181      171.13     54.28                                   
REMARK 500    LEU D 208      -67.24    -90.75                                   
REMARK 500    ASN D 237       37.08   -141.05                                   
REMARK 500    ASP D 254     -105.49    -90.68                                   
REMARK 500    GLU D 255      142.02     63.68                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
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                              CO A 502  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CO3 A 503   O2                                                     
REMARK 620 2 ASP A 236   OD2 112.7                                              
REMARK 620 3 GLU A 266   OE2  88.3 159.0                                        
REMARK 620 4 GLU A 266   OE1 142.4 103.8  55.5                                  
REMARK 620 5 HIS A 401   CD2  93.5  82.6  97.0  99.9                            
REMARK 620 6 CO3 A 503   C    26.0 122.2  76.6 122.2 117.6                      
REMARK 620 7 GLU A 266   CD  116.6 130.7  28.3  28.1  94.2 102.8                
REMARK 620 8 HIS A 401   NE2  69.7 108.7  78.1 107.3  30.2  90.2  88.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO B 502  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CO3 B 503   O2                                                     
REMARK 620 2 GLU B 266   OE1  99.8                                              
REMARK 620 3 ASP B 236   OD2 106.6 153.6                                        
REMARK 620 4 HIS B 401   NE2  88.5  81.1  99.4                                  
REMARK 620 5 GLU B 266   CD  127.2  28.6 125.6  90.7                            
REMARK 620 6 GLU B 266   OE2 144.1  55.3 100.8 109.6  28.0                      
REMARK 620 7 CO3 B 503   C    26.2  79.0 126.2 100.8 103.5 117.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO D 501  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 266   OE2                                                    
REMARK 620 2 ASP D 236   OD2  92.7                                              
REMARK 620 3 HIS D 401   NE2 108.4  96.9                                        
REMARK 620 4 CO3 D 503   O2  134.1 129.9  85.3                                  
REMARK 620 5 GLU D 266   CD   25.5 115.1  92.6 114.8                            
REMARK 620 6 CO3 D 503   O3  111.0 102.4 134.8  51.2 114.6                      
REMARK 620 7 GLU D 266   OE1  52.0 135.6  74.9  93.5  26.5 114.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO C 502  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 236   OD2                                                    
REMARK 620 2 HIS C 401   NE2  98.8                                              
REMARK 620 3 GLU C 266   OE2 161.0  92.0                                        
REMARK 620 4 GLU C 266   OE1 103.2 112.3  58.0                                  
REMARK 620 5 CO3 C 503   O3  113.5  80.9  83.6 138.7                            
REMARK 620 6 GLU C 266   CD  132.3  98.9  29.5  29.3 112.9                      
REMARK 620 7 CO3 C 503   O2  112.0 130.6  71.0  97.5  52.0  88.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO C 501  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 236   OD1                                                    
REMARK 620 2 ASP C 307   OD1  89.7                                              
REMARK 620 3 HIS C  82   NE2  88.4 100.4                                        
REMARK 620 4 CO3 C 503   O2  126.2 137.7 101.9                                  
REMARK 620 5 ASP C 307   OD2 144.5  56.6  87.3  89.1                            
REMARK 620 6 ASP C 307   CG  117.4  28.3  94.6 114.1  28.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO D 502  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 236   OD1                                                    
REMARK 620 2 CO3 D 503   O3  122.5                                              
REMARK 620 3 ASP D 307   OD1  96.9 118.6                                        
REMARK 620 4 HIS D  82   NE2  90.5 127.9  92.2                                  
REMARK 620 5 ASP D 307   OD2 150.8  79.2  54.0  89.3                            
REMARK 620 6 ASP D 307   CG  123.9  97.3  27.1  94.0  27.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO A 501  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 236   OD1                                                    
REMARK 620 2 ASP A 307   OD2  92.3                                              
REMARK 620 3 HIS A  82   NE2  85.2  88.8                                        
REMARK 620 4 ASP A 307   OD1 149.0  58.5  83.9                                  
REMARK 620 5 ASP A 307   CG  121.9  29.6  90.1  29.5                            
REMARK 620 6 CO3 A 503   O3  127.8 137.0 107.2  83.2 108.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CO B 501  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 236   OD1                                                    
REMARK 620 2 ASP B 307   OD1  92.9                                              
REMARK 620 3 HIS B  82   NE2 100.0  92.5                                        
REMARK 620 4 ASP B 307   OD2 146.6  54.7  76.4                                  
REMARK 620 5 CO3 B 503   O1  130.2 130.3 101.1  82.4                            
REMARK 620 6 ASP B 307   CG  120.2  27.3  86.0  27.5 105.9                      
REMARK 620 7 HIS B  82   CE1  77.7 109.2  27.3 103.7 103.9 110.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE D 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4NJR   RELATED DB: PDB                                   
REMARK 900 ZNZNPAAP ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS AERUGINOSA          
REMARK 900 WITH ZINC IN CATALYTIC SITE                                          
REMARK 900 RELATED ID: 4OID   RELATED DB: PDB                                   
REMARK 900 D236A MUTATION FROM ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS          
REMARK 900 AERUGINOSA 4OID                                                      
REMARK 900 RELATED ID: 4OIW   RELATED DB: PDB                                   
DBREF  4NJQ A    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4NJQ B    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4NJQ C    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
DBREF  4NJQ D    1   429  UNP    Q9HYZ3   APEB_PSEAE       1    429             
SEQRES   1 A  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 A  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 A  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 A  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 A  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 A  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 A  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 A  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 A  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 A  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 A  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 A  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 A  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 A  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 A  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 A  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 A  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 A  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 A  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 A  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 A  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 A  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 A  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 A  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 A  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 A  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 A  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 A  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 A  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 A  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 A  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 A  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 A  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
SEQRES   1 B  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 B  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 B  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 B  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 B  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 B  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 B  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 B  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 B  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 B  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 B  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 B  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 B  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 B  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 B  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 B  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 B  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 B  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 B  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 B  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 B  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 B  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 B  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 B  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 B  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 B  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 B  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 B  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 B  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 B  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 B  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 B  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 B  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
SEQRES   1 C  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 C  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 C  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 C  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 C  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 C  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 C  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 C  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 C  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 C  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 C  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 C  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 C  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 C  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 C  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 C  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 C  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 C  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 C  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 C  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 C  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 C  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 C  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 C  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 C  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 C  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 C  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 C  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 C  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 C  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 C  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 C  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 C  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
SEQRES   1 D  429  MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP PHE LEU          
SEQRES   2 D  429  LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA SER LEU          
SEQRES   3 D  429  ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG LEU ASP          
SEQRES   4 D  429  GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY ARG TYR          
SEQRES   5 D  429  TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA ILE ARG          
SEQRES   6 D  429  LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE ARG LEU          
SEQRES   7 D  429  VAL GLY ALA HIS THR ASP SER PRO CYS LEU ARG VAL LYS          
SEQRES   8 D  429  PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU GLN LEU          
SEQRES   9 D  429  GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA PRO TRP          
SEQRES  10 D  429  PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL THR PHE          
SEQRES  11 D  429  ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL ASP PHE          
SEQRES  12 D  429  ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA ILE HIS          
SEQRES  13 D  429  LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE ASN ALA          
SEQRES  14 D  429  GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU ALA PRO          
SEQRES  15 D  429  GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP GLU GLN          
SEQRES  16 D  429  LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL VAL LEU          
SEQRES  17 D  429  ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER ALA ALA          
SEQRES  18 D  429  VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY ALA ARG          
SEQRES  19 D  429  LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU GLU ALA          
SEQRES  20 D  429  LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE LEU VAL          
SEQRES  21 D  429  CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER HIS CYS          
SEQRES  22 D  429  GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU ARG ARG          
SEQRES  23 D  429  LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA ILE GLN          
SEQRES  24 D  429  ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS GLY VAL          
SEQRES  25 D  429  HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN HIS GLY          
SEQRES  26 D  429  PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE ASN SER          
SEQRES  27 D  429  ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA GLY PHE          
SEQRES  28 D  429  PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO VAL GLN          
SEQRES  29 D  429  SER PHE VAL THR ARG SER ASP MET GLY CYS GLY SER THR          
SEQRES  30 D  429  ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL ARG THR          
SEQRES  31 D  429  VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS SER ILE          
SEQRES  32 D  429  ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS LEU VAL          
SEQRES  33 D  429  LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU LEU PRO          
HET     CO  A 501       1                                                       
HET     CO  A 502       1                                                       
HET    CO3  A 503       4                                                       
HET    NHE  A 504      13                                                       
HET     CO  B 501       1                                                       
HET     CO  B 502       1                                                       
HET    CO3  B 503       4                                                       
HET     CO  C 501       1                                                       
HET     CO  C 502       1                                                       
HET    CO3  C 503       4                                                       
HET    NHE  C 504      13                                                       
HET     CO  D 501       1                                                       
HET     CO  D 502       1                                                       
HET    CO3  D 503       4                                                       
HET    NHE  D 504      13                                                       
HETNAM      CO COBALT (II) ION                                                  
HETNAM     CO3 CARBONATE ION                                                    
HETNAM     NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID                        
HETSYN     NHE N-CYCLOHEXYLTAURINE; CHES                                        
FORMUL   5   CO    8(CO 2+)                                                     
FORMUL   7  CO3    4(C O3 2-)                                                   
FORMUL   8  NHE    3(C8 H17 N O3 S)                                             
FORMUL  20  HOH   *103(H2 O)                                                    
HELIX    1   1 ALA A    3  ALA A   15  1                                  13    
HELIX    2   2 THR A   18  ALA A   33  1                                  16    
HELIX    3   3 SER A   70  GLY A   75  1                                   6    
HELIX    4   4 PHE A  114  PHE A  118  5                                   5    
HELIX    5   5 ALA A  154  ASN A  158  5                                   5    
HELIX    6   6 ALA A  160  GLY A  164  5                                   5    
HELIX    7   7 ASN A  168  LEU A  173  1                                   6    
HELIX    8   8 ASP A  187  GLY A  201  1                                  15    
HELIX    9   9 ARG A  234  ASN A  250  1                                  17    
HELIX   10  10 PHE A  279  LEU A  288  1                                  10    
HELIX   11  11 ASP A  292  GLN A  299  1                                   8    
HELIX   12  12 HIS A  313  HIS A  320  5                                   8    
HELIX   13  13 ASP A  321  GLY A  325  5                                   5    
HELIX   14  14 ASN A  345  SER A  359  1                                  15    
HELIX   15  15 HIS A  410  ALA A  424  1                                  15    
HELIX   16  16 ARG B    2  ALA B   15  1                                  14    
HELIX   17  17 THR B   18  ALA B   33  1                                  16    
HELIX   18  18 SER B   70  GLY B   75  1                                   6    
HELIX   19  19 PHE B  114  PHE B  118  5                                   5    
HELIX   20  20 ALA B  154  ASN B  158  5                                   5    
HELIX   21  21 ALA B  160  GLY B  164  5                                   5    
HELIX   22  22 ASN B  168  LEU B  173  1                                   6    
HELIX   23  23 ASP B  187  GLY B  201  1                                  15    
HELIX   24  24 ARG B  234  ALA B  251  1                                  18    
HELIX   25  25 PHE B  279  ARG B  286  1                                   8    
HELIX   26  26 ASP B  292  GLN B  299  1                                   8    
HELIX   27  27 TYR B  316  HIS B  320  5                                   5    
HELIX   28  28 ASN B  345  SER B  359  1                                  15    
HELIX   29  29 HIS B  410  SER B  425  1                                  16    
HELIX   30  30 ARG C    2  SER C   16  1                                  15    
HELIX   31  31 THR C   18  ALA C   33  1                                  16    
HELIX   32  32 SER C   70  GLY C   75  1                                   6    
HELIX   33  33 PHE C  114  PHE C  118  5                                   5    
HELIX   34  34 ALA C  154  ASN C  158  5                                   5    
HELIX   35  35 ALA C  160  GLY C  164  5                                   5    
HELIX   36  36 ASN C  168  LEU C  173  1                                   6    
HELIX   37  37 ASP C  187  GLY C  201  1                                  15    
HELIX   38  38 ARG C  234  ALA C  251  1                                  18    
HELIX   39  39 PHE C  279  ARG C  286  1                                   8    
HELIX   40  40 GLU C  290  GLN C  299  1                                  10    
HELIX   41  41 TYR C  316  HIS C  320  5                                   5    
HELIX   42  42 ASN C  345  ASP C  358  1                                  14    
HELIX   43  43 HIS C  410  ALA C  424  1                                  15    
HELIX   44  44 ARG D    2  SER D   16  1                                  15    
HELIX   45  45 THR D   18  ALA D   33  1                                  16    
HELIX   46  46 SER D   70  GLY D   75  1                                   6    
HELIX   47  47 PHE D  114  PHE D  118  5                                   5    
HELIX   48  48 ALA D  154  ASN D  158  5                                   5    
HELIX   49  49 ALA D  160  GLY D  164  5                                   5    
HELIX   50  50 ASN D  168  LEU D  173  1                                   6    
HELIX   51  51 ASP D  187  GLY D  201  1                                  15    
HELIX   52  52 ARG D  234  ALA D  251  1                                  18    
HELIX   53  53 PHE D  279  LEU D  287  1                                   9    
HELIX   54  54 ASP D  292  GLN D  299  1                                   8    
HELIX   55  55 TYR D  316  HIS D  320  5                                   5    
HELIX   56  56 ASN D  345  SER D  359  1                                  15    
HELIX   57  57 HIS D  410  ALA D  424  1                                  15    
SHEET    1   A 9 ARG A  36  LEU A  38  0                                        
SHEET    2   A 9 ARG A  51  ARG A  56  1  O  ARG A  51   N  ARG A  36           
SHEET    3   A 9 SER A  60  ARG A  65 -1  O  ILE A  64   N  TYR A  52           
SHEET    4   A 9 CYS A 257  THR A 262 -1  O  CYS A 261   N  LEU A  61           
SHEET    5   A 9 ARG A  77  HIS A  82  1  N  VAL A  79   O  VAL A 260           
SHEET    6   A 9 LEU A 302  ALA A 306  1  O  VAL A 304   N  LEU A  78           
SHEET    7   A 9 THR A 390  GLY A 394  1  O  VAL A 391   N  SER A 305           
SHEET    8   A 9 VAL A 333  LYS A 335 -1  N  VAL A 333   O  GLY A 394           
SHEET    9   A 9 GLN A 364  PHE A 366  1  O  GLN A 364   N  ILE A 334           
SHEET    1   B 3 CYS A  87  ARG A  98  0                                        
SHEET    2   B 3 PHE A 101  TYR A 109 -1  O  GLY A 105   N  LYS A  91           
SHEET    3   B 3 ILE A 176  GLN A 179 -1  O  ALA A 178   N  LEU A 102           
SHEET    1   C 3 LYS A 135  ASP A 142  0                                        
SHEET    2   C 3 LEU A 122  ALA A 132 -1  N  VAL A 128   O  ARG A 139           
SHEET    3   C 3 VAL A 206  ASP A 216 -1  O  VAL A 206   N  ARG A 131           
SHEET    1   D 3 ALA A 221  VAL A 223  0                                        
SHEET    2   D 3 PHE A 229  GLY A 232 -1  O  ALA A 231   N  ALA A 221           
SHEET    3   D 3 GLU A 405  GLY A 408 -1  O  ALA A 407   N  ILE A 230           
SHEET    1   E 2 ALA A 309  HIS A 310  0                                        
SHEET    2   E 2 PRO A 396  THR A 397  1  O  THR A 397   N  ALA A 309           
SHEET    1   F 9 ARG B  36  LEU B  38  0                                        
SHEET    2   F 9 ARG B  51  ARG B  56  1  O  ARG B  51   N  ARG B  36           
SHEET    3   F 9 SER B  60  ARG B  65 -1  O  ILE B  64   N  TYR B  52           
SHEET    4   F 9 ASN B 256  THR B 262 -1  O  CYS B 257   N  ARG B  65           
SHEET    5   F 9 PHE B  76  HIS B  82  1  N  VAL B  79   O  VAL B 260           
SHEET    6   F 9 LEU B 302  ALA B 306  1  O  VAL B 304   N  LEU B  78           
SHEET    7   F 9 THR B 390  GLY B 394  1  O  ILE B 393   N  SER B 305           
SHEET    8   F 9 VAL B 333  LYS B 335 -1  N  VAL B 333   O  GLY B 394           
SHEET    9   F 9 GLN B 364  PHE B 366  1  O  GLN B 364   N  ILE B 334           
SHEET    1   G 6 LYS B 135  ASP B 142  0                                        
SHEET    2   G 6 LEU B 122  ALA B 132 -1  N  ALA B 132   O  LYS B 135           
SHEET    3   G 6 VAL B 206  ASP B 216 -1  O  ASP B 209   N  THR B 129           
SHEET    4   G 6 CYS B  87  ARG B  98 -1  N  LEU B  88   O  PHE B 214           
SHEET    5   G 6 PHE B 101  TYR B 109 -1  O  GLU B 107   N  ARG B  89           
SHEET    6   G 6 ILE B 176  GLN B 179 -1  O  ILE B 177   N  LEU B 102           
SHEET    1   H 5 ALA B 221  VAL B 223  0                                        
SHEET    2   H 5 PHE B 229  GLY B 232 -1  O  PHE B 229   N  VAL B 223           
SHEET    3   H 5 GLU B 405  GLY B 408 -1  O  ALA B 407   N  ILE B 230           
SHEET    4   H 5 PRO B 396  PHE B 398 -1  N  PHE B 398   O  LEU B 406           
SHEET    5   H 5 ALA B 309  HIS B 310  1  N  ALA B 309   O  THR B 397           
SHEET    1   I 9 ARG C  36  ARG C  37  0                                        
SHEET    2   I 9 ARG C  51  ARG C  56  1  O  ARG C  51   N  ARG C  36           
SHEET    3   I 9 SER C  60  ARG C  65 -1  O  ILE C  64   N  TYR C  52           
SHEET    4   I 9 CYS C 257  THR C 262 -1  O  CYS C 257   N  ARG C  65           
SHEET    5   I 9 ARG C  77  HIS C  82  1  N  VAL C  79   O  VAL C 260           
SHEET    6   I 9 LEU C 302  ALA C 306  1  O  ALA C 306   N  GLY C  80           
SHEET    7   I 9 THR C 390  GLY C 394  1  O  ILE C 393   N  SER C 305           
SHEET    8   I 9 VAL C 333  LYS C 335 -1  N  VAL C 333   O  GLY C 394           
SHEET    9   I 9 GLN C 364  PHE C 366  1  O  GLN C 364   N  ILE C 334           
SHEET    1   J 3 CYS C  87  ARG C  98  0                                        
SHEET    2   J 3 PHE C 101  TYR C 109 -1  O  GLU C 107   N  ARG C  89           
SHEET    3   J 3 ILE C 176  GLN C 179 -1  O  ALA C 178   N  LEU C 102           
SHEET    1   K 3 GLU C 137  ASP C 142  0                                        
SHEET    2   K 3 LEU C 122  ARG C 131 -1  N  PHE C 130   O  GLU C 137           
SHEET    3   K 3 VAL C 206  ASP C 216 -1  O  ASP C 209   N  THR C 129           
SHEET    1   L 5 ALA C 221  VAL C 223  0                                        
SHEET    2   L 5 PHE C 229  GLY C 232 -1  O  PHE C 229   N  VAL C 223           
SHEET    3   L 5 GLU C 405  GLY C 408 -1  O  ALA C 407   N  ILE C 230           
SHEET    4   L 5 PRO C 396  PHE C 398 -1  N  PHE C 398   O  LEU C 406           
SHEET    5   L 5 ALA C 309  HIS C 310  1  N  ALA C 309   O  THR C 397           
SHEET    1   M 9 ARG D  36  LEU D  38  0                                        
SHEET    2   M 9 ARG D  51  ARG D  56  1  O  ARG D  51   N  ARG D  36           
SHEET    3   M 9 SER D  60  ARG D  65 -1  O  ILE D  64   N  TYR D  52           
SHEET    4   M 9 ASN D 256  THR D 262 -1  O  LEU D 259   N  ALA D  63           
SHEET    5   M 9 PHE D  76  HIS D  82  1  N  VAL D  79   O  VAL D 260           
SHEET    6   M 9 LEU D 302  ALA D 306  1  O  VAL D 304   N  LEU D  78           
SHEET    7   M 9 THR D 390  GLY D 394  1  O  ILE D 393   N  SER D 305           
SHEET    8   M 9 VAL D 333  LYS D 335 -1  N  VAL D 333   O  GLY D 394           
SHEET    9   M 9 GLN D 364  PHE D 366  1  O  GLN D 364   N  ILE D 334           
SHEET    1   N 6 LYS D 135  ASP D 142  0                                        
SHEET    2   N 6 LEU D 122  ALA D 132 -1  N  VAL D 128   O  ARG D 139           
SHEET    3   N 6 VAL D 206  ASP D 216 -1  O  VAL D 206   N  ARG D 131           
SHEET    4   N 6 CYS D  87  ARG D  98 -1  N  LEU D  88   O  PHE D 214           
SHEET    5   N 6 PHE D 101  TYR D 109 -1  O  TYR D 109   N  CYS D  87           
SHEET    6   N 6 ILE D 176  GLN D 179 -1  O  ALA D 178   N  LEU D 102           
SHEET    1   O 5 ALA D 221  VAL D 223  0                                        
SHEET    2   O 5 PHE D 229  GLY D 232 -1  O  ALA D 231   N  ALA D 221           
SHEET    3   O 5 GLU D 405  GLY D 408 -1  O  ALA D 407   N  ILE D 230           
SHEET    4   O 5 PRO D 396  PHE D 398 -1  N  PHE D 398   O  LEU D 406           
SHEET    5   O 5 ALA D 309  HIS D 310  1  N  ALA D 309   O  THR D 397           
LINK        CO    CO A 502                 O2  CO3 A 503     1555   1555  1.74  
LINK        CO    CO B 502                 O2  CO3 B 503     1555   1555  1.80  
LINK         OE2 GLU D 266                CO    CO D 501     1555   1555  1.82  
LINK         OE1 GLU B 266                CO    CO B 502     1555   1555  1.84  
LINK         OD2 ASP A 236                CO    CO A 502     1555   1555  1.87  
LINK         OD2 ASP C 236                CO    CO C 502     1555   1555  1.90  
LINK         OD2 ASP B 236                CO    CO B 502     1555   1555  1.92  
LINK         OD2 ASP D 236                CO    CO D 501     1555   1555  2.00  
LINK         OD1 ASP C 236                CO    CO C 501     1555   1555  2.04  
LINK         OD1 ASP D 236                CO    CO D 502     1555   1555  2.06  
LINK         OD1 ASP A 236                CO    CO A 501     1555   1555  2.06  
LINK         OD1 ASP B 236                CO    CO B 501     1555   1555  2.07  
LINK         NE2 HIS C 401                CO    CO C 502     1555   1555  2.09  
LINK        CO    CO D 502                 O3  CO3 D 503     1555   1555  2.12  
LINK         OD1 ASP D 307                CO    CO D 502     1555   1555  2.13  
LINK         OD1 ASP B 307                CO    CO B 501     1555   1555  2.14  
LINK         OD2 ASP A 307                CO    CO A 501     1555   1555  2.15  
LINK         NE2 HIS B  82                CO    CO B 501     1555   1555  2.19  
LINK         NE2 HIS B 401                CO    CO B 502     1555   1555  2.21  
LINK         OE2 GLU C 266                CO    CO C 502     1555   1555  2.22  
LINK         NE2 HIS D 401                CO    CO D 501     1555   1555  2.23  
LINK         OD1 ASP C 307                CO    CO C 501     1555   1555  2.23  
LINK         NE2 HIS A  82                CO    CO A 501     1555   1555  2.24  
LINK         NE2 HIS D  82                CO    CO D 502     1555   1555  2.25  
LINK         NE2 HIS C  82                CO    CO C 501     1555   1555  2.27  
LINK         OD1 ASP A 307                CO    CO A 501     1555   1555  2.32  
LINK         OE2 GLU A 266                CO    CO A 502     1555   1555  2.34  
LINK        CO    CO C 501                 O2  CO3 C 503     1555   1555  2.35  
LINK         OE1 GLU C 266                CO    CO C 502     1555   1555  2.36  
LINK         OD2 ASP C 307                CO    CO C 501     1555   1555  2.36  
LINK         OE1 GLU A 266                CO    CO A 502     1555   1555  2.37  
LINK         CD  GLU B 266                CO    CO B 502     1555   1555  2.49  
LINK        CO    CO C 502                 O3  CO3 C 503     1555   1555  2.51  
LINK        CO    CO D 501                 O2  CO3 D 503     1555   1555  2.52  
LINK         CG  ASP A 307                CO    CO A 501     1555   1555  2.53  
LINK         CD  GLU C 266                CO    CO C 502     1555   1555  2.55  
LINK         CD2 HIS A 401                CO    CO A 502     1555   1555  2.57  
LINK         OD2 ASP B 307                CO    CO B 501     1555   1555  2.58  
LINK        CO    CO B 501                 O1  CO3 B 503     1555   1555  2.58  
LINK         OD2 ASP D 307                CO    CO D 502     1555   1555  2.60  
LINK         CD  GLU D 266                CO    CO D 501     1555   1555  2.62  
LINK         CG  ASP C 307                CO    CO C 501     1555   1555  2.62  
LINK        CO    CO A 502                 C   CO3 A 503     1555   1555  2.62  
LINK         CD  GLU A 266                CO    CO A 502     1555   1555  2.63  
LINK         OE2 GLU B 266                CO    CO B 502     1555   1555  2.64  
LINK        CO    CO B 502                 C   CO3 B 503     1555   1555  2.64  
LINK        CO    CO A 501                 O3  CO3 A 503     1555   1555  2.66  
LINK        CO    CO C 502                 O2  CO3 C 503     1555   1555  2.67  
LINK         CG  ASP B 307                CO    CO B 501     1555   1555  2.67  
LINK         NE2 HIS A 401                CO    CO A 502     1555   1555  2.68  
LINK         CG  ASP D 307                CO    CO D 502     1555   1555  2.68  
LINK        CO    CO D 501                 O3  CO3 D 503     1555   1555  2.72  
LINK         CE1 HIS B  82                CO    CO B 501     1555   1555  2.80  
LINK         OE1 GLU D 266                CO    CO D 501     1555   1555  2.80  
CISPEP   1 ARG A    2    ALA A    3          0         8.96                     
CISPEP   2 GLY A   49    GLY A   50          0         2.85                     
CISPEP   3 ALA A  181    PRO A  182          0       -21.58                     
CISPEP   4 PRO A  182    GLY A  183          0         9.97                     
CISPEP   5 ASP A  236    ASN A  237          0         3.30                     
CISPEP   6 MET A  400    HIS A  401          0        -6.21                     
CISPEP   7 PRO B  182    GLY B  183          0        -8.97                     
CISPEP   8 ASP B  236    ASN B  237          0         3.27                     
CISPEP   9 ASP C  236    ASN C  237          0        -1.82                     
CISPEP  10 ASN D  133    GLY D  134          0        -4.06                     
CISPEP  11 GLY D  183    GLU D  184          0       -15.49                     
CISPEP  12 ASP D  236    ASN D  237          0         7.16                     
CISPEP  13 ALA D  383    SER D  384          0         0.13                     
SITE     1 AC1  5 HIS A  82  ASP A 236  ASP A 307   CO A 502                    
SITE     2 AC1  5 CO3 A 503                                                     
SITE     1 AC2  5 ASP A 236  GLU A 266  HIS A 401   CO A 501                    
SITE     2 AC2  5 CO3 A 503                                                     
SITE     1 AC3  7 ASP A 236  GLU A 266  ASP A 307  HIS A 401                    
SITE     2 AC3  7  CO A 501   CO A 502  HIS D 156                               
SITE     1 AC4  3 ARG A  41  GLU A 137  ARG A 139                               
SITE     1 AC5  5 HIS B  82  ASP B 236  ASP B 307   CO B 502                    
SITE     2 AC5  5 CO3 B 503                                                     
SITE     1 AC6  5 ASP B 236  GLU B 266  HIS B 401   CO B 501                    
SITE     2 AC6  5 CO3 B 503                                                     
SITE     1 AC7 10 HIS B  82  ASP B 236  GLU B 265  GLU B 266                    
SITE     2 AC7 10 ASP B 307  MET B 400  HIS B 401   CO B 501                    
SITE     3 AC7 10  CO B 502  HIS C 156                                          
SITE     1 AC8  5 HIS C  82  ASP C 236  ASP C 307   CO C 502                    
SITE     2 AC8  5 CO3 C 503                                                     
SITE     1 AC9  5 ASP C 236  GLU C 266  HIS C 401   CO C 501                    
SITE     2 AC9  5 CO3 C 503                                                     
SITE     1 BC1 11 HIS B 156  HIS C  82  GLU C 265  GLU C 266                    
SITE     2 BC1 11 ASP C 307  ARG C 341  MET C 400  HIS C 401                    
SITE     3 BC1 11  CO C 501   CO C 502  HOH C 624                               
SITE     1 BC2  5 GLU C 137  ARG C 139  HOH C 604  HOH C 610                    
SITE     2 BC2  5 SER D 426                                                     
SITE     1 BC3  5 ASP D 236  GLU D 266  HIS D 401   CO D 502                    
SITE     2 BC3  5 CO3 D 503                                                     
SITE     1 BC4  5 HIS D  82  ASP D 236  ASP D 307   CO D 501                    
SITE     2 BC4  5 CO3 D 503                                                     
SITE     1 BC5  7 HIS A 156  ASP D 236  ASP D 307  MET D 400                    
SITE     2 BC5  7 HIS D 401   CO D 501   CO D 502                               
SITE     1 BC6  3 GLU D 137  ARG D 139  HOH D 603                               
CRYST1  133.205  133.205  322.316  90.00  90.00 120.00 H 3          36          
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      0.007507  0.004334  0.000000        0.00000                         
SCALE2      0.000000  0.008669  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003103        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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