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Database: PDB
Entry: 1WPX
LinkDB: 1WPX
Original site: 1WPX 
HEADER    HYDROLASE                               14-SEP-04   1WPX              
TITLE     CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE Y INHIBITOR COMPLEXED WITH THE  
TITLE    2 COGNATE PROTEINASE                                                   
CAVEAT     1WPX    NAG A 820 HAS WRONG CHIRALITY AT ATOM C1 NAG A 830 HAS WRONG 
CAVEAT   2 1WPX    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYPEPTIDASE Y;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CARBOXYPEPTIDASE YSCY;                                      
COMPND   5 EC: 3.4.16.5;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CARBOXYPEPTIDASE Y INHIBITOR;                              
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: CPY INHIBITOR, IC, IC, DKA1 PROTEIN, NSP1 PROTEIN, TFS1     
COMPND  10 PROTEIN                                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   7 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   8 ORGANISM_TAXID: 4932                                                 
KEYWDS    CARBOXYPEPTIDASE INHIBITOR, SERINE PROTEINASE INHIBITOR, PROTEINASE-  
KEYWDS   2 INHIBITOR COMPLEX, PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN,         
KEYWDS   3 PHOSPHOLIPID, HYDROLASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MIMA,M.HAYASHIDA,T.FUJII,Y.NARITA,R.HAYASHI,M.UEDA,Y.HATA           
REVDAT   4   29-JUL-20 1WPX    1       CAVEAT COMPND REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   13-JUL-11 1WPX    1       VERSN                                    
REVDAT   2   24-FEB-09 1WPX    1       VERSN                                    
REVDAT   1   01-MAR-05 1WPX    0                                                
JRNL        AUTH   J.MIMA,M.HAYASHIDA,T.FUJII,Y.NARITA,R.HAYASHI,M.UEDA,Y.HATA  
JRNL        TITL   STRUCTURE OF THE CARBOXYPEPTIDASE Y INHIBITOR I(C) IN        
JRNL        TITL 2 COMPLEX WITH THE COGNATE PROTEINASE REVEALS A NOVEL MODE OF  
JRNL        TITL 3 THE PROTEINASE-PROTEIN INHIBITOR INTERACTION                 
JRNL        REF    J.MOL.BIOL.                   V. 346  1323 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15713484                                                     
JRNL        DOI    10.1016/J.JMB.2004.12.051                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1566324.260                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 27780                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2456                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4386                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 179                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4960                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.93000                                              
REMARK   3    B22 (A**2) : -7.25000                                             
REMARK   3    B33 (A**2) : -0.68000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.820                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 40.48                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CAPPING.PARAM                                  
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : CAPPING.TOP                                    
REMARK   3  TOPOLOGY FILE  5   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1WPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-SEP-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000023865.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JAN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 4.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28017                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 1.95M AMMONIUM      
REMARK 280  SULFATE, PH 4.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       40.56450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       32.57000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       93.29500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       32.57000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.56450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       93.29500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS B   573                                                      
REMARK 465     SER B   574                                                      
REMARK 465     VAL B   575                                                      
REMARK 465     PRO B   576                                                      
REMARK 465     GLN B   577                                                      
REMARK 465     ALA B   578                                                      
REMARK 465     GLU B   622                                                      
REMARK 465     ALA B   623                                                      
REMARK 465     THR B   624                                                      
REMARK 465     HIS B   625                                                      
REMARK 465     GLU B   626                                                      
REMARK 465     THR B   627                                                      
REMARK 465     SER B   628                                                      
REMARK 465     GLY B   629                                                      
REMARK 465     ALA B   630                                                      
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    ILE A  10      -72.57     38.94                                   
REMARK 500    ASP A  11       84.73   -153.26                                   
REMARK 500    GLU A  26       -1.30   -149.53                                   
REMARK 500    ASN A  39     -100.03   -107.66                                   
REMARK 500    ALA A  88      148.09   -174.36                                   
REMARK 500    ASN A  98        7.49     84.45                                   
REMARK 500    SER A 106      -77.26    -83.02                                   
REMARK 500    SER A 107      175.37    -57.24                                   
REMARK 500    VAL A 134      -45.00   -137.18                                   
REMARK 500    LYS A 136       13.96    -65.12                                   
REMARK 500    SER A 146     -119.55     60.66                                   
REMARK 500    ASN A 176       56.86     34.90                                   
REMARK 500    CYS A 341       45.24   -144.16                                   
REMARK 500    LYS A 382      113.96   -163.49                                   
REMARK 500    LYS A 385     -125.45     57.67                                   
REMARK 500    ALA B 557       30.34    -95.22                                   
REMARK 500    LYS B 569       88.86    -66.27                                   
REMARK 500    GLN B 570      -37.66    176.52                                   
REMARK 500    MET B 571        6.22    -63.69                                   
REMARK 500    ASP B 587      128.00    -34.75                                   
REMARK 500    ASP B 597       54.37   -116.63                                   
REMARK 500    SER B 607      130.05    -38.08                                   
REMARK 500    GLU B 608       81.92     74.22                                   
REMARK 500    PHE B 634      146.71   -174.50                                   
REMARK 500    LYS B 641      -89.32    -36.95                                   
REMARK 500    ALA B 653       49.90   -153.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BD9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1BEH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1A44   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1QOU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FJJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FUX   RELATED DB: PDB                                   
DBREF  1WPX A    1   421  UNP    P00729   CBPY_YEAST     112    532             
DBREF  1WPX B  501   719  UNP    P14306   CPYI_YEAST       1    219             
SEQRES   1 A  421  LYS ILE LYS ASP PRO LYS ILE LEU GLY ILE ASP PRO ASN          
SEQRES   2 A  421  VAL THR GLN TYR THR GLY TYR LEU ASP VAL GLU ASP GLU          
SEQRES   3 A  421  ASP LYS HIS PHE PHE PHE TRP THR PHE GLU SER ARG ASN          
SEQRES   4 A  421  ASP PRO ALA LYS ASP PRO VAL ILE LEU TRP LEU ASN GLY          
SEQRES   5 A  421  GLY PRO GLY CYS SER SER LEU THR GLY LEU PHE PHE GLU          
SEQRES   6 A  421  LEU GLY PRO SER SER ILE GLY PRO ASP LEU LYS PRO ILE          
SEQRES   7 A  421  GLY ASN PRO TYR SER TRP ASN SER ASN ALA THR VAL ILE          
SEQRES   8 A  421  PHE LEU ASP GLN PRO VAL ASN VAL GLY PHE SER TYR SER          
SEQRES   9 A  421  GLY SER SER GLY VAL SER ASN THR VAL ALA ALA GLY LYS          
SEQRES  10 A  421  ASP VAL TYR ASN PHE LEU GLU LEU PHE PHE ASP GLN PHE          
SEQRES  11 A  421  PRO GLU TYR VAL ASN LYS GLY GLN ASP PHE HIS ILE ALA          
SEQRES  12 A  421  GLY GLU SER TYR ALA GLY HIS TYR ILE PRO VAL PHE ALA          
SEQRES  13 A  421  SER GLU ILE LEU SER HIS LYS ASP ARG ASN PHE ASN LEU          
SEQRES  14 A  421  THR SER VAL LEU ILE GLY ASN GLY LEU THR ASP PRO LEU          
SEQRES  15 A  421  THR GLN TYR ASN TYR TYR GLU PRO MET ALA CYS GLY GLU          
SEQRES  16 A  421  GLY GLY GLU PRO SER VAL LEU PRO SER GLU GLU CYS SER          
SEQRES  17 A  421  ALA MET GLU ASP SER LEU GLU ARG CYS LEU GLY LEU ILE          
SEQRES  18 A  421  GLU SER CYS TYR ASP SER GLN SER VAL TRP SER CYS VAL          
SEQRES  19 A  421  PRO ALA THR ILE TYR CYS ASN ASN ALA GLN LEU ALA PRO          
SEQRES  20 A  421  TYR GLN ARG THR GLY ARG ASN VAL TYR ASP ILE ARG LYS          
SEQRES  21 A  421  ASP CYS GLU GLY GLY ASN LEU CYS TYR PRO THR LEU GLN          
SEQRES  22 A  421  ASP ILE ASP ASP TYR LEU ASN GLN ASP TYR VAL LYS GLU          
SEQRES  23 A  421  ALA VAL GLY ALA GLU VAL ASP HIS TYR GLU SER CYS ASN          
SEQRES  24 A  421  PHE ASP ILE ASN ARG ASN PHE LEU PHE ALA GLY ASP TRP          
SEQRES  25 A  421  MET LYS PRO TYR HIS THR ALA VAL THR ASP LEU LEU ASN          
SEQRES  26 A  421  GLN ASP LEU PRO ILE LEU VAL TYR ALA GLY ASP LYS ASP          
SEQRES  27 A  421  PHE ILE CYS ASN TRP LEU GLY ASN LYS ALA TRP THR ASP          
SEQRES  28 A  421  VAL LEU PRO TRP LYS TYR ASP GLU GLU PHE ALA SER GLN          
SEQRES  29 A  421  LYS VAL ARG ASN TRP THR ALA SER ILE THR ASP GLU VAL          
SEQRES  30 A  421  ALA GLY GLU VAL LYS SER TYR LYS HIS PHE THR TYR LEU          
SEQRES  31 A  421  ARG VAL PHE ASN GLY GLY HIS MET VAL PRO PHE ASP VAL          
SEQRES  32 A  421  PRO GLU ASN ALA LEU SER MET VAL ASN GLU TRP ILE HIS          
SEQRES  33 A  421  GLY GLY PHE SER LEU                                          
SEQRES   1 B  220  ACE MET ASN GLN ALA ILE ASP PHE ALA GLN ALA SER ILE          
SEQRES   2 B  220  ASP SER TYR LYS LYS HIS GLY ILE LEU GLU ASP VAL ILE          
SEQRES   3 B  220  HIS ASP THR SER PHE GLN PRO SER GLY ILE LEU ALA VAL          
SEQRES   4 B  220  GLU TYR SER SER SER ALA PRO VAL ALA MET GLY ASN THR          
SEQRES   5 B  220  LEU PRO THR GLU LYS ALA ARG SER LYS PRO GLN PHE GLN          
SEQRES   6 B  220  PHE THR PHE ASN LYS GLN MET GLN LYS SER VAL PRO GLN          
SEQRES   7 B  220  ALA ASN ALA TYR VAL PRO GLN ASP ASP ASP LEU PHE THR          
SEQRES   8 B  220  LEU VAL MET THR ASP PRO ASP ALA PRO SER LYS THR ASP          
SEQRES   9 B  220  HIS LYS TRP SER GLU PHE CYS HIS LEU VAL GLU CYS ASP          
SEQRES  10 B  220  LEU LYS LEU LEU ASN GLU ALA THR HIS GLU THR SER GLY          
SEQRES  11 B  220  ALA THR GLU PHE PHE ALA SER GLU PHE ASN THR LYS GLY          
SEQRES  12 B  220  SER ASN THR LEU ILE GLU TYR MET GLY PRO ALA PRO PRO          
SEQRES  13 B  220  LYS GLY SER GLY PRO HIS ARG TYR VAL PHE LEU LEU TYR          
SEQRES  14 B  220  LYS GLN PRO LYS GLY VAL ASP SER SER LYS PHE SER LYS          
SEQRES  15 B  220  ILE LYS ASP ARG PRO ASN TRP GLY TYR GLY THR PRO ALA          
SEQRES  16 B  220  THR GLY VAL GLY LYS TRP ALA LYS GLU ASN ASN LEU GLN          
SEQRES  17 B  220  LEU VAL ALA SER ASN PHE PHE TYR ALA GLU THR LYS              
MODRES 1WPX ASN A   87  ASN  GLYCOSYLATION SITE                                 
MODRES 1WPX ASN A  168  ASN  GLYCOSYLATION SITE                                 
MODRES 1WPX ASN A  368  ASN  GLYCOSYLATION SITE                                 
HET    ACE  B 500       3                                                       
HET    NAG  A 810      14                                                       
HET    NAG  A 820      14                                                       
HET    NAG  A 830      14                                                       
HET    SO4  A 901       5                                                       
HET    SO4  B 902       5                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL   8  HOH   *51(H2 O)                                                     
HELIX    1   1 ASP A    4  LEU A    8  5                                   5    
HELIX    2   2 SER A   58  PHE A   64  1                                   7    
HELIX    3   3 SER A   83  ASN A   87  5                                   5    
HELIX    4   4 ASN A  111  PHE A  130  1                                  20    
HELIX    5   5 PRO A  131  LYS A  136  1                                   6    
HELIX    6   6 TYR A  147  HIS A  162  1                                  16    
HELIX    7   7 ASP A  180  TYR A  185  1                                   6    
HELIX    8   8 TYR A  187  CYS A  193  1                                   7    
HELIX    9   9 PRO A  203  GLN A  228  1                                  26    
HELIX   10  10 SER A  229  LEU A  245  1                                  17    
HELIX   11  11 LEU A  245  THR A  251  1                                   7    
HELIX   12  12 THR A  271  ASN A  280  1                                  10    
HELIX   13  13 GLN A  281  GLY A  289  1                                   9    
HELIX   14  14 ASN A  299  PHE A  308  1                                  10    
HELIX   15  15 HIS A  317  GLN A  326  1                                  10    
HELIX   16  16 ASN A  342  LEU A  353  1                                  12    
HELIX   17  17 TYR A  357  GLN A  364  1                                   8    
HELIX   18  18 MET A  398  VAL A  403  1                                   6    
HELIX   19  19 VAL A  403  HIS A  416  1                                  14    
HELIX   20  20 MET B  501  ILE B  505  5                                   5    
HELIX   21  21 ASP B  506  HIS B  518  1                                  13    
HELIX   22  22 GLY B  519  VAL B  524  1                                   6    
HELIX   23  23 PRO B  553  ARG B  558  5                                   6    
HELIX   24  24 ASP B  675  PHE B  679  5                                   5    
HELIX   25  25 ARG B  685  TYR B  690  5                                   6    
HELIX   26  26 GLY B  696  GLU B  703  1                                   8    
SHEET    1   A11 ILE A   2  LYS A   3  0                                        
SHEET    2   A11 GLN A  16  ASP A  22 -1  O  THR A  18   N  LYS A   3           
SHEET    3   A11 HIS A  29  PHE A  35 -1  O  THR A  34   N  TYR A  17           
SHEET    4   A11 THR A  89  LEU A  93 -1  O  PHE A  92   N  TRP A  33           
SHEET    5   A11 VAL A  46  LEU A  50  1  N  TRP A  49   O  ILE A  91           
SHEET    6   A11 PHE A 140  GLU A 145  1  O  ALA A 143   N  LEU A  48           
SHEET    7   A11 SER A 171  GLY A 175  1  O  LEU A 173   N  ILE A 142           
SHEET    8   A11 ILE A 330  GLY A 335  1  O  LEU A 331   N  ILE A 174           
SHEET    9   A11 PHE A 387  VAL A 392  1  O  THR A 388   N  VAL A 332           
SHEET   10   A11 VAL A 377  TYR A 384 -1  N  LYS A 382   O  TYR A 389           
SHEET   11   A11 ARG A 367  THR A 370 -1  N  TRP A 369   O  GLY A 379           
SHEET    1   B 2 SER A  69  ILE A  71  0                                        
SHEET    2   B 2 PRO A  77  GLY A  79 -1  O  ILE A  78   N  SER A  70           
SHEET    1   C 6 ALA B 544  VAL B 546  0                                        
SHEET    2   C 6 GLY B 534  SER B 541 -1  N  SER B 541   O  ALA B 544           
SHEET    3   C 6 GLN B 562  ASN B 568 -1  O  GLN B 562   N  GLU B 539           
SHEET    4   C 6 PHE B 633  ASN B 639 -1  O  SER B 636   N  PHE B 565           
SHEET    5   C 6 PHE B 609  LEU B 619 -1  N  LYS B 618   O  ASN B 639           
SHEET    6   C 6 ASN B 644  ILE B 647 -1  O  ASN B 644   N  CYS B 615           
SHEET    1   D 8 ALA B 544  VAL B 546  0                                        
SHEET    2   D 8 GLY B 534  SER B 541 -1  N  SER B 541   O  ALA B 544           
SHEET    3   D 8 GLN B 562  ASN B 568 -1  O  GLN B 562   N  GLU B 539           
SHEET    4   D 8 PHE B 633  ASN B 639 -1  O  SER B 636   N  PHE B 565           
SHEET    5   D 8 PHE B 609  LEU B 619 -1  N  LYS B 618   O  ASN B 639           
SHEET    6   D 8 PHE B 589  ASP B 595 -1  N  PHE B 589   O  LEU B 617           
SHEET    7   D 8 HIS B 661  LYS B 669 -1  O  TYR B 668   N  THR B 590           
SHEET    8   D 8 GLN B 707  ALA B 716 -1  O  VAL B 709   N  LEU B 667           
SSBOND   1 CYS A   56    CYS A  298                          1555   1555  2.03  
SSBOND   2 CYS A  193    CYS A  207                          1555   1555  2.03  
SSBOND   3 CYS A  217    CYS A  240                          1555   1555  2.03  
SSBOND   4 CYS A  224    CYS A  233                          1555   1555  2.02  
SSBOND   5 CYS A  262    CYS A  268                          1555   1555  2.02  
LINK         ND2 ASN A  87                 C1  NAG A 810     1555   1555  1.45  
LINK         ND2 ASN A 168                 C1  NAG A 820     1555   1555  1.45  
LINK         ND2 ASN A 368                 C1  NAG A 830     1555   1555  1.45  
LINK         C   ACE B 500                 N   MET B 501     1555   1555  1.33  
CISPEP   1 GLY A   53    PRO A   54          0        -0.10                     
CISPEP   2 GLN A   95    PRO A   96          0        -0.23                     
CISPEP   3 ALA B  598    PRO B  599          0        -0.08                     
CRYST1   81.129  186.590   65.140  90.00  90.00  90.00 P 21 21 21    4          
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      0.012326  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005359  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015352        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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