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Database: PDB
Entry: 5Z2C
LinkDB: 5Z2C
Original site: 5Z2C 
HEADER    IMMUNE SYSTEM                           02-JAN-18   5Z2C              
TITLE     CRYSTAL STRUCTURE OF ALPK-1 N-TERMINAL DOMAIN IN COMPLEX WITH ADP-    
TITLE    2 HEPTOSE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-PROTEIN KINASE 1;                                    
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I;                                    
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN;                                         
COMPND   5 SYNONYM: CHROMOSOME 4 KINASE,LYMPHOCYTE ALPHA-PROTEIN KINASE;        
COMPND   6 EC: 2.7.11.-;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALPK1, KIAA1527, LAK;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-SUMO                                  
KEYWDS    PATTERN RECOGNITION RECEPTOR, KINASE, IMMUNE SYSTEM                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.DING,Y.SHE,F.SHAO                                                   
REVDAT   3   19-SEP-18 5Z2C    1       JRNL                                     
REVDAT   2   29-AUG-18 5Z2C    1       JRNL                                     
REVDAT   1   22-AUG-18 5Z2C    0                                                
JRNL        AUTH   P.ZHOU,Y.SHE,N.DONG,P.LI,H.HE,A.BORIO,Q.WU,S.LU,X.DING,      
JRNL        AUTH 2 Y.CAO,Y.XU,W.GAO,M.DONG,J.DING,D.C.WANG,A.ZAMYATINA,F.SHAO   
JRNL        TITL   ALPHA-KINASE 1 IS A CYTOSOLIC INNATE IMMUNE RECEPTOR FOR     
JRNL        TITL 2 BACTERIAL ADP-HEPTOSE.                                       
JRNL        REF    NATURE                        V. 561   122 2018              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   30111836                                                     
JRNL        DOI    10.1038/S41586-018-0433-3                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.89                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 173963                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.150                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 48.8966 -  6.2481    0.96    12217   142  0.1661 0.1658        
REMARK   3     2  6.2481 -  4.9608    0.99    12467   146  0.2369 0.2402        
REMARK   3     3  4.9608 -  4.3342    0.95    12030   139  0.2039 0.2116        
REMARK   3     4  4.3342 -  3.9381    0.98    12338   144  0.2181 0.2638        
REMARK   3     5  3.9381 -  3.6559    0.99    12437   145  0.2354 0.3116        
REMARK   3     6  3.6559 -  3.4404    0.99    12408   143  0.2556 0.2589        
REMARK   3     7  3.4404 -  3.2682    0.99    12373   144  0.2773 0.2915        
REMARK   3     8  3.2682 -  3.1259    0.95    12020   140  0.2951 0.3482        
REMARK   3     9  3.1259 -  3.0056    0.98    12313   143  0.3077 0.3256        
REMARK   3    10  3.0056 -  2.9019    0.98    12273   143  0.3150 0.3576        
REMARK   3    11  2.9019 -  2.8112    0.98    12394   144  0.3101 0.3242        
REMARK   3    12  2.8112 -  2.7308    0.98    12217   143  0.3095 0.3286        
REMARK   3    13  2.7308 -  2.6590    0.98    12349   143  0.3183 0.3104        
REMARK   3    14  2.6590 -  2.5941    0.96    12127   141  0.3302 0.3625        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.005          31253                                  
REMARK   3   ANGLE     :  0.599          42341                                  
REMARK   3   CHIRALITY :  0.040           4967                                  
REMARK   3   PLANARITY :  0.004           5329                                  
REMARK   3   DIHEDRAL  : 15.192          18969                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5Z2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300006355.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97853                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 174023                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.990                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM FORMATE, 0.1M SODIUM         
REMARK 280  ACETATE, PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       84.63000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      107.19400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.63000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      107.19400            
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, 3, 4, 5, 6, 7, 8, 9                               
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
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: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     TYR C    68                                                      
REMARK 465     LYS C    69                                                      
REMARK 465     GLN C    70                                                      
REMARK 465     ALA C    71                                                      
REMARK 465     VAL C    72                                                      
REMARK 465     GLY C    73                                                      
REMARK 465     PRO C    74                                                      
REMARK 465     GLU C    75                                                      
REMARK 465     ASP C    76                                                      
REMARK 465     LYS C    77                                                      
REMARK 465     THR C    78                                                      
REMARK 465     ASN C    79                                                      
REMARK 465     ARG C   340                                                      
REMARK 465     ASP C   341                                                      
REMARK 465     ASP C   342                                                      
REMARK 465     GLU C   343                                                      
REMARK 465     VAL C   427                                                      
REMARK 465     LEU C   446                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D    70                                                      
REMARK 465     ALA D    71                                                      
REMARK 465     VAL D    72                                                      
REMARK 465     GLY D    73                                                      
REMARK 465     PRO D    74                                                      
REMARK 465     GLU D    75                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     LYS D    77                                                      
REMARK 465     THR D    78                                                      
REMARK 465     ASN D    79                                                      
REMARK 465     ASP D   341                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LYS E    65                                                      
REMARK 465     LYS E    69                                                      
REMARK 465     GLN E    70                                                      
REMARK 465     ALA E    71                                                      
REMARK 465     VAL E    72                                                      
REMARK 465     GLY E    73                                                      
REMARK 465     PRO E    74                                                      
REMARK 465     GLU E    75                                                      
REMARK 465     ASP E    76                                                      
REMARK 465     LYS E    77                                                      
REMARK 465     THR E    78                                                      
REMARK 465     ASN E    79                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F    69                                                      
REMARK 465     GLN F    70                                                      
REMARK 465     ALA F    71                                                      
REMARK 465     VAL F    72                                                      
REMARK 465     GLY F    73                                                      
REMARK 465     PRO F    74                                                      
REMARK 465     GLU F    75                                                      
REMARK 465     ASP F    76                                                      
REMARK 465     LYS F    77                                                      
REMARK 465     THR F    78                                                      
REMARK 465     ASN F    79                                                      
REMARK 465     LEU F   446                                                      
REMARK 465     MET G     1                                                      
REMARK 465     LYS G    65                                                      
REMARK 465     TRP G    66                                                      
REMARK 465     GLN G    67                                                      
REMARK 465     TYR G    68                                                      
REMARK 465     LYS G    69                                                      
REMARK 465     GLN G    70                                                      
REMARK 465     ALA G    71                                                      
REMARK 465     VAL G    72                                                      
REMARK 465     GLY G    73                                                      
REMARK 465     PRO G    74                                                      
REMARK 465     GLU G    75                                                      
REMARK 465     ASP G    76                                                      
REMARK 465     LYS G    77                                                      
REMARK 465     THR G    78                                                      
REMARK 465     ASN G    79                                                      
REMARK 465     ASP G   341                                                      
REMARK 465     LEU G   446                                                      
REMARK 465     MET H     1                                                      
REMARK 465     LYS H    65                                                      
REMARK 465     TRP H    66                                                      
REMARK 465     GLN H    67                                                      
REMARK 465     TYR H    68                                                      
REMARK 465     LYS H    69                                                      
REMARK 465     GLN H    70                                                      
REMARK 465     ALA H    71                                                      
REMARK 465     VAL H    72                                                      
REMARK 465     GLY H    73                                                      
REMARK 465     PRO H    74                                                      
REMARK 465     GLU H    75                                                      
REMARK 465     ASP H    76                                                      
REMARK 465     LYS H    77                                                      
REMARK 465     THR H    78                                                      
REMARK 465     ASN H    79                                                      
REMARK 465     ARG H   340                                                      
REMARK 465     ASP H   341                                                      
REMARK 465     ASP H   342                                                      
REMARK 465     GLU H   343                                                      
REMARK 465     VAL H   427                                                      
REMARK 465     ASP H   428                                                      
REMARK 465     LEU H   446                                                      
REMARK 465     MET I     1                                                      
REMARK 465     TYR I    68                                                      
REMARK 465     LYS I    69                                                      
REMARK 465     GLN I    70                                                      
REMARK 465     ALA I    71                                                      
REMARK 465     VAL I    72                                                      
REMARK 465     GLY I    73                                                      
REMARK 465     PRO I    74                                                      
REMARK 465     GLU I    75                                                      
REMARK 465     ASP I    76                                                      
REMARK 465     LYS I    77                                                      
REMARK 465     THR I    78                                                      
REMARK 465     ASN I    79                                                      
REMARK 465     GLU I   319                                                      
REMARK 465     LEU I   320                                                      
REMARK 465     LYS I   321                                                      
REMARK 465     ASN I   322                                                      
REMARK 465     LEU I   323                                                      
REMARK 465     ARG I   340                                                      
REMARK 465     ASP I   341                                                      
REMARK 465     ASP I   342                                                      
REMARK 465     GLU I   343                                                      
REMARK 465     GLN I   420                                                      
REMARK 465     VAL I   421                                                      
REMARK 465     GLN I   422                                                      
REMARK 465     SER I   423                                                      
REMARK 465     PHE I   424                                                      
REMARK 465     SER I   425                                                      
REMARK 465     ASN I   426                                                      
REMARK 465     VAL I   427                                                      
REMARK 465     CYS I   439                                                      
REMARK 465     ARG I   440                                                      
REMARK 465     LEU I   441                                                      
REMARK 465     ASP I   442                                                      
REMARK 465     LYS I   443                                                      
REMARK 465     LEU I   444                                                      
REMARK 465     ILE I   445                                                      
REMARK 465     LEU I   446                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY H   176     OH   TYR H   183              1.31            
REMARK 500   CE1  PHE H   424     CG   PRO H   434              1.94            
REMARK 500   ND2  ASN H   426     CG   GLU H   435              1.98            
REMARK 500   O    GLU G   438     NZ   LYS G   443              2.02            
REMARK 500   CE1  PHE H   424     N    PRO H   434              2.03            
REMARK 500   CE1  PHE H   424     CA   PRO H   434              2.03            
REMARK 500   ND2  ASN H   426     N    GLU H   435              2.06            
REMARK 500   OG   SER B   266     O    LYS B   443              2.11            
REMARK 500   ND1  HIS I   365     CD2  LEU I   419              2.11            
REMARK 500   OH   TYR H   254     OG   SER H   277              2.14            
REMARK 500   OG   SER I   289     OG1  THR I   292              2.16            
REMARK 500   O    LEU I   337     N    LYS I   339              2.16            
REMARK 500   OE2  GLU D   438     NZ   LYS D   443              2.17            
REMARK 500   O    PHE I   332     CD2  LEU I   336              2.17            
REMARK 500   C    GLY H   176     OH   TYR H   183              2.18            
REMARK 500   O    ASP C   428     N    ARG C   430              2.19            
REMARK 500   ND1  HIS I   324     OE1  GLU I   327              2.19            
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   O    ASN G   259     NE2  GLN I   262    11511     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    ASP A  27       74.13   -153.49                                   
REMARK 500    LYS A  77       42.88    -94.23                                   
REMARK 500    ASN A 264       57.65    -93.59                                   
REMARK 500    ASP A 341     -132.25     58.81                                   
REMARK 500    ASP B  27       75.40   -154.77                                   
REMARK 500    LYS B  77       37.22    -90.80                                   
REMARK 500    ASN B 264       57.72    -93.15                                   
REMARK 500    ASP B 341     -129.49     60.08                                   
REMARK 500    GLU B 371       62.49   -100.38                                   
REMARK 500    LEU B 441      -38.20   -132.67                                   
REMARK 500    ASP C  27       74.14   -154.26                                   
REMARK 500    ASN C 264       59.28    -95.24                                   
REMARK 500    ASP C 429      -21.86    -33.86                                   
REMARK 500    ASP D  27       75.31   -155.13                                   
REMARK 500    TYR D  68     -168.39   -127.91                                   
REMARK 500    ASN D 264       58.70    -96.04                                   
REMARK 500    ASN D 426      138.69   -171.68                                   
REMARK 500    ASP E  27       75.77   -154.53                                   
REMARK 500    ASN E 264       57.27    -95.26                                   
REMARK 500    ASP E 341     -135.26     40.23                                   
REMARK 500    ASP E 342       47.34   -143.94                                   
REMARK 500    GLN E 420       74.90    -55.91                                   
REMARK 500    ASP F  27       75.52   -155.53                                   
REMARK 500    ASP F 341     -145.67     60.33                                   
REMARK 500    GLU F 371       62.84   -114.84                                   
REMARK 500    ASP G  27       75.42   -154.71                                   
REMARK 500    ASN G 264       59.50    -96.25                                   
REMARK 500    GLU G 371       80.94   -164.02                                   
REMARK 500    ASP H  27       73.09   -156.06                                   
REMARK 500    ASN H 264       58.23    -98.48                                   
REMARK 500    GLU H 371       67.01   -117.86                                   
REMARK 500    GLN H 420      -13.07     70.54                                   
REMARK 500    LYS H 443       13.62    -69.77                                   
REMARK 500    ASP I  27       75.09   -154.67                                   
REMARK 500    ASN I 264       58.95    -96.28                                   
REMARK 500    THR I 338      -15.10    -34.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU G 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU H 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AYU I 501                 
DBREF  5Z2C A    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C B    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C C    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C D    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C E    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C F    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C G    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C H    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
DBREF  5Z2C I    1   446  UNP    Q96QP1   ALPK1_HUMAN      1    446             
SEQRES   1 A  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 A  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 A  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 A  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 A  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 A  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 A  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 A  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 A  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 A  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 A  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 A  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 A  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 A  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 A  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 A  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 A  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 A  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 A  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 A  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 A  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 A  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 A  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 A  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 A  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 A  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 A  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 A  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 A  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 A  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 A  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 A  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 A  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 A  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 A  446  LYS LEU ILE LEU                                              
SEQRES   1 B  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 B  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 B  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 B  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 B  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 B  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 B  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 B  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 B  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 B  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 B  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 B  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 B  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 B  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 B  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 B  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 B  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 B  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 B  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 B  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 B  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 B  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 B  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 B  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 B  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 B  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 B  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 B  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 B  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 B  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 B  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 B  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 B  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 B  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 B  446  LYS LEU ILE LEU                                              
SEQRES   1 C  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 C  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 C  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 C  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 C  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 C  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 C  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 C  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 C  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 C  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 C  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 C  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 C  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 C  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 C  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 C  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 C  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 C  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 C  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 C  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 C  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 C  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 C  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 C  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 C  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 C  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 C  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 C  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 C  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 C  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 C  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 C  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 C  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 C  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 C  446  LYS LEU ILE LEU                                              
SEQRES   1 D  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 D  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 D  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 D  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 D  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 D  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 D  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 D  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 D  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 D  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 D  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 D  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 D  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 D  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 D  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 D  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 D  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 D  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 D  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 D  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 D  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 D  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 D  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 D  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 D  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 D  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 D  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 D  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 D  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 D  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 D  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 D  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 D  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 D  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 D  446  LYS LEU ILE LEU                                              
SEQRES   1 E  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 E  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 E  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 E  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 E  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 E  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 E  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 E  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 E  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 E  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 E  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 E  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 E  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 E  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 E  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 E  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 E  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 E  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 E  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 E  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 E  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 E  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 E  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 E  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 E  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 E  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 E  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 E  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 E  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 E  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 E  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 E  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 E  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 E  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 E  446  LYS LEU ILE LEU                                              
SEQRES   1 F  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 F  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 F  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 F  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 F  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 F  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 F  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 F  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 F  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 F  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 F  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 F  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 F  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 F  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 F  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 F  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 F  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 F  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 F  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 F  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 F  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 F  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 F  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 F  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 F  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 F  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 F  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 F  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 F  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 F  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 F  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 F  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 F  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 F  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 F  446  LYS LEU ILE LEU                                              
SEQRES   1 G  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 G  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 G  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 G  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 G  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 G  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 G  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 G  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 G  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 G  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 G  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 G  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 G  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 G  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 G  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 G  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 G  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 G  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 G  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 G  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 G  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 G  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 G  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 G  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 G  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 G  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 G  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 G  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 G  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 G  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 G  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 G  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 G  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 G  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 G  446  LYS LEU ILE LEU                                              
SEQRES   1 H  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 H  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 H  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 H  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 H  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 H  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 H  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 H  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 H  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 H  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 H  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 H  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 H  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 H  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 H  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 H  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 H  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 H  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 H  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 H  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 H  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 H  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 H  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 H  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 H  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 H  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 H  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 H  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 H  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 H  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 H  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 H  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 H  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 H  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 H  446  LYS LEU ILE LEU                                              
SEQRES   1 I  446  MET ASN ASN GLN LYS VAL VAL ALA VAL LEU LEU GLN GLU          
SEQRES   2 I  446  CYS LYS GLN VAL LEU ASP GLN LEU LEU LEU GLU ALA PRO          
SEQRES   3 I  446  ASP VAL SER GLU GLU ASP LYS SER GLU ASP GLN ARG CYS          
SEQRES   4 I  446  ARG ALA LEU LEU PRO SER GLU LEU ARG THR LEU ILE GLN          
SEQRES   5 I  446  GLU ALA LYS GLU MET LYS TRP PRO PHE VAL PRO GLU LYS          
SEQRES   6 I  446  TRP GLN TYR LYS GLN ALA VAL GLY PRO GLU ASP LYS THR          
SEQRES   7 I  446  ASN LEU LYS ASP VAL ILE GLY ALA GLY LEU GLN GLN LEU          
SEQRES   8 I  446  LEU ALA SER LEU ARG ALA SER ILE LEU ALA ARG ASP CYS          
SEQRES   9 I  446  ALA ALA ALA ALA ALA ILE VAL PHE LEU VAL ASP ARG PHE          
SEQRES  10 I  446  LEU TYR GLY LEU ASP VAL SER GLY LYS LEU LEU GLN VAL          
SEQRES  11 I  446  ALA LYS GLY LEU HIS LYS LEU GLN PRO ALA THR PRO ILE          
SEQRES  12 I  446  ALA PRO GLN VAL VAL ILE ARG GLN ALA ARG ILE SER VAL          
SEQRES  13 I  446  ASN SER GLY LYS LEU LEU LYS ALA GLU TYR ILE LEU SER          
SEQRES  14 I  446  SER LEU ILE SER ASN ASN GLY ALA THR GLY THR TRP LEU          
SEQRES  15 I  446  TYR ARG ASN GLU SER ASP LYS VAL LEU VAL GLN SER VAL          
SEQRES  16 I  446  CYS ILE GLN ILE ARG GLY GLN ILE LEU GLN LYS LEU GLY          
SEQRES  17 I  446  MET TRP TYR GLU ALA ALA GLU LEU ILE TRP ALA SER ILE          
SEQRES  18 I  446  VAL GLY TYR LEU ALA LEU PRO GLN PRO ASP LYS LYS GLY          
SEQRES  19 I  446  LEU SER THR SER LEU GLY ILE LEU ALA ASP ILE PHE VAL          
SEQRES  20 I  446  SER MET SER LYS ASN ASP TYR GLU LYS PHE LYS ASN ASN          
SEQRES  21 I  446  PRO GLN ILE ASN LEU SER LEU LEU LYS GLU PHE ASP HIS          
SEQRES  22 I  446  HIS LEU LEU SER ALA ALA GLU ALA CYS LYS LEU ALA ALA          
SEQRES  23 I  446  ALA PHE SER ALA TYR THR PRO LEU PHE VAL LEU THR ALA          
SEQRES  24 I  446  VAL ASN ILE ARG GLY THR CYS LEU LEU SER TYR SER SER          
SEQRES  25 I  446  SER ASN ASP CYS PRO PRO GLU LEU LYS ASN LEU HIS LEU          
SEQRES  26 I  446  CYS GLU ALA LYS GLU ALA PHE GLU ILE GLY LEU LEU THR          
SEQRES  27 I  446  LYS ARG ASP ASP GLU PRO VAL THR GLY LYS GLN GLU LEU          
SEQRES  28 I  446  HIS SER PHE VAL LYS ALA ALA PHE GLY LEU THR THR VAL          
SEQRES  29 I  446  HIS ARG ARG LEU HIS GLY GLU THR GLY THR VAL HIS ALA          
SEQRES  30 I  446  ALA SER GLN LEU CYS LYS GLU ALA MET GLY LYS LEU TYR          
SEQRES  31 I  446  ASN PHE SER THR SER SER ARG SER GLN ASP ARG GLU ALA          
SEQRES  32 I  446  LEU SER GLN GLU VAL MET SER VAL ILE ALA GLN VAL LYS          
SEQRES  33 I  446  GLU HIS LEU GLN VAL GLN SER PHE SER ASN VAL ASP ASP          
SEQRES  34 I  446  ARG SER TYR VAL PRO GLU SER PHE GLU CYS ARG LEU ASP          
SEQRES  35 I  446  LYS LEU ILE LEU                                              
HET    AYU  A 501      40                                                       
HET    AYU  B 501      40                                                       
HET    AYU  C 501      40                                                       
HET    AYU  D 501      40                                                       
HET    AYU  E 501      40                                                       
HET    AYU  F 501      40                                                       
HET    AYU  G 501      40                                                       
HET    AYU  H 501      40                                                       
HET    AYU  I 501      40                                                       
HETNAM     AYU [[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-                       
HETNAM   2 AYU  BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]           
HETNAM   3 AYU  [(2S,3S,4S,5S,6R)-6-[(1S)-1,2-BIS(OXIDANYL)ETHYL]-3,4,          
HETNAM   4 AYU  5-TRIS(OXIDANYL)OXAN-2-YL] HYDROGEN PHOSPHATE                   
FORMUL  10  AYU    9(C17 H27 N5 O16 P2)                                         
HELIX    1 AA1 ASN A    3  GLU A   24  1                                  22    
HELIX    2 AA2 SER A   29  LEU A   42  1                                  14    
HELIX    3 AA3 PRO A   44  GLU A   56  1                                  13    
HELIX    4 AA4 GLY A   73  LYS A   77  5                                   5    
HELIX    5 AA5 ASN A   79  GLY A   87  1                                   9    
HELIX    6 AA6 GLY A   87  ALA A  101  1                                  15    
HELIX    7 AA7 ASP A  103  LEU A  121  1                                  19    
HELIX    8 AA8 VAL A  123  GLN A  138  1                                  16    
HELIX    9 AA9 ALA A  144  SER A  158  1                                  15    
HELIX   10 AB1 LYS A  160  ASN A  174  1                                  15    
HELIX   11 AB2 GLU A  186  LEU A  207  1                                  22    
HELIX   12 AB3 MET A  209  ALA A  226  1                                  18    
HELIX   13 AB4 ASP A  231  MET A  249  1                                  19    
HELIX   14 AB5 SER A  250  ASN A  259  1                                  10    
HELIX   15 AB6 LEU A  265  PHE A  271  1                                   7    
HELIX   16 AB7 HIS A  273  SER A  289  1                                  17    
HELIX   17 AB8 THR A  292  SER A  312  1                                  21    
HELIX   18 AB9 PRO A  317  THR A  338  1                                  22    
HELIX   19 AC1 GLY A  347  GLY A  370  1                                  24    
HELIX   20 AC2 THR A  372  SER A  395  1                                  24    
HELIX   21 AC3 ARG A  397  LEU A  419  1                                  23    
HELIX   22 AC4 LEU A  441  ILE A  445  5                                   5    
HELIX   23 AC5 ASN B    3  GLU B   24  1                                  22    
HELIX   24 AC6 SER B   29  LEU B   42  1                                  14    
HELIX   25 AC7 PRO B   44  GLU B   56  1                                  13    
HELIX   26 AC8 ASN B   79  GLY B   87  1                                   9    
HELIX   27 AC9 GLY B   87  ALA B  101  1                                  15    
HELIX   28 AD1 ASP B  103  LEU B  121  1                                  19    
HELIX   29 AD2 VAL B  123  GLN B  138  1                                  16    
HELIX   30 AD3 ALA B  144  GLY B  159  1                                  16    
HELIX   31 AD4 LYS B  160  ASN B  174  1                                  15    
HELIX   32 AD5 GLU B  186  LEU B  207  1                                  22    
HELIX   33 AD6 MET B  209  ALA B  226  1                                  18    
HELIX   34 AD7 ASP B  231  MET B  249  1                                  19    
HELIX   35 AD8 SER B  250  ASN B  259  1                                  10    
HELIX   36 AD9 LEU B  265  PHE B  271  1                                   7    
HELIX   37 AE1 HIS B  273  SER B  289  1                                  17    
HELIX   38 AE2 THR B  292  SER B  312  1                                  21    
HELIX   39 AE3 PRO B  317  THR B  338  1                                  22    
HELIX   40 AE4 GLY B  347  HIS B  369  1                                  23    
HELIX   41 AE5 THR B  372  SER B  395  1                                  24    
HELIX   42 AE6 ARG B  397  LEU B  419  1                                  23    
HELIX   43 AE7 ASN C    3  GLU C   24  1                                  22    
HELIX   44 AE8 SER C   29  LEU C   42  1                                  14    
HELIX   45 AE9 PRO C   44  GLU C   56  1                                  13    
HELIX   46 AF1 LYS C   81  GLY C   87  1                                   7    
HELIX   47 AF2 GLY C   87  ALA C  101  1                                  15    
HELIX   48 AF3 ASP C  103  LEU C  121  1                                  19    
HELIX   49 AF4 VAL C  123  GLN C  138  1                                  16    
HELIX   50 AF5 ALA C  144  SER C  158  1                                  15    
HELIX   51 AF6 LYS C  160  ASN C  174  1                                  15    
HELIX   52 AF7 ASN C  185  LEU C  207  1                                  23    
HELIX   53 AF8 MET C  209  ALA C  226  1                                  18    
HELIX   54 AF9 ASP C  231  MET C  249  1                                  19    
HELIX   55 AG1 SER C  250  ASN C  259  1                                  10    
HELIX   56 AG2 LEU C  265  PHE C  271  1                                   7    
HELIX   57 AG3 HIS C  273  SER C  289  1                                  17    
HELIX   58 AG4 THR C  292  SER C  312  1                                  21    
HELIX   59 AG5 LEU C  320  THR C  338  1                                  19    
HELIX   60 AG6 GLY C  347  HIS C  369  1                                  23    
HELIX   61 AG7 THR C  372  SER C  395  1                                  24    
HELIX   62 AG8 ARG C  397  LEU C  419  1                                  23    
HELIX   63 AG9 ASN D    3  GLU D   24  1                                  22    
HELIX   64 AH1 SER D   29  LEU D   42  1                                  14    
HELIX   65 AH2 PRO D   44  GLU D   56  1                                  13    
HELIX   66 AH3 LYS D   81  GLY D   87  1                                   7    
HELIX   67 AH4 GLY D   87  ALA D  101  1                                  15    
HELIX   68 AH5 ASP D  103  LEU D  121  1                                  19    
HELIX   69 AH6 VAL D  123  GLN D  138  1                                  16    
HELIX   70 AH7 ALA D  144  SER D  158  1                                  15    
HELIX   71 AH8 LYS D  160  ASN D  174  1                                  15    
HELIX   72 AH9 ASN D  185  LEU D  207  1                                  23    
HELIX   73 AI1 MET D  209  ALA D  226  1                                  18    
HELIX   74 AI2 ASP D  231  MET D  249  1                                  19    
HELIX   75 AI3 SER D  250  ASN D  259  1                                  10    
HELIX   76 AI4 LEU D  265  GLU D  270  1                                   6    
HELIX   77 AI5 HIS D  273  SER D  289  1                                  17    
HELIX   78 AI6 THR D  292  SER D  312  1                                  21    
HELIX   79 AI7 PRO D  317  GLU D  319  5                                   3    
HELIX   80 AI8 LEU D  320  THR D  338  1                                  19    
HELIX   81 AI9 GLY D  347  GLY D  370  1                                  24    
HELIX   82 AJ1 THR D  372  SER D  395  1                                  24    
HELIX   83 AJ2 ARG D  397  LEU D  419  1                                  23    
HELIX   84 AJ3 PRO D  434  GLU D  438  5                                   5    
HELIX   85 AJ4 ARG D  440  LEU D  444  5                                   5    
HELIX   86 AJ5 ASN E    3  GLU E   24  1                                  22    
HELIX   87 AJ6 SER E   29  LEU E   42  1                                  14    
HELIX   88 AJ7 PRO E   44  GLU E   56  1                                  13    
HELIX   89 AJ8 LYS E   81  GLY E   87  1                                   7    
HELIX   90 AJ9 GLY E   87  ALA E  101  1                                  15    
HELIX   91 AK1 ASP E  103  LEU E  121  1                                  19    
HELIX   92 AK2 VAL E  123  GLN E  138  1                                  16    
HELIX   93 AK3 ALA E  144  SER E  158  1                                  15    
HELIX   94 AK4 LYS E  160  ASN E  174  1                                  15    
HELIX   95 AK5 GLU E  186  LEU E  207  1                                  22    
HELIX   96 AK6 MET E  209  ALA E  226  1                                  18    
HELIX   97 AK7 ASP E  231  MET E  249  1                                  19    
HELIX   98 AK8 SER E  250  ASN E  259  1                                  10    
HELIX   99 AK9 LEU E  265  GLU E  270  1                                   6    
HELIX  100 AL1 HIS E  273  SER E  289  1                                  17    
HELIX  101 AL2 THR E  292  SER E  312  1                                  21    
HELIX  102 AL3 LEU E  320  THR E  338  1                                  19    
HELIX  103 AL4 GLY E  347  HIS E  369  1                                  23    
HELIX  104 AL5 THR E  372  SER E  395  1                                  24    
HELIX  105 AL6 ARG E  397  LEU E  419  1                                  23    
HELIX  106 AL7 ASN F    3  GLU F   24  1                                  22    
HELIX  107 AL8 SER F   29  LEU F   42  1                                  14    
HELIX  108 AL9 PRO F   44  GLU F   56  1                                  13    
HELIX  109 AM1 LYS F   81  GLY F   87  1                                   7    
HELIX  110 AM2 GLY F   87  ALA F  101  1                                  15    
HELIX  111 AM3 ASP F  103  LEU F  121  1                                  19    
HELIX  112 AM4 VAL F  123  GLN F  138  1                                  16    
HELIX  113 AM5 ALA F  144  GLY F  159  1                                  16    
HELIX  114 AM6 LYS F  160  ASN F  174  1                                  15    
HELIX  115 AM7 ASN F  185  LEU F  207  1                                  23    
HELIX  116 AM8 MET F  209  ALA F  226  1                                  18    
HELIX  117 AM9 ASP F  231  MET F  249  1                                  19    
HELIX  118 AN1 SER F  250  ASN F  259  1                                  10    
HELIX  119 AN2 LEU F  265  PHE F  271  1                                   7    
HELIX  120 AN3 HIS F  273  SER F  289  1                                  17    
HELIX  121 AN4 THR F  292  SER F  312  1                                  21    
HELIX  122 AN5 PRO F  317  THR F  338  1                                  22    
HELIX  123 AN6 GLY F  347  HIS F  369  1                                  23    
HELIX  124 AN7 THR F  372  SER F  395  1                                  24    
HELIX  125 AN8 ARG F  397  LEU F  419  1                                  23    
HELIX  126 AN9 ARG F  440  ILE F  445  5                                   6    
HELIX  127 AO1 ASN G    3  GLU G   24  1                                  22    
HELIX  128 AO2 SER G   29  LEU G   42  1                                  14    
HELIX  129 AO3 PRO G   44  GLU G   56  1                                  13    
HELIX  130 AO4 LYS G   81  GLY G   87  1                                   7    
HELIX  131 AO5 GLY G   87  ALA G  101  1                                  15    
HELIX  132 AO6 ASP G  103  LEU G  121  1                                  19    
HELIX  133 AO7 VAL G  123  GLN G  138  1                                  16    
HELIX  134 AO8 ALA G  144  SER G  158  1                                  15    
HELIX  135 AO9 LYS G  160  ASN G  174  1                                  15    
HELIX  136 AP1 ASN G  185  LEU G  207  1                                  23    
HELIX  137 AP2 MET G  209  ALA G  226  1                                  18    
HELIX  138 AP3 ASP G  231  MET G  249  1                                  19    
HELIX  139 AP4 SER G  250  ASN G  259  1                                  10    
HELIX  140 AP5 LEU G  265  PHE G  271  1                                   7    
HELIX  141 AP6 HIS G  273  SER G  289  1                                  17    
HELIX  142 AP7 THR G  292  SER G  312  1                                  21    
HELIX  143 AP8 PRO G  317  THR G  338  1                                  22    
HELIX  144 AP9 GLY G  347  HIS G  369  1                                  23    
HELIX  145 AQ1 THR G  372  SER G  395  1                                  24    
HELIX  146 AQ2 ARG G  397  LEU G  419  1                                  23    
HELIX  147 AQ3 ARG G  440  ILE G  445  5                                   6    
HELIX  148 AQ4 ASN H    3  GLU H   24  1                                  22    
HELIX  149 AQ5 SER H   29  LEU H   42  1                                  14    
HELIX  150 AQ6 PRO H   44  GLU H   56  1                                  13    
HELIX  151 AQ7 LYS H   81  GLY H   87  1                                   7    
HELIX  152 AQ8 GLY H   87  ALA H  101  1                                  15    
HELIX  153 AQ9 ASP H  103  LEU H  121  1                                  19    
HELIX  154 AR1 VAL H  123  GLN H  138  1                                  16    
HELIX  155 AR2 ALA H  144  SER H  158  1                                  15    
HELIX  156 AR3 LYS H  160  ASN H  174  1                                  15    
HELIX  157 AR4 ASN H  185  LEU H  207  1                                  23    
HELIX  158 AR5 MET H  209  ALA H  226  1                                  18    
HELIX  159 AR6 ASP H  231  MET H  249  1                                  19    
HELIX  160 AR7 SER H  250  ASN H  259  1                                  10    
HELIX  161 AR8 LEU H  265  PHE H  271  1                                   7    
HELIX  162 AR9 HIS H  273  SER H  289  1                                  17    
HELIX  163 AS1 THR H  292  SER H  312  1                                  21    
HELIX  164 AS2 PRO H  317  GLU H  319  5                                   3    
HELIX  165 AS3 LEU H  320  LEU H  337  1                                  18    
HELIX  166 AS4 GLY H  347  HIS H  369  1                                  23    
HELIX  167 AS5 THR H  372  SER H  395  1                                  24    
HELIX  168 AS6 ARG H  397  LEU H  419  1                                  23    
HELIX  169 AS7 ASN I    3  GLU I   24  1                                  22    
HELIX  170 AS8 SER I   29  LEU I   42  1                                  14    
HELIX  171 AS9 PRO I   44  GLU I   56  1                                  13    
HELIX  172 AT1 LYS I   81  GLY I   87  1                                   7    
HELIX  173 AT2 GLY I   87  ALA I  101  1                                  15    
HELIX  174 AT3 ASP I  103  LEU I  121  1                                  19    
HELIX  175 AT4 VAL I  123  GLN I  138  1                                  16    
HELIX  176 AT5 ALA I  144  SER I  158  1                                  15    
HELIX  177 AT6 LYS I  160  ASN I  174  1                                  15    
HELIX  178 AT7 ASN I  185  LEU I  207  1                                  23    
HELIX  179 AT8 MET I  209  ALA I  226  1                                  18    
HELIX  180 AT9 ASP I  231  MET I  249  1                                  19    
HELIX  181 AU1 SER I  250  ASN I  259  1                                  10    
HELIX  182 AU2 LEU I  265  GLU I  270  1                                   6    
HELIX  183 AU3 HIS I  273  SER I  289  1                                  17    
HELIX  184 AU4 THR I  292  SER I  312  1                                  21    
HELIX  185 AU5 LEU I  325  THR I  338  1                                  14    
HELIX  186 AU6 GLY I  347  GLY I  370  1                                  24    
HELIX  187 AU7 THR I  372  SER I  395  1                                  24    
HELIX  188 AU8 ARG I  397  LEU I  419  1                                  23    
SITE     1 AC1 16 PHE A  61  GLN A  67  TYR A  68  ARG A 116                    
SITE     2 AC1 16 GLN A 146  ARG A 150  ARG A 153  VAL A 195                    
SITE     3 AC1 16 GLN A 198  TYR A 224  ASP A 231  LYS A 233                    
SITE     4 AC1 16 GLY A 234  SER A 236  THR A 237  PHE A 295                    
SITE     1 AC2 17 PHE B  61  GLN B  67  TYR B  68  ARG B 116                    
SITE     2 AC2 17 TYR B 119  GLN B 146  ARG B 150  ARG B 153                    
SITE     3 AC2 17 VAL B 195  GLN B 198  TYR B 224  ASP B 231                    
SITE     4 AC2 17 LYS B 233  GLY B 234  SER B 236  THR B 237                    
SITE     5 AC2 17 PHE B 295                                                     
SITE     1 AC3 16 PHE C  61  GLN C  67  ARG C 116  TYR C 119                    
SITE     2 AC3 16 GLN C 146  ARG C 150  ARG C 153  VAL C 195                    
SITE     3 AC3 16 GLN C 198  TYR C 224  ASP C 231  LYS C 233                    
SITE     4 AC3 16 GLY C 234  SER C 236  THR C 237  PHE C 295                    
SITE     1 AC4 16 PHE D  61  GLN D  67  ARG D 116  TYR D 119                    
SITE     2 AC4 16 GLN D 146  ARG D 150  ARG D 153  VAL D 195                    
SITE     3 AC4 16 GLN D 198  TYR D 224  ASP D 231  LYS D 233                    
SITE     4 AC4 16 GLY D 234  SER D 236  THR D 237  PHE D 295                    
SITE     1 AC5 17 PHE E  61  GLN E  67  TYR E  68  ARG E 116                    
SITE     2 AC5 17 TYR E 119  GLN E 146  ARG E 150  ARG E 153                    
SITE     3 AC5 17 VAL E 195  GLN E 198  TYR E 224  ASP E 231                    
SITE     4 AC5 17 LYS E 233  GLY E 234  SER E 236  THR E 237                    
SITE     5 AC5 17 PHE E 295                                                     
SITE     1 AC6 17 PHE F  61  GLN F  67  TYR F  68  ARG F 116                    
SITE     2 AC6 17 TYR F 119  GLN F 146  ARG F 150  ARG F 153                    
SITE     3 AC6 17 VAL F 195  GLN F 198  TYR F 224  ASP F 231                    
SITE     4 AC6 17 LYS F 233  GLY F 234  SER F 236  THR F 237                    
SITE     5 AC6 17 PHE F 295                                                     
SITE     1 AC7 16 PHE G  61  ARG G 116  TYR G 119  GLN G 146                    
SITE     2 AC7 16 ARG G 150  ARG G 153  VAL G 195  GLN G 198                    
SITE     3 AC7 16 TYR G 224  ASP G 231  LYS G 233  GLY G 234                    
SITE     4 AC7 16 SER G 236  THR G 237  SER G 289  PHE G 295                    
SITE     1 AC8 16 PHE H  61  ARG H 116  TYR H 119  GLN H 146                    
SITE     2 AC8 16 ILE H 149  ARG H 150  ARG H 153  VAL H 195                    
SITE     3 AC8 16 GLN H 198  TYR H 224  ASP H 231  LYS H 233                    
SITE     4 AC8 16 GLY H 234  SER H 236  THR H 237  PHE H 295                    
SITE     1 AC9 15 PHE I  61  GLN I  67  ARG I 116  TYR I 119                    
SITE     2 AC9 15 GLN I 146  ARG I 150  ARG I 153  VAL I 195                    
SITE     3 AC9 15 TYR I 224  ASP I 231  LYS I 233  GLY I 234                    
SITE     4 AC9 15 SER I 236  THR I 237  PHE I 295                               
CRYST1  169.260  214.388  173.151  90.00 110.33  90.00 C 1 2 1      36          
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      0.005908  0.000000  0.002189        0.00000                         
SCALE2      0.000000  0.004664  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006159        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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