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Database: PDB
Entry: 3HR4
LinkDB: 3HR4
Original site: 3HR4 
HEADER    OXIDOREDUCTASE/METAL BINDING PROTEIN    08-JUN-09   3HR4              
TITLE     HUMAN INOS REDUCTASE AND CALMODULIN COMPLEX                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NITRIC OXIDE SYNTHASE, INDUCIBLE;                          
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: RESIDUES 503-715;                                          
COMPND   5 SYNONYM: INDUCIBLE NO SYNTHASE, INDUCIBLE NOS, INOS, NOS TYPE II,    
COMPND   6 HEPATOCYTE NOS, HEP-NOS;                                             
COMPND   7 EC: 1.14.13.39;                                                      
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CALMODULIN;                                                
COMPND  11 CHAIN: B, D, F, H;                                                   
COMPND  12 SYNONYM: CAM;                                                        
COMPND  13 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: CALMODULIN, INDUCIBLE NITRIC OXIDE SYNTHASE, NOS2, NOS2A;      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI+;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,      
SOURCE  16 CAM3, CAMC, CAMIII;                                                  
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PKK-CAM                                   
KEYWDS    INDUCIBLE NITRIC OXIDE SYNTHASE, NOS, INOS, CALMODULIN, CALMODULIN-   
KEYWDS   2 BINDING, FAD, FMN, HEME, IRON, METAL-BINDING, NADP, OXIDOREDUCTASE,  
KEYWDS   3 PHOSPHOPROTEIN, ISOPEPTIDE BOND, METHYLATION, OXIDOREDUCTASE-METAL   
KEYWDS   4 BINDING PROTEIN COMPLEX                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.XIA,I.MISRA,T.IYANAKI,J.J.K.KIM                                     
REVDAT   2   05-SEP-12 3HR4    1       REMARK VERSN                             
REVDAT   1   08-SEP-09 3HR4    0                                                
JRNL        AUTH   C.XIA,I.MISRA,T.IYANAKI,J.J.K.KIM                            
JRNL        TITL   REGULATION OF INTERDOMAIN INTERACTIONS BY CAM IN INDUCIBLE   
JRNL        TITL 2 NITRIC OXIDE SYNTHASE                                        
JRNL        REF    J.BIOL.CHEM.                               2009              
JRNL        REFN                   ESSN 1083-351X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 428243.600                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 48283                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.309                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2414                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5888                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3820                       
REMARK   3   BIN FREE R VALUE                    : 0.4110                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 309                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10383                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 140                                     
REMARK   3   SOLVENT ATOMS            : 71                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.64000                                             
REMARK   3    B22 (A**2) : 12.86000                                             
REMARK   3    B33 (A**2) : -24.50000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.21000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.48                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 30.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.55                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.400 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.400 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.870 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.870 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 32.86                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : COFAC_FM                                       
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : COFAC_FM                                       
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3HR4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053480.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48283                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: 1TLL, 1NIW, 1FOT                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8K, SODIUM ACETATE, SODIUM           
REMARK 280  CHLORATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K   
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       80.42000            
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 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 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 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 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     HIS A   497                                                      
REMARK 465     HIS A   498                                                      
REMARK 465     HIS A   499                                                      
REMARK 465     HIS A   500                                                      
REMARK 465     HIS A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     ASP A   503                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     ARG A   506                                                      
REMARK 465     ARG A   507                                                      
REMARK 465     PRO A   508                                                      
REMARK 465     LYS A   509                                                      
REMARK 465     ARG A   510                                                      
REMARK 465     SER A   700                                                      
REMARK 465     ASN A   701                                                      
REMARK 465     VAL A   702                                                      
REMARK 465     THR A   703                                                      
REMARK 465     TRP A   704                                                      
REMARK 465     ASP A   705                                                      
REMARK 465     PRO A   706                                                      
REMARK 465     HIS A   707                                                      
REMARK 465     HIS A   708                                                      
REMARK 465     TYR A   709                                                      
REMARK 465     ARG A   710                                                      
REMARK 465     LEU A   711                                                      
REMARK 465     VAL A   712                                                      
REMARK 465     GLN A   713                                                      
REMARK 465     ASP A   714                                                      
REMARK 465     SER A   715                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     HIS C   497                                                      
REMARK 465     HIS C   498                                                      
REMARK 465     HIS C   499                                                      
REMARK 465     HIS C   500                                                      
REMARK 465     HIS C   501                                                      
REMARK 465     HIS C   502                                                      
REMARK 465     ASP C   503                                                      
REMARK 465     GLU C   504                                                      
REMARK 465     LYS C   505                                                      
REMARK 465     ARG C   506                                                      
REMARK 465     ARG C   507                                                      
REMARK 465     PRO C   508                                                      
REMARK 465     LYS C   509                                                      
REMARK 465     ARG C   510                                                      
REMARK 465     ARG C   511                                                      
REMARK 465     SER C   700                                                      
REMARK 465     ASN C   701                                                      
REMARK 465     VAL C   702                                                      
REMARK 465     THR C   703                                                      
REMARK 465     TRP C   704                                                      
REMARK 465     ASP C   705                                                      
REMARK 465     PRO C   706                                                      
REMARK 465     HIS C   707                                                      
REMARK 465     HIS C   708                                                      
REMARK 465     TYR C   709                                                      
REMARK 465     ARG C   710                                                      
REMARK 465     LEU C   711                                                      
REMARK 465     VAL C   712                                                      
REMARK 465     GLN C   713                                                      
REMARK 465     ASP C   714                                                      
REMARK 465     SER C   715                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LYS D   148                                                      
REMARK 465     HIS E   497                                                      
REMARK 465     HIS E   498                                                      
REMARK 465     HIS E   499                                                      
REMARK 465     HIS E   500                                                      
REMARK 465     HIS E   501                                                      
REMARK 465     HIS E   502                                                      
REMARK 465     ASP E   503                                                      
REMARK 465     GLU E   504                                                      
REMARK 465     LYS E   505                                                      
REMARK 465     ARG E   506                                                      
REMARK 465     ARG E   507                                                      
REMARK 465     PRO E   508                                                      
REMARK 465     LYS E   509                                                      
REMARK 465     ARG E   510                                                      
REMARK 465     SER E   700                                                      
REMARK 465     ASN E   701                                                      
REMARK 465     VAL E   702                                                      
REMARK 465     THR E   703                                                      
REMARK 465     TRP E   704                                                      
REMARK 465     ASP E   705                                                      
REMARK 465     PRO E   706                                                      
REMARK 465     HIS E   707                                                      
REMARK 465     HIS E   708                                                      
REMARK 465     TYR E   709                                                      
REMARK 465     ARG E   710                                                      
REMARK 465     LEU E   711                                                      
REMARK 465     VAL E   712                                                      
REMARK 465     GLN E   713                                                      
REMARK 465     ASP E   714                                                      
REMARK 465     SER E   715                                                      
REMARK 465     MET F     0                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     LYS F   148                                                      
REMARK 465     HIS G   497                                                      
REMARK 465     HIS G   498                                                      
REMARK 465     HIS G   499                                                      
REMARK 465     HIS G   500                                                      
REMARK 465     HIS G   501                                                      
REMARK 465     HIS G   502                                                      
REMARK 465     ASP G   503                                                      
REMARK 465     GLU G   504                                                      
REMARK 465     LYS G   505                                                      
REMARK 465     ARG G   506                                                      
REMARK 465     ARG G   507                                                      
REMARK 465     PRO G   508                                                      
REMARK 465     LYS G   509                                                      
REMARK 465     ARG G   510                                                      
REMARK 465     ARG G   511                                                      
REMARK 465     THR G   699                                                      
REMARK 465     SER G   700                                                      
REMARK 465     ASN G   701                                                      
REMARK 465     VAL G   702                                                      
REMARK 465     THR G   703                                                      
REMARK 465     TRP G   704                                                      
REMARK 465     ASP G   705                                                      
REMARK 465     PRO G   706                                                      
REMARK 465     HIS G   707                                                      
REMARK 465     HIS G   708                                                      
REMARK 465     TYR G   709                                                      
REMARK 465     ARG G   710                                                      
REMARK 465     LEU G   711                                                      
REMARK 465     VAL G   712                                                      
REMARK 465     GLN G   713                                                      
REMARK 465     ASP G   714                                                      
REMARK 465     SER G   715                                                      
REMARK 465     MET H     0                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     ASP H     2                                                      
REMARK 465     LYS H   148                                                      
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     ARG A 511    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 512    CG   CD   OE1  OE2                                  
REMARK 470     THR A 699    OG1  CG2                                            
REMARK 470     LEU C 612    CG   CD1  CD2                                       
REMARK 470     LYS C 613    CG   CD   CE   NZ                                   
REMARK 470     GLU C 614    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 615    CG   CD1  CD2                                       
REMARK 470     THR C 699    OG1  CG2                                            
REMARK 470     GLN D   3    CG   CD   OE1  NE2                                  
REMARK 470     LEU D   4    CG   CD1  CD2                                       
REMARK 470     ARG E 511    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 613    CG   CD   CE   NZ                                   
REMARK 470     GLU E 614    CG   CD   OE1  OE2                                  
REMARK 470     LEU E 615    CG   CD1  CD2                                       
REMARK 470     THR E 699    OG1  CG2                                            
REMARK 470     GLU G 512    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 613    CG   CD   CE   NZ                                   
REMARK 470     GLU G 614    CG   CD   OE1  OE2                                  
REMARK 470     ASN G 616    CG   OD1  ND2                                       
REMARK 470     GLU H 119    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE H 130    CG1  CG2  CD1                                       
REMARK 470     GLU H 139    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 142    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN H   137     N    GLU H   139              2.15            
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    LEU D   4   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    LYS G 613   N   -  CA  -  C   ANGL. DEV. =  22.3 DEGREES          
REMARK 500    GLU G 614   N   -  CA  -  CB  ANGL. DEV. = -18.3 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    GLU A 512      173.24    175.43                                   
REMARK 500    ALA A 564      -21.67   -156.55                                   
REMARK 500    ASN A 566       64.94   -113.36                                   
REMARK 500    LEU A 577      -34.80    -39.92                                   
REMARK 500    ASN A 601       20.92    -69.60                                   
REMARK 500    SER A 608      -72.63    -63.33                                   
REMARK 500    LEU A 609      -28.48    -38.86                                   
REMARK 500    PHE A 619     -171.95    -58.84                                   
REMARK 500    SER A 628      110.67   -160.15                                   
REMARK 500    SER A 629      -29.65    -39.30                                   
REMARK 500    GLU A 661      -32.29    -39.32                                   
REMARK 500    PHE A 669      -72.34    -48.29                                   
REMARK 500    ASP A 685       72.75     55.21                                   
REMARK 500    PRO A 695      174.55    -48.75                                   
REMARK 500    LEU B   4       93.03     82.91                                   
REMARK 500    GLU B   6      -35.85    -36.12                                   
REMARK 500    ASP B  56       87.77    -69.82                                   
REMARK 500    ASP B  93       84.51    -68.87                                   
REMARK 500    MET B 124       -6.89    -59.56                                   
REMARK 500    ARG B 126        2.33    -64.38                                   
REMARK 500    ALA B 128        7.95   -161.78                                   
REMARK 500    ASP B 131       34.32    -95.00                                   
REMARK 500    VAL C 517      -61.03    -91.62                                   
REMARK 500    GLU C 546      -69.85   -123.17                                   
REMARK 500    LYS C 549      -43.44   -145.92                                   
REMARK 500    ALA C 564      -24.56   -145.53                                   
REMARK 500    PHE C 565     -168.78   -121.87                                   
REMARK 500    LYS C 574       39.89    -71.89                                   
REMARK 500    ARG C 584      -28.55   -142.44                                   
REMARK 500    LYS C 607      -73.41    -53.66                                   
REMARK 500    LEU C 609      -99.92    -50.15                                   
REMARK 500    PHE C 610      -38.20    -28.66                                   
REMARK 500    LEU C 612      103.23    -46.53                                   
REMARK 500    GLU C 614       89.80     73.57                                   
REMARK 500    ASN C 616       97.85   -162.04                                   
REMARK 500    PHE C 619     -161.24    -79.97                                   
REMARK 500    SER C 629       22.18    -78.00                                   
REMARK 500    HIS C 647      -71.27    -56.20                                   
REMARK 500    LEU C 648       65.44    -60.32                                   
REMARK 500    ALA C 650      127.19    -27.22                                   
REMARK 500    SER C 663       28.32   -155.29                                   
REMARK 500    GLU C 682      -64.28    -90.46                                   
REMARK 500    THR C 683       15.77    -59.71                                   
REMARK 500    PHE C 684       -9.18   -140.70                                   
REMARK 500    ASP C 685       74.80     58.84                                   
REMARK 500    LYS C 689      -89.03    -21.64                                   
REMARK 500    GLN C 690      -23.32    -39.55                                   
REMARK 500    THR D   5      134.31    107.43                                   
REMARK 500    ASP D  56       76.26    -64.99                                   
REMARK 500    ALA D  73        5.32    -65.65                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     115 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  511     GLU A  512                  110.13                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS G 613        13.5      L          L   OUTSIDE RANGE           
REMARK 500    GLU G 614        51.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  20   OD1                                                    
REMARK 620 2 ASP B  22   OD1  78.6                                              
REMARK 620 3 ASP B  22   OD2 115.7  44.6                                        
REMARK 620 4 ASP B  24   OD2  76.4  67.8 100.4                                  
REMARK 620 5 THR B  26   O    89.6 137.6 150.6  69.8                            
REMARK 620 6 GLU B  31   OE1 133.8 133.8  89.3 139.6  82.6                      
REMARK 620 7 GLU B  31   OE2  98.7  97.9  69.2 165.5 124.2  52.7                
REMARK 620 8 HOH B 152   O   153.2  87.0  64.7  77.3  85.9  71.7 105.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  56   OD1                                                    
REMARK 620 2 ASP B  58   OD2  66.4                                              
REMARK 620 3 ASN B  60   OD1  74.9  72.4                                        
REMARK 620 4 THR B  62   O    64.7 130.8  89.8                                  
REMARK 620 5 GLU B  67   OE1  95.9 110.3 168.7  80.2                            
REMARK 620 6 GLU B  67   OE2  87.5  60.6 133.0 121.6  51.4                      
REMARK 620 7 ASP B  58   OD1 109.7  45.4  71.0 160.8 119.1  74.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD1                                                    
REMARK 620 2 ASP B  95   OD1  66.3                                              
REMARK 620 3 ASP B  95   OD2 105.9  46.4                                        
REMARK 620 4 ASN B  97   OD1  85.5  65.3  91.0                                  
REMARK 620 5 TYR B  99   O   108.5 140.3 141.5  75.1                            
REMARK 620 6 GLU B 104   OE1 117.9 143.6 103.2 146.9  75.3                      
REMARK 620 7 GLU B 104   OE2  96.2  91.7  63.6 154.1 127.7  52.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 129   OD2                                                    
REMARK 620 2 ASP B 131   OD1 100.2                                              
REMARK 620 3 ASP B 133   OD2  82.9  77.2                                        
REMARK 620 4 GLN B 135   O    71.1 152.2  75.5                                  
REMARK 620 5 GLU B 140   OE1  95.4  86.6 163.1 119.9                            
REMARK 620 6 GLU B 140   OE2  97.8 135.2 145.9  72.6  51.0                      
REMARK 620 7 ASP B 133   OD1 122.8  57.9  43.2 103.7 129.8 136.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  20   OD1                                                    
REMARK 620 2 ASP D  22   OD1  80.7                                              
REMARK 620 3 ASP D  24   OD2  88.9  79.6                                        
REMARK 620 4 THR D  26   O    94.8 151.5  72.1                                  
REMARK 620 5 GLU D  31   OE1 129.1 136.9 124.3  66.4                            
REMARK 620 6 GLU D  31   OE2 101.0  99.1 169.7 109.4  50.5                      
REMARK 620 7 HOH D 162   O   159.0  91.9  70.4  82.4  68.8  99.5                
REMARK 620 8 ASP D  22   OD2 117.2  45.3 105.9 148.0  91.7  67.2  67.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  56   OD1                                                    
REMARK 620 2 ASP D  58   OD1 119.7                                              
REMARK 620 3 ASP D  58   OD2  70.8  52.2                                        
REMARK 620 4 ASN D  60   OD1  82.8  94.6  70.8                                  
REMARK 620 5 THR D  62   O    66.2 173.2 131.5  82.5                            
REMARK 620 6 GLU D  67   OE1  87.1 105.6 122.0 159.7  77.4                      
REMARK 620 7 GLU D  67   OE2  90.0  65.4  81.0 151.7 119.4  45.1                
REMARK 620 8 HOH D 161   O   173.2  66.6 116.0  99.8 107.7  88.6  90.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  93   OD1                                                    
REMARK 620 2 ASP D  95   OD1  79.3                                              
REMARK 620 3 ASN D  97   OD1  87.1  90.1                                        
REMARK 620 4 TYR D  99   O    80.2 155.6  75.8                                  
REMARK 620 5 GLU D 104   OE1  94.0 116.4 153.2  78.0                            
REMARK 620 6 GLU D 104   OE2  93.0  68.8 158.5 125.5  48.3                      
REMARK 620 7 HOH D 163   O   157.2  78.0  93.9 122.1  95.2  77.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 129   OD2                                                    
REMARK 620 2 ASP D 131   OD1  75.0                                              
REMARK 620 3 ASP D 133   OD2  82.6  72.9                                        
REMARK 620 4 GLN D 135   O    89.0 147.5  77.2                                  
REMARK 620 5 GLU D 140   OE1  91.6  74.3 147.0 135.4                            
REMARK 620 6 GLU D 140   OE2 117.3 125.8 154.4  86.6  54.0                      
REMARK 620 7 HOH D 157   O   139.1  71.7  65.3 106.8 101.5 101.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  20   OD1                                                    
REMARK 620 2 ASP F  22   OD1  78.3                                              
REMARK 620 3 ASP F  24   OD2  71.8  77.4                                        
REMARK 620 4 THR F  26   O    65.6 143.3  84.8                                  
REMARK 620 5 GLU F  31   OE1 116.0 113.5 167.2  89.4                            
REMARK 620 6 GLU F  31   OE2 104.9  64.6 141.5 130.0  48.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  56   OD1                                                    
REMARK 620 2 ASP F  58   OD1 111.2                                              
REMARK 620 3 ASP F  58   OD2  67.4  47.4                                        
REMARK 620 4 ASN F  60   OD1  66.4  73.0  70.7                                  
REMARK 620 5 GLU F  67   OE1  90.6 149.8 135.3 136.6                            
REMARK 620 6 GLU F  67   OE2  87.8 101.1  82.2 148.0  57.6                      
REMARK 620 7 HOH F 158   O    95.1 105.4 126.3  56.0  92.6 150.1                
REMARK 620 8 THR F  62   O    49.0 138.9 112.6  66.0  71.2 111.8  53.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  93   OD1                                                    
REMARK 620 2 ASP F  95   OD2  72.9                                              
REMARK 620 3 ASN F  97   OD1  93.9  78.8                                        
REMARK 620 4 TYR F  99   O   108.5 160.7  81.9                                  
REMARK 620 5 GLU F 104   OE1 103.6 127.9 151.3  71.1                            
REMARK 620 6 GLU F 104   OE2  93.1  77.0 151.6 121.6  51.0                      
REMARK 620 7 HOH F 154   O   154.7  81.8  80.2  95.1  92.4  81.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 129   OD2                                                    
REMARK 620 2 ASP F 131   OD1  80.2                                              
REMARK 620 3 ASP F 133   OD2  90.5  81.5                                        
REMARK 620 4 GLN F 135   O    83.1 159.9  87.6                                  
REMARK 620 5 GLU F 140   OE1 109.2 102.2 160.3  93.8                            
REMARK 620 6 GLU F 140   OE2  76.2  62.4 142.9 123.9  48.3                      
REMARK 620 7 HOH F 152   O   162.8  89.7  74.1 103.5  86.4 111.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  20   OD1                                                    
REMARK 620 2 ASP H  22   OD1  63.9                                              
REMARK 620 3 ASP H  22   OD2 107.4  48.9                                        
REMARK 620 4 ASP H  24   OD2  75.1  60.9  92.2                                  
REMARK 620 5 THR H  26   O    85.5 139.9 166.6  87.6                            
REMARK 620 6 GLU H  31   OE1 128.3 127.3  83.2 156.4  91.7                      
REMARK 620 7 GLU H  31   OE2  85.3  81.4  62.9 142.1 123.4  54.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  56   OD1                                                    
REMARK 620 2 ASP H  58   OD2  68.1                                              
REMARK 620 3 THR H  62   O    62.5 129.8                                        
REMARK 620 4 GLU H  67   OE1  99.9 125.0  73.9                                  
REMARK 620 5 GLU H  67   OE2  86.3  69.6 114.5  55.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  93   OD2                                                    
REMARK 620 2 ASN H  97   OD1  65.0                                              
REMARK 620 3 TYR H  99   O    68.4  77.0                                        
REMARK 620 4 GLU H 104   OE1 122.9 153.4  83.0                                  
REMARK 620 5 GLU H 104   OE2 123.1 145.8 137.0  55.4                            
REMARK 620 6 ASP H  93   OD1  42.2  71.6 110.4 132.7  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 204  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 133   OD1                                                    
REMARK 620 2 ASP H 133   OD2  45.3                                              
REMARK 620 3 GLN H 135   O    64.3  61.1                                        
REMARK 620 4 GLU H 140   OE2 144.2 100.5  91.6                                  
REMARK 620 5 GLU H 140   OE1 129.9  92.0 124.2  43.0                            
REMARK 620 6 ASP H 131   OD2  84.4  82.4 142.5 104.1  61.2                      
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 FMN A 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN E 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN G 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 204                  
DBREF  3HR4 A  503   715  UNP    P35228   NOS2_HUMAN     503    715             
DBREF  3HR4 B    0   148  UNP    P62158   CALM_HUMAN       1    149             
DBREF  3HR4 C  503   715  UNP    P35228   NOS2_HUMAN     503    715             
DBREF  3HR4 D    0   148  UNP    P62158   CALM_HUMAN       1    149             
DBREF  3HR4 E  503   715  UNP    P35228   NOS2_HUMAN     503    715             
DBREF  3HR4 F    0   148  UNP    P62158   CALM_HUMAN       1    149             
DBREF  3HR4 G  503   715  UNP    P35228   NOS2_HUMAN     503    715             
DBREF  3HR4 H    0   148  UNP    P62158   CALM_HUMAN       1    149             
SEQADV 3HR4 HIS A  497  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS A  498  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS A  499  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS A  500  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS A  501  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS A  502  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS C  497  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS C  498  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS C  499  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS C  500  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS C  501  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS C  502  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS E  497  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS E  498  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS E  499  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS E  500  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS E  501  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS E  502  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS G  497  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS G  498  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS G  499  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS G  500  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS G  501  UNP  P35228              EXPRESSION TAG                 
SEQADV 3HR4 HIS G  502  UNP  P35228              EXPRESSION TAG                 
SEQRES   1 A  219  HIS HIS HIS HIS HIS HIS ASP GLU LYS ARG ARG PRO LYS          
SEQRES   2 A  219  ARG ARG GLU ILE PRO LEU LYS VAL LEU VAL LYS ALA VAL          
SEQRES   3 A  219  LEU PHE ALA CYS MET LEU MET ARG LYS THR MET ALA SER          
SEQRES   4 A  219  ARG VAL ARG VAL THR ILE LEU PHE ALA THR GLU THR GLY          
SEQRES   5 A  219  LYS SER GLU ALA LEU ALA TRP ASP LEU GLY ALA LEU PHE          
SEQRES   6 A  219  SER CYS ALA PHE ASN PRO LYS VAL VAL CYS MET ASP LYS          
SEQRES   7 A  219  TYR ARG LEU SER CYS LEU GLU GLU GLU ARG LEU LEU LEU          
SEQRES   8 A  219  VAL VAL THR SER THR PHE GLY ASN GLY ASP CYS PRO GLY          
SEQRES   9 A  219  ASN GLY GLU LYS LEU LYS LYS SER LEU PHE MET LEU LYS          
SEQRES  10 A  219  GLU LEU ASN ASN LYS PHE ARG TYR ALA VAL PHE GLY LEU          
SEQRES  11 A  219  GLY SER SER MET TYR PRO ARG PHE CYS ALA PHE ALA HIS          
SEQRES  12 A  219  ASP ILE ASP GLN LYS LEU SER HIS LEU GLY ALA SER GLN          
SEQRES  13 A  219  LEU THR PRO MET GLY GLU GLY ASP GLU LEU SER GLY GLN          
SEQRES  14 A  219  GLU ASP ALA PHE ARG SER TRP ALA VAL GLN THR PHE LYS          
SEQRES  15 A  219  ALA ALA CYS GLU THR PHE ASP VAL ARG GLY LYS GLN HIS          
SEQRES  16 A  219  ILE GLN ILE PRO LYS LEU TYR THR SER ASN VAL THR TRP          
SEQRES  17 A  219  ASP PRO HIS HIS TYR ARG LEU VAL GLN ASP SER                  
SEQRES   1 B  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 B  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 B  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 B  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 B  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 B  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 B  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 B  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 B  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 B  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 B  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 B  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 C  219  HIS HIS HIS HIS HIS HIS ASP GLU LYS ARG ARG PRO LYS          
SEQRES   2 C  219  ARG ARG GLU ILE PRO LEU LYS VAL LEU VAL LYS ALA VAL          
SEQRES   3 C  219  LEU PHE ALA CYS MET LEU MET ARG LYS THR MET ALA SER          
SEQRES   4 C  219  ARG VAL ARG VAL THR ILE LEU PHE ALA THR GLU THR GLY          
SEQRES   5 C  219  LYS SER GLU ALA LEU ALA TRP ASP LEU GLY ALA LEU PHE          
SEQRES   6 C  219  SER CYS ALA PHE ASN PRO LYS VAL VAL CYS MET ASP LYS          
SEQRES   7 C  219  TYR ARG LEU SER CYS LEU GLU GLU GLU ARG LEU LEU LEU          
SEQRES   8 C  219  VAL VAL THR SER THR PHE GLY ASN GLY ASP CYS PRO GLY          
SEQRES   9 C  219  ASN GLY GLU LYS LEU LYS LYS SER LEU PHE MET LEU LYS          
SEQRES  10 C  219  GLU LEU ASN ASN LYS PHE ARG TYR ALA VAL PHE GLY LEU          
SEQRES  11 C  219  GLY SER SER MET TYR PRO ARG PHE CYS ALA PHE ALA HIS          
SEQRES  12 C  219  ASP ILE ASP GLN LYS LEU SER HIS LEU GLY ALA SER GLN          
SEQRES  13 C  219  LEU THR PRO MET GLY GLU GLY ASP GLU LEU SER GLY GLN          
SEQRES  14 C  219  GLU ASP ALA PHE ARG SER TRP ALA VAL GLN THR PHE LYS          
SEQRES  15 C  219  ALA ALA CYS GLU THR PHE ASP VAL ARG GLY LYS GLN HIS          
SEQRES  16 C  219  ILE GLN ILE PRO LYS LEU TYR THR SER ASN VAL THR TRP          
SEQRES  17 C  219  ASP PRO HIS HIS TYR ARG LEU VAL GLN ASP SER                  
SEQRES   1 D  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 D  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 D  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 D  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 D  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 D  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 D  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 D  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 D  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 D  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 D  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 D  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 E  219  HIS HIS HIS HIS HIS HIS ASP GLU LYS ARG ARG PRO LYS          
SEQRES   2 E  219  ARG ARG GLU ILE PRO LEU LYS VAL LEU VAL LYS ALA VAL          
SEQRES   3 E  219  LEU PHE ALA CYS MET LEU MET ARG LYS THR MET ALA SER          
SEQRES   4 E  219  ARG VAL ARG VAL THR ILE LEU PHE ALA THR GLU THR GLY          
SEQRES   5 E  219  LYS SER GLU ALA LEU ALA TRP ASP LEU GLY ALA LEU PHE          
SEQRES   6 E  219  SER CYS ALA PHE ASN PRO LYS VAL VAL CYS MET ASP LYS          
SEQRES   7 E  219  TYR ARG LEU SER CYS LEU GLU GLU GLU ARG LEU LEU LEU          
SEQRES   8 E  219  VAL VAL THR SER THR PHE GLY ASN GLY ASP CYS PRO GLY          
SEQRES   9 E  219  ASN GLY GLU LYS LEU LYS LYS SER LEU PHE MET LEU LYS          
SEQRES  10 E  219  GLU LEU ASN ASN LYS PHE ARG TYR ALA VAL PHE GLY LEU          
SEQRES  11 E  219  GLY SER SER MET TYR PRO ARG PHE CYS ALA PHE ALA HIS          
SEQRES  12 E  219  ASP ILE ASP GLN LYS LEU SER HIS LEU GLY ALA SER GLN          
SEQRES  13 E  219  LEU THR PRO MET GLY GLU GLY ASP GLU LEU SER GLY GLN          
SEQRES  14 E  219  GLU ASP ALA PHE ARG SER TRP ALA VAL GLN THR PHE LYS          
SEQRES  15 E  219  ALA ALA CYS GLU THR PHE ASP VAL ARG GLY LYS GLN HIS          
SEQRES  16 E  219  ILE GLN ILE PRO LYS LEU TYR THR SER ASN VAL THR TRP          
SEQRES  17 E  219  ASP PRO HIS HIS TYR ARG LEU VAL GLN ASP SER                  
SEQRES   1 F  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 F  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 F  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 F  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 F  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 F  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 F  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 F  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 F  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 F  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 F  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 F  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 G  219  HIS HIS HIS HIS HIS HIS ASP GLU LYS ARG ARG PRO LYS          
SEQRES   2 G  219  ARG ARG GLU ILE PRO LEU LYS VAL LEU VAL LYS ALA VAL          
SEQRES   3 G  219  LEU PHE ALA CYS MET LEU MET ARG LYS THR MET ALA SER          
SEQRES   4 G  219  ARG VAL ARG VAL THR ILE LEU PHE ALA THR GLU THR GLY          
SEQRES   5 G  219  LYS SER GLU ALA LEU ALA TRP ASP LEU GLY ALA LEU PHE          
SEQRES   6 G  219  SER CYS ALA PHE ASN PRO LYS VAL VAL CYS MET ASP LYS          
SEQRES   7 G  219  TYR ARG LEU SER CYS LEU GLU GLU GLU ARG LEU LEU LEU          
SEQRES   8 G  219  VAL VAL THR SER THR PHE GLY ASN GLY ASP CYS PRO GLY          
SEQRES   9 G  219  ASN GLY GLU LYS LEU LYS LYS SER LEU PHE MET LEU LYS          
SEQRES  10 G  219  GLU LEU ASN ASN LYS PHE ARG TYR ALA VAL PHE GLY LEU          
SEQRES  11 G  219  GLY SER SER MET TYR PRO ARG PHE CYS ALA PHE ALA HIS          
SEQRES  12 G  219  ASP ILE ASP GLN LYS LEU SER HIS LEU GLY ALA SER GLN          
SEQRES  13 G  219  LEU THR PRO MET GLY GLU GLY ASP GLU LEU SER GLY GLN          
SEQRES  14 G  219  GLU ASP ALA PHE ARG SER TRP ALA VAL GLN THR PHE LYS          
SEQRES  15 G  219  ALA ALA CYS GLU THR PHE ASP VAL ARG GLY LYS GLN HIS          
SEQRES  16 G  219  ILE GLN ILE PRO LYS LEU TYR THR SER ASN VAL THR TRP          
SEQRES  17 G  219  ASP PRO HIS HIS TYR ARG LEU VAL GLN ASP SER                  
SEQRES   1 H  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 H  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 H  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 H  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 H  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 H  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 H  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 H  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 H  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 H  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 H  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 H  149  GLN MET MET THR ALA LYS                                      
HET    FMN  A 999      31                                                       
HET     CA  B 201       1                                                       
HET     CA  B 202       1                                                       
HET     CA  B 203       1                                                       
HET     CA  B 204       1                                                       
HET    FMN  C 999      31                                                       
HET     CA  D 201       1                                                       
HET     CA  D 202       1                                                       
HET     CA  D 203       1                                                       
HET     CA  D 204       1                                                       
HET    FMN  E 999      31                                                       
HET     CA  F 201       1                                                       
HET     CA  F 202       1                                                       
HET     CA  F 203       1                                                       
HET     CA  F 204       1                                                       
HET    FMN  G 999      31                                                       
HET     CA  H 201       1                                                       
HET     CA  H 202       1                                                       
HET     CA  H 203       1                                                       
HET     CA  H 204       1                                                       
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM      CA CALCIUM ION                                                      
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   9  FMN    4(C17 H21 N4 O9 P)                                           
FORMUL  10   CA    16(CA 2+)                                                    
FORMUL  29  HOH   *71(H2 O)                                                     
HELIX    1   1 PRO A  514  SER A  535  1                                  22    
HELIX    2   2 GLY A  548  SER A  562  1                                  15    
HELIX    3   3 ASP A  573  TYR A  575  5                                   3    
HELIX    4   4 ARG A  576  GLU A  582  5                                   7    
HELIX    5   5 PRO A  599  ASN A  601  5                                   3    
HELIX    6   6 GLY A  602  LEU A  612  1                                  11    
HELIX    7   7 CYS A  635  GLY A  649  1                                  15    
HELIX    8   8 GLY A  664  PHE A  684  1                                  21    
HELIX    9   9 GLY A  688  ILE A  692  5                                   5    
HELIX   10  10 THR B    5  ASP B   20  1                                  16    
HELIX   11  11 THR B   28  LEU B   39  1                                  12    
HELIX   12  12 THR B   44  ASP B   56  1                                  13    
HELIX   13  13 PHE B   65  LYS B   77  1                                  13    
HELIX   14  14 ASP B   80  ASP B   93  1                                  14    
HELIX   15  15 SER B  101  LEU B  112  1                                  12    
HELIX   16  16 THR B  117  GLU B  127  1                                  11    
HELIX   17  17 ASN B  137  THR B  146  1                                  10    
HELIX   18  18 PRO C  514  ARG C  536  1                                  23    
HELIX   19  19 GLU C  551  SER C  562  1                                  12    
HELIX   20  20 ARG C  576  GLU C  582  5                                   7    
HELIX   21  21 PRO C  599  LEU C  612  1                                  14    
HELIX   22  22 CYS C  635  LEU C  648  1                                  14    
HELIX   23  23 GLY C  664  THR C  683  1                                  20    
HELIX   24  24 GLY C  688  ILE C  692  5                                   5    
HELIX   25  25 THR D    5  ASP D   20  1                                  16    
HELIX   26  26 THR D   28  LEU D   39  1                                  12    
HELIX   27  27 THR D   44  ASP D   56  1                                  13    
HELIX   28  28 PHE D   65  MET D   76  1                                  12    
HELIX   29  29 ASP D   80  ASP D   93  1                                  14    
HELIX   30  30 SER D  101  LEU D  112  1                                  12    
HELIX   31  31 THR D  117  ARG D  126  1                                  10    
HELIX   32  32 TYR D  138  ALA D  147  1                                  10    
HELIX   33  33 PRO E  514  ALA E  534  1                                  21    
HELIX   34  34 GLY E  548  PHE E  561  1                                  14    
HELIX   35  35 SER E  562  ALA E  564  5                                   3    
HELIX   36  36 ASP E  573  TYR E  575  5                                   3    
HELIX   37  37 ARG E  576  GLU E  581  5                                   6    
HELIX   38  38 PRO E  599  ASN E  601  5                                   3    
HELIX   39  39 GLY E  602  PHE E  610  1                                   9    
HELIX   40  40 CYS E  635  LEU E  648  1                                  14    
HELIX   41  41 GLY E  664  LYS E  678  1                                  15    
HELIX   42  42 THR F    5  ASP F   20  1                                  16    
HELIX   43  43 THR F   28  LEU F   39  1                                  12    
HELIX   44  44 THR F   44  GLU F   54  1                                  11    
HELIX   45  45 PHE F   65  LYS F   77  1                                  13    
HELIX   46  46 SER F   81  ASP F   93  1                                  13    
HELIX   47  47 SER F  101  LEU F  112  1                                  12    
HELIX   48  48 THR F  117  ARG F  126  1                                  10    
HELIX   49  49 TYR F  138  THR F  146  1                                   9    
HELIX   50  50 PRO G  514  SER G  535  1                                  22    
HELIX   51  51 GLY G  548  SER G  562  1                                  15    
HELIX   52  52 ARG G  576  LEU G  580  5                                   5    
HELIX   53  53 GLU G  603  MET G  611  1                                   9    
HELIX   54  54 CYS G  635  GLY G  649  1                                  15    
HELIX   55  55 GLU G  661  THR G  683  1                                  23    
HELIX   56  56 THR H    5  ASP H   20  1                                  16    
HELIX   57  57 THR H   28  ARG H   37  1                                  10    
HELIX   58  58 SER H   38  GLY H   40  5                                   3    
HELIX   59  59 THR H   44  ASP H   56  1                                  13    
HELIX   60  60 ASP H   64  MET H   76  1                                  13    
HELIX   61  61 SER H   81  VAL H   91  1                                  11    
HELIX   62  62 SER H  101  LEU H  112  1                                  12    
HELIX   63  63 THR H  117  GLU H  127  1                                  11    
HELIX   64  64 TYR H  138  THR H  146  1                                   9    
SHEET    1   A 5 ASN A 566  CYS A 571  0                                        
SHEET    2   A 5 ARG A 538  ALA A 544  1  N  ILE A 541   O  VAL A 570           
SHEET    3   A 5 LEU A 585  SER A 591  1  O  LEU A 587   N  LEU A 542           
SHEET    4   A 5 ARG A 620  GLY A 627  1  O  PHE A 624   N  VAL A 588           
SHEET    5   A 5 SER A 651  GLN A 652  1  O  SER A 651   N  TYR A 621           
SHEET    1   B 5 ASN A 566  CYS A 571  0                                        
SHEET    2   B 5 ARG A 538  ALA A 544  1  N  ILE A 541   O  VAL A 570           
SHEET    3   B 5 LEU A 585  SER A 591  1  O  LEU A 587   N  LEU A 542           
SHEET    4   B 5 ARG A 620  GLY A 627  1  O  PHE A 624   N  VAL A 588           
SHEET    5   B 5 GLY A 657  ASP A 660  1  O  GLY A 659   N  GLY A 627           
SHEET    1   C 2 THR B  26  ILE B  27  0                                        
SHEET    2   C 2 ILE B  63  ASP B  64 -1  O  ILE B  63   N  ILE B  27           
SHEET    1   D 5 ASN C 566  CYS C 571  0                                        
SHEET    2   D 5 ARG C 538  ALA C 544  1  N  ILE C 541   O  VAL C 570           
SHEET    3   D 5 LEU C 585  SER C 591  1  O  VAL C 589   N  LEU C 542           
SHEET    4   D 5 ARG C 620  GLY C 627  1  O  ARG C 620   N  LEU C 586           
SHEET    5   D 5 SER C 651  ASP C 660  1  O  GLY C 659   N  GLY C 625           
SHEET    1   E 2 THR D  26  ILE D  27  0                                        
SHEET    2   E 2 ILE D  63  ASP D  64 -1  O  ILE D  63   N  ILE D  27           
SHEET    1   F 2 TYR D  99  ILE D 100  0                                        
SHEET    2   F 2 VAL D 136  ASN D 137 -1  O  VAL D 136   N  ILE D 100           
SHEET    1   G 5 LYS E 568  CYS E 571  0                                        
SHEET    2   G 5 THR E 540  PHE E 543  1  N  ILE E 541   O  VAL E 570           
SHEET    3   G 5 LEU E 585  SER E 591  1  O  LEU E 587   N  LEU E 542           
SHEET    4   G 5 ARG E 620  GLY E 627  1  O  LEU E 626   N  THR E 590           
SHEET    5   G 5 SER E 651  ASP E 660  1  O  GLY E 659   N  GLY E 625           
SHEET    1   H 2 THR F  26  ILE F  27  0                                        
SHEET    2   H 2 ILE F  63  ASP F  64 -1  O  ILE F  63   N  ILE F  27           
SHEET    1   I 2 TYR F  99  ILE F 100  0                                        
SHEET    2   I 2 VAL F 136  ASN F 137 -1  O  VAL F 136   N  ILE F 100           
SHEET    1   J 5 PHE G 565  ASN G 566  0                                        
SHEET    2   J 5 VAL G 537  ALA G 544  1  N  VAL G 537   O  ASN G 566           
SHEET    3   J 5 LEU G 585  SER G 591  1  O  LEU G 587   N  LEU G 542           
SHEET    4   J 5 ARG G 620  GLY G 627  1  O  PHE G 624   N  THR G 590           
SHEET    5   J 5 SER G 651  ASP G 660  1  O  GLY G 659   N  GLY G 625           
LINK         OD1 ASP B  20                CA    CA B 201     1555   1555  2.29  
LINK         OD1 ASP B  22                CA    CA B 201     1555   1555  2.81  
LINK         OD2 ASP B  22                CA    CA B 201     1555   1555  2.93  
LINK         OD2 ASP B  24                CA    CA B 201     1555   1555  2.50  
LINK         O   THR B  26                CA    CA B 201     1555   1555  2.53  
LINK         OE1 GLU B  31                CA    CA B 201     1555   1555  2.28  
LINK         OE2 GLU B  31                CA    CA B 201     1555   1555  2.62  
LINK         OD1 ASP B  56                CA    CA B 202     1555   1555  2.84  
LINK         OD2 ASP B  58                CA    CA B 202     1555   1555  2.30  
LINK         OD1 ASN B  60                CA    CA B 202     1555   1555  2.16  
LINK         O   THR B  62                CA    CA B 202     1555   1555  2.21  
LINK         OE1 GLU B  67                CA    CA B 202     1555   1555  2.58  
LINK         OE2 GLU B  67                CA    CA B 202     1555   1555  2.49  
LINK         OD1 ASP B  93                CA    CA B 203     1555   1555  2.19  
LINK         OD1 ASP B  95                CA    CA B 203     1555   1555  2.34  
LINK         OD2 ASP B  95                CA    CA B 203     1555   1555  2.99  
LINK         OD1 ASN B  97                CA    CA B 203     1555   1555  2.13  
LINK         O   TYR B  99                CA    CA B 203     1555   1555  2.23  
LINK         OE1 GLU B 104                CA    CA B 203     1555   1555  2.41  
LINK         OE2 GLU B 104                CA    CA B 203     1555   1555  2.56  
LINK         OD2 ASP B 129                CA    CA B 204     1555   1555  2.20  
LINK         OD1 ASP B 131                CA    CA B 204     1555   1555  2.79  
LINK         OD2 ASP B 133                CA    CA B 204     1555   1555  2.22  
LINK         O   GLN B 135                CA    CA B 204     1555   1555  2.48  
LINK         OE1 GLU B 140                CA    CA B 204     1555   1555  2.50  
LINK         OE2 GLU B 140                CA    CA B 204     1555   1555  2.59  
LINK         OD1 ASP D  20                CA    CA D 201     1555   1555  2.37  
LINK         OD1 ASP D  22                CA    CA D 201     1555   1555  2.65  
LINK         OD2 ASP D  24                CA    CA D 201     1555   1555  2.37  
LINK         O   THR D  26                CA    CA D 201     1555   1555  2.56  
LINK         OE1 GLU D  31                CA    CA D 201     1555   1555  2.77  
LINK         OE2 GLU D  31                CA    CA D 201     1555   1555  2.22  
LINK         OD1 ASP D  56                CA    CA D 202     1555   1555  2.39  
LINK         OD1 ASP D  58                CA    CA D 202     1555   1555  2.52  
LINK         OD2 ASP D  58                CA    CA D 202     1555   1555  2.47  
LINK         OD1 ASN D  60                CA    CA D 202     1555   1555  2.31  
LINK         O   THR D  62                CA    CA D 202     1555   1555  2.54  
LINK         OE1 GLU D  67                CA    CA D 202     1555   1555  2.68  
LINK         OE2 GLU D  67                CA    CA D 202     1555   1555  2.99  
LINK         OD1 ASP D  93                CA    CA D 203     1555   1555  2.19  
LINK         OD1 ASP D  95                CA    CA D 203     1555   1555  2.10  
LINK         OD1 ASN D  97                CA    CA D 203     1555   1555  2.77  
LINK         O   TYR D  99                CA    CA D 203     1555   1555  2.20  
LINK         OE1 GLU D 104                CA    CA D 203     1555   1555  2.56  
LINK         OE2 GLU D 104                CA    CA D 203     1555   1555  2.79  
LINK         OD2 ASP D 129                CA    CA D 204     1555   1555  2.28  
LINK         OD1 ASP D 131                CA    CA D 204     1555   1555  2.59  
LINK         OD2 ASP D 133                CA    CA D 204     1555   1555  2.40  
LINK         O   GLN D 135                CA    CA D 204     1555   1555  2.39  
LINK         OE1 GLU D 140                CA    CA D 204     1555   1555  2.39  
LINK         OE2 GLU D 140                CA    CA D 204     1555   1555  2.43  
LINK         OD1 ASP F  20                CA    CA F 201     1555   1555  2.54  
LINK         OD1 ASP F  22                CA    CA F 201     1555   1555  2.37  
LINK         OD2 ASP F  24                CA    CA F 201     1555   1555  2.52  
LINK         O   THR F  26                CA    CA F 201     1555   1555  2.19  
LINK         OE1 GLU F  31                CA    CA F 201     1555   1555  2.37  
LINK         OE2 GLU F  31                CA    CA F 201     1555   1555  2.84  
LINK         OD1 ASP F  56                CA    CA F 202     1555   1555  2.55  
LINK         OD1 ASP F  58                CA    CA F 202     1555   1555  2.93  
LINK         OD2 ASP F  58                CA    CA F 202     1555   1555  2.39  
LINK         OD1 ASN F  60                CA    CA F 202     1555   1555  2.70  
LINK         OE1 GLU F  67                CA    CA F 202     1555   1555  2.35  
LINK         OE2 GLU F  67                CA    CA F 202     1555   1555  2.21  
LINK         OD1 ASP F  93                CA    CA F 203     1555   1555  2.21  
LINK         OD2 ASP F  95                CA    CA F 203     1555   1555  2.44  
LINK         OD1 ASN F  97                CA    CA F 203     1555   1555  2.46  
LINK         O   TYR F  99                CA    CA F 203     1555   1555  2.29  
LINK         OE1 GLU F 104                CA    CA F 203     1555   1555  2.45  
LINK         OE2 GLU F 104                CA    CA F 203     1555   1555  2.67  
LINK         OD2 ASP F 129                CA    CA F 204     1555   1555  2.19  
LINK         OD1 ASP F 131                CA    CA F 204     1555   1555  2.37  
LINK         OD2 ASP F 133                CA    CA F 204     1555   1555  2.16  
LINK         O   GLN F 135                CA    CA F 204     1555   1555  2.28  
LINK         OE1 GLU F 140                CA    CA F 204     1555   1555  2.16  
LINK         OE2 GLU F 140                CA    CA F 204     1555   1555  2.89  
LINK         OD1 ASP H  20                CA    CA H 201     1555   1555  2.11  
LINK         OD1 ASP H  22                CA    CA H 201     1555   1555  2.40  
LINK         OD2 ASP H  22                CA    CA H 201     1555   1555  2.83  
LINK         OD2 ASP H  24                CA    CA H 201     1555   1555  2.40  
LINK         O   THR H  26                CA    CA H 201     1555   1555  2.04  
LINK         OE1 GLU H  31                CA    CA H 201     1555   1555  2.16  
LINK         OE2 GLU H  31                CA    CA H 201     1555   1555  2.59  
LINK         OD1 ASP H  56                CA    CA H 202     1555   1555  2.33  
LINK         OD2 ASP H  58                CA    CA H 202     1555   1555  2.46  
LINK         O   THR H  62                CA    CA H 202     1555   1555  2.83  
LINK         OE1 GLU H  67                CA    CA H 202     1555   1555  2.43  
LINK         OE2 GLU H  67                CA    CA H 202     1555   1555  2.27  
LINK         OD2 ASP H  93                CA    CA H 203     1555   1555  3.00  
LINK         OD1 ASN H  97                CA    CA H 203     1555   1555  2.43  
LINK         O   TYR H  99                CA    CA H 203     1555   1555  2.32  
LINK         OE1 GLU H 104                CA    CA H 203     1555   1555  2.30  
LINK         OE2 GLU H 104                CA    CA H 203     1555   1555  2.42  
LINK         OD1 ASP H 133                CA    CA H 204     1555   1555  2.92  
LINK         OD2 ASP H 133                CA    CA H 204     1555   1555  2.78  
LINK         O   GLN H 135                CA    CA H 204     1555   1555  2.14  
LINK         OE2 GLU H 140                CA    CA H 204     1555   1555  2.94  
LINK        CA    CA B 201                 O   HOH B 152     1555   1555  2.23  
LINK        CA    CA D 201                 O   HOH D 162     1555   1555  2.11  
LINK        CA    CA D 202                 O   HOH D 161     1555   1555  2.10  
LINK        CA    CA D 203                 O   HOH D 163     1555   1555  2.59  
LINK        CA    CA D 204                 O   HOH D 157     1555   1555  2.23  
LINK        CA    CA F 202                 O   HOH F 158     1555   1555  2.30  
LINK        CA    CA F 203                 O   HOH F 154     1555   1555  2.21  
LINK        CA    CA F 204                 O   HOH F 152     1555   1555  2.52  
LINK         OD2 ASP D  22                CA    CA D 201     1555   1555  3.01  
LINK         OE1 GLU H 140                CA    CA H 204     1555   1555  3.04  
LINK         OD1 ASP B  58                CA    CA B 202     1555   1555  3.07  
LINK         O   THR F  62                CA    CA F 202     1555   1555  3.07  
LINK         OD2 ASP H 131                CA    CA H 204     1555   1555  3.08  
LINK         OD1 ASP H  93                CA    CA H 203     1555   1555  3.11  
LINK         OD1 ASP B 133                CA    CA B 204     1555   1555  3.20  
SITE     1 AC1 22 THR A 545  GLU A 546  THR A 547  GLY A 548                    
SITE     2 AC1 22 LYS A 549  SER A 550  SER A 591  THR A 592                    
SITE     3 AC1 22 PHE A 593  GLY A 594  LEU A 626  GLY A 627                    
SITE     4 AC1 22 SER A 628  TYR A 631  ARG A 633  PHE A 634                    
SITE     5 AC1 22 CYS A 635  GLU A 661  GLN A 665  ASN C 595                    
SITE     6 AC1 22 GLY C 596  ASP C 597                                          
SITE     1 AC2  6 ASP B  20  ASP B  22  ASP B  24  THR B  26                    
SITE     2 AC2  6 GLU B  31  HOH B 152                                          
SITE     1 AC3  5 ASP B  56  ASP B  58  ASN B  60  THR B  62                    
SITE     2 AC3  5 GLU B  67                                                     
SITE     1 AC4  5 ASP B  93  ASP B  95  ASN B  97  TYR B  99                    
SITE     2 AC4  5 GLU B 104                                                     
SITE     1 AC5  5 ASP B 129  ASP B 131  ASP B 133  GLN B 135                    
SITE     2 AC5  5 GLU B 140                                                     
SITE     1 AC6 20 THR C 545  GLU C 546  THR C 547  LYS C 549                    
SITE     2 AC6 20 SER C 550  SER C 591  THR C 592  PHE C 593                    
SITE     3 AC6 20 GLY C 594  ASN C 595  GLY C 596  LEU C 626                    
SITE     4 AC6 20 GLY C 627  SER C 628  TYR C 631  ARG C 633                    
SITE     5 AC6 20 PHE C 634  CYS C 635  GLU C 661  GLN C 665                    
SITE     1 AC7  6 ASP D  20  ASP D  22  ASP D  24  THR D  26                    
SITE     2 AC7  6 GLU D  31  HOH D 162                                          
SITE     1 AC8  6 ASP D  56  ASP D  58  ASN D  60  THR D  62                    
SITE     2 AC8  6 GLU D  67  HOH D 161                                          
SITE     1 AC9  6 ASP D  93  ASP D  95  ASN D  97  TYR D  99                    
SITE     2 AC9  6 GLU D 104  HOH D 163                                          
SITE     1 BC1  6 ASP D 129  ASP D 131  ASP D 133  GLN D 135                    
SITE     2 BC1  6 GLU D 140  HOH D 157                                          
SITE     1 BC2 22 THR E 545  GLU E 546  THR E 547  GLY E 548                    
SITE     2 BC2 22 LYS E 549  SER E 550  SER E 591  THR E 592                    
SITE     3 BC2 22 PHE E 593  GLY E 594  LEU E 626  GLY E 627                    
SITE     4 BC2 22 SER E 628  TYR E 631  ARG E 633  PHE E 634                    
SITE     5 BC2 22 CYS E 635  GLU E 661  GLN E 665  ASN G 595                    
SITE     6 BC2 22 GLY G 596  ASP G 597                                          
SITE     1 BC3  5 ASP F  20  ASP F  22  ASP F  24  THR F  26                    
SITE     2 BC3  5 GLU F  31                                                     
SITE     1 BC4  7 ASP F  56  ASP F  58  ASN F  60  THR F  62                    
SITE     2 BC4  7 ASP F  64  GLU F  67  HOH F 158                               
SITE     1 BC5  6 ASP F  93  ASP F  95  ASN F  97  TYR F  99                    
SITE     2 BC5  6 GLU F 104  HOH F 154                                          
SITE     1 BC6  6 ASP F 129  ASP F 131  ASP F 133  GLN F 135                    
SITE     2 BC6  6 GLU F 140  HOH F 152                                          
SITE     1 BC7 20 THR G 545  GLU G 546  THR G 547  GLY G 548                    
SITE     2 BC7 20 LYS G 549  SER G 550  SER G 591  THR G 592                    
SITE     3 BC7 20 PHE G 593  GLY G 594  GLY G 596  LEU G 626                    
SITE     4 BC7 20 GLY G 627  SER G 628  TYR G 631  ARG G 633                    
SITE     5 BC7 20 PHE G 634  CYS G 635  GLU G 661  GLN G 665                    
SITE     1 BC8  5 ASP H  20  ASP H  22  ASP H  24  THR H  26                    
SITE     2 BC8  5 GLU H  31                                                     
SITE     1 BC9  6 ASP H  56  ASP H  58  ASN H  60  THR H  62                    
SITE     2 BC9  6 ASP H  64  GLU H  67                                          
SITE     1 CC1  5 ASP H  93  ASP H  95  ASN H  97  TYR H  99                    
SITE     2 CC1  5 GLU H 104                                                     
SITE     1 CC2  6 ASP H 129  ASP H 131  ASP H 133  GLN H 135                    
SITE     2 CC2  6 ASN H 137  GLU H 140                                          
CRYST1   36.600  160.840  127.770  90.00  90.37  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      0.027322  0.000000  0.000176        0.00000                         
SCALE2      0.000000  0.006217  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007827        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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