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Database: PDB
Entry: 4ISL
LinkDB: 4ISL
Original site: 4ISL 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           16-JAN-13   4ISL              
TITLE     CRYSTAL STRUCTURE OF THE INACTIVE MATRIPTASE IN COMPLEX WITH ITS      
TITLE    2 INHIBITOR HAI-1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KUNITZ-TYPE PROTEASE INHIBITOR 1;                          
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: KUNITZ DOMAIN I (UNP RESIDUES 245-304);                    
COMPND   5 SYNONYM: HEPATOCYTE GROWTH FACTOR ACTIVATOR INHIBITOR TYPE 1, HAI-1; 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SUPPRESSOR OF TUMORIGENICITY 14 PROTEIN;                   
COMPND   9 CHAIN: A;                                                            
COMPND  10 FRAGMENT: SERINE PROTEASE DOMAIN (UNP RESIDUES 615-855);             
COMPND  11 SYNONYM: MATRIPTASE, MEMBRANE-TYPE SERINE PROTEASE 1, MT-SP1,        
COMPND  12 PROSTAMIN, SERINE PROTEASE 14, SERINE PROTEASE TADG-15, TUMOR-       
COMPND  13 ASSOCIATED DIFFERENTIALLY-EXPRESSED GENE 15 PROTEIN;                 
COMPND  14 EC: 3.4.21.109;                                                      
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 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: HAI1, SPINT1, UNQ223/PRO256;                                   
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: S2;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMT/BIP/V5-HIS-A;                         
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: PRSS14, SNC19, ST14, TADG15;                                   
SOURCE  16 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE  17 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;                           
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: X-33;                                      
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA                               
KEYWDS    BETA BARREL, SERINE PROTEASE INHIBITOR, EPITHELIUM, HYDROLASE-        
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.D.HUANG,B.Y.ZHAO,C.YUAN,R.LI                                        
REVDAT   3   15-NOV-17 4ISL    1       REMARK                                   
REVDAT   2   15-MAY-13 4ISL    1       JRNL                                     
REVDAT   1   06-MAR-13 4ISL    0                                                
JRNL        AUTH   B.ZHAO,C.YUAN,R.LI,D.QU,M.HUANG,J.C.NGO                      
JRNL        TITL   CRYSTAL STRUCTURES OF MATRIPTASE IN COMPLEX WITH ITS         
JRNL        TITL 2 INHIBITOR HEPATOCYTE GROWTH FACTOR ACTIVATOR INHIBITOR-1.    
JRNL        REF    J.BIOL.CHEM.                  V. 288 11155 2013              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   23443661                                                     
JRNL        DOI    10.1074/JBC.M113.454611                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 16250                          
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) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 823                             
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) : 2.29                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.35                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1056                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 52                           
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2347                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 172                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.61000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.314         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.224         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.534         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2512 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3395 ; 1.080 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   303 ; 5.425 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   120 ;33.330 ;23.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   379 ;15.662 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;15.473 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   345 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1946 ; 0.004 ; 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):  1509 ; 0.389 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2414 ; 0.788 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1003 ; 1.203 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   981 ; 2.061 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4ISL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000077156.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29858                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14900                            
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: 3P8G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 20% (W/V) POLYETHYLENE   
REMARK 280  GLYCOL 8000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  295K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       89.49850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       30.96700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       30.96700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      134.24775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       30.96700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       30.96700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       44.74925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       30.96700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       30.96700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      134.24775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       30.96700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       30.96700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       44.74925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       89.49850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 483  LIES ON A SPECIAL POSITION.                          
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    HIS A 143   NE2   HIS A 143   CD2    -0.094                       
REMARK 500    ALA A 221   C     ALA A 221   O      -0.119                       
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    ARG A  60C      42.81     39.72                                   
REMARK 500    SER A 214      -77.00   -124.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 305                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IS5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ISN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ISO   RELATED DB: PDB                                   
DBREF  4ISL B  245   304  UNP    O43278   SPIT1_HUMAN    245    304             
DBREF  4ISL A   16   244  UNP    Q9Y5Y6   ST14_HUMAN     615    855             
SEQADV 4ISL GLN A  164  UNP  Q9Y5Y6    ASN   772 ENGINEERED MUTATION            
SEQADV 4ISL ALA A  195  UNP  Q9Y5Y6    SER   805 ENGINEERED MUTATION            
SEQRES   1 B   60  GLN THR GLU ASP TYR CYS LEU ALA SER ASN LYS VAL GLY          
SEQRES   2 B   60  ARG CYS ARG GLY SER PHE PRO ARG TRP TYR TYR ASP PRO          
SEQRES   3 B   60  THR GLU GLN ILE CYS LYS SER PHE VAL TYR GLY GLY CYS          
SEQRES   4 B   60  LEU GLY ASN LYS ASN ASN TYR LEU ARG GLU GLU GLU CYS          
SEQRES   5 B   60  ILE LEU ALA CYS ARG GLY VAL GLN                              
SEQRES   1 A  241  VAL VAL GLY GLY THR ASP ALA ASP GLU GLY GLU TRP PRO          
SEQRES   2 A  241  TRP GLN VAL SER LEU HIS ALA LEU GLY GLN GLY HIS ILE          
SEQRES   3 A  241  CYS GLY ALA SER LEU ILE SER PRO ASN TRP LEU VAL SER          
SEQRES   4 A  241  ALA ALA HIS CYS TYR ILE ASP ASP ARG GLY PHE ARG TYR          
SEQRES   5 A  241  SER ASP PRO THR GLN TRP THR ALA PHE LEU GLY LEU HIS          
SEQRES   6 A  241  ASP GLN SER GLN ARG SER ALA PRO GLY VAL GLN GLU ARG          
SEQRES   7 A  241  ARG LEU LYS ARG ILE ILE SER HIS PRO PHE PHE ASN ASP          
SEQRES   8 A  241  PHE THR PHE ASP TYR ASP ILE ALA LEU LEU GLU LEU GLU          
SEQRES   9 A  241  LYS PRO ALA GLU TYR SER SER MET VAL ARG PRO ILE CYS          
SEQRES  10 A  241  LEU PRO ASP ALA SER HIS VAL PHE PRO ALA GLY LYS ALA          
SEQRES  11 A  241  ILE TRP VAL THR GLY TRP GLY HIS THR GLN TYR GLY GLY          
SEQRES  12 A  241  THR GLY ALA LEU ILE LEU GLN LYS GLY GLU ILE ARG VAL          
SEQRES  13 A  241  ILE GLN GLN THR THR CYS GLU ASN LEU LEU PRO GLN GLN          
SEQRES  14 A  241  ILE THR PRO ARG MET MET CYS VAL GLY PHE LEU SER GLY          
SEQRES  15 A  241  GLY VAL ASP SER CYS GLN GLY ASP ALA GLY GLY PRO LEU          
SEQRES  16 A  241  SER SER VAL GLU ALA ASP GLY ARG ILE PHE GLN ALA GLY          
SEQRES  17 A  241  VAL VAL SER TRP GLY ASP GLY CYS ALA GLN ARG ASN LYS          
SEQRES  18 A  241  PRO GLY VAL TYR THR ARG LEU PRO LEU PHE ARG ASP TRP          
SEQRES  19 A  241  ILE LYS GLU ASN THR GLY VAL                                  
HET    PG4  B 401      13                                                       
HET    GOL  A 301       6                                                       
HET    GOL  A 302       6                                                       
HET    PGE  A 303      10                                                       
HET    GOL  A 304       6                                                       
HET    GSH  A 305      20                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     GOL GLYCEROL                                                         
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     GSH GLUTATHIONE                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  PG4    C8 H18 O5                                                    
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   6  PGE    C6 H14 O4                                                    
FORMUL   8  GSH    C10 H17 N3 O6 S                                              
FORMUL   9  HOH   *172(H2 O)                                                    
HELIX    1   1 GLN B  245  ALA B  252  1                                   8    
HELIX    2   2 ARG B  292  ARG B  301  1                                  10    
HELIX    3   3 ALA A   55  TYR A   59  5                                   5    
HELIX    4   4 ASP A   60I THR A   62  5                                   3    
HELIX    5   5 GLN A  164  LEU A  172  1                                   9    
HELIX    6   6 PHE A  234  GLY A  243  1                                  10    
SHEET    1   A 2 PHE B 263  ASP B 269  0                                        
SHEET    2   A 2 ILE B 274  TYR B 280 -1  O  PHE B 278   N  ARG B 265           
SHEET    1   B 8 THR A  20  ASP A  21  0                                        
SHEET    2   B 8 GLN A 156  VAL A 162 -1  O  LYS A 157   N  THR A  20           
SHEET    3   B 8 MET A 180  GLY A 184 -1  O  GLY A 184   N  ARG A 161           
SHEET    4   B 8 GLY A 226  ARG A 230 -1  O  TYR A 228   N  MET A 181           
SHEET    5   B 8 ILE A 207  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    6   B 8 PRO A 198  VAL A 202 -1  N  SER A 201   O  PHE A 208           
SHEET    7   B 8 ALA A 135  GLY A 140 -1  N  TRP A 137   O  SER A 200           
SHEET    8   B 8 GLN A 156  VAL A 162 -1  O  ILE A 160   N  ILE A 136           
SHEET    1   C 7 GLN A  30  ALA A  35  0                                        
SHEET    2   C 7 GLY A  39  LEU A  46 -1  O  ILE A  41   N  LEU A  33           
SHEET    3   C 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   C 7 ALA A 104  LEU A 108 -1  O  ALA A 104   N  SER A  54           
SHEET    5   C 7 GLN A  81  SER A  90 -1  N  LYS A  86   O  GLU A 107           
SHEET    6   C 7 TRP A  64  LEU A  68 -1  N  ALA A  66   O  ARG A  83           
SHEET    7   C 7 GLN A  30  ALA A  35 -1  N  HIS A  34   O  THR A  65           
SSBOND   1 CYS B  250    CYS B  300                          1555   1555  2.03  
SSBOND   2 CYS B  259    CYS B  283                          1555   1555  2.04  
SSBOND   3 CYS B  275    CYS B  296                          1555   1555  2.07  
SSBOND   4 CYS A   42    CYS A   58                          1555   1555  2.02  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.02  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.06  
SITE     1 AC1  5 LEU A  36  GLY A  37  LEU B 291  ARG B 292                    
SITE     2 AC1  5 HOH B 531                                                     
SITE     1 AC2  9 PHE A 130  VAL A 162  ILE A 163  GLN A 164                    
SITE     2 AC2  9 GLN A 165  MET A 181  ARG A 230  GLU B 272                    
SITE     3 AC2  9 HOH B 527                                                     
SITE     1 AC3  9 HIS A  57  CYS A  58  TYR A  59  ILE A  60                    
SITE     2 AC3  9 ASP A  60B PHE B 263  ARG B 265  TYR B 280                    
SITE     3 AC3  9 GLY B 282                                                     
SITE     1 AC4  4 GLN A 145  SER A 186  GLY A 187  ALA A 221                    
SITE     1 AC5  4 GLU A  26  TRP A 137  LYS A 157  HOH A 469                    
SITE     1 AC6  7 TRP A  29  ARG A 119  PRO A 120  ILE A 121                    
SITE     2 AC6  7 CYS A 122  ARG A 206  ILE A 207                               
CRYST1   61.934   61.934  178.997  90.00  90.00  90.00 P 43 21 2     8          
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      0.016146  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016146  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005587        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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