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Database: PDB
Entry: 4IQR
LinkDB: 4IQR
Original site: 4IQR 
HEADER    TRANSCRIPTION/DNA                       13-JAN-13   4IQR              
TITLE     MULTI-DOMAIN ORGANIZATION OF THE HNF4ALPHA NUCLEAR RECEPTOR COMPLEX ON
TITLE    2 DNA                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 4-ALPHA;                         
COMPND   3 CHAIN: A, B, E, F;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 55-377;                                       
COMPND   5 SYNONYM: HNF-4-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 2 GROUP A MEMBER 1, 
COMPND   6 TRANSCRIPTION FACTOR 14, TCF-14, TRANSCRIPTION FACTOR HNF-4;         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA (5'-                                                   
COMPND  10 D(*GP*GP*AP*AP*CP*TP*AP*GP*GP*TP*CP*AP*AP*AP*GP*GP*TP*CP*AP*G)-3');  
COMPND  11 CHAIN: C, G;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA (5'-                                                   
COMPND  15 D(*CP*CP*TP*GP*AP*CP*CP*TP*TP*TP*GP*AP*CP*CP*TP*AP*GP*TP*TP*C)-3');  
COMPND  16 CHAIN: D, H;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: NUCLEAR RECEPTOR COACTIVATOR 2;                            
COMPND  20 CHAIN: I, J, K, L;                                                   
COMPND  21 FRAGMENT: LXXLL MOTIF PEPTIDE (UNP RESIDUES 685-697);                
COMPND  22 SYNONYM: NCOA-2, CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 75, BHLHE75, 
COMPND  23 TRANSCRIPTIONAL INTERMEDIARY FACTOR 2, HTIF2;                        
COMPND  24 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: HNF4A, HNF4, NR2A1, TCF14;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 MOL_ID: 3;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 MOL_ID: 4;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSCRIPTION FACTOR, TRANSCRIPTION-DNA COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.CHANDRA,P.HUANG,Y.KIM,F.RASTINEJAD                                  
REVDAT   2   23-OCT-13 4IQR    1       JRNL                                     
REVDAT   1   20-MAR-13 4IQR    0                                                
JRNL        AUTH   V.CHANDRA,P.HUANG,N.POTLURI,D.WU,Y.KIM,F.RASTINEJAD          
JRNL        TITL   MULTIDOMAIN INTEGRATION IN THE STRUCTURE OF THE HNF-4 ALPHA  
JRNL        TITL 2 NUCLEAR RECEPTOR COMPLEX.                                    
JRNL        REF    NATURE                        V. 495   394 2013              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   23485969                                                     
JRNL        DOI    10.1038/NATURE11966                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.3                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 50589                          
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) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2559                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3540                       
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 435                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10083                                   
REMARK   3   NUCLEIC ACID ATOMS       : 1628                                    
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 87.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.75000                                             
REMARK   3    B22 (A**2) : -5.22000                                             
REMARK   3    B33 (A**2) : -5.53000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -19.39000                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.58                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.51                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.63                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.004                           
REMARK   3   BOND ANGLES            (DEGREES) : 0.90                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4IQR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077090.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK HIGH-RESOLUTION     
REMARK 200                                   DOUBLE-CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50948                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.68800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRIES 3FS1 AND 3CBB                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 25MM NH4CL, 25MM MGCL2 AND     
REMARK 280  PEG 3350 , PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K  
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       28.79800            
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                                                    
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 35780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, J, I                      
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12150 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H, L, K                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     HIS A    37                                                      
REMARK 465     HIS A    38                                                      
REMARK 465     VAL A    39                                                      
REMARK 465     ASP A    40                                                      
REMARK 465     ASP A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     ASP A    43                                                      
REMARK 465     LYS A    44                                                      
REMARK 465     MET A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     VAL A    47                                                      
REMARK 465     SER A    48                                                      
REMARK 465     ARG A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     ARG A   127                                                      
REMARK 465     ILE A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     THR A   130                                                      
REMARK 465     ARG A   131                                                      
REMARK 465     ARG A   132                                                      
REMARK 465     SER A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     TYR A   135                                                      
REMARK 465     GLU A   136                                                      
REMARK 465     ASP A   137                                                      
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     LEU A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     MET B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     HIS B    35                                                      
REMARK 465     HIS B    36                                                      
REMARK 465     HIS B    37                                                      
REMARK 465     HIS B    38                                                      
REMARK 465     VAL B    39                                                      
REMARK 465     ASP B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     LYS B    44                                                      
REMARK 465     MET B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     VAL B    47                                                      
REMARK 465     SER B    48                                                      
REMARK 465     ARG B   154                                                      
REMARK 465     GLN B   155                                                      
REMARK 465     ILE B   156                                                      
REMARK 465     THR B   157                                                      
REMARK 465     SER B   158                                                      
REMARK 465     PRO B   159                                                      
REMARK 465     VAL B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     ILE B   163                                                      
REMARK 465     ASN B   164                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     MET E    31                                                      
REMARK 465     ALA E    32                                                      
REMARK 465     HIS E    33                                                      
REMARK 465     HIS E    34                                                      
REMARK 465     HIS E    35                                                      
REMARK 465     HIS E    36                                                      
REMARK 465     HIS E    37                                                      
REMARK 465     HIS E    38                                                      
REMARK 465     VAL E    39                                                      
REMARK 465     ASP E    40                                                      
REMARK 465     ASP E    41                                                      
REMARK 465     ASP E    42                                                      
REMARK 465     ASP E    43                                                      
REMARK 465     LYS E    44                                                      
REMARK 465     MET E    45                                                      
REMARK 465     GLY E    46                                                      
REMARK 465     VAL E    47                                                      
REMARK 465     SER E    48                                                      
REMARK 465     GLU E   124                                                      
REMARK 465     ARG E   125                                                      
REMARK 465     ASP E   126                                                      
REMARK 465     ARG E   127                                                      
REMARK 465     ILE E   128                                                      
REMARK 465     SER E   129                                                      
REMARK 465     THR E   130                                                      
REMARK 465     ARG E   131                                                      
REMARK 465     ARG E   132                                                      
REMARK 465     SER E   133                                                      
REMARK 465     SER E   134                                                      
REMARK 465     TYR E   135                                                      
REMARK 465     GLU E   136                                                      
REMARK 465     ASP E   137                                                      
REMARK 465     SER E   138                                                      
REMARK 465     SER E   139                                                      
REMARK 465     LEU E   140                                                      
REMARK 465     MET F    31                                                      
REMARK 465     ALA F    32                                                      
REMARK 465     HIS F    33                                                      
REMARK 465     HIS F    34                                                      
REMARK 465     HIS F    35                                                      
REMARK 465     HIS F    36                                                      
REMARK 465     HIS F    37                                                      
REMARK 465     HIS F    38                                                      
REMARK 465     VAL F    39                                                      
REMARK 465     ASP F    40                                                      
REMARK 465     ASP F    41                                                      
REMARK 465     ASP F    42                                                      
REMARK 465     ASP F    43                                                      
REMARK 465     LYS F    44                                                      
REMARK 465     MET F    45                                                      
REMARK 465     GLY F    46                                                      
REMARK 465     VAL F    47                                                      
REMARK 465     SER F    48                                                      
REMARK 465     GLN F   155                                                      
REMARK 465     ILE F   156                                                      
REMARK 465     THR F   157                                                      
REMARK 465     SER F   158                                                      
REMARK 465     PRO F   159                                                      
REMARK 465     VAL F   160                                                      
REMARK 465     GLU I   685                                                      
REMARK 465     LYS I   686                                                      
REMARK 465     HIS I   687                                                      
REMARK 465     ASP I   696                                                      
REMARK 465     SER I   697                                                      
REMARK 465     GLU J   685                                                      
REMARK 465     LYS J   686                                                      
REMARK 465     SER J   697                                                      
REMARK 465     GLU K   685                                                      
REMARK 465     LYS K   686                                                      
REMARK 465     HIS K   687                                                      
REMARK 465     ASP K   696                                                      
REMARK 465     SER K   697                                                      
REMARK 465     GLU L   685                                                      
REMARK 465     LYS L   686                                                      
REMARK 465     HIS L   687                                                      
REMARK 465     ASP L   696                                                      
REMARK 465     SER L   697                                                      
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    ILE A  53      -72.62    -95.21                                   
REMARK 500    TYR A  63       12.16     54.71                                   
REMARK 500    PHE A  89     -139.24   -142.40                                   
REMARK 500    LYS A  99       66.08   -103.89                                   
REMARK 500    ASN A 123       64.99    166.18                                   
REMARK 500    ASN A 144       41.42   -105.84                                   
REMARK 500    VAL A 151       22.36    -79.37                                   
REMARK 500    LEU A 152      -38.45   -138.19                                   
REMARK 500    THR A 157     -151.41    -80.63                                   
REMARK 500    PRO A 159       90.97    -53.67                                   
REMARK 500    ASP A 239      -24.92     69.30                                   
REMARK 500    ALA A 250      -91.31     55.60                                   
REMARK 500    LEU A 263      -57.88   -123.25                                   
REMARK 500    ALA A 355      144.58   -176.04                                   
REMARK 500    ILE B  53      -48.37   -141.75                                   
REMARK 500    ARG B  57      102.50    -43.49                                   
REMARK 500    SER B  66      105.81    -53.23                                   
REMARK 500    PHE B  89     -134.52   -135.86                                   
REMARK 500    LYS B  99       -6.72   -167.36                                   
REMARK 500    ARG B 125     -153.18   -118.18                                   
REMARK 500    ASP B 126     -154.28    -77.36                                   
REMARK 500    ARG B 127      -64.34   -107.59                                   
REMARK 500    THR B 130       26.43     45.24                                   
REMARK 500    TYR B 135      170.06     58.52                                   
REMARK 500    GLU B 136      148.97     69.19                                   
REMARK 500    ASP B 137       30.78   -156.23                                   
REMARK 500    SER B 142      -87.93    -82.59                                   
REMARK 500    ILE B 143      -88.85     35.90                                   
REMARK 500    LEU B 146       40.34   -107.72                                   
REMARK 500    LEU B 147      -47.12   -153.69                                   
REMARK 500    ALA B 250     -128.97     53.19                                   
REMARK 500    LEU B 263      -57.56   -125.66                                   
REMARK 500    ARG B 317       68.49   -102.40                                   
REMARK 500    ASP B 320       11.89   -165.51                                   
REMARK 500    ALA B 355      118.55   -171.86                                   
REMARK 500    LYS B 356      105.67    -55.36                                   
REMARK 500    ALA E  52       12.91    -67.93                                   
REMARK 500    ILE E  53      -65.65   -128.42                                   
REMARK 500    ASP E  56     -175.17    -67.47                                   
REMARK 500    PHE E  89     -119.28   -114.33                                   
REMARK 500    ALA E 213      -70.76    -37.95                                   
REMARK 500    ASP E 239        0.60     59.15                                   
REMARK 500    PRO E 247       -2.97    -59.93                                   
REMARK 500    ALA E 250     -119.96     51.17                                   
REMARK 500    LEU E 263      -59.18   -122.62                                   
REMARK 500    ASP E 316       35.54    -82.15                                   
REMARK 500    LEU E 330        0.83    -67.32                                   
REMARK 500    PHE E 352      -58.71   -123.87                                   
REMARK 500    ALA F  52       32.77    -70.94                                   
REMARK 500    ILE F  53      -44.64   -144.11                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      79 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DG C3008         0.05    SIDE CHAIN                              
REMARK 500     DA G3014         0.05    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  54   SG                                                     
REMARK 620 2 CYS A  71   SG  112.9                                              
REMARK 620 3 CYS A  68   SG  102.1  90.5                                        
REMARK 620 4 CYS A  51   SG  113.7 116.0 118.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E  54   SG                                                     
REMARK 620 2 CYS E  71   SG  123.0                                              
REMARK 620 3 CYS E  51   SG  108.7 113.7                                        
REMARK 620 4 CYS E  68   SG  105.5  95.4 108.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E  93   SG                                                     
REMARK 620 2 CYS E 106   SG  109.9                                              
REMARK 620 3 CYS E  87   SG  101.4 122.1                                        
REMARK 620 4 CYS E 103   SG  113.0 109.9 100.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  87   SG                                                     
REMARK 620 2 CYS F  93   SG  109.9                                              
REMARK 620 3 CYS F 106   SG  117.4  91.4                                        
REMARK 620 4 CYS F 103   SG  115.7 104.7 113.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  87   SG                                                     
REMARK 620 2 CYS B  93   SG  107.0                                              
REMARK 620 3 CYS B 106   SG  104.3 107.4                                        
REMARK 620 4 CYS B 103   SG  106.2 120.3 110.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 103   SG                                                     
REMARK 620 2 CYS A  93   SG  100.3                                              
REMARK 620 3 CYS A  87   SG  122.8 100.9                                        
REMARK 620 4 CYS A 106   SG  108.3  94.4 122.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  54   SG                                                     
REMARK 620 2 CYS B  71   SG   97.2                                              
REMARK 620 3 CYS B  51   SG   97.6 111.1                                        
REMARK 620 4 CYS B  68   SG  107.8 120.4 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  54   SG                                                     
REMARK 620 2 CYS F  71   SG  122.0                                              
REMARK 620 3 CYS F  51   SG  106.5  98.6                                        
REMARK 620 4 CYS F  68   SG  104.1 116.8 107.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 403                  
DBREF  4IQR A   46   368  UNP    P41235   HNF4A_HUMAN     55    377             
DBREF  4IQR B   46   368  UNP    P41235   HNF4A_HUMAN     55    377             
DBREF  4IQR E   46   368  UNP    P41235   HNF4A_HUMAN     55    377             
DBREF  4IQR F   46   368  UNP    P41235   HNF4A_HUMAN     55    377             
DBREF  4IQR I  685   697  UNP    Q15596   NCOA2_HUMAN    685    697             
DBREF  4IQR J  685   697  UNP    Q15596   NCOA2_HUMAN    685    697             
DBREF  4IQR K  685   697  UNP    Q15596   NCOA2_HUMAN    685    697             
DBREF  4IQR L  685   697  UNP    Q15596   NCOA2_HUMAN    685    697             
DBREF  4IQR C 3001  3020  PDB    4IQR     4IQR          3001   3020             
DBREF  4IQR G 3001  3020  PDB    4IQR     4IQR          3001   3020             
DBREF  4IQR D 4000  4019  PDB    4IQR     4IQR          4000   4019             
DBREF  4IQR H 4000  4019  PDB    4IQR     4IQR          4000   4019             
SEQADV 4IQR MET A   31  UNP  P41235              INITIATING METHIONINE          
SEQADV 4IQR ALA A   32  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS A   33  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS A   34  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS A   35  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS A   36  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS A   37  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS A   38  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR VAL A   39  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP A   40  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP A   41  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP A   42  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP A   43  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR LYS A   44  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR MET A   45  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR MET B   31  UNP  P41235              INITIATING METHIONINE          
SEQADV 4IQR ALA B   32  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS B   33  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS B   34  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS B   35  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS B   36  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS B   37  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS B   38  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR VAL B   39  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP B   40  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP B   41  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP B   42  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP B   43  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR LYS B   44  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR MET B   45  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR MET E   31  UNP  P41235              INITIATING METHIONINE          
SEQADV 4IQR ALA E   32  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS E   33  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS E   34  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS E   35  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS E   36  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS E   37  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS E   38  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR VAL E   39  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP E   40  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP E   41  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP E   42  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP E   43  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR LYS E   44  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR MET E   45  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR MET F   31  UNP  P41235              INITIATING METHIONINE          
SEQADV 4IQR ALA F   32  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS F   33  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS F   34  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS F   35  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS F   36  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS F   37  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR HIS F   38  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR VAL F   39  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP F   40  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP F   41  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP F   42  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR ASP F   43  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR LYS F   44  UNP  P41235              EXPRESSION TAG                 
SEQADV 4IQR MET F   45  UNP  P41235              EXPRESSION TAG                 
SEQRES   1 A  338  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 A  338  LYS MET GLY VAL SER ALA LEU CYS ALA ILE CYS GLY ASP          
SEQRES   3 A  338  ARG ALA THR GLY LYS HIS TYR GLY ALA SER SER CYS ASP          
SEQRES   4 A  338  GLY CYS LYS GLY PHE PHE ARG ARG SER VAL ARG LYS ASN          
SEQRES   5 A  338  HIS MET TYR SER CYS ARG PHE SER ARG GLN CYS VAL VAL          
SEQRES   6 A  338  ASP LYS ASP LYS ARG ASN GLN CYS ARG TYR CYS ARG LEU          
SEQRES   7 A  338  LYS LYS CYS PHE ARG ALA GLY MET LYS LYS GLU ALA VAL          
SEQRES   8 A  338  GLN ASN GLU ARG ASP ARG ILE SER THR ARG ARG SER SER          
SEQRES   9 A  338  TYR GLU ASP SER SER LEU PRO SER ILE ASN ALA LEU LEU          
SEQRES  10 A  338  GLN ALA GLU VAL LEU SER ARG GLN ILE THR SER PRO VAL          
SEQRES  11 A  338  SER GLY ILE ASN GLY ASP ILE ARG ALA LYS LYS ILE ALA          
SEQRES  12 A  338  SER ILE ALA ASP VAL CYS GLU SER MET LYS GLU GLN LEU          
SEQRES  13 A  338  LEU VAL LEU VAL GLU TRP ALA LYS TYR ILE PRO ALA PHE          
SEQRES  14 A  338  CYS GLU LEU PRO LEU ASP ASP GLN VAL ALA LEU LEU ARG          
SEQRES  15 A  338  ALA HIS ALA GLY GLU HIS LEU LEU LEU GLY ALA THR LYS          
SEQRES  16 A  338  ARG SER MET VAL PHE LYS ASP VAL LEU LEU LEU GLY ASN          
SEQRES  17 A  338  ASP TYR ILE VAL PRO ARG HIS CYS PRO GLU LEU ALA GLU          
SEQRES  18 A  338  MET SER ARG VAL SER ILE ARG ILE LEU ASP GLU LEU VAL          
SEQRES  19 A  338  LEU PRO PHE GLN GLU LEU GLN ILE ASP ASP ASN GLU TYR          
SEQRES  20 A  338  ALA TYR LEU LYS ALA ILE ILE PHE PHE ASP PRO ASP ALA          
SEQRES  21 A  338  LYS GLY LEU SER ASP PRO GLY LYS ILE LYS ARG LEU ARG          
SEQRES  22 A  338  SER GLN VAL GLN VAL SER LEU GLU ASP TYR ILE ASN ASP          
SEQRES  23 A  338  ARG GLN TYR ASP SER ARG GLY ARG PHE GLY GLU LEU LEU          
SEQRES  24 A  338  LEU LEU LEU PRO THR LEU GLN SER ILE THR TRP GLN MET          
SEQRES  25 A  338  ILE GLU GLN ILE GLN PHE ILE LYS LEU PHE GLY MET ALA          
SEQRES  26 A  338  LYS ILE ASP ASN LEU LEU GLN GLU MET LEU LEU GLY GLY          
SEQRES   1 B  338  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 B  338  LYS MET GLY VAL SER ALA LEU CYS ALA ILE CYS GLY ASP          
SEQRES   3 B  338  ARG ALA THR GLY LYS HIS TYR GLY ALA SER SER CYS ASP          
SEQRES   4 B  338  GLY CYS LYS GLY PHE PHE ARG ARG SER VAL ARG LYS ASN          
SEQRES   5 B  338  HIS MET TYR SER CYS ARG PHE SER ARG GLN CYS VAL VAL          
SEQRES   6 B  338  ASP LYS ASP LYS ARG ASN GLN CYS ARG TYR CYS ARG LEU          
SEQRES   7 B  338  LYS LYS CYS PHE ARG ALA GLY MET LYS LYS GLU ALA VAL          
SEQRES   8 B  338  GLN ASN GLU ARG ASP ARG ILE SER THR ARG ARG SER SER          
SEQRES   9 B  338  TYR GLU ASP SER SER LEU PRO SER ILE ASN ALA LEU LEU          
SEQRES  10 B  338  GLN ALA GLU VAL LEU SER ARG GLN ILE THR SER PRO VAL          
SEQRES  11 B  338  SER GLY ILE ASN GLY ASP ILE ARG ALA LYS LYS ILE ALA          
SEQRES  12 B  338  SER ILE ALA ASP VAL CYS GLU SER MET LYS GLU GLN LEU          
SEQRES  13 B  338  LEU VAL LEU VAL GLU TRP ALA LYS TYR ILE PRO ALA PHE          
SEQRES  14 B  338  CYS GLU LEU PRO LEU ASP ASP GLN VAL ALA LEU LEU ARG          
SEQRES  15 B  338  ALA HIS ALA GLY GLU HIS LEU LEU LEU GLY ALA THR LYS          
SEQRES  16 B  338  ARG SER MET VAL PHE LYS ASP VAL LEU LEU LEU GLY ASN          
SEQRES  17 B  338  ASP TYR ILE VAL PRO ARG HIS CYS PRO GLU LEU ALA GLU          
SEQRES  18 B  338  MET SER ARG VAL SER ILE ARG ILE LEU ASP GLU LEU VAL          
SEQRES  19 B  338  LEU PRO PHE GLN GLU LEU GLN ILE ASP ASP ASN GLU TYR          
SEQRES  20 B  338  ALA TYR LEU LYS ALA ILE ILE PHE PHE ASP PRO ASP ALA          
SEQRES  21 B  338  LYS GLY LEU SER ASP PRO GLY LYS ILE LYS ARG LEU ARG          
SEQRES  22 B  338  SER GLN VAL GLN VAL SER LEU GLU ASP TYR ILE ASN ASP          
SEQRES  23 B  338  ARG GLN TYR ASP SER ARG GLY ARG PHE GLY GLU LEU LEU          
SEQRES  24 B  338  LEU LEU LEU PRO THR LEU GLN SER ILE THR TRP GLN MET          
SEQRES  25 B  338  ILE GLU GLN ILE GLN PHE ILE LYS LEU PHE GLY MET ALA          
SEQRES  26 B  338  LYS ILE ASP ASN LEU LEU GLN GLU MET LEU LEU GLY GLY          
SEQRES   1 C   20   DG  DG  DA  DA  DC  DT  DA  DG  DG  DT  DC  DA  DA          
SEQRES   2 C   20   DA  DG  DG  DT  DC  DA  DG                                  
SEQRES   1 D   20   DC  DC  DT  DG  DA  DC  DC  DT  DT  DT  DG  DA  DC          
SEQRES   2 D   20   DC  DT  DA  DG  DT  DT  DC                                  
SEQRES   1 E  338  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 E  338  LYS MET GLY VAL SER ALA LEU CYS ALA ILE CYS GLY ASP          
SEQRES   3 E  338  ARG ALA THR GLY LYS HIS TYR GLY ALA SER SER CYS ASP          
SEQRES   4 E  338  GLY CYS LYS GLY PHE PHE ARG ARG SER VAL ARG LYS ASN          
SEQRES   5 E  338  HIS MET TYR SER CYS ARG PHE SER ARG GLN CYS VAL VAL          
SEQRES   6 E  338  ASP LYS ASP LYS ARG ASN GLN CYS ARG TYR CYS ARG LEU          
SEQRES   7 E  338  LYS LYS CYS PHE ARG ALA GLY MET LYS LYS GLU ALA VAL          
SEQRES   8 E  338  GLN ASN GLU ARG ASP ARG ILE SER THR ARG ARG SER SER          
SEQRES   9 E  338  TYR GLU ASP SER SER LEU PRO SER ILE ASN ALA LEU LEU          
SEQRES  10 E  338  GLN ALA GLU VAL LEU SER ARG GLN ILE THR SER PRO VAL          
SEQRES  11 E  338  SER GLY ILE ASN GLY ASP ILE ARG ALA LYS LYS ILE ALA          
SEQRES  12 E  338  SER ILE ALA ASP VAL CYS GLU SER MET LYS GLU GLN LEU          
SEQRES  13 E  338  LEU VAL LEU VAL GLU TRP ALA LYS TYR ILE PRO ALA PHE          
SEQRES  14 E  338  CYS GLU LEU PRO LEU ASP ASP GLN VAL ALA LEU LEU ARG          
SEQRES  15 E  338  ALA HIS ALA GLY GLU HIS LEU LEU LEU GLY ALA THR LYS          
SEQRES  16 E  338  ARG SER MET VAL PHE LYS ASP VAL LEU LEU LEU GLY ASN          
SEQRES  17 E  338  ASP TYR ILE VAL PRO ARG HIS CYS PRO GLU LEU ALA GLU          
SEQRES  18 E  338  MET SER ARG VAL SER ILE ARG ILE LEU ASP GLU LEU VAL          
SEQRES  19 E  338  LEU PRO PHE GLN GLU LEU GLN ILE ASP ASP ASN GLU TYR          
SEQRES  20 E  338  ALA TYR LEU LYS ALA ILE ILE PHE PHE ASP PRO ASP ALA          
SEQRES  21 E  338  LYS GLY LEU SER ASP PRO GLY LYS ILE LYS ARG LEU ARG          
SEQRES  22 E  338  SER GLN VAL GLN VAL SER LEU GLU ASP TYR ILE ASN ASP          
SEQRES  23 E  338  ARG GLN TYR ASP SER ARG GLY ARG PHE GLY GLU LEU LEU          
SEQRES  24 E  338  LEU LEU LEU PRO THR LEU GLN SER ILE THR TRP GLN MET          
SEQRES  25 E  338  ILE GLU GLN ILE GLN PHE ILE LYS LEU PHE GLY MET ALA          
SEQRES  26 E  338  LYS ILE ASP ASN LEU LEU GLN GLU MET LEU LEU GLY GLY          
SEQRES   1 F  338  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 F  338  LYS MET GLY VAL SER ALA LEU CYS ALA ILE CYS GLY ASP          
SEQRES   3 F  338  ARG ALA THR GLY LYS HIS TYR GLY ALA SER SER CYS ASP          
SEQRES   4 F  338  GLY CYS LYS GLY PHE PHE ARG ARG SER VAL ARG LYS ASN          
SEQRES   5 F  338  HIS MET TYR SER CYS ARG PHE SER ARG GLN CYS VAL VAL          
SEQRES   6 F  338  ASP LYS ASP LYS ARG ASN GLN CYS ARG TYR CYS ARG LEU          
SEQRES   7 F  338  LYS LYS CYS PHE ARG ALA GLY MET LYS LYS GLU ALA VAL          
SEQRES   8 F  338  GLN ASN GLU ARG ASP ARG ILE SER THR ARG ARG SER SER          
SEQRES   9 F  338  TYR GLU ASP SER SER LEU PRO SER ILE ASN ALA LEU LEU          
SEQRES  10 F  338  GLN ALA GLU VAL LEU SER ARG GLN ILE THR SER PRO VAL          
SEQRES  11 F  338  SER GLY ILE ASN GLY ASP ILE ARG ALA LYS LYS ILE ALA          
SEQRES  12 F  338  SER ILE ALA ASP VAL CYS GLU SER MET LYS GLU GLN LEU          
SEQRES  13 F  338  LEU VAL LEU VAL GLU TRP ALA LYS TYR ILE PRO ALA PHE          
SEQRES  14 F  338  CYS GLU LEU PRO LEU ASP ASP GLN VAL ALA LEU LEU ARG          
SEQRES  15 F  338  ALA HIS ALA GLY GLU HIS LEU LEU LEU GLY ALA THR LYS          
SEQRES  16 F  338  ARG SER MET VAL PHE LYS ASP VAL LEU LEU LEU GLY ASN          
SEQRES  17 F  338  ASP TYR ILE VAL PRO ARG HIS CYS PRO GLU LEU ALA GLU          
SEQRES  18 F  338  MET SER ARG VAL SER ILE ARG ILE LEU ASP GLU LEU VAL          
SEQRES  19 F  338  LEU PRO PHE GLN GLU LEU GLN ILE ASP ASP ASN GLU TYR          
SEQRES  20 F  338  ALA TYR LEU LYS ALA ILE ILE PHE PHE ASP PRO ASP ALA          
SEQRES  21 F  338  LYS GLY LEU SER ASP PRO GLY LYS ILE LYS ARG LEU ARG          
SEQRES  22 F  338  SER GLN VAL GLN VAL SER LEU GLU ASP TYR ILE ASN ASP          
SEQRES  23 F  338  ARG GLN TYR ASP SER ARG GLY ARG PHE GLY GLU LEU LEU          
SEQRES  24 F  338  LEU LEU LEU PRO THR LEU GLN SER ILE THR TRP GLN MET          
SEQRES  25 F  338  ILE GLU GLN ILE GLN PHE ILE LYS LEU PHE GLY MET ALA          
SEQRES  26 F  338  LYS ILE ASP ASN LEU LEU GLN GLU MET LEU LEU GLY GLY          
SEQRES   1 G   20   DG  DG  DA  DA  DC  DT  DA  DG  DG  DT  DC  DA  DA          
SEQRES   2 G   20   DA  DG  DG  DT  DC  DA  DG                                  
SEQRES   1 H   20   DC  DC  DT  DG  DA  DC  DC  DT  DT  DT  DG  DA  DC          
SEQRES   2 H   20   DC  DT  DA  DG  DT  DT  DC                                  
SEQRES   1 I   13  GLU LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER          
SEQRES   1 J   13  GLU LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER          
SEQRES   1 K   13  GLU LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER          
SEQRES   1 L   13  GLU LYS HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP SER          
HET    MYR  A 401      16                                                       
HET     ZN  A 402       1                                                       
HET     ZN  A 403       1                                                       
HET    MYR  B 401      16                                                       
HET     ZN  B 402       1                                                       
HET     ZN  B 403       1                                                       
HET    MYR  E 401      16                                                       
HET     ZN  E 402       1                                                       
HET     ZN  E 403       1                                                       
HET    MYR  F 401      16                                                       
HET     ZN  F 402       1                                                       
HET     ZN  F 403       1                                                       
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM      ZN ZINC ION                                                         
FORMUL  13  MYR    4(C14 H28 O2)                                                
FORMUL  14   ZN    8(ZN 2+)                                                     
HELIX    1   1 CYS A   68  ASN A   82  1                                  15    
HELIX    2   2 CYS A  103  ALA A  114  1                                  12    
HELIX    3   3 ALA A  145  ARG A  154  1                                  10    
HELIX    4   4 ASP A  166  LYS A  170  5                                   5    
HELIX    5   5 SER A  174  TYR A  195  1                                  22    
HELIX    6   6 ILE A  196  LEU A  202  1                                   7    
HELIX    7   7 PRO A  203  ARG A  212  1                                  10    
HELIX    8   8 HIS A  214  MET A  228  1                                  15    
HELIX    9   9 LEU A  249  GLU A  251  5                                   3    
HELIX   10  10 MET A  252  LEU A  263  1                                  12    
HELIX   11  11 LEU A  263  GLN A  271  1                                   9    
HELIX   12  12 ASP A  273  PHE A  286  1                                  14    
HELIX   13  13 ASP A  295  ASN A  315  1                                  21    
HELIX   14  14 GLY A  323  LEU A  330  1                                   8    
HELIX   15  15 LEU A  330  PHE A  352  1                                  23    
HELIX   16  16 ASP A  358  LEU A  365  1                                   8    
HELIX   17  17 CYS B   68  LYS B   81  1                                  14    
HELIX   18  18 ASP B   96  ARG B  100  5                                   5    
HELIX   19  19 CYS B  103  ARG B  113  1                                  11    
HELIX   20  20 ASP B  166  LYS B  170  5                                   5    
HELIX   21  21 SER B  174  TYR B  195  1                                  22    
HELIX   22  22 ILE B  196  GLU B  201  1                                   6    
HELIX   23  23 PRO B  203  HIS B  214  1                                  12    
HELIX   24  24 HIS B  214  MET B  228  1                                  15    
HELIX   25  25 CYS B  246  GLU B  251  5                                   6    
HELIX   26  26 MET B  252  LEU B  263  1                                  12    
HELIX   27  27 LEU B  263  GLN B  271  1                                   9    
HELIX   28  28 ASP B  273  PHE B  286  1                                  14    
HELIX   29  29 ASP B  295  ASN B  315  1                                  21    
HELIX   30  30 ARG B  317  ARG B  322  1                                   6    
HELIX   31  31 GLY B  323  LEU B  330  1                                   8    
HELIX   32  32 LEU B  330  LEU B  351  1                                  22    
HELIX   33  33 ASP B  358  LEU B  365  1                                   8    
HELIX   34  72 ALA B  145  LEU B  152  1                                   8    
HELIX   35  34 CYS E   68  ASN E   82  1                                  15    
HELIX   36  35 CYS E  103  GLY E  115  1                                  13    
HELIX   37  36 LYS E  117  VAL E  121  5                                   5    
HELIX   38  37 SER E  142  ARG E  154  1                                  13    
HELIX   39  38 GLN E  155  THR E  157  5                                   3    
HELIX   40  39 ASP E  166  LYS E  170  5                                   5    
HELIX   41  40 SER E  174  TYR E  195  1                                  22    
HELIX   42  41 ILE E  196  GLU E  201  1                                   6    
HELIX   43  42 PRO E  203  HIS E  214  1                                  12    
HELIX   44  43 HIS E  214  MET E  228  1                                  15    
HELIX   45  44 LEU E  249  GLU E  251  5                                   3    
HELIX   46  45 MET E  252  LEU E  263  1                                  12    
HELIX   47  46 LEU E  263  GLN E  271  1                                   9    
HELIX   48  47 ASP E  273  PHE E  286  1                                  14    
HELIX   49  48 ASP E  295  ASP E  316  1                                  22    
HELIX   50  49 GLY E  323  LEU E  330  1                                   8    
HELIX   51  50 LEU E  330  LEU E  351  1                                  22    
HELIX   52  51 ASP E  358  LEU E  365  1                                   8    
HELIX   53  52 CYS F   68  LYS F   81  1                                  14    
HELIX   54  53 CYS F  103  GLY F  115  1                                  13    
HELIX   55  54 LYS F  117  VAL F  121  5                                   5    
HELIX   56  55 SER F  142  LEU F  152  1                                  11    
HELIX   57  56 SER F  174  TYR F  195  1                                  22    
HELIX   58  57 ILE F  196  GLU F  201  1                                   6    
HELIX   59  58 PRO F  203  HIS F  214  1                                  12    
HELIX   60  59 HIS F  214  MET F  228  1                                  15    
HELIX   61  60 CYS F  246  ALA F  250  5                                   5    
HELIX   62  61 GLU F  251  LEU F  263  1                                  13    
HELIX   63  62 LEU F  263  GLN F  271  1                                   9    
HELIX   64  63 ASP F  273  PHE F  286  1                                  14    
HELIX   65  64 ASP F  295  ASP F  316  1                                  22    
HELIX   66  65 GLY F  323  LEU F  330  1                                   8    
HELIX   67  66 LEU F  331  GLY F  353  1                                  23    
HELIX   68  67 ASP F  358  LEU F  365  1                                   8    
HELIX   69  68 ILE I  689  GLN I  695  1                                   7    
HELIX   70  69 LYS J  688  GLN J  695  1                                   8    
HELIX   71  70 ILE K  689  LEU K  694  1                                   6    
HELIX   72  71 ILE L  689  GLN L  695  1                                   7    
SHEET    1   A 2 LYS A  61  HIS A  62  0                                        
SHEET    2   A 2 ALA A  65  SER A  66 -1  O  ALA A  65   N  HIS A  62           
SHEET    1   B 2 VAL A 233  LEU A 235  0                                        
SHEET    2   B 2 ILE A 241  PRO A 243 -1  O  VAL A 242   N  LEU A 234           
SHEET    1   C 2 GLY B  60  HIS B  62  0                                        
SHEET    2   C 2 ALA B  65  SER B  67 -1  O  ALA B  65   N  HIS B  62           
SHEET    1   D 2 VAL B 233  LEU B 235  0                                        
SHEET    2   D 2 ILE B 241  PRO B 243 -1  O  VAL B 242   N  LEU B 234           
SHEET    1   E 2 LYS E  61  HIS E  62  0                                        
SHEET    2   E 2 ALA E  65  SER E  66 -1  O  ALA E  65   N  HIS E  62           
SHEET    1   F 2 VAL E 233  LEU E 235  0                                        
SHEET    2   F 2 ILE E 241  PRO E 243 -1  O  VAL E 242   N  LEU E 234           
SHEET    1   G 2 LYS F  61  HIS F  62  0                                        
SHEET    2   G 2 ALA F  65  SER F  66 -1  O  ALA F  65   N  HIS F  62           
SHEET    1   H 2 VAL F 233  LEU F 235  0                                        
SHEET    2   H 2 ILE F 241  PRO F 243 -1  O  VAL F 242   N  LEU F 234           
LINK         SG  CYS A  54                ZN    ZN A 402     1555   1555  2.13  
LINK         SG  CYS E  54                ZN    ZN E 402     1555   1555  2.19  
LINK         SG  CYS E  71                ZN    ZN E 402     1555   1555  2.21  
LINK         SG  CYS E  93                ZN    ZN E 403     1555   1555  2.21  
LINK         SG  CYS F  87                ZN    ZN F 403     1555   1555  2.21  
LINK         SG  CYS E 106                ZN    ZN E 403     1555   1555  2.22  
LINK         SG  CYS B  87                ZN    ZN B 403     1555   1555  2.22  
LINK         SG  CYS A 103                ZN    ZN A 403     1555   1555  2.22  
LINK         SG  CYS E  87                ZN    ZN E 403     1555   1555  2.25  
LINK         SG  CYS A  93                ZN    ZN A 403     1555   1555  2.25  
LINK         SG  CYS B  54                ZN    ZN B 402     1555   1555  2.26  
LINK         SG  CYS F  54                ZN    ZN F 402     1555   1555  2.26  
LINK         SG  CYS B  93                ZN    ZN B 403     1555   1555  2.28  
LINK         SG  CYS E  51                ZN    ZN E 402     1555   1555  2.28  
LINK         SG  CYS E 103                ZN    ZN E 403     1555   1555  2.31  
LINK         SG  CYS E  68                ZN    ZN E 402     1555   1555  2.32  
LINK         SG  CYS B  71                ZN    ZN B 402     1555   1555  2.33  
LINK         SG  CYS A  87                ZN    ZN A 403     1555   1555  2.33  
LINK         SG  CYS F  71                ZN    ZN F 402     1555   1555  2.35  
LINK         SG  CYS F  93                ZN    ZN F 403     1555   1555  2.35  
LINK         SG  CYS F  51                ZN    ZN F 402     1555   1555  2.37  
LINK         SG  CYS A  71                ZN    ZN A 402     1555   1555  2.37  
LINK         SG  CYS B 106                ZN    ZN B 403     1555   1555  2.40  
LINK         SG  CYS F 106                ZN    ZN F 403     1555   1555  2.44  
LINK         SG  CYS A  68                ZN    ZN A 402     1555   1555  2.47  
LINK         SG  CYS A  51                ZN    ZN A 402     1555   1555  2.48  
LINK         SG  CYS A 106                ZN    ZN A 403     1555   1555  2.48  
LINK         SG  CYS B  51                ZN    ZN B 402     1555   1555  2.52  
LINK         SG  CYS F 103                ZN    ZN F 403     1555   1555  2.53  
LINK         SG  CYS B  68                ZN    ZN B 402     1555   1555  2.55  
LINK         SG  CYS B 103                ZN    ZN B 403     1555   1555  2.56  
LINK         SG  CYS F  68                ZN    ZN F 402     1555   1555  2.77  
SITE     1 AC1  7 SER A 181  GLN A 185  ARG A 226  LEU A 236                    
SITE     2 AC1  7 GLY A 237  MET A 252  GLN A 345                               
SITE     1 AC2  4 CYS A  51  CYS A  54  CYS A  68  CYS A  71                    
SITE     1 AC3  4 CYS A  87  CYS A  93  CYS A 103  CYS A 106                    
SITE     1 AC4  7 VAL B 178  SER B 181  GLN B 185  ARG B 226                    
SITE     2 AC4  7 LEU B 236  GLY B 237  MET B 252                               
SITE     1 AC5  4 CYS B  51  CYS B  54  CYS B  68  CYS B  71                    
SITE     1 AC6  4 CYS B  87  CYS B  93  CYS B 103  CYS B 106                    
SITE     1 AC7 10 VAL E 178  SER E 181  MET E 182  GLN E 185                    
SITE     2 AC7 10 ARG E 226  LEU E 236  GLY E 237  MET E 252                    
SITE     3 AC7 10 SER E 256  ILE E 259                                          
SITE     1 AC8  4 CYS E  51  CYS E  54  CYS E  68  CYS E  71                    
SITE     1 AC9  4 CYS E  87  CYS E  93  CYS E 103  CYS E 106                    
SITE     1 BC1  9 SER F 181  GLN F 185  ALA F 223  ARG F 226                    
SITE     2 BC1  9 MET F 252  VAL F 255  SER F 256  ILE F 259                    
SITE     3 BC1  9 ILE F 346                                                     
SITE     1 BC2  4 CYS F  51  CYS F  54  CYS F  68  CYS F  71                    
SITE     1 BC3  4 CYS F  87  CYS F  93  CYS F 103  CYS F 106                    
CRYST1  119.786   57.596  166.305  90.00  96.30  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      0.008348  0.000000  0.000922        0.00000                         
SCALE2      0.000000  0.017362  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006050        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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