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Database: PDB
Entry: 3EOX
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Original site: 3EOX 
HEADER    BLOOD CLOTTING                          29-SEP-08   3EOX              
TITLE     HIGH QUALITY STRUCTURE OF CLEAVED PAI-1-STAB                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLASMINOGEN ACTIVATOR INHIBITOR 1;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PAI-1;                                                     
COMPND   5 SYNONYM: PAI-1, PAI, ENDOTHELIAL PLASMINOGEN ACTIVATOR INHIBITOR;    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SERPINE1, PAI1, PLANH1;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: MC1061;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PIGE20                                    
KEYWDS    CLEAVED PLASMINOGEN ACTIVATOR INHIBITOR-1, PAI-1, SERPIN, STABILIZED, 
KEYWDS   2 GLYCOPROTEIN, PLASMINOGEN ACTIVATION, PROTEASE INHIBITOR, SECRETED,  
KEYWDS   3 SERINE PROTEASE INHIBITOR, BLOOD CLOTTING                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DEWILDE,P.J.DECLERCK,A.RABIJNS,S.V.STRELKOV                         
REVDAT   5   01-NOV-23 3EOX    1       REMARK                                   
REVDAT   4   10-NOV-21 3EOX    1       REMARK SEQADV                            
REVDAT   3   25-OCT-17 3EOX    1       REMARK                                   
REVDAT   2   13-JUL-11 3EOX    1       VERSN                                    
REVDAT   1   17-FEB-09 3EOX    0                                                
JRNL        AUTH   M.DEWILDE,S.V.STRELKOV,A.RABIJNS,P.J.DECLERCK                
JRNL        TITL   HIGH QUALITY STRUCTURE OF CLEAVED PAI-1-STAB.                
JRNL        REF    J.STRUCT.BIOL.                V. 165   126 2009              
JRNL        REFN                   ISSN 1047-8477                               
JRNL        PMID   19059484                                                     
JRNL        DOI    10.1016/J.JSB.2008.11.001                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12280                          
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 + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 603                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 806                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 50                           
REMARK   3   BIN FREE R VALUE                    : 0.3280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2942                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 123                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 5.98                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : 0.16000                                              
REMARK   3    B33 (A**2) : -0.24000                                             
REMARK   3    B12 (A**2) : 0.08000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.354         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.253         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.519        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3030 ; 0.004 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4116 ; 0.792 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   371 ; 4.691 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   137 ;32.363 ;23.796       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   513 ;13.987 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;12.413 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   466 ; 0.055 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2289 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1855 ; 0.181 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3020 ; 0.359 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1175 ; 0.544 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1094 ; 0.977 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   379                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0940 -27.4390  22.0820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0785 T22:   0.1030                                     
REMARK   3      T33:   0.1875 T12:  -0.0038                                     
REMARK   3      T13:   0.0146 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5702 L22:   1.8915                                     
REMARK   3      L33:   1.2076 L12:  -0.2298                                     
REMARK   3      L13:  -0.0363 L23:  -0.6317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0373 S12:   0.0434 S13:   0.1167                       
REMARK   3      S21:  -0.0131 S22:  -0.0130 S23:   0.0056                       
REMARK   3      S31:  -0.0621 S32:  -0.0163 S33:  -0.0243                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3EOX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-OCT-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049592.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8084                             
REMARK 200  MONOCHROMATOR                  : SI 111 HORIZONTALLY FOCUSSING      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12280                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.730                             
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 9PAI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M LITHIUM SULPHATE MONOHYDRATE, 15%   
REMARK 280  PEG 8000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -Y,-X,-Z+2/3                                            
REMARK 290       5555   -X+Y,Y,-Z+1/3                                           
REMARK 290       6555   X,X-Y,-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 -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       47.22133            
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       94.44267            
REMARK 290   SMTRY1   4  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000       94.44267            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       47.22133            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  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 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   118                                                      
REMARK 465     SER A   119                                                      
REMARK 465     SER A   344                                                      
REMARK 465     ALA A   345                                                      
REMARK 465     ARG A   346                                                      
REMARK 465     MET A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     PRO A   349                                                      
REMARK 465     GLU A   350                                                      
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     GLN A   56   CA   CB   CG   CD   OE1  NE2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A  56   N     GLN A  56   CA      0.158                       
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    SER A  27       61.64   -117.75                                   
REMARK 500    LYS A  88      -52.79     63.56                                   
REMARK 500    ASN A 172      113.14   -170.04                                   
REMARK 500    PHE A 302      -35.99     72.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DB2   RELATED DB: PDB                                   
REMARK 900 STABILIZED, INTACT, ACTIVE CONFORMATION OF PAI-1                     
REMARK 900 RELATED ID: 9PAI   RELATED DB: PDB                                   
REMARK 900 CLEAVED SUBSTRATE VARIANT OF PAI-1                                   
DBREF  3EOX A    1   379  UNP    P05121   PAI1_HUMAN      24    402             
SEQADV 3EOX HIS A  150  UNP  P05121    ASN   173 ENGINEERED MUTATION            
SEQADV 3EOX THR A  154  UNP  P05121    LYS   177 ENGINEERED MUTATION            
SEQADV 3EOX PRO A  301  UNP  P05121    GLN   324 ENGINEERED MUTATION            
SEQADV 3EOX LEU A  319  UNP  P05121    GLN   342 ENGINEERED MUTATION            
SEQADV 3EOX ILE A  354  UNP  P05121    MET   377 ENGINEERED MUTATION            
SEQRES   1 A  379  VAL HIS HIS PRO PRO SER TYR VAL ALA HIS LEU ALA SER          
SEQRES   2 A  379  ASP PHE GLY VAL ARG VAL PHE GLN GLN VAL ALA GLN ALA          
SEQRES   3 A  379  SER LYS ASP ARG ASN VAL VAL PHE SER PRO TYR GLY VAL          
SEQRES   4 A  379  ALA SER VAL LEU ALA MET LEU GLN LEU THR THR GLY GLY          
SEQRES   5 A  379  GLU THR GLN GLN GLN ILE GLN ALA ALA MET GLY PHE LYS          
SEQRES   6 A  379  ILE ASP ASP LYS GLY MET ALA PRO ALA LEU ARG HIS LEU          
SEQRES   7 A  379  TYR LYS GLU LEU MET GLY PRO TRP ASN LYS ASP GLU ILE          
SEQRES   8 A  379  SER THR THR ASP ALA ILE PHE VAL GLN ARG ASP LEU LYS          
SEQRES   9 A  379  LEU VAL GLN GLY PHE MET PRO HIS PHE PHE ARG LEU PHE          
SEQRES  10 A  379  ARG SER THR VAL LYS GLN VAL ASP PHE SER GLU VAL GLU          
SEQRES  11 A  379  ARG ALA ARG PHE ILE ILE ASN ASP TRP VAL LYS THR HIS          
SEQRES  12 A  379  THR LYS GLY MET ILE SER HIS LEU LEU GLY THR GLY ALA          
SEQRES  13 A  379  VAL ASP GLN LEU THR ARG LEU VAL LEU VAL ASN ALA LEU          
SEQRES  14 A  379  TYR PHE ASN GLY GLN TRP LYS THR PRO PHE PRO ASP SER          
SEQRES  15 A  379  SER THR HIS ARG ARG LEU PHE HIS LYS SER ASP GLY SER          
SEQRES  16 A  379  THR VAL SER VAL PRO MET MET ALA GLN THR ASN LYS PHE          
SEQRES  17 A  379  ASN TYR THR GLU PHE THR THR PRO ASP GLY HIS TYR TYR          
SEQRES  18 A  379  ASP ILE LEU GLU LEU PRO TYR HIS GLY ASP THR LEU SER          
SEQRES  19 A  379  MET PHE ILE ALA ALA PRO TYR GLU LYS GLU VAL PRO LEU          
SEQRES  20 A  379  SER ALA LEU THR ASN ILE LEU SER ALA GLN LEU ILE SER          
SEQRES  21 A  379  HIS TRP LYS GLY ASN MET THR ARG LEU PRO ARG LEU LEU          
SEQRES  22 A  379  VAL LEU PRO LYS PHE SER LEU GLU THR GLU VAL ASP LEU          
SEQRES  23 A  379  ARG LYS PRO LEU GLU ASN LEU GLY MET THR ASP MET PHE          
SEQRES  24 A  379  ARG PRO PHE GLN ALA ASP PHE THR SER LEU SER ASP GLN          
SEQRES  25 A  379  GLU PRO LEU HIS VAL ALA LEU ALA LEU GLN LYS VAL LYS          
SEQRES  26 A  379  ILE GLU VAL ASN GLU SER GLY THR VAL ALA SER SER SER          
SEQRES  27 A  379  THR ALA VAL ILE VAL SER ALA ARG MET ALA PRO GLU GLU          
SEQRES  28 A  379  ILE ILE ILE ASP ARG PRO PHE LEU PHE VAL VAL ARG HIS          
SEQRES  29 A  379  ASN PRO THR GLY THR VAL LEU PHE MET GLY GLN VAL MET          
SEQRES  30 A  379  GLU PRO                                                      
FORMUL   2  HOH   *123(H2 O)                                                    
HELIX    1   1 HIS A    2  SER A   27  1                                  26    
HELIX    2   2 SER A   35  THR A   50  1                                  16    
HELIX    3   3 GLY A   51  GLY A   63  1                                  13    
HELIX    4   4 GLY A   70  GLY A   84  1                                  15    
HELIX    5   5 PRO A   85  LYS A   88  5                                   4    
HELIX    6   6 GLY A  108  ARG A  115  1                                   8    
HELIX    7   7 GLU A  128  HIS A  143  1                                  16    
HELIX    8   8 PRO A  180  THR A  184  5                                   5    
HELIX    9   9 LEU A  247  ASN A  252  1                                   6    
HELIX   10  10 SER A  255  ASN A  265  1                                  11    
HELIX   11  11 LEU A  286  LEU A  293  1                                   8    
HELIX   12  12 THR A  296  ARG A  300  5                                   5    
SHEET    1   A 7 VAL A  32  PHE A  34  0                                        
SHEET    2   A 7 THR A 369  VAL A 376 -1  O  MET A 373   N  PHE A  34           
SHEET    3   A 7 PHE A 358  HIS A 364 -1  N  VAL A 362   O  PHE A 372           
SHEET    4   A 7 LEU A 233  PRO A 240 -1  N  PHE A 236   O  VAL A 361           
SHEET    5   A 7 TYR A 220  PRO A 227 -1  N  ASP A 222   O  ALA A 239           
SHEET    6   A 7 THR A 196  THR A 214 -1  N  PHE A 213   O  TYR A 221           
SHEET    7   A 7 HIS A 185  HIS A 190 -1  N  PHE A 189   O  VAL A 197           
SHEET    1   B 8 VAL A  32  PHE A  34  0                                        
SHEET    2   B 8 THR A 369  VAL A 376 -1  O  MET A 373   N  PHE A  34           
SHEET    3   B 8 PHE A 358  HIS A 364 -1  N  VAL A 362   O  PHE A 372           
SHEET    4   B 8 LEU A 233  PRO A 240 -1  N  PHE A 236   O  VAL A 361           
SHEET    5   B 8 TYR A 220  PRO A 227 -1  N  ASP A 222   O  ALA A 239           
SHEET    6   B 8 THR A 196  THR A 214 -1  N  PHE A 213   O  TYR A 221           
SHEET    7   B 8 THR A 267  PRO A 276 -1  O  LEU A 275   N  MET A 202           
SHEET    8   B 8 ILE A 352  ILE A 353  1  O  ILE A 352   N  LEU A 272           
SHEET    1   C 6 LYS A 122  VAL A 124  0                                        
SHEET    2   C 6 GLU A  90  GLN A 100  1  N  VAL A  99   O  VAL A 124           
SHEET    3   C 6 LEU A 163  GLN A 174 -1  O  ASN A 172   N  GLU A  90           
SHEET    4   C 6 GLY A 332  ILE A 342 -1  O  SER A 337   N  LEU A 169           
SHEET    5   C 6 LEU A 319  VAL A 328 -1  N  GLU A 327   O  VAL A 334           
SHEET    6   C 6 PHE A 278  ASP A 285 -1  N  PHE A 278   O  VAL A 328           
CISPEP   1 ASN A  172    GLY A  173          0         3.60                     
CRYST1   71.174   71.174  141.664  90.00  90.00 120.00 P 31 1 2      6          
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      0.014050  0.008112  0.000000        0.00000                         
SCALE2      0.000000  0.016224  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007059        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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