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Database: PDB
Entry: 1FXY
LinkDB: 1FXY
Original site: 1FXY 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           22-APR-98   1FXY              
TITLE     COAGULATION FACTOR XA-TRYPSIN CHIMERA INHIBITED WITH D-PHE-PRO-ARG-   
TITLE    2 CHLOROMETHYLKETONE                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR XA-TRYPSIN CHIMERA;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: UT5600                                     
KEYWDS    CHIMERA, PROTEASE, CHLOROMETHYLKETONE, HYDROLASE-HYDROLASE INHIBITOR  
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.P.HOPFNER,E.KOPETZKI,G.-B.KRESSE,R.HUBER,W.BODE,R.A.ENGH            
REVDAT   3   13-JUL-11 1FXY    1       VERSN                                    
REVDAT   2   24-FEB-09 1FXY    1       VERSN                                    
REVDAT   1   17-JUN-98 1FXY    0                                                
JRNL        AUTH   K.P.HOPFNER,E.KOPETZKI,G.B.KRESSE,W.BODE,R.HUBER,R.A.ENGH    
JRNL        TITL   NEW ENZYME LINEAGES BY SUBDOMAIN SHUFFLING.                  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  95  9813 1998              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   9707558                                                      
JRNL        DOI    10.1073/PNAS.95.17.9813                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 10714                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
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            : 1730                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 82                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.24                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FXY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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        : MAY-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 280                                
REMARK 200  PH                             : 7.8                                
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA)          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
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) : 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: X-PLOR 3.8                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 15% PEG    
REMARK 280  6K, 100 MM HEPES, PH 7.8.                                           
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       32.75500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.46000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       32.75500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.46000            
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 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   BIOMT1   2 -1.000000  0.000000  0.000000       37.87357            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       70.30305            
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     SER A  246                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   23   NZ                                                  
REMARK 480     ASP A   24   CB   CG   OD1  OD2                                  
REMARK 480     GLU A   36   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU A   37   CB   CG   CD   OE1  OE2                             
REMARK 480     ASN A   38   CB   CG   OD1  ND2                                  
REMARK 480     LYS A   62   CB   CG   CD   CE   NZ                              
REMARK 480     ARG A   63   NE   CZ   NH1  NH2                                  
REMARK 480     ARG A   71   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU A   74   CG   CD   OE1  OE2                                  
REMARK 480     GLN A   75   CG   CD   OE1  NE2                                  
REMARK 480     GLU A   77   CB   CG   CD   OE1  OE2                             
REMARK 480     LYS A   90   NZ                                                  
REMARK 480     LYS A   96   CE   NZ                                             
REMARK 480     LYS A  109   CE   NZ                                             
REMARK 480     THR A  125   CG2                                                 
REMARK 480     LYS A  135   NZ                                                  
REMARK 480     ASP A  153   OD1  OD2                                            
REMARK 480     GLU A  154   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  167   CE   NZ                                             
REMARK 480     GLU A  186   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  188   NZ                                                  
REMARK 480     ASN A  202   CG   OD1  ND2                                       
REMARK 480     ASP A  217   CB                                                  
REMARK 480     LYS A  236   CE   NZ                                             
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    SER A 214      -69.23   -123.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE UNBOUND FORM OF THE INHIBITOR IS D-PHE-PRO-ARG-                  
REMARK 600 CHLOROMETHYLKETONE. UPON REACTION WITH PROTEIN IT FORMS TWO          
REMARK 600 COVALENT BONDS: 1) A COVALENT BOND TO SER 195 FORMING A HEMIKETAL    
REMARK 600 AR7 AND 2) A COVALENT BOND TO NE2 OF HIS 57                          
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]    
REMARK 630 AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE                   
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     0G6 A     1                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    DPN PRO AR7 0QE                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0G6 A 1                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES ARE NUMBERED ACCORDING TO THE CHYMOTRYPSIN                  
REMARK 999 NUMBERING SYSTEM.  THE MOLECULE IS A CHIMERIC CONSTRUCT              
REMARK 999 COMPOSED OF RESIDUES 16 - 121 FROM HUMAN COAGULATION FACTOR          
REMARK 999 XA AND RESIDUES 122 - 246 FROM HUMAN TRYPSIN I.  THE                 
REMARK 999 N-TERMINAL 15 RESIDUES WERE CLEAVED OFF PROTEOLYTICALLY.             
DBREF  1FXY A  122   246  UNP    P07477   TRY1_HUMAN     127    247             
SEQRES   1 A  228  ILE VAL GLY GLY TYR ASN CYS LYS ASP GLY GLU VAL PRO          
SEQRES   2 A  228  TRP GLN ALA LEU LEU ILE ASN GLU GLU ASN GLU GLY PHE          
SEQRES   3 A  228  CYS GLY GLY THR ILE LEU SER GLU PHE TYR ILE LEU THR          
SEQRES   4 A  228  ALA ALA HIS CYS LEU TYR GLN ALA LYS ARG PHE LYS VAL          
SEQRES   5 A  228  ARG VAL GLY ASP ARG ASN THR GLU GLN GLU GLU GLY GLY          
SEQRES   6 A  228  GLU ALA VAL HIS GLU VAL GLU VAL VAL ILE LYS HIS ASN          
SEQRES   7 A  228  ARG PHE THR LYS GLU THR TYR ASP PHE ASP ILE ALA VAL          
SEQRES   8 A  228  LEU ARG LEU LYS THR PRO ILE THR PHE ARG MET ASN VAL          
SEQRES   9 A  228  ALA PRO ALA SER LEU PRO THR ALA PRO PRO ALA THR GLY          
SEQRES  10 A  228  THR LYS CYS LEU ILE SER GLY TRP GLY ASN THR ALA SER          
SEQRES  11 A  228  SER GLY ALA ASP TYR PRO ASP GLU LEU GLN CYS LEU ASP          
SEQRES  12 A  228  ALA PRO VAL LEU SER GLN ALA LYS CYS GLU ALA SER TYR          
SEQRES  13 A  228  PRO GLY LYS ILE THR SER ASN MET PHE CYS VAL GLY PHE          
SEQRES  14 A  228  LEU GLU GLY GLY LYS ASP SER CYS GLN GLY ASP SER GLY          
SEQRES  15 A  228  GLY PRO VAL VAL CYS ASN GLY GLN LEU GLN GLY VAL VAL          
SEQRES  16 A  228  SER TRP GLY ASP GLY CYS ALA GLN LYS ASN LYS PRO GLY          
SEQRES  17 A  228  VAL TYR THR LYS VAL TYR ASN TYR VAL LYS TRP ILE LYS          
SEQRES  18 A  228  ASN THR ILE ALA ALA ASN SER                                  
HET    0G6  A   1      30                                                       
HETNAM     0G6 D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)                      
HETNAM   2 0G6  METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-                  
HETNAM   3 0G6  PROLINAMIDE                                                     
HETSYN     0G6 PPACK                                                            
FORMUL   2  0G6    C21 H34 CL N6 O3 1+                                          
FORMUL   3  HOH   *82(H2 O)                                                     
HELIX    1   1 ALA A   56  CYS A   58  5                                   3    
HELIX    2   2 GLN A  165  SER A  171  1                                   7    
HELIX    3   3 VAL A  231  ALA A  244  5                                  14    
SHEET    1   A 4 GLU A  80  GLU A  84  0                                        
SHEET    2   A 4 LYS A  65  GLY A  69 -1  N  VAL A  68   O  ALA A  81           
SHEET    3   A 4 GLN A  30  ILE A  34 -1  N  ILE A  34   O  LYS A  65           
SHEET    4   A 4 GLY A  40  THR A  45 -1  N  GLY A  44   O  ALA A  31           
SHEET    1   B 3 TYR A  51  THR A  54  0                                        
SHEET    2   B 3 ALA A 104  LEU A 108 -1  N  LEU A 106   O  ILE A  52           
SHEET    3   B 3 VAL A  85  LYS A  90 -1  N  ILE A  89   O  VAL A 105           
SHEET    1   C 6 GLN A 156  PRO A 161  0                                        
SHEET    2   C 6 LYS A 135  GLY A 140 -1  N  GLY A 140   O  GLN A 156           
SHEET    3   C 6 PRO A 198  CYS A 201 -1  N  VAL A 200   O  LEU A 137           
SHEET    4   C 6 GLN A 204  TRP A 215 -1  N  GLY A 211   O  VAL A 199           
SHEET    5   C 6 GLY A 226  LYS A 230 -1  N  THR A 229   O  VAL A 212           
SHEET    6   C 6 MET A 180  VAL A 183 -1  N  VAL A 183   O  GLY A 226           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.02  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.03  
LINK         OG  SER A 195                 C2  0G6 A   1     1555   1555  1.41  
LINK         NE2 HIS A  57                 C3  0G6 A   1     1555   1555  1.50  
SITE     1 AC1 22 HIS A  57  GLN A  61  GLN A  75  GLU A  76                    
SITE     2 AC1 22 TYR A  99  MET A 116  ASN A 117  LYS A 175                    
SITE     3 AC1 22 ASP A 189  SER A 190  CYS A 191  GLN A 192                    
SITE     4 AC1 22 GLY A 193  SER A 195  SER A 214  TRP A 215                    
SITE     5 AC1 22 GLY A 216  GLY A 219  GLY A 226  HOH A 247                    
SITE     6 AC1 22 HOH A 273  HOH A 327                                          
CRYST1   65.510   48.920   75.540  90.00 111.46  90.00 C 1 2 1       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      0.015265  0.000000  0.006001        0.00000                         
SCALE2      0.000000  0.020442  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014224        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system