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Database: PDB
Entry: 6HCS
LinkDB: 6HCS
Original site: 6HCS 
HEADER    PROTEIN BINDING                         16-AUG-18   6HCS              
TITLE     CRYSTAL STRUCTURE OF CAM-PEPTIDE COMPLEX CONTAINING AZF AT POSITION   
TITLE    2 108                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN-1;                                              
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT
COMPND   7 BETA;                                                                
COMPND   8 CHAIN: B, D, F, H;                                                   
COMPND   9 SYNONYM: CAMK-II SUBUNIT BETA;                                       
COMPND  10 EC: 2.7.11.17;                                                       
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CALM1, CALM, CAM, CAM1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: RAT;                                                
SOURCE  12 ORGANISM_TAXID: 10116                                                
KEYWDS    CALMODULIN, UNNATURAL AMINO ACID, AZF, PROTEIN BINDING                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CREON,I.JOSTS,H.TIDOW                                               
REVDAT   3   17-JAN-24 6HCS    1       LINK                                     
REVDAT   2   19-DEC-18 6HCS    1       REMARK                                   
REVDAT   1   05-DEC-18 6HCS    0                                                
JRNL        AUTH   A.CREON,I.JOSTS,S.NIEBLING,N.HUSE,H.TIDOW                    
JRNL        TITL   CONFORMATION-SPECIFIC DETECTION OF CALMODULIN BINDING USING  
JRNL        TITL 2 THE UNNATURAL AMINO ACID P-AZIDO-PHENYLALANINE (AZF) AS AN   
JRNL        TITL 3 IR-SENSOR.                                                   
JRNL        REF    STRUCT DYN                    V.   5 64701 2018              
JRNL        REFN                   ESSN 2329-7778                               
JRNL        PMID   30474048                                                     
JRNL        DOI    10.1063/1.5053466                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 45027                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.262                           
REMARK   3   R VALUE            (WORKING SET) : 0.260                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2256                            
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 43.1289 -  5.0372    0.95     2771   129  0.2497 0.2849        
REMARK   3     2  5.0372 -  3.9991    0.96     2672   160  0.2354 0.2639        
REMARK   3     3  3.9991 -  3.4938    0.95     2640   125  0.2447 0.2503        
REMARK   3     4  3.4938 -  3.1745    0.95     2599   148  0.2540 0.3092        
REMARK   3     5  3.1745 -  2.9470    0.98     2673   147  0.2708 0.3273        
REMARK   3     6  2.9470 -  2.7733    0.99     2716   141  0.2792 0.3126        
REMARK   3     7  2.7733 -  2.6344    0.99     2667   134  0.2615 0.3043        
REMARK   3     8  2.6344 -  2.5198    0.97     2645   147  0.2607 0.2850        
REMARK   3     9  2.5198 -  2.4228    0.97     2647   148  0.2665 0.3040        
REMARK   3    10  2.4228 -  2.3392    0.98     2667   134  0.2702 0.3352        
REMARK   3    11  2.3392 -  2.2660    0.98     2670   143  0.2690 0.3159        
REMARK   3    12  2.2660 -  2.2013    0.98     2638   148  0.2751 0.3105        
REMARK   3    13  2.2013 -  2.1433    0.99     2725   121  0.2793 0.2895        
REMARK   3    14  2.1433 -  2.0910    0.99     2654   138  0.2966 0.3066        
REMARK   3    15  2.0910 -  2.0435    0.99     2707   140  0.3047 0.3428        
REMARK   3    16  2.0435 -  2.0000    0.99     2680   153  0.3173 0.3488        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.590           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.007           5031                                  
REMARK   3   ANGLE     :  0.859           6711                                  
REMARK   3   CHIRALITY :  0.046            744                                  
REMARK   3   PLANARITY :  0.004            893                                  
REMARK   3   DIHEDRAL  : 35.148           1892                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 6HCS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011316.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.917143                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1CDM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, LITHIUM CHLORIDE, SODIUM       
REMARK 280  CHLORIDE, PH 5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       18.60700            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8300 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8540 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8600 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8620 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     MET A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     GLU A    83                                                      
REMARK 465     ALA A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     GLU A   150                                                      
REMARK 465     GLY A   151                                                      
REMARK 465     THR A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     LEU A   154                                                      
REMARK 465     GLU A   155                                                      
REMARK 465     VAL A   156                                                      
REMARK 465     LEU A   157                                                      
REMARK 465     PHE A   158                                                      
REMARK 465     GLN A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     HIS A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     LEU B   290                                                      
REMARK 465     LYS B   291                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     ASN B   312                                                      
REMARK 465     PHE B   313                                                      
REMARK 465     SER B   314                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     LYS C    77                                                      
REMARK 465     ASP C    78                                                      
REMARK 465     THR C    79                                                      
REMARK 465     ASP C    80                                                      
REMARK 465     SER C    81                                                      
REMARK 465     GLU C    82                                                      
REMARK 465     ALA C   147                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     LEU C   149                                                      
REMARK 465     GLU C   150                                                      
REMARK 465     GLY C   151                                                      
REMARK 465     THR C   152                                                      
REMARK 465     GLY C   153                                                      
REMARK 465     LEU C   154                                                      
REMARK 465     GLU C   155                                                      
REMARK 465     VAL C   156                                                      
REMARK 465     LEU C   157                                                      
REMARK 465     PHE C   158                                                      
REMARK 465     GLN C   159                                                      
REMARK 465     GLY C   160                                                      
REMARK 465     HIS C   161                                                      
REMARK 465     HIS C   162                                                      
REMARK 465     HIS C   163                                                      
REMARK 465     HIS C   164                                                      
REMARK 465     HIS C   165                                                      
REMARK 465     HIS C   166                                                      
REMARK 465     LEU D   290                                                      
REMARK 465     LYS D   291                                                      
REMARK 465     LYS D   292                                                      
REMARK 465     SER D   314                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     LYS E    77                                                      
REMARK 465     ASP E    78                                                      
REMARK 465     THR E    79                                                      
REMARK 465     ASP E    80                                                      
REMARK 465     SER E    81                                                      
REMARK 465     GLU E    82                                                      
REMARK 465     GLU E    83                                                      
REMARK 465     ALA E   147                                                      
REMARK 465     LYS E   148                                                      
REMARK 465     LEU E   149                                                      
REMARK 465     GLU E   150                                                      
REMARK 465     GLY E   151                                                      
REMARK 465     THR E   152                                                      
REMARK 465     GLY E   153                                                      
REMARK 465     LEU E   154                                                      
REMARK 465     GLU E   155                                                      
REMARK 465     VAL E   156                                                      
REMARK 465     LEU E   157                                                      
REMARK 465     PHE E   158                                                      
REMARK 465     GLN E   159                                                      
REMARK 465     GLY E   160                                                      
REMARK 465     HIS E   161                                                      
REMARK 465     HIS E   162                                                      
REMARK 465     HIS E   163                                                      
REMARK 465     HIS E   164                                                      
REMARK 465     HIS E   165                                                      
REMARK 465     HIS E   166                                                      
REMARK 465     LEU F   290                                                      
REMARK 465     LYS F   291                                                      
REMARK 465     LYS F   292                                                      
REMARK 465     ARG F   311                                                      
REMARK 465     ASN F   312                                                      
REMARK 465     PHE F   313                                                      
REMARK 465     SER F   314                                                      
REMARK 465     MET G     0                                                      
REMARK 465     ALA G     1                                                      
REMARK 465     LYS G    77                                                      
REMARK 465     ASP G    78                                                      
REMARK 465     THR G    79                                                      
REMARK 465     ASP G    80                                                      
REMARK 465     SER G    81                                                      
REMARK 465     GLU G    82                                                      
REMARK 465     GLU G    83                                                      
REMARK 465     ALA G   147                                                      
REMARK 465     LYS G   148                                                      
REMARK 465     LEU G   149                                                      
REMARK 465     GLU G   150                                                      
REMARK 465     GLY G   151                                                      
REMARK 465     THR G   152                                                      
REMARK 465     GLY G   153                                                      
REMARK 465     LEU G   154                                                      
REMARK 465     GLU G   155                                                      
REMARK 465     VAL G   156                                                      
REMARK 465     LEU G   157                                                      
REMARK 465     PHE G   158                                                      
REMARK 465     GLN G   159                                                      
REMARK 465     GLY G   160                                                      
REMARK 465     HIS G   161                                                      
REMARK 465     HIS G   162                                                      
REMARK 465     HIS G   163                                                      
REMARK 465     HIS G   164                                                      
REMARK 465     HIS G   165                                                      
REMARK 465     HIS G   166                                                      
REMARK 465     LEU H   290                                                      
REMARK 465     LYS H   291                                                      
REMARK 465     LYS H   292                                                      
REMARK 465     ARG H   311                                                      
REMARK 465     ASN H   312                                                      
REMARK 465     PHE H   313                                                      
REMARK 465     SER H   314                                                      
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     MET E  76    CG   SD   CE                                        
REMARK 470     MET G  76    CG   SD   CE                                        
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   N2   4II G   108     OG1  THR H   306              1.64            
REMARK 500   O    THR C   146     O    HOH C   301              2.13            
REMARK 500   N2   4II G   108     O    ALA H   302              2.14            
REMARK 500   N    PHE F   293     O    HOH F   401              2.16            
REMARK 500   O    HOH C   356     O    HOH D   406              2.17            
REMARK 500   O    THR E   146     O    HOH E   301              2.18            
REMARK 500   O    HOH A   345     O    HOH A   379              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    HIS A 107   O   -  C   -  N   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    4II A 108   O   -  C   -  N   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    HIS C 107   O   -  C   -  N   ANGL. DEV. = -11.3 DEGREES          
REMARK 500    4II C 108   O   -  C   -  N   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    MET E 109   C   -  N   -  CA  ANGL. DEV. =  20.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG D 311       54.44   -144.34                                   
REMARK 500    ASN D 312     -128.84     65.42                                   
REMARK 500    ASP E  20       73.61    -66.53                                   
REMARK 500    ASN E  42       79.33   -118.36                                   
REMARK 500    THR E  62     -166.30   -127.75                                   
REMARK 500    GLN G   3     -167.94   -173.39                                   
REMARK 500    ASP G  56       88.06    -68.01                                   
REMARK 500    ASP G  93       85.10    -67.42                                   
REMARK 500    ASN G  97        2.49    -68.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    HIS A 107         16.49                                           
REMARK 500    HIS C 107         11.13                                           
REMARK 500    HIS E 107        -10.17                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 398        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH A 399        DISTANCE =  7.34 ANGSTROMS                       
REMARK 525    HOH A 400        DISTANCE =  8.21 ANGSTROMS                       
REMARK 525    HOH C 393        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH C 394        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH E 317        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH E 318        DISTANCE =  7.73 ANGSTROMS                       
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                              CA A 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  74.7                                              
REMARK 620 3 ASP A  24   OD1  84.4  73.0                                        
REMARK 620 4 THR A  26   O    87.5 151.1  83.0                                  
REMARK 620 5 GLU A  31   OE1 110.0 128.5 156.0  78.7                            
REMARK 620 6 GLU A  31   OE2  96.7  77.0 148.5 128.5  51.6                      
REMARK 620 7 HOH A 342   O   158.1  86.3  79.6 105.2  90.2  89.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  76.8                                              
REMARK 620 3 ASN A  60   OD1  89.2  78.8                                        
REMARK 620 4 THR A  62   O    79.5 150.5  83.5                                  
REMARK 620 5 GLU A  67   OE1 103.3 121.1 158.2  81.4                            
REMARK 620 6 GLU A  67   OE2  83.3  73.2 152.0 121.2  49.0                      
REMARK 620 7 HOH A 312   O   151.6  78.1  98.9 128.3  78.6  76.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD1  84.7                                              
REMARK 620 3 ASN A  97   OD1  84.0  76.8                                        
REMARK 620 4 TYR A  99   O    88.6 155.6  79.1                                  
REMARK 620 5 GLU A 104   OE1  99.5  76.1 152.2 128.3                            
REMARK 620 6 GLU A 104   OE2 105.0 127.8 153.8  76.7  51.8                      
REMARK 620 7 HOH A 313   O   170.3  86.1  90.7  98.4  81.4  83.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  79.8                                              
REMARK 620 3 ASP A 133   OD1  86.4  76.3                                        
REMARK 620 4 GLN A 135   O    84.7 152.2  79.9                                  
REMARK 620 5 GLU A 140   OE1  89.5  76.7 153.0 126.3                            
REMARK 620 6 GLU A 140   OE2 112.4 127.8 150.5  79.5  54.0                      
REMARK 620 7 HOH A 311   O   161.6  86.5  78.5 102.7  99.2  85.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  20   OD1                                                    
REMARK 620 2 ASP C  22   OD1  75.4                                              
REMARK 620 3 ASP C  24   OD1  87.6  71.9                                        
REMARK 620 4 THR C  26   O    84.1 148.1  83.2                                  
REMARK 620 5 GLU C  31   OE1 109.5 133.7 151.2  76.0                            
REMARK 620 6 GLU C  31   OE2  95.0  81.6 151.8 124.9  52.4                      
REMARK 620 7 HOH C 320   O   159.8  85.2  80.9 110.8  88.0  87.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  56   OD1                                                    
REMARK 620 2 ASP C  58   OD1  77.0                                              
REMARK 620 3 ASN C  60   OD1  91.4  80.9                                        
REMARK 620 4 THR C  62   O    83.0 155.0  84.7                                  
REMARK 620 5 GLU C  67   OE1 100.1 116.8 160.5  81.2                            
REMARK 620 6 GLU C  67   OE2  81.6  69.4 150.3 122.5  48.3                      
REMARK 620 7 HOH C 307   O   149.6  75.3  96.3 126.8  81.7  77.3                
REMARK 620 8 HOH C 347   O   146.5 131.2  78.3  64.4  83.5 122.0  63.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  93   OD1                                                    
REMARK 620 2 ASP C  95   OD1  82.4                                              
REMARK 620 3 ASN C  97   OD1  86.4  76.7                                        
REMARK 620 4 TYR C  99   O    90.0 156.2  80.4                                  
REMARK 620 5 GLU C 104   OE1  95.2  76.2 152.4 127.1                            
REMARK 620 6 GLU C 104   OE2 102.9 127.6 154.6  76.1  51.4                      
REMARK 620 7 HOH C 312   O   167.5  85.3  92.9 102.2  79.7  82.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 129   OD1                                                    
REMARK 620 2 ASP C 131   OD1  79.6                                              
REMARK 620 3 ASP C 133   OD1  85.7  76.2                                        
REMARK 620 4 GLN C 135   O    85.2 151.4  78.6                                  
REMARK 620 5 GLU C 140   OE1  91.1  79.8 156.0 124.8                            
REMARK 620 6 GLU C 140   OE2 114.9 129.1 148.2  79.3  52.9                      
REMARK 620 7 HOH C 306   O   159.2  85.1  77.1 102.4 100.0  85.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  20   OD1                                                    
REMARK 620 2 ASP E  22   OD1  67.4                                              
REMARK 620 3 ASP E  24   OD1  69.5  70.0                                        
REMARK 620 4 THR E  26   O    71.2 136.0  82.3                                  
REMARK 620 5 GLU E  31   OE1 110.9 126.3 163.2  82.1                            
REMARK 620 6 GLU E  31   OE2  93.6  69.6 139.6 128.0  56.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  56   OD2                                                    
REMARK 620 2 ASN E  60   OD1  71.0                                              
REMARK 620 3 THR E  62   O    82.1  62.7                                        
REMARK 620 4 GLU E  67   OE1 107.5 149.2  86.5                                  
REMARK 620 5 GLU E  67   OE2  74.8 145.4 118.1  49.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  93   OD2                                                    
REMARK 620 2 ASP E  95   OD1  76.2                                              
REMARK 620 3 ASN E  97   OD1  87.5  70.5                                        
REMARK 620 4 TYR E  99   O    99.8 149.2  78.9                                  
REMARK 620 5 GLU E 104   OE1  90.5  82.9 153.1 127.8                            
REMARK 620 6 GLU E 104   OE2 112.7 134.3 149.9  75.9  53.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 129   OD1                                                    
REMARK 620 2 ASP E 131   OD1  77.9                                              
REMARK 620 3 ASP E 133   OD1  93.2  86.4                                        
REMARK 620 4 GLN E 135   O    77.5 145.8  71.7                                  
REMARK 620 5 GLU E 140   OE1  90.1  76.0 161.0 127.2                            
REMARK 620 6 GLU E 140   OE2 105.3 123.1 147.5  86.2  47.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  20   OD1                                                    
REMARK 620 2 ASP G  22   OD2 128.2                                              
REMARK 620 3 THR G  26   O    74.7 154.4                                        
REMARK 620 4 GLU G  31   OE1 116.1  95.8  80.7                                  
REMARK 620 5 GLU G  31   OE2  98.2  71.0 121.9  50.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  56   OD1                                                    
REMARK 620 2 ASP G  58   OD1  65.4                                              
REMARK 620 3 ASN G  60   OD1  85.0  71.8                                        
REMARK 620 4 THR G  62   O    84.8 143.3  85.2                                  
REMARK 620 5 GLU G  67   OE1 103.6 122.9 164.9  83.2                            
REMARK 620 6 GLU G  67   OE2  75.8  69.4 141.0 125.4  54.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  93   OD2                                                    
REMARK 620 2 ASP G  95   OD1 123.2                                              
REMARK 620 3 ASN G  97   OD1  88.7  92.9                                        
REMARK 620 4 TYR G  99   O    99.2 137.5  88.3                                  
REMARK 620 5 GLU G 104   OE1  94.5  61.9 151.7 118.8                            
REMARK 620 6 GLU G 104   OE2 108.3  94.4 153.3  69.2  49.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 129   OD1                                                    
REMARK 620 2 ASP G 131   OD1  77.4                                              
REMARK 620 3 ASP G 133   OD2  84.0  79.7                                        
REMARK 620 4 GLN G 135   O    88.9 146.1  68.0                                  
REMARK 620 5 GLU G 140   OE1  92.8  80.7 160.4 131.4                            
REMARK 620 6 GLU G 140   OE2  99.8 133.3 146.9  79.2  52.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 204                  
DBREF  6HCS A    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6HCS B  290   314  UNP    P08413   KCC2B_RAT      291    315             
DBREF  6HCS C    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6HCS D  290   314  UNP    P08413   KCC2B_RAT      291    315             
DBREF  6HCS E    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6HCS F  290   314  UNP    P08413   KCC2B_RAT      291    315             
DBREF  6HCS G    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6HCS H  290   314  UNP    P08413   KCC2B_RAT      291    315             
SEQADV 6HCS 4II A  108  UNP  P0DP23    VAL   109 ENGINEERED MUTATION            
SEQADV 6HCS LEU A  149  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU A  150  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY A  151  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS THR A  152  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY A  153  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU A  154  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU A  155  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS VAL A  156  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU A  157  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS PHE A  158  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLN A  159  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY A  160  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS A  161  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS A  162  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS A  163  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS A  164  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS A  165  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS A  166  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS 4II C  108  UNP  P0DP23    VAL   109 ENGINEERED MUTATION            
SEQADV 6HCS LEU C  149  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU C  150  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY C  151  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS THR C  152  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY C  153  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU C  154  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU C  155  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS VAL C  156  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU C  157  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS PHE C  158  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLN C  159  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY C  160  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS C  161  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS C  162  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS C  163  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS C  164  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS C  165  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS C  166  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS 4II E  108  UNP  P0DP23    VAL   109 ENGINEERED MUTATION            
SEQADV 6HCS LEU E  149  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU E  150  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY E  151  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS THR E  152  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY E  153  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU E  154  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU E  155  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS VAL E  156  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU E  157  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS PHE E  158  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLN E  159  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY E  160  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS E  161  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS E  162  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS E  163  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS E  164  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS E  165  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS E  166  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS 4II G  108  UNP  P0DP23    VAL   109 ENGINEERED MUTATION            
SEQADV 6HCS LEU G  149  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU G  150  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY G  151  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS THR G  152  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY G  153  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU G  154  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLU G  155  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS VAL G  156  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS LEU G  157  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS PHE G  158  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLN G  159  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS GLY G  160  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS G  161  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS G  162  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS G  163  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS G  164  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS G  165  UNP  P0DP23              EXPRESSION TAG                 
SEQADV 6HCS HIS G  166  UNP  P0DP23              EXPRESSION TAG                 
SEQRES   1 A  167  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 A  167  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 A  167  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 A  167  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 A  167  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 A  167  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 A  167  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 A  167  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 A  167  GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 A  167  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 A  167  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 A  167  GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU          
SEQRES  13 A  167  VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B   25  LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA          
SEQRES   2 B   25  ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER              
SEQRES   1 C  167  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 C  167  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 C  167  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 C  167  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 C  167  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 C  167  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 C  167  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 C  167  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 C  167  GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 C  167  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 C  167  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 C  167  GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU          
SEQRES  13 C  167  VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS                  
SEQRES   1 D   25  LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA          
SEQRES   2 D   25  ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER              
SEQRES   1 E  167  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 E  167  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 E  167  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 E  167  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 E  167  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 E  167  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 E  167  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 E  167  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 E  167  GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 E  167  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 E  167  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 E  167  GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU          
SEQRES  13 E  167  VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS                  
SEQRES   1 F   25  LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA          
SEQRES   2 F   25  ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER              
SEQRES   1 G  167  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 G  167  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 G  167  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 G  167  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 G  167  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 G  167  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 G  167  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 G  167  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 G  167  GLU LEU ARG HIS 4II MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 G  167  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 G  167  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 G  167  GLN MET MET THR ALA LYS LEU GLU GLY THR GLY LEU GLU          
SEQRES  13 G  167  VAL LEU PHE GLN GLY HIS HIS HIS HIS HIS HIS                  
SEQRES   1 H   25  LEU LYS LYS PHE ASN ALA ARG ARG LYS LEU LYS GLY ALA          
SEQRES   2 H   25  ILE LEU THR THR MET LEU ALA THR ARG ASN PHE SER              
MODRES 6HCS 4II A  108  VAL  MODIFIED RESIDUE                                   
MODRES 6HCS 4II C  108  VAL  MODIFIED RESIDUE                                   
MODRES 6HCS 4II E  108  VAL  MODIFIED RESIDUE                                   
MODRES 6HCS 4II G  108  VAL  MODIFIED RESIDUE                                   
HET    4II  A 108      14                                                       
HET    4II  C 108      14                                                       
HET    4II  E 108      14                                                       
HET    4II  G 108      14                                                       
HET     CA  A 201       1                                                       
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  A 204       1                                                       
HET     CA  C 201       1                                                       
HET     CA  C 202       1                                                       
HET     CA  C 203       1                                                       
HET     CA  C 204       1                                                       
HET     CA  E 201       1                                                       
HET     CA  E 202       1                                                       
HET     CA  E 203       1                                                       
HET     CA  E 204       1                                                       
HET     CA  G 201       1                                                       
HET     CA  G 202       1                                                       
HET     CA  G 203       1                                                       
HET     CA  G 204       1                                                       
HETNAM     4II (2~{S})-2-AZANYL-3-(4-AZIDOPHENYL)PROPANOIC ACID                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   1  4II    4(C9 H10 N4 O2)                                              
FORMUL   9   CA    16(CA 2+)                                                    
FORMUL  25  HOH   *243(H2 O)                                                    
HELIX    1 AA1 THR A    5  ASP A   20  1                                  16    
HELIX    2 AA2 THR A   28  LEU A   39  1                                  12    
HELIX    3 AA3 THR A   44  ASP A   56  1                                  13    
HELIX    4 AA4 ASP A   64  LYS A   75  1                                  12    
HELIX    5 AA5 ILE A   85  ASP A   93  1                                   9    
HELIX    6 AA6 SER A  101  LEU A  112  1                                  12    
HELIX    7 AA7 THR A  117  ASP A  129  1                                  13    
HELIX    8 AA8 TYR A  138  THR A  146  1                                   9    
HELIX    9 AA9 ASN B  294  THR B  310  1                                  17    
HELIX   10 AB1 THR C    5  ASP C   20  1                                  16    
HELIX   11 AB2 THR C   28  LEU C   39  1                                  12    
HELIX   12 AB3 THR C   44  ASP C   56  1                                  13    
HELIX   13 AB4 ASP C   64  ARG C   74  1                                  11    
HELIX   14 AB5 GLU C   84  ASP C   93  1                                  10    
HELIX   15 AB6 SER C  101  LEU C  112  1                                  12    
HELIX   16 AB7 THR C  117  ASP C  129  1                                  13    
HELIX   17 AB8 TYR C  138  THR C  146  1                                   9    
HELIX   18 AB9 ASN D  294  THR D  310  1                                  17    
HELIX   19 AC1 THR E    5  ASP E   20  1                                  16    
HELIX   20 AC2 THR E   28  SER E   38  1                                  11    
HELIX   21 AC3 THR E   44  GLU E   54  1                                  11    
HELIX   22 AC4 PHE E   65  LYS E   75  1                                  11    
HELIX   23 AC5 ILE E   85  ASP E   93  1                                   9    
HELIX   24 AC6 SER E  101  ASN E  111  1                                  11    
HELIX   25 AC7 THR E  117  ASP E  129  1                                  13    
HELIX   26 AC8 TYR E  138  MET E  145  1                                   8    
HELIX   27 AC9 ASN F  294  THR F  310  1                                  17    
HELIX   28 AD1 THR G    5  ASP G   20  1                                  16    
HELIX   29 AD2 THR G   28  LEU G   39  1                                  12    
HELIX   30 AD3 THR G   44  ASP G   56  1                                  13    
HELIX   31 AD4 PHE G   65  LYS G   75  1                                  11    
HELIX   32 AD5 ILE G   85  ASP G   93  1                                   9    
HELIX   33 AD6 SER G  101  ASN G  111  1                                  11    
HELIX   34 AD7 THR G  117  ASP G  129  1                                  13    
HELIX   35 AD8 ASN G  137  MET G  145  1                                   9    
HELIX   36 AD9 ASN H  294  THR H  310  1                                  17    
SHEET    1 AA1 2 TYR A  99  ILE A 100  0                                        
SHEET    2 AA1 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
SHEET    1 AA2 2 TYR C  99  ILE C 100  0                                        
SHEET    2 AA2 2 VAL C 136  ASN C 137 -1  O  VAL C 136   N  ILE C 100           
SHEET    1 AA3 2 THR E  26  ILE E  27  0                                        
SHEET    2 AA3 2 ILE E  63  ASP E  64 -1  O  ILE E  63   N  ILE E  27           
SHEET    1 AA4 2 TYR E  99  ILE E 100  0                                        
SHEET    2 AA4 2 VAL E 136  ASN E 137 -1  O  VAL E 136   N  ILE E 100           
SHEET    1 AA5 2 THR G  26  ILE G  27  0                                        
SHEET    2 AA5 2 ILE G  63  ASP G  64 -1  O  ILE G  63   N  ILE G  27           
LINK         C   HIS A 107                 N   4II A 108     1555   1555  1.43  
LINK         C   4II A 108                 N   MET A 109     1555   1555  1.43  
LINK         C   HIS C 107                 N   4II C 108     1555   1555  1.42  
LINK         C   4II C 108                 N   MET C 109     1555   1555  1.43  
LINK         C   HIS E 107                 N   4II E 108     1555   1555  1.43  
LINK         C   4II E 108                 N   MET E 109     1555   1555  1.43  
LINK         C   HIS G 107                 N   4II G 108     1555   1555  1.43  
LINK         C   4II G 108                 N   MET G 109     1555   1555  1.43  
LINK         N3  4II G 108                 O   ALA H 302     1555   1555  1.30  
LINK         N1  4II G 108                 OG1 THR H 306     1555   1555  1.30  
LINK         OD1 ASP A  20                CA    CA A 201     1555   1555  2.38  
LINK         OD1 ASP A  22                CA    CA A 201     1555   1555  2.48  
LINK         OD1 ASP A  24                CA    CA A 201     1555   1555  2.41  
LINK         O   THR A  26                CA    CA A 201     1555   1555  2.21  
LINK         OE1 GLU A  31                CA    CA A 201     1555   1555  2.54  
LINK         OE2 GLU A  31                CA    CA A 201     1555   1555  2.44  
LINK         OD1 ASP A  56                CA    CA A 202     1555   1555  2.28  
LINK         OD1 ASP A  58                CA    CA A 202     1555   1555  2.44  
LINK         OD1 ASN A  60                CA    CA A 202     1555   1555  2.44  
LINK         O   THR A  62                CA    CA A 202     1555   1555  2.45  
LINK         OE1 GLU A  67                CA    CA A 202     1555   1555  2.64  
LINK         OE2 GLU A  67                CA    CA A 202     1555   1555  2.65  
LINK         OD1 ASP A  93                CA    CA A 203     1555   1555  2.26  
LINK         OD1 ASP A  95                CA    CA A 203     1555   1555  2.34  
LINK         OD1 ASN A  97                CA    CA A 203     1555   1555  2.51  
LINK         O   TYR A  99                CA    CA A 203     1555   1555  2.31  
LINK         OE1 GLU A 104                CA    CA A 203     1555   1555  2.57  
LINK         OE2 GLU A 104                CA    CA A 203     1555   1555  2.54  
LINK         OD1 ASP A 129                CA    CA A 204     1555   1555  2.36  
LINK         OD1 ASP A 131                CA    CA A 204     1555   1555  2.44  
LINK         OD1 ASP A 133                CA    CA A 204     1555   1555  2.50  
LINK         O   GLN A 135                CA    CA A 204     1555   1555  2.42  
LINK         OE1 GLU A 140                CA    CA A 204     1555   1555  2.53  
LINK         OE2 GLU A 140                CA    CA A 204     1555   1555  2.39  
LINK        CA    CA A 201                 O   HOH A 342     1555   1555  2.57  
LINK        CA    CA A 202                 O   HOH A 312     1555   1555  2.46  
LINK        CA    CA A 203                 O   HOH A 313     1555   1555  2.46  
LINK        CA    CA A 204                 O   HOH A 311     1555   1555  2.41  
LINK         OD1 ASP C  20                CA    CA C 201     1555   1555  2.35  
LINK         OD1 ASP C  22                CA    CA C 201     1555   1555  2.43  
LINK         OD1 ASP C  24                CA    CA C 201     1555   1555  2.48  
LINK         O   THR C  26                CA    CA C 201     1555   1555  2.35  
LINK         OE1 GLU C  31                CA    CA C 201     1555   1555  2.51  
LINK         OE2 GLU C  31                CA    CA C 201     1555   1555  2.47  
LINK         OD1 ASP C  56                CA    CA C 202     1555   1555  2.35  
LINK         OD1 ASP C  58                CA    CA C 202     1555   1555  2.40  
LINK         OD1 ASN C  60                CA    CA C 202     1555   1555  2.41  
LINK         O   THR C  62                CA    CA C 202     1555   1555  2.40  
LINK         OE1 GLU C  67                CA    CA C 202     1555   1555  2.62  
LINK         OE2 GLU C  67                CA    CA C 202     1555   1555  2.75  
LINK         OD1 ASP C  93                CA    CA C 203     1555   1555  2.24  
LINK         OD1 ASP C  95                CA    CA C 203     1555   1555  2.37  
LINK         OD1 ASN C  97                CA    CA C 203     1555   1555  2.52  
LINK         O   TYR C  99                CA    CA C 203     1555   1555  2.29  
LINK         OE1 GLU C 104                CA    CA C 203     1555   1555  2.51  
LINK         OE2 GLU C 104                CA    CA C 203     1555   1555  2.58  
LINK         OD1 ASP C 129                CA    CA C 204     1555   1555  2.40  
LINK         OD1 ASP C 131                CA    CA C 204     1555   1555  2.44  
LINK         OD1 ASP C 133                CA    CA C 204     1555   1555  2.36  
LINK         O   GLN C 135                CA    CA C 204     1555   1555  2.45  
LINK         OE1 GLU C 140                CA    CA C 204     1555   1555  2.42  
LINK         OE2 GLU C 140                CA    CA C 204     1555   1555  2.48  
LINK        CA    CA C 201                 O   HOH C 320     1555   1555  2.59  
LINK        CA    CA C 202                 O   HOH C 307     1555   1555  2.52  
LINK        CA    CA C 202                 O   HOH C 347     1555   1555  2.91  
LINK        CA    CA C 203                 O   HOH C 312     1555   1555  2.39  
LINK        CA    CA C 204                 O   HOH C 306     1555   1555  2.48  
LINK         OD1 ASP E  20                CA    CA E 204     1555   1555  2.61  
LINK         OD1 ASP E  22                CA    CA E 204     1555   1555  2.49  
LINK         OD1 ASP E  24                CA    CA E 204     1555   1555  2.71  
LINK         O   THR E  26                CA    CA E 204     1555   1555  2.44  
LINK         OE1 GLU E  31                CA    CA E 204     1555   1555  2.29  
LINK         OE2 GLU E  31                CA    CA E 204     1555   1555  2.37  
LINK         OD2 ASP E  56                CA    CA E 203     1555   1555  2.37  
LINK         OD1 ASN E  60                CA    CA E 203     1555   1555  2.36  
LINK         O   THR E  62                CA    CA E 203     1555   1555  2.73  
LINK         OE1 GLU E  67                CA    CA E 203     1555   1555  2.45  
LINK         OE2 GLU E  67                CA    CA E 203     1555   1555  2.77  
LINK         OD2 ASP E  93                CA    CA E 202     1555   1555  2.46  
LINK         OD1 ASP E  95                CA    CA E 202     1555   1555  2.93  
LINK         OD1 ASN E  97                CA    CA E 202     1555   1555  2.54  
LINK         O   TYR E  99                CA    CA E 202     1555   1555  2.36  
LINK         OE1 GLU E 104                CA    CA E 202     1555   1555  2.38  
LINK         OE2 GLU E 104                CA    CA E 202     1555   1555  2.52  
LINK         OD1 ASP E 129                CA    CA E 201     1555   1555  2.41  
LINK         OD1 ASP E 131                CA    CA E 201     1555   1555  2.51  
LINK         OD1 ASP E 133                CA    CA E 201     1555   1555  2.74  
LINK         O   GLN E 135                CA    CA E 201     1555   1555  2.73  
LINK         OE1 GLU E 140                CA    CA E 201     1555   1555  2.84  
LINK         OE2 GLU E 140                CA    CA E 201     1555   1555  2.55  
LINK         OD1 ASP G  20                CA    CA G 204     1555   1555  2.46  
LINK         OD2 ASP G  22                CA    CA G 204     1555   1555  3.05  
LINK         O   THR G  26                CA    CA G 204     1555   1555  2.34  
LINK         OE1 GLU G  31                CA    CA G 204     1555   1555  2.57  
LINK         OE2 GLU G  31                CA    CA G 204     1555   1555  2.59  
LINK         OD1 ASP G  56                CA    CA G 201     1555   1555  2.65  
LINK         OD1 ASP G  58                CA    CA G 201     1555   1555  2.64  
LINK         OD1 ASN G  60                CA    CA G 201     1555   1555  2.41  
LINK         O   THR G  62                CA    CA G 201     1555   1555  2.44  
LINK         OE1 GLU G  67                CA    CA G 201     1555   1555  2.37  
LINK         OE2 GLU G  67                CA    CA G 201     1555   1555  2.51  
LINK         OD2 ASP G  93                CA    CA G 202     1555   1555  2.37  
LINK         OD1 ASP G  95                CA    CA G 202     1555   1555  3.08  
LINK         OD1 ASN G  97                CA    CA G 202     1555   1555  2.58  
LINK         O   TYR G  99                CA    CA G 202     1555   1555  2.20  
LINK         OE1 GLU G 104                CA    CA G 202     1555   1555  2.47  
LINK         OE2 GLU G 104                CA    CA G 202     1555   1555  2.73  
LINK         OD1 ASP G 129                CA    CA G 203     1555   1555  2.42  
LINK         OD1 ASP G 131                CA    CA G 203     1555   1555  2.47  
LINK         OD2 ASP G 133                CA    CA G 203     1555   1555  2.40  
LINK         O   GLN G 135                CA    CA G 203     1555   1555  2.43  
LINK         OE1 GLU G 140                CA    CA G 203     1555   1555  2.43  
LINK         OE2 GLU G 140                CA    CA G 203     1555   1555  2.47  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 342                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 312                                          
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 313                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 311                                          
SITE     1 AC5  6 ASP C  20  ASP C  22  ASP C  24  THR C  26                    
SITE     2 AC5  6 GLU C  31  HOH C 320                                          
SITE     1 AC6  7 ASP C  56  ASP C  58  ASN C  60  THR C  62                    
SITE     2 AC6  7 GLU C  67  HOH C 307  HOH C 347                               
SITE     1 AC7  6 ASP C  93  ASP C  95  ASN C  97  TYR C  99                    
SITE     2 AC7  6 GLU C 104  HOH C 312                                          
SITE     1 AC8  6 ASP C 129  ASP C 131  ASP C 133  GLN C 135                    
SITE     2 AC8  6 GLU C 140  HOH C 306                                          
SITE     1 AC9  5 ASP E 129  ASP E 131  ASP E 133  GLN E 135                    
SITE     2 AC9  5 GLU E 140                                                     
SITE     1 AD1  5 ASP E  93  ASP E  95  ASN E  97  TYR E  99                    
SITE     2 AD1  5 GLU E 104                                                     
SITE     1 AD2  5 ASP E  56  ASP E  58  ASN E  60  THR E  62                    
SITE     2 AD2  5 GLU E  67                                                     
SITE     1 AD3  5 ASP E  20  ASP E  22  ASP E  24  THR E  26                    
SITE     2 AD3  5 GLU E  31                                                     
SITE     1 AD4  5 ASP G  56  ASP G  58  ASN G  60  THR G  62                    
SITE     2 AD4  5 GLU G  67                                                     
SITE     1 AD5  5 ASP G  93  ASP G  95  ASN G  97  TYR G  99                    
SITE     2 AD5  5 GLU G 104                                                     
SITE     1 AD6  5 ASP G 129  ASP G 131  ASP G 133  GLN G 135                    
SITE     2 AD6  5 GLU G 140                                                     
SITE     1 AD7  5 ASP G  20  ASP G  22  ASP G  24  THR G  26                    
SITE     2 AD7  5 GLU G  31                                                     
CRYST1   76.263   37.214  121.193  90.00 100.21  90.00 P 1 21 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      0.013113  0.000000  0.002361        0.00000                         
SCALE2      0.000000  0.026872  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008384        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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