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Database: PDB
Entry: 4ISO
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Original site: 4ISO 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           16-JAN-13   4ISO              
TITLE     CRYSTAL STRUCTURE OF MATRIPTASE IN COMPLEX WITH ITS INHIBITOR HAI-1   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF TUMORIGENICITY 14 PROTEIN;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SERINE PROTEASE DOMAIN (UNP RESIDUES 615-855);             
COMPND   5 SYNONYM: MATRIPTASE, MEMBRANE-TYPE SERINE PROTEASE 1, MT-SP1,        
COMPND   6 PROSTAMIN, SERINE PROTEASE 14, SERINE PROTEASE TADG-15, TUMOR-       
COMPND   7 ASSOCIATED DIFFERENTIALLY-EXPRESSED GENE 15 PROTEIN;                 
COMPND   8 EC: 3.4.21.109;                                                      
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: KUNITZ-TYPE PROTEASE INHIBITOR 1;                          
COMPND  13 CHAIN: B;                                                            
COMPND  14 FRAGMENT: KUNITZ DOMAIN I (UNP RESISDUES 245-304);                   
COMPND  15 SYNONYM: HEPATOCYTE GROWTH FACTOR ACTIVATOR INHIBITOR TYPE 1, HAI-1; 
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRSS14, SNC19, ST14, TADG15;                                   
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: X-33;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAA;                              
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: HAI1, SPINT1, UNQ223/PRO256;                                   
SOURCE  17 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: S2;                                        
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PMT/BIP/V5-HIS-A                          
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   5   15-NOV-17 4ISO    1       REMARK                                   
REVDAT   4   29-OCT-14 4ISO    1       AUTHOR                                   
REVDAT   3   30-JUL-14 4ISO    1       REMARK                                   
REVDAT   2   15-MAY-13 4ISO    1       JRNL                                     
REVDAT   1   06-MAR-13 4ISO    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.    2.01 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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23138                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1194                            
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) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1598                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 94                           
REMARK   3   BIN FREE R VALUE                    : 0.2130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2348                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 182                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.70000                                              
REMARK   3    B22 (A**2) : 0.70000                                              
REMARK   3    B33 (A**2) : -1.40000                                             
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): 0.173         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.155         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.297         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2476 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3340 ; 1.414 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   297 ; 6.050 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;32.747 ;23.534       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   374 ;15.019 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.452 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   341 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1902 ; 0.007 ; 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):  1484 ; 0.789 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2375 ; 1.519 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   992 ; 2.442 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   965 ; 4.015 ; 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 4ISO 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_1000077159.                                   
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   : 42554                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
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     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28300                            
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   (%): 51.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
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       89.17750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       30.68600            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       30.68600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      133.76625            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       30.68600            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       30.68600            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       44.58875            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       30.68600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       30.68600            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      133.76625            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       30.68600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       30.68600            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       44.58875            
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       89.17750            
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: 4340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 459  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU B   247     O    HOH A   538     6555     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLY A 148   C     THR A 150   N       0.238                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A 148   O   -  C   -  N   ANGL. DEV. = -14.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 214      -69.53   -123.78                                   
REMARK 500    ASN B 289      105.86   -162.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 148         18.43                                           
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 GSH A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ISN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ISL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4IS5   RELATED DB: PDB                                   
DBREF  4ISO A   16   244  UNP    Q9Y5Y6   ST14_HUMAN     615    855             
DBREF  4ISO B  245   304  UNP    O43278   SPIT1_HUMAN    245    304             
SEQADV 4ISO GLN A  164  UNP  Q9Y5Y6    ASN   772 ENGINEERED MUTATION            
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 SER 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                                  
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                              
HET    GSH  A 301      20                                                       
HET    GOL  A 302       6                                                       
HET    GOL  A 303       6                                                       
HET    PEG  A 304       7                                                       
HET    PEG  A 305       7                                                       
HET    PGE  A 306      10                                                       
HET    PEG  B 401       7                                                       
HET    PEG  B 402       7                                                       
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GSH    C10 H17 N3 O6 S                                              
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6  PEG    4(C4 H10 O3)                                                 
FORMUL   8  PGE    C6 H14 O4                                                    
FORMUL  11  HOH   *182(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 ASP A   60I THR A   62  5                                   3    
HELIX    3   3 GLN A  164  LEU A  172  1                                   9    
HELIX    4   4 PHE A  234  GLY A  243  1                                  10    
HELIX    5   5 THR B  246  LEU B  251  1                                   6    
HELIX    6   6 ARG B  292  ARG B  301  1                                  10    
SHEET    1   A 8 THR A  20  ASP A  21  0                                        
SHEET    2   A 8 GLN A 156  VAL A 162 -1  O  LYS A 157   N  THR A  20           
SHEET    3   A 8 MET A 180  GLY A 184 -1  O  GLY A 184   N  ARG A 161           
SHEET    4   A 8 GLY A 226  ARG A 230 -1  O  TYR A 228   N  MET A 181           
SHEET    5   A 8 ILE A 207  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    6   A 8 PRO A 198  VAL A 202 -1  N  SER A 201   O  PHE A 208           
SHEET    7   A 8 ALA A 135  GLY A 140 -1  N  TRP A 137   O  SER A 200           
SHEET    8   A 8 GLN A 156  VAL A 162 -1  O  ILE A 160   N  ILE A 136           
SHEET    1   B 7 GLN A  30  ALA A  35  0                                        
SHEET    2   B 7 GLY A  39  LEU A  46 -1  O  ILE A  41   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 ALA A 104  LEU A 108 -1  O  ALA A 104   N  SER A  54           
SHEET    5   B 7 GLN A  81  SER A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    6   B 7 TRP A  64  LEU A  68 -1  N  ALA A  66   O  ARG A  83           
SHEET    7   B 7 GLN A  30  ALA A  35 -1  N  HIS A  34   O  THR A  65           
SHEET    1   C 2 PHE B 263  TYR B 268  0                                        
SHEET    2   C 2 CYS B 275  TYR B 280 -1  O  TYR B 280   N  PHE B 263           
SSBOND   1 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   2 CYS A  168    CYS A  182                          1555   1555  2.02  
SSBOND   3 CYS A  191    CYS A  220                          1555   1555  2.16  
SSBOND   4 CYS B  250    CYS B  300                          1555   1555  2.03  
SSBOND   5 CYS B  259    CYS B  283                          1555   1555  2.08  
SSBOND   6 CYS B  275    CYS B  296                          1555   1555  2.10  
SITE     1 AC1  9 TRP A  29  TYR A 114  ARG A 119  PRO A 120                    
SITE     2 AC1  9 CYS A 122  ARG A 206  ILE A 207  HOH A 462                    
SITE     3 AC1  9 HOH A 535                                                     
SITE     1 AC2 10 PHE A 130  VAL A 162  ILE A 163  GLN A 164                    
SITE     2 AC2 10 GLN A 165  MET A 181  ARG A 230  HOH A 447                    
SITE     3 AC2 10 GLU B 272  HOH B 531                                          
SITE     1 AC3 11 HIS A  57  CYS A  58  TYR A  59  ILE A  60                    
SITE     2 AC3 11 ASP A  60B TYR A  60G HOH A 472  PHE B 263                    
SITE     3 AC3 11 ARG B 265  TYR B 280  GLY B 282                               
SITE     1 AC4  4 LEU A  36  THR A  65  ARG A  84  HOH A 460                    
SITE     1 AC5 10 ASP A  23  GLU A  24  GLY A  25  GLU A  26                    
SITE     2 AC5 10 TRP A  27  PRO A  28  HIS A  71  MET A 117                    
SITE     3 AC5 10 LEU A 155  HOH A 465                                          
SITE     1 AC6  5 SER A 186  GLY A 187  ALA A 221  GLN A 221A                   
SITE     2 AC6  5 ARG A 222                                                     
SITE     1 AC7  4 LEU A  36  GLY A  37  LEU B 291  ARG B 292                    
SITE     1 AC8  2 GLY B 285  LYS B 287                                          
CRYST1   61.372   61.372  178.355  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      0.016294  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016294  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005607        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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