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Database: PDB
Entry: 3K70
LinkDB: 3K70
Original site: 3K70 
HEADER    HYDROLASE/DNA                           11-OCT-09   3K70              
TITLE     CRYSTAL STRUCTURE OF THE COMPLETE INITIATION COMPLEX OF               
TITLE    2 RECBCD                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXODEOXYRIBONUCLEASE V BETA CHAIN;                         
COMPND   3 CHAIN: B, E;                                                         
COMPND   4 SYNONYM: EXODEOXYRIBONUCLEASE V 135 KDA POLYPEPTIDE;                 
COMPND   5 EC: 3.1.11.5;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EXODEOXYRIBONUCLEASE V GAMMA CHAIN;                        
COMPND   9 CHAIN: C, F;                                                         
COMPND  10 SYNONYM: EXODEOXYRIBONUCLEASE V 125 KDA POLYPEPTIDE;                 
COMPND  11 EC: 3.1.11.5;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: EXODEOXYRIBONUCLEASE V ALPHA CHAIN;                        
COMPND  15 CHAIN: D, G;                                                         
COMPND  16 SYNONYM: EXODEOXYRIBONUCLEASE V 67 KDA POLYPEPTIDE;                  
COMPND  17 EC: 3.1.11.5;                                                        
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: DNA (46-MER);                                              
COMPND  21 CHAIN: X, Y;                                                         
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 OTHER_DETAILS: DNA HAIRPIN                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B2820, JW2788, RECB, RORA;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  11 ORGANISM_TAXID: 83333;                                               
SOURCE  12 STRAIN: K12;                                                         
SOURCE  13 GENE: B2822, JW2790, RECC;                                           
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  19 ORGANISM_TAXID: 83333;                                               
SOURCE  20 STRAIN: K12;                                                         
SOURCE  21 GENE: B2819, JW2787, RECD;                                           
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 SYNTHETIC: YES;                                                      
SOURCE  27 OTHER_DETAILS: SYNTHESIZED DNA                                       
KEYWDS    RECOMBINATION, HELICASE, NUCLEASE, HYDROLASE, DNA REPAIR,             
KEYWDS   2 ATP-BINDING, DNA DAMAGE, ENDONUCLEASE, EXONUCLEASE,                  
KEYWDS   3 NUCLEOTIDE-BINDING, HYDROLASE/DNA COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SAIKRISHNAN,D.B.WIGLEY                                              
REVDAT   1   10-NOV-09 3K70    0                                                
JRNL        AUTH   K.SAIKRISHNAN,S.P.GRIFFITHS,N.COOK,R.COURT,                  
JRNL        AUTH 2 D.B.WIGLEY                                                   
JRNL        TITL   DNA BINDING TO RECD: ROLE OF THE 1B DOMAIN IN SF1B           
JRNL        TITL 2 HELICASE ACTIVITY.                                           
JRNL        REF    EMBO J.                       V.  27  2222 2008              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   18668125                                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.R.SINGLETON,M.S.DILLINGHAM,M.GAUDIER,                      
REMARK   1  AUTH 2 S.C.KOWALCZYKOWSKI,D.B.WIGLEY                                
REMARK   1  TITL   CRYSTAL STRUCTURE OF RECBCD ENZYME REVEALS A                 
REMARK   1  TITL 2 MACHINE FOR PROCESSING DNA BREAKS.                           
REMARK   1  REF    NATURE                        V. 432   187 2004              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   15538360                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 97231                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4709                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.83                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 773                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 45060                                   
REMARK   3   NUCLEIC ACID ATOMS       : 1870                                    
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3K70 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055625.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-06                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 97332                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1W36                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.0, 300 MM CALCIUM      
REMARK 280  ACETATE, 6-8% PEG 20000, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 285.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
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                                                                      
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       66.90000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      167.40000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       96.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      167.40000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       66.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       96.45000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE QUATERNARY STATE OF THE BIOMOLECULE IS                   
REMARK 300 HETEROTETRAMERIC: THE HETEROTRIMERIC PROTEIN COMPLEXES I.E.          
REMARK 300 CHAIN B,C,D AND E,F,G, ARE BOUND TO DNA CHAIN X AND Y,               
REMARK 300 RESPECTIVELY.                                                        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 123950 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, X                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24090 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 124200 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, Y                            
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 B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ILE B   247                                                      
REMARK 465     PHE B   289                                                      
REMARK 465     SER B   290                                                      
REMARK 465     GLN B   291                                                      
REMARK 465     ARG B   292                                                      
REMARK 465     PHE B   293                                                      
REMARK 465     LEU B   294                                                      
REMARK 465     GLU B   295                                                      
REMARK 465     ASP B   296                                                      
REMARK 465     ARG B   297                                                      
REMARK 465     THR B   298                                                      
REMARK 465     LYS B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     GLU B   303                                                      
REMARK 465     THR B   304                                                      
REMARK 465     MET B  1175                                                      
REMARK 465     THR B  1176                                                      
REMARK 465     LEU B  1177                                                      
REMARK 465     GLU B  1178                                                      
REMARK 465     GLU B  1179                                                      
REMARK 465     ALA B  1180                                                      
REMARK 465     SER C  1122                                                      
REMARK 465     GLY D   249                                                      
REMARK 465     SER D   250                                                      
REMARK 465     LYS D   467                                                      
REMARK 465     ILE D   468                                                      
REMARK 465     HIS D   469                                                      
REMARK 465     ARG D   470                                                      
REMARK 465     HIS D   471                                                      
REMARK 465     PRO D   472                                                      
REMARK 465     HIS D   473                                                      
REMARK 465     SER D   474                                                      
REMARK 465     ARG D   475                                                      
REMARK 465     TRP D   476                                                      
REMARK 465     TYR D   477                                                      
REMARK 465     GLU D   478                                                      
REMARK 465     GLY D   479                                                      
REMARK 465     ARG D   480                                                      
REMARK 465     PRO D   481                                                      
REMARK 465     VAL D   482                                                      
REMARK 465     MET D   483                                                      
REMARK 465     ILE D   484                                                      
REMARK 465     ALA D   485                                                      
REMARK 465     ARG D   486                                                      
REMARK 465     ASN D   487                                                      
REMARK 465     ASP D   488                                                      
REMARK 465     SER D   489                                                      
REMARK 465     ALA D   490                                                      
REMARK 465     LEU D   491                                                      
REMARK 465     GLY D   492                                                      
REMARK 465     LEU D   493                                                      
REMARK 465     PHE D   494                                                      
REMARK 465     ASN D   495                                                      
REMARK 465     GLY D   496                                                      
REMARK 465     ASP D   497                                                      
REMARK 465     ILE D   498                                                      
REMARK 465     GLY D   499                                                      
REMARK 465     ILE D   500                                                      
REMARK 465     ALA D   501                                                      
REMARK 465     LEU D   502                                                      
REMARK 465     ASP D   503                                                      
REMARK 465     ARG D   504                                                      
REMARK 465     GLY D   505                                                      
REMARK 465     GLN D   506                                                      
REMARK 465     GLY D   507                                                      
REMARK 465     THR D   508                                                      
REMARK 465     ARG D   509                                                      
REMARK 465     VAL D   510                                                      
REMARK 465     TRP D   511                                                      
REMARK 465     PHE D   512                                                      
REMARK 465     ALA D   513                                                      
REMARK 465     MET D   514                                                      
REMARK 465     PRO D   515                                                      
REMARK 465     ASP D   516                                                      
REMARK 465     GLY D   517                                                      
REMARK 465     ASN D   518                                                      
REMARK 465     ILE D   519                                                      
REMARK 465     LYS D   520                                                      
REMARK 465     SER D   521                                                      
REMARK 465     VAL D   522                                                      
REMARK 465     GLN D   523                                                      
REMARK 465     ARG D   607                                                      
REMARK 465     GLU D   608                                                      
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     ILE E   247                                                      
REMARK 465     PHE E   289                                                      
REMARK 465     SER E   290                                                      
REMARK 465     GLN E   291                                                      
REMARK 465     ARG E   292                                                      
REMARK 465     PHE E   293                                                      
REMARK 465     LEU E   294                                                      
REMARK 465     GLU E   295                                                      
REMARK 465     ASP E   296                                                      
REMARK 465     ARG E   297                                                      
REMARK 465     THR E   298                                                      
REMARK 465     LYS E   299                                                      
REMARK 465     ALA E   300                                                      
REMARK 465     GLY E   301                                                      
REMARK 465     GLY E   302                                                      
REMARK 465     GLU E   303                                                      
REMARK 465     THR E   304                                                      
REMARK 465     MET E  1175                                                      
REMARK 465     THR E  1176                                                      
REMARK 465     LEU E  1177                                                      
REMARK 465     GLU E  1178                                                      
REMARK 465     GLU E  1179                                                      
REMARK 465     ALA E  1180                                                      
REMARK 465     SER F  1122                                                      
REMARK 465     GLY G   249                                                      
REMARK 465     SER G   250                                                      
REMARK 465     LYS G   467                                                      
REMARK 465     ILE G   468                                                      
REMARK 465     HIS G   469                                                      
REMARK 465     ARG G   470                                                      
REMARK 465     HIS G   471                                                      
REMARK 465     PRO G   472                                                      
REMARK 465     HIS G   473                                                      
REMARK 465     SER G   474                                                      
REMARK 465     ARG G   475                                                      
REMARK 465     TRP G   476                                                      
REMARK 465     TYR G   477                                                      
REMARK 465     GLU G   478                                                      
REMARK 465     GLY G   479                                                      
REMARK 465     ARG G   480                                                      
REMARK 465     PRO G   481                                                      
REMARK 465     VAL G   482                                                      
REMARK 465     MET G   483                                                      
REMARK 465     ILE G   484                                                      
REMARK 465     ALA G   485                                                      
REMARK 465     ARG G   486                                                      
REMARK 465     ASN G   487                                                      
REMARK 465     ASP G   488                                                      
REMARK 465     SER G   489                                                      
REMARK 465     ALA G   490                                                      
REMARK 465     LEU G   491                                                      
REMARK 465     GLY G   492                                                      
REMARK 465     LEU G   493                                                      
REMARK 465     PHE G   494                                                      
REMARK 465     ASN G   495                                                      
REMARK 465     GLY G   496                                                      
REMARK 465     ASP G   497                                                      
REMARK 465     ILE G   498                                                      
REMARK 465     GLY G   499                                                      
REMARK 465     ILE G   500                                                      
REMARK 465     ALA G   501                                                      
REMARK 465     LEU G   502                                                      
REMARK 465     ASP G   503                                                      
REMARK 465     ARG G   504                                                      
REMARK 465     GLY G   505                                                      
REMARK 465     GLN G   506                                                      
REMARK 465     GLY G   507                                                      
REMARK 465     THR G   508                                                      
REMARK 465     ARG G   509                                                      
REMARK 465     VAL G   510                                                      
REMARK 465     TRP G   511                                                      
REMARK 465     PHE G   512                                                      
REMARK 465     ALA G   513                                                      
REMARK 465     MET G   514                                                      
REMARK 465     PRO G   515                                                      
REMARK 465     ASP G   516                                                      
REMARK 465     GLY G   517                                                      
REMARK 465     ASN G   518                                                      
REMARK 465     ILE G   519                                                      
REMARK 465     LYS G   520                                                      
REMARK 465     SER G   521                                                      
REMARK 465     VAL G   522                                                      
REMARK 465     GLN G   523                                                      
REMARK 465     ARG G   607                                                      
REMARK 465     GLU G   608                                                      
REMARK 465      DT X    26                                                      
REMARK 465      DT X    27                                                      
REMARK 465      DC X    28                                                      
REMARK 465      DC X    29                                                      
REMARK 465      DC X    30                                                      
REMARK 465      DT Y    26                                                      
REMARK 465      DT Y    27                                                      
REMARK 465      DC Y    28                                                      
REMARK 465      DC Y    29                                                      
REMARK 465      DC Y    30                                                      
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      DT X  31    P    OP1  OP2                                       
REMARK 470      DT Y  31    P    OP1  OP2                                       
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    THR D   226     N    GLU D   228              2.04            
REMARK 500   O    THR G   226     N    GLU G   228              2.06            
REMARK 500   O    TYR C   685     N    ARG C   687              2.12            
REMARK 500   OG1  THR E   740     OP1   DA Y    49              2.13            
REMARK 500   O    TYR F   685     N    ARG F   687              2.13            
REMARK 500   O    THR F   116     N    ASP F   118              2.17            
REMARK 500   OD1  ASP D   275     O4   5IU X     2              2.18            
REMARK 500   O    THR C   116     N    ASP C   118              2.18            
REMARK 500   NH2  ARG F   968     OP1  5IU Y     9              2.19            
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    ASP B 244   N   -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    PRO B 308   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    PRO B 308   C   -  N   -  CA  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    PRO B 308   C   -  N   -  CD  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    PRO B 320   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    TRP B 878   N   -  CA  -  C   ANGL. DEV. = -18.0 DEGREES          
REMARK 500    PRO B 938   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO B1052   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO C 658   C   -  N   -  CA  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    GLY C1083   N   -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    PRO D 224   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    ALA D 237   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    THR D 239   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES          
REMARK 500    HIS D 255   N   -  CA  -  C   ANGL. DEV. =  17.6 DEGREES          
REMARK 500    HIS D 256   N   -  CA  -  C   ANGL. DEV. =  21.1 DEGREES          
REMARK 500    LEU D 261   CB  -  CG  -  CD2 ANGL. DEV. = -10.8 DEGREES          
REMARK 500    PRO D 528   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ASP E 244   N   -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    PRO E 308   N   -  CA  -  C   ANGL. DEV. =  16.2 DEGREES          
REMARK 500    PRO E 308   C   -  N   -  CA  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    PRO E 308   C   -  N   -  CD  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    PRO E 320   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO E 938   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO E1052   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO F 658   C   -  N   -  CA  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    GLY F1083   N   -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ALA G 237   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    THR G 239   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    LEU G 261   CB  -  CG  -  CD2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    PRO G 528   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500     DA X  11   O3' -  P   -  OP1 ANGL. DEV. =  13.7 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    VAL B   4      102.13     62.73                                   
REMARK 500    THR B   7      108.29    -59.40                                   
REMARK 500    GLU B  18      104.35     29.55                                   
REMARK 500    SER B  24      178.37    -51.46                                   
REMARK 500    LEU B  44     -174.36    -58.80                                   
REMARK 500    PRO B  51      -59.58    -23.60                                   
REMARK 500    GLU B  57       35.09    -86.71                                   
REMARK 500    GLU B  58      -17.05   -145.14                                   
REMARK 500    ALA B  86        4.73    -69.90                                   
REMARK 500    GLU B  90       13.48     50.05                                   
REMARK 500    ASN B  94      116.32   -167.22                                   
REMARK 500    PRO B  95     -119.34    -14.33                                   
REMARK 500    LEU B  96      -70.82     -7.35                                   
REMARK 500    LYS B 107      -29.34    -37.80                                   
REMARK 500    GLU B 123       15.39   -152.18                                   
REMARK 500    CYS B 133      -73.38    -55.23                                   
REMARK 500    ASN B 138       -5.40    -59.63                                   
REMARK 500    ASN B 140       42.43   -105.98                                   
REMARK 500    ASP B 155     -101.29    -38.42                                   
REMARK 500    GLU B 156      -61.93     59.47                                   
REMARK 500    ARG B 177      -59.12    -29.55                                   
REMARK 500    ARG B 195       -9.57    -52.59                                   
REMARK 500    LEU B 201      -18.80     81.28                                   
REMARK 500    ASP B 214       21.87    -48.72                                   
REMARK 500    ASP B 215       -6.80   -159.56                                   
REMARK 500    SER B 220      -76.44    -42.80                                   
REMARK 500    GLN B 235       17.85    -65.57                                   
REMARK 500    TRP B 236      -35.25   -140.76                                   
REMARK 500    ASP B 238       69.25   -117.76                                   
REMARK 500    ALA B 239        2.42   -177.84                                   
REMARK 500    VAL B 240       55.39    -99.49                                   
REMARK 500    ASP B 244     -160.14    -41.46                                   
REMARK 500    ALA B 245     -165.75   -163.63                                   
REMARK 500    SER B 249      -92.25    -78.30                                   
REMARK 500    SER B 250       -6.72    -43.50                                   
REMARK 500    ILE B 252      157.84    -40.29                                   
REMARK 500    ARG B 254       30.66    -86.74                                   
REMARK 500    ARG B 259      -93.99    -33.67                                   
REMARK 500    SER B 260      -33.38    -34.72                                   
REMARK 500    ASN B 261        5.51    -56.00                                   
REMARK 500    LYS B 268       35.43    -75.04                                   
REMARK 500    ILE B 269     -123.50     63.38                                   
REMARK 500    SER B 270       -2.06     80.21                                   
REMARK 500    GLU B 276       82.58      0.93                                   
REMARK 500    TYR B 280       55.66    -69.83                                   
REMARK 500    GLN B 281      -76.79   -102.47                                   
REMARK 500    LEU B 282      -48.18    146.14                                   
REMARK 500    HIS B 307      155.98    142.77                                   
REMARK 500    PRO B 308     -170.24    -24.82                                   
REMARK 500    PHE B 310       11.06   -167.69                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     865 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DA Y  10         0.05    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP B 244        24.0      L          L   OUTSIDE RANGE           
REMARK 500    ALA B 245        24.9      L          L   OUTSIDE RANGE           
REMARK 500    PRO B 308        24.8      L          L   OUTSIDE RANGE           
REMARK 500    TRP B 878        45.8      L          L   OUTSIDE RANGE           
REMARK 500    CYS B1050        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 271        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 551        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ARG C1082        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ASP D 236        18.5      L          L   OUTSIDE RANGE           
REMARK 500    THR D 239        46.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS D 256        21.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP E 244        24.0      L          L   OUTSIDE RANGE           
REMARK 500    ALA E 245        24.9      L          L   OUTSIDE RANGE           
REMARK 500    CYS E1050        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP F 271        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP F 551        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP G 236        18.4      L          L   OUTSIDE RANGE           
REMARK 500    THR G 239        45.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B4000  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 956   NE2                                                    
REMARK 620 2 ASP B1067   OD2  77.3                                              
REMARK 620 3 ASP B1080   OD1 129.2  79.8                                        
REMARK 620 4 TYR B1081   O    63.7  78.7  67.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E4000  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 956   NE2                                                    
REMARK 620 2 ASP E1067   OD2  86.2                                              
REMARK 620 3 ASP E1080   OD1 134.0  78.1                                        
REMARK 620 4 TYR E1081   O    67.6  83.5  67.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4000                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 4000                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1W36   RELATED DB: PDB                                   
REMARK 900 RECBCD:DNA COMPLEX                                                   
DBREF  3K70 B    1  1180  UNP    P08394   EX5B_ECOLI       1   1180             
DBREF  3K70 C    1  1122  UNP    P07648   EX5C_ECOLI       1   1122             
DBREF  3K70 D    1   608  UNP    P04993   EX5A_ECOLI       1    608             
DBREF  3K70 E    1  1180  UNP    P08394   EX5B_ECOLI       1   1180             
DBREF  3K70 F    1  1122  UNP    P07648   EX5C_ECOLI       1   1122             
DBREF  3K70 G    1   608  UNP    P04993   EX5A_ECOLI       1    608             
DBREF  3K70 X    1    51  PDB    3K70     3K70             1     51             
DBREF  3K70 Y    1    51  PDB    3K70     3K70             1     51             
SEQRES   1 B 1180  MET SER ASP VAL ALA GLU THR LEU ASP PRO LEU ARG LEU          
SEQRES   2 B 1180  PRO LEU GLN GLY GLU ARG LEU ILE GLU ALA SER ALA GLY          
SEQRES   3 B 1180  THR GLY LYS THR PHE THR ILE ALA ALA LEU TYR LEU ARG          
SEQRES   4 B 1180  LEU LEU LEU GLY LEU GLY GLY SER ALA ALA PHE PRO ARG          
SEQRES   5 B 1180  PRO LEU THR VAL GLU GLU LEU LEU VAL VAL THR PHE THR          
SEQRES   6 B 1180  GLU ALA ALA THR ALA GLU LEU ARG GLY ARG ILE ARG SER          
SEQRES   7 B 1180  ASN ILE HIS GLU LEU ARG ILE ALA CYS LEU ARG GLU THR          
SEQRES   8 B 1180  THR ASP ASN PRO LEU TYR GLU ARG LEU LEU GLU GLU ILE          
SEQRES   9 B 1180  ASP ASP LYS ALA GLN ALA ALA GLN TRP LEU LEU LEU ALA          
SEQRES  10 B 1180  GLU ARG GLN MET ASP GLU ALA ALA VAL PHE THR ILE HIS          
SEQRES  11 B 1180  GLY PHE CYS GLN ARG MET LEU ASN LEU ASN ALA PHE GLU          
SEQRES  12 B 1180  SER GLY MET LEU PHE GLU GLN GLN LEU ILE GLU ASP GLU          
SEQRES  13 B 1180  SER LEU LEU ARG TYR GLN ALA CYS ALA ASP PHE TRP ARG          
SEQRES  14 B 1180  ARG HIS CYS TYR PRO LEU PRO ARG GLU ILE ALA GLN VAL          
SEQRES  15 B 1180  VAL PHE GLU THR TRP LYS GLY PRO GLN ALA LEU LEU ARG          
SEQRES  16 B 1180  ASP ILE ASN ARG TYR LEU GLN GLY GLU ALA PRO VAL ILE          
SEQRES  17 B 1180  LYS ALA PRO PRO PRO ASP ASP GLU THR LEU ALA SER ARG          
SEQRES  18 B 1180  HIS ALA GLN ILE VAL ALA ARG ILE ASP THR VAL LYS GLN          
SEQRES  19 B 1180  GLN TRP ARG ASP ALA VAL GLY GLU LEU ASP ALA LEU ILE          
SEQRES  20 B 1180  GLU SER SER GLY ILE ASP ARG ARG LYS PHE ASN ARG SER          
SEQRES  21 B 1180  ASN GLN ALA LYS TRP ILE ASP LYS ILE SER ALA TRP ALA          
SEQRES  22 B 1180  GLU GLU GLU THR ASN SER TYR GLN LEU PRO GLU SER LEU          
SEQRES  23 B 1180  GLU LYS PHE SER GLN ARG PHE LEU GLU ASP ARG THR LYS          
SEQRES  24 B 1180  ALA GLY GLY GLU THR PRO ARG HIS PRO LEU PHE GLU ALA          
SEQRES  25 B 1180  ILE ASP GLN LEU LEU ALA GLU PRO LEU SER ILE ARG ASP          
SEQRES  26 B 1180  LEU VAL ILE THR ARG ALA LEU ALA GLU ILE ARG GLU THR          
SEQRES  27 B 1180  VAL ALA ARG GLU LYS ARG ARG ARG GLY GLU LEU GLY PHE          
SEQRES  28 B 1180  ASP ASP MET LEU SER ARG LEU ASP SER ALA LEU ARG SER          
SEQRES  29 B 1180  GLU SER GLY GLU VAL LEU ALA ALA ALA ILE ARG THR ARG          
SEQRES  30 B 1180  PHE PRO VAL ALA MET ILE ASP GLU PHE GLN ASP THR ASP          
SEQRES  31 B 1180  PRO GLN GLN TYR ARG ILE PHE ARG ARG ILE TRP HIS HIS          
SEQRES  32 B 1180  GLN PRO GLU THR ALA LEU LEU LEU ILE GLY ASP PRO LYS          
SEQRES  33 B 1180  GLN ALA ILE TYR ALA PHE ARG GLY ALA ASP ILE PHE THR          
SEQRES  34 B 1180  TYR MET LYS ALA ARG SER GLU VAL HIS ALA HIS TYR THR          
SEQRES  35 B 1180  LEU ASP THR ASN TRP ARG SER ALA PRO GLY MET VAL ASN          
SEQRES  36 B 1180  SER VAL ASN LYS LEU PHE SER GLN THR ASP ASP ALA PHE          
SEQRES  37 B 1180  MET PHE ARG GLU ILE PRO PHE ILE PRO VAL LYS SER ALA          
SEQRES  38 B 1180  GLY LYS ASN GLN ALA LEU ARG PHE VAL PHE LYS GLY GLU          
SEQRES  39 B 1180  THR GLN PRO ALA MET LYS MET TRP LEU MET GLU GLY GLU          
SEQRES  40 B 1180  SER CYS GLY VAL GLY ASP TYR GLN SER THR MET ALA GLN          
SEQRES  41 B 1180  VAL CYS ALA ALA GLN ILE ARG ASP TRP LEU GLN ALA GLY          
SEQRES  42 B 1180  GLN ARG GLY GLU ALA LEU LEU MET ASN GLY ASP ASP ALA          
SEQRES  43 B 1180  ARG PRO VAL ARG ALA SER ASP ILE SER VAL LEU VAL ARG          
SEQRES  44 B 1180  SER ARG GLN GLU ALA ALA GLN VAL ARG ASP ALA LEU THR          
SEQRES  45 B 1180  LEU LEU GLU ILE PRO SER VAL TYR LEU SER ASN ARG ASP          
SEQRES  46 B 1180  SER VAL PHE GLU THR LEU GLU ALA GLN GLU MET LEU TRP          
SEQRES  47 B 1180  LEU LEU GLN ALA VAL MET THR PRO GLU ARG GLU ASN THR          
SEQRES  48 B 1180  LEU ARG SER ALA LEU ALA THR SER MET MET GLY LEU ASN          
SEQRES  49 B 1180  ALA LEU ASP ILE GLU THR LEU ASN ASN ASP GLU HIS ALA          
SEQRES  50 B 1180  TRP ASP VAL VAL VAL GLU GLU PHE ASP GLY TYR ARG GLN          
SEQRES  51 B 1180  ILE TRP ARG LYS ARG GLY VAL MET PRO MET LEU ARG ALA          
SEQRES  52 B 1180  LEU MET SER ALA ARG ASN ILE ALA GLU ASN LEU LEU ALA          
SEQRES  53 B 1180  THR ALA GLY GLY GLU ARG ARG LEU THR ASP ILE LEU HIS          
SEQRES  54 B 1180  ILE SER GLU LEU LEU GLN GLU ALA GLY THR GLN LEU GLU          
SEQRES  55 B 1180  SER GLU HIS ALA LEU VAL ARG TRP LEU SER GLN HIS ILE          
SEQRES  56 B 1180  LEU GLU PRO ASP SER ASN ALA SER SER GLN GLN MET ARG          
SEQRES  57 B 1180  LEU GLU SER ASP LYS HIS LEU VAL GLN ILE VAL THR ILE          
SEQRES  58 B 1180  HIS LYS SER LYS GLY LEU GLU TYR PRO LEU VAL TRP LEU          
SEQRES  59 B 1180  PRO PHE ILE THR ASN PHE ARG VAL GLN GLU GLN ALA PHE          
SEQRES  60 B 1180  TYR HIS ASP ARG HIS SER PHE GLU ALA VAL LEU ASP LEU          
SEQRES  61 B 1180  ASN ALA ALA PRO GLU SER VAL ASP LEU ALA GLU ALA GLU          
SEQRES  62 B 1180  ARG LEU ALA GLU ASP LEU ARG LEU LEU TYR VAL ALA LEU          
SEQRES  63 B 1180  THR ARG SER VAL TRP HIS CYS SER LEU GLY VAL ALA PRO          
SEQRES  64 B 1180  LEU VAL ARG ARG ARG GLY ASP LYS LYS GLY ASP THR ASP          
SEQRES  65 B 1180  VAL HIS GLN SER ALA LEU GLY ARG LEU LEU GLN LYS GLY          
SEQRES  66 B 1180  GLU PRO GLN ASP ALA ALA GLY LEU ARG THR CYS ILE GLU          
SEQRES  67 B 1180  ALA LEU CYS ASP ASP ASP ILE ALA TRP GLN THR ALA GLN          
SEQRES  68 B 1180  THR GLY ASP ASN GLN PRO TRP GLN VAL ASN ASP VAL SER          
SEQRES  69 B 1180  THR ALA GLU LEU ASN ALA LYS THR LEU GLN ARG LEU PRO          
SEQRES  70 B 1180  GLY ASP ASN TRP ARG VAL THR SER TYR SER GLY LEU GLN          
SEQRES  71 B 1180  GLN ARG GLY HIS GLY ILE ALA GLN ASP LEU MET PRO ARG          
SEQRES  72 B 1180  LEU ASP VAL ASP ALA ALA GLY VAL ALA SER VAL VAL GLU          
SEQRES  73 B 1180  GLU PRO THR LEU THR PRO HIS GLN PHE PRO ARG GLY ALA          
SEQRES  74 B 1180  SER PRO GLY THR PHE LEU HIS SER LEU PHE GLU ASP LEU          
SEQRES  75 B 1180  ASP PHE THR GLN PRO VAL ASP PRO ASN TRP VAL ARG GLU          
SEQRES  76 B 1180  LYS LEU GLU LEU GLY GLY PHE GLU SER GLN TRP GLU PRO          
SEQRES  77 B 1180  VAL LEU THR GLU TRP ILE THR ALA VAL LEU GLN ALA PRO          
SEQRES  78 B 1180  LEU ASN GLU THR GLY VAL SER LEU SER GLN LEU SER ALA          
SEQRES  79 B 1180  ARG ASN LYS GLN VAL GLU MET GLU PHE TYR LEU PRO ILE          
SEQRES  80 B 1180  SER GLU PRO LEU ILE ALA SER GLN LEU ASP THR LEU ILE          
SEQRES  81 B 1180  ARG GLN PHE ASP PRO LEU SER ALA GLY CYS PRO PRO LEU          
SEQRES  82 B 1180  GLU PHE MET GLN VAL ARG GLY MET LEU LYS GLY PHE ILE          
SEQRES  83 B 1180  ASP LEU VAL PHE ARG HIS GLU GLY ARG TYR TYR LEU LEU          
SEQRES  84 B 1180  ASP TYR LYS SER ASN TRP LEU GLY GLU ASP SER SER ALA          
SEQRES  85 B 1180  TYR THR GLN GLN ALA MET ALA ALA ALA MET GLN ALA HIS          
SEQRES  86 B 1180  ARG TYR ASP LEU GLN TYR GLN LEU TYR THR LEU ALA LEU          
SEQRES  87 B 1180  HIS ARG TYR LEU ARG HIS ARG ILE ALA ASP TYR ASP TYR          
SEQRES  88 B 1180  GLU HIS HIS PHE GLY GLY VAL ILE TYR LEU PHE LEU ARG          
SEQRES  89 B 1180  GLY VAL ASP LYS GLU HIS PRO GLN GLN GLY ILE TYR THR          
SEQRES  90 B 1180  THR ARG PRO ASN ALA GLY LEU ILE ALA LEU MET ASP GLU          
SEQRES  91 B 1180  MET PHE ALA GLY MET THR LEU GLU GLU ALA                      
SEQRES   1 C 1122  MET LEU ARG VAL TYR HIS SER ASN ARG LEU ASP VAL LEU          
SEQRES   2 C 1122  GLU ALA LEU MET GLU PHE ILE VAL GLU ARG GLU ARG LEU          
SEQRES   3 C 1122  ASP ASP PRO PHE GLU PRO GLU MET ILE LEU VAL GLN SER          
SEQRES   4 C 1122  THR GLY MET ALA GLN TRP LEU GLN MET THR LEU SER GLN          
SEQRES   5 C 1122  LYS PHE GLY ILE ALA ALA ASN ILE ASP PHE PRO LEU PRO          
SEQRES   6 C 1122  ALA SER PHE ILE TRP ASP MET PHE VAL ARG VAL LEU PRO          
SEQRES   7 C 1122  GLU ILE PRO LYS GLU SER ALA PHE ASN LYS GLN SER MET          
SEQRES   8 C 1122  SER TRP LYS LEU MET THR LEU LEU PRO GLN LEU LEU GLU          
SEQRES   9 C 1122  ARG GLU ASP PHE THR LEU LEU ARG HIS TYR LEU THR ASP          
SEQRES  10 C 1122  ASP SER ASP LYS ARG LYS LEU PHE GLN LEU SER SER LYS          
SEQRES  11 C 1122  ALA ALA ASP LEU PHE ASP GLN TYR LEU VAL TYR ARG PRO          
SEQRES  12 C 1122  ASP TRP LEU ALA GLN TRP GLU THR GLY HIS LEU VAL GLU          
SEQRES  13 C 1122  GLY LEU GLY GLU ALA GLN ALA TRP GLN ALA PRO LEU TRP          
SEQRES  14 C 1122  LYS ALA LEU VAL GLU TYR THR HIS GLN LEU GLY GLN PRO          
SEQRES  15 C 1122  ARG TRP HIS ARG ALA ASN LEU TYR GLN ARG PHE ILE GLU          
SEQRES  16 C 1122  THR LEU GLU SER ALA THR THR CYS PRO PRO GLY LEU PRO          
SEQRES  17 C 1122  SER ARG VAL PHE ILE CYS GLY ILE SER ALA LEU PRO PRO          
SEQRES  18 C 1122  VAL TYR LEU GLN ALA LEU GLN ALA LEU GLY LYS HIS ILE          
SEQRES  19 C 1122  GLU ILE HIS LEU LEU PHE THR ASN PRO CYS ARG TYR TYR          
SEQRES  20 C 1122  TRP GLY ASP ILE LYS ASP PRO ALA TYR LEU ALA LYS LEU          
SEQRES  21 C 1122  LEU THR ARG GLN ARG ARG HIS SER PHE GLU ASP ARG GLU          
SEQRES  22 C 1122  LEU PRO LEU PHE ARG ASP SER GLU ASN ALA GLY GLN LEU          
SEQRES  23 C 1122  PHE ASN SER ASP GLY GLU GLN ASP VAL GLY ASN PRO LEU          
SEQRES  24 C 1122  LEU ALA SER TRP GLY LYS LEU GLY ARG ASP TYR ILE TYR          
SEQRES  25 C 1122  LEU LEU SER ASP LEU GLU SER SER GLN GLU LEU ASP ALA          
SEQRES  26 C 1122  PHE VAL ASP VAL THR PRO ASP ASN LEU LEU HIS ASN ILE          
SEQRES  27 C 1122  GLN SER ASP ILE LEU GLU LEU GLU ASN ARG ALA VAL ALA          
SEQRES  28 C 1122  GLY VAL ASN ILE GLU GLU PHE SER ARG SER ASP ASN LYS          
SEQRES  29 C 1122  ARG PRO LEU ASP PRO LEU ASP SER SER ILE THR PHE HIS          
SEQRES  30 C 1122  VAL CYS HIS SER PRO GLN ARG GLU VAL GLU VAL LEU HIS          
SEQRES  31 C 1122  ASP ARG LEU LEU ALA MET LEU GLU GLU ASP PRO THR LEU          
SEQRES  32 C 1122  THR PRO ARG ASP ILE ILE VAL MET VAL ALA ASP ILE ASP          
SEQRES  33 C 1122  SER TYR SER PRO PHE ILE GLN ALA VAL PHE GLY SER ALA          
SEQRES  34 C 1122  PRO ALA ASP ARG TYR LEU PRO TYR ALA ILE SER ASP ARG          
SEQRES  35 C 1122  ARG ALA ARG GLN SER HIS PRO VAL LEU GLU ALA PHE ILE          
SEQRES  36 C 1122  SER LEU LEU SER LEU PRO ASP SER ARG PHE VAL SER GLU          
SEQRES  37 C 1122  ASP VAL LEU ALA LEU LEU ASP VAL PRO VAL LEU ALA ALA          
SEQRES  38 C 1122  ARG PHE ASP ILE THR GLU GLU GLY LEU ARG TYR LEU ARG          
SEQRES  39 C 1122  GLN TRP VAL ASN GLU SER GLY ILE ARG TRP GLY ILE ASP          
SEQRES  40 C 1122  ASP ASP ASN VAL ARG GLU LEU GLU LEU PRO ALA THR GLY          
SEQRES  41 C 1122  GLN HIS THR TRP ARG PHE GLY LEU THR ARG MET LEU LEU          
SEQRES  42 C 1122  GLY TYR ALA MET GLU SER ALA GLN GLY GLU TRP GLN SER          
SEQRES  43 C 1122  VAL LEU PRO TYR ASP GLU SER SER GLY LEU ILE ALA GLU          
SEQRES  44 C 1122  LEU VAL GLY HIS LEU ALA SER LEU LEU MET GLN LEU ASN          
SEQRES  45 C 1122  ILE TRP ARG ARG GLY LEU ALA GLN GLU ARG PRO LEU GLU          
SEQRES  46 C 1122  GLU TRP LEU PRO VAL CYS ARG ASP MET LEU ASN ALA PHE          
SEQRES  47 C 1122  PHE LEU PRO ASP ALA GLU THR GLU ALA ALA MET THR LEU          
SEQRES  48 C 1122  ILE GLU GLN GLN TRP GLN ALA ILE ILE ALA GLU GLY LEU          
SEQRES  49 C 1122  GLY ALA GLN TYR GLY ASP ALA VAL PRO LEU SER LEU LEU          
SEQRES  50 C 1122  ARG ASP GLU LEU ALA GLN ARG LEU ASP GLN GLU ARG ILE          
SEQRES  51 C 1122  SER GLN ARG PHE LEU ALA GLY PRO VAL ASN ILE CYS THR          
SEQRES  52 C 1122  LEU MET PRO MET ARG SER ILE PRO PHE LYS VAL VAL CYS          
SEQRES  53 C 1122  LEU LEU GLY MET ASN ASP GLY VAL TYR PRO ARG GLN LEU          
SEQRES  54 C 1122  ALA PRO LEU GLY PHE ASP LEU MET SER GLN LYS PRO LYS          
SEQRES  55 C 1122  ARG GLY ASP ARG SER ARG ARG ASP ASP ASP ARG TYR LEU          
SEQRES  56 C 1122  PHE LEU GLU ALA LEU ILE SER ALA GLN GLN LYS LEU TYR          
SEQRES  57 C 1122  ILE SER TYR ILE GLY ARG SER ILE GLN ASP ASN SER GLU          
SEQRES  58 C 1122  ARG PHE PRO SER VAL LEU VAL GLN GLU LEU ILE ASP TYR          
SEQRES  59 C 1122  ILE GLY GLN SER HIS TYR LEU PRO GLY ASP GLU ALA LEU          
SEQRES  60 C 1122  ASN CYS ASP GLU SER GLU ALA ARG VAL LYS ALA HIS LEU          
SEQRES  61 C 1122  THR CYS LEU HIS THR ARG MET PRO PHE ASP PRO GLN ASN          
SEQRES  62 C 1122  TYR GLN PRO GLY GLU ARG GLN SER TYR ALA ARG GLU TRP          
SEQRES  63 C 1122  LEU PRO ALA ALA SER GLN ALA GLY LYS ALA HIS SER GLU          
SEQRES  64 C 1122  PHE VAL GLN PRO LEU PRO PHE THR LEU PRO GLU THR VAL          
SEQRES  65 C 1122  PRO LEU GLU THR LEU GLN ARG PHE TRP ALA HIS PRO VAL          
SEQRES  66 C 1122  ARG ALA PHE PHE GLN MET ARG LEU GLN VAL ASN PHE ARG          
SEQRES  67 C 1122  THR GLU ASP SER GLU ILE PRO ASP THR GLU PRO PHE ILE          
SEQRES  68 C 1122  LEU GLU GLY LEU SER ARG TYR GLN ILE ASN GLN GLN LEU          
SEQRES  69 C 1122  LEU ASN ALA LEU VAL GLU GLN ASP ASP ALA GLU ARG LEU          
SEQRES  70 C 1122  PHE ARG ARG PHE ARG ALA ALA GLY ASP LEU PRO TYR GLY          
SEQRES  71 C 1122  ALA PHE GLY GLU ILE PHE TRP GLU THR GLN CYS GLN GLU          
SEQRES  72 C 1122  MET GLN GLN LEU ALA ASP ARG VAL ILE ALA CYS ARG GLN          
SEQRES  73 C 1122  PRO GLY GLN SER MET GLU ILE ASP LEU ALA CYS ASN GLY          
SEQRES  74 C 1122  VAL GLN ILE THR GLY TRP LEU PRO GLN VAL GLN PRO ASP          
SEQRES  75 C 1122  GLY LEU LEU ARG TRP ARG PRO SER LEU LEU SER VAL ALA          
SEQRES  76 C 1122  GLN GLY MET GLN LEU TRP LEU GLU HIS LEU VAL TYR CYS          
SEQRES  77 C 1122  ALA SER GLY GLY ASN GLY GLU SER ARG LEU PHE LEU ARG          
SEQRES  78 C 1122  LYS ASP GLY GLU TRP ARG PHE PRO PRO LEU ALA ALA GLU          
SEQRES  79 C 1122  GLN ALA LEU HIS TYR LEU SER GLN LEU ILE GLU GLY TYR          
SEQRES  80 C 1122  ARG GLU GLY MET SER ALA PRO LEU LEU VAL LEU PRO GLU          
SEQRES  81 C 1122  SER GLY GLY ALA TRP LEU LYS THR CYS TYR ASP ALA GLN          
SEQRES  82 C 1122  ASN ASP ALA MET LEU ASP ASP ASP SER THR LEU GLN LYS          
SEQRES  83 C 1122  ALA ARG THR LYS PHE LEU GLN ALA TYR GLU GLY ASN MET          
SEQRES  84 C 1122  MET VAL ARG GLY GLU GLY ASP ASP ILE TRP TYR GLN ARG          
SEQRES  85 C 1122  LEU TRP ARG GLN LEU THR PRO GLU THR MET GLU ALA ILE          
SEQRES  86 C 1122  VAL GLU GLN SER GLN ARG PHE LEU LEU PRO LEU PHE ARG          
SEQRES  87 C 1122  PHE ASN GLN SER                                              
SEQRES   1 D  608  MET LYS LEU GLN LYS GLN LEU LEU GLU ALA VAL GLU HIS          
SEQRES   2 D  608  LYS GLN LEU ARG PRO LEU ASP VAL GLN PHE ALA LEU THR          
SEQRES   3 D  608  VAL ALA GLY ASP GLU HIS PRO ALA VAL THR LEU ALA ALA          
SEQRES   4 D  608  ALA LEU LEU SER HIS ASP ALA GLY GLU GLY HIS VAL CYS          
SEQRES   5 D  608  LEU PRO LEU SER ARG LEU GLU ASN ASN GLU ALA SER HIS          
SEQRES   6 D  608  PRO LEU LEU ALA THR CYS VAL SER GLU ILE GLY GLU LEU          
SEQRES   7 D  608  GLN ASN TRP GLU GLU CYS LEU LEU ALA SER GLN ALA VAL          
SEQRES   8 D  608  SER ARG GLY ASP GLU PRO THR PRO MET ILE LEU CYS GLY          
SEQRES   9 D  608  ASP ARG LEU TYR LEU ASN ARG MET TRP CYS ASN GLU ARG          
SEQRES  10 D  608  THR VAL ALA ARG PHE PHE ASN GLU VAL ASN HIS ALA ILE          
SEQRES  11 D  608  GLU VAL ASP GLU ALA LEU LEU ALA GLN THR LEU ASP LYS          
SEQRES  12 D  608  LEU PHE PRO VAL SER ASP GLU ILE ASN TRP GLN LYS VAL          
SEQRES  13 D  608  ALA ALA ALA VAL ALA LEU THR ARG ARG ILE SER VAL ILE          
SEQRES  14 D  608  SER GLY GLY PRO GLY THR GLY LYS THR THR THR VAL ALA          
SEQRES  15 D  608  LYS LEU LEU ALA ALA LEU ILE GLN MET ALA ASP GLY GLU          
SEQRES  16 D  608  ARG CYS ARG ILE ARG LEU ALA ALA PRO THR GLY LYS ALA          
SEQRES  17 D  608  ALA ALA ARG LEU THR GLU SER LEU GLY LYS ALA LEU ARG          
SEQRES  18 D  608  GLN LEU PRO LEU THR ASP GLU GLN LYS LYS ARG ILE PRO          
SEQRES  19 D  608  GLU ASP ALA SER THR LEU HIS ARG LEU LEU GLY ALA GLN          
SEQRES  20 D  608  PRO GLY SER GLN ARG LEU ARG HIS HIS ALA GLY ASN PRO          
SEQRES  21 D  608  LEU HIS LEU ASP VAL LEU VAL VAL ASP GLU ALA SER MET          
SEQRES  22 D  608  ILE ASP LEU PRO MET MET SER ARG LEU ILE ASP ALA LEU          
SEQRES  23 D  608  PRO ASP HIS ALA ARG VAL ILE PHE LEU GLY ASP ARG ASP          
SEQRES  24 D  608  GLN LEU ALA SER VAL GLU ALA GLY ALA VAL LEU GLY ASP          
SEQRES  25 D  608  ILE CYS ALA TYR ALA ASN ALA GLY PHE THR ALA GLU ARG          
SEQRES  26 D  608  ALA ARG GLN LEU SER ARG LEU THR GLY THR HIS VAL PRO          
SEQRES  27 D  608  ALA GLY THR GLY THR GLU ALA ALA SER LEU ARG ASP SER          
SEQRES  28 D  608  LEU CYS LEU LEU GLN LYS SER TYR ARG PHE GLY SER ASP          
SEQRES  29 D  608  SER GLY ILE GLY GLN LEU ALA ALA ALA ILE ASN ARG GLY          
SEQRES  30 D  608  ASP LYS THR ALA VAL LYS THR VAL PHE GLN GLN ASP PHE          
SEQRES  31 D  608  THR ASP ILE GLU LYS ARG LEU LEU GLN SER GLY GLU ASP          
SEQRES  32 D  608  TYR ILE ALA MET LEU GLU GLU ALA LEU ALA GLY TYR GLY          
SEQRES  33 D  608  ARG TYR LEU ASP LEU LEU GLN ALA ARG ALA GLU PRO ASP          
SEQRES  34 D  608  LEU ILE ILE GLN ALA PHE ASN GLU TYR GLN LEU LEU CYS          
SEQRES  35 D  608  ALA LEU ARG GLU GLY PRO PHE GLY VAL ALA GLY LEU ASN          
SEQRES  36 D  608  GLU ARG ILE GLU GLN PHE MET GLN GLN LYS ARG LYS ILE          
SEQRES  37 D  608  HIS ARG HIS PRO HIS SER ARG TRP TYR GLU GLY ARG PRO          
SEQRES  38 D  608  VAL MET ILE ALA ARG ASN ASP SER ALA LEU GLY LEU PHE          
SEQRES  39 D  608  ASN GLY ASP ILE GLY ILE ALA LEU ASP ARG GLY GLN GLY          
SEQRES  40 D  608  THR ARG VAL TRP PHE ALA MET PRO ASP GLY ASN ILE LYS          
SEQRES  41 D  608  SER VAL GLN PRO SER ARG LEU PRO GLU HIS GLU THR THR          
SEQRES  42 D  608  TRP ALA MET THR VAL HIS LYS SER GLN GLY SER GLU PHE          
SEQRES  43 D  608  ASP HIS ALA ALA LEU ILE LEU PRO SER GLN ARG THR PRO          
SEQRES  44 D  608  VAL VAL THR ARG GLU LEU VAL TYR THR ALA VAL THR ARG          
SEQRES  45 D  608  ALA ARG ARG ARG LEU SER LEU TYR ALA ASP GLU ARG ILE          
SEQRES  46 D  608  LEU SER ALA ALA ILE ALA THR ARG THR GLU ARG ARG SER          
SEQRES  47 D  608  GLY LEU ALA ALA LEU PHE SER SER ARG GLU                      
SEQRES   1 E 1180  MET SER ASP VAL ALA GLU THR LEU ASP PRO LEU ARG LEU          
SEQRES   2 E 1180  PRO LEU GLN GLY GLU ARG LEU ILE GLU ALA SER ALA GLY          
SEQRES   3 E 1180  THR GLY LYS THR PHE THR ILE ALA ALA LEU TYR LEU ARG          
SEQRES   4 E 1180  LEU LEU LEU GLY LEU GLY GLY SER ALA ALA PHE PRO ARG          
SEQRES   5 E 1180  PRO LEU THR VAL GLU GLU LEU LEU VAL VAL THR PHE THR          
SEQRES   6 E 1180  GLU ALA ALA THR ALA GLU LEU ARG GLY ARG ILE ARG SER          
SEQRES   7 E 1180  ASN ILE HIS GLU LEU ARG ILE ALA CYS LEU ARG GLU THR          
SEQRES   8 E 1180  THR ASP ASN PRO LEU TYR GLU ARG LEU LEU GLU GLU ILE          
SEQRES   9 E 1180  ASP ASP LYS ALA GLN ALA ALA GLN TRP LEU LEU LEU ALA          
SEQRES  10 E 1180  GLU ARG GLN MET ASP GLU ALA ALA VAL PHE THR ILE HIS          
SEQRES  11 E 1180  GLY PHE CYS GLN ARG MET LEU ASN LEU ASN ALA PHE GLU          
SEQRES  12 E 1180  SER GLY MET LEU PHE GLU GLN GLN LEU ILE GLU ASP GLU          
SEQRES  13 E 1180  SER LEU LEU ARG TYR GLN ALA CYS ALA ASP PHE TRP ARG          
SEQRES  14 E 1180  ARG HIS CYS TYR PRO LEU PRO ARG GLU ILE ALA GLN VAL          
SEQRES  15 E 1180  VAL PHE GLU THR TRP LYS GLY PRO GLN ALA LEU LEU ARG          
SEQRES  16 E 1180  ASP ILE ASN ARG TYR LEU GLN GLY GLU ALA PRO VAL ILE          
SEQRES  17 E 1180  LYS ALA PRO PRO PRO ASP ASP GLU THR LEU ALA SER ARG          
SEQRES  18 E 1180  HIS ALA GLN ILE VAL ALA ARG ILE ASP THR VAL LYS GLN          
SEQRES  19 E 1180  GLN TRP ARG ASP ALA VAL GLY GLU LEU ASP ALA LEU ILE          
SEQRES  20 E 1180  GLU SER SER GLY ILE ASP ARG ARG LYS PHE ASN ARG SER          
SEQRES  21 E 1180  ASN GLN ALA LYS TRP ILE ASP LYS ILE SER ALA TRP ALA          
SEQRES  22 E 1180  GLU GLU GLU THR ASN SER TYR GLN LEU PRO GLU SER LEU          
SEQRES  23 E 1180  GLU LYS PHE SER GLN ARG PHE LEU GLU ASP ARG THR LYS          
SEQRES  24 E 1180  ALA GLY GLY GLU THR PRO ARG HIS PRO LEU PHE GLU ALA          
SEQRES  25 E 1180  ILE ASP GLN LEU LEU ALA GLU PRO LEU SER ILE ARG ASP          
SEQRES  26 E 1180  LEU VAL ILE THR ARG ALA LEU ALA GLU ILE ARG GLU THR          
SEQRES  27 E 1180  VAL ALA ARG GLU LYS ARG ARG ARG GLY GLU LEU GLY PHE          
SEQRES  28 E 1180  ASP ASP MET LEU SER ARG LEU ASP SER ALA LEU ARG SER          
SEQRES  29 E 1180  GLU SER GLY GLU VAL LEU ALA ALA ALA ILE ARG THR ARG          
SEQRES  30 E 1180  PHE PRO VAL ALA MET ILE ASP GLU PHE GLN ASP THR ASP          
SEQRES  31 E 1180  PRO GLN GLN TYR ARG ILE PHE ARG ARG ILE TRP HIS HIS          
SEQRES  32 E 1180  GLN PRO GLU THR ALA LEU LEU LEU ILE GLY ASP PRO LYS          
SEQRES  33 E 1180  GLN ALA ILE TYR ALA PHE ARG GLY ALA ASP ILE PHE THR          
SEQRES  34 E 1180  TYR MET LYS ALA ARG SER GLU VAL HIS ALA HIS TYR THR          
SEQRES  35 E 1180  LEU ASP THR ASN TRP ARG SER ALA PRO GLY MET VAL ASN          
SEQRES  36 E 1180  SER VAL ASN LYS LEU PHE SER GLN THR ASP ASP ALA PHE          
SEQRES  37 E 1180  MET PHE ARG GLU ILE PRO PHE ILE PRO VAL LYS SER ALA          
SEQRES  38 E 1180  GLY LYS ASN GLN ALA LEU ARG PHE VAL PHE LYS GLY GLU          
SEQRES  39 E 1180  THR GLN PRO ALA MET LYS MET TRP LEU MET GLU GLY GLU          
SEQRES  40 E 1180  SER CYS GLY VAL GLY ASP TYR GLN SER THR MET ALA GLN          
SEQRES  41 E 1180  VAL CYS ALA ALA GLN ILE ARG ASP TRP LEU GLN ALA GLY          
SEQRES  42 E 1180  GLN ARG GLY GLU ALA LEU LEU MET ASN GLY ASP ASP ALA          
SEQRES  43 E 1180  ARG PRO VAL ARG ALA SER ASP ILE SER VAL LEU VAL ARG          
SEQRES  44 E 1180  SER ARG GLN GLU ALA ALA GLN VAL ARG ASP ALA LEU THR          
SEQRES  45 E 1180  LEU LEU GLU ILE PRO SER VAL TYR LEU SER ASN ARG ASP          
SEQRES  46 E 1180  SER VAL PHE GLU THR LEU GLU ALA GLN GLU MET LEU TRP          
SEQRES  47 E 1180  LEU LEU GLN ALA VAL MET THR PRO GLU ARG GLU ASN THR          
SEQRES  48 E 1180  LEU ARG SER ALA LEU ALA THR SER MET MET GLY LEU ASN          
SEQRES  49 E 1180  ALA LEU ASP ILE GLU THR LEU ASN ASN ASP GLU HIS ALA          
SEQRES  50 E 1180  TRP ASP VAL VAL VAL GLU GLU PHE ASP GLY TYR ARG GLN          
SEQRES  51 E 1180  ILE TRP ARG LYS ARG GLY VAL MET PRO MET LEU ARG ALA          
SEQRES  52 E 1180  LEU MET SER ALA ARG ASN ILE ALA GLU ASN LEU LEU ALA          
SEQRES  53 E 1180  THR ALA GLY GLY GLU ARG ARG LEU THR ASP ILE LEU HIS          
SEQRES  54 E 1180  ILE SER GLU LEU LEU GLN GLU ALA GLY THR GLN LEU GLU          
SEQRES  55 E 1180  SER GLU HIS ALA LEU VAL ARG TRP LEU SER GLN HIS ILE          
SEQRES  56 E 1180  LEU GLU PRO ASP SER ASN ALA SER SER GLN GLN MET ARG          
SEQRES  57 E 1180  LEU GLU SER ASP LYS HIS LEU VAL GLN ILE VAL THR ILE          
SEQRES  58 E 1180  HIS LYS SER LYS GLY LEU GLU TYR PRO LEU VAL TRP LEU          
SEQRES  59 E 1180  PRO PHE ILE THR ASN PHE ARG VAL GLN GLU GLN ALA PHE          
SEQRES  60 E 1180  TYR HIS ASP ARG HIS SER PHE GLU ALA VAL LEU ASP LEU          
SEQRES  61 E 1180  ASN ALA ALA PRO GLU SER VAL ASP LEU ALA GLU ALA GLU          
SEQRES  62 E 1180  ARG LEU ALA GLU ASP LEU ARG LEU LEU TYR VAL ALA LEU          
SEQRES  63 E 1180  THR ARG SER VAL TRP HIS CYS SER LEU GLY VAL ALA PRO          
SEQRES  64 E 1180  LEU VAL ARG ARG ARG GLY ASP LYS LYS GLY ASP THR ASP          
SEQRES  65 E 1180  VAL HIS GLN SER ALA LEU GLY ARG LEU LEU GLN LYS GLY          
SEQRES  66 E 1180  GLU PRO GLN ASP ALA ALA GLY LEU ARG THR CYS ILE GLU          
SEQRES  67 E 1180  ALA LEU CYS ASP ASP ASP ILE ALA TRP GLN THR ALA GLN          
SEQRES  68 E 1180  THR GLY ASP ASN GLN PRO TRP GLN VAL ASN ASP VAL SER          
SEQRES  69 E 1180  THR ALA GLU LEU ASN ALA LYS THR LEU GLN ARG LEU PRO          
SEQRES  70 E 1180  GLY ASP ASN TRP ARG VAL THR SER TYR SER GLY LEU GLN          
SEQRES  71 E 1180  GLN ARG GLY HIS GLY ILE ALA GLN ASP LEU MET PRO ARG          
SEQRES  72 E 1180  LEU ASP VAL ASP ALA ALA GLY VAL ALA SER VAL VAL GLU          
SEQRES  73 E 1180  GLU PRO THR LEU THR PRO HIS GLN PHE PRO ARG GLY ALA          
SEQRES  74 E 1180  SER PRO GLY THR PHE LEU HIS SER LEU PHE GLU ASP LEU          
SEQRES  75 E 1180  ASP PHE THR GLN PRO VAL ASP PRO ASN TRP VAL ARG GLU          
SEQRES  76 E 1180  LYS LEU GLU LEU GLY GLY PHE GLU SER GLN TRP GLU PRO          
SEQRES  77 E 1180  VAL LEU THR GLU TRP ILE THR ALA VAL LEU GLN ALA PRO          
SEQRES  78 E 1180  LEU ASN GLU THR GLY VAL SER LEU SER GLN LEU SER ALA          
SEQRES  79 E 1180  ARG ASN LYS GLN VAL GLU MET GLU PHE TYR LEU PRO ILE          
SEQRES  80 E 1180  SER GLU PRO LEU ILE ALA SER GLN LEU ASP THR LEU ILE          
SEQRES  81 E 1180  ARG GLN PHE ASP PRO LEU SER ALA GLY CYS PRO PRO LEU          
SEQRES  82 E 1180  GLU PHE MET GLN VAL ARG GLY MET LEU LYS GLY PHE ILE          
SEQRES  83 E 1180  ASP LEU VAL PHE ARG HIS GLU GLY ARG TYR TYR LEU LEU          
SEQRES  84 E 1180  ASP TYR LYS SER ASN TRP LEU GLY GLU ASP SER SER ALA          
SEQRES  85 E 1180  TYR THR GLN GLN ALA MET ALA ALA ALA MET GLN ALA HIS          
SEQRES  86 E 1180  ARG TYR ASP LEU GLN TYR GLN LEU TYR THR LEU ALA LEU          
SEQRES  87 E 1180  HIS ARG TYR LEU ARG HIS ARG ILE ALA ASP TYR ASP TYR          
SEQRES  88 E 1180  GLU HIS HIS PHE GLY GLY VAL ILE TYR LEU PHE LEU ARG          
SEQRES  89 E 1180  GLY VAL ASP LYS GLU HIS PRO GLN GLN GLY ILE TYR THR          
SEQRES  90 E 1180  THR ARG PRO ASN ALA GLY LEU ILE ALA LEU MET ASP GLU          
SEQRES  91 E 1180  MET PHE ALA GLY MET THR LEU GLU GLU ALA                      
SEQRES   1 F 1122  MET LEU ARG VAL TYR HIS SER ASN ARG LEU ASP VAL LEU          
SEQRES   2 F 1122  GLU ALA LEU MET GLU PHE ILE VAL GLU ARG GLU ARG LEU          
SEQRES   3 F 1122  ASP ASP PRO PHE GLU PRO GLU MET ILE LEU VAL GLN SER          
SEQRES   4 F 1122  THR GLY MET ALA GLN TRP LEU GLN MET THR LEU SER GLN          
SEQRES   5 F 1122  LYS PHE GLY ILE ALA ALA ASN ILE ASP PHE PRO LEU PRO          
SEQRES   6 F 1122  ALA SER PHE ILE TRP ASP MET PHE VAL ARG VAL LEU PRO          
SEQRES   7 F 1122  GLU ILE PRO LYS GLU SER ALA PHE ASN LYS GLN SER MET          
SEQRES   8 F 1122  SER TRP LYS LEU MET THR LEU LEU PRO GLN LEU LEU GLU          
SEQRES   9 F 1122  ARG GLU ASP PHE THR LEU LEU ARG HIS TYR LEU THR ASP          
SEQRES  10 F 1122  ASP SER ASP LYS ARG LYS LEU PHE GLN LEU SER SER LYS          
SEQRES  11 F 1122  ALA ALA ASP LEU PHE ASP GLN TYR LEU VAL TYR ARG PRO          
SEQRES  12 F 1122  ASP TRP LEU ALA GLN TRP GLU THR GLY HIS LEU VAL GLU          
SEQRES  13 F 1122  GLY LEU GLY GLU ALA GLN ALA TRP GLN ALA PRO LEU TRP          
SEQRES  14 F 1122  LYS ALA LEU VAL GLU TYR THR HIS GLN LEU GLY GLN PRO          
SEQRES  15 F 1122  ARG TRP HIS ARG ALA ASN LEU TYR GLN ARG PHE ILE GLU          
SEQRES  16 F 1122  THR LEU GLU SER ALA THR THR CYS PRO PRO GLY LEU PRO          
SEQRES  17 F 1122  SER ARG VAL PHE ILE CYS GLY ILE SER ALA LEU PRO PRO          
SEQRES  18 F 1122  VAL TYR LEU GLN ALA LEU GLN ALA LEU GLY LYS HIS ILE          
SEQRES  19 F 1122  GLU ILE HIS LEU LEU PHE THR ASN PRO CYS ARG TYR TYR          
SEQRES  20 F 1122  TRP GLY ASP ILE LYS ASP PRO ALA TYR LEU ALA LYS LEU          
SEQRES  21 F 1122  LEU THR ARG GLN ARG ARG HIS SER PHE GLU ASP ARG GLU          
SEQRES  22 F 1122  LEU PRO LEU PHE ARG ASP SER GLU ASN ALA GLY GLN LEU          
SEQRES  23 F 1122  PHE ASN SER ASP GLY GLU GLN ASP VAL GLY ASN PRO LEU          
SEQRES  24 F 1122  LEU ALA SER TRP GLY LYS LEU GLY ARG ASP TYR ILE TYR          
SEQRES  25 F 1122  LEU LEU SER ASP LEU GLU SER SER GLN GLU LEU ASP ALA          
SEQRES  26 F 1122  PHE VAL ASP VAL THR PRO ASP ASN LEU LEU HIS ASN ILE          
SEQRES  27 F 1122  GLN SER ASP ILE LEU GLU LEU GLU ASN ARG ALA VAL ALA          
SEQRES  28 F 1122  GLY VAL ASN ILE GLU GLU PHE SER ARG SER ASP ASN LYS          
SEQRES  29 F 1122  ARG PRO LEU ASP PRO LEU ASP SER SER ILE THR PHE HIS          
SEQRES  30 F 1122  VAL CYS HIS SER PRO GLN ARG GLU VAL GLU VAL LEU HIS          
SEQRES  31 F 1122  ASP ARG LEU LEU ALA MET LEU GLU GLU ASP PRO THR LEU          
SEQRES  32 F 1122  THR PRO ARG ASP ILE ILE VAL MET VAL ALA ASP ILE ASP          
SEQRES  33 F 1122  SER TYR SER PRO PHE ILE GLN ALA VAL PHE GLY SER ALA          
SEQRES  34 F 1122  PRO ALA ASP ARG TYR LEU PRO TYR ALA ILE SER ASP ARG          
SEQRES  35 F 1122  ARG ALA ARG GLN SER HIS PRO VAL LEU GLU ALA PHE ILE          
SEQRES  36 F 1122  SER LEU LEU SER LEU PRO ASP SER ARG PHE VAL SER GLU          
SEQRES  37 F 1122  ASP VAL LEU ALA LEU LEU ASP VAL PRO VAL LEU ALA ALA          
SEQRES  38 F 1122  ARG PHE ASP ILE THR GLU GLU GLY LEU ARG TYR LEU ARG          
SEQRES  39 F 1122  GLN TRP VAL ASN GLU SER GLY ILE ARG TRP GLY ILE ASP          
SEQRES  40 F 1122  ASP ASP ASN VAL ARG GLU LEU GLU LEU PRO ALA THR GLY          
SEQRES  41 F 1122  GLN HIS THR TRP ARG PHE GLY LEU THR ARG MET LEU LEU          
SEQRES  42 F 1122  GLY TYR ALA MET GLU SER ALA GLN GLY GLU TRP GLN SER          
SEQRES  43 F 1122  VAL LEU PRO TYR ASP GLU SER SER GLY LEU ILE ALA GLU          
SEQRES  44 F 1122  LEU VAL GLY HIS LEU ALA SER LEU LEU MET GLN LEU ASN          
SEQRES  45 F 1122  ILE TRP ARG ARG GLY LEU ALA GLN GLU ARG PRO LEU GLU          
SEQRES  46 F 1122  GLU TRP LEU PRO VAL CYS ARG ASP MET LEU ASN ALA PHE          
SEQRES  47 F 1122  PHE LEU PRO ASP ALA GLU THR GLU ALA ALA MET THR LEU          
SEQRES  48 F 1122  ILE GLU GLN GLN TRP GLN ALA ILE ILE ALA GLU GLY LEU          
SEQRES  49 F 1122  GLY ALA GLN TYR GLY ASP ALA VAL PRO LEU SER LEU LEU          
SEQRES  50 F 1122  ARG ASP GLU LEU ALA GLN ARG LEU ASP GLN GLU ARG ILE          
SEQRES  51 F 1122  SER GLN ARG PHE LEU ALA GLY PRO VAL ASN ILE CYS THR          
SEQRES  52 F 1122  LEU MET PRO MET ARG SER ILE PRO PHE LYS VAL VAL CYS          
SEQRES  53 F 1122  LEU LEU GLY MET ASN ASP GLY VAL TYR PRO ARG GLN LEU          
SEQRES  54 F 1122  ALA PRO LEU GLY PHE ASP LEU MET SER GLN LYS PRO LYS          
SEQRES  55 F 1122  ARG GLY ASP ARG SER ARG ARG ASP ASP ASP ARG TYR LEU          
SEQRES  56 F 1122  PHE LEU GLU ALA LEU ILE SER ALA GLN GLN LYS LEU TYR          
SEQRES  57 F 1122  ILE SER TYR ILE GLY ARG SER ILE GLN ASP ASN SER GLU          
SEQRES  58 F 1122  ARG PHE PRO SER VAL LEU VAL GLN GLU LEU ILE ASP TYR          
SEQRES  59 F 1122  ILE GLY GLN SER HIS TYR LEU PRO GLY ASP GLU ALA LEU          
SEQRES  60 F 1122  ASN CYS ASP GLU SER GLU ALA ARG VAL LYS ALA HIS LEU          
SEQRES  61 F 1122  THR CYS LEU HIS THR ARG MET PRO PHE ASP PRO GLN ASN          
SEQRES  62 F 1122  TYR GLN PRO GLY GLU ARG GLN SER TYR ALA ARG GLU TRP          
SEQRES  63 F 1122  LEU PRO ALA ALA SER GLN ALA GLY LYS ALA HIS SER GLU          
SEQRES  64 F 1122  PHE VAL GLN PRO LEU PRO PHE THR LEU PRO GLU THR VAL          
SEQRES  65 F 1122  PRO LEU GLU THR LEU GLN ARG PHE TRP ALA HIS PRO VAL          
SEQRES  66 F 1122  ARG ALA PHE PHE GLN MET ARG LEU GLN VAL ASN PHE ARG          
SEQRES  67 F 1122  THR GLU ASP SER GLU ILE PRO ASP THR GLU PRO PHE ILE          
SEQRES  68 F 1122  LEU GLU GLY LEU SER ARG TYR GLN ILE ASN GLN GLN LEU          
SEQRES  69 F 1122  LEU ASN ALA LEU VAL GLU GLN ASP ASP ALA GLU ARG LEU          
SEQRES  70 F 1122  PHE ARG ARG PHE ARG ALA ALA GLY ASP LEU PRO TYR GLY          
SEQRES  71 F 1122  ALA PHE GLY GLU ILE PHE TRP GLU THR GLN CYS GLN GLU          
SEQRES  72 F 1122  MET GLN GLN LEU ALA ASP ARG VAL ILE ALA CYS ARG GLN          
SEQRES  73 F 1122  PRO GLY GLN SER MET GLU ILE ASP LEU ALA CYS ASN GLY          
SEQRES  74 F 1122  VAL GLN ILE THR GLY TRP LEU PRO GLN VAL GLN PRO ASP          
SEQRES  75 F 1122  GLY LEU LEU ARG TRP ARG PRO SER LEU LEU SER VAL ALA          
SEQRES  76 F 1122  GLN GLY MET GLN LEU TRP LEU GLU HIS LEU VAL TYR CYS          
SEQRES  77 F 1122  ALA SER GLY GLY ASN GLY GLU SER ARG LEU PHE LEU ARG          
SEQRES  78 F 1122  LYS ASP GLY GLU TRP ARG PHE PRO PRO LEU ALA ALA GLU          
SEQRES  79 F 1122  GLN ALA LEU HIS TYR LEU SER GLN LEU ILE GLU GLY TYR          
SEQRES  80 F 1122  ARG GLU GLY MET SER ALA PRO LEU LEU VAL LEU PRO GLU          
SEQRES  81 F 1122  SER GLY GLY ALA TRP LEU LYS THR CYS TYR ASP ALA GLN          
SEQRES  82 F 1122  ASN ASP ALA MET LEU ASP ASP ASP SER THR LEU GLN LYS          
SEQRES  83 F 1122  ALA ARG THR LYS PHE LEU GLN ALA TYR GLU GLY ASN MET          
SEQRES  84 F 1122  MET VAL ARG GLY GLU GLY ASP ASP ILE TRP TYR GLN ARG          
SEQRES  85 F 1122  LEU TRP ARG GLN LEU THR PRO GLU THR MET GLU ALA ILE          
SEQRES  86 F 1122  VAL GLU GLN SER GLN ARG PHE LEU LEU PRO LEU PHE ARG          
SEQRES  87 F 1122  PHE ASN GLN SER                                              
SEQRES   1 G  608  MET LYS LEU GLN LYS GLN LEU LEU GLU ALA VAL GLU HIS          
SEQRES   2 G  608  LYS GLN LEU ARG PRO LEU ASP VAL GLN PHE ALA LEU THR          
SEQRES   3 G  608  VAL ALA GLY ASP GLU HIS PRO ALA VAL THR LEU ALA ALA          
SEQRES   4 G  608  ALA LEU LEU SER HIS ASP ALA GLY GLU GLY HIS VAL CYS          
SEQRES   5 G  608  LEU PRO LEU SER ARG LEU GLU ASN ASN GLU ALA SER HIS          
SEQRES   6 G  608  PRO LEU LEU ALA THR CYS VAL SER GLU ILE GLY GLU LEU          
SEQRES   7 G  608  GLN ASN TRP GLU GLU CYS LEU LEU ALA SER GLN ALA VAL          
SEQRES   8 G  608  SER ARG GLY ASP GLU PRO THR PRO MET ILE LEU CYS GLY          
SEQRES   9 G  608  ASP ARG LEU TYR LEU ASN ARG MET TRP CYS ASN GLU ARG          
SEQRES  10 G  608  THR VAL ALA ARG PHE PHE ASN GLU VAL ASN HIS ALA ILE          
SEQRES  11 G  608  GLU VAL ASP GLU ALA LEU LEU ALA GLN THR LEU ASP LYS          
SEQRES  12 G  608  LEU PHE PRO VAL SER ASP GLU ILE ASN TRP GLN LYS VAL          
SEQRES  13 G  608  ALA ALA ALA VAL ALA LEU THR ARG ARG ILE SER VAL ILE          
SEQRES  14 G  608  SER GLY GLY PRO GLY THR GLY LYS THR THR THR VAL ALA          
SEQRES  15 G  608  LYS LEU LEU ALA ALA LEU ILE GLN MET ALA ASP GLY GLU          
SEQRES  16 G  608  ARG CYS ARG ILE ARG LEU ALA ALA PRO THR GLY LYS ALA          
SEQRES  17 G  608  ALA ALA ARG LEU THR GLU SER LEU GLY LYS ALA LEU ARG          
SEQRES  18 G  608  GLN LEU PRO LEU THR ASP GLU GLN LYS LYS ARG ILE PRO          
SEQRES  19 G  608  GLU ASP ALA SER THR LEU HIS ARG LEU LEU GLY ALA GLN          
SEQRES  20 G  608  PRO GLY SER GLN ARG LEU ARG HIS HIS ALA GLY ASN PRO          
SEQRES  21 G  608  LEU HIS LEU ASP VAL LEU VAL VAL ASP GLU ALA SER MET          
SEQRES  22 G  608  ILE ASP LEU PRO MET MET SER ARG LEU ILE ASP ALA LEU          
SEQRES  23 G  608  PRO ASP HIS ALA ARG VAL ILE PHE LEU GLY ASP ARG ASP          
SEQRES  24 G  608  GLN LEU ALA SER VAL GLU ALA GLY ALA VAL LEU GLY ASP          
SEQRES  25 G  608  ILE CYS ALA TYR ALA ASN ALA GLY PHE THR ALA GLU ARG          
SEQRES  26 G  608  ALA ARG GLN LEU SER ARG LEU THR GLY THR HIS VAL PRO          
SEQRES  27 G  608  ALA GLY THR GLY THR GLU ALA ALA SER LEU ARG ASP SER          
SEQRES  28 G  608  LEU CYS LEU LEU GLN LYS SER TYR ARG PHE GLY SER ASP          
SEQRES  29 G  608  SER GLY ILE GLY GLN LEU ALA ALA ALA ILE ASN ARG GLY          
SEQRES  30 G  608  ASP LYS THR ALA VAL LYS THR VAL PHE GLN GLN ASP PHE          
SEQRES  31 G  608  THR ASP ILE GLU LYS ARG LEU LEU GLN SER GLY GLU ASP          
SEQRES  32 G  608  TYR ILE ALA MET LEU GLU GLU ALA LEU ALA GLY TYR GLY          
SEQRES  33 G  608  ARG TYR LEU ASP LEU LEU GLN ALA ARG ALA GLU PRO ASP          
SEQRES  34 G  608  LEU ILE ILE GLN ALA PHE ASN GLU TYR GLN LEU LEU CYS          
SEQRES  35 G  608  ALA LEU ARG GLU GLY PRO PHE GLY VAL ALA GLY LEU ASN          
SEQRES  36 G  608  GLU ARG ILE GLU GLN PHE MET GLN GLN LYS ARG LYS ILE          
SEQRES  37 G  608  HIS ARG HIS PRO HIS SER ARG TRP TYR GLU GLY ARG PRO          
SEQRES  38 G  608  VAL MET ILE ALA ARG ASN ASP SER ALA LEU GLY LEU PHE          
SEQRES  39 G  608  ASN GLY ASP ILE GLY ILE ALA LEU ASP ARG GLY GLN GLY          
SEQRES  40 G  608  THR ARG VAL TRP PHE ALA MET PRO ASP GLY ASN ILE LYS          
SEQRES  41 G  608  SER VAL GLN PRO SER ARG LEU PRO GLU HIS GLU THR THR          
SEQRES  42 G  608  TRP ALA MET THR VAL HIS LYS SER GLN GLY SER GLU PHE          
SEQRES  43 G  608  ASP HIS ALA ALA LEU ILE LEU PRO SER GLN ARG THR PRO          
SEQRES  44 G  608  VAL VAL THR ARG GLU LEU VAL TYR THR ALA VAL THR ARG          
SEQRES  45 G  608  ALA ARG ARG ARG LEU SER LEU TYR ALA ASP GLU ARG ILE          
SEQRES  46 G  608  LEU SER ALA ALA ILE ALA THR ARG THR GLU ARG ARG SER          
SEQRES  47 G  608  GLY LEU ALA ALA LEU PHE SER SER ARG GLU                      
SEQRES   1 X   51  5IU 5IU 5IU 5IU 5IU  DA 5IU  DC 5IU  DA  DA  DT  DG          
SEQRES   2 X   51   DC  DG  DA  DG  DC  DA  DC  DT  DG  DC  DT  DA  DT          
SEQRES   3 X   51   DT  DC  DC  DC  DT  DA  DG  DC  DA  DG  DT  DG  DC          
SEQRES   4 X   51   DT  DC  DG  DC  DA  DT 5IU  DA  DG  DA 5IU  DA              
SEQRES   1 Y   51  5IU 5IU 5IU 5IU 5IU  DA 5IU  DC 5IU  DA  DA  DT  DG          
SEQRES   2 Y   51   DC  DG  DA  DG  DC  DA  DC  DT  DG  DC  DT  DA  DT          
SEQRES   3 Y   51   DT  DC  DC  DC  DT  DA  DG  DC  DA  DG  DT  DG  DC          
SEQRES   4 Y   51   DT  DC  DG  DC  DA  DT 5IU  DA  DG  DA 5IU  DA              
MODRES 3K70 5IU X    1   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X    2   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X    3   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X    4   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X    5   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X    7   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X    9   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X   46   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU X   50   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y    1   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y    2   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y    3   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y    4   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y    5   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y    7   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y    9   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y   46   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
MODRES 3K70 5IU Y   50   DU  5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE            
HET    5IU  X   1      17                                                       
HET    5IU  X   2      20                                                       
HET    5IU  X   3      20                                                       
HET    5IU  X   4      20                                                       
HET    5IU  X   5      20                                                       
HET    5IU  X   7      20                                                       
HET    5IU  X   9      20                                                       
HET    5IU  X  46      20                                                       
HET    5IU  X  50      20                                                       
HET    5IU  Y   1      17                                                       
HET    5IU  Y   2      20                                                       
HET    5IU  Y   3      20                                                       
HET    5IU  Y   4      20                                                       
HET    5IU  Y   5      20                                                       
HET    5IU  Y   7      20                                                       
HET    5IU  Y   9      20                                                       
HET    5IU  Y  46      20                                                       
HET    5IU  Y  50      20                                                       
HET     CA  B4000       1                                                       
HET     CA  E4000       1                                                       
HETNAM     5IU 5-IODO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE                          
HETNAM      CA CALCIUM ION                                                      
FORMUL   7  5IU    18(C9 H12 I N2 O8 P)                                         
FORMUL   9   CA    2(CA 2+)                                                     
HELIX    1   1 ASP B    9  LEU B   13  5                                   5    
HELIX    2   2 GLY B   28  LEU B   42  1                                  15    
HELIX    3   3 THR B   55  GLU B   57  5                                   3    
HELIX    4   4 THR B   65  ARG B   89  1                                  25    
HELIX    5   5 ASN B   94  GLU B  102  1                                   9    
HELIX    6   6 ASP B  106  MET B  121  1                                  16    
HELIX    7   7 ASP B  122  ALA B  124  5                                   3    
HELIX    8   8 ILE B  129  ASN B  138  1                                  10    
HELIX    9   9 ASN B  140  GLY B  145  1                                   6    
HELIX   10  10 LEU B  158  TYR B  173  1                                  16    
HELIX   11  11 PRO B  176  TRP B  187  1                                  12    
HELIX   12  12 GLY B  189  ASN B  198  1                                  10    
HELIX   13  13 THR B  217  THR B  231  1                                  15    
HELIX   14  14 LYS B  233  ASP B  238  1                                   6    
HELIX   15  15 ARG B  254  ASN B  261  1                                   8    
HELIX   16  16 GLN B  262  ILE B  266  5                                   5    
HELIX   17  17 ILE B  323  GLY B  347  1                                  25    
HELIX   18  18 GLY B  350  LEU B  362  1                                  13    
HELIX   19  19 SER B  364  SER B  366  5                                   3    
HELIX   20  20 GLY B  367  PHE B  378  1                                  12    
HELIX   21  21 PHE B  386  THR B  389  5                                   4    
HELIX   22  22 ASP B  390  HIS B  402  1                                  13    
HELIX   23  23 ASP B  414  ALA B  418  5                                   5    
HELIX   24  24 TYR B  420  GLY B  424  5                                   5    
HELIX   25  25 ASP B  426  VAL B  437  1                                  12    
HELIX   26  26 ALA B  450  PHE B  461  1                                  12    
HELIX   27  27 GLY B  482  GLN B  485  5                                   4    
HELIX   28  28 GLY B  512  ARG B  535  1                                  24    
HELIX   29  29 ARG B  550  ASP B  553  5                                   4    
HELIX   30  30 SER B  560  LEU B  573  1                                  14    
HELIX   31  31 SER B  586  GLU B  589  5                                   4    
HELIX   32  32 THR B  590  MET B  604  1                                  15    
HELIX   33  33 ARG B  608  THR B  618  1                                  11    
HELIX   34  34 SER B  619  GLY B  622  5                                   4    
HELIX   35  35 ASN B  624  ASN B  633  1                                  10    
HELIX   36  36 ASP B  634  GLY B  656  1                                  23    
HELIX   37  37 GLY B  656  ARG B  668  1                                  13    
HELIX   38  38 ASN B  669  ALA B  676  1                                   8    
HELIX   39  39 GLY B  679  THR B  699  1                                  21    
HELIX   40  40 SER B  703  GLU B  717  1                                  15    
HELIX   41  41 SER B  731  LEU B  735  5                                   5    
HELIX   42  42 ILE B  741  LYS B  745  1                                   5    
HELIX   43  43 ALA B  783  ARG B  808  1                                  26    
HELIX   44  44 THR B  831  GLN B  835  5                                   5    
HELIX   45  45 SER B  836  GLN B  843  1                                   8    
HELIX   46  46 ASP B  849  LEU B  860  1                                  12    
HELIX   47  47 ILE B  916  MET B  921  1                                   6    
HELIX   48  48 GLY B  948  PHE B  959  1                                  12    
HELIX   49  49 ASP B  969  GLY B  981  1                                  13    
HELIX   50  50 GLU B  983  GLN B  985  5                                   3    
HELIX   51  51 TRP B  986  GLN B  999  1                                  14    
HELIX   52  52 SER B 1008  LEU B 1012  5                                   5    
HELIX   53  53 SER B 1013  ARG B 1015  5                                   3    
HELIX   54  54 ILE B 1032  ASP B 1044  1                                  13    
HELIX   55  55 PRO B 1045  GLY B 1049  5                                   5    
HELIX   56  56 ASP B 1089  TYR B 1093  5                                   5    
HELIX   57  57 THR B 1094  HIS B 1105  1                                  12    
HELIX   58  58 ARG B 1106  ILE B 1126  1                                  21    
HELIX   59  59 ASP B 1130  PHE B 1135  1                                   6    
HELIX   60  60 ALA B 1162  GLY B 1174  1                                  13    
HELIX   61  61 ARG C    9  GLU C   24  1                                  16    
HELIX   62  62 SER C   39  LYS C   53  1                                  15    
HELIX   63  63 LEU C   64  LEU C   77  1                                  14    
HELIX   64  64 ASN C   87  LEU C  103  1                                  17    
HELIX   65  65 PHE C  108  LEU C  115  1                                   8    
HELIX   66  66 LYS C  121  LEU C  139  1                                  19    
HELIX   67  67 ARG C  142  GLU C  150  1                                   9    
HELIX   68  68 ALA C  161  LEU C  179  1                                  19    
HELIX   69  69 LEU C  189  SER C  199  1                                  11    
HELIX   70  70 PRO C  220  GLY C  231  1                                  12    
HELIX   71  71 ASN C  297  TRP C  303  1                                   7    
HELIX   72  72 GLY C  304  SER C  315  1                                  12    
HELIX   73  73 ASN C  333  LEU C  345  1                                  13    
HELIX   74  74 ASN C  354  ARG C  360  1                                   7    
HELIX   75  75 SER C  381  ASP C  400  1                                  20    
HELIX   76  76 THR C  404  ARG C  406  5                                   3    
HELIX   77  77 TYR C  418  PHE C  426  1                                   9    
HELIX   78  78 ARG C  445  SER C  447  5                                   3    
HELIX   79  79 HIS C  448  LEU C  458  1                                  11    
HELIX   80  80 SER C  459  SER C  463  5                                   5    
HELIX   81  81 VAL C  466  ASP C  475  1                                  10    
HELIX   82  82 VAL C  476  ARG C  482  1                                   7    
HELIX   83  83 THR C  486  GLY C  501  1                                  16    
HELIX   84  84 ASP C  508  GLU C  513  1                                   6    
HELIX   85  85 THR C  523  ALA C  536  1                                  14    
HELIX   86  86 ILE C  557  LEU C  578  1                                  22    
HELIX   87  87 PRO C  583  LEU C  588  5                                   6    
HELIX   88  88 PRO C  589  PHE C  599  1                                  11    
HELIX   89  89 ALA C  603  ALA C  626  1                                  24    
HELIX   90  90 PRO C  633  GLU C  648  1                                  16    
HELIX   91  91 ASP C  695  LYS C  700  1                                   6    
HELIX   92  92 SER C  707  SER C  722  1                                  16    
HELIX   93  93 SER C  745  GLN C  757  1                                  13    
HELIX   94  94 ASN C  768  LEU C  780  1                                  13    
HELIX   95  95 ASP C  790  GLN C  795  5                                   6    
HELIX   96  96 ALA C  803  GLU C  805  5                                   3    
HELIX   97  97 TRP C  806  SER C  811  1                                   6    
HELIX   98  98 LEU C  834  ARG C  839  1                                   6    
HELIX   99  99 HIS C  843  MET C  851  1                                   9    
HELIX  100 100 GLU C  873  GLU C  890  1                                  18    
HELIX  101 101 ASP C  893  ALA C  904  1                                  12    
HELIX  102 102 TYR C  909  ALA C  933  1                                  25    
HELIX  103 103 SER C  973  SER C  990  1                                  18    
HELIX  104 104 ALA C 1012  ALA C 1033  1                                  22    
HELIX  105 105 GLU C 1040  TYR C 1050  1                                  11    
HELIX  106 106 ALA C 1052  ALA C 1056  5                                   5    
HELIX  107 107 SER C 1062  GLU C 1076  1                                  15    
HELIX  108 108 ASP C 1087  TRP C 1094  1                                   8    
HELIX  109 109 THR C 1098  ASN C 1120  1                                  23    
HELIX  110 110 LEU D    3  HIS D   13  1                                  11    
HELIX  111 111 ARG D   17  ALA D   28  1                                  12    
HELIX  112 112 HIS D   32  GLU D   48  1                                  17    
HELIX  113 113 SER D   56  GLU D   59  5                                   4    
HELIX  114 114 ASN D   60  SER D   64  5                                   5    
HELIX  115 115 ASN D   80  SER D   88  1                                   9    
HELIX  116 116 ASN D  110  PHE D  123  1                                  14    
HELIX  117 117 ASP D  133  PHE D  145  1                                  13    
HELIX  118 118 ASN D  152  THR D  163  1                                  12    
HELIX  119 119 GLY D  176  MET D  191  1                                  16    
HELIX  120 120 THR D  205  GLY D  217  1                                  13    
HELIX  121 121 GLY D  217  GLN D  222  1                                   6    
HELIX  122 122 GLU D  270  ILE D  274  5                                   5    
HELIX  123 123 ASP D  275  LEU D  286  1                                  12    
HELIX  124 124 GLN D  300  GLU D  305  1                                   6    
HELIX  125 125 VAL D  309  CYS D  314  1                                   6    
HELIX  126 126 ALA D  315  ASN D  318  5                                   4    
HELIX  127 127 THR D  322  THR D  333  1                                  12    
HELIX  128 128 LEU D  348  ASP D  350  5                                   3    
HELIX  129 129 GLY D  366  ASN D  375  1                                  10    
HELIX  130 130 GLY D  377  GLN D  387  1                                  11    
HELIX  131 131 GLN D  388  PHE D  390  5                                   3    
HELIX  132 132 ASP D  403  TYR D  415  1                                  13    
HELIX  133 133 TYR D  415  ALA D  424  1                                  10    
HELIX  134 134 ASP D  429  ASN D  436  1                                   8    
HELIX  135 135 GLY D  450  GLN D  460  1                                  11    
HELIX  136 136 GLN D  460  LYS D  465  1                                   6    
HELIX  137 137 THR D  562  THR D  571  1                                  10    
HELIX  138 138 ARG D  584  ILE D  590  1                                   7    
HELIX  139 139 ASP E    9  LEU E   13  5                                   5    
HELIX  140 140 GLY E   28  LEU E   42  1                                  15    
HELIX  141 141 THR E   55  GLU E   57  5                                   3    
HELIX  142 142 THR E   65  ARG E   89  1                                  25    
HELIX  143 143 ASN E   94  GLU E  102  1                                   9    
HELIX  144 144 ASP E  106  MET E  121  1                                  16    
HELIX  145 145 ASP E  122  ALA E  124  5                                   3    
HELIX  146 146 ILE E  129  ASN E  138  1                                  10    
HELIX  147 147 ASN E  140  GLY E  145  1                                   6    
HELIX  148 148 GLU E  156  TYR E  173  1                                  18    
HELIX  149 149 PRO E  176  GLU E  185  1                                  10    
HELIX  150 150 GLY E  189  ASN E  198  1                                  10    
HELIX  151 151 THR E  217  THR E  231  1                                  15    
HELIX  152 152 LYS E  233  ASP E  238  1                                   6    
HELIX  153 153 ARG E  254  ASN E  261  1                                   8    
HELIX  154 154 GLN E  262  ILE E  266  5                                   5    
HELIX  155 155 ILE E  323  GLY E  347  1                                  25    
HELIX  156 156 GLY E  350  LEU E  362  1                                  13    
HELIX  157 157 SER E  364  SER E  366  5                                   3    
HELIX  158 158 GLY E  367  PHE E  378  1                                  12    
HELIX  159 159 PHE E  386  THR E  389  5                                   4    
HELIX  160 160 ASP E  390  HIS E  402  1                                  13    
HELIX  161 161 ASP E  414  ALA E  418  5                                   5    
HELIX  162 162 TYR E  420  GLY E  424  5                                   5    
HELIX  163 163 ASP E  426  VAL E  437  1                                  12    
HELIX  164 164 ALA E  450  PHE E  461  1                                  12    
HELIX  165 165 GLY E  482  GLN E  485  5                                   4    
HELIX  166 166 GLY E  512  ARG E  535  1                                  24    
HELIX  167 167 ARG E  550  ASP E  553  5                                   4    
HELIX  168 168 SER E  560  LEU E  573  1                                  14    
HELIX  169 169 SER E  586  GLU E  589  5                                   4    
HELIX  170 170 THR E  590  MET E  604  1                                  15    
HELIX  171 171 ARG E  608  THR E  618  1                                  11    
HELIX  172 172 SER E  619  GLY E  622  5                                   4    
HELIX  173 173 ASN E  624  ASP E  634  1                                  11    
HELIX  174 174 ASP E  634  GLY E  656  1                                  23    
HELIX  175 175 GLY E  656  ARG E  668  1                                  13    
HELIX  176 176 ASN E  669  ALA E  676  1                                   8    
HELIX  177 177 GLY E  679  THR E  699  1                                  21    
HELIX  178 178 SER E  703  GLU E  717  1                                  15    
HELIX  179 179 SER E  731  LEU E  735  5                                   5    
HELIX  180 180 ILE E  741  LYS E  745  1                                   5    
HELIX  181 181 ALA E  783  ARG E  808  1                                  26    
HELIX  182 182 THR E  831  GLN E  835  5                                   5    
HELIX  183 183 SER E  836  GLN E  843  1                                   8    
HELIX  184 184 ASP E  849  LEU E  860  1                                  12    
HELIX  185 185 ILE E  916  MET E  921  1                                   6    
HELIX  186 186 GLY E  948  PHE E  959  1                                  12    
HELIX  187 187 ASP E  969  GLY E  981  1                                  13    
HELIX  188 188 GLU E  983  GLN E  985  5                                   3    
HELIX  189 189 TRP E  986  GLN E  999  1                                  14    
HELIX  190 190 SER E 1008  LEU E 1012  5                                   5    
HELIX  191 191 SER E 1013  ARG E 1015  5                                   3    
HELIX  192 192 ILE E 1032  ASP E 1044  1                                  13    
HELIX  193 193 PRO E 1045  GLY E 1049  5                                   5    
HELIX  194 194 ASP E 1089  TYR E 1093  5                                   5    
HELIX  195 195 THR E 1094  HIS E 1105  1                                  12    
HELIX  196 196 ARG E 1106  ILE E 1126  1                                  21    
HELIX  197 197 ASP E 1130  PHE E 1135  1                                   6    
HELIX  198 198 ALA E 1162  GLY E 1174  1                                  13    
HELIX  199 199 ARG F    9  GLU F   24  1                                  16    
HELIX  200 200 SER F   39  LYS F   53  1                                  15    
HELIX  201 201 LEU F   64  LEU F   77  1                                  14    
HELIX  202 202 ASN F   87  LEU F  103  1                                  17    
HELIX  203 203 PHE F  108  LEU F  115  1                                   8    
HELIX  204 204 LYS F  121  LEU F  139  1                                  19    
HELIX  205 205 ARG F  142  GLU F  150  1                                   9    
HELIX  206 206 ALA F  161  LEU F  179  1                                  19    
HELIX  207 207 LEU F  189  SER F  199  1                                  11    
HELIX  208 208 PRO F  220  GLY F  231  1                                  12    
HELIX  209 209 ASN F  297  TRP F  303  1                                   7    
HELIX  210 210 GLY F  304  SER F  315  1                                  12    
HELIX  211 211 ASN F  333  LEU F  345  1                                  13    
HELIX  212 212 ASN F  354  ARG F  360  1                                   7    
HELIX  213 213 SER F  381  ASP F  400  1                                  20    
HELIX  214 214 THR F  404  ARG F  406  5                                   3    
HELIX  215 215 TYR F  418  PHE F  426  1                                   9    
HELIX  216 216 ARG F  445  SER F  447  5                                   3    
HELIX  217 217 HIS F  448  LEU F  458  1                                  11    
HELIX  218 218 SER F  459  SER F  463  5                                   5    
HELIX  219 219 VAL F  466  LEU F  474  1                                   9    
HELIX  220 220 VAL F  476  ARG F  482  1                                   7    
HELIX  221 221 THR F  486  GLY F  501  1                                  16    
HELIX  222 222 ASP F  508  GLU F  513  1                                   6    
HELIX  223 223 THR F  523  ALA F  536  1                                  14    
HELIX  224 224 ILE F  557  LEU F  578  1                                  22    
HELIX  225 225 PRO F  583  LEU F  588  5                                   6    
HELIX  226 226 PRO F  589  PHE F  599  1                                  11    
HELIX  227 227 ALA F  603  ALA F  626  1                                  24    
HELIX  228 228 PRO F  633  GLU F  648  1                                  16    
HELIX  229 229 ASP F  695  LYS F  700  1                                   6    
HELIX  230 230 SER F  707  SER F  722  1                                  16    
HELIX  231 231 SER F  745  GLN F  757  1                                  13    
HELIX  232 232 ASN F  768  LEU F  780  1                                  13    
HELIX  233 233 ASP F  790  GLN F  795  5                                   6    
HELIX  234 234 ALA F  803  GLU F  805  5                                   3    
HELIX  235 235 TRP F  806  SER F  811  1                                   6    
HELIX  236 236 LEU F  834  ARG F  839  1                                   6    
HELIX  237 237 HIS F  843  MET F  851  1                                   9    
HELIX  238 238 GLU F  873  GLU F  890  1                                  18    
HELIX  239 239 ASP F  893  GLY F  905  1                                  13    
HELIX  240 240 TYR F  909  ALA F  933  1                                  25    
HELIX  241 241 SER F  973  SER F  990  1                                  18    
HELIX  242 242 ALA F 1012  ALA F 1033  1                                  22    
HELIX  243 243 GLU F 1040  TYR F 1050  1                                  11    
HELIX  244 244 ALA F 1052  ALA F 1056  5                                   5    
HELIX  245 245 SER F 1062  GLU F 1076  1                                  15    
HELIX  246 246 ASP F 1087  TRP F 1094  1                                   8    
HELIX  247 247 THR F 1098  ASN F 1120  1                                  23    
HELIX  248 248 LEU G    3  HIS G   13  1                                  11    
HELIX  249 249 ARG G   17  ALA G   28  1                                  12    
HELIX  250 250 HIS G   32  GLU G   48  1                                  17    
HELIX  251 251 SER G   56  GLU G   59  5                                   4    
HELIX  252 252 ASN G   60  SER G   64  5                                   5    
HELIX  253 253 ASN G   80  SER G   88  1                                   9    
HELIX  254 254 ASN G  110  PHE G  123  1                                  14    
HELIX  255 255 ASP G  133  PHE G  145  1                                  13    
HELIX  256 256 ASN G  152  THR G  163  1                                  12    
HELIX  257 257 GLY G  176  MET G  191  1                                  16    
HELIX  258 258 THR G  205  GLY G  217  1                                  13    
HELIX  259 259 GLY G  217  LEU G  223  1                                   7    
HELIX  260 260 GLU G  270  ILE G  274  5                                   5    
HELIX  261 261 ASP G  275  LEU G  286  1                                  12    
HELIX  262 262 GLN G  300  GLU G  305  1                                   6    
HELIX  263 263 VAL G  309  CYS G  314  1                                   6    
HELIX  264 264 ALA G  315  ASN G  318  5                                   4    
HELIX  265 265 THR G  322  THR G  333  1                                  12    
HELIX  266 266 LEU G  348  ASP G  350  5                                   3    
HELIX  267 267 GLY G  366  ASN G  375  1                                  10    
HELIX  268 268 GLY G  377  GLN G  387  1                                  11    
HELIX  269 269 GLN G  388  PHE G  390  5                                   3    
HELIX  270 270 ASP G  403  TYR G  415  1                                  13    
HELIX  271 271 TYR G  415  ALA G  424  1                                  10    
HELIX  272 272 ASP G  429  ASN G  436  1                                   8    
HELIX  273 273 GLY G  450  GLN G  460  1                                  11    
HELIX  274 274 THR G  562  THR G  571  1                                  10    
HELIX  275 275 ARG G  584  ILE G  590  1                                   7    
SHEET    1   A 7 GLU B   6  THR B   7  0                                        
SHEET    2   A 7 HIS B 440  THR B 442  1  O  HIS B 440   N  GLU B   6           
SHEET    3   A 7 ARG B  19  GLU B  22  1  N  GLU B  22   O  TYR B 441           
SHEET    4   A 7 ALA B 408  GLY B 413  1  O  LEU B 411   N  ILE B  21           
SHEET    5   A 7 VAL B 380  ASP B 384  1  N  ILE B 383   O  ILE B 412           
SHEET    6   A 7 LEU B  59  THR B  63  1  N  LEU B  60   O  MET B 382           
SHEET    7   A 7 VAL B 126  THR B 128  1  O  PHE B 127   N  THR B  63           
SHEET    1   B 2 GLN B 151  LEU B 152  0                                        
SHEET    2   B 2 GLU B 348  LEU B 349  1  O  LEU B 349   N  GLN B 151           
SHEET    1   C 2 THR B 445  ASN B 446  0                                        
SHEET    2   C 2 LYS B 479  SER B 480  1  O  LYS B 479   N  ASN B 446           
SHEET    1   D 2 LEU B 487  PHE B 491  0                                        
SHEET    2   D 2 ALA B 538  ASN B 542 -1  O  MET B 541   N  ARG B 488           
SHEET    1   E 4 TYR B 749  LEU B 754  0                                        
SHEET    2   E 4 SER B 809  VAL B 817  1  O  GLY B 816   N  LEU B 754           
SHEET    3   E 4 MET B 499  LEU B 503  1  N  TRP B 502   O  VAL B 817           
SHEET    4   E 4 ILE B 865  THR B 869  1  O  GLN B 868   N  LEU B 503           
SHEET    1   F 3 SER B 555  VAL B 558  0                                        
SHEET    2   F 3 VAL B 736  THR B 740  1  O  GLN B 737   N  VAL B 556           
SHEET    3   F 3 SER B 578  TYR B 580  1  N  VAL B 579   O  ILE B 738           
SHEET    1   G 2 PHE B 767  HIS B 769  0                                        
SHEET    2   G 2 ALA B 776  LEU B 778 -1  O  VAL B 777   N  TYR B 768           
SHEET    1   H 3 TRP B 901  THR B 904  0                                        
SHEET    2   H 3 ARG B1059  PHE B1070  1  O  ARG B1059   N  ARG B 902           
SHEET    3   H 3 LYS B1017  TYR B1024 -1  N  PHE B1023   O  GLY B1064           
SHEET    1   I 3 LEU B1079  TYR B1081  0                                        
SHEET    2   I 3 ILE B1139  LEU B1141  1  O  ILE B1139   N  ASP B1080           
SHEET    3   I 3 ILE B1155  THR B1157 -1  O  TYR B1156   N  TYR B1140           
SHEET    1   J 5 MET C  34  LEU C  36  0                                        
SHEET    2   J 5 ARG C 210  CYS C 214  1  O  PHE C 212   N  LEU C  36           
SHEET    3   J 5 GLU C 235  THR C 241  1  O  HIS C 237   N  VAL C 211           
SHEET    4   J 5 LEU C   2  SER C   7  1  N  ARG C   3   O  LEU C 238           
SHEET    5   J 5 SER C 320  ALA C 325  1  O  LEU C 323   N  HIS C   6           
SHEET    1   K 2 ARG C 365  PRO C 366  0                                        
SHEET    2   K 2 HIS C 759  TYR C 760  1  O  TYR C 760   N  ARG C 365           
SHEET    1   L 7 ALA C 438  ILE C 439  0                                        
SHEET    2   L 7 ASN C 660  THR C 663  1  O  ILE C 661   N  ALA C 438           
SHEET    3   L 7 ILE C 408  VAL C 412  1  N  VAL C 410   O  ASN C 660           
SHEET    4   L 7 PHE C 672  LEU C 678  1  O  CYS C 676   N  ILE C 409           
SHEET    5   L 7 ALA C 723  ILE C 732  1  O  TYR C 728   N  VAL C 675           
SHEET    6   L 7 THR C 375  CYS C 379  1  N  HIS C 377   O  ILE C 729           
SHEET    7   L 7 THR C 781  LEU C 783  1  O  CYS C 782   N  PHE C 376           
SHEET    1   M 2 ARG C 442  ARG C 443  0                                        
SHEET    2   M 2 ARG C 649  ILE C 650 -1  O  ILE C 650   N  ARG C 442           
SHEET    1   N 3 VAL C 832  PRO C 833  0                                        
SHEET    2   N 3 ILE C 952  GLN C 960  1  O  THR C 953   N  VAL C 832           
SHEET    3   N 3 GLN C 939  ILE C 943 -1  N  GLN C 939   O  VAL C 959           
SHEET    1   O 5 VAL C 832  PRO C 833  0                                        
SHEET    2   O 5 ILE C 952  GLN C 960  1  O  THR C 953   N  VAL C 832           
SHEET    3   O 5 GLY C 963  TRP C 967 -1  O  GLY C 963   N  GLN C 960           
SHEET    4   O 5 GLU C 995  PHE C 999  1  O  ARG C 997   N  ARG C 966           
SHEET    5   O 5 GLU C1005  PHE C1008 -1  O  PHE C1008   N  SER C 996           
SHEET    1   P 4 CYS D  52  PRO D  54  0                                        
SHEET    2   P 4 ARG D 106  LEU D 109 -1  O  LEU D 107   N  LEU D  53           
SHEET    3   P 4 MET D 100  CYS D 103 -1  N  ILE D 101   O  TYR D 108           
SHEET    4   P 4 VAL D  91  SER D  92  1  N  SER D  92   O  LEU D 102           
SHEET    1   Q 6 SER D 238  THR D 239  0                                        
SHEET    2   Q 6 ILE D 199  ALA D 203  1  N  ALA D 203   O  SER D 238           
SHEET    3   Q 6 VAL D 265  VAL D 268  1  O  VAL D 267   N  ALA D 202           
SHEET    4   Q 6 ARG D 291  GLY D 296  1  O  ARG D 291   N  LEU D 266           
SHEET    5   Q 6 ILE D 166  SER D 170  1  N  ILE D 169   O  PHE D 294           
SHEET    6   Q 6 LEU D 352  LEU D 354  1  O  CYS D 353   N  SER D 170           
SHEET    1   R 2 ALA D 246  GLN D 247  0                                        
SHEET    2   R 2 ARG D 252  LEU D 253 -1  O  ARG D 252   N  GLN D 247           
SHEET    1   S 5 GLU D 394  LEU D 398  0                                        
SHEET    2   S 5 LEU D 577  ALA D 581  1  O  LEU D 577   N  LYS D 395           
SHEET    3   S 5 ALA D 549  ILE D 552  1  N  LEU D 551   O  SER D 578           
SHEET    4   S 5 LEU D 440  CYS D 442  1  N  LEU D 441   O  ILE D 552           
SHEET    5   S 5 ALA D 535  THR D 537  1  O  MET D 536   N  LEU D 440           
SHEET    1   T 7 GLU E   6  THR E   7  0                                        
SHEET    2   T 7 HIS E 440  THR E 442  1  O  HIS E 440   N  GLU E   6           
SHEET    3   T 7 ARG E  19  GLU E  22  1  N  GLU E  22   O  TYR E 441           
SHEET    4   T 7 ALA E 408  GLY E 413  1  O  LEU E 411   N  ILE E  21           
SHEET    5   T 7 VAL E 380  ASP E 384  1  N  ILE E 383   O  ILE E 412           
SHEET    6   T 7 LEU E  59  THR E  63  1  N  LEU E  60   O  MET E 382           
SHEET    7   T 7 VAL E 126  THR E 128  1  O  PHE E 127   N  THR E  63           
SHEET    1   U 2 GLN E 151  LEU E 152  0                                        
SHEET    2   U 2 GLU E 348  LEU E 349  1  O  LEU E 349   N  GLN E 151           
SHEET    1   V 2 THR E 445  ASN E 446  0                                        
SHEET    2   V 2 LYS E 479  SER E 480  1  O  LYS E 479   N  ASN E 446           
SHEET    1   W 2 LEU E 487  PHE E 491  0                                        
SHEET    2   W 2 ALA E 538  ASN E 542 -1  O  MET E 541   N  ARG E 488           
SHEET    1   X 4 TYR E 749  LEU E 754  0                                        
SHEET    2   X 4 SER E 809  VAL E 817  1  O  GLY E 816   N  LEU E 754           
SHEET    3   X 4 MET E 499  LEU E 503  1  N  TRP E 502   O  VAL E 817           
SHEET    4   X 4 ILE E 865  THR E 869  1  O  GLN E 868   N  LEU E 503           
SHEET    1   Y 3 SER E 555  VAL E 558  0                                        
SHEET    2   Y 3 VAL E 736  THR E 740  1  O  GLN E 737   N  VAL E 556           
SHEET    3   Y 3 SER E 578  TYR E 580  1  N  VAL E 579   O  ILE E 738           
SHEET    1   Z 2 PHE E 767  HIS E 769  0                                        
SHEET    2   Z 2 ALA E 776  LEU E 778 -1  O  VAL E 777   N  TYR E 768           
SHEET    1  AA 3 TRP E 901  THR E 904  0                                        
SHEET    2  AA 3 ARG E1059  PHE E1070  1  O  ARG E1059   N  ARG E 902           
SHEET    3  AA 3 LYS E1017  TYR E1024 -1  N  PHE E1023   O  GLY E1064           
SHEET    1  AB 3 LEU E1079  TYR E1081  0                                        
SHEET    2  AB 3 ILE E1139  LEU E1141  1  O  ILE E1139   N  ASP E1080           
SHEET    3  AB 3 ILE E1155  THR E1157 -1  O  TYR E1156   N  TYR E1140           
SHEET    1  AC 5 MET F  34  LEU F  36  0                                        
SHEET    2  AC 5 ARG F 210  CYS F 214  1  O  PHE F 212   N  LEU F  36           
SHEET    3  AC 5 GLU F 235  THR F 241  1  O  HIS F 237   N  VAL F 211           
SHEET    4  AC 5 LEU F   2  SER F   7  1  N  ARG F   3   O  LEU F 238           
SHEET    5  AC 5 SER F 320  ALA F 325  1  O  LEU F 323   N  HIS F   6           
SHEET    1  AD 2 ARG F 365  PRO F 366  0                                        
SHEET    2  AD 2 HIS F 759  TYR F 760  1  O  TYR F 760   N  ARG F 365           
SHEET    1  AE 7 ALA F 438  ILE F 439  0                                        
SHEET    2  AE 7 ASN F 660  THR F 663  1  O  ILE F 661   N  ALA F 438           
SHEET    3  AE 7 ILE F 408  VAL F 412  1  N  VAL F 410   O  CYS F 662           
SHEET    4  AE 7 PHE F 672  LEU F 678  1  O  CYS F 676   N  ILE F 409           
SHEET    5  AE 7 ALA F 723  ILE F 732  1  O  TYR F 728   N  VAL F 675           
SHEET    6  AE 7 THR F 375  CYS F 379  1  N  HIS F 377   O  ILE F 729           
SHEET    7  AE 7 THR F 781  LEU F 783  1  O  CYS F 782   N  PHE F 376           
SHEET    1  AF 2 ARG F 442  ARG F 443  0                                        
SHEET    2  AF 2 ARG F 649  ILE F 650 -1  O  ILE F 650   N  ARG F 442           
SHEET    1  AG 3 VAL F 832  PRO F 833  0                                        
SHEET    2  AG 3 ILE F 952  GLN F 960  1  O  THR F 953   N  VAL F 832           
SHEET    3  AG 3 GLN F 939  ILE F 943 -1  N  GLN F 939   O  VAL F 959           
SHEET    1  AH 5 VAL F 832  PRO F 833  0                                        
SHEET    2  AH 5 ILE F 952  GLN F 960  1  O  THR F 953   N  VAL F 832           
SHEET    3  AH 5 GLY F 963  TRP F 967 -1  O  GLY F 963   N  GLN F 960           
SHEET    4  AH 5 GLU F 995  PHE F 999  1  O  ARG F 997   N  ARG F 966           
SHEET    5  AH 5 GLU F1005  PHE F1008 -1  O  PHE F1008   N  SER F 996           
SHEET    1  AI 4 CYS G  52  PRO G  54  0                                        
SHEET    2  AI 4 ARG G 106  LEU G 109 -1  O  LEU G 107   N  LEU G  53           
SHEET    3  AI 4 MET G 100  CYS G 103 -1  N  ILE G 101   O  TYR G 108           
SHEET    4  AI 4 VAL G  91  SER G  92  1  N  SER G  92   O  LEU G 102           
SHEET    1  AJ 6 SER G 238  THR G 239  0                                        
SHEET    2  AJ 6 ILE G 199  ALA G 203  1  N  ALA G 203   O  SER G 238           
SHEET    3  AJ 6 VAL G 265  VAL G 268  1  O  VAL G 267   N  ALA G 202           
SHEET    4  AJ 6 ARG G 291  GLY G 296  1  O  ARG G 291   N  LEU G 266           
SHEET    5  AJ 6 ILE G 166  SER G 170  1  N  ILE G 169   O  PHE G 294           
SHEET    6  AJ 6 LEU G 352  LEU G 354  1  O  CYS G 353   N  SER G 170           
SHEET    1  AK 2 GLY G 245  GLN G 247  0                                        
SHEET    2  AK 2 ARG G 252  ARG G 254 -1  O  ARG G 254   N  GLY G 245           
SHEET    1  AL 5 GLU G 394  LEU G 398  0                                        
SHEET    2  AL 5 LEU G 577  ALA G 581  1  O  LEU G 577   N  LYS G 395           
SHEET    3  AL 5 HIS G 548  ILE G 552  1  N  LEU G 551   O  SER G 578           
SHEET    4  AL 5 TYR G 438  CYS G 442  1  N  LEU G 441   O  ILE G 552           
SHEET    5  AL 5 ALA G 535  THR G 537  1  O  MET G 536   N  LEU G 440           
LINK         NE2 HIS B 956                CA    CA B4000     1555   1555  2.81  
LINK         OD2 ASP B1067                CA    CA B4000     1555   1555  2.43  
LINK         OD1 ASP B1080                CA    CA B4000     1555   1555  2.26  
LINK         O   TYR B1081                CA    CA B4000     1555   1555  2.84  
LINK         NE2 HIS E 956                CA    CA E4000     1555   1555  2.62  
LINK         OD2 ASP E1067                CA    CA E4000     1555   1555  2.32  
LINK         OD1 ASP E1080                CA    CA E4000     1555   1555  2.34  
LINK         O   TYR E1081                CA    CA E4000     1555   1555  2.72  
LINK         O3' 5IU X   1                 P   5IU X   2     1555   1555  1.60  
LINK         O3' 5IU X   2                 P   5IU X   3     1555   1555  1.62  
LINK         O3' 5IU X   3                 P   5IU X   4     1555   1555  1.60  
LINK         O3' 5IU X   4                 P   5IU X   5     1555   1555  1.61  
LINK         O3' 5IU X   5                 P    DA X   6     1555   1555  1.61  
LINK         O3'  DA X   6                 P   5IU X   7     1555   1555  1.60  
LINK         O3' 5IU X   7                 P    DC X   8     1555   1555  1.61  
LINK         O3'  DC X   8                 P   5IU X   9     1555   1555  1.61  
LINK         O3' 5IU X   9                 P    DA X  10     1555   1555  1.60  
LINK         O3'  DT X  45                 P   5IU X  46     1555   1555  1.61  
LINK         O3' 5IU X  46                 P    DA X  47     1555   1555  1.61  
LINK         O3'  DA X  49                 P   5IU X  50     1555   1555  1.59  
LINK         O3' 5IU X  50                 P    DA X  51     1555   1555  1.60  
LINK         O3' 5IU Y   1                 P   5IU Y   2     1555   1555  1.61  
LINK         O3' 5IU Y   2                 P   5IU Y   3     1555   1555  1.62  
LINK         O3' 5IU Y   3                 P   5IU Y   4     1555   1555  1.60  
LINK         O3' 5IU Y   4                 P   5IU Y   5     1555   1555  1.61  
LINK         O3' 5IU Y   5                 P    DA Y   6     1555   1555  1.61  
LINK         O3'  DA Y   6                 P   5IU Y   7     1555   1555  1.60  
LINK         O3' 5IU Y   7                 P    DC Y   8     1555   1555  1.61  
LINK         O3'  DC Y   8                 P   5IU Y   9     1555   1555  1.60  
LINK         O3' 5IU Y   9                 P    DA Y  10     1555   1555  1.59  
LINK         O3'  DT Y  45                 P   5IU Y  46     1555   1555  1.61  
LINK         O3' 5IU Y  46                 P    DA Y  47     1555   1555  1.61  
LINK         O3'  DA Y  49                 P   5IU Y  50     1555   1555  1.59  
LINK         O3' 5IU Y  50                 P    DA Y  51     1555   1555  1.60  
SITE     1 AC1  5 HIS B 956  ASP B1067  ASP B1080  TYR B1081                    
SITE     2 AC1  5 LYS B1082                                                     
SITE     1 AC2  4 HIS E 956  ASP E1067  ASP E1080  TYR E1081                    
CRYST1  133.800  192.900  334.800  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007474  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005184  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002987        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system