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Database: PDB
Entry: 2I9A
LinkDB: 2I9A
Original site: 2I9A 
HEADER    HYDROLASE                               05-SEP-06   2I9A              
TITLE     CRYSTAL STRUCTURE OF THE FREE AMINOTERMINAL FRAGMENT OF UROKINASE TYPE
TITLE    2 PLASMINOGEN ACTIVATOR (ATF)                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: N-TERMINAL FRAGMENT OF UROKINASE, RESIDUES 21-163;         
COMPND   5 EC: 3.4.21.73;                                                       
COMPND   6 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: PLAU;                                                          
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER'S S2 CELLS;                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMT/BIP/V5-HIS                            
KEYWDS    GROWTH FACTOR-LIKE DOMAIN, KRINGLE DOMAIN, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LUBKOWSKI,C.BARINKA                                                 
REVDAT   5   18-OCT-17 2I9A    1       REMARK                                   
REVDAT   4   13-JUL-11 2I9A    1       VERSN                                    
REVDAT   3   24-FEB-09 2I9A    1       VERSN                                    
REVDAT   2   05-DEC-06 2I9A    1       JRNL                                     
REVDAT   1   28-NOV-06 2I9A    0                                                
JRNL        AUTH   C.BARINKA,G.PARRY,J.CALLAHAN,D.E.SHAW,A.KUO,K.BDEIR,         
JRNL        AUTH 2 D.B.CINES,A.MAZAR,J.LUBKOWSKI                                
JRNL        TITL   STRUCTURAL BASIS OF INTERACTION BETWEEN UROKINASE-TYPE       
JRNL        TITL 2 PLASMINOGEN ACTIVATOR AND ITS RECEPTOR.                      
JRNL        REF    J.MOL.BIOL.                   V. 363   482 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16979660                                                     
JRNL        DOI    10.1016/J.JMB.2006.08.063                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 51775                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2757                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3223                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 159                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3897                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 361                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.40000                                             
REMARK   3    B12 (A**2) : 0.60000                                              
REMARK   3    B13 (A**2) : -0.75000                                             
REMARK   3    B23 (A**2) : -0.46000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.125         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.559         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4046 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5493 ; 1.489 ; 1.920       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   493 ; 6.336 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   198 ;32.287 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   633 ;13.186 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;16.955 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   542 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3152 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1690 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2759 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   297 ; 0.125 ; 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):    93 ; 0.220 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.143 ; 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):  2505 ; 0.945 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3939 ; 1.544 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1761 ; 2.534 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1554 ; 3.810 ; 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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    11        A   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8976 -21.5679  11.9219              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1135 T22:  -0.1121                                     
REMARK   3      T33:  -0.0457 T12:   0.0018                                     
REMARK   3      T13:  -0.0250 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0149 L22:   3.2058                                     
REMARK   3      L33:   1.9821 L12:  -0.0878                                     
REMARK   3      L13:  -0.2195 L23:   1.2002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0314 S12:   0.0719 S13:  -0.1471                       
REMARK   3      S21:  -0.2673 S22:  -0.0179 S23:   0.2845                       
REMARK   3      S31:  -0.0365 S32:  -0.0624 S33:   0.0492                       
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 :   B    11        B   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9236  14.5811 -12.5860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1393 T22:  -0.1044                                     
REMARK   3      T33:  -0.1084 T12:  -0.0249                                     
REMARK   3      T13:  -0.0042 T23:   0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3627 L22:   1.0650                                     
REMARK   3      L33:   3.6435 L12:  -0.2424                                     
REMARK   3      L13:  -0.7174 L23:   0.3892                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1526 S12:  -0.0321 S13:  -0.0370                       
REMARK   3      S21:   0.1065 S22:   0.0126 S23:  -0.0247                       
REMARK   3      S31:   0.1348 S32:   0.2299 S33:   0.1400                       
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 :   C    11        C   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8654 -41.7918  17.0832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1341 T22:  -0.0980                                     
REMARK   3      T33:  -0.1206 T12:  -0.0124                                     
REMARK   3      T13:   0.0143 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7118 L22:   2.8025                                     
REMARK   3      L33:   1.3353 L12:  -1.4365                                     
REMARK   3      L13:   0.4633 L23:  -0.6349                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0311 S12:  -0.0522 S13:   0.1207                       
REMARK   3      S21:   0.0468 S22:  -0.0288 S23:  -0.0907                       
REMARK   3      S31:  -0.0176 S32:   0.1201 S33:   0.0599                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    11        D   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8240   3.3816  27.0875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1334 T22:  -0.1502                                     
REMARK   3      T33:  -0.1215 T12:  -0.0181                                     
REMARK   3      T13:   0.0099 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9408 L22:   1.3173                                     
REMARK   3      L33:   1.9763 L12:  -0.6539                                     
REMARK   3      L13:   0.7095 L23:  -0.4773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0124 S12:   0.0069 S13:   0.0707                       
REMARK   3      S21:  -0.0441 S22:   0.0239 S23:  -0.0537                       
REMARK   3      S31:  -0.2062 S32:  -0.0532 S33:  -0.0363                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2I9A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000039298.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10.5                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.13539                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 225 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54650                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.6300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.22100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.580                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1URK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM DIHYDROGEN PHOSPHATE, 0.8   
REMARK 280  M POTASSIUM HYDROGEN PHOSPHATE, 200 MM LITHIUM SULFATE, 100 MM      
REMARK 280  CHES, PH 10.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER. THERE ARE 4 BIOLOGICAL     
REMARK 300 UNITS IN THE ASYMMETRIC UNIT.                                        
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     LYS A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     PRO A   137                                                      
REMARK 465     SER A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     GLU A   142                                                      
REMARK 465     GLU A   143                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     ASP B   133                                                      
REMARK 465     GLY B   134                                                      
REMARK 465     LYS B   135                                                      
REMARK 465     LYS B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     SER B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     PRO B   140                                                      
REMARK 465     PRO B   141                                                      
REMARK 465     GLU B   142                                                      
REMARK 465     GLU B   143                                                      
REMARK 465     ARG C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     VAL C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     ASN C    10                                                      
REMARK 465     GLY C   134                                                      
REMARK 465     LYS C   135                                                      
REMARK 465     LYS C   136                                                      
REMARK 465     PRO C   137                                                      
REMARK 465     SER C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     PRO C   140                                                      
REMARK 465     PRO C   141                                                      
REMARK 465     GLU C   142                                                      
REMARK 465     GLU C   143                                                      
REMARK 465     ARG D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     VAL D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     GLY D   134                                                      
REMARK 465     LYS D   135                                                      
REMARK 465     LYS D   136                                                      
REMARK 465     PRO D   137                                                      
REMARK 465     SER D   138                                                      
REMARK 465     SER D   139                                                      
REMARK 465     PRO D   140                                                      
REMARK 465     PRO D   141                                                      
REMARK 465     GLU D   142                                                      
REMARK 465     GLU D   143                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A  12    CG   OD1  OD2                                       
REMARK 470     LYS A  35    CD   CE   NZ                                        
REMARK 470     GLN A  93    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  40    CD   OE1  NE2                                       
REMARK 470     GLN B  93    CD   OE1  NE2                                       
REMARK 470     LYS C  35    CD   CE   NZ                                        
REMARK 470     GLN C  40    CG   CD   OE1  NE2                                  
REMARK 470     GLN C  93    CD   OE1  NE2                                       
REMARK 470     ASN D  27    CG   OD1  ND2                                       
REMARK 470     LYS D  35    CG   CD   CE   NZ                                   
REMARK 470     GLN D  93    CD   OE1  NE2                                       
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    ASP B  65   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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    CYS A  11     -131.71   -119.57                                   
REMARK 500    SER A  63       27.80   -150.51                                   
REMARK 500    VAL A 128      140.18    -38.53                                   
REMARK 500    CYS B  11     -131.48   -117.81                                   
REMARK 500    SER B  63       27.76   -147.61                                   
REMARK 500    ARG B 108     -178.75    -69.96                                   
REMARK 500    SER C  63       20.19   -149.41                                   
REMARK 500    ARG C 108     -171.10    -68.24                                   
REMARK 500    SER D  63       20.55   -147.38                                   
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 C 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 805                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2I9B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ATF-UROKINASE RECEPTOR COMPLEX                  
DBREF  2I9A A    1   143  UNP    P00749   UROK_HUMAN      21    163             
DBREF  2I9A B    1   143  UNP    P00749   UROK_HUMAN      21    163             
DBREF  2I9A C    1   143  UNP    P00749   UROK_HUMAN      21    163             
DBREF  2I9A D    1   143  UNP    P00749   UROK_HUMAN      21    163             
SEQADV 2I9A ARG A   -1  UNP  P00749              CLONING ARTIFACT               
SEQADV 2I9A SER A    0  UNP  P00749              CLONING ARTIFACT               
SEQADV 2I9A ARG B   -1  UNP  P00749              CLONING ARTIFACT               
SEQADV 2I9A SER B    0  UNP  P00749              CLONING ARTIFACT               
SEQADV 2I9A ARG C   -1  UNP  P00749              CLONING ARTIFACT               
SEQADV 2I9A SER C    0  UNP  P00749              CLONING ARTIFACT               
SEQADV 2I9A ARG D   -1  UNP  P00749              CLONING ARTIFACT               
SEQADV 2I9A SER D    0  UNP  P00749              CLONING ARTIFACT               
SEQRES   1 A  145  ARG SER SER ASN GLU LEU HIS GLN VAL PRO SER ASN CYS          
SEQRES   2 A  145  ASP CYS LEU ASN GLY GLY THR CYS VAL SER ASN LYS TYR          
SEQRES   3 A  145  PHE SER ASN ILE HIS TRP CYS ASN CYS PRO LYS LYS PHE          
SEQRES   4 A  145  GLY GLY GLN HIS CYS GLU ILE ASP LYS SER LYS THR CYS          
SEQRES   5 A  145  TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS ALA SER          
SEQRES   6 A  145  THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP ASN SER          
SEQRES   7 A  145  ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS ARG SER          
SEQRES   8 A  145  ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN TYR CYS          
SEQRES   9 A  145  ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS TYR VAL          
SEQRES  10 A  145  GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS MET VAL          
SEQRES  11 A  145  HIS ASP CYS ALA ASP GLY LYS LYS PRO SER SER PRO PRO          
SEQRES  12 A  145  GLU GLU                                                      
SEQRES   1 B  145  ARG SER SER ASN GLU LEU HIS GLN VAL PRO SER ASN CYS          
SEQRES   2 B  145  ASP CYS LEU ASN GLY GLY THR CYS VAL SER ASN LYS TYR          
SEQRES   3 B  145  PHE SER ASN ILE HIS TRP CYS ASN CYS PRO LYS LYS PHE          
SEQRES   4 B  145  GLY GLY GLN HIS CYS GLU ILE ASP LYS SER LYS THR CYS          
SEQRES   5 B  145  TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS ALA SER          
SEQRES   6 B  145  THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP ASN SER          
SEQRES   7 B  145  ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS ARG SER          
SEQRES   8 B  145  ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN TYR CYS          
SEQRES   9 B  145  ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS TYR VAL          
SEQRES  10 B  145  GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS MET VAL          
SEQRES  11 B  145  HIS ASP CYS ALA ASP GLY LYS LYS PRO SER SER PRO PRO          
SEQRES  12 B  145  GLU GLU                                                      
SEQRES   1 C  145  ARG SER SER ASN GLU LEU HIS GLN VAL PRO SER ASN CYS          
SEQRES   2 C  145  ASP CYS LEU ASN GLY GLY THR CYS VAL SER ASN LYS TYR          
SEQRES   3 C  145  PHE SER ASN ILE HIS TRP CYS ASN CYS PRO LYS LYS PHE          
SEQRES   4 C  145  GLY GLY GLN HIS CYS GLU ILE ASP LYS SER LYS THR CYS          
SEQRES   5 C  145  TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS ALA SER          
SEQRES   6 C  145  THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP ASN SER          
SEQRES   7 C  145  ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS ARG SER          
SEQRES   8 C  145  ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN TYR CYS          
SEQRES   9 C  145  ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS TYR VAL          
SEQRES  10 C  145  GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS MET VAL          
SEQRES  11 C  145  HIS ASP CYS ALA ASP GLY LYS LYS PRO SER SER PRO PRO          
SEQRES  12 C  145  GLU GLU                                                      
SEQRES   1 D  145  ARG SER SER ASN GLU LEU HIS GLN VAL PRO SER ASN CYS          
SEQRES   2 D  145  ASP CYS LEU ASN GLY GLY THR CYS VAL SER ASN LYS TYR          
SEQRES   3 D  145  PHE SER ASN ILE HIS TRP CYS ASN CYS PRO LYS LYS PHE          
SEQRES   4 D  145  GLY GLY GLN HIS CYS GLU ILE ASP LYS SER LYS THR CYS          
SEQRES   5 D  145  TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS ALA SER          
SEQRES   6 D  145  THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP ASN SER          
SEQRES   7 D  145  ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS ARG SER          
SEQRES   8 D  145  ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN TYR CYS          
SEQRES   9 D  145  ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS TYR VAL          
SEQRES  10 D  145  GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS MET VAL          
SEQRES  11 D  145  HIS ASP CYS ALA ASP GLY LYS LYS PRO SER SER PRO PRO          
SEQRES  12 D  145  GLU GLU                                                      
HET    PO4  C 802       5                                                       
HET    PO4  D 803       5                                                       
HET    PO4  D 804       5                                                       
HET    PO4  D 805       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   5  PO4    4(O4 P 3-)                                                   
FORMUL   9  HOH   *361(H2 O)                                                    
HELIX    1   1 THR A   78  GLN A   82  5                                   5    
HELIX    2   2 ASP A   90  GLY A   95  1                                   6    
HELIX    3   3 THR B   78  GLN B   82  5                                   5    
HELIX    4   4 ASP B   90  GLY B   95  1                                   6    
HELIX    5   5 THR C   78  GLN C   82  5                                   5    
HELIX    6   6 ASP C   90  GLY C   95  1                                   6    
HELIX    7   7 THR D   78  GLN D   82  5                                   5    
HELIX    8   8 ASP D   90  GLY D   95  1                                   6    
SHEET    1   A 2 THR A  18  SER A  21  0                                        
SHEET    2   A 2 HIS A  29  ASN A  32 -1  O  ASN A  32   N  THR A  18           
SHEET    1   B 2 PHE A  37  GLY A  38  0                                        
SHEET    2   B 2 ILE A  44  ASP A  45 -1  O  ILE A  44   N  GLY A  38           
SHEET    1   C 2 CYS A  50  TYR A  51  0                                        
SHEET    2   C 2 HIS A 129  ASP A 130  1  O  HIS A 129   N  TYR A  51           
SHEET    1   D 2 TRP A 112  VAL A 117  0                                        
SHEET    2   D 2 LYS A 120  GLU A 125 -1  O  LEU A 122   N  VAL A 115           
SHEET    1   E 2 THR B  18  SER B  21  0                                        
SHEET    2   E 2 HIS B  29  ASN B  32 -1  O  TRP B  30   N  VAL B  20           
SHEET    1   F 2 PHE B  37  GLY B  38  0                                        
SHEET    2   F 2 ILE B  44  ASP B  45 -1  O  ILE B  44   N  GLY B  38           
SHEET    1   G 2 CYS B  50  TYR B  51  0                                        
SHEET    2   G 2 HIS B 129  ASP B 130  1  O  HIS B 129   N  TYR B  51           
SHEET    1   H 2 TRP B 112  VAL B 117  0                                        
SHEET    2   H 2 LYS B 120  GLU B 125 -1  O  LYS B 120   N  VAL B 117           
SHEET    1   I 2 THR C  18  SER C  21  0                                        
SHEET    2   I 2 HIS C  29  ASN C  32 -1  O  ASN C  32   N  THR C  18           
SHEET    1   J 2 PHE C  37  GLY C  38  0                                        
SHEET    2   J 2 ILE C  44  ASP C  45 -1  O  ILE C  44   N  GLY C  38           
SHEET    1   K 2 TRP C 112  VAL C 117  0                                        
SHEET    2   K 2 LYS C 120  GLU C 125 -1  O  LYS C 120   N  VAL C 117           
SHEET    1   L 2 THR D  18  SER D  21  0                                        
SHEET    2   L 2 HIS D  29  ASN D  32 -1  O  ASN D  32   N  THR D  18           
SHEET    1   M 2 PHE D  37  GLY D  38  0                                        
SHEET    2   M 2 ILE D  44  ASP D  45 -1  O  ILE D  44   N  GLY D  38           
SHEET    1   N 2 TRP D 112  VAL D 117  0                                        
SHEET    2   N 2 LYS D 120  GLU D 125 -1  O  LEU D 122   N  VAL D 115           
SSBOND   1 CYS A   11    CYS A   19                          1555   1555  2.04  
SSBOND   2 CYS A   13    CYS A   31                          1555   1555  2.05  
SSBOND   3 CYS A   33    CYS A   42                          1555   1555  2.07  
SSBOND   4 CYS A   50    CYS A  131                          1555   1555  2.04  
SSBOND   5 CYS A   71    CYS A  113                          1555   1555  2.05  
SSBOND   6 CYS A  102    CYS A  126                          1555   1555  2.02  
SSBOND   7 CYS B   11    CYS B   19                          1555   1555  2.03  
SSBOND   8 CYS B   13    CYS B   31                          1555   1555  2.03  
SSBOND   9 CYS B   33    CYS B   42                          1555   1555  2.09  
SSBOND  10 CYS B   50    CYS B  131                          1555   1555  2.05  
SSBOND  11 CYS B   71    CYS B  113                          1555   1555  2.05  
SSBOND  12 CYS B  102    CYS B  126                          1555   1555  2.01  
SSBOND  13 CYS C   11    CYS C   19                          1555   1555  2.00  
SSBOND  14 CYS C   13    CYS C   31                          1555   1555  2.06  
SSBOND  15 CYS C   33    CYS C   42                          1555   1555  2.08  
SSBOND  16 CYS C   50    CYS C  131                          1555   1555  2.06  
SSBOND  17 CYS C   71    CYS C  113                          1555   1555  2.03  
SSBOND  18 CYS C  102    CYS C  126                          1555   1555  2.03  
SSBOND  19 CYS D   11    CYS D   19                          1555   1555  2.01  
SSBOND  20 CYS D   13    CYS D   31                          1555   1555  2.02  
SSBOND  21 CYS D   33    CYS D   42                          1555   1555  2.04  
SSBOND  22 CYS D   50    CYS D  131                          1555   1555  2.06  
SSBOND  23 CYS D   71    CYS D  113                          1555   1555  2.05  
SSBOND  24 CYS D  102    CYS D  126                          1555   1555  2.01  
SITE     1 AC1  4 ARG B 109  ASN C  75  HIS C  87  LYS C  98                    
SITE     1 AC2  8 ARG A 109  HOH A 190  ASN D  75  HIS D  87                    
SITE     2 AC2  8 LYS D  98  HOH D 872  HOH D 883  HOH D 895                    
SITE     1 AC3  3 ARG D 110  HIS D 129  HOH D 901                               
SITE     1 AC4  2 ARG D 108  ARG D 109                                          
CRYST1   47.603   64.327   64.623 107.62  92.11  95.75 P 1           4          
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      0.021007  0.002115  0.001498        0.00000                         
SCALE2      0.000000  0.015624  0.005061        0.00000                         
SCALE3      0.000000  0.000000  0.016277        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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