GenomeNet

Database: PDB
Entry: 5D1Y
LinkDB: 5D1Y
Original site: 5D1Y 
HEADER    OXIDOREDUCTASE                          04-AUG-15   5D1Y              
TITLE     LOW RESOLUTION CRYSTAL STRUCTURE OF HUMAN RIBONUCLEOTIDE REDUCTASE    
TITLE    2 ALPHA6 HEXAMER IN COMPLEX WITH DATP                                  
CAVEAT     5D1Y    RESIDUE A THR 90 AND RESIDUE A LYS 91 ARE NOT PROPERLY       
CAVEAT   2 5D1Y    LINKED: DISTANCE BETWEEN C AND N IS 11.08. RESIDUE B THR 90  
CAVEAT   3 5D1Y    AND RESIDUE B LYS 91 ARE NOT PROPERLY LINKED: DISTANCE       
CAVEAT   4 5D1Y    BETWEEN C AND N IS 5.88.                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT;        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M1,            
COMPND   5 RIBONUCLEOTIDE REDUCTASE LARGE SUBUNIT;                              
COMPND   6 EC: 1.17.4.1;                                                        
COMPND   7 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: RRM1, RR1;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    DEOXYRIBONUCLEOTIDE, OLIGOMERIZATION, ATP CONE, OXIDOREDUCTASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.ANDO,H.LI,E.J.BRIGNOLE,S.THOMPSON,M.I.MCLAUGHLIN,J.PAGE,F.ASTURIAS, 
AUTHOR   2 J.STUBBE,C.L.DRENNAN                                                 
REVDAT   4   22-NOV-17 5D1Y    1       REMARK                                   
REVDAT   3   20-SEP-17 5D1Y    1       JRNL   REMARK                            
REVDAT   2   27-JAN-16 5D1Y    1       JRNL                                     
REVDAT   1   20-JAN-16 5D1Y    0                                                
JRNL        AUTH   N.ANDO,H.LI,E.J.BRIGNOLE,S.THOMPSON,M.I.MCLAUGHLIN,J.E.PAGE, 
JRNL        AUTH 2 F.J.ASTURIAS,J.STUBBE,C.L.DRENNAN                            
JRNL        TITL   ALLOSTERIC INHIBITION OF HUMAN RIBONUCLEOTIDE REDUCTASE BY   
JRNL        TITL 2 DATP ENTAILS THE STABILIZATION OF A HEXAMER.                 
JRNL        REF    BIOCHEMISTRY                  V.  55   373 2016              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   26727048                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.5B01207                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    9.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 9.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 75.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 6110                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.407                           
REMARK   3   R VALUE            (WORKING SET) : 0.405                           
REMARK   3   FREE R VALUE                     : 0.426                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.020                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 612                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 75.9042 - 14.2707    1.00     1465   163  0.4075 0.4296        
REMARK   3     2 14.2707 - 11.3392    1.00     1365   151  0.4006 0.4472        
REMARK   3     3 11.3392 -  9.9094    1.00     1338   150  0.3973 0.3772        
REMARK   3     4  9.9094 -  9.0050    1.00     1330   148  0.4169 0.4395        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 1.740            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 50.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.01                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 633.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.101          11577                                  
REMARK   3   ANGLE     :  1.512          15743                                  
REMARK   3   CHIRALITY :  0.096           1783                                  
REMARK   3   PLANARITY :  0.009           2008                                  
REMARK   3   DIHEDRAL  : 20.896           4158                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5D1Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212340.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9179                             
REMARK 200  MONOCHROMATOR                  : SI(111) CRYSTAL                    
REMARK 200  OPTICS                         : WHITE BEAM COLLIMATING MIRROR,     
REMARK 200                                   VERTICALLY FOCUSING RH-COATED SI   
REMARK 200                                   MIRROR, HORIZONTALLY FOCUSING      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE, XDS                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6141                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 9.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.861                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 15.70                              
REMARK 200  R MERGE                    (I) : 0.27400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 9.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 10.10                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 16.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.96200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.1                                          
REMARK 200 STARTING MODEL: 3HNC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: HEXAGONAL                                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 88.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 10.3                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 32% V/V JEFFAMINE M600,    
REMARK 280  10 MM DTT, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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      178.00500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      178.00500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      178.00500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      178.00500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      178.00500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      178.00500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000      178.00500            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000      178.00500            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000      178.00500            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000      178.00500            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000      178.00500            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000      178.00500            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000      178.00500            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000      178.00500            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000      178.00500            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000      178.00500            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000      178.00500            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000      178.00500            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000      267.00750            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       89.00250            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       89.00250            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000      267.00750            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000      267.00750            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      267.00750            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       89.00250            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       89.00250            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      267.00750            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       89.00250            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000      267.00750            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       89.00250            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000      267.00750            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       89.00250            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       89.00250            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       89.00250            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000      267.00750            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       89.00250            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000      267.00750            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000      267.00750            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000      267.00750            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       89.00250            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       89.00250            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000      267.00750            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000      267.00750            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       89.00250            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       89.00250            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       89.00250            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       89.00250            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000      267.00750            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       89.00250            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000      267.00750            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       89.00250            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000      267.00750            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000      267.00750            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000      267.00750            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 53030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLY A   290                                                      
REMARK 465     ASN A   291                                                      
REMARK 465     LYS A   292                                                      
REMARK 465     ARG A   293                                                      
REMARK 465     PRO A   294                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     LYS A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     GLN A   323                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     ALA A   325                                                      
REMARK 465     PRO A   743                                                      
REMARK 465     ALA A   744                                                      
REMARK 465     ALA A   745                                                      
REMARK 465     ASN A   746                                                      
REMARK 465     PRO A   747                                                      
REMARK 465     ILE A   748                                                      
REMARK 465     GLN A   749                                                      
REMARK 465     PHE A   750                                                      
REMARK 465     THR A   751                                                      
REMARK 465     LEU A   752                                                      
REMARK 465     ASN A   753                                                      
REMARK 465     LYS A   754                                                      
REMARK 465     GLU A   755                                                      
REMARK 465     LYS A   756                                                      
REMARK 465     LEU A   757                                                      
REMARK 465     LYS A   758                                                      
REMARK 465     ASP A   759                                                      
REMARK 465     LYS A   760                                                      
REMARK 465     GLU A   761                                                      
REMARK 465     LYS A   762                                                      
REMARK 465     VAL A   763                                                      
REMARK 465     SER A   764                                                      
REMARK 465     LYS A   765                                                      
REMARK 465     GLU A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     GLU A   768                                                      
REMARK 465     GLU A   769                                                      
REMARK 465     LYS A   770                                                      
REMARK 465     GLU A   771                                                      
REMARK 465     ARG A   772                                                      
REMARK 465     ASN A   773                                                      
REMARK 465     THR A   774                                                      
REMARK 465     ALA A   775                                                      
REMARK 465     ALA A   776                                                      
REMARK 465     MET A   777                                                      
REMARK 465     VAL A   778                                                      
REMARK 465     CYS A   779                                                      
REMARK 465     SER A   780                                                      
REMARK 465     LEU A   781                                                      
REMARK 465     GLU A   782                                                      
REMARK 465     ASN A   783                                                      
REMARK 465     ARG A   784                                                      
REMARK 465     ASP A   785                                                      
REMARK 465     GLU A   786                                                      
REMARK 465     CYS A   787                                                      
REMARK 465     LEU A   788                                                      
REMARK 465     MET A   789                                                      
REMARK 465     CYS A   790                                                      
REMARK 465     GLY A   791                                                      
REMARK 465     SER A   792                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     ARG B   293                                                      
REMARK 465     LEU B   630                                                      
REMARK 465     SER B   631                                                      
REMARK 465     PRO B   743                                                      
REMARK 465     ALA B   744                                                      
REMARK 465     ALA B   745                                                      
REMARK 465     ASN B   746                                                      
REMARK 465     PRO B   747                                                      
REMARK 465     ILE B   748                                                      
REMARK 465     GLN B   749                                                      
REMARK 465     PHE B   750                                                      
REMARK 465     THR B   751                                                      
REMARK 465     LEU B   752                                                      
REMARK 465     ASN B   753                                                      
REMARK 465     LYS B   754                                                      
REMARK 465     GLU B   755                                                      
REMARK 465     LYS B   756                                                      
REMARK 465     LEU B   757                                                      
REMARK 465     LYS B   758                                                      
REMARK 465     ASP B   759                                                      
REMARK 465     LYS B   760                                                      
REMARK 465     GLU B   761                                                      
REMARK 465     LYS B   762                                                      
REMARK 465     VAL B   763                                                      
REMARK 465     SER B   764                                                      
REMARK 465     LYS B   765                                                      
REMARK 465     GLU B   766                                                      
REMARK 465     GLU B   767                                                      
REMARK 465     GLU B   768                                                      
REMARK 465     GLU B   769                                                      
REMARK 465     LYS B   770                                                      
REMARK 465     GLU B   771                                                      
REMARK 465     ARG B   772                                                      
REMARK 465     ASN B   773                                                      
REMARK 465     THR B   774                                                      
REMARK 465     ALA B   775                                                      
REMARK 465     ALA B   776                                                      
REMARK 465     MET B   777                                                      
REMARK 465     VAL B   778                                                      
REMARK 465     CYS B   779                                                      
REMARK 465     SER B   780                                                      
REMARK 465     LEU B   781                                                      
REMARK 465     GLU B   782                                                      
REMARK 465     ASN B   783                                                      
REMARK 465     ARG B   784                                                      
REMARK 465     ASP B   785                                                      
REMARK 465     GLU B   786                                                      
REMARK 465     CYS B   787                                                      
REMARK 465     LEU B   788                                                      
REMARK 465     MET B   789                                                      
REMARK 465     CYS B   790                                                      
REMARK 465     GLY B   791                                                      
REMARK 465     SER B   792                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     GLU A  89    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
REMARK 470     HIS A 108    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     GLU A 181    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 212    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 244    OG                                                  
REMARK 470     LYS A 315    CG   CD   CE   NZ                                   
REMARK 470     LYS A 316    CG   CD   CE   NZ                                   
REMARK 470     GLU A 365    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 369    CG   CD   CE   NZ                                   
REMARK 470     LYS A 376    CG   CD   CE   NZ                                   
REMARK 470     LYS A 385    CG   CD   CE   NZ                                   
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     ASP A 577    CG   OD1  OD2                                       
REMARK 470     LYS A 582    CG   CD   CE   NZ                                   
REMARK 470     LYS A 590    CG   CD   CE   NZ                                   
REMARK 470     GLN A 609    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 627    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 628    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 633    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 654    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 658    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 675    CG   OD1  OD2                                       
REMARK 470     GLU A 714    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 719    CG   CD   CE   NZ                                   
REMARK 470     MET A 723    CG   SD   CE                                        
REMARK 470     LYS B  17    CG   CD   CE   NZ                                   
REMARK 470     ARG B  21    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     LYS B  42    CG   CD   CE   NZ                                   
REMARK 470     GLU B  62    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  70    CG   CD   CE   NZ                                   
REMARK 470     LYS B  88    CG   CD   CE   NZ                                   
REMARK 470     LYS B  92    CG   CD   CE   NZ                                   
REMARK 470     ASN B 106    CG   OD1  ND2                                       
REMARK 470     ASN B 109    CG   OD1  ND2                                       
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     LYS B 118    CG   CD   CE   NZ                                   
REMARK 470     ASP B 129    CG   OD1  OD2                                       
REMARK 470     ARG B 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 181    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 317    CG   OD1  ND2                                       
REMARK 470     LYS B 320    CG   CD   CE   NZ                                   
REMARK 470     GLU B 321    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 322    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 340    CG   CD   CE   NZ                                   
REMARK 470     LYS B 376    CG   CD   CE   NZ                                   
REMARK 470     LYS B 385    CG   CD   CE   NZ                                   
REMARK 470     GLU B 395    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 399    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 438    CG   CD   CE   NZ                                   
REMARK 470     GLU B 458    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 548    CG   CD   CE   NZ                                   
REMARK 470     LYS B 582    CG   CD   CE   NZ                                   
REMARK 470     GLU B 586    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 587    CG   CD   CE   NZ                                   
REMARK 470     GLN B 609    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 628    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 647    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 653    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 654    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 656    CG   CD   CE   NZ                                   
REMARK 470     GLN B 658    CG   CD   OE1  NE2                                  
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   CA   LEU A    86     CZ   PHE A   141              0.36            
REMARK 500   CG   HIS B    87     CZ   PHE B   141              0.52            
REMARK 500   OE2  GLU A    62     OH   TYR A   145              0.63            
REMARK 500   CG2  VAL A   278     CG   TYR B   285              0.64            
REMARK 500   ND2  ASN A   270     C    GLY B   289              0.71            
REMARK 500   C    THR B    90     NE   ARG B   166              0.85            
REMARK 500   CD2  TYR A   285     CG2  VAL B   278              0.99            
REMARK 500   ND2  ASN A   270     N    GLY B   290              1.00            
REMARK 500   NE2  HIS B    87     CG   PHE B   141              1.03            
REMARK 500   NE2  HIS B    87     CD2  PHE B   141              1.06            
REMARK 500   O    THR B    90     CZ   ARG B   166              1.06            
REMARK 500   N    LEU A    86     CE1  PHE A   141              1.08            
REMARK 500   ND1  HIS B    87     CZ   PHE B   141              1.14            
REMARK 500   ND2  ASN A   270     O    GLY B   289              1.52            
REMARK 500   O    THR B    90     NH2  ARG B   166              1.57            
REMARK 500   NH2  ARG A   277     NH1  ARG B   284              1.57            
REMARK 500   CG   ASN A   270     N    GLY B   290              1.61            
REMARK 500   CD2  LEU A    86     N    PHE A   141              1.62            
REMARK 500   CG2  THR B    90     OD1  ASP B   140              1.63            
REMARK 500   CE1  HIS B    87     CE1  PHE B   141              1.68            
REMARK 500   CG2  ILE A   228     CD   LYS B   243              1.69            
REMARK 500   O    THR B    90     NE   ARG B   166              1.69            
REMARK 500   OD1  ASN A   270     CA   GLY B   290              1.70            
REMARK 500   CB   VAL A   278     CD2  TYR B   285              1.74            
REMARK 500   CE1  HIS B    87     CG   PHE B   141              1.74            
REMARK 500   CD   GLU A    62     OH   TYR A   145              1.77            
REMARK 500   CB   LEU A    86     CZ   PHE A   141              1.77            
REMARK 500   O    GLU A    89     NH1  ARG A   166              1.78            
REMARK 500   O    LEU A    86     CE2  PHE A   141              1.78            
REMARK 500   CA   THR B    90     NE   ARG B   166              1.79            
REMARK 500   CE1  HIS B    87     CZ   PHE B   141              1.79            
REMARK 500   NE2  HIS B    87     CE1  PHE B   141              1.80            
REMARK 500   NE2  HIS B    87     CZ   PHE B   141              1.83            
REMARK 500   O    THR B    90     NH1  ARG B   166              1.83            
REMARK 500   CE1  HIS B    87     CD2  PHE B   141              1.84            
REMARK 500   CD1  TYR A   285     CG1  VAL B   278              1.85            
REMARK 500   CD2  LEU A    86     CG   PHE A   141              1.85            
REMARK 500   CG   HIS B    87     CE2  PHE B   141              1.86            
REMARK 500   CE1  HIS B    87     CE2  PHE B   141              1.87            
REMARK 500   CD2  LEU A    86     CA   PHE A   141              1.89            
REMARK 500   CG1  VAL A   278     CG   TYR B   285              1.91            
REMARK 500   CB   HIS B    87     CZ   PHE B   141              1.95            
REMARK 500   OH   TYR A   232     CB   VAL B   286              1.95            
REMARK 500   CA   THR B    90     CD   ARG B   166              1.95            
REMARK 500   CB   TYR A   285     CG2  VAL B   278              1.95            
REMARK 500   N    HIS A    87     CE2  PHE A   141              1.96            
REMARK 500   ND2  ASN A   270     CA   GLY B   289              1.98            
REMARK 500   CG2  VAL A   278     CD1  TYR B   285              2.00            
REMARK 500   OD1  ASN A   106     CD1  TYR B   261              2.01            
REMARK 500   CG   ASN A   270     C    GLY B   289              2.02            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      81 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD1  TYR A    27     CD1  TYR A    27    22554     0.73            
REMARK 500   CG   TYR A    27     CE1  TYR A    27    22554     0.90            
REMARK 500   CE2  TYR A    27     CZ   TYR A    27    22554     1.07            
REMARK 500   CD2  TYR A    27     CZ   TYR A    27    22554     1.15            
REMARK 500   CD2  TYR A    27     CE1  TYR A    27    22554     1.27            
REMARK 500   CE2  TYR A    27     CE2  TYR A    27    22554     1.27            
REMARK 500   CG   TYR A    27     CD1  TYR A    27    22554     1.45            
REMARK 500   CE   MET A    14     O    PHE B    15     9555     1.67            
REMARK 500   CD2  TYR A    27     OH   TYR A    27    22554     1.67            
REMARK 500   CD1  TYR A    27     CE1  TYR A    27    22554     1.69            
REMARK 500   CE   MET A    14     C    PHE B    15     9555     1.69            
REMARK 500   CE2  TYR A    27     OH   TYR A    27    22554     1.78            
REMARK 500   CB   ASP A    16     CG   MET B    14     9555     1.79            
REMARK 500   CG   MET A    14     CA   PHE B    15     9555     1.82            
REMARK 500   N    MET A    14     OD2  ASP B    16     9555     1.84            
REMARK 500   CG   MET A    14     CD2  PHE B    15     9555     1.86            
REMARK 500   CZ   TYR A    27     CZ   TYR A    27    22554     1.93            
REMARK 500   CB   MET A    14     C    PHE B    15     9555     1.95            
REMARK 500   CD2  PHE A    15     O    VAL B    13     9555     1.96            
REMARK 500   SD   MET A    14     CG   PHE B    15     9555     2.03            
REMARK 500   CG   MET A    14     C    PHE B    15     9555     2.04            
REMARK 500   CG   TYR A    27     CZ   TYR A    27    22554     2.04            
REMARK 500   SD   MET A    14     CA   PHE B    15     9555     2.05            
REMARK 500   CB   TYR A    27     CE1  TYR A    27    22554     2.06            
REMARK 500   N    MET A    14     CG   ASP B    16     9555     2.08            
REMARK 500   CB   MET A    14     CB   PHE B    15     9555     2.09            
REMARK 500   SD   MET A    14     CD2  PHE B    15     9555     2.10            
REMARK 500   CE1  TYR A    27     CE2  TYR A    27    22554     2.12            
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    ARG A 499   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU B 220   CA  -  CB  -  CG  ANGL. DEV. =  16.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 180     -112.23     54.25                                   
REMARK 500    LYS A 224      -94.60    -60.23                                   
REMARK 500    ALA A 245       -0.15     58.22                                   
REMARK 500    ASP A 287      -72.96    -82.57                                   
REMARK 500    PRO A 303       -4.68    -57.79                                   
REMARK 500    LEU A 312       41.63    -71.30                                   
REMARK 500    ASP A 313      -19.46   -157.92                                   
REMARK 500    SER A 426     -163.07   -112.76                                   
REMARK 500    ALA A 600       81.46   -160.74                                   
REMARK 500    PRO A 601      104.03    -55.85                                   
REMARK 500    SER A 616     -133.20     58.93                                   
REMARK 500    LEU A 630     -113.36     53.00                                   
REMARK 500    ASN A 638      114.14    -38.62                                   
REMARK 500    GLN A 704     -123.16   -105.60                                   
REMARK 500    SER A 705     -164.72   -129.77                                   
REMARK 500    TYR A 737      -93.77    -79.07                                   
REMARK 500    GLN B  45      -71.13    -54.11                                   
REMARK 500    LYS B 180     -121.24     35.29                                   
REMARK 500    LYS B 224      -82.94    -57.05                                   
REMARK 500    LYS B 320       19.67   -158.08                                   
REMARK 500    GLU B 321      -60.41     61.26                                   
REMARK 500    SER B 426     -164.51   -110.24                                   
REMARK 500    ASN B 427     -169.75   -105.40                                   
REMARK 500    LEU B 598      -46.62   -133.07                                   
REMARK 500    ALA B 600       83.53   -160.39                                   
REMARK 500    PRO B 601       99.56    -56.33                                   
REMARK 500    SER B 616     -132.62     54.63                                   
REMARK 500    GLN B 704     -133.54   -102.08                                   
REMARK 500    TYR B 737      -98.03    -86.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5D1Y A    1   792  UNP    P23921   RIR1_HUMAN       1    792             
DBREF  5D1Y B    1   792  UNP    P23921   RIR1_HUMAN       1    792             
SEQADV 5D1Y MET A  -19  UNP  P23921              INITIATING METHIONINE          
SEQADV 5D1Y GLY A  -18  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER A  -17  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER A  -16  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS A  -15  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS A  -14  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS A  -13  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS A  -12  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS A  -11  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS A  -10  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER A   -9  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER A   -8  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y GLY A   -7  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y LEU A   -6  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y VAL A   -5  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y PRO A   -4  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y ARG A   -3  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y GLY A   -2  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER A   -1  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS A    0  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y MET B  -19  UNP  P23921              INITIATING METHIONINE          
SEQADV 5D1Y GLY B  -18  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER B  -17  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER B  -16  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS B  -15  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS B  -14  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS B  -13  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS B  -12  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS B  -11  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS B  -10  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER B   -9  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER B   -8  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y GLY B   -7  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y LEU B   -6  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y VAL B   -5  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y PRO B   -4  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y ARG B   -3  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y GLY B   -2  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y SER B   -1  UNP  P23921              EXPRESSION TAG                 
SEQADV 5D1Y HIS B    0  UNP  P23921              EXPRESSION TAG                 
SEQRES   1 A  812  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  812  LEU VAL PRO ARG GLY SER HIS MET HIS VAL ILE LYS ARG          
SEQRES   3 A  812  ASP GLY ARG GLN GLU ARG VAL MET PHE ASP LYS ILE THR          
SEQRES   4 A  812  SER ARG ILE GLN LYS LEU CYS TYR GLY LEU ASN MET ASP          
SEQRES   5 A  812  PHE VAL ASP PRO ALA GLN ILE THR MET LYS VAL ILE GLN          
SEQRES   6 A  812  GLY LEU TYR SER GLY VAL THR THR VAL GLU LEU ASP THR          
SEQRES   7 A  812  LEU ALA ALA GLU THR ALA ALA THR LEU THR THR LYS HIS          
SEQRES   8 A  812  PRO ASP TYR ALA ILE LEU ALA ALA ARG ILE ALA VAL SER          
SEQRES   9 A  812  ASN LEU HIS LYS GLU THR LYS LYS VAL PHE SER ASP VAL          
SEQRES  10 A  812  MET GLU ASP LEU TYR ASN TYR ILE ASN PRO HIS ASN GLY          
SEQRES  11 A  812  LYS HIS SER PRO MET VAL ALA LYS SER THR LEU ASP ILE          
SEQRES  12 A  812  VAL LEU ALA ASN LYS ASP ARG LEU ASN SER ALA ILE ILE          
SEQRES  13 A  812  TYR ASP ARG ASP PHE SER TYR ASN TYR PHE GLY PHE LYS          
SEQRES  14 A  812  THR LEU GLU ARG SER TYR LEU LEU LYS ILE ASN GLY LYS          
SEQRES  15 A  812  VAL ALA GLU ARG PRO GLN HIS MET LEU MET ARG VAL SER          
SEQRES  16 A  812  VAL GLY ILE HIS LYS GLU ASP ILE ASP ALA ALA ILE GLU          
SEQRES  17 A  812  THR TYR ASN LEU LEU SER GLU ARG TRP PHE THR HIS ALA          
SEQRES  18 A  812  SER PRO THR LEU PHE ASN ALA GLY THR ASN ARG PRO GLN          
SEQRES  19 A  812  LEU SER SER CYS PHE LEU LEU SER MET LYS ASP ASP SER          
SEQRES  20 A  812  ILE GLU GLY ILE TYR ASP THR LEU LYS GLN CYS ALA LEU          
SEQRES  21 A  812  ILE SER LYS SER ALA GLY GLY ILE GLY VAL ALA VAL SER          
SEQRES  22 A  812  CYS ILE ARG ALA THR GLY SER TYR ILE ALA GLY THR ASN          
SEQRES  23 A  812  GLY ASN SER ASN GLY LEU VAL PRO MET LEU ARG VAL TYR          
SEQRES  24 A  812  ASN ASN THR ALA ARG TYR VAL ASP GLN GLY GLY ASN LYS          
SEQRES  25 A  812  ARG PRO GLY ALA PHE ALA ILE TYR LEU GLU PRO TRP HIS          
SEQRES  26 A  812  LEU ASP ILE PHE GLU PHE LEU ASP LEU LYS LYS ASN THR          
SEQRES  27 A  812  GLY LYS GLU GLU GLN ARG ALA ARG ASP LEU PHE PHE ALA          
SEQRES  28 A  812  LEU TRP ILE PRO ASP LEU PHE MET LYS ARG VAL GLU THR          
SEQRES  29 A  812  ASN GLN ASP TRP SER LEU MET CYS PRO ASN GLU CYS PRO          
SEQRES  30 A  812  GLY LEU ASP GLU VAL TRP GLY GLU GLU PHE GLU LYS LEU          
SEQRES  31 A  812  TYR ALA SER TYR GLU LYS GLN GLY ARG VAL ARG LYS VAL          
SEQRES  32 A  812  VAL LYS ALA GLN GLN LEU TRP TYR ALA ILE ILE GLU SER          
SEQRES  33 A  812  GLN THR GLU THR GLY THR PRO TYR MET LEU TYR LYS ASP          
SEQRES  34 A  812  SER CYS ASN ARG LYS SER ASN GLN GLN ASN LEU GLY THR          
SEQRES  35 A  812  ILE LYS CYS SER ASN LEU CYS THR GLU ILE VAL GLU TYR          
SEQRES  36 A  812  THR SER LYS ASP GLU VAL ALA VAL CYS ASN LEU ALA SER          
SEQRES  37 A  812  LEU ALA LEU ASN MET TYR VAL THR SER GLU HIS THR TYR          
SEQRES  38 A  812  ASP PHE LYS LYS LEU ALA GLU VAL THR LYS VAL VAL VAL          
SEQRES  39 A  812  ARG ASN LEU ASN LYS ILE ILE ASP ILE ASN TYR TYR PRO          
SEQRES  40 A  812  VAL PRO GLU ALA CYS LEU SER ASN LYS ARG HIS ARG PRO          
SEQRES  41 A  812  ILE GLY ILE GLY VAL GLN GLY LEU ALA ASP ALA PHE ILE          
SEQRES  42 A  812  LEU MET ARG TYR PRO PHE GLU SER ALA GLU ALA GLN LEU          
SEQRES  43 A  812  LEU ASN LYS GLN ILE PHE GLU THR ILE TYR TYR GLY ALA          
SEQRES  44 A  812  LEU GLU ALA SER CYS ASP LEU ALA LYS GLU GLN GLY PRO          
SEQRES  45 A  812  TYR GLU THR TYR GLU GLY SER PRO VAL SER LYS GLY ILE          
SEQRES  46 A  812  LEU GLN TYR ASP MET TRP ASN VAL THR PRO THR ASP LEU          
SEQRES  47 A  812  TRP ASP TRP LYS VAL LEU LYS GLU LYS ILE ALA LYS TYR          
SEQRES  48 A  812  GLY ILE ARG ASN SER LEU LEU ILE ALA PRO MET PRO THR          
SEQRES  49 A  812  ALA SER THR ALA GLN ILE LEU GLY ASN ASN GLU SER ILE          
SEQRES  50 A  812  GLU PRO TYR THR SER ASN ILE TYR THR ARG ARG VAL LEU          
SEQRES  51 A  812  SER GLY GLU PHE GLN ILE VAL ASN PRO HIS LEU LEU LYS          
SEQRES  52 A  812  ASP LEU THR GLU ARG GLY LEU TRP HIS GLU GLU MET LYS          
SEQRES  53 A  812  ASN GLN ILE ILE ALA CYS ASN GLY SER ILE GLN SER ILE          
SEQRES  54 A  812  PRO GLU ILE PRO ASP ASP LEU LYS GLN LEU TYR LYS THR          
SEQRES  55 A  812  VAL TRP GLU ILE SER GLN LYS THR VAL LEU LYS MET ALA          
SEQRES  56 A  812  ALA GLU ARG GLY ALA PHE ILE ASP GLN SER GLN SER LEU          
SEQRES  57 A  812  ASN ILE HIS ILE ALA GLU PRO ASN TYR GLY LYS LEU THR          
SEQRES  58 A  812  SER MET HIS PHE TYR GLY TRP LYS GLN GLY LEU LYS THR          
SEQRES  59 A  812  GLY MET TYR TYR LEU ARG THR ARG PRO ALA ALA ASN PRO          
SEQRES  60 A  812  ILE GLN PHE THR LEU ASN LYS GLU LYS LEU LYS ASP LYS          
SEQRES  61 A  812  GLU LYS VAL SER LYS GLU GLU GLU GLU LYS GLU ARG ASN          
SEQRES  62 A  812  THR ALA ALA MET VAL CYS SER LEU GLU ASN ARG ASP GLU          
SEQRES  63 A  812  CYS LEU MET CYS GLY SER                                      
SEQRES   1 B  812  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  812  LEU VAL PRO ARG GLY SER HIS MET HIS VAL ILE LYS ARG          
SEQRES   3 B  812  ASP GLY ARG GLN GLU ARG VAL MET PHE ASP LYS ILE THR          
SEQRES   4 B  812  SER ARG ILE GLN LYS LEU CYS TYR GLY LEU ASN MET ASP          
SEQRES   5 B  812  PHE VAL ASP PRO ALA GLN ILE THR MET LYS VAL ILE GLN          
SEQRES   6 B  812  GLY LEU TYR SER GLY VAL THR THR VAL GLU LEU ASP THR          
SEQRES   7 B  812  LEU ALA ALA GLU THR ALA ALA THR LEU THR THR LYS HIS          
SEQRES   8 B  812  PRO ASP TYR ALA ILE LEU ALA ALA ARG ILE ALA VAL SER          
SEQRES   9 B  812  ASN LEU HIS LYS GLU THR LYS LYS VAL PHE SER ASP VAL          
SEQRES  10 B  812  MET GLU ASP LEU TYR ASN TYR ILE ASN PRO HIS ASN GLY          
SEQRES  11 B  812  LYS HIS SER PRO MET VAL ALA LYS SER THR LEU ASP ILE          
SEQRES  12 B  812  VAL LEU ALA ASN LYS ASP ARG LEU ASN SER ALA ILE ILE          
SEQRES  13 B  812  TYR ASP ARG ASP PHE SER TYR ASN TYR PHE GLY PHE LYS          
SEQRES  14 B  812  THR LEU GLU ARG SER TYR LEU LEU LYS ILE ASN GLY LYS          
SEQRES  15 B  812  VAL ALA GLU ARG PRO GLN HIS MET LEU MET ARG VAL SER          
SEQRES  16 B  812  VAL GLY ILE HIS LYS GLU ASP ILE ASP ALA ALA ILE GLU          
SEQRES  17 B  812  THR TYR ASN LEU LEU SER GLU ARG TRP PHE THR HIS ALA          
SEQRES  18 B  812  SER PRO THR LEU PHE ASN ALA GLY THR ASN ARG PRO GLN          
SEQRES  19 B  812  LEU SER SER CYS PHE LEU LEU SER MET LYS ASP ASP SER          
SEQRES  20 B  812  ILE GLU GLY ILE TYR ASP THR LEU LYS GLN CYS ALA LEU          
SEQRES  21 B  812  ILE SER LYS SER ALA GLY GLY ILE GLY VAL ALA VAL SER          
SEQRES  22 B  812  CYS ILE ARG ALA THR GLY SER TYR ILE ALA GLY THR ASN          
SEQRES  23 B  812  GLY ASN SER ASN GLY LEU VAL PRO MET LEU ARG VAL TYR          
SEQRES  24 B  812  ASN ASN THR ALA ARG TYR VAL ASP GLN GLY GLY ASN LYS          
SEQRES  25 B  812  ARG PRO GLY ALA PHE ALA ILE TYR LEU GLU PRO TRP HIS          
SEQRES  26 B  812  LEU ASP ILE PHE GLU PHE LEU ASP LEU LYS LYS ASN THR          
SEQRES  27 B  812  GLY LYS GLU GLU GLN ARG ALA ARG ASP LEU PHE PHE ALA          
SEQRES  28 B  812  LEU TRP ILE PRO ASP LEU PHE MET LYS ARG VAL GLU THR          
SEQRES  29 B  812  ASN GLN ASP TRP SER LEU MET CYS PRO ASN GLU CYS PRO          
SEQRES  30 B  812  GLY LEU ASP GLU VAL TRP GLY GLU GLU PHE GLU LYS LEU          
SEQRES  31 B  812  TYR ALA SER TYR GLU LYS GLN GLY ARG VAL ARG LYS VAL          
SEQRES  32 B  812  VAL LYS ALA GLN GLN LEU TRP TYR ALA ILE ILE GLU SER          
SEQRES  33 B  812  GLN THR GLU THR GLY THR PRO TYR MET LEU TYR LYS ASP          
SEQRES  34 B  812  SER CYS ASN ARG LYS SER ASN GLN GLN ASN LEU GLY THR          
SEQRES  35 B  812  ILE LYS CYS SER ASN LEU CYS THR GLU ILE VAL GLU TYR          
SEQRES  36 B  812  THR SER LYS ASP GLU VAL ALA VAL CYS ASN LEU ALA SER          
SEQRES  37 B  812  LEU ALA LEU ASN MET TYR VAL THR SER GLU HIS THR TYR          
SEQRES  38 B  812  ASP PHE LYS LYS LEU ALA GLU VAL THR LYS VAL VAL VAL          
SEQRES  39 B  812  ARG ASN LEU ASN LYS ILE ILE ASP ILE ASN TYR TYR PRO          
SEQRES  40 B  812  VAL PRO GLU ALA CYS LEU SER ASN LYS ARG HIS ARG PRO          
SEQRES  41 B  812  ILE GLY ILE GLY VAL GLN GLY LEU ALA ASP ALA PHE ILE          
SEQRES  42 B  812  LEU MET ARG TYR PRO PHE GLU SER ALA GLU ALA GLN LEU          
SEQRES  43 B  812  LEU ASN LYS GLN ILE PHE GLU THR ILE TYR TYR GLY ALA          
SEQRES  44 B  812  LEU GLU ALA SER CYS ASP LEU ALA LYS GLU GLN GLY PRO          
SEQRES  45 B  812  TYR GLU THR TYR GLU GLY SER PRO VAL SER LYS GLY ILE          
SEQRES  46 B  812  LEU GLN TYR ASP MET TRP ASN VAL THR PRO THR ASP LEU          
SEQRES  47 B  812  TRP ASP TRP LYS VAL LEU LYS GLU LYS ILE ALA LYS TYR          
SEQRES  48 B  812  GLY ILE ARG ASN SER LEU LEU ILE ALA PRO MET PRO THR          
SEQRES  49 B  812  ALA SER THR ALA GLN ILE LEU GLY ASN ASN GLU SER ILE          
SEQRES  50 B  812  GLU PRO TYR THR SER ASN ILE TYR THR ARG ARG VAL LEU          
SEQRES  51 B  812  SER GLY GLU PHE GLN ILE VAL ASN PRO HIS LEU LEU LYS          
SEQRES  52 B  812  ASP LEU THR GLU ARG GLY LEU TRP HIS GLU GLU MET LYS          
SEQRES  53 B  812  ASN GLN ILE ILE ALA CYS ASN GLY SER ILE GLN SER ILE          
SEQRES  54 B  812  PRO GLU ILE PRO ASP ASP LEU LYS GLN LEU TYR LYS THR          
SEQRES  55 B  812  VAL TRP GLU ILE SER GLN LYS THR VAL LEU LYS MET ALA          
SEQRES  56 B  812  ALA GLU ARG GLY ALA PHE ILE ASP GLN SER GLN SER LEU          
SEQRES  57 B  812  ASN ILE HIS ILE ALA GLU PRO ASN TYR GLY LYS LEU THR          
SEQRES  58 B  812  SER MET HIS PHE TYR GLY TRP LYS GLN GLY LEU LYS THR          
SEQRES  59 B  812  GLY MET TYR TYR LEU ARG THR ARG PRO ALA ALA ASN PRO          
SEQRES  60 B  812  ILE GLN PHE THR LEU ASN LYS GLU LYS LEU LYS ASP LYS          
SEQRES  61 B  812  GLU LYS VAL SER LYS GLU GLU GLU GLU LYS GLU ARG ASN          
SEQRES  62 B  812  THR ALA ALA MET VAL CYS SER LEU GLU ASN ARG ASP GLU          
SEQRES  63 B  812  CYS LEU MET CYS GLY SER                                      
HELIX    1 AA1 MET A   14  LYS A   24  1                                  11    
HELIX    2 AA2 ASP A   35  GLN A   45  1                                  11    
HELIX    3 AA3 THR A   52  LEU A   67  1                                  16    
HELIX    4 AA4 THR A   68  HIS A   71  5                                   4    
HELIX    5 AA5 PRO A   72  GLU A   89  1                                  18    
HELIX    6 AA6 VAL A   93  ASN A  103  1                                  11    
HELIX    7 AA7 ALA A  117  ASN A  127  1                                  11    
HELIX    8 AA8 ASN A  127  ILE A  135  1                                   9    
HELIX    9 AA9 ILE A  136  TYR A  143  5                                   8    
HELIX   10 AB1 ASN A  144  TYR A  155  1                                  12    
HELIX   11 AB2 ARG A  166  LYS A  180  1                                  15    
HELIX   12 AB3 ASP A  182  GLU A  195  1                                  14    
HELIX   13 AB4 ALA A  201  ALA A  208  1                                   8    
HELIX   14 AB5 SER A  227  SER A  244  1                                  18    
HELIX   15 AB6 LEU A  272  VAL A  286  1                                  15    
HELIX   16 AB7 ASP A  307  LEU A  312  1                                   6    
HELIX   17 AB8 PRO A  335  THR A  344  1                                  10    
HELIX   18 AB9 GLY A  358  VAL A  362  5                                   5    
HELIX   19 AC1 TRP A  363  GLN A  377  1                                  15    
HELIX   20 AC2 ALA A  386  GLY A  401  1                                  16    
HELIX   21 AC3 LYS A  408  LYS A  414  1                                   7    
HELIX   22 AC4 GLN A  417  GLY A  421  5                                   5    
HELIX   23 AC5 ASN A  452  VAL A  455  5                                   4    
HELIX   24 AC6 ASP A  462  ASN A  484  1                                  23    
HELIX   25 AC7 VAL A  488  ARG A  499  1                                  12    
HELIX   26 AC8 GLY A  507  MET A  515  1                                   9    
HELIX   27 AC9 SER A  521  GLY A  551  1                                  31    
HELIX   28 AD1 SER A  559  GLY A  564  5                                   6    
HELIX   29 AD2 LEU A  566  TRP A  571  1                                   6    
HELIX   30 AD3 ASP A  580  GLY A  592  1                                  13    
HELIX   31 AD4 THR A  604  GLY A  612  1                                   9    
HELIX   32 AD5 ASN A  638  ARG A  648  1                                  11    
HELIX   33 AD6 HIS A  652  CYS A  662  1                                  11    
HELIX   34 AD7 PRO A  673  TYR A  680  1                                   8    
HELIX   35 AD8 SER A  687  ALA A  700  1                                  14    
HELIX   36 AD9 ASN A  716  GLN A  730  1                                  15    
HELIX   37 AE1 MET B   14  LYS B   24  1                                  11    
HELIX   38 AE2 ASP B   35  GLY B   46  1                                  12    
HELIX   39 AE3 THR B   53  LEU B   67  1                                  15    
HELIX   40 AE4 THR B   68  HIS B   71  5                                   4    
HELIX   41 AE5 PRO B   72  GLU B   89  1                                  18    
HELIX   42 AE6 VAL B   93  ASN B  103  1                                  11    
HELIX   43 AE7 ALA B  117  ASN B  127  1                                  11    
HELIX   44 AE8 ASN B  127  ILE B  135  1                                   9    
HELIX   45 AE9 ILE B  136  TYR B  143  5                                   8    
HELIX   46 AF1 ASN B  144  TYR B  155  1                                  12    
HELIX   47 AF2 ARG B  166  LYS B  180  1                                  15    
HELIX   48 AF3 ASP B  182  GLU B  195  1                                  14    
HELIX   49 AF4 ALA B  201  ALA B  208  1                                   8    
HELIX   50 AF5 SER B  227  SER B  244  1                                  18    
HELIX   51 AF6 GLY B  271  VAL B  286  1                                  16    
HELIX   52 AF7 ASP B  307  LEU B  312  1                                   6    
HELIX   53 AF8 PRO B  335  ASN B  345  1                                  11    
HELIX   54 AF9 GLY B  358  VAL B  362  5                                   5    
HELIX   55 AG1 TRP B  363  GLN B  377  1                                  15    
HELIX   56 AG2 ALA B  386  GLY B  401  1                                  16    
HELIX   57 AG3 LYS B  408  LYS B  414  1                                   7    
HELIX   58 AG4 GLN B  417  GLY B  421  5                                   5    
HELIX   59 AG5 ASN B  452  VAL B  455  5                                   4    
HELIX   60 AG6 ASP B  462  ASN B  484  1                                  23    
HELIX   61 AG7 VAL B  488  ARG B  499  1                                  12    
HELIX   62 AG8 GLY B  507  MET B  515  1                                   9    
HELIX   63 AG9 SER B  521  GLY B  551  1                                  31    
HELIX   64 AH1 PRO B  560  GLY B  564  5                                   5    
HELIX   65 AH2 LEU B  566  TRP B  571  1                                   6    
HELIX   66 AH3 ASP B  580  GLY B  592  1                                  13    
HELIX   67 AH4 THR B  604  GLY B  612  1                                   9    
HELIX   68 AH5 ASN B  638  ARG B  648  1                                  11    
HELIX   69 AH6 HIS B  652  ALA B  661  1                                  10    
HELIX   70 AH7 PRO B  673  TYR B  680  1                                   8    
HELIX   71 AH8 SER B  687  ALA B  700  1                                  14    
HELIX   72 AH9 ASN B  716  GLY B  731  1                                  16    
SHEET    1 AA1 2 LYS A 158  ILE A 159  0                                        
SHEET    2 AA1 2 LYS A 162  VAL A 163 -1  O  LYS A 162   N  ILE A 159           
SHEET    1 AA2 3 PHE A 198  HIS A 200  0                                        
SHEET    2 AA2 3 LEU A 446  ALA A 450 -1  O  SER A 448   N  THR A 199           
SHEET    3 AA2 3 GLY A 502  GLN A 506  1  O  GLY A 504   N  ALA A 447           
SHEET    1 AA3 7 ALA A 442  CYS A 444  0                                        
SHEET    2 AA3 7 CYS A 218  SER A 222 -1  N  LEU A 220   O  ALA A 442           
SHEET    3 AA3 7 GLY A 247  ALA A 251  1  O  GLY A 249   N  LEU A 221           
SHEET    4 AA3 7 PHE A 297  LEU A 301  1  O  ALA A 298   N  ILE A 248           
SHEET    5 AA3 7 LEU A 328  ILE A 334  1  O  PHE A 329   N  ILE A 299           
SHEET    6 AA3 7 TYR A 404  TYR A 407  1  O  LEU A 406   N  ILE A 334           
SHEET    7 AA3 7 THR A 734  MET A 736 -1  O  MET A 736   N  MET A 405           
SHEET    1 AA4 2 TYR A 261  ILE A 262  0                                        
SHEET    2 AA4 2 GLY A 267  ASN A 268 -1  O  GLY A 267   N  ILE A 262           
SHEET    1 AA5 2 ASP A 347  LEU A 350  0                                        
SHEET    2 AA5 2 LYS A 382  LYS A 385 -1  O  LYS A 382   N  LEU A 350           
SHEET    1 AA6 2 ILE A 624  VAL A 629  0                                        
SHEET    2 AA6 2 GLY A 632  VAL A 637 -1  O  ILE A 636   N  TYR A 625           
SHEET    1 AA7 2 ILE A 710  HIS A 711  0                                        
SHEET    2 AA7 2 LEU A 739  ARG A 740  1  O  ARG A 740   N  ILE A 710           
SHEET    1 AA8 3 GLN B  10  ARG B  12  0                                        
SHEET    2 AA8 3 HIS B   2  ILE B   4 -1  N  VAL B   3   O  GLU B  11           
SHEET    3 AA8 3 VAL B  51  THR B  52  1  O  VAL B  51   N  ILE B   4           
SHEET    1 AA9 2 LYS B 158  ILE B 159  0                                        
SHEET    2 AA9 2 LYS B 162  VAL B 163 -1  O  LYS B 162   N  ILE B 159           
SHEET    1 AB1 3 PHE B 198  HIS B 200  0                                        
SHEET    2 AB1 3 LEU B 446  ALA B 450 -1  O  SER B 448   N  THR B 199           
SHEET    3 AB1 3 GLY B 502  GLN B 506  1  O  GLY B 504   N  ALA B 447           
SHEET    1 AB2 7 ALA B 442  CYS B 444  0                                        
SHEET    2 AB2 7 CYS B 218  SER B 222 -1  N  CYS B 218   O  CYS B 444           
SHEET    3 AB2 7 GLY B 247  ALA B 251  1  O  GLY B 249   N  LEU B 221           
SHEET    4 AB2 7 PHE B 297  LEU B 301  1  O  TYR B 300   N  VAL B 250           
SHEET    5 AB2 7 PHE B 329  ILE B 334  1  O  PHE B 329   N  ILE B 299           
SHEET    6 AB2 7 TYR B 404  TYR B 407  1  O  LEU B 406   N  ILE B 334           
SHEET    7 AB2 7 THR B 734  MET B 736 -1  O  MET B 736   N  MET B 405           
SHEET    1 AB3 2 TYR B 261  ILE B 262  0                                        
SHEET    2 AB3 2 GLY B 267  ASN B 268 -1  O  GLY B 267   N  ILE B 262           
SHEET    1 AB4 2 ASP B 347  LEU B 350  0                                        
SHEET    2 AB4 2 LYS B 382  LYS B 385 -1  O  LYS B 382   N  LEU B 350           
SHEET    1 AB5 2 ILE B 624  ARG B 627  0                                        
SHEET    2 AB5 2 PHE B 634  VAL B 637 -1  O  ILE B 636   N  TYR B 625           
SHEET    1 AB6 2 ILE B 710  HIS B 711  0                                        
SHEET    2 AB6 2 LEU B 739  ARG B 740  1  O  ARG B 740   N  ILE B 710           
LINK         OE2 GLU A  62                 CZ  TYR A 145     1555   1555  1.38  
LINK         N   LEU A  86                 CZ  PHE A 141     1555   1555  1.35  
LINK         CA  LEU A  86                 CE1 PHE A 141     1555   1555  1.24  
LINK         CA  LEU A  86                 CE2 PHE A 141     1555   1555  1.41  
LINK         C   LEU A  86                 CE2 PHE A 141     1555   1555  1.11  
LINK         C   LEU A  86                 CZ  PHE A 141     1555   1555  1.30  
LINK         CB  LEU A  86                 CG  PHE A 141     1555   1555  1.11  
LINK         CB  LEU A  86                 CD1 PHE A 141     1555   1555  1.26  
LINK         CB  LEU A  86                 CD2 PHE A 141     1555   1555  1.30  
LINK         CB  LEU A  86                 CE1 PHE A 141     1555   1555  1.61  
LINK         CB  LEU A  86                 CE2 PHE A 141     1555   1555  1.63  
LINK         CG  LEU A  86                 CG  PHE A 141     1555   1555  1.65  
LINK         CG  LEU A  86                 CD2 PHE A 141     1555   1555  1.20  
LINK         CD2 LEU A  86                 CB  PHE A 141     1555   1555  1.61  
LINK         CG2 THR A  90                 C   TYR A 137     1555   1555  1.60  
LINK         CG2 THR A  90                 O   TYR A 137     1555   1555  1.40  
LINK         CG  ASN A 106                 CE1 TYR B 261     1555   1555  1.58  
LINK         OD1 ASN A 106                 CE1 TYR B 261     1555   1555  1.36  
LINK         CG  ASN A 270                 CA  GLY B 290     1555   1555  1.64  
LINK         CB  VAL A 278                 CD1 TYR B 285     1555   1555  1.60  
LINK         CB  VAL A 278                 CG  TYR B 285     1555   1555  1.11  
LINK         CG1 VAL A 278                 CD1 TYR B 285     1555   1555  1.15  
LINK         CG2 VAL A 278                 CB  TYR B 285     1555   1555  1.20  
LINK         CG2 VAL A 278                 CD2 TYR B 285     1555   1555  1.38  
LINK         CG  TYR A 285                 CG2 VAL B 278     1555   1555  1.28  
LINK         CG  HIS B  87                 CE1 PHE B 141     1555   1555  1.38  
LINK         ND1 HIS B  87                 CE1 PHE B 141     1555   1555  1.38  
LINK         CD2 HIS B  87                 CE2 PHE B 141     1555   1555  1.51  
LINK         CD2 HIS B  87                 CE1 PHE B 141     1555   1555  1.64  
LINK         CD2 HIS B  87                 CZ  PHE B 141     1555   1555  1.25  
LINK         CE1 HIS B  87                 CD1 PHE B 141     1555   1555  1.64  
LINK         NE2 HIS B  87                 CE2 PHE B 141     1555   1555  1.51  
LINK         NE2 HIS B  87                 CD1 PHE B 141     1555   1555  1.43  
LINK         C   THR B  90                 CD  ARG B 166     1555   1555  1.57  
LINK         C   THR B  90                 CZ  ARG B 166     1555   1555  1.36  
LINK         CB  MET A  14                 N   ASP B  16     1555   9555  1.46  
LINK         CG  MET A  14                 CG  PHE B  15     1555   9555  1.50  
LINK         CG  MET A  14                 CB  PHE B  15     1555   9555  1.07  
LINK         SD  MET A  14                 C   PHE B  15     1555   9555  1.69  
LINK         SD  MET A  14                 O   PHE B  15     1555   9555  1.53  
LINK         CE  MET A  14                 CA  PHE B  15     1555   9555  1.51  
LINK         CB  ASP A  16                 SD  MET B  14     1555   9555  1.95  
CISPEP   1 THR A  402    PRO A  403          0         7.16                     
CISPEP   2 THR B  402    PRO B  403          0        11.39                     
CRYST1  356.010  356.010  356.010  90.00  90.00  90.00 P 41 3 2     48          
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      0.002809  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002809        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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