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Database: PDB
Entry: 1N0Y
LinkDB: 1N0Y
Original site: 1N0Y 
HEADER    METAL BINDING PROTEIN                   15-OCT-02   1N0Y              
TITLE     CRYSTAL STRUCTURE OF PB-BOUND CALMODULIN                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PARAMECIUM TETRAURELIA;                         
SOURCE   3 ORGANISM_TAXID: 5888;                                                
SOURCE   4 GENE: CAM;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKK233-3                                  
KEYWDS    CALMODULIN, LEAD, METAL BINDING PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.WILSON,A.T.BRUNGER                                                
REVDAT   6   14-FEB-24 1N0Y    1       REMARK LINK                              
REVDAT   5   11-OCT-17 1N0Y    1       REMARK                                   
REVDAT   4   13-JUL-11 1N0Y    1       VERSN                                    
REVDAT   3   01-SEP-09 1N0Y    1       REMARK                                   
REVDAT   2   24-FEB-09 1N0Y    1       VERSN                                    
REVDAT   1   30-SEP-03 1N0Y    0                                                
JRNL        AUTH   M.A.WILSON,A.T.BRUNGER                                       
JRNL        TITL   DOMAIN FLEXIBILITY IN THE 1.75 A RESOLUTION STRUCTURE OF     
JRNL        TITL 2 PB2+-CALMODULIN.                                             
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  59  1782 2003              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   14501118                                                     
JRNL        DOI    10.1107/S0907444903016846                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 33157                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3312                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2112                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.2440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1311                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 149                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : -0.94000                                             
REMARK   3    B33 (A**2) : 1.45000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.71000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.097         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.091         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.653         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1331 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1781 ; 1.219 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   164 ; 0.755 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   196 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1011 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   711 ; 0.272 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   105 ; 0.097 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.295 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   824 ; 0.544 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1313 ; 1.090 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   507 ; 2.331 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   468 ; 3.825 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017382.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.946                              
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(311) BENT        
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33157                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD, SHARP                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, SODIUM CACODYLATE, SODIUM           
REMARK 280  ACETATE, LEAD NITRATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       50.46800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       15.39600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       50.46800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       15.39600            
REMARK 290   SMTRY3   4  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 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 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     ALA A    88                                                      
REMARK 465     PHE A    89                                                      
REMARK 465     LYS A    90                                                      
REMARK 465     VAL A    91                                                      
REMARK 465     PHE A    92                                                      
REMARK 465     ASP A    93                                                      
REMARK 465     ARG A    94                                                      
REMARK 465     ASP A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     ASN A    97                                                      
REMARK 465     GLY A    98                                                      
REMARK 465     LEU A    99                                                      
REMARK 465     ILE A   100                                                      
REMARK 465     SER A   101                                                      
REMARK 465     ALA A   102                                                      
REMARK 465     ALA A   103                                                      
REMARK 465     GLU A   104                                                      
REMARK 465     LEU A   105                                                      
REMARK 465     ARG A   106                                                      
REMARK 465     HIS A   107                                                      
REMARK 465     VAL A   108                                                      
REMARK 465     MET A   109                                                      
REMARK 465     THR A   110                                                      
REMARK 465     ASN A   111                                                      
REMARK 465     LEU A   112                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     GLU A   114                                                      
REMARK 465     LYS A   115                                                      
REMARK 465     LEU A   116                                                      
REMARK 465     THR A   117                                                      
REMARK 465     ASP A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     GLU A   120                                                      
REMARK 465     VAL A   121                                                      
REMARK 465     ASP A   122                                                      
REMARK 465     GLU A   123                                                      
REMARK 465     MET A   124                                                      
REMARK 465     ILE A   125                                                      
REMARK 465     ARG A   126                                                      
REMARK 465     GLU A   127                                                      
REMARK 465     ALA A   128                                                      
REMARK 465     ASP A   129                                                      
REMARK 465     ILE A   130                                                      
REMARK 465     ASP A   131                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     HIS A   135                                                      
REMARK 465     ILE A   136                                                      
REMARK 465     ASN A   137                                                      
REMARK 465     TYR A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLU A   140                                                      
REMARK 465     PHE A   141                                                      
REMARK 465     VAL A   142                                                      
REMARK 465     ARG A   143                                                      
REMARK 465     MET A   144                                                      
REMARK 465     MET A   145                                                      
REMARK 465     VAL A   146                                                      
REMARK 465     SER A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLU B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     ILE B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     PHE B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     PHE B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     PHE B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     LYS B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     ILE B    27                                                      
REMARK 465     THR B    28                                                      
REMARK 465     THR B    29                                                      
REMARK 465     LYS B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     LEU B    32                                                      
REMARK 465     GLY B    33                                                      
REMARK 465     THR B    34                                                      
REMARK 465     VAL B    35                                                      
REMARK 465     MET B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     LEU B    39                                                      
REMARK 465     GLY B    40                                                      
REMARK 465     GLN B    41                                                      
REMARK 465     ASN B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     THR B    44                                                      
REMARK 465     GLU B    45                                                      
REMARK 465     ALA B    46                                                      
REMARK 465     GLU B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     GLN B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     MET B    51                                                      
REMARK 465     ILE B    52                                                      
REMARK 465     ASN B    53                                                      
REMARK 465     GLU B    54                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     ASP B    56                                                      
REMARK 465     ALA B    57                                                      
REMARK 465     ASP B    58                                                      
REMARK 465     GLY B    59                                                      
REMARK 465     ASN B    60                                                      
REMARK 465     GLY B    61                                                      
REMARK 465     THR B    62                                                      
REMARK 465     ILE B    63                                                      
REMARK 465     ASP B    64                                                      
REMARK 465     PHE B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     PHE B    68                                                      
REMARK 465     LYS B   148                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  42       57.45   -154.80                                   
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                              PB A 507  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A   2   OE1                                                    
REMARK 620 2 GLU A   2   OE2  50.1                                              
REMARK 620 3 CAC A1001   O2   69.2 116.9                                        
REMARK 620 4 HOH A1020   O    76.3  80.4  69.3                                  
REMARK 620 5 GLU B  83   OE1 131.5 151.9  64.7  74.1                            
REMARK 620 6 GLU B  84   OE2 111.3  64.5 142.6  74.5  96.8                      
REMARK 620 7 GLU B 123   OE1 105.4  76.5 143.1 146.8 120.3  74.2                
REMARK 620 8 GLU B 123   OE2  81.9  88.1 100.0 158.0 119.8 117.2  43.9          
REMARK 620 9 GLU B 127   OE2 114.0 149.5  65.6 124.6  58.5 133.9  85.7  62.3    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB B 505  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A   2   OE2                                                    
REMARK 620 2 HOH A1031   O    88.6                                              
REMARK 620 3 GLU B  84   OE1  67.9  81.7                                        
REMARK 620 4 GLU B  84   OE2  64.4 130.5  50.6                                  
REMARK 620 5 GLU B  87   OE2 145.3  99.7  80.0  85.4                            
REMARK 620 6 GLU B  87   OE1 130.2 141.1 111.2  77.6  50.5                      
REMARK 620 7 GLU B 123   OE1  75.8 127.0 133.0  87.4 121.7  71.5                
REMARK 620 8 HOH B2052   O   144.1  72.3 135.1 149.8  69.5  73.5  91.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB A 502  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A   7   OE1                                                    
REMARK 620 2 GLU A   7   OE2  51.6                                              
REMARK 620 3 ASP A  58   OD2  80.8 129.7                                        
REMARK 620 4 GLU B 114   OE1 146.7 161.5  66.8                                  
REMARK 620 5 LYS B 115   O   113.8  63.5 146.8  98.2                            
REMARK 620 6 GLU B 120   OE1 101.4  76.8 135.4  96.4  73.3                      
REMARK 620 7 GLU B 120   OE2  78.7  96.8  87.5  91.6 123.6  50.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB A 504  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  11   OE2                                                    
REMARK 620 2 GLU A  11   OE1  50.4                                              
REMARK 620 3 GLU A  14   OE1  84.0  72.6                                        
REMARK 620 4 GLU A  14   OE2  97.4 115.1  46.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB A 503  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  70.2                                              
REMARK 620 3 ASP A  24   OD1  75.2  85.5                                        
REMARK 620 4 THR A  26   O    71.6 141.6  80.3                                  
REMARK 620 5 THR A  26   OG1 108.6 131.3  50.0  58.9                            
REMARK 620 6 GLU A  31   OE1 112.9 129.5 145.1  71.3  96.9                      
REMARK 620 7 GLU A  31   OE2  95.0  78.8 163.6 109.5 146.3  50.8                
REMARK 620 8 HOH A1006   O   153.8  83.6 102.1 134.3  87.5  84.5  80.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB A 501  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD2 112.5                                              
REMARK 620 3 ASP A  58   OD1  76.2  44.2                                        
REMARK 620 4 ASN A  60   OD1  74.4 105.1  71.5                                  
REMARK 620 5 THR A  62   O    69.5 176.2 135.3  72.2                            
REMARK 620 6 ASP A  64   OD2 148.8  54.7  98.8 134.0 125.3                      
REMARK 620 7 GLU A  67   OE1  86.0 101.9 124.6 151.1  81.3  71.4                
REMARK 620 8 GLU A  67   OE2  76.7  64.7  78.3 142.1 119.0  72.2  46.5          
REMARK 620 9 HOH A1015   O   138.8 103.4 121.7  77.4  73.6  70.2 106.2 139.5    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB A 500  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  58   OD2                                                    
REMARK 620 2 ASP A  64   OD1 115.2                                              
REMARK 620 3 ASP A  64   OD2  76.9  44.0                                        
REMARK 620 4 GLU A  67   OE2  67.2  77.0  79.8                                  
REMARK 620 5 GLU B 114   OE1  83.3 118.2  94.2 150.5                            
REMARK 620 6 GLU B 114   OE2 130.1  76.5  84.6 153.0  52.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CAC A1001  AS                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  PB B 506  PB                                                      
REMARK 620 2 CAC A1001   O1   72.0                                              
REMARK 620 3 CAC A1001   O2   41.7 112.6                                        
REMARK 620 4 CAC A1001   C1  116.4 109.3 110.1                                  
REMARK 620 5 CAC A1001   C2  134.3 109.3 109.1 106.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB B 506  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAC A1001   O1                                                     
REMARK 620 2 CAC A1001   O2   55.6                                              
REMARK 620 3 ASP B  80   OD1  70.2  78.4                                        
REMARK 620 4 GLU B  83   OE1 128.4  77.4  81.5                                  
REMARK 620 5 GLU B  83   OE2 175.5 122.5 105.6  48.0                            
REMARK 620 6 GLU B 127   OE1  71.1  81.7 141.3 125.7 113.1                      
REMARK 620 7 GLU B 127   OE2 108.0  77.6 151.1  77.8  74.7  48.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB B 509  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAC A1001   O1                                                     
REMARK 620 2 ASP B  80   OD1  81.7                                              
REMARK 620 3 ASP B  80   OD2  95.8  46.6                                        
REMARK 620 4 HOH B2041   O   138.1 120.1  80.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB B 510  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD1                                                    
REMARK 620 2 ASP B  95   OD1  82.4                                              
REMARK 620 3 ASP B  95   OD2 120.8  38.4                                        
REMARK 620 4 ASN B  97   OD1  82.1  75.4  83.9                                  
REMARK 620 5 LEU B  99   O    90.3 155.0 142.4  79.9                            
REMARK 620 6 GLU B 104   OE1 101.4 129.1 113.7 155.4  75.8                      
REMARK 620 7 GLU B 104   OE2  98.9  77.3  71.8 152.4 127.6  51.8                
REMARK 620 8 HOH B2050   O   168.0  88.4  50.7  88.1  94.9  90.3  86.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PB B 508  PB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 129   OD1                                                    
REMARK 620 2 ASP B 131   OD1  72.3                                              
REMARK 620 3 ASP B 131   OD2 111.4  43.3                                        
REMARK 620 4 ASP B 133   OD1  76.8  70.3  96.8                                  
REMARK 620 5 HIS B 135   O    75.5 139.9 171.4  79.6                            
REMARK 620 6 GLU B 140   OE1 108.9 132.0 100.8 157.7  81.1                      
REMARK 620 7 GLU B 140   OE2  87.7  83.9  68.0 152.8 118.3  49.0                
REMARK 620 8 HOH B2027   O   152.9  83.9  53.0  83.1 118.6  96.7 102.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2001                
DBREF  1N0Y A    1   148  UNP    P07463   CALM_PARTE       1    148             
DBREF  1N0Y B    1   148  UNP    P07463   CALM_PARTE       1    148             
SEQRES   1 A  148  ALA GLU GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE ALA LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU SER LEU MET ALA ARG LYS MET LYS GLU          
SEQRES   7 A  148  GLN ASP SER GLU GLU GLU LEU ILE GLU ALA PHE LYS VAL          
SEQRES   8 A  148  PHE ASP ARG ASP GLY ASN GLY LEU ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP ASP GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY HIS ILE ASN TYR GLU GLU PHE VAL ARG          
SEQRES  12 A  148  MET MET VAL SER LYS                                          
SEQRES   1 B  148  ALA GLU GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 B  148  GLU ALA PHE ALA LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 B  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 B  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 B  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 B  148  PRO GLU PHE LEU SER LEU MET ALA ARG LYS MET LYS GLU          
SEQRES   7 B  148  GLN ASP SER GLU GLU GLU LEU ILE GLU ALA PHE LYS VAL          
SEQRES   8 B  148  PHE ASP ARG ASP GLY ASN GLY LEU ILE SER ALA ALA GLU          
SEQRES   9 B  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 B  148  ASP ASP GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 B  148  ASP GLY ASP GLY HIS ILE ASN TYR GLU GLU PHE VAL ARG          
SEQRES  12 B  148  MET MET VAL SER LYS                                          
HET     PB  A 500       1                                                       
HET     PB  A 501       1                                                       
HET     PB  A 502       1                                                       
HET     PB  A 503       1                                                       
HET     PB  A 504       1                                                       
HET     PB  A 507       1                                                       
HET     PB  A 513       1                                                       
HET    CAC  A1001       5                                                       
HET     PB  B 505       1                                                       
HET     PB  B 506       1                                                       
HET     PB  B 508       1                                                       
HET     PB  B 509       1                                                       
HET     PB  B 510       1                                                       
HET     PB  B 511       1                                                       
HET     PB  B 512       1                                                       
HET    ACT  B2001       4                                                       
HETNAM      PB LEAD (II) ION                                                    
HETNAM     CAC CACODYLATE ION                                                   
HETNAM     ACT ACETATE ION                                                      
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   3   PB    14(PB 2+)                                                    
FORMUL  10  CAC    C2 H6 AS O2 1-                                               
FORMUL  18  ACT    C2 H3 O2 1-                                                  
FORMUL  19  HOH   *149(H2 O)                                                    
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  SER A   38  1                                  11    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 PHE A   65  GLU A   84  1                                  20    
HELIX    5   5 LEU B   69  ASP B   93  1                                  25    
HELIX    6   6 SER B  101  LEU B  112  1                                  12    
HELIX    7   7 THR B  117  GLU B  127  1                                  11    
HELIX    8   8 TYR B  138  VAL B  146  1                                   9    
SHEET    1   A 2 THR A  26  ILE A  27  0                                        
SHEET    2   A 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1   B 2 LEU B  99  ILE B 100  0                                        
SHEET    2   B 2 ILE B 136  ASN B 137 -1  O  ILE B 136   N  ILE B 100           
LINK         OE1 GLU A   2                PB    PB A 507     1555   1555  2.47  
LINK         OE2 GLU A   2                PB    PB A 507     1555   1555  2.69  
LINK         OE2 GLU A   2                PB    PB B 505     1555   1555  3.08  
LINK         OE1 GLU A   7                PB    PB A 502     1555   1555  2.64  
LINK         OE2 GLU A   7                PB    PB A 502     1555   1555  2.36  
LINK         OE2 GLU A  11                PB    PB A 504     1555   1555  2.48  
LINK         OE1 GLU A  11                PB    PB A 504     1555   1555  2.66  
LINK         OE1 GLU A  14                PB    PB A 504     1555   1555  2.32  
LINK         OE2 GLU A  14                PB    PB A 504     1555   1555  3.04  
LINK         OD1 ASP A  20                PB    PB A 503     1555   1555  2.30  
LINK         OD1 ASP A  22                PB    PB A 503     1555   1555  2.51  
LINK         OD1 ASP A  24                PB    PB A 503     1555   1555  2.62  
LINK         O   THR A  26                PB    PB A 503     1555   1555  2.67  
LINK         OG1 THR A  26                PB    PB A 503     1555   1555  3.49  
LINK         OE1 GLU A  31                PB    PB A 503     1555   1555  2.58  
LINK         OE2 GLU A  31                PB    PB A 503     1555   1555  2.54  
LINK         OD1 ASP A  56                PB    PB A 501     1555   1555  2.25  
LINK         OD2 ASP A  58                PB    PB A 500     1555   1555  2.41  
LINK         OD2 ASP A  58                PB    PB A 501     1555   1555  3.13  
LINK         OD1 ASP A  58                PB    PB A 501     1555   1555  2.45  
LINK         OD2 ASP A  58                PB    PB A 502     1545   1555  3.12  
LINK         OD1 ASN A  60                PB    PB A 501     1555   1555  2.35  
LINK         O   THR A  62                PB    PB A 501     1555   1555  2.52  
LINK         OD1 ASP A  64                PB    PB A 500     1555   1555  3.16  
LINK         OD2 ASP A  64                PB    PB A 500     1555   1555  2.37  
LINK         OD2 ASP A  64                PB    PB A 501     1555   1555  3.34  
LINK         OE2 GLU A  67                PB    PB A 500     1555   1555  3.23  
LINK         OE1 GLU A  67                PB    PB A 501     1555   1555  2.75  
LINK         OE2 GLU A  67                PB    PB A 501     1555   1555  2.82  
LINK        PB    PB A 500                 OE1 GLU B 114     1555   1555  2.50  
LINK        PB    PB A 500                 OE2 GLU B 114     1555   1555  2.51  
LINK        PB    PB A 501                 O   HOH A1015     1555   1555  3.24  
LINK        PB    PB A 502                 OE1 GLU B 114     1555   1545  2.78  
LINK        PB    PB A 502                 O   LYS B 115     1555   1545  2.87  
LINK        PB    PB A 502                 OE1 GLU B 120     1555   1545  2.67  
LINK        PB    PB A 502                 OE2 GLU B 120     1555   1545  2.46  
LINK        PB    PB A 503                 O   HOH A1006     1555   1555  2.60  
LINK        PB    PB A 507                 O2  CAC A1001     1555   1555  2.46  
LINK        PB    PB A 507                 O   HOH A1020     1555   1555  2.91  
LINK        PB    PB A 507                 OE1 GLU B  83     1555   1555  3.13  
LINK        PB    PB A 507                 OE2 GLU B  84     1555   1555  3.00  
LINK        PB    PB A 507                 OE1 GLU B 123     1555   1545  3.04  
LINK        PB    PB A 507                 OE2 GLU B 123     1555   1545  2.78  
LINK        PB    PB A 507                 OE2 GLU B 127     1555   1545  3.10  
LINK        PB    PB A 507                 O   HOH B2034     1555   1545  3.45  
LINK        AS   CAC A1001                PB    PB B 506     1555   1555  3.44  
LINK         O1  CAC A1001                PB    PB B 506     1555   1555  3.33  
LINK         O2  CAC A1001                PB    PB B 506     1555   1555  2.45  
LINK         O1  CAC A1001                PB    PB B 509     1555   1555  2.38  
LINK         O   HOH A1031                PB    PB B 505     1555   1555  2.90  
LINK         OD1 ASP B  80                PB    PB B 506     1555   1555  2.75  
LINK         OD1 ASP B  80                PB    PB B 509     1555   1555  2.97  
LINK         OD2 ASP B  80                PB    PB B 509     1555   1555  2.44  
LINK         OE1 GLU B  83                PB    PB B 506     1555   1555  2.41  
LINK         OE2 GLU B  83                PB    PB B 506     1555   1555  2.88  
LINK         OE1 GLU B  84                PB    PB B 505     1555   1555  2.56  
LINK         OE2 GLU B  84                PB    PB B 505     1555   1555  2.58  
LINK         OE2 GLU B  87                PB    PB B 505     1555   1555  2.47  
LINK         OE1 GLU B  87                PB    PB B 505     1555   1555  2.66  
LINK         OD1 ASP B  93                PB    PB B 510     1555   1555  2.36  
LINK         OD1 ASP B  95                PB    PB B 510     1555   1555  2.35  
LINK         OD2 ASP B  95                PB    PB B 510     1555   1555  3.48  
LINK         OD1 ASN B  97                PB    PB B 510     1555   1555  2.36  
LINK         O   LEU B  99                PB    PB B 510     1555   1555  2.28  
LINK         OE1 GLU B 104                PB    PB B 510     1555   1555  2.49  
LINK         OE2 GLU B 104                PB    PB B 510     1555   1555  2.54  
LINK         OE1 GLU B 123                PB    PB B 505     1545   1555  2.69  
LINK         OE1 GLU B 127                PB    PB B 506     1545   1555  2.82  
LINK         OE2 GLU B 127                PB    PB B 506     1545   1555  2.43  
LINK         OD1 ASP B 129                PB    PB B 508     1555   1555  2.37  
LINK         OD1 ASP B 131                PB    PB B 508     1555   1555  2.47  
LINK         OD2 ASP B 131                PB    PB B 508     1555   1555  3.19  
LINK         OD1 ASP B 133                PB    PB B 508     1555   1555  2.25  
LINK         O   HIS B 135                PB    PB B 508     1555   1555  2.52  
LINK         OE1 GLU B 140                PB    PB B 508     1555   1555  2.47  
LINK         OE2 GLU B 140                PB    PB B 508     1555   1555  2.78  
LINK        PB    PB B 505                 O   HOH B2052     1555   1545  2.77  
LINK        PB    PB B 508                 O   HOH B2027     1555   1555  2.83  
LINK        PB    PB B 509                 O   HOH B2041     1555   1555  2.68  
LINK        PB    PB B 510                 O   HOH B2050     1555   1555  2.38  
SITE     1 AC1  4 ASP A  58  ASP A  64  GLU A  67  GLU B 114                    
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 ASP A  64  GLU A  67                                          
SITE     1 AC3  5 GLU A   7  ASP A  58  GLU B 114  LYS B 115                    
SITE     2 AC3  5 GLU B 120                                                     
SITE     1 AC4  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC4  6 GLU A  31  HOH A1006                                          
SITE     1 AC5  2 GLU A  11  GLU A  14                                          
SITE     1 AC6  6 GLU A   2  HOH A1031  GLU B  84  GLU B  87                    
SITE     2 AC6  6 GLU B 123  HOH B2052                                          
SITE     1 AC7  4 CAC A1001  ASP B  80  GLU B  83  GLU B 127                    
SITE     1 AC8  7 GLU A   2  CAC A1001  HOH A1020  GLU B  83                    
SITE     2 AC8  7 GLU B  84  GLU B 123  GLU B 127                               
SITE     1 AC9  6 ASP B 129  ASP B 131  ASP B 133  HIS B 135                    
SITE     2 AC9  6 GLU B 140  HOH B2027                                          
SITE     1 BC1  3 CAC A1001  ASP B  80  HOH B2041                               
SITE     1 BC2  6 ASP B  93  ASP B  95  ASN B  97  LEU B  99                    
SITE     2 BC2  6 GLU B 104  HOH B2050                                          
SITE     1 BC3 10 ALA A   1  GLU A   2   PB A 507  HOH A1020                    
SITE     2 BC3 10 HOH A1034  ASP B  80  GLU B  83  GLU B 127                    
SITE     3 BC3 10  PB B 506   PB B 509                                          
SITE     1 BC4  3 VAL B 108  ASN B 111  LEU B 112                               
CRYST1  100.936   30.792  113.084  90.00 109.31  90.00 C 1 2 1       8          
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      0.009907  0.000000  0.003471        0.00000                         
SCALE2      0.000000  0.032476  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009370        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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