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Database: PDB
Entry: 1YC0
LinkDB: 1YC0
Original site: 1YC0 
HEADER    HYDROLASE/INHIBITOR                     21-DEC-04   1YC0              
TITLE     SHORT FORM HGFA WITH FIRST KUNITZ DOMAIN FROM HAI-1                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOCYTE GROWTH FACTOR ACTIVATOR;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 373-655;                        
COMPND   5 SYNONYM: HGF ACTIVATOR, HGFA;                                        
COMPND   6 EC: 3.4.21.-;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: KUNITZ-TYPE PROTEASE INHIBITOR 1;                          
COMPND  10 CHAIN: I;                                                            
COMPND  11 FRAGMENT: SEQUENCE DATABASE RESIDUES 245-303;                        
COMPND  12 SYNONYM: HEPATOCYTE GROWTH FACTOR ACTIVATOR INHIBITOR TYPE 1, HAI-1, 
COMPND  13 KUNITZ DOMAIN FROM HAI-1;                                            
COMPND  14 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: HGFAC;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: SPINT1, HAI1;                                                  
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: 58F3;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PKD1                                      
KEYWDS    HYDROLASE/INHIBITOR, HYDROLASE-INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHIA,J.STAMOS,D.KIRCHHOFER,B.FAN,J.WU,R.T.CORPUZ,L.SANTELL,         
AUTHOR   2 R.A.LAZARUS,C.EIGENBROT                                              
REVDAT   3   13-JUL-11 1YC0    1       VERSN                                    
REVDAT   2   24-FEB-09 1YC0    1       VERSN                                    
REVDAT   1   15-FEB-05 1YC0    0                                                
JRNL        AUTH   S.SHIA,J.STAMOS,D.KIRCHHOFER,B.FAN,J.WU,R.T.CORPUZ,          
JRNL        AUTH 2 L.SANTELL,R.A.LAZARUS,C.EIGENBROT                            
JRNL        TITL   CONFORMATIONAL LABILITY IN SERINE PROTEASE ACTIVE SITES:     
JRNL        TITL 2 STRUCTURES OF HEPATOCYTE GROWTH FACTOR ACTIVATOR (HGFA)      
JRNL        TITL 3 ALONE AND WITH THE INHIBITORY DOMAIN FROM HGFA INHIBITOR-1B. 
JRNL        REF    J.MOL.BIOL.                   V. 346  1335 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15713485                                                     
JRNL        DOI    10.1016/J.JMB.2004.12.048                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.07                                        
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 18983                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 966                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2566                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 142                          
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2429                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 119                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 55.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.40000                                              
REMARK   3    B22 (A**2) : 0.40000                                              
REMARK   3    B33 (A**2) : -0.61000                                             
REMARK   3    B12 (A**2) : 0.20000                                              
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): 0.296         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.218         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.143         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.764         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2511 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3409 ; 1.096 ; 1.939       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   310 ; 3.944 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   114 ;34.754 ;22.895       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   385 ;12.888 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;15.217 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   351 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1954 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1171 ; 0.228 ; 0.200       
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):   164 ; 0.123 ; 0.200       
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):    18 ; 0.141 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.110 ; 0.200       
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):  1551 ; 2.562 ; 2.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2485 ; 4.495 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   960 ; 3.050 ; 2.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   924 ; 4.766 ; 5.000       
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  : 3                                          
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 :   I   238        I   303                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6542  55.1084  57.4159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1936 T22:   0.0178                                     
REMARK   3      T33:   0.1118 T12:  -0.0201                                     
REMARK   3      T13:  -0.0061 T23:  -0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8421 L22:   0.9059                                     
REMARK   3      L33:   3.9927 L12:   0.0928                                     
REMARK   3      L13:  -0.3309 L23:  -0.3194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1435 S12:   0.0345 S13:  -0.0550                       
REMARK   3      S21:   0.1320 S22:  -0.1412 S23:   0.1242                       
REMARK   3      S31:   0.1331 S32:  -0.1698 S33:  -0.0023                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   408        A   646                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.7356  65.4459  33.0609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1643 T22:   0.0506                                     
REMARK   3      T33:   0.0851 T12:   0.0906                                     
REMARK   3      T13:  -0.0171 T23:  -0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6342 L22:   0.8179                                     
REMARK   3      L33:   0.5925 L12:  -0.2395                                     
REMARK   3      L13:  -0.0057 L23:   0.1552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0736 S12:   0.0190 S13:   0.0401                       
REMARK   3      S21:  -0.0661 S22:  -0.0655 S23:  -0.0301                       
REMARK   3      S31:   0.0243 S32:  -0.0140 S33:  -0.0081                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   393        A   400                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2631  66.8231  19.1141              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2073 T22:   0.4065                                     
REMARK   3      T33:   0.2392 T12:   0.1896                                     
REMARK   3      T13:   0.1234 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7787 L22:   4.8109                                     
REMARK   3      L33:  12.3328 L12:   5.1122                                     
REMARK   3      L13:   2.7993 L23:  -2.4074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1442 S12:   1.8066 S13:  -0.6428                       
REMARK   3      S21:  -0.1984 S22:  -0.1130 S23:  -1.7561                       
REMARK   3      S31:   0.2057 S32:   1.8333 S33:  -0.0312                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1YC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB031361.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-04                          
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               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17975                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07800                            
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1FAK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% MPD, PH 8.5, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 292K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.74533            
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      117.49067            
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        0.00000            
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      117.49067            
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       58.74533            
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: 1790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I                                  
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     VAL A   373                                                      
REMARK 465     GLN A   374                                                      
REMARK 465     LEU A   375                                                      
REMARK 465     SER A   376                                                      
REMARK 465     PRO A   377                                                      
REMARK 465     ASP A   378                                                      
REMARK 465     LEU A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     THR A   382                                                      
REMARK 465     LEU A   383                                                      
REMARK 465     PRO A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     PRO A   386                                                      
REMARK 465     ALA A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     GLY A   390                                                      
REMARK 465     ARG A   391                                                      
REMARK 465     GLN A   392                                                      
REMARK 465     ARG A   401                                                      
REMARK 465     THR A   402                                                      
REMARK 465     PHE A   403                                                      
REMARK 465     LEU A   404                                                      
REMARK 465     ARG A   405                                                      
REMARK 465     PRO A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     PRO A   647                                                      
REMARK 465     PRO A   648                                                      
REMARK 465     ARG A   649                                                      
REMARK 465     ARG A   650                                                      
REMARK 465     LEU A   651                                                      
REMARK 465     VAL A   652                                                      
REMARK 465     ALA A   653                                                      
REMARK 465     PRO A   654                                                      
REMARK 465     SER A   655                                                      
REMARK 465     MET I   229                                                      
REMARK 465     LYS I   230                                                      
REMARK 465     HIS I   231                                                      
REMARK 465     GLN I   232                                                      
REMARK 465     HIS I   233                                                      
REMARK 465     GLN I   234                                                      
REMARK 465     HIS I   235                                                      
REMARK 465     GLN I   236                                                      
REMARK 465     HIS I   237                                                      
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    HIS A 398      -18.69     73.31                                   
REMARK 500    HIS A 465      -50.12   -123.27                                   
REMARK 500    CYS A 510     -107.00   -106.91                                   
REMARK 500    VAL A 572     -105.74   -101.83                                   
REMARK 500    ASP A 588       62.76   -110.59                                   
REMARK 500    CYS A 589       80.25     24.29                                   
REMARK 500    LYS A 590     -119.82   -125.05                                   
REMARK 500    ASP A 592      167.77    179.24                                   
REMARK 500    SER A 617      -64.81   -127.89                                   
REMARK 500    HIS A 626       -2.13     71.90                                   
REMARK 500    ILE A 645       67.28   -106.74                                   
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 PO4 I 304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YBW   RELATED DB: PDB                                   
REMARK 900 SHORT FORM HGFA ALONE                                                
DBREF  1YC0 A  373   655  UNP    Q04756   HGFA_HUMAN     373    655             
DBREF  1YC0 I  245   303  UNP    O43278   SPIT1_HUMAN    245    303             
SEQADV 1YC0 MET I  229  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 LYS I  230  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 HIS I  231  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 GLN I  232  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 HIS I  233  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 GLN I  234  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 HIS I  235  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 GLN I  236  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 HIS I  237  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 GLN I  238  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 HIS I  239  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 GLN I  240  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 HIS I  241  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 GLN I  242  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 MET I  243  UNP  O43278              CLONING ARTIFACT               
SEQADV 1YC0 HIS I  244  UNP  O43278              CLONING ARTIFACT               
SEQRES   1 A  283  VAL GLN LEU SER PRO ASP LEU LEU ALA THR LEU PRO GLU          
SEQRES   2 A  283  PRO ALA SER PRO GLY ARG GLN ALA CYS GLY ARG ARG HIS          
SEQRES   3 A  283  LYS LYS ARG THR PHE LEU ARG PRO ARG ILE ILE GLY GLY          
SEQRES   4 A  283  SER SER SER LEU PRO GLY SER HIS PRO TRP LEU ALA ALA          
SEQRES   5 A  283  ILE TYR ILE GLY ASP SER PHE CYS ALA GLY SER LEU VAL          
SEQRES   6 A  283  HIS THR CYS TRP VAL VAL SER ALA ALA HIS CYS PHE SER          
SEQRES   7 A  283  HIS SER PRO PRO ARG ASP SER VAL SER VAL VAL LEU GLY          
SEQRES   8 A  283  GLN HIS PHE PHE ASN ARG THR THR ASP VAL THR GLN THR          
SEQRES   9 A  283  PHE GLY ILE GLU LYS TYR ILE PRO TYR THR LEU TYR SER          
SEQRES  10 A  283  VAL PHE ASN PRO SER ASP HIS ASP LEU VAL LEU ILE ARG          
SEQRES  11 A  283  LEU LYS LYS LYS GLY ASP ARG CYS ALA THR ARG SER GLN          
SEQRES  12 A  283  PHE VAL GLN PRO ILE CYS LEU PRO GLU PRO GLY SER THR          
SEQRES  13 A  283  PHE PRO ALA GLY HIS LYS CYS GLN ILE ALA GLY TRP GLY          
SEQRES  14 A  283  HIS LEU ASP GLU ASN VAL SER GLY TYR SER SER SER LEU          
SEQRES  15 A  283  ARG GLU ALA LEU VAL PRO LEU VAL ALA ASP HIS LYS CYS          
SEQRES  16 A  283  SER SER PRO GLU VAL TYR GLY ALA ASP ILE SER PRO ASN          
SEQRES  17 A  283  MET LEU CYS ALA GLY TYR PHE ASP CYS LYS SER ASP ALA          
SEQRES  18 A  283  CYS GLN GLY ASP SER GLY GLY PRO LEU ALA CYS GLU LYS          
SEQRES  19 A  283  ASN GLY VAL ALA TYR LEU TYR GLY ILE ILE SER TRP GLY          
SEQRES  20 A  283  ASP GLY CYS GLY ARG LEU HIS LYS PRO GLY VAL TYR THR          
SEQRES  21 A  283  ARG VAL ALA ASN TYR VAL ASP TRP ILE ASN ASP ARG ILE          
SEQRES  22 A  283  ARG PRO PRO ARG ARG LEU VAL ALA PRO SER                      
SEQRES   1 I   75  MET LYS HIS GLN HIS GLN HIS GLN HIS GLN HIS GLN HIS          
SEQRES   2 I   75  GLN MET HIS GLN THR GLU ASP TYR CYS LEU ALA SER ASN          
SEQRES   3 I   75  LYS VAL GLY ARG CYS ARG GLY SER PHE PRO ARG TRP TYR          
SEQRES   4 I   75  TYR ASP PRO THR GLU GLN ILE CYS LYS SER PHE VAL TYR          
SEQRES   5 I   75  GLY GLY CYS LEU GLY ASN LYS ASN ASN TYR LEU ARG GLU          
SEQRES   6 I   75  GLU GLU CYS ILE LEU ALA CYS ARG GLY VAL                      
HET    PO4  I 304       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  HOH   *119(H2 O)                                                    
HELIX    1   1 ALA A  445  SER A  450  5                                   6    
HELIX    2   2 PRO A  454  ASP A  456  5                                   3    
HELIX    3   3 ALA A  563  SER A  568  1                                   6    
HELIX    4   4 TYR A  573  ILE A  577  5                                   5    
HELIX    5   5 TYR A  637  ILE A  645  1                                   9    
HELIX    6   6 GLN I  240  LEU I  251  1                                  12    
HELIX    7   7 ARG I  292  CYS I  300  1                                   9    
SHEET    1   A 7 SER A 412  SER A 413  0                                        
SHEET    2   A 7 ARG A 555  PRO A 560 -1  O  GLU A 556   N  SER A 412           
SHEET    3   A 7 LYS A 534  GLY A 539 -1  N  CYS A 535   O  VAL A 559           
SHEET    4   A 7 PRO A 601  LYS A 606 -1  O  ALA A 603   N  GLN A 536           
SHEET    5   A 7 VAL A 609  TRP A 618 -1  O  GLY A 614   N  LEU A 602           
SHEET    6   A 7 GLY A 629  ARG A 633 -1  O  VAL A 630   N  TRP A 618           
SHEET    7   A 7 MET A 581  ALA A 584 -1  N  LEU A 582   O  TYR A 631           
SHEET    1   B 7 GLN A 475  PHE A 477  0                                        
SHEET    2   B 7 VAL A 458  LEU A 462 -1  N  LEU A 462   O  GLN A 475           
SHEET    3   B 7 LEU A 422  ILE A 427 -1  N  ALA A 424   O  VAL A 461           
SHEET    4   B 7 SER A 430  HIS A 438 -1  O  CYS A 432   N  ILE A 425           
SHEET    5   B 7 TRP A 441  SER A 444 -1  O  VAL A 443   N  SER A 435           
SHEET    6   B 7 VAL A 499  LEU A 503 -1  O  ILE A 501   N  VAL A 442           
SHEET    7   B 7 ILE A 479  PRO A 484 -1  N  ILE A 483   O  LEU A 500           
SHEET    1   C 2 PHE I 263  ASP I 269  0                                        
SHEET    2   C 2 ILE I 274  TYR I 280 -1  O  LYS I 276   N  TYR I 267           
SSBOND   1 CYS A  394    CYS A  521                          1555   1555  2.02  
SSBOND   2 CYS A  432    CYS A  448                          1555   1555  2.02  
SSBOND   3 CYS A  440    CYS A  510                          1555   1555  2.04  
SSBOND   4 CYS A  535    CYS A  604                          1555   1555  2.03  
SSBOND   5 CYS A  567    CYS A  583                          1555   1555  2.02  
SSBOND   6 CYS A  594    CYS A  622                          1555   1555  2.03  
SSBOND   7 CYS I  250    CYS I  300                          1555   1555  2.03  
SSBOND   8 CYS I  259    CYS I  283                          1555   1555  2.03  
SSBOND   9 CYS I  275    CYS I  296                          1555   1555  2.03  
SITE     1 AC1  4 HIS A 451  ARG I 265  TYR I 280  HOH I 327                    
CRYST1   76.218   76.218  176.236  90.00  90.00 120.00 P 31 2 1      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      0.013120  0.007575  0.000000        0.00000                         
SCALE2      0.000000  0.015150  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005674        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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