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Database: PDB
Entry: 2H8R
LinkDB: 2H8R
Original site: 2H8R 
HEADER    TRANSCRIPTION ACTIVATOR/DNA             07-JUN-06   2H8R              
TITLE     HEPATOCYTE NUCLEAR FACTOR 1B BOUND TO DNA: MODY5 GENE                 
TITLE    2 PRODUCT                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 1-BETA;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DNA BINDING DOMAIN (RESIDUES 91-310);                      
COMPND   5 SYNONYM: HNF-1BETA, HNF-1B, VARIANT HEPATIC NUCLEAR FACTOR           
COMPND   6 1, VHNF1, HOMEOPROTEIN LFB3, TRANSCRIPTION FACTOR 2, TCF-2;          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-                                                        
COMPND  10 D(*CP*TP*TP*GP*GP*TP*TP*AP*AP*TP*AP*AP*TP*TP*CP*AP*CP*CP*AP          
COMPND  11 *G)-3';                                                              
COMPND  12 CHAIN: E;                                                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: 5'-                                                        
COMPND  16 D(*GP*CP*TP*GP*GP*TP*GP*AP*AP*TP*TP*AP*TP*TP*AP*AP*CP*CP*AP          
COMPND  17 *A)-3';                                                              
COMPND  18 CHAIN: F;                                                            
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET41A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES                                                       
KEYWDS    TRASNCRIPTION FACTOR, POU, HOMEO, PROTEIN-DNA, HUMAN                  
KEYWDS   2 DISEASE, TRANSCRIPTION ACTIVATOR/DNA COMPLEX                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LU,G.B.RHA,Y.I.CHI                                                  
REVDAT   3   24-FEB-09 2H8R    1       VERSN                                    
REVDAT   2   12-FEB-08 2H8R    1       JRNL                                     
REVDAT   1   19-JUN-07 2H8R    0                                                
JRNL        AUTH   P.LU,G.B.RHA,Y.I.CHI                                         
JRNL        TITL   STRUCTURAL BASIS OF DISEASE-CAUSING MUTATIONS IN             
JRNL        TITL 2 HEPATOCYTE NUCLEAR FACTOR 1BETA.                             
JRNL        REF    BIOCHEMISTRY                  V.  46 12071 2007              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17924661                                                     
JRNL        DOI    10.1021/BI7010527                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.LU,Y.LI,A.GORMAN,Y.I.CHI                                   
REMARK   1  TITL   CRYSTALLIZATION OF HEPATOCYTE NUCLEAR FACTOR 1BETA           
REMARK   1  TITL 2 IN COMPLEX WITH DNA.                                         
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   525 2006              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11992                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 637                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 528                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 53.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 24                           
REMARK   3   BIN FREE R VALUE                    : 0.4150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2916                                    
REMARK   3   NUCLEIC ACID ATOMS       : 814                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 7                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.24                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.43000                                              
REMARK   3    B22 (A**2) : 5.43000                                              
REMARK   3    B33 (A**2) : -8.15000                                             
REMARK   3    B12 (A**2) : 2.72000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.538         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.374         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.564        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.903                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.829                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3866 ; 0.079 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5362 ; 5.450 ; 2.206       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   348 ;12.042 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   530 ; 0.258 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2697 ; 0.020 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2269 ; 0.374 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   248 ; 0.294 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    12 ; 0.236 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.470 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1756 ; 2.542 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2814 ; 4.678 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2110 ; 5.745 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2548 ; 8.674 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  3866 ; 3.686 ; 2.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):     7 ;20.239 ; 2.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3717 ; 5.174 ; 2.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2H8R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038071.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97923                            
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK MONOCHROMATOR       
REMARK 200                                   HIGH-RESOLUTION DOUBLE-CRYSTAL     
REMARK 200                                   SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12582                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.27300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.350                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1IC8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6%(V/V) PEG300, 5%(V/V) PEG8000, 8%      
REMARK 280  (V/V) GLYCEROL, 100MM TRIS, PH 8.0, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 295K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       87.34450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       50.42837            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       24.14467            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       87.34450            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       50.42837            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       24.14467            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       87.34450            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       50.42837            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       24.14467            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      100.85674            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       48.28933            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000      100.85674            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       48.28933            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000      100.85674            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       48.28933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: DIMER WHEN BINDING TO DNA                                    
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 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     GLN A   188                                                      
REMARK 465     SER A   189                                                      
REMARK 465     SER A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     ASN A   192                                                      
REMARK 465     MET A   193                                                      
REMARK 465     THR A   194                                                      
REMARK 465     ASP A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     GLN A   199                                                      
REMARK 465     ASP A   200                                                      
REMARK 465     GLN A   201                                                      
REMARK 465     LEU A   202                                                      
REMARK 465     LEU A   203                                                      
REMARK 465     PHE A   204                                                      
REMARK 465     LEU A   205                                                      
REMARK 465     PHE A   206                                                      
REMARK 465     PRO A   207                                                      
REMARK 465     GLU A   208                                                      
REMARK 465     PHE A   209                                                      
REMARK 465     SER A   210                                                      
REMARK 465     GLN A   211                                                      
REMARK 465     GLN A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     PRO A   216                                                      
REMARK 465     GLY A   217                                                      
REMARK 465     GLN A   218                                                      
REMARK 465     SER A   219                                                      
REMARK 465     ASP A   220                                                      
REMARK 465     ASP A   221                                                      
REMARK 465     ALA A   222                                                      
REMARK 465     CYS A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     PRO A   226                                                      
REMARK 465     THR A   227                                                      
REMARK 465     ASN A   228                                                      
REMARK 465     LYS A   229                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     THR B   186                                                      
REMARK 465     VAL B   187                                                      
REMARK 465     GLN B   188                                                      
REMARK 465     SER B   189                                                      
REMARK 465     SER B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     ASN B   192                                                      
REMARK 465     MET B   193                                                      
REMARK 465     THR B   194                                                      
REMARK 465     ASP B   195                                                      
REMARK 465     LYS B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     GLN B   199                                                      
REMARK 465     ASP B   200                                                      
REMARK 465     GLN B   201                                                      
REMARK 465     LEU B   202                                                      
REMARK 465     LEU B   203                                                      
REMARK 465     PHE B   204                                                      
REMARK 465     LEU B   205                                                      
REMARK 465     PHE B   206                                                      
REMARK 465     PRO B   207                                                      
REMARK 465     GLU B   208                                                      
REMARK 465     PHE B   209                                                      
REMARK 465     SER B   210                                                      
REMARK 465     GLN B   211                                                      
REMARK 465     GLN B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     GLY B   215                                                      
REMARK 465     PRO B   216                                                      
REMARK 465     GLY B   217                                                      
REMARK 465     GLN B   218                                                      
REMARK 465     SER B   219                                                      
REMARK 465     ASP B   220                                                      
REMARK 465     ASP B   221                                                      
REMARK 465     ALA B   222                                                      
REMARK 465     CYS B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     GLU B   225                                                      
REMARK 465     PRO B   226                                                      
REMARK 465     THR B   227                                                      
REMARK 465     ASN B   228                                                      
REMARK 465     LYS B   229                                                      
REMARK 465     LYS B   230                                                      
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   O    SER B   257     N    GLU B   259              1.90            
REMARK 500   OP1  DC  F     3     OP2  DT  F     4              1.98            
REMARK 500   O    GLN B   106     N    ALA B   108              2.08            
REMARK 500   OG   SER A   279     OG   SER A   281              2.14            
REMARK 500   O    CYS A   268     N    ALA A   271              2.15            
REMARK 500   O    ARG A   304     N    GLU A   306              2.17            
REMARK 500   C3'  DG  F     5     OP2  DG  F     6              2.18            
REMARK 500   O    SER A   279     O    SER A   281              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DC E   1   O5'    DC E   1   C5'     0.193                       
REMARK 500     DC E   1   C5'    DC E   1   C4'     0.111                       
REMARK 500     DC E   1   C4'    DC E   1   C3'     0.075                       
REMARK 500     DC E   1   O4'    DC E   1   C4'     0.080                       
REMARK 500     DC E   1   O3'    DC E   1   C3'     0.105                       
REMARK 500     DC E   1   C1'    DC E   1   N1      0.106                       
REMARK 500     DC E   1   C2     DC E   1   O2      0.129                       
REMARK 500     DC E   1   N1     DC E   1   C2      0.119                       
REMARK 500     DC E   1   N1     DC E   1   C6      0.065                       
REMARK 500     DC E   1   C2     DC E   1   N3      0.137                       
REMARK 500     DC E   1   N3     DC E   1   C4      0.083                       
REMARK 500     DC E   1   C5     DC E   1   C6      0.050                       
REMARK 500     DT E   2   P      DT E   2   OP1     0.174                       
REMARK 500     DT E   2   P      DT E   2   O5'     0.196                       
REMARK 500     DT E   2   O5'    DT E   2   C5'     0.108                       
REMARK 500     DT E   2   C5'    DT E   2   C4'     0.043                       
REMARK 500     DT E   2   O3'    DT E   2   C3'     0.093                       
REMARK 500     DT E   2   C1'    DT E   2   N1      0.099                       
REMARK 500     DT E   2   N1     DT E   2   C2      0.131                       
REMARK 500     DT E   2   C2     DT E   2   N3      0.134                       
REMARK 500     DT E   2   N3     DT E   2   C4      0.062                       
REMARK 500     DT E   2   C4     DT E   2   C5      0.060                       
REMARK 500     DT E   2   C5     DT E   2   C6      0.083                       
REMARK 500     DT E   2   C6     DT E   2   N1      0.093                       
REMARK 500     DT E   2   C2     DT E   2   O2      0.150                       
REMARK 500     DC E   1   O3'    DT E   2   P       0.146                       
REMARK 500     DT E   3   P      DT E   3   OP2     0.151                       
REMARK 500     DT E   3   P      DT E   3   O5'     0.102                       
REMARK 500     DT E   3   C5'    DT E   3   C4'     0.043                       
REMARK 500     DT E   3   C2     DT E   3   N3      0.086                       
REMARK 500     DT E   3   N3     DT E   3   C4      0.087                       
REMARK 500     DT E   3   C4     DT E   3   C5      0.090                       
REMARK 500     DT E   3   C5     DT E   3   C6      0.055                       
REMARK 500     DT E   3   C2     DT E   3   O2      0.069                       
REMARK 500     DT E   3   C4     DT E   3   O4      0.094                       
REMARK 500     DT E   2   O3'    DT E   3   P       0.207                       
REMARK 500     DG E   4   P      DG E   4   OP1     0.108                       
REMARK 500     DG E   4   P      DG E   4   OP2     0.118                       
REMARK 500     DG E   4   P      DG E   4   O5'     0.159                       
REMARK 500     DG E   4   O5'    DG E   4   C5'     0.217                       
REMARK 500     DG E   4   C5'    DG E   4   C4'     0.076                       
REMARK 500     DG E   4   O3'    DG E   4   C3'    -0.038                       
REMARK 500     DG E   4   C4     DG E   4   C5      0.056                       
REMARK 500     DG E   4   C6     DG E   4   N1     -0.057                       
REMARK 500     DG E   5   O3'    DG E   5   C3'    -0.097                       
REMARK 500     DG E   5   C6     DG E   5   N1     -0.044                       
REMARK 500     DG E   5   C5     DG E   5   N7     -0.053                       
REMARK 500     DG E   5   C8     DG E   5   N9     -0.045                       
REMARK 500     DT E   6   C5'    DT E   6   C4'     0.043                       
REMARK 500     DT E   7   P      DT E   7   OP2     0.153                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     597 BOND DEVIATIONS.                              
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     DC E   1   O4' -  C4' -  C3' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DC E   1   C5' -  C4' -  C3' ANGL. DEV. =  15.2 DEGREES          
REMARK 500     DC E   1   C5' -  C4' -  O4' ANGL. DEV. =   7.0 DEGREES          
REMARK 500     DC E   1   C4' -  C3' -  C2' ANGL. DEV. =   6.8 DEGREES          
REMARK 500     DC E   1   N1  -  C1' -  C2' ANGL. DEV. =  12.3 DEGREES          
REMARK 500     DC E   1   O4' -  C1' -  N1  ANGL. DEV. =  -7.0 DEGREES          
REMARK 500     DC E   1   N1  -  C2  -  N3  ANGL. DEV. =  -7.3 DEGREES          
REMARK 500     DC E   1   C2  -  N3  -  C4  ANGL. DEV. =   6.8 DEGREES          
REMARK 500     DC E   1   N3  -  C4  -  C5  ANGL. DEV. =  -3.5 DEGREES          
REMARK 500     DC E   1   C5  -  C6  -  N1  ANGL. DEV. =   5.6 DEGREES          
REMARK 500     DC E   1   N1  -  C2  -  O2  ANGL. DEV. =   6.1 DEGREES          
REMARK 500     DT E   2   OP1 -  P   -  OP2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500     DT E   2   P   -  O5' -  C5' ANGL. DEV. =  11.9 DEGREES          
REMARK 500     DT E   2   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT E   2   N3  -  C4  -  C5  ANGL. DEV. =   3.8 DEGREES          
REMARK 500     DT E   2   O3' -  P   -  OP2 ANGL. DEV. = -16.5 DEGREES          
REMARK 500     DT E   2   O3' -  P   -  OP1 ANGL. DEV. =  12.6 DEGREES          
REMARK 500     DT E   3   O5' -  P   -  OP1 ANGL. DEV. = -10.2 DEGREES          
REMARK 500     DT E   3   N1  -  C1' -  C2' ANGL. DEV. =  11.0 DEGREES          
REMARK 500     DT E   3   O4' -  C1' -  N1  ANGL. DEV. = -10.2 DEGREES          
REMARK 500     DT E   3   N3  -  C4  -  C5  ANGL. DEV. =  -6.5 DEGREES          
REMARK 500     DT E   3   N1  -  C2  -  O2  ANGL. DEV. =  -8.6 DEGREES          
REMARK 500     DT E   3   N3  -  C2  -  O2  ANGL. DEV. =   9.0 DEGREES          
REMARK 500     DT E   3   N3  -  C4  -  O4  ANGL. DEV. =   4.6 DEGREES          
REMARK 500     DT E   3   C6  -  N1  -  C1' ANGL. DEV. =  12.5 DEGREES          
REMARK 500     DT E   3   C2  -  N1  -  C1' ANGL. DEV. = -15.7 DEGREES          
REMARK 500     DT E   3   O3' -  P   -  OP2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500     DG E   4   OP1 -  P   -  OP2 ANGL. DEV. =  11.0 DEGREES          
REMARK 500     DG E   4   O5' -  P   -  OP1 ANGL. DEV. = -12.8 DEGREES          
REMARK 500     DG E   4   C5' -  C4' -  O4' ANGL. DEV. =   7.7 DEGREES          
REMARK 500     DG E   4   N1  -  C2  -  N3  ANGL. DEV. =  11.6 DEGREES          
REMARK 500     DG E   4   C2  -  N3  -  C4  ANGL. DEV. = -12.7 DEGREES          
REMARK 500     DG E   4   C5  -  C6  -  N1  ANGL. DEV. =  -6.5 DEGREES          
REMARK 500     DG E   4   N1  -  C2  -  N2  ANGL. DEV. = -14.8 DEGREES          
REMARK 500     DG E   4   C5  -  C6  -  O6  ANGL. DEV. =   8.6 DEGREES          
REMARK 500     DG E   5   OP1 -  P   -  OP2 ANGL. DEV. =  15.7 DEGREES          
REMARK 500     DG E   5   O5' -  P   -  OP1 ANGL. DEV. = -12.5 DEGREES          
REMARK 500     DG E   5   C1' -  O4' -  C4' ANGL. DEV. =  -6.8 DEGREES          
REMARK 500     DG E   5   C4' -  C3' -  C2' ANGL. DEV. =  -6.6 DEGREES          
REMARK 500     DG E   5   O4' -  C1' -  N9  ANGL. DEV. =  11.1 DEGREES          
REMARK 500     DG E   5   N1  -  C2  -  N3  ANGL. DEV. =   5.8 DEGREES          
REMARK 500     DG E   5   C2  -  N3  -  C4  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500     DG E   5   N3  -  C4  -  C5  ANGL. DEV. =  -4.1 DEGREES          
REMARK 500     DG E   5   C4  -  C5  -  C6  ANGL. DEV. =   9.9 DEGREES          
REMARK 500     DG E   5   C5  -  C6  -  N1  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500     DG E   5   N7  -  C8  -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500     DG E   5   C8  -  N9  -  C4  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500     DG E   5   N9  -  C4  -  C5  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DG E   5   C6  -  C5  -  N7  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500     DG E   5   N1  -  C2  -  N2  ANGL. DEV. =  -9.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     580 ANGLE DEVIATIONS.                             
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    ASN A  99       74.25   -119.04                                   
REMARK 500    MET A 113      -27.83    -36.91                                   
REMARK 500    PRO A 118      -38.66    -39.29                                   
REMARK 500    ASP A 141      -93.16    -58.57                                   
REMARK 500    VAL A 142      -62.07    -17.68                                   
REMARK 500    ASN A 155      -73.79    -88.96                                   
REMARK 500    VAL A 173      -76.92    -20.96                                   
REMARK 500    GLU A 178      -75.37    -26.87                                   
REMARK 500    THR A 186     -169.58    -78.22                                   
REMARK 500    ASN A 234      170.04    -41.43                                   
REMARK 500    ALA A 241      -74.54    -32.99                                   
REMARK 500    ALA A 249      -10.86    -48.43                                   
REMARK 500    LYS A 258      -51.96    -19.14                                   
REMARK 500    GLU A 260      -72.28    -44.50                                   
REMARK 500    ARG A 261      -77.16    -39.71                                   
REMARK 500    GLU A 262      -36.62    -15.80                                   
REMARK 500    ASN A 269      -29.04    -32.30                                   
REMARK 500    GLU A 272      -38.29    -29.92                                   
REMARK 500    PRO A 280      -12.39    -43.74                                   
REMARK 500    ARG A 303      -15.48   -157.90                                   
REMARK 500    ARG A 304      -68.70   -103.34                                   
REMARK 500    LYS A 305       28.59    -51.35                                   
REMARK 500    GLU A 306       34.57   -147.69                                   
REMARK 500    ILE B  91      -28.40    -38.53                                   
REMARK 500    GLN B  96        0.22    -54.94                                   
REMARK 500    THR B 100      171.13    -42.09                                   
REMARK 500    ALA B 103      -57.63    -26.91                                   
REMARK 500    GLU B 105      -62.87    -20.13                                   
REMARK 500    ARG B 107      -11.10    -43.74                                   
REMARK 500    MET B 113      -32.01    -38.83                                   
REMARK 500    ASP B 117      107.77    -46.95                                   
REMARK 500    LYS B 123      -71.80    -53.97                                   
REMARK 500    MET B 124      -55.59    -20.22                                   
REMARK 500    ASN B 133       89.03     53.64                                   
REMARK 500    GLU B 138       -3.40    -45.43                                   
REMARK 500    SER B 151      -39.86    -30.29                                   
REMARK 500    THR B 162      -66.57    -23.64                                   
REMARK 500    GLU B 178      -37.67    -33.87                                   
REMARK 500    PHE B 183      -82.04   -118.86                                   
REMARK 500    ARG B 232      134.65      5.39                                   
REMARK 500    ASN B 234      129.11    -22.13                                   
REMARK 500    TYR B 250       -6.64   -141.04                                   
REMARK 500    ASP B 251      105.75    -54.43                                   
REMARK 500    ASN B 255       89.21     40.54                                   
REMARK 500    LYS B 258       -3.97    -34.83                                   
REMARK 500    GLU B 262      -29.77    -37.88                                   
REMARK 500    PRO B 280        1.57    -52.50                                   
REMARK 500    GLU B 293      -79.20    -50.71                                   
REMARK 500    VAL B 294      -39.52    -38.95                                   
REMARK 500    GLU B 306      -93.21    -34.13                                   
REMARK 500    GLU B 307      -62.47    -22.72                                   
REMARK 500    ALA B 308      -19.58    -22.61                                   
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 PHE A  183     ASN A  184                 -143.30                    
REMARK 500 LEU A  286     GLY A  287                  148.91                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2H8R A   91   310  UNP    P35680   HNF1B_HUMAN     91    310             
DBREF  2H8R B   91   310  UNP    P35680   HNF1B_HUMAN     91    310             
DBREF  2H8R E    1    20  PDB    2H8R     2H8R             1     20             
DBREF  2H8R F    2    21  PDB    2H8R     2H8R             2     21             
SEQADV 2H8R SER A   90  UNP  P35680              CLONING ARTIFACT               
SEQADV 2H8R SER B   90  UNP  P35680              CLONING ARTIFACT               
SEQRES   1 A  221  SER ILE LEU LYS GLU LEU GLN ALA LEU ASN THR GLU GLU          
SEQRES   2 A  221  ALA ALA GLU GLN ARG ALA GLU VAL ASP ARG MET LEU SER          
SEQRES   3 A  221  GLU ASP PRO TRP ARG ALA ALA LYS MET ILE LYS GLY TYR          
SEQRES   4 A  221  MET GLN GLN HIS ASN ILE PRO GLN ARG GLU VAL VAL ASP          
SEQRES   5 A  221  VAL THR GLY LEU ASN GLN SER HIS LEU SER GLN HIS LEU          
SEQRES   6 A  221  ASN LYS GLY THR PRO MET LYS THR GLN LYS ARG ALA ALA          
SEQRES   7 A  221  LEU TYR THR TRP TYR VAL ARG LYS GLN ARG GLU ILE LEU          
SEQRES   8 A  221  ARG GLN PHE ASN GLN THR VAL GLN SER SER GLY ASN MET          
SEQRES   9 A  221  THR ASP LYS SER SER GLN ASP GLN LEU LEU PHE LEU PHE          
SEQRES  10 A  221  PRO GLU PHE SER GLN GLN SER HIS GLY PRO GLY GLN SER          
SEQRES  11 A  221  ASP ASP ALA CYS SER GLU PRO THR ASN LYS LYS MET ARG          
SEQRES  12 A  221  ARG ASN ARG PHE LYS TRP GLY PRO ALA SER GLN GLN ILE          
SEQRES  13 A  221  LEU TYR GLN ALA TYR ASP ARG GLN LYS ASN PRO SER LYS          
SEQRES  14 A  221  GLU GLU ARG GLU ALA LEU VAL GLU GLU CYS ASN ARG ALA          
SEQRES  15 A  221  GLU CYS LEU GLN ARG GLY VAL SER PRO SER LYS ALA HIS          
SEQRES  16 A  221  GLY LEU GLY SER ASN LEU VAL THR GLU VAL ARG VAL TYR          
SEQRES  17 A  221  ASN TRP PHE ALA ASN ARG ARG LYS GLU GLU ALA PHE ARG          
SEQRES   1 B  221  SER ILE LEU LYS GLU LEU GLN ALA LEU ASN THR GLU GLU          
SEQRES   2 B  221  ALA ALA GLU GLN ARG ALA GLU VAL ASP ARG MET LEU SER          
SEQRES   3 B  221  GLU ASP PRO TRP ARG ALA ALA LYS MET ILE LYS GLY TYR          
SEQRES   4 B  221  MET GLN GLN HIS ASN ILE PRO GLN ARG GLU VAL VAL ASP          
SEQRES   5 B  221  VAL THR GLY LEU ASN GLN SER HIS LEU SER GLN HIS LEU          
SEQRES   6 B  221  ASN LYS GLY THR PRO MET LYS THR GLN LYS ARG ALA ALA          
SEQRES   7 B  221  LEU TYR THR TRP TYR VAL ARG LYS GLN ARG GLU ILE LEU          
SEQRES   8 B  221  ARG GLN PHE ASN GLN THR VAL GLN SER SER GLY ASN MET          
SEQRES   9 B  221  THR ASP LYS SER SER GLN ASP GLN LEU LEU PHE LEU PHE          
SEQRES  10 B  221  PRO GLU PHE SER GLN GLN SER HIS GLY PRO GLY GLN SER          
SEQRES  11 B  221  ASP ASP ALA CYS SER GLU PRO THR ASN LYS LYS MET ARG          
SEQRES  12 B  221  ARG ASN ARG PHE LYS TRP GLY PRO ALA SER GLN GLN ILE          
SEQRES  13 B  221  LEU TYR GLN ALA TYR ASP ARG GLN LYS ASN PRO SER LYS          
SEQRES  14 B  221  GLU GLU ARG GLU ALA LEU VAL GLU GLU CYS ASN ARG ALA          
SEQRES  15 B  221  GLU CYS LEU GLN ARG GLY VAL SER PRO SER LYS ALA HIS          
SEQRES  16 B  221  GLY LEU GLY SER ASN LEU VAL THR GLU VAL ARG VAL TYR          
SEQRES  17 B  221  ASN TRP PHE ALA ASN ARG ARG LYS GLU GLU ALA PHE ARG          
SEQRES   1 E   20   DC  DT  DT  DG  DG  DT  DT  DA  DA  DT  DA  DA  DT          
SEQRES   2 E   20   DT  DC  DA  DC  DC  DA  DG                                  
SEQRES   1 F   20   DG  DC  DT  DG  DG  DT  DG  DA  DA  DT  DT  DA  DT          
SEQRES   2 F   20   DT  DA  DA  DC  DC  DA  DA                                  
FORMUL   5  HOH   *7(H2 O)                                                      
HELIX    1   1 SER A   90  ASN A   99  1                                  10    
HELIX    2   2 THR A  100  LEU A  114  1                                  15    
HELIX    3   3 ASP A  117  ASN A  133  1                                  17    
HELIX    4   4 PRO A  135  GLY A  144  1                                  10    
HELIX    5   5 ASN A  146  ASN A  155  1                                  10    
HELIX    6   6 LYS A  161  GLN A  182  1                                  22    
HELIX    7   7 GLY A  239  GLN A  253  1                                  15    
HELIX    8   8 SER A  257  ARG A  276  1                                  20    
HELIX    9   9 LYS A  282  GLY A  287  5                                   6    
HELIX   10  10 THR A  292  LYS A  305  1                                  14    
HELIX   11  11 SER B   90  ASN B   99  1                                  10    
HELIX   12  12 THR B  100  MET B  113  1                                  14    
HELIX   13  13 ASP B  117  ASN B  133  1                                  17    
HELIX   14  14 GLN B  136  GLY B  144  1                                   9    
HELIX   15  15 ASN B  146  LYS B  156  1                                  11    
HELIX   16  16 LYS B  161  GLN B  182  1                                  22    
HELIX   17  17 GLY B  239  ALA B  249  1                                  11    
HELIX   18  18 SER B  257  GLY B  277  1                                  21    
HELIX   19  19 SER B  279  ALA B  283  5                                   5    
HELIX   20  20 LEU B  286  LEU B  290  5                                   5    
HELIX   21  21 THR B  292  GLU B  307  1                                  16    
CRYST1  174.689  174.689   72.434  90.00  90.00 120.00 H 3          18          
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      0.005724  0.003305  0.000000        0.00000                         
SCALE2      0.000000  0.006610  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013806        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system