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Database: PDB
Entry: 2O8T
LinkDB: 2O8T
Original site: 2O8T 
HEADER    HYDROLASE                               12-DEC-06   2O8T              
TITLE     CRYSTAL STRUCTURE AND BINDING EPITOPES OF UROKINASE-TYPE              
TITLE    2 PLASMINOGEN ACTIVATOR (C122A/N145Q) IN COMPLEX WITH                  
TITLE    3 INHIBITORS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE PLASMINOGEN ACTIVATOR;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 16-250 (159-411);                                 
COMPND   5 SYNONYM: UPA;                                                        
COMPND   6 EC: 3.4.21.73;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: PICHIA PASTORIS;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: X-33;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: SELECTIVE;                                 
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA                               
KEYWDS    UROKINASE-TYPE PLASMINOGEN ACTIVATOR, BENZAMIDINE,                    
KEYWDS   2 PHENYLGUANIDINE, CONTACT AREA, HYDROLASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.ZHAO,C.YUAN,L.JIANG,Z.HUANG,M.HUANG                                 
REVDAT   2   24-FEB-09 2O8T    1       VERSN                                    
REVDAT   1   25-DEC-07 2O8T    0                                                
JRNL        AUTH   G.ZHAO,C.YUAN,L.JIANG,Z.HUANG,M.HUANG                        
JRNL        TITL   CRYSTAL STRUCTURE AND BINDING EPITOPES OF                    
JRNL        TITL 2 UROKINASE-TYPE PLASMINOGEN ACTIVATOR                         
JRNL        TITL 3 (C122A/N145Q/S195A) IN COMPLEX WITH INHIBITORS               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1510898.160                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 38545                          
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) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1364                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5800                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 97                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1825                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.73000                                             
REMARK   3    B22 (A**2) : -1.73000                                             
REMARK   3    B33 (A**2) : 3.46000                                              
REMARK   3    B12 (A**2) : -0.02000                                             
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) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
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) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.71                            
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        : 0.38                                                 
REMARK   3   BSOL        : 59.53                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
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  : PEG_PAR.TXT                                    
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   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2O8T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB040831.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.4                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER SMART 6000                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.06200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 18.900                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M SODIUM CITRATE (PH4.5)             
REMARK 280  BUFFER, 1.95M (NH4)2SO4, 0.05% NAN3, 5% PEG400, VAPOR               
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.45500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.90371            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       14.20333            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       60.45500            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.90371            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       14.20333            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       60.45500            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.90371            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       14.20333            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.80742            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       28.40667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.80742            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       28.40667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.80742            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       28.40667            
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 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     ARG A    36                                                      
REMARK 465     HIS A    37                                                      
REMARK 465     ARG A    37A                                                     
REMARK 465     GLY A    37B                                                     
REMARK 465     GLY A    37C                                                     
REMARK 465     SER A    37D                                                     
REMARK 465     ASP A    97                                                      
REMARK 465     THR A    97A                                                     
REMARK 465     LEU A    97B                                                     
REMARK 465     SER A   110                                                      
REMARK 465     LYS A   110A                                                     
REMARK 465     GLU A   110B                                                     
REMARK 465     GLY A   110C                                                     
REMARK 465     ARG A   110D                                                     
REMARK 465     LYS A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     ASN A   246                                                      
REMARK 465     GLY A   247                                                      
REMARK 465     LEU A   248                                                      
REMARK 465     ALA A   249                                                      
REMARK 465     LEU A   250                                                      
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    GLN A  27       63.55   -162.34                                   
REMARK 500    VAL A  41      -63.31   -108.35                                   
REMARK 500    SER A  54     -153.95   -148.25                                   
REMARK 500    TYR A 127       35.70     39.14                                   
REMARK 500    TYR A 171     -104.16    -93.76                                   
REMARK 500    LEU A 203       36.18    -74.99                                   
REMARK 500    GLN A 204       85.38     61.38                                   
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 A5104        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A5234        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A5253        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A5274        DISTANCE =  6.63 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 314                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 315                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 5084                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2O8U   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN(C122A/N145Q/S195A) IN COMPLEX WITH                  
REMARK 900 DIFFERENT INHIBITORS                                                 
REMARK 900 RELATED ID: 2O8W   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN(C122A/N145Q/S195A) IN COMPLEX WITH                  
REMARK 900 DIFFERENT INHIBITORS                                                 
DBREF  2O8T A   16   250  UNP    Q5PY49   Q5PY49_HUMAN   159    411             
SEQADV 2O8T ALA A  122  UNP  Q5PY49    CYS   279 ENGINEERED                     
SEQADV 2O8T GLN A  145  UNP  Q5PY49    ASN   302 ENGINEERED                     
SEQRES   1 A  253  ILE ILE GLY GLY GLU PHE THR THR ILE GLU ASN GLN PRO          
SEQRES   2 A  253  TRP PHE ALA ALA ILE TYR ARG ARG HIS ARG GLY GLY SER          
SEQRES   3 A  253  VAL THR TYR VAL CYS GLY GLY SER LEU ILE SER PRO CYS          
SEQRES   4 A  253  TRP VAL ILE SER ALA THR HIS CYS PHE ILE ASP TYR PRO          
SEQRES   5 A  253  LYS LYS GLU ASP TYR ILE VAL TYR LEU GLY ARG SER ARG          
SEQRES   6 A  253  LEU ASN SER ASN THR GLN GLY GLU MET LYS PHE GLU VAL          
SEQRES   7 A  253  GLU ASN LEU ILE LEU HIS LYS ASP TYR SER ALA ASP THR          
SEQRES   8 A  253  LEU ALA HIS HIS ASN ASP ILE ALA LEU LEU LYS ILE ARG          
SEQRES   9 A  253  SER LYS GLU GLY ARG CYS ALA GLN PRO SER ARG THR ILE          
SEQRES  10 A  253  GLN THR ILE ALA LEU PRO SER MET TYR ASN ASP PRO GLN          
SEQRES  11 A  253  PHE GLY THR SER CYS GLU ILE THR GLY PHE GLY LYS GLU          
SEQRES  12 A  253  GLN SER THR ASP TYR LEU TYR PRO GLU GLN LEU LYS MET          
SEQRES  13 A  253  THR VAL VAL LYS LEU ILE SER HIS ARG GLU CYS GLN GLN          
SEQRES  14 A  253  PRO HIS TYR TYR GLY SER GLU VAL THR THR LYS MET LEU          
SEQRES  15 A  253  CYS ALA ALA ASP PRO GLN TRP LYS THR ASP SER CYS GLN          
SEQRES  16 A  253  GLY ASP SER GLY GLY PRO LEU VAL CYS SER LEU GLN GLY          
SEQRES  17 A  253  ARG MET THR LEU THR GLY ILE VAL SER TRP GLY ARG GLY          
SEQRES  18 A  253  CYS ALA LEU LYS ASP LYS PRO GLY VAL TYR THR ARG VAL          
SEQRES  19 A  253  SER HIS PHE LEU PRO TRP ILE ARG SER HIS THR LYS GLU          
SEQRES  20 A  253  GLU ASN GLY LEU ALA LEU                                      
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    1PE  A 314      16                                                       
HET    1PE  A 315      16                                                       
HET    PEG  A5084       7                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     1PE PEG400                                                           
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  1PE    2(C10 H22 O6)                                                
FORMUL   6  PEG    C4 H10 O3                                                    
FORMUL   7  HOH   *220(H2 O)                                                    
HELIX    1   1 THR A   23  GLN A   27  5                                   5    
HELIX    2   2 ALA A   55  PHE A   59  5                                   5    
HELIX    3   3 LYS A   61  ASP A   63  5                                   4    
HELIX    4   4 SER A  164  GLN A  169  1                                   6    
HELIX    5   5 TYR A  172  VAL A  176  5                                   5    
HELIX    6   6 PHE A  234  THR A  242  1                                   9    
SHEET    1   A 8 GLU A  20  PHE A  21  0                                        
SHEET    2   A 8 LYS A 156  ILE A 163 -1  O  MET A 157   N  GLU A  20           
SHEET    3   A 8 MET A 180  ALA A 184 -1  O  CYS A 182   N  ILE A 163           
SHEET    4   A 8 GLY A 226  ARG A 230 -1  O  TYR A 228   N  LEU A 181           
SHEET    5   A 8 MET A 207  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    6   A 8 PRO A 198  SER A 202 -1  N  CYS A 201   O  THR A 208           
SHEET    7   A 8 SER A 135  GLY A 140 -1  N  GLU A 137   O  VAL A 200           
SHEET    8   A 8 LYS A 156  ILE A 163 -1  O  VAL A 160   N  CYS A 136           
SHEET    1   B 7 PHE A  30  TYR A  34  0                                        
SHEET    2   B 7 TYR A  40  SER A  48 -1  O  VAL A  41   N  ILE A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  ILE A  53   N  SER A  45           
SHEET    4   B 7 ALA A 104  ARG A 109 -1  O  LEU A 106   N  VAL A  52           
SHEET    5   B 7 MET A  81  LEU A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    6   B 7 ILE A  65  LEU A  68 -1  N  VAL A  66   O  PHE A  83           
SHEET    7   B 7 PHE A  30  TYR A  34 -1  N  TYR A  34   O  ILE A  65           
SSBOND   1 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   2 CYS A   50    CYS A  111                          1555   1555  2.03  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.04  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.05  
SITE     1 AC1  3 ILE A  47  LEU A 123  HOH A5100                               
SITE     1 AC2  9 HIS A  57  GLN A 192  GLY A 193  ASP A 194                    
SITE     2 AC2  9 SER A 195  HOH A5138  HOH A5182  HOH A5196                    
SITE     3 AC2  9 HOH A5280                                                     
SITE     1 AC3 11 ASN A  74  SER A 135  CYS A 136  GLU A 137                    
SITE     2 AC3 11 VAL A 159  SER A 202  GLN A 204  MET A 207                    
SITE     3 AC3 11 1PE A 315  HOH A5203  HOH A5284                               
SITE     1 AC4  5 VAL A  38  THR A  39  ASN A  74  1PE A 314                    
SITE     2 AC4  5 HOH A5143                                                     
SITE     1 AC5  4 GLY A 133  LEU A 162  ILE A 163  PRO A 185A                   
CRYST1  120.910  120.910   42.610  90.00  90.00 120.00 H 3           9          
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      0.008271  0.004775  0.000000        0.00000                         
SCALE2      0.000000  0.009550  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023469        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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