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Database: PDB
Entry: 5M5P
LinkDB: 5M5P
Original site: 5M5P 
HEADER    HYDROLASE                               22-OCT-16   5M5P              
TITLE     S. CEREVISIAE SPLICEOSOMAL HELICASE BRR2 (271-END) IN COMPLEX WITH THE
TITLE    2 JAB/MPN DOMAIN OF S. CEREVISIAE PRP8                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRE-MRNA-SPLICING HELICASE BRR2;                           
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 271-2163;                                     
COMPND   5 SYNONYM: PROTEIN SNU246;                                             
COMPND   6 EC: 3.6.4.13;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PRE-MRNA-SPLICING FACTOR 8;                                
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 2147-2413;                                    
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 GENE: BRR2, RSS1, SNU246, YER172C, SYGP-ORF66;                       
SOURCE   7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   8 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  13 S288C);                                                              
SOURCE  14 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  15 ORGANISM_TAXID: 559292;                                              
SOURCE  16 GENE: PRP8, DBF3, DNA39, RNA8, SLT21, USA2, YHR165C;                 
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PETM-11                                   
KEYWDS    SPLICING, HELICASE, COMPLEX, HYDROLASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BECKE,E.ABSMEIER,J.WOLLENHAUPT,K.F.SANTOS,M.C.WAHL                  
REVDAT   6   21-NOV-18 5M5P    1       REMARK LINK                              
REVDAT   5   18-OCT-17 5M5P    1       REMARK                                   
REVDAT   4   06-SEP-17 5M5P    1       REMARK                                   
REVDAT   3   25-JAN-17 5M5P    1       JRNL                                     
REVDAT   2   11-JAN-17 5M5P    1       JRNL                                     
REVDAT   1   07-DEC-16 5M5P    0                                                
JRNL        AUTH   E.ABSMEIER,C.BECKE,J.WOLLENHAUPT,K.F.SANTOS,M.C.WAHL         
JRNL        TITL   INTERPLAY OF CIS- AND TRANS-REGULATORY MECHANISMS IN THE     
JRNL        TITL 2 SPLICEOSOMAL RNA HELICASE BRR2.                              
JRNL        REF    CELL CYCLE                    V.  16   100 2017              
JRNL        REFN                   ESSN 1551-4005                               
JRNL        PMID   27880071                                                     
JRNL        DOI    10.1080/15384101.2016.1255384                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 51754                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.309                           
REMARK   3   R VALUE            (WORKING SET) : 0.307                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2666                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 95.5397 - 11.2015    0.98     2730   150  0.2573 0.3182        
REMARK   3     2 11.2015 -  8.8930    1.00     2619   164  0.2155 0.2257        
REMARK   3     3  8.8930 -  7.7695    1.00     2631   144  0.2542 0.2880        
REMARK   3     4  7.7695 -  7.0594    1.00     2622   127  0.2965 0.2867        
REMARK   3     5  7.0594 -  6.5535    1.00     2604   146  0.3121 0.3567        
REMARK   3     6  6.5535 -  6.1672    1.00     2556   148  0.3376 0.3786        
REMARK   3     7  6.1672 -  5.8584    1.00     2613   130  0.3449 0.4073        
REMARK   3     8  5.8584 -  5.6034    1.00     2571   139  0.3437 0.3486        
REMARK   3     9  5.6034 -  5.3877    1.00     2597   128  0.3475 0.3539        
REMARK   3    10  5.3877 -  5.2018    1.00     2553   144  0.3571 0.3744        
REMARK   3    11  5.2018 -  5.0392    1.00     2567   125  0.3492 0.3810        
REMARK   3    12  5.0392 -  4.8951    1.00     2566   145  0.3497 0.3627        
REMARK   3    13  4.8951 -  4.7663    1.00     2541   151  0.3570 0.4007        
REMARK   3    14  4.7663 -  4.6500    1.00     2563   154  0.3541 0.3941        
REMARK   3    15  4.6500 -  4.5443    1.00     2565   117  0.3608 0.3896        
REMARK   3    16  4.5443 -  4.4476    1.00     2537   135  0.3581 0.3903        
REMARK   3    17  4.4476 -  4.3586    1.00     2537   146  0.3767 0.4003        
REMARK   3    18  4.3586 -  4.2764    1.00     2581   133  0.3865 0.3818        
REMARK   3    19  4.2764 -  4.2000    1.00     2535   140  0.3806 0.4335        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.740            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.060           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 157.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          34379                                  
REMARK   3   ANGLE     :  0.757          46599                                  
REMARK   3   CHIRALITY :  0.030           5277                                  
REMARK   3   PLANARITY :  0.004           5951                                  
REMARK   3   DIHEDRAL  : 10.120          12777                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 21660                                       
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 2896                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5M5P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001984.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-13; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : BESSY; BESSY                       
REMARK 200  BEAMLINE                       : 14.2; 14.1                         
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9184; 0.9184                     
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225; NULL               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51802                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.31500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4BGD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NEEDLES                                                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 9.2% (W/V) PEG 4000     
REMARK 280  0.4 M MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       92.98500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.43500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       92.98500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       98.43500            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 94760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 96290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   267                                                      
REMARK 465     ALA A   268                                                      
REMARK 465     GLU A   269                                                      
REMARK 465     PHE A   270                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     THR A   394                                                      
REMARK 465     THR A   395                                                      
REMARK 465     HIS A   396                                                      
REMARK 465     SER A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     ARG A   399                                                      
REMARK 465     GLU A   400                                                      
REMARK 465     LEU A   401                                                      
REMARK 465     ASP A   402                                                      
REMARK 465     SER A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     ASP A   405                                                      
REMARK 465     ASP A   406                                                      
REMARK 465     GLN A   407                                                      
REMARK 465     PRO A   408                                                      
REMARK 465     GLN A   409                                                      
REMARK 465     SER A   410                                                      
REMARK 465     SER A   411                                                      
REMARK 465     GLU A   412                                                      
REMARK 465     ALA A   413                                                      
REMARK 465     LYS A   414                                                      
REMARK 465     ARG A   415                                                      
REMARK 465     THR A   416                                                      
REMARK 465     LYS A   417                                                      
REMARK 465     PHE A   418                                                      
REMARK 465     SER A   419                                                      
REMARK 465     GLU A  1826                                                      
REMARK 465     ALA A  1827                                                      
REMARK 465     GLU A  1828                                                      
REMARK 465     VAL A  1829                                                      
REMARK 465     THR A  1830                                                      
REMARK 465     ALA A  1831                                                      
REMARK 465     GLU A  1832                                                      
REMARK 465     VAL A  1833                                                      
REMARK 465     ASN A  1834                                                      
REMARK 465     GLY A  1835                                                      
REMARK 465     GLY A  1836                                                      
REMARK 465     ASP A  1837                                                      
REMARK 465     ASP A  1838                                                      
REMARK 465     GLU A  1839                                                      
REMARK 465     ALA A  1840                                                      
REMARK 465     GLY B  2144                                                      
REMARK 465     ALA B  2145                                                      
REMARK 465     MET B  2146                                                      
REMARK 465     SER B  2147                                                      
REMARK 465     SER B  2396                                                      
REMARK 465     GLU B  2397                                                      
REMARK 465     LEU B  2398                                                      
REMARK 465     ALA B  2399                                                      
REMARK 465     GLY B  2400                                                      
REMARK 465     ASP B  2401                                                      
REMARK 465     GLU B  2402                                                      
REMARK 465     GLU B  2403                                                      
REMARK 465     LEU B  2404                                                      
REMARK 465     GLU B  2405                                                      
REMARK 465     ALA B  2406                                                      
REMARK 465     GLU B  2407                                                      
REMARK 465     GLN B  2408                                                      
REMARK 465     ILE B  2409                                                      
REMARK 465     ASP B  2410                                                      
REMARK 465     VAL B  2411                                                      
REMARK 465     PHE B  2412                                                      
REMARK 465     SER B  2413                                                      
REMARK 465     GLY C   267                                                      
REMARK 465     ALA C   268                                                      
REMARK 465     GLU C   269                                                      
REMARK 465     PHE C   270                                                      
REMARK 465     LYS C   271                                                      
REMARK 465     LEU C   272                                                      
REMARK 465     SER C   273                                                      
REMARK 465     ASP C   274                                                      
REMARK 465     HIS C   396                                                      
REMARK 465     SER C   397                                                      
REMARK 465     LYS C   398                                                      
REMARK 465     ARG C   399                                                      
REMARK 465     GLU C   400                                                      
REMARK 465     LEU C   401                                                      
REMARK 465     ASP C   402                                                      
REMARK 465     SER C   403                                                      
REMARK 465     GLY C   404                                                      
REMARK 465     ASP C   405                                                      
REMARK 465     ASP C   406                                                      
REMARK 465     GLN C   407                                                      
REMARK 465     PRO C   408                                                      
REMARK 465     GLN C   409                                                      
REMARK 465     SER C   410                                                      
REMARK 465     SER C   411                                                      
REMARK 465     GLU C   412                                                      
REMARK 465     ALA C   413                                                      
REMARK 465     LYS C   414                                                      
REMARK 465     ARG C   415                                                      
REMARK 465     THR C   416                                                      
REMARK 465     LYS C   417                                                      
REMARK 465     PHE C   418                                                      
REMARK 465     SER C   419                                                      
REMARK 465     GLU C  1826                                                      
REMARK 465     ALA C  1827                                                      
REMARK 465     GLU C  1828                                                      
REMARK 465     VAL C  1829                                                      
REMARK 465     THR C  1830                                                      
REMARK 465     ALA C  1831                                                      
REMARK 465     GLU C  1832                                                      
REMARK 465     VAL C  1833                                                      
REMARK 465     ASN C  1834                                                      
REMARK 465     GLY C  1835                                                      
REMARK 465     GLY C  1836                                                      
REMARK 465     ASP C  1837                                                      
REMARK 465     ASP C  1838                                                      
REMARK 465     GLU C  1839                                                      
REMARK 465     ALA C  1840                                                      
REMARK 465     GLY D  2144                                                      
REMARK 465     ALA D  2145                                                      
REMARK 465     MET D  2146                                                      
REMARK 465     SER D  2147                                                      
REMARK 465     SER D  2396                                                      
REMARK 465     GLU D  2397                                                      
REMARK 465     LEU D  2398                                                      
REMARK 465     ALA D  2399                                                      
REMARK 465     GLY D  2400                                                      
REMARK 465     ASP D  2401                                                      
REMARK 465     GLU D  2402                                                      
REMARK 465     GLU D  2403                                                      
REMARK 465     LEU D  2404                                                      
REMARK 465     GLU D  2405                                                      
REMARK 465     ALA D  2406                                                      
REMARK 465     GLU D  2407                                                      
REMARK 465     GLN D  2408                                                      
REMARK 465     ILE D  2409                                                      
REMARK 465     ASP D  2410                                                      
REMARK 465     VAL D  2411                                                      
REMARK 465     PHE D  2412                                                      
REMARK 465     SER D  2413                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CA   ASN A  1287     HE1  PHE A  1308              0.46            
REMARK 500   OD1  ASN A  1287     HZ   PHE A  1308              0.64            
REMARK 500   CA   ASN A  1287     CE1  PHE A  1308              0.64            
REMARK 500   CG   ASN A  1287     CZ   PHE A  1308              0.79            
REMARK 500   CG   ASN A  1287     HZ   PHE A  1308              0.84            
REMARK 500   CB   ASN A  1287     CE1  PHE A  1308              0.94            
REMARK 500   HB2  ALA A  1208     HG   SER A  1307              0.94            
REMARK 500   HB3  ALA A  1208     OG   SER A  1307              1.02            
REMARK 500   CB   ASN A  1287     CZ   PHE A  1308              1.08            
REMARK 500   HA   ASN A  1287     HD1  PHE A  1308              1.12            
REMARK 500   C    ASN A  1287     HE1  PHE A  1308              1.12            
REMARK 500   HB3  ALA A  1208     HG   SER A  1307              1.14            
REMARK 500   CB   ALA A  1208     HG   SER A  1307              1.22            
REMARK 500   HB3  ASN A  1287     CD2  PHE A  1308              1.28            
REMARK 500   HB3  ASN A  1287     CG   PHE A  1308              1.29            
REMARK 500   HA   ASN A  1287     CD1  PHE A  1308              1.29            
REMARK 500   HA   ASN A  1287     HE1  PHE A  1308              1.29            
REMARK 500   OD1  ASN A  1287     CZ   PHE A  1308              1.32            
REMARK 500   HB3  ASN A  1287     CD1  PHE A  1308              1.37            
REMARK 500   HA   ASN A  1287     CE1  PHE A  1308              1.38            
REMARK 500   HB3  ASN A  1287     CE2  PHE A  1308              1.40            
REMARK 500   O    PHE A  1308     H    GLY A  1310              1.47            
REMARK 500   HB3  ASN A  1287     CE1  PHE A  1308              1.48            
REMARK 500   CG   ASN A  1287     CE2  PHE A  1308              1.48            
REMARK 500   O    ASP A   963     H    GLN A   965              1.49            
REMARK 500   HB3  ASN A  1287     CZ   PHE A  1308              1.50            
REMARK 500   N    ASN A  1287     HE1  PHE A  1308              1.51            
REMARK 500   O    ASP C   963     H    LEU C   966              1.53            
REMARK 500   CB   ASN A  1287     CD1  PHE A  1308              1.53            
REMARK 500   H    LYS C  1312     OG   SER C  1787              1.55            
REMARK 500   CA   ASN A  1287     CD1  PHE A  1308              1.56            
REMARK 500   O    TYR C   897     HG   SER C   900              1.57            
REMARK 500   N    ASN A  1287     CE1  PHE A  1308              1.62            
REMARK 500   CB   ALA A  1208     OG   SER A  1307              1.67            
REMARK 500   CB   ASN A  1287     CE2  PHE A  1308              1.71            
REMARK 500   OD1  ASN A  1309     OD1  ASP B  2249              1.81            
REMARK 500   C    ASN A  1287     CE1  PHE A  1308              1.90            
REMARK 500   CA   ASN A  1287     CZ   PHE A  1308              1.95            
REMARK 500   CG   ASN A  1287     CE1  PHE A  1308              2.01            
REMARK 500   CB   ASN A  1287     CG   PHE A  1308              2.04            
REMARK 500   O    PRO A  1286     CD1  PHE A  1308              2.06            
REMARK 500   OD1  ASN A  1287     CE2  PHE A  1308              2.08            
REMARK 500   ND2  ASN A  1287     CZ   PHE A  1308              2.08            
REMARK 500   CB   ASN A  1287     CD2  PHE A  1308              2.09            
REMARK 500   O    ASP A   963     N    GLN A   965              2.11            
REMARK 500   NH2  ARG C  1540     O    ALA C  1710              2.13            
REMARK 500   ND2  ASN A  1287     CE2  PHE A  1308              2.15            
REMARK 500   OG1  THR C  1625     OD1  ASP C  1648              2.15            
REMARK 500   O    PHE A  1308     N    GLY A  1310              2.16            
REMARK 500   OD1  ASP A   959     OG   SER A   961              2.16            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS C  1051     OE1  GLU C  1357     3444     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 324       49.59    -90.78                                   
REMARK 500    HIS A 325      -92.60   -121.39                                   
REMARK 500    ARG A 353      -72.74    -55.56                                   
REMARK 500    SER A 437     -125.94     62.63                                   
REMARK 500    LEU A 440       34.53    -86.94                                   
REMARK 500    SER A 493       56.66    -57.51                                   
REMARK 500    PRO A 522     -179.61    -61.14                                   
REMARK 500    HIS A 541       42.28    -77.46                                   
REMARK 500    HIS A 542      -16.56   -144.40                                   
REMARK 500    LEU A 552       36.30    -95.14                                   
REMARK 500    PHE A 555      114.67   -167.72                                   
REMARK 500    GLN A 575      -74.52    -70.60                                   
REMARK 500    THR A 589       78.50    -65.76                                   
REMARK 500    SER A 595       42.65    -85.61                                   
REMARK 500    HIS A 637       -2.95    -58.97                                   
REMARK 500    TRP A 656      -76.43   -102.07                                   
REMARK 500    LYS A 659     -108.96     57.40                                   
REMARK 500    GLN A 662       -7.78     67.06                                   
REMARK 500    ASN A 676       15.32     80.18                                   
REMARK 500    SER A 746     -158.27   -139.92                                   
REMARK 500    ARG A 747      -89.34    -90.11                                   
REMARK 500    GLU A 764      -92.85   -131.99                                   
REMARK 500    ASN A 773      103.74   -166.63                                   
REMARK 500    SER A 777      -51.23   -141.07                                   
REMARK 500    THR A 783      -91.80    -88.55                                   
REMARK 500    PRO A 791      177.32    -54.14                                   
REMARK 500    ALA A 806       84.24    -69.13                                   
REMARK 500    THR A 850      -47.17     68.98                                   
REMARK 500    VAL A 895      -77.14      9.51                                   
REMARK 500    ASN A 903       35.21   -158.46                                   
REMARK 500    ASP A 994       76.77     61.56                                   
REMARK 500    VAL A1044       93.00    -65.74                                   
REMARK 500    ASP A1070       54.31    -96.05                                   
REMARK 500    GLU A1174       44.19    -83.57                                   
REMARK 500    THR A1175      142.69   -172.20                                   
REMARK 500    ASP A1225       77.19   -118.93                                   
REMARK 500    ASP A1249      -65.17    -93.82                                   
REMARK 500    SER A1307      -80.76     41.76                                   
REMARK 500    PHE A1308      -70.43     47.84                                   
REMARK 500    ASN A1309       12.39    -37.07                                   
REMARK 500    PRO A1320     -167.21    -76.97                                   
REMARK 500    ILE A1329      138.05     62.38                                   
REMARK 500    GLU A1344      -69.65     65.48                                   
REMARK 500    LYS A1392      -71.54    -84.60                                   
REMARK 500    ASN A1399      117.88   -167.03                                   
REMARK 500    ALA A1420       16.19   -157.47                                   
REMARK 500    ASN A1426     -159.20    -87.81                                   
REMARK 500    ARG A1457        4.81    -66.14                                   
REMARK 500    GLU A1469      -30.54   -135.82                                   
REMARK 500    GLU A1503      -47.14     63.36                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     159 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5M5P A  271  2163  UNP    P32639   BRR2_YEAST     271   2163             
DBREF  5M5P B 2147  2413  UNP    P33334   PRP8_YEAST    2147   2413             
DBREF  5M5P C  271  2163  UNP    P32639   BRR2_YEAST     271   2163             
DBREF  5M5P D 2147  2413  UNP    P33334   PRP8_YEAST    2147   2413             
SEQADV 5M5P GLY A  267  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P ALA A  268  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P GLU A  269  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P PHE A  270  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P GLY B 2144  UNP  P33334              EXPRESSION TAG                 
SEQADV 5M5P ALA B 2145  UNP  P33334              EXPRESSION TAG                 
SEQADV 5M5P MET B 2146  UNP  P33334              EXPRESSION TAG                 
SEQADV 5M5P GLY C  267  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P ALA C  268  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P GLU C  269  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P PHE C  270  UNP  P32639              EXPRESSION TAG                 
SEQADV 5M5P GLY D 2144  UNP  P33334              EXPRESSION TAG                 
SEQADV 5M5P ALA D 2145  UNP  P33334              EXPRESSION TAG                 
SEQADV 5M5P MET D 2146  UNP  P33334              EXPRESSION TAG                 
SEQRES   1 A 1897  GLY ALA GLU PHE LYS LEU SER ASP SER LYS THR SER ASN          
SEQRES   2 A 1897  ILE GLU SER VAL PRO ILE TYR SER ILE ASP GLU PHE PHE          
SEQRES   3 A 1897  LEU GLN ARG LYS LEU ARG SER GLU LEU GLY TYR LYS ASP          
SEQRES   4 A 1897  THR SER VAL ILE GLN ASP LEU SER GLU LYS ILE LEU ASN          
SEQRES   5 A 1897  ASP ILE GLU THR LEU GLU HIS ASN PRO VAL ALA LEU GLU          
SEQRES   6 A 1897  GLN LYS LEU VAL ASP LEU LEU LYS PHE GLU ASN ILE SER          
SEQRES   7 A 1897  LEU ALA GLU PHE ILE LEU LYS ASN ARG SER THR ILE PHE          
SEQRES   8 A 1897  TRP GLY ILE ARG LEU ALA LYS SER THR GLU ASN GLU ILE          
SEQRES   9 A 1897  PRO ASN LEU ILE GLU LYS MET VAL ALA LYS GLY LEU ASN          
SEQRES  10 A 1897  ASP LEU VAL GLU GLN TYR LYS PHE ARG GLU THR THR HIS          
SEQRES  11 A 1897  SER LYS ARG GLU LEU ASP SER GLY ASP ASP GLN PRO GLN          
SEQRES  12 A 1897  SER SER GLU ALA LYS ARG THR LYS PHE SER ASN PRO ALA          
SEQRES  13 A 1897  ILE PRO PRO VAL ILE ASP LEU GLU LYS ILE LYS PHE ASP          
SEQRES  14 A 1897  GLU SER SER LYS LEU MET THR VAL THR LYS VAL SER LEU          
SEQRES  15 A 1897  PRO GLU GLY SER PHE LYS ARG VAL LYS PRO GLN TYR ASP          
SEQRES  16 A 1897  GLU ILE HIS ILE PRO ALA PRO SER LYS PRO VAL ILE ASP          
SEQRES  17 A 1897  TYR GLU LEU LYS GLU ILE THR SER LEU PRO ASP TRP CYS          
SEQRES  18 A 1897  GLN GLU ALA PHE PRO SER SER GLU THR THR SER LEU ASN          
SEQRES  19 A 1897  PRO ILE GLN SER LYS VAL PHE HIS ALA ALA PHE GLU GLY          
SEQRES  20 A 1897  ASP SER ASN MET LEU ILE CYS ALA PRO THR GLY SER GLY          
SEQRES  21 A 1897  LYS THR ASN ILE ALA LEU LEU THR VAL LEU LYS ALA LEU          
SEQRES  22 A 1897  SER HIS HIS TYR ASN PRO LYS THR LYS LYS LEU ASN LEU          
SEQRES  23 A 1897  SER ALA PHE LYS ILE VAL TYR ILE ALA PRO LEU LYS ALA          
SEQRES  24 A 1897  LEU VAL GLN GLU GLN VAL ARG GLU PHE GLN ARG ARG LEU          
SEQRES  25 A 1897  ALA PHE LEU GLY ILE LYS VAL ALA GLU LEU THR GLY ASP          
SEQRES  26 A 1897  SER ARG LEU SER ARG LYS GLN ILE ASP GLU THR GLN VAL          
SEQRES  27 A 1897  LEU VAL SER THR PRO GLU LYS TRP ASP ILE THR THR ARG          
SEQRES  28 A 1897  ASN SER ASN ASN LEU ALA ILE VAL GLU LEU VAL ARG LEU          
SEQRES  29 A 1897  LEU ILE ILE ASP GLU ILE HIS LEU LEU HIS ASP ASP ARG          
SEQRES  30 A 1897  GLY PRO VAL LEU GLU SER ILE VAL ALA ARG THR PHE TRP          
SEQRES  31 A 1897  ALA SER LYS TYR GLY GLN GLU TYR PRO ARG ILE ILE GLY          
SEQRES  32 A 1897  LEU SER ALA THR LEU PRO ASN TYR GLU ASP VAL GLY ARG          
SEQRES  33 A 1897  PHE LEU ARG VAL PRO LYS GLU GLY LEU PHE TYR PHE ASP          
SEQRES  34 A 1897  SER SER PHE ARG PRO CYS PRO LEU SER GLN GLN PHE CYS          
SEQRES  35 A 1897  GLY ILE LYS GLU ARG ASN SER LEU LYS LYS LEU LYS ALA          
SEQRES  36 A 1897  MET ASN ASP ALA CYS TYR GLU LYS VAL LEU GLU SER ILE          
SEQRES  37 A 1897  ASN GLU GLY ASN GLN ILE ILE VAL PHE VAL HIS SER ARG          
SEQRES  38 A 1897  LYS GLU THR SER ARG THR ALA THR TRP LEU LYS ASN LYS          
SEQRES  39 A 1897  PHE ALA GLU GLU ASN ILE THR HIS LYS LEU THR LYS ASN          
SEQRES  40 A 1897  ASP ALA GLY SER LYS GLN ILE LEU LYS THR GLU ALA ALA          
SEQRES  41 A 1897  ASN VAL LEU ASP PRO SER LEU ARG LYS LEU ILE GLU SER          
SEQRES  42 A 1897  GLY ILE GLY THR HIS HIS ALA GLY LEU THR ARG SER ASP          
SEQRES  43 A 1897  ARG SER LEU SER GLU ASP LEU PHE ALA ASP GLY LEU LEU          
SEQRES  44 A 1897  GLN VAL LEU VAL CYS THR ALA THR LEU ALA TRP GLY VAL          
SEQRES  45 A 1897  ASN LEU PRO ALA HIS THR VAL ILE ILE LYS GLY THR ASP          
SEQRES  46 A 1897  VAL TYR SER PRO GLU LYS GLY SER TRP GLU GLN LEU SER          
SEQRES  47 A 1897  PRO GLN ASP VAL LEU GLN MET LEU GLY ARG ALA GLY ARG          
SEQRES  48 A 1897  PRO ARG TYR ASP THR PHE GLY GLU GLY ILE ILE ILE THR          
SEQRES  49 A 1897  ASP GLN SER ASN VAL GLN TYR TYR LEU SER VAL LEU ASN          
SEQRES  50 A 1897  GLN GLN LEU PRO ILE GLU SER GLN PHE VAL SER LYS LEU          
SEQRES  51 A 1897  VAL ASP ASN LEU ASN ALA GLU VAL VAL ALA GLY ASN ILE          
SEQRES  52 A 1897  LYS CYS ARG ASN ASP ALA VAL ASN TRP LEU ALA TYR THR          
SEQRES  53 A 1897  TYR LEU TYR VAL ARG MET LEU ALA SER PRO MET LEU TYR          
SEQRES  54 A 1897  LYS VAL PRO ASP ILE SER SER ASP GLY GLN LEU LYS LYS          
SEQRES  55 A 1897  PHE ARG GLU SER LEU VAL HIS SER ALA LEU CYS ILE LEU          
SEQRES  56 A 1897  LYS GLU GLN GLU LEU VAL LEU TYR ASP ALA GLU ASN ASP          
SEQRES  57 A 1897  VAL ILE GLU ALA THR ASP LEU GLY ASN ILE ALA SER SER          
SEQRES  58 A 1897  PHE TYR ILE ASN HIS ALA SER MET ASP VAL TYR ASN ARG          
SEQRES  59 A 1897  GLU LEU ASP GLU HIS THR THR GLN ILE ASP LEU PHE ARG          
SEQRES  60 A 1897  ILE PHE SER MET SER GLU GLU PHE LYS TYR VAL SER VAL          
SEQRES  61 A 1897  ARG TYR GLU GLU LYS ARG GLU LEU LYS GLN LEU LEU GLU          
SEQRES  62 A 1897  LYS ALA PRO ILE PRO ILE ARG GLU ASP ILE ASP ASP PRO          
SEQRES  63 A 1897  LEU ALA LYS VAL ASN VAL LEU LEU GLN SER TYR PHE SER          
SEQRES  64 A 1897  GLN LEU LYS PHE GLU GLY PHE ALA LEU ASN SER ASP ILE          
SEQRES  65 A 1897  VAL PHE ILE HIS GLN ASN ALA GLY ARG LEU LEU ARG ALA          
SEQRES  66 A 1897  MET PHE GLU ILE CYS LEU LYS ARG GLY TRP GLY HIS PRO          
SEQRES  67 A 1897  THR ARG MET LEU LEU ASN LEU CYS LYS SER ALA THR THR          
SEQRES  68 A 1897  LYS MET TRP PRO THR ASN CYS PRO LEU ARG GLN PHE LYS          
SEQRES  69 A 1897  THR CYS PRO VAL GLU VAL ILE LYS ARG LEU GLU ALA SER          
SEQRES  70 A 1897  THR VAL PRO TRP GLY ASP TYR LEU GLN LEU GLU THR PRO          
SEQRES  71 A 1897  ALA GLU VAL GLY ARG ALA ILE ARG SER GLU LYS TYR GLY          
SEQRES  72 A 1897  LYS GLN VAL TYR ASP LEU LEU LYS ARG PHE PRO LYS MET          
SEQRES  73 A 1897  SER VAL THR CYS ASN ALA GLN PRO ILE THR ARG SER VAL          
SEQRES  74 A 1897  MET ARG PHE ASN ILE GLU ILE ILE ALA ASP TRP ILE TRP          
SEQRES  75 A 1897  ASP MET ASN VAL HIS GLY SER LEU GLU PRO PHE LEU LEU          
SEQRES  76 A 1897  MET LEU GLU ASP THR ASP GLY ASP SER ILE LEU TYR TYR          
SEQRES  77 A 1897  ASP VAL LEU PHE ILE THR PRO ASP ILE VAL GLY HIS GLU          
SEQRES  78 A 1897  PHE THR LEU SER PHE THR TYR GLU LEU LYS GLN HIS ASN          
SEQRES  79 A 1897  GLN ASN ASN LEU PRO PRO ASN PHE PHE LEU THR LEU ILE          
SEQRES  80 A 1897  SER GLU ASN TRP TRP HIS SER GLU PHE GLU ILE PRO VAL          
SEQRES  81 A 1897  SER PHE ASN GLY PHE LYS LEU PRO LYS LYS PHE PRO PRO          
SEQRES  82 A 1897  PRO THR PRO LEU LEU GLU ASN ILE SER ILE SER THR SER          
SEQRES  83 A 1897  GLU LEU GLY ASN ASP ASP PHE SER GLU VAL PHE GLU PHE          
SEQRES  84 A 1897  LYS THR PHE ASN LYS ILE GLN SER GLN VAL PHE GLU SER          
SEQRES  85 A 1897  LEU TYR ASN SER ASN ASP SER VAL PHE VAL GLY SER GLY          
SEQRES  86 A 1897  LYS GLY THR GLY LYS THR ALA MET ALA GLU LEU ALA LEU          
SEQRES  87 A 1897  LEU ASN HIS TRP ARG GLN ASN LYS GLY ARG ALA VAL TYR          
SEQRES  88 A 1897  ILE ASN PRO SER GLY GLU LYS ILE ASP PHE LEU LEU SER          
SEQRES  89 A 1897  ASP TRP ASN LYS ARG PHE SER HIS LEU ALA GLY GLY LYS          
SEQRES  90 A 1897  ILE ILE ASN LYS LEU GLY ASN ASP PRO SER LEU ASN LEU          
SEQRES  91 A 1897  LYS LEU LEU ALA LYS SER HIS VAL LEU LEU ALA THR PRO          
SEQRES  92 A 1897  VAL GLN PHE GLU LEU LEU SER ARG ARG TRP ARG GLN ARG          
SEQRES  93 A 1897  LYS ASN ILE GLN SER LEU GLU LEU MET ILE TYR ASP ASP          
SEQRES  94 A 1897  ALA HIS GLU ILE SER GLN GLY VAL TYR GLY ALA VAL TYR          
SEQRES  95 A 1897  GLU THR LEU ILE SER ARG MET ILE PHE ILE ALA THR GLN          
SEQRES  96 A 1897  LEU GLU LYS LYS ILE ARG PHE VAL CYS LEU SER ASN CYS          
SEQRES  97 A 1897  LEU ALA ASN ALA ARG ASP PHE GLY GLU TRP ALA GLY MET          
SEQRES  98 A 1897  THR LYS SER ASN ILE TYR ASN PHE SER PRO SER GLU ARG          
SEQRES  99 A 1897  ILE GLU PRO LEU GLU ILE ASN ILE GLN SER PHE LYS ASP          
SEQRES 100 A 1897  VAL GLU HIS ILE SER PHE ASN PHE SER MET LEU GLN MET          
SEQRES 101 A 1897  ALA PHE GLU ALA SER ALA ALA ALA ALA GLY ASN ARG ASN          
SEQRES 102 A 1897  SER SER SER VAL PHE LEU PRO SER ARG LYS ASP CYS MET          
SEQRES 103 A 1897  GLU VAL ALA SER ALA PHE MET LYS PHE SER LYS ALA ILE          
SEQRES 104 A 1897  GLU TRP ASP MET LEU ASN VAL GLU GLU GLU GLN ILE VAL          
SEQRES 105 A 1897  PRO TYR ILE GLU LYS LEU THR ASP GLY HIS LEU ARG ALA          
SEQRES 106 A 1897  PRO LEU LYS HIS GLY VAL GLY ILE LEU TYR LYS GLY MET          
SEQRES 107 A 1897  ALA SER ASN ASP GLU ARG ILE VAL LYS ARG LEU TYR GLU          
SEQRES 108 A 1897  TYR GLY ALA VAL SER VAL LEU LEU ILE SER LYS ASP CYS          
SEQRES 109 A 1897  SER ALA PHE ALA CYS LYS THR ASP GLU VAL ILE ILE LEU          
SEQRES 110 A 1897  GLY THR ASN LEU TYR ASP GLY ALA GLU HIS LYS TYR MET          
SEQRES 111 A 1897  PRO TYR THR ILE ASN GLU LEU LEU GLU MET VAL GLY LEU          
SEQRES 112 A 1897  ALA SER GLY ASN ASP SER MET ALA GLY LYS VAL LEU ILE          
SEQRES 113 A 1897  LEU THR SER HIS ASN MET LYS ALA TYR TYR LYS LYS PHE          
SEQRES 114 A 1897  LEU ILE GLU PRO LEU PRO THR GLU SER TYR LEU GLN TYR          
SEQRES 115 A 1897  ILE ILE HIS ASP THR LEU ASN ASN GLU ILE ALA ASN SER          
SEQRES 116 A 1897  ILE ILE GLN SER LYS GLN ASP CYS VAL ASP TRP PHE THR          
SEQRES 117 A 1897  TYR SER TYR PHE TYR ARG ARG ILE HIS VAL ASN PRO SER          
SEQRES 118 A 1897  TYR TYR GLY VAL ARG ASP THR SER PRO HIS GLY ILE SER          
SEQRES 119 A 1897  VAL PHE LEU SER ASN LEU VAL GLU THR CYS LEU ASN ASP          
SEQRES 120 A 1897  LEU VAL GLU SER SER PHE ILE GLU ILE ASP ASP THR GLU          
SEQRES 121 A 1897  ALA GLU VAL THR ALA GLU VAL ASN GLY GLY ASP ASP GLU          
SEQRES 122 A 1897  ALA THR GLU ILE ILE SER THR LEU SER ASN GLY LEU ILE          
SEQRES 123 A 1897  ALA SER HIS TYR GLY VAL SER PHE PHE THR ILE GLN SER          
SEQRES 124 A 1897  PHE VAL SER SER LEU SER ASN THR SER THR LEU LYS ASN          
SEQRES 125 A 1897  MET LEU TYR VAL LEU SER THR ALA VAL GLU PHE GLU SER          
SEQRES 126 A 1897  VAL PRO LEU ARG LYS GLY ASP ARG ALA LEU LEU VAL LYS          
SEQRES 127 A 1897  LEU SER LYS ARG LEU PRO LEU ARG PHE PRO GLU HIS THR          
SEQRES 128 A 1897  SER SER GLY SER VAL SER PHE LYS VAL PHE LEU LEU LEU          
SEQRES 129 A 1897  GLN ALA TYR PHE SER ARG LEU GLU LEU PRO VAL ASP PHE          
SEQRES 130 A 1897  GLN ASN ASP LEU LYS ASP ILE LEU GLU LYS VAL VAL PRO          
SEQRES 131 A 1897  LEU ILE ASN VAL VAL VAL ASP ILE LEU SER ALA ASN GLY          
SEQRES 132 A 1897  TYR LEU ASN ALA THR THR ALA MET ASP LEU ALA GLN MET          
SEQRES 133 A 1897  LEU ILE GLN GLY VAL TRP ASP VAL ASP ASN PRO LEU ARG          
SEQRES 134 A 1897  GLN ILE PRO HIS PHE ASN ASN LYS ILE LEU GLU LYS CYS          
SEQRES 135 A 1897  LYS GLU ILE ASN VAL GLU THR VAL TYR ASP ILE MET ALA          
SEQRES 136 A 1897  LEU GLU ASP GLU GLU ARG ASP GLU ILE LEU THR LEU THR          
SEQRES 137 A 1897  ASP SER GLN LEU ALA GLN VAL ALA ALA PHE VAL ASN ASN          
SEQRES 138 A 1897  TYR PRO ASN VAL GLU LEU THR TYR SER LEU ASN ASN SER          
SEQRES 139 A 1897  ASP SER LEU ILE SER GLY VAL LYS GLN LYS ILE THR ILE          
SEQRES 140 A 1897  GLN LEU THR ARG ASP VAL GLU PRO GLU ASN LEU GLN VAL          
SEQRES 141 A 1897  THR SER GLU LYS TYR PRO PHE ASP LYS LEU GLU SER TRP          
SEQRES 142 A 1897  TRP LEU VAL LEU GLY GLU VAL SER LYS LYS GLU LEU TYR          
SEQRES 143 A 1897  ALA ILE LYS LYS VAL THR LEU ASN LYS GLU THR GLN GLN          
SEQRES 144 A 1897  TYR GLU LEU GLU PHE ASP THR PRO THR SER GLY LYS HIS          
SEQRES 145 A 1897  ASN LEU THR ILE TRP CYS VAL CYS ASP SER TYR LEU ASP          
SEQRES 146 A 1897  ALA ASP LYS GLU LEU SER PHE GLU ILE ASN VAL LYS              
SEQRES   1 B  270  GLY ALA MET SER SER LYS ASN GLU TRP ARG LYS SER ALA          
SEQRES   2 B  270  ILE ALA ASN THR LEU LEU TYR LEU ARG LEU LYS ASN ILE          
SEQRES   3 B  270  TYR VAL SER ALA ASP ASP PHE VAL GLU GLU GLN ASN VAL          
SEQRES   4 B  270  TYR VAL LEU PRO LYS ASN LEU LEU LYS LYS PHE ILE GLU          
SEQRES   5 B  270  ILE SER ASP VAL LYS ILE GLN VAL ALA ALA PHE ILE TYR          
SEQRES   6 B  270  GLY MET SER ALA LYS ASP HIS PRO LYS VAL LYS GLU ILE          
SEQRES   7 B  270  LYS THR VAL VAL LEU VAL PRO GLN LEU GLY HIS VAL GLY          
SEQRES   8 B  270  SER VAL GLN ILE SER ASN ILE PRO ASP ILE GLY ASP LEU          
SEQRES   9 B  270  PRO ASP THR GLU GLY LEU GLU LEU LEU GLY TRP ILE HIS          
SEQRES  10 B  270  THR GLN THR GLU GLU LEU LYS PHE MET ALA ALA SER GLU          
SEQRES  11 B  270  VAL ALA THR HIS SER LYS LEU PHE ALA ASP LYS LYS ARG          
SEQRES  12 B  270  ASP CYS ILE ASP ILE SER ILE PHE SER THR PRO GLY SER          
SEQRES  13 B  270  VAL SER LEU SER ALA TYR ASN LEU THR ASP GLU GLY TYR          
SEQRES  14 B  270  GLN TRP GLY GLU GLU ASN LYS ASP ILE MET ASN VAL LEU          
SEQRES  15 B  270  SER GLU GLY PHE GLU PRO THR PHE SER THR HIS ALA GLN          
SEQRES  16 B  270  LEU LEU LEU SER ASP ARG ILE THR GLY ASN PHE ILE ILE          
SEQRES  17 B  270  PRO SER GLY ASN VAL TRP ASN TYR THR PHE MET GLY THR          
SEQRES  18 B  270  ALA PHE ASN GLN GLU GLY ASP TYR ASN PHE LYS TYR GLY          
SEQRES  19 B  270  ILE PRO LEU GLU PHE TYR ASN GLU MET HIS ARG PRO VAL          
SEQRES  20 B  270  HIS PHE LEU GLN PHE SER GLU LEU ALA GLY ASP GLU GLU          
SEQRES  21 B  270  LEU GLU ALA GLU GLN ILE ASP VAL PHE SER                      
SEQRES   1 C 1897  GLY ALA GLU PHE LYS LEU SER ASP SER LYS THR SER ASN          
SEQRES   2 C 1897  ILE GLU SER VAL PRO ILE TYR SER ILE ASP GLU PHE PHE          
SEQRES   3 C 1897  LEU GLN ARG LYS LEU ARG SER GLU LEU GLY TYR LYS ASP          
SEQRES   4 C 1897  THR SER VAL ILE GLN ASP LEU SER GLU LYS ILE LEU ASN          
SEQRES   5 C 1897  ASP ILE GLU THR LEU GLU HIS ASN PRO VAL ALA LEU GLU          
SEQRES   6 C 1897  GLN LYS LEU VAL ASP LEU LEU LYS PHE GLU ASN ILE SER          
SEQRES   7 C 1897  LEU ALA GLU PHE ILE LEU LYS ASN ARG SER THR ILE PHE          
SEQRES   8 C 1897  TRP GLY ILE ARG LEU ALA LYS SER THR GLU ASN GLU ILE          
SEQRES   9 C 1897  PRO ASN LEU ILE GLU LYS MET VAL ALA LYS GLY LEU ASN          
SEQRES  10 C 1897  ASP LEU VAL GLU GLN TYR LYS PHE ARG GLU THR THR HIS          
SEQRES  11 C 1897  SER LYS ARG GLU LEU ASP SER GLY ASP ASP GLN PRO GLN          
SEQRES  12 C 1897  SER SER GLU ALA LYS ARG THR LYS PHE SER ASN PRO ALA          
SEQRES  13 C 1897  ILE PRO PRO VAL ILE ASP LEU GLU LYS ILE LYS PHE ASP          
SEQRES  14 C 1897  GLU SER SER LYS LEU MET THR VAL THR LYS VAL SER LEU          
SEQRES  15 C 1897  PRO GLU GLY SER PHE LYS ARG VAL LYS PRO GLN TYR ASP          
SEQRES  16 C 1897  GLU ILE HIS ILE PRO ALA PRO SER LYS PRO VAL ILE ASP          
SEQRES  17 C 1897  TYR GLU LEU LYS GLU ILE THR SER LEU PRO ASP TRP CYS          
SEQRES  18 C 1897  GLN GLU ALA PHE PRO SER SER GLU THR THR SER LEU ASN          
SEQRES  19 C 1897  PRO ILE GLN SER LYS VAL PHE HIS ALA ALA PHE GLU GLY          
SEQRES  20 C 1897  ASP SER ASN MET LEU ILE CYS ALA PRO THR GLY SER GLY          
SEQRES  21 C 1897  LYS THR ASN ILE ALA LEU LEU THR VAL LEU LYS ALA LEU          
SEQRES  22 C 1897  SER HIS HIS TYR ASN PRO LYS THR LYS LYS LEU ASN LEU          
SEQRES  23 C 1897  SER ALA PHE LYS ILE VAL TYR ILE ALA PRO LEU LYS ALA          
SEQRES  24 C 1897  LEU VAL GLN GLU GLN VAL ARG GLU PHE GLN ARG ARG LEU          
SEQRES  25 C 1897  ALA PHE LEU GLY ILE LYS VAL ALA GLU LEU THR GLY ASP          
SEQRES  26 C 1897  SER ARG LEU SER ARG LYS GLN ILE ASP GLU THR GLN VAL          
SEQRES  27 C 1897  LEU VAL SER THR PRO GLU LYS TRP ASP ILE THR THR ARG          
SEQRES  28 C 1897  ASN SER ASN ASN LEU ALA ILE VAL GLU LEU VAL ARG LEU          
SEQRES  29 C 1897  LEU ILE ILE ASP GLU ILE HIS LEU LEU HIS ASP ASP ARG          
SEQRES  30 C 1897  GLY PRO VAL LEU GLU SER ILE VAL ALA ARG THR PHE TRP          
SEQRES  31 C 1897  ALA SER LYS TYR GLY GLN GLU TYR PRO ARG ILE ILE GLY          
SEQRES  32 C 1897  LEU SER ALA THR LEU PRO ASN TYR GLU ASP VAL GLY ARG          
SEQRES  33 C 1897  PHE LEU ARG VAL PRO LYS GLU GLY LEU PHE TYR PHE ASP          
SEQRES  34 C 1897  SER SER PHE ARG PRO CYS PRO LEU SER GLN GLN PHE CYS          
SEQRES  35 C 1897  GLY ILE LYS GLU ARG ASN SER LEU LYS LYS LEU LYS ALA          
SEQRES  36 C 1897  MET ASN ASP ALA CYS TYR GLU LYS VAL LEU GLU SER ILE          
SEQRES  37 C 1897  ASN GLU GLY ASN GLN ILE ILE VAL PHE VAL HIS SER ARG          
SEQRES  38 C 1897  LYS GLU THR SER ARG THR ALA THR TRP LEU LYS ASN LYS          
SEQRES  39 C 1897  PHE ALA GLU GLU ASN ILE THR HIS LYS LEU THR LYS ASN          
SEQRES  40 C 1897  ASP ALA GLY SER LYS GLN ILE LEU LYS THR GLU ALA ALA          
SEQRES  41 C 1897  ASN VAL LEU ASP PRO SER LEU ARG LYS LEU ILE GLU SER          
SEQRES  42 C 1897  GLY ILE GLY THR HIS HIS ALA GLY LEU THR ARG SER ASP          
SEQRES  43 C 1897  ARG SER LEU SER GLU ASP LEU PHE ALA ASP GLY LEU LEU          
SEQRES  44 C 1897  GLN VAL LEU VAL CYS THR ALA THR LEU ALA TRP GLY VAL          
SEQRES  45 C 1897  ASN LEU PRO ALA HIS THR VAL ILE ILE LYS GLY THR ASP          
SEQRES  46 C 1897  VAL TYR SER PRO GLU LYS GLY SER TRP GLU GLN LEU SER          
SEQRES  47 C 1897  PRO GLN ASP VAL LEU GLN MET LEU GLY ARG ALA GLY ARG          
SEQRES  48 C 1897  PRO ARG TYR ASP THR PHE GLY GLU GLY ILE ILE ILE THR          
SEQRES  49 C 1897  ASP GLN SER ASN VAL GLN TYR TYR LEU SER VAL LEU ASN          
SEQRES  50 C 1897  GLN GLN LEU PRO ILE GLU SER GLN PHE VAL SER LYS LEU          
SEQRES  51 C 1897  VAL ASP ASN LEU ASN ALA GLU VAL VAL ALA GLY ASN ILE          
SEQRES  52 C 1897  LYS CYS ARG ASN ASP ALA VAL ASN TRP LEU ALA TYR THR          
SEQRES  53 C 1897  TYR LEU TYR VAL ARG MET LEU ALA SER PRO MET LEU TYR          
SEQRES  54 C 1897  LYS VAL PRO ASP ILE SER SER ASP GLY GLN LEU LYS LYS          
SEQRES  55 C 1897  PHE ARG GLU SER LEU VAL HIS SER ALA LEU CYS ILE LEU          
SEQRES  56 C 1897  LYS GLU GLN GLU LEU VAL LEU TYR ASP ALA GLU ASN ASP          
SEQRES  57 C 1897  VAL ILE GLU ALA THR ASP LEU GLY ASN ILE ALA SER SER          
SEQRES  58 C 1897  PHE TYR ILE ASN HIS ALA SER MET ASP VAL TYR ASN ARG          
SEQRES  59 C 1897  GLU LEU ASP GLU HIS THR THR GLN ILE ASP LEU PHE ARG          
SEQRES  60 C 1897  ILE PHE SER MET SER GLU GLU PHE LYS TYR VAL SER VAL          
SEQRES  61 C 1897  ARG TYR GLU GLU LYS ARG GLU LEU LYS GLN LEU LEU GLU          
SEQRES  62 C 1897  LYS ALA PRO ILE PRO ILE ARG GLU ASP ILE ASP ASP PRO          
SEQRES  63 C 1897  LEU ALA LYS VAL ASN VAL LEU LEU GLN SER TYR PHE SER          
SEQRES  64 C 1897  GLN LEU LYS PHE GLU GLY PHE ALA LEU ASN SER ASP ILE          
SEQRES  65 C 1897  VAL PHE ILE HIS GLN ASN ALA GLY ARG LEU LEU ARG ALA          
SEQRES  66 C 1897  MET PHE GLU ILE CYS LEU LYS ARG GLY TRP GLY HIS PRO          
SEQRES  67 C 1897  THR ARG MET LEU LEU ASN LEU CYS LYS SER ALA THR THR          
SEQRES  68 C 1897  LYS MET TRP PRO THR ASN CYS PRO LEU ARG GLN PHE LYS          
SEQRES  69 C 1897  THR CYS PRO VAL GLU VAL ILE LYS ARG LEU GLU ALA SER          
SEQRES  70 C 1897  THR VAL PRO TRP GLY ASP TYR LEU GLN LEU GLU THR PRO          
SEQRES  71 C 1897  ALA GLU VAL GLY ARG ALA ILE ARG SER GLU LYS TYR GLY          
SEQRES  72 C 1897  LYS GLN VAL TYR ASP LEU LEU LYS ARG PHE PRO LYS MET          
SEQRES  73 C 1897  SER VAL THR CYS ASN ALA GLN PRO ILE THR ARG SER VAL          
SEQRES  74 C 1897  MET ARG PHE ASN ILE GLU ILE ILE ALA ASP TRP ILE TRP          
SEQRES  75 C 1897  ASP MET ASN VAL HIS GLY SER LEU GLU PRO PHE LEU LEU          
SEQRES  76 C 1897  MET LEU GLU ASP THR ASP GLY ASP SER ILE LEU TYR TYR          
SEQRES  77 C 1897  ASP VAL LEU PHE ILE THR PRO ASP ILE VAL GLY HIS GLU          
SEQRES  78 C 1897  PHE THR LEU SER PHE THR TYR GLU LEU LYS GLN HIS ASN          
SEQRES  79 C 1897  GLN ASN ASN LEU PRO PRO ASN PHE PHE LEU THR LEU ILE          
SEQRES  80 C 1897  SER GLU ASN TRP TRP HIS SER GLU PHE GLU ILE PRO VAL          
SEQRES  81 C 1897  SER PHE ASN GLY PHE LYS LEU PRO LYS LYS PHE PRO PRO          
SEQRES  82 C 1897  PRO THR PRO LEU LEU GLU ASN ILE SER ILE SER THR SER          
SEQRES  83 C 1897  GLU LEU GLY ASN ASP ASP PHE SER GLU VAL PHE GLU PHE          
SEQRES  84 C 1897  LYS THR PHE ASN LYS ILE GLN SER GLN VAL PHE GLU SER          
SEQRES  85 C 1897  LEU TYR ASN SER ASN ASP SER VAL PHE VAL GLY SER GLY          
SEQRES  86 C 1897  LYS GLY THR GLY LYS THR ALA MET ALA GLU LEU ALA LEU          
SEQRES  87 C 1897  LEU ASN HIS TRP ARG GLN ASN LYS GLY ARG ALA VAL TYR          
SEQRES  88 C 1897  ILE ASN PRO SER GLY GLU LYS ILE ASP PHE LEU LEU SER          
SEQRES  89 C 1897  ASP TRP ASN LYS ARG PHE SER HIS LEU ALA GLY GLY LYS          
SEQRES  90 C 1897  ILE ILE ASN LYS LEU GLY ASN ASP PRO SER LEU ASN LEU          
SEQRES  91 C 1897  LYS LEU LEU ALA LYS SER HIS VAL LEU LEU ALA THR PRO          
SEQRES  92 C 1897  VAL GLN PHE GLU LEU LEU SER ARG ARG TRP ARG GLN ARG          
SEQRES  93 C 1897  LYS ASN ILE GLN SER LEU GLU LEU MET ILE TYR ASP ASP          
SEQRES  94 C 1897  ALA HIS GLU ILE SER GLN GLY VAL TYR GLY ALA VAL TYR          
SEQRES  95 C 1897  GLU THR LEU ILE SER ARG MET ILE PHE ILE ALA THR GLN          
SEQRES  96 C 1897  LEU GLU LYS LYS ILE ARG PHE VAL CYS LEU SER ASN CYS          
SEQRES  97 C 1897  LEU ALA ASN ALA ARG ASP PHE GLY GLU TRP ALA GLY MET          
SEQRES  98 C 1897  THR LYS SER ASN ILE TYR ASN PHE SER PRO SER GLU ARG          
SEQRES  99 C 1897  ILE GLU PRO LEU GLU ILE ASN ILE GLN SER PHE LYS ASP          
SEQRES 100 C 1897  VAL GLU HIS ILE SER PHE ASN PHE SER MET LEU GLN MET          
SEQRES 101 C 1897  ALA PHE GLU ALA SER ALA ALA ALA ALA GLY ASN ARG ASN          
SEQRES 102 C 1897  SER SER SER VAL PHE LEU PRO SER ARG LYS ASP CYS MET          
SEQRES 103 C 1897  GLU VAL ALA SER ALA PHE MET LYS PHE SER LYS ALA ILE          
SEQRES 104 C 1897  GLU TRP ASP MET LEU ASN VAL GLU GLU GLU GLN ILE VAL          
SEQRES 105 C 1897  PRO TYR ILE GLU LYS LEU THR ASP GLY HIS LEU ARG ALA          
SEQRES 106 C 1897  PRO LEU LYS HIS GLY VAL GLY ILE LEU TYR LYS GLY MET          
SEQRES 107 C 1897  ALA SER ASN ASP GLU ARG ILE VAL LYS ARG LEU TYR GLU          
SEQRES 108 C 1897  TYR GLY ALA VAL SER VAL LEU LEU ILE SER LYS ASP CYS          
SEQRES 109 C 1897  SER ALA PHE ALA CYS LYS THR ASP GLU VAL ILE ILE LEU          
SEQRES 110 C 1897  GLY THR ASN LEU TYR ASP GLY ALA GLU HIS LYS TYR MET          
SEQRES 111 C 1897  PRO TYR THR ILE ASN GLU LEU LEU GLU MET VAL GLY LEU          
SEQRES 112 C 1897  ALA SER GLY ASN ASP SER MET ALA GLY LYS VAL LEU ILE          
SEQRES 113 C 1897  LEU THR SER HIS ASN MET LYS ALA TYR TYR LYS LYS PHE          
SEQRES 114 C 1897  LEU ILE GLU PRO LEU PRO THR GLU SER TYR LEU GLN TYR          
SEQRES 115 C 1897  ILE ILE HIS ASP THR LEU ASN ASN GLU ILE ALA ASN SER          
SEQRES 116 C 1897  ILE ILE GLN SER LYS GLN ASP CYS VAL ASP TRP PHE THR          
SEQRES 117 C 1897  TYR SER TYR PHE TYR ARG ARG ILE HIS VAL ASN PRO SER          
SEQRES 118 C 1897  TYR TYR GLY VAL ARG ASP THR SER PRO HIS GLY ILE SER          
SEQRES 119 C 1897  VAL PHE LEU SER ASN LEU VAL GLU THR CYS LEU ASN ASP          
SEQRES 120 C 1897  LEU VAL GLU SER SER PHE ILE GLU ILE ASP ASP THR GLU          
SEQRES 121 C 1897  ALA GLU VAL THR ALA GLU VAL ASN GLY GLY ASP ASP GLU          
SEQRES 122 C 1897  ALA THR GLU ILE ILE SER THR LEU SER ASN GLY LEU ILE          
SEQRES 123 C 1897  ALA SER HIS TYR GLY VAL SER PHE PHE THR ILE GLN SER          
SEQRES 124 C 1897  PHE VAL SER SER LEU SER ASN THR SER THR LEU LYS ASN          
SEQRES 125 C 1897  MET LEU TYR VAL LEU SER THR ALA VAL GLU PHE GLU SER          
SEQRES 126 C 1897  VAL PRO LEU ARG LYS GLY ASP ARG ALA LEU LEU VAL LYS          
SEQRES 127 C 1897  LEU SER LYS ARG LEU PRO LEU ARG PHE PRO GLU HIS THR          
SEQRES 128 C 1897  SER SER GLY SER VAL SER PHE LYS VAL PHE LEU LEU LEU          
SEQRES 129 C 1897  GLN ALA TYR PHE SER ARG LEU GLU LEU PRO VAL ASP PHE          
SEQRES 130 C 1897  GLN ASN ASP LEU LYS ASP ILE LEU GLU LYS VAL VAL PRO          
SEQRES 131 C 1897  LEU ILE ASN VAL VAL VAL ASP ILE LEU SER ALA ASN GLY          
SEQRES 132 C 1897  TYR LEU ASN ALA THR THR ALA MET ASP LEU ALA GLN MET          
SEQRES 133 C 1897  LEU ILE GLN GLY VAL TRP ASP VAL ASP ASN PRO LEU ARG          
SEQRES 134 C 1897  GLN ILE PRO HIS PHE ASN ASN LYS ILE LEU GLU LYS CYS          
SEQRES 135 C 1897  LYS GLU ILE ASN VAL GLU THR VAL TYR ASP ILE MET ALA          
SEQRES 136 C 1897  LEU GLU ASP GLU GLU ARG ASP GLU ILE LEU THR LEU THR          
SEQRES 137 C 1897  ASP SER GLN LEU ALA GLN VAL ALA ALA PHE VAL ASN ASN          
SEQRES 138 C 1897  TYR PRO ASN VAL GLU LEU THR TYR SER LEU ASN ASN SER          
SEQRES 139 C 1897  ASP SER LEU ILE SER GLY VAL LYS GLN LYS ILE THR ILE          
SEQRES 140 C 1897  GLN LEU THR ARG ASP VAL GLU PRO GLU ASN LEU GLN VAL          
SEQRES 141 C 1897  THR SER GLU LYS TYR PRO PHE ASP LYS LEU GLU SER TRP          
SEQRES 142 C 1897  TRP LEU VAL LEU GLY GLU VAL SER LYS LYS GLU LEU TYR          
SEQRES 143 C 1897  ALA ILE LYS LYS VAL THR LEU ASN LYS GLU THR GLN GLN          
SEQRES 144 C 1897  TYR GLU LEU GLU PHE ASP THR PRO THR SER GLY LYS HIS          
SEQRES 145 C 1897  ASN LEU THR ILE TRP CYS VAL CYS ASP SER TYR LEU ASP          
SEQRES 146 C 1897  ALA ASP LYS GLU LEU SER PHE GLU ILE ASN VAL LYS              
SEQRES   1 D  270  GLY ALA MET SER SER LYS ASN GLU TRP ARG LYS SER ALA          
SEQRES   2 D  270  ILE ALA ASN THR LEU LEU TYR LEU ARG LEU LYS ASN ILE          
SEQRES   3 D  270  TYR VAL SER ALA ASP ASP PHE VAL GLU GLU GLN ASN VAL          
SEQRES   4 D  270  TYR VAL LEU PRO LYS ASN LEU LEU LYS LYS PHE ILE GLU          
SEQRES   5 D  270  ILE SER ASP VAL LYS ILE GLN VAL ALA ALA PHE ILE TYR          
SEQRES   6 D  270  GLY MET SER ALA LYS ASP HIS PRO LYS VAL LYS GLU ILE          
SEQRES   7 D  270  LYS THR VAL VAL LEU VAL PRO GLN LEU GLY HIS VAL GLY          
SEQRES   8 D  270  SER VAL GLN ILE SER ASN ILE PRO ASP ILE GLY ASP LEU          
SEQRES   9 D  270  PRO ASP THR GLU GLY LEU GLU LEU LEU GLY TRP ILE HIS          
SEQRES  10 D  270  THR GLN THR GLU GLU LEU LYS PHE MET ALA ALA SER GLU          
SEQRES  11 D  270  VAL ALA THR HIS SER LYS LEU PHE ALA ASP LYS LYS ARG          
SEQRES  12 D  270  ASP CYS ILE ASP ILE SER ILE PHE SER THR PRO GLY SER          
SEQRES  13 D  270  VAL SER LEU SER ALA TYR ASN LEU THR ASP GLU GLY TYR          
SEQRES  14 D  270  GLN TRP GLY GLU GLU ASN LYS ASP ILE MET ASN VAL LEU          
SEQRES  15 D  270  SER GLU GLY PHE GLU PRO THR PHE SER THR HIS ALA GLN          
SEQRES  16 D  270  LEU LEU LEU SER ASP ARG ILE THR GLY ASN PHE ILE ILE          
SEQRES  17 D  270  PRO SER GLY ASN VAL TRP ASN TYR THR PHE MET GLY THR          
SEQRES  18 D  270  ALA PHE ASN GLN GLU GLY ASP TYR ASN PHE LYS TYR GLY          
SEQRES  19 D  270  ILE PRO LEU GLU PHE TYR ASN GLU MET HIS ARG PRO VAL          
SEQRES  20 D  270  HIS PHE LEU GLN PHE SER GLU LEU ALA GLY ASP GLU GLU          
SEQRES  21 D  270  LEU GLU ALA GLU GLN ILE ASP VAL PHE SER                      
HELIX    1 AA1 THR A  277  SER A  282  1                                   6    
HELIX    2 AA2 PRO A  284  ILE A  288  5                                   5    
HELIX    3 AA3 PHE A  291  GLY A  302  1                                  12    
HELIX    4 AA4 ASP A  305  LEU A  323  1                                  19    
HELIX    5 AA5 ASN A  326  LEU A  338  1                                  13    
HELIX    6 AA6 ASN A  342  ASN A  352  1                                  11    
HELIX    7 AA7 ASN A  352  ALA A  363  1                                  12    
HELIX    8 AA8 SER A  365  ALA A  379  1                                  15    
HELIX    9 AA9 GLY A  381  LYS A  390  1                                  10    
HELIX   10 AB1 ASP A  428  LYS A  433  1                                   6    
HELIX   11 AB2 GLU A  479  LEU A  483  5                                   5    
HELIX   12 AB3 PRO A  484  PHE A  491  5                                   8    
HELIX   13 AB4 ASN A  500  VAL A  506  1                                   7    
HELIX   14 AB5 VAL A  506  GLU A  512  1                                   7    
HELIX   15 AB6 GLY A  526  LEU A  539  1                                  14    
HELIX   16 AB7 SER A  540  TYR A  543  5                                   4    
HELIX   17 AB8 LEU A  563  ARG A  576  1                                  14    
HELIX   18 AB9 ARG A  577  GLY A  582  5                                   6    
HELIX   19 AC1 LYS A  597  THR A  602  5                                   6    
HELIX   20 AC2 THR A  608  ASN A  618  1                                  11    
HELIX   21 AC3 SER A  619  LEU A  622  5                                   4    
HELIX   22 AC4 ILE A  636  ASP A  641  5                                   6    
HELIX   23 AC5 ARG A  643  ALA A  657  1                                  15    
HELIX   24 AC6 ASN A  676  LEU A  684  1                                   9    
HELIX   25 AC7 ASP A  695  ARG A  699  5                                   5    
HELIX   26 AC8 LEU A  716  ASN A  735  1                                  20    
HELIX   27 AC9 LYS A  748  GLU A  763  1                                  16    
HELIX   28 AD1 SER A  777  THR A  783  1                                   7    
HELIX   29 AD2 SER A  792  ILE A  797  1                                   6    
HELIX   30 AD3 THR A  809  ASP A  822  1                                  14    
HELIX   31 AD4 ALA A  832  GLY A  837  1                                   6    
HELIX   32 AD5 SER A  864  GLY A  873  1                                  10    
HELIX   33 AD6 VAL A  895  LEU A  902  1                                   8    
HELIX   34 AD7 PHE A  912  ALA A  926  1                                  15    
HELIX   35 AD8 CYS A  931  ALA A  940  1                                  10    
HELIX   36 AD9 THR A  942  SER A  951  1                                  10    
HELIX   37 AE1 ASP A  959  GLY A  964  1                                   6    
HELIX   38 AE2 LEU A  966  GLN A  984  1                                  19    
HELIX   39 AE3 THR A  999  PHE A 1008  1                                  10    
HELIX   40 AE4 ASN A 1011  LEU A 1022  1                                  12    
HELIX   41 AE5 THR A 1027  MET A 1037  1                                  11    
HELIX   42 AE6 SER A 1038  LYS A 1042  5                                   5    
HELIX   43 AE7 ARG A 1047  GLU A 1059  1                                  13    
HELIX   44 AE8 ASP A 1071  PHE A 1084  1                                  14    
HELIX   45 AE9 GLY A 1091  ARG A 1119  1                                  29    
HELIX   46 AF1 TRP A 1121  LYS A 1138  1                                  18    
HELIX   47 AF2 CYS A 1144  PHE A 1149  5                                   6    
HELIX   48 AF3 PRO A 1153  ALA A 1162  1                                  10    
HELIX   49 AF4 PRO A 1166  TYR A 1170  5                                   5    
HELIX   50 AF5 THR A 1175  ILE A 1183  1                                   9    
HELIX   51 AF6 SER A 1185  LYS A 1197  1                                  13    
HELIX   52 AF7 ASP A 1229  GLY A 1234  1                                   6    
HELIX   53 AF8 THR A 1260  VAL A 1264  5                                   5    
HELIX   54 AF9 LYS A 1277  ASN A 1283  1                                   7    
HELIX   55 AG1 SER A 1330  LEU A 1334  5                                   5    
HELIX   56 AG2 ASN A 1336  GLU A 1344  1                                   9    
HELIX   57 AG3 ASN A 1349  PHE A 1356  1                                   8    
HELIX   58 AG4 PHE A 1356  ASN A 1361  1                                   6    
HELIX   59 AG5 GLY A 1375  GLN A 1390  1                                  16    
HELIX   60 AG6 SER A 1401  ASN A 1413  1                                  13    
HELIX   61 AG7 PHE A 1416  GLY A 1421  1                                   6    
HELIX   62 AG8 ASP A 1431  LYS A 1441  1                                  11    
HELIX   63 AG9 THR A 1448  ARG A 1457  1                                  10    
HELIX   64 AH1 ARG A 1462  SER A 1467  1                                   6    
HELIX   65 AH2 ASP A 1475  SER A 1480  5                                   6    
HELIX   66 AH3 GLN A 1481  LEU A 1502  1                                  22    
HELIX   67 AH4 ASN A 1517  ALA A 1525  1                                   9    
HELIX   68 AH5 THR A 1528  SER A 1530  5                                   3    
HELIX   69 AH6 ASN A 1560  GLY A 1576  1                                  17    
HELIX   70 AH7 SER A 1587  LYS A 1603  1                                  17    
HELIX   71 AH8 ILE A 1617  LYS A 1623  5                                   7    
HELIX   72 AH9 ASP A 1626  HIS A 1628  5                                   3    
HELIX   73 AI1 LEU A 1629  HIS A 1635  1                                   7    
HELIX   74 AI2 ALA A 1645  GLY A 1659  1                                  15    
HELIX   75 AI3 ASP A 1669  PHE A 1673  5                                   5    
HELIX   76 AI4 THR A 1699  GLY A 1708  1                                  10    
HELIX   77 AI5 HIS A 1726  GLU A 1738  1                                  13    
HELIX   78 AI6 TYR A 1745  TYR A 1748  5                                   4    
HELIX   79 AI7 ILE A 1749  ASN A 1760  1                                  12    
HELIX   80 AI8 SER A 1765  THR A 1774  1                                  10    
HELIX   81 AI9 SER A 1776  HIS A 1783  1                                   8    
HELIX   82 AJ1 SER A 1795  SER A 1817  1                                  23    
HELIX   83 AJ2 LEU A 1847  GLY A 1857  1                                  11    
HELIX   84 AJ3 SER A 1859  SER A 1868  1                                  10    
HELIX   85 AJ4 THR A 1875  THR A 1885  1                                  11    
HELIX   86 AJ5 ALA A 1886  GLU A 1890  5                                   5    
HELIX   87 AJ6 ASP A 1898  LYS A 1907  1                                  10    
HELIX   88 AJ7 SER A 1921  SER A 1935  1                                  15    
HELIX   89 AJ8 PRO A 1940  LYS A 1953  1                                  14    
HELIX   90 AJ9 VAL A 1954  ASN A 1968  1                                  15    
HELIX   91 AK1 ASN A 1972  GLY A 1986  1                                  15    
HELIX   92 AK2 ASN A 2001  ILE A 2011  1                                  11    
HELIX   93 AK3 VAL A 2016  ALA A 2021  1                                   6    
HELIX   94 AK4 GLU A 2023  ASP A 2028  1                                   6    
HELIX   95 AK5 THR A 2034  ASN A 2046  1                                  13    
HELIX   96 AK6 ASN B 2150  ASN B 2159  1                                  10    
HELIX   97 AK7 THR B 2160  LYS B 2167  5                                   8    
HELIX   98 AK8 LYS B 2187  ILE B 2196  1                                  10    
HELIX   99 AK9 ALA B 2270  ALA B 2282  1                                  13    
HELIX  100 AL1 THR B 2308  ASN B 2318  1                                  11    
HELIX  101 AL2 GLU B 2330  THR B 2332  5                                   3    
HELIX  102 AL3 MET B 2362  PHE B 2366  5                                   5    
HELIX  103 AL4 ARG B 2388  LEU B 2393  1                                   6    
HELIX  104 AL5 THR C  277  SER C  282  1                                   6    
HELIX  105 AL6 PRO C  284  ILE C  288  5                                   5    
HELIX  106 AL7 PHE C  291  GLY C  302  1                                  12    
HELIX  107 AL8 ASP C  305  LEU C  323  1                                  19    
HELIX  108 AL9 ASN C  326  LEU C  338  1                                  13    
HELIX  109 AM1 ASN C  342  ASN C  352  1                                  11    
HELIX  110 AM2 ASN C  352  ALA C  363  1                                  12    
HELIX  111 AM3 SER C  365  ALA C  379  1                                  15    
HELIX  112 AM4 GLY C  381  TYR C  389  1                                   9    
HELIX  113 AM5 ASP C  428  LYS C  433  1                                   6    
HELIX  114 AM6 PRO C  484  PHE C  491  5                                   8    
HELIX  115 AM7 ASN C  500  VAL C  506  1                                   7    
HELIX  116 AM8 VAL C  506  GLU C  512  1                                   7    
HELIX  117 AM9 GLY C  526  LEU C  539  1                                  14    
HELIX  118 AN1 SER C  540  TYR C  543  5                                   4    
HELIX  119 AN2 LEU C  563  ARG C  576  1                                  14    
HELIX  120 AN3 LEU C  578  GLY C  582  5                                   5    
HELIX  121 AN4 GLN C  598  THR C  602  5                                   5    
HELIX  122 AN5 THR C  608  ASN C  618  1                                  11    
HELIX  123 AN6 ASN C  621  GLU C  626  1                                   6    
HELIX  124 AN7 ILE C  636  ASP C  641  5                                   6    
HELIX  125 AN8 ARG C  643  PHE C  655  1                                  13    
HELIX  126 AN9 ASN C  676  LEU C  684  1                                   9    
HELIX  127 AO1 ASP C  695  ARG C  699  5                                   5    
HELIX  128 AO2 SER C  715  LYS C  717  5                                   3    
HELIX  129 AO3 LYS C  718  GLU C  736  1                                  19    
HELIX  130 AO4 LYS C  748  GLU C  763  1                                  16    
HELIX  131 AO5 SER C  777  ALA C  785  1                                   9    
HELIX  132 AO6 SER C  792  ILE C  797  1                                   6    
HELIX  133 AO7 GLU C  798  GLY C  800  5                                   3    
HELIX  134 AO8 THR C  809  ASP C  822  1                                  14    
HELIX  135 AO9 ALA C  832  TRP C  836  5                                   5    
HELIX  136 AP1 SER C  864  GLY C  873  1                                  10    
HELIX  137 AP2 ASN C  894  LEU C  902  1                                   9    
HELIX  138 AP3 PHE C  912  ALA C  926  1                                  15    
HELIX  139 AP4 CYS C  931  LEU C  939  1                                   9    
HELIX  140 AP5 THR C  942  SER C  951  1                                  10    
HELIX  141 AP6 SER C  951  LYS C  956  1                                   6    
HELIX  142 AP7 ASP C  959  GLY C  964  1                                   6    
HELIX  143 AP8 LEU C  966  GLN C  984  1                                  19    
HELIX  144 AP9 THR C  999  PHE C 1008  1                                  10    
HELIX  145 AQ1 ASN C 1011  LEU C 1022  1                                  12    
HELIX  146 AQ2 THR C 1027  MET C 1037  1                                  11    
HELIX  147 AQ3 SER C 1038  LYS C 1042  5                                   5    
HELIX  148 AQ4 ARG C 1047  GLU C 1049  5                                   3    
HELIX  149 AQ5 GLU C 1050  LYS C 1060  1                                  11    
HELIX  150 AQ6 ASP C 1071  PHE C 1084  1                                  14    
HELIX  151 AQ7 GLY C 1091  GLY C 1120  1                                  30    
HELIX  152 AQ8 TRP C 1121  LYS C 1138  1                                  18    
HELIX  153 AQ9 CYS C 1144  PHE C 1149  5                                   6    
HELIX  154 AR1 PRO C 1153  ALA C 1162  1                                  10    
HELIX  155 AR2 TRP C 1167  GLN C 1172  1                                   6    
HELIX  156 AR3 THR C 1175  ILE C 1183  1                                   9    
HELIX  157 AR4 SER C 1185  LYS C 1197  1                                  13    
HELIX  158 AR5 ASP C 1229  GLY C 1234  1                                   6    
HELIX  159 AR6 THR C 1260  VAL C 1264  5                                   5    
HELIX  160 AR7 LYS C 1277  ASN C 1283  1                                   7    
HELIX  161 AR8 SER C 1330  LEU C 1334  5                                   5    
HELIX  162 AR9 ASN C 1336  GLU C 1344  1                                   9    
HELIX  163 AS1 ASN C 1349  ASN C 1361  1                                  13    
HELIX  164 AS2 GLY C 1375  GLN C 1390  1                                  16    
HELIX  165 AS3 SER C 1401  ASN C 1413  1                                  13    
HELIX  166 AS4 ASP C 1431  LYS C 1441  1                                  11    
HELIX  167 AS5 THR C 1448  ARG C 1457  1                                  10    
HELIX  168 AS6 ARG C 1462  SER C 1467  1                                   6    
HELIX  169 AS7 ASP C 1475  SER C 1480  5                                   6    
HELIX  170 AS8 GLN C 1481  LEU C 1502  1                                  22    
HELIX  171 AS9 ASN C 1517  ALA C 1525  1                                   9    
HELIX  172 AT1 THR C 1528  SER C 1530  5                                   3    
HELIX  173 AT2 ASN C 1560  GLY C 1576  1                                  17    
HELIX  174 AT3 SER C 1587  LYS C 1603  1                                  17    
HELIX  175 AT4 VAL C 1618  LYS C 1623  5                                   6    
HELIX  176 AT5 ASP C 1626  HIS C 1628  5                                   3    
HELIX  177 AT6 LEU C 1629  HIS C 1635  1                                   7    
HELIX  178 AT7 ALA C 1645  TYR C 1658  1                                  14    
HELIX  179 AT8 ASP C 1669  PHE C 1673  5                                   5    
HELIX  180 AT9 THR C 1699  GLY C 1708  1                                  10    
HELIX  181 AU1 HIS C 1726  LEU C 1736  1                                  11    
HELIX  182 AU2 TYR C 1745  TYR C 1748  5                                   4    
HELIX  183 AU3 ILE C 1749  ASN C 1760  1                                  12    
HELIX  184 AU4 SER C 1765  THR C 1774  1                                  10    
HELIX  185 AU5 SER C 1776  HIS C 1783  1                                   8    
HELIX  186 AU6 SER C 1795  SER C 1817  1                                  23    
HELIX  187 AU7 LEU C 1847  GLY C 1857  1                                  11    
HELIX  188 AU8 SER C 1859  SER C 1868  1                                  10    
HELIX  189 AU9 THR C 1875  THR C 1885  1                                  11    
HELIX  190 AV1 ALA C 1886  GLU C 1890  5                                   5    
HELIX  191 AV2 ASP C 1898  SER C 1906  1                                   9    
HELIX  192 AV3 SER C 1921  SER C 1935  1                                  15    
HELIX  193 AV4 PRO C 1940  LYS C 1953  1                                  14    
HELIX  194 AV5 VAL C 1954  SER C 1966  1                                  13    
HELIX  195 AV6 ASN C 1972  GLY C 1986  1                                  15    
HELIX  196 AV7 ASN C 2001  ILE C 2011  1                                  11    
HELIX  197 AV8 THR C 2015  ALA C 2021  1                                   7    
HELIX  198 AV9 GLU C 2023  ASP C 2028  1                                   6    
HELIX  199 AW1 THR C 2034  ASN C 2046  1                                  13    
HELIX  200 AW2 ASN D 2150  ASN D 2159  1                                  10    
HELIX  201 AW3 THR D 2160  LYS D 2167  5                                   8    
HELIX  202 AW4 LYS D 2187  ILE D 2196  1                                  10    
HELIX  203 AW5 ALA D 2270  ALA D 2282  1                                  13    
HELIX  204 AW6 THR D 2308  ASN D 2318  1                                  11    
HELIX  205 AW7 GLU D 2330  THR D 2332  5                                   3    
HELIX  206 AW8 MET D 2362  PHE D 2366  5                                   5    
HELIX  207 AW9 ARG D 2388  LEU D 2393  1                                   6    
SHEET    1 AA1 8 PHE A 453  LYS A 457  0                                        
SHEET    2 AA1 8 TYR A 460  ILE A 465 -1  O  GLU A 462   N  ARG A 455           
SHEET    3 AA1 8 LEU A 703  ILE A 710 -1  O  GLY A 709   N  ASP A 461           
SHEET    4 AA1 8 GLY A 884  ASP A 891  1  O  GLY A 886   N  SER A 704           
SHEET    5 AA1 8 THR A 844  ILE A 847  1  N  VAL A 845   O  ILE A 887           
SHEET    6 AA1 8 ILE A 740  PHE A 743  1  N  PHE A 743   O  ILE A 846           
SHEET    7 AA1 8 VAL A 827  CYS A 830  1  O  LEU A 828   N  VAL A 742           
SHEET    8 AA1 8 ILE A 801  HIS A 804  1  N  GLY A 802   O  VAL A 829           
SHEET    1 AA2 7 VAL A 585  GLU A 587  0                                        
SHEET    2 AA2 7 VAL A 604  SER A 607  1  O  VAL A 606   N  ALA A 586           
SHEET    3 AA2 7 LYS A 556  ILE A 560  1  N  TYR A 559   O  SER A 607           
SHEET    4 AA2 7 VAL A 628  ASP A 634  1  O  ASP A 634   N  ILE A 560           
SHEET    5 AA2 7 ARG A 666  SER A 671  1  O  LEU A 670   N  ILE A 633           
SHEET    6 AA2 7 MET A 517  CYS A 520  1  N  ILE A 519   O  GLY A 669           
SHEET    7 AA2 7 LEU A 691  TYR A 693  1  O  PHE A 692   N  LEU A 518           
SHEET    1 AA3 2 ASP A 851  SER A 854  0                                        
SHEET    2 AA3 2 SER A 859  GLN A 862 -1  O  SER A 859   N  SER A 854           
SHEET    1 AA4 2 VAL A 987  ASP A 990  0                                        
SHEET    2 AA4 2 VAL A 995  ALA A 998 -1  O  GLU A 997   N  LEU A 988           
SHEET    1 AA5 3 MET A1202  THR A1212  0                                        
SHEET    2 AA5 3 VAL A1215  ALA A1224 -1  O  GLU A1221   N  THR A1205           
SHEET    3 AA5 3 PHE A1268  GLU A1275 -1  O  LEU A1270   N  ILE A1220           
SHEET    1 AA6 4 ILE A1251  ILE A1259  0                                        
SHEET    2 AA6 4 GLU A1237  GLU A1244 -1  N  LEU A1241   O  ASP A1255           
SHEET    3 AA6 4 PHE A1288  SER A1294 -1  O  ILE A1293   N  LEU A1240           
SHEET    4 AA6 4 PHE A1302  VAL A1306 -1  O  ILE A1304   N  LEU A1290           
SHEET    1 AA7 7 ILE A1424  ILE A1425  0                                        
SHEET    2 AA7 7 VAL A1444  ALA A1447  1  O  LEU A1446   N  ILE A1425           
SHEET    3 AA7 7 ALA A1395  ILE A1398  1  N  TYR A1397   O  LEU A1445           
SHEET    4 AA7 7 LEU A1470  TYR A1473  1  O  ILE A1472   N  ILE A1398           
SHEET    5 AA7 7 ARG A1507  SER A1512  1  O  VAL A1509   N  MET A1471           
SHEET    6 AA7 7 VAL A1366  GLY A1369  1  N  VAL A1368   O  SER A1512           
SHEET    7 AA7 7 ILE A1532  ASN A1534  1  O  TYR A1533   N  GLY A1369           
SHEET    1 AA8 6 LEU A1544  PHE A1551  0                                        
SHEET    2 AA8 6 GLY A1718  SER A1725  1  O  VAL A1720   N  ASN A1547           
SHEET    3 AA8 6 GLU A1679  LEU A1683  1  N  ILE A1682   O  LEU A1721           
SHEET    4 AA8 6 SER A1581  LEU A1585  1  N  SER A1582   O  ILE A1681           
SHEET    5 AA8 6 VAL A1663  SER A1667  1  O  ILE A1666   N  VAL A1583           
SHEET    6 AA8 6 GLY A1638  LEU A1640  1  N  GLY A1638   O  LEU A1665           
SHEET    1 AA9 2 ASN A1686  ASP A1689  0                                        
SHEET    2 AA9 2 LYS A1694  PRO A1697 -1  O  MET A1696   N  LEU A1687           
SHEET    1 AB1 2 ILE A1820  ASP A1823  0                                        
SHEET    2 AB1 2 ILE A1843  THR A1846 -1  O  ILE A1843   N  ASP A1823           
SHEET    1 AB2 3 VAL A2051  LEU A2057  0                                        
SHEET    2 AB2 3 LYS A2068  ARG A2077 -1  O  GLN A2074   N  THR A2054           
SHEET    3 AB2 3 THR A2123  ASP A2131 -1  O  GLN A2124   N  LEU A2075           
SHEET    1 AB3 4 GLU A2110  THR A2118  0                                        
SHEET    2 AB3 4 SER A2098  GLU A2105 -1  N  TRP A2099   O  VAL A2117           
SHEET    3 AB3 4 GLY A2136  CYS A2146 -1  O  TRP A2143   N  VAL A2102           
SHEET    4 AB3 4 LYS A2154  VAL A2162 -1  O  PHE A2158   N  LEU A2140           
SHEET    1 AB4 8 ILE B2169  VAL B2171  0                                        
SHEET    2 AB4 8 VAL B2300  LEU B2307  1  O  LEU B2302   N  TYR B2170           
SHEET    3 AB4 8 ILE B2289  PHE B2294 -1  N  ASP B2290   O  TYR B2305           
SHEET    4 AB4 8 GLU B2254  GLN B2262  1  N  TRP B2258   O  ILE B2291           
SHEET    5 AB4 8 ALA B2204  SER B2211 -1  N  GLY B2209   O  GLU B2254           
SHEET    6 AB4 8 VAL B2218  VAL B2225 -1  O  THR B2223   N  TYR B2208           
SHEET    7 AB4 8 VAL B2182  PRO B2186  1  N  VAL B2182   O  LYS B2219           
SHEET    8 AB4 8 LEU B2339  SER B2342  1  O  LEU B2340   N  TYR B2183           
SHEET    1 AB5 8 SER B2334  HIS B2336  0                                        
SHEET    2 AB5 8 VAL B2300  LEU B2307 -1  N  ASN B2306   O  THR B2335           
SHEET    3 AB5 8 ILE B2289  PHE B2294 -1  N  ASP B2290   O  TYR B2305           
SHEET    4 AB5 8 GLU B2254  GLN B2262  1  N  TRP B2258   O  ILE B2291           
SHEET    5 AB5 8 ALA B2204  SER B2211 -1  N  GLY B2209   O  GLU B2254           
SHEET    6 AB5 8 VAL B2218  VAL B2225 -1  O  THR B2223   N  TYR B2208           
SHEET    7 AB5 8 ASN B2348  PRO B2352  1  O  ASN B2348   N  VAL B2224           
SHEET    8 AB5 8 PHE B2374  GLY B2377 -1  O  LYS B2375   N  ILE B2351           
SHEET    1 AB6 2 GLN B2229  GLY B2231  0                                        
SHEET    2 AB6 2 VAL B2236  ILE B2238 -1  O  GLN B2237   N  LEU B2230           
SHEET    1 AB7 8 PHE C 453  LYS C 457  0                                        
SHEET    2 AB7 8 TYR C 460  ILE C 465 -1  O  GLU C 462   N  ARG C 455           
SHEET    3 AB7 8 LEU C 703  ILE C 710 -1  O  GLY C 709   N  ASP C 461           
SHEET    4 AB7 8 GLY C 884  ASP C 891  1  O  THR C 890   N  ILE C 710           
SHEET    5 AB7 8 THR C 844  ILE C 847  1  N  VAL C 845   O  ILE C 887           
SHEET    6 AB7 8 ILE C 740  PHE C 743  1  N  PHE C 743   O  ILE C 846           
SHEET    7 AB7 8 VAL C 827  CYS C 830  1  O  LEU C 828   N  VAL C 742           
SHEET    8 AB7 8 GLY C 802  HIS C 804  1  N  HIS C 804   O  VAL C 829           
SHEET    1 AB8 7 VAL C 585  GLU C 587  0                                        
SHEET    2 AB8 7 VAL C 604  SER C 607  1  O  VAL C 606   N  ALA C 586           
SHEET    3 AB8 7 LYS C 556  ILE C 560  1  N  ILE C 557   O  LEU C 605           
SHEET    4 AB8 7 VAL C 628  ASP C 634  1  O  ASP C 634   N  ILE C 560           
SHEET    5 AB8 7 ARG C 666  SER C 671  1  O  LEU C 670   N  ILE C 633           
SHEET    6 AB8 7 MET C 517  CYS C 520  1  N  ILE C 519   O  SER C 671           
SHEET    7 AB8 7 PHE C 692  TYR C 693  1  O  PHE C 692   N  CYS C 520           
SHEET    1 AB9 2 ASP C 851  SER C 854  0                                        
SHEET    2 AB9 2 SER C 859  GLN C 862 -1  O  GLU C 861   N  VAL C 852           
SHEET    1 AC1 2 VAL C 987  ASP C 990  0                                        
SHEET    2 AC1 2 VAL C 995  ALA C 998 -1  O  VAL C 995   N  ASP C 990           
SHEET    1 AC2 3 MET C1202  THR C1212  0                                        
SHEET    2 AC2 3 VAL C1215  ALA C1224 -1  O  ASN C1219   N  ASN C1207           
SHEET    3 AC2 3 PHE C1268  GLU C1275 -1  O  LEU C1270   N  ILE C1220           
SHEET    1 AC3 4 ILE C1251  ILE C1259  0                                        
SHEET    2 AC3 4 GLU C1237  GLU C1244 -1  N  LEU C1241   O  ASP C1255           
SHEET    3 AC3 4 ASN C1287  SER C1294 -1  O  ILE C1293   N  LEU C1240           
SHEET    4 AC3 4 PHE C1302  SER C1307 -1  O  ILE C1304   N  LEU C1290           
SHEET    1 AC4 7 ILE C1424  ILE C1425  0                                        
SHEET    2 AC4 7 VAL C1444  ALA C1447  1  O  VAL C1444   N  ILE C1425           
SHEET    3 AC4 7 ALA C1395  ILE C1398  1  N  TYR C1397   O  LEU C1445           
SHEET    4 AC4 7 LEU C1470  TYR C1473  1  O  ILE C1472   N  VAL C1396           
SHEET    5 AC4 7 ARG C1507  SER C1512  1  O  VAL C1509   N  TYR C1473           
SHEET    6 AC4 7 VAL C1366  GLY C1369  1  N  VAL C1368   O  SER C1512           
SHEET    7 AC4 7 ILE C1532  ASN C1534  1  O  TYR C1533   N  GLY C1369           
SHEET    1 AC5 6 LEU C1544  PHE C1551  0                                        
SHEET    2 AC5 6 GLY C1718  SER C1725  1  O  GLY C1718   N  GLU C1545           
SHEET    3 AC5 6 GLU C1679  LEU C1683  1  N  ILE C1682   O  LEU C1721           
SHEET    4 AC5 6 SER C1581  LEU C1585  1  N  SER C1582   O  ILE C1681           
SHEET    5 AC5 6 VAL C1663  SER C1667  1  O  ILE C1666   N  VAL C1583           
SHEET    6 AC5 6 GLY C1638  LEU C1640  1  N  GLY C1638   O  VAL C1663           
SHEET    1 AC6 2 ASN C1686  ASP C1689  0                                        
SHEET    2 AC6 2 LYS C1694  PRO C1697 -1  O  LYS C1694   N  ASP C1689           
SHEET    1 AC7 2 ILE C1820  ASP C1823  0                                        
SHEET    2 AC7 2 ILE C1843  THR C1846 -1  O  ILE C1843   N  ASP C1823           
SHEET    1 AC8 3 VAL C2051  LEU C2057  0                                        
SHEET    2 AC8 3 LYS C2068  ARG C2077 -1  O  GLN C2074   N  THR C2054           
SHEET    3 AC8 3 THR C2123  ASP C2131 -1  O  TYR C2126   N  ILE C2073           
SHEET    1 AC9 4 GLU C2110  THR C2118  0                                        
SHEET    2 AC9 4 SER C2098  GLU C2105 -1  N  TRP C2099   O  VAL C2117           
SHEET    3 AC9 4 GLY C2136  CYS C2146 -1  O  VAL C2145   N  TRP C2100           
SHEET    4 AC9 4 LYS C2154  VAL C2162 -1  O  LEU C2156   N  ILE C2142           
SHEET    1 AD1 8 ILE D2169  VAL D2171  0                                        
SHEET    2 AD1 8 VAL D2300  LEU D2307  1  O  LEU D2302   N  TYR D2170           
SHEET    3 AD1 8 ILE D2289  PHE D2294 -1  N  ASP D2290   O  TYR D2305           
SHEET    4 AD1 8 GLU D2254  GLN D2262  1  N  HIS D2260   O  ILE D2293           
SHEET    5 AD1 8 ALA D2204  SER D2211 -1  N  GLY D2209   O  GLU D2254           
SHEET    6 AD1 8 VAL D2218  VAL D2225 -1  O  THR D2223   N  TYR D2208           
SHEET    7 AD1 8 VAL D2182  PRO D2186  1  N  VAL D2182   O  LYS D2219           
SHEET    8 AD1 8 LEU D2339  SER D2342  1  O  LEU D2340   N  TYR D2183           
SHEET    1 AD2 8 SER D2334  HIS D2336  0                                        
SHEET    2 AD2 8 VAL D2300  LEU D2307 -1  N  ASN D2306   O  THR D2335           
SHEET    3 AD2 8 ILE D2289  PHE D2294 -1  N  ASP D2290   O  TYR D2305           
SHEET    4 AD2 8 GLU D2254  GLN D2262  1  N  HIS D2260   O  ILE D2293           
SHEET    5 AD2 8 ALA D2204  SER D2211 -1  N  GLY D2209   O  GLU D2254           
SHEET    6 AD2 8 VAL D2218  VAL D2225 -1  O  THR D2223   N  TYR D2208           
SHEET    7 AD2 8 ASN D2348  PRO D2352  1  O  ILE D2350   N  VAL D2224           
SHEET    8 AD2 8 PHE D2374  TYR D2376 -1  O  LYS D2375   N  ILE D2351           
SHEET    1 AD3 2 GLN D2229  GLY D2231  0                                        
SHEET    2 AD3 2 VAL D2236  ILE D2238 -1  O  GLN D2237   N  LEU D2230           
CRYST1  185.970  196.870  191.030  90.00  90.00  90.00 P 21 21 2     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      0.005377  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005079  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005235        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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