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Database: PDB
Entry: 1PSN
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Original site: 1PSN 
HEADER    HYDROLASE (ACID PROTEINASE)             23-JAN-95   1PSN              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN PEPSIN AND ITS COMPLEX WITH            
TITLE    2 PEPSTATIN                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEPSIN 3A;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.23.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    HYDROLASE (ACID PROTEINASE)                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.FUJINAGA,M.M.CHERNAIA,N.TARASOVA,S.C.MOSIMANN,M.N.G.JAMES           
REVDAT   2   24-FEB-09 1PSN    1       VERSN                                    
REVDAT   1   20-APR-95 1PSN    0                                                
JRNL        AUTH   M.FUJINAGA,M.M.CHERNAIA,N.I.TARASOVA,S.C.MOSIMANN,           
JRNL        AUTH 2 M.N.JAMES                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN PEPSIN AND ITS COMPLEX            
JRNL        TITL 2 WITH PEPSTATIN.                                              
JRNL        REF    PROTEIN SCI.                  V.   4   960 1995              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   7663352                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.R.SIELECKI,A.A.FEDOROV,A.BOODHOO,N.S.ANDREEVA,             
REMARK   1  AUTH 2 M.N.G.JAMES                                                  
REMARK   1  TITL   MOLECULAR AND CRYSTAL STRUCTURES OF MONOCLINIC               
REMARK   1  TITL 2 PORCINE PEPSIN REFINED AT 1.8 ANGSTROMS RESOLUTION           
REMARK   1  REF    J.MOL.BIOL.                   V. 214   143 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : GROMOS                                               
REMARK   3   AUTHORS     : FUJINAGA,GROS,VAN GUNSTEREN                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21303                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2438                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 136                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.39                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.81                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES WITH ZERO OCCUPANCIES AND        
REMARK   3  NEGATIVE B-FACTORS ARE DISORDERED AND THEIR POSITIONS ARE NOT       
REMARK   3  CONSIDERED TO HAVE BEEN DETERMINED.                                 
REMARK   4                                                                      
REMARK   4 1PSN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-94                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
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          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SAN DIEGO MULTIWIRE DETECTION      
REMARK 200                                   SYSTEM                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAN DIEGO SOFTWARE                 
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33057                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 75.0                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       35.98500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       20.57500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       75.79500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       20.57500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.98500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       75.79500            
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: 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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     VAL A    1                                                       
REMARK 475     SER A  241                                                       
REMARK 475     ASP A  242                                                       
REMARK 475     GLY A  243                                                       
REMARK 475     GLU A  294                                                       
REMARK 475     SER A  295                                                       
REMARK 475     GLY A  296                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A 125   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 159       16.41     57.02                                   
REMARK 500    ASN A 240     -162.67   -100.71                                   
REMARK 500    GLU A 279       61.23     61.28                                   
REMARK 500    SER A 295       42.83   -103.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    PHE A  27         0.08    SIDE_CHAIN                              
REMARK 500    TYR A 154         0.10    SIDE_CHAIN                              
REMARK 500    TYR A 175         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LEU A 301         12.62                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 399        DISTANCE =  6.70 ANGSTROMS                       
REMARK 525    HOH A 403        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A 419        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A 440        DISTANCE =  6.13 ANGSTROMS                       
DBREF  1PSN A    1   326  UNP    P00790   PEPA_HUMAN      63    388             
SEQRES   1 A  326  VAL ASP GLU GLN PRO LEU GLU ASN TYR LEU ASP MET GLU          
SEQRES   2 A  326  TYR PHE GLY THR ILE GLY ILE GLY THR PRO ALA GLN ASP          
SEQRES   3 A  326  PHE THR VAL VAL PHE ASP THR GLY SER SER ASN LEU TRP          
SEQRES   4 A  326  VAL PRO SER VAL TYR CYS SER SER LEU ALA CYS THR ASN          
SEQRES   5 A  326  HIS ASN ARG PHE ASN PRO GLU ASP SER SER THR TYR GLN          
SEQRES   6 A  326  SER THR SER GLU THR VAL SER ILE THR TYR GLY THR GLY          
SEQRES   7 A  326  SER MET THR GLY ILE LEU GLY TYR ASP THR VAL GLN VAL          
SEQRES   8 A  326  GLY GLY ILE SER ASP THR ASN GLN ILE PHE GLY LEU SER          
SEQRES   9 A  326  GLU THR GLU PRO GLY SER PHE LEU TYR TYR ALA PRO PHE          
SEQRES  10 A  326  ASP GLY ILE LEU GLY LEU ALA TYR PRO SER ILE SER SER          
SEQRES  11 A  326  SER GLY ALA THR PRO VAL PHE ASP ASN ILE TRP ASN GLN          
SEQRES  12 A  326  GLY LEU VAL SER GLN ASP LEU PHE SER VAL TYR LEU SER          
SEQRES  13 A  326  ALA ASP ASP GLN SER GLY SER VAL VAL ILE PHE GLY GLY          
SEQRES  14 A  326  ILE ASP SER SER TYR TYR THR GLY SER LEU ASN TRP VAL          
SEQRES  15 A  326  PRO VAL THR VAL GLU GLY TYR TRP GLN ILE THR VAL ASP          
SEQRES  16 A  326  SER ILE THR MET ASN GLY GLU ALA ILE ALA CYS ALA GLU          
SEQRES  17 A  326  GLY CYS GLN ALA ILE VAL ASP THR GLY THR SER LEU LEU          
SEQRES  18 A  326  THR GLY PRO THR SER PRO ILE ALA ASN ILE GLN SER ASP          
SEQRES  19 A  326  ILE GLY ALA SER GLU ASN SER ASP GLY ASP MET VAL VAL          
SEQRES  20 A  326  SER CYS SER ALA ILE SER SER LEU PRO ASP ILE VAL PHE          
SEQRES  21 A  326  THR ILE ASN GLY VAL GLN TYR PRO VAL PRO PRO SER ALA          
SEQRES  22 A  326  TYR ILE LEU GLN SER GLU GLY SER CYS ILE SER GLY PHE          
SEQRES  23 A  326  GLN GLY MET ASN LEU PRO THR GLU SER GLY GLU LEU TRP          
SEQRES  24 A  326  ILE LEU GLY ASP VAL PHE ILE ARG GLN TYR PHE THR VAL          
SEQRES  25 A  326  PHE ASP ARG ALA ASN ASN GLN VAL GLY LEU ALA PRO VAL          
SEQRES  26 A  326  ALA                                                          
FORMUL   2  HOH   *136(H2 O)                                                    
HELIX    1   1 LEU A   48  ASN A   52  1                                   5    
HELIX    2   2 PRO A   58  ASP A   60  5                                   3    
HELIX    3   3 PHE A  111  TYR A  114  1                                   4    
HELIX    4   4 PRO A  126  ILE A  128  5                                   3    
HELIX    5   5 SER A  130  GLY A  132  5                                   3    
HELIX    6   6 VAL A  136  ASN A  142  1                                   7    
HELIX    7   7 SER A  172  TYR A  174  5                                   3    
HELIX    8   8 THR A  225  ASP A  234  1                                  10    
HELIX    9   9 CYS A  249  SER A  254  5                                   6    
HELIX   10  10 PRO A  271  TYR A  274  1                                   4    
HELIX   11  11 ASP A  303  ILE A  306  1                                   4    
SHEET    1   A 6 ASP A   2  PRO A   5  0                                        
SHEET    2   A 6 VAL A 164  PHE A 167 -1  N  PHE A 167   O  ASP A   2           
SHEET    3   A 6 LEU A 150  TYR A 154 -1  N  TYR A 154   O  VAL A 164           
SHEET    4   A 6 TYR A 309  ASP A 314 -1  N  PHE A 313   O  PHE A 151           
SHEET    5   A 6 GLN A 319  PRO A 324 -1  N  ALA A 323   O  PHE A 310           
SHEET    6   A 6 ASN A 180  PRO A 183 -1  N  VAL A 182   O  VAL A 320           
SHEET    1   B 4 GLU A   7  TYR A   9  0                                        
SHEET    2   B 4 GLU A  13  ILE A  20 -1  N  PHE A  15   O  GLU A   7           
SHEET    3   B 4 GLN A  25  ASP A  32 -1  N  VAL A  29   O  GLY A  16           
SHEET    4   B 4 GLY A 119  GLY A 122  1  N  GLY A 119   O  VAL A  30           
SHEET    1   C 3 THR A  70  THR A  74  0                                        
SHEET    2   C 3 SER A  79  ASP A  87 -1  N  GLY A  82   O  VAL A  71           
SHEET    3   C 3 GLN A  99  THR A 106 -1  N  THR A 106   O  THR A  81           
SHEET    1   D 2 VAL A  89  VAL A  91  0                                        
SHEET    2   D 2 ILE A  94  ASP A  96 -1  N  ASP A  96   O  VAL A  89           
SHEET    1   E 3 GLN A 191  VAL A 194  0                                        
SHEET    2   E 3 CYS A 210  VAL A 214 -1  N  ALA A 212   O  ILE A 192           
SHEET    3   E 3 LEU A 298  LEU A 301  1  N  TRP A 299   O  GLN A 211           
SHEET    1   F 4 VAL A 265  VAL A 269  0                                        
SHEET    2   F 4 ILE A 258  ILE A 262 -1  N  ILE A 262   O  VAL A 265           
SHEET    3   F 4 SER A 196  MET A 199 -1  N  THR A 198   O  VAL A 259           
SHEET    4   F 4 GLU A 202  ALA A 205 -1  N  ALA A 205   O  ILE A 197           
SHEET    1   G 2 LEU A 221  GLY A 223  0                                        
SHEET    2   G 2 PHE A 286  GLY A 288  1  N  GLN A 287   O  LEU A 221           
SHEET    1   H 2 ILE A 275  SER A 278  0                                        
SHEET    2   H 2 SER A 281  SER A 284 -1  N  ILE A 283   O  LEU A 276           
SSBOND   1 CYS A   45    CYS A   50                          1555   1555  2.03  
SSBOND   2 CYS A  206    CYS A  210                          1555   1555  2.04  
SSBOND   3 CYS A  249    CYS A  282                          1555   1555  2.04  
CISPEP   1 THR A   22    PRO A   23          0        -4.09                     
CRYST1   71.970  151.590   41.150  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      0.013895  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006597  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024301        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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