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Database: PDB
Entry: 3BT1
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Original site: 3BT1 
HEADER    IMMUNE SYSTEM                           27-DEC-07   3BT1              
TITLE     STRUCTURE OF UROKINASE RECEPTOR, UROKINASE AND VITRONECTIN COMPLEX    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UROKINASE-TYPE PLASMINOGEN ACTIVATOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UROKINASE AMINO TERMINAL FRAGMENT, UROKINASE-TYPE          
COMPND   5 PLASMINOGEN ACTIVATOR LONG CHAIN A, UNP RESIDUES 21-153;             
COMPND   6 SYNONYM: UPA, U-PLASMINOGEN ACTIVATOR;                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: VITRONECTIN;                                               
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: SOMETOMEDIN-B DOMAIN;                                      
COMPND  12 SYNONYM: SERUM-SPREADING FACTOR, S-PROTEIN, V75;                     
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR;          
COMPND  16 CHAIN: U;                                                            
COMPND  17 SYNONYM: UPAR, U-PAR, MONOCYTE ACTIVATION ANTIGEN MO3, CD87 ANTIGEN; 
COMPND  18 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: S2 CELLS;                                  
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMT/BIP;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: VTN;                                                           
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: PLAUR, MO3, UPAR;                                              
SOURCE  26 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  27 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: S2 CELLS;                                  
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  31 EXPRESSION_SYSTEM_PLASMID: PMT/BIP                                   
KEYWDS    PROTEIN-PROTEIN COMPLEX, GLYCOPROTEIN, GPI-ANCHOR, LIPOPROTEIN,       
KEYWDS   2 MEMBRANE, RECEPTOR, SECRETED, BLOOD COAGULATION, EGF-LIKE DOMAIN,    
KEYWDS   3 FIBRINOLYSIS, HYDROLASE, KRINGLE, PHOSPHOPROTEIN, PLASMINOGEN        
KEYWDS   4 ACTIVATION, PROTEASE, SERINE PROTEASE, ZYMOGEN, CELL ADHESION,       
KEYWDS   5 HEPARIN-BINDING, SULFATION, IMMUNOGLOBULIN DOMAIN, IMMUNE SYSTEM     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HUANG                                                               
REVDAT   4   13-JUL-11 3BT1    1       VERSN                                    
REVDAT   3   24-FEB-09 3BT1    1       VERSN                                    
REVDAT   2   22-APR-08 3BT1    1       JRNL                                     
REVDAT   1   25-MAR-08 3BT1    0                                                
JRNL        AUTH   Q.HUAI,A.ZHOU,L.LIN,A.P.MAZAR,G.C.PARRY,J.CALLAHAN,D.E.SHAW, 
JRNL        AUTH 2 B.FURIE,B.C.FURIE,M.HUANG                                    
JRNL        TITL   CRYSTAL STRUCTURES OF TWO HUMAN VITRONECTIN, UROKINASE AND   
JRNL        TITL 2 UROKINASE RECEPTOR COMPLEXES                                 
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  15   422 2008              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   18376415                                                     
JRNL        DOI    10.1038/NSMB.1404                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 13778                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 726                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1005                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3990                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 54                           
REMARK   3   BIN FREE R VALUE                    : 0.5980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3394                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 82.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.48000                                              
REMARK   3    B22 (A**2) : -3.25000                                             
REMARK   3    B33 (A**2) : 2.77000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.439         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.374         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.465        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3560 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2473 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4821 ; 1.821 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5921 ; 1.048 ; 3.016       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   434 ; 9.464 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;36.371 ;24.302       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   595 ;21.248 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;19.560 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   510 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3950 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   686 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1061 ; 0.266 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2877 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1752 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2006 ; 0.100 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   114 ; 0.196 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     2 ; 0.163 ; 0.200       
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):    17 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.246 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.064 ; 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):  2697 ; 0.746 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   909 ; 0.105 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3478 ; 0.958 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1573 ; 1.356 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1343 ; 2.154 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.05                                          
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 3BT1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB045932.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
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                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14540                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.80300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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 2FD6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 3350, 50MM HEPES PH 7.5,         
REMARK 280  MICRODIALYSIS, TEMPERATURE 295K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       48.67650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.59350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.67650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.59350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, U                               
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.9 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, U                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     ASP A   133                                                      
REMARK 465     ARG U    -1                                                      
REMARK 465     SER U     0                                                      
REMARK 465     ARG U    83                                                      
REMARK 465     ALA U    84                                                      
REMARK 465     LEU U   276                                                      
REMARK 465     ASP U   277                                                      
REMARK 465     VAL U   278                                                      
REMARK 465     GLN U   279                                                      
REMARK 465     TYR U   280                                                      
REMARK 465     ARG U   281                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN U    52     O5   NAG U  1052              1.68            
REMARK 500   O    THR U    54     O    LEU U    66              2.13            
REMARK 500   O    LEU U     1     N    CYS U    17              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU U  33   CB    GLU U  33   CG      0.114                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU U 144   CA  -  CB  -  CG  ANGL. DEV. =  14.5 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      167.92     69.08                                   
REMARK 500    ASP A  12       42.10    -94.37                                   
REMARK 500    ASN A  27       32.15     39.56                                   
REMARK 500    LYS A  35     -110.11     57.64                                   
REMARK 500    ASN A  54      -63.35     84.43                                   
REMARK 500    ARG A  59     -144.84   -108.14                                   
REMARK 500    ALA A  62      116.50    118.00                                   
REMARK 500    ASP A  65     -159.94    -90.74                                   
REMARK 500    ARG A  88       49.50   -157.12                                   
REMARK 500    SER A  89      -88.98     46.39                                   
REMARK 500    ASP A  90       -1.71    -57.06                                   
REMARK 500    ASN A 107       54.00     36.37                                   
REMARK 500    LEU A 119     -106.09    -90.16                                   
REMARK 500    LYS A 120      112.22    -15.37                                   
REMARK 500    MET A 127       75.19    -43.29                                   
REMARK 500    GLU B   3     -112.16   -105.76                                   
REMARK 500    SER B   4      124.42     55.68                                   
REMARK 500    ARG B   8      -61.25     62.75                                   
REMARK 500    CYS B   9       -7.45     80.47                                   
REMARK 500    THR B  10       56.91   -154.52                                   
REMARK 500    LYS B  18     -108.97    -67.39                                   
REMARK 500    CYS B  39       70.63   -118.12                                   
REMARK 500    LYS B  40       47.34    176.93                                   
REMARK 500    GLU U  16       98.47    -64.72                                   
REMARK 500    CYS U  17       56.48    -54.25                                   
REMARK 500    ALA U  18     -163.95     77.85                                   
REMARK 500    LEU U  19     -144.77    -96.46                                   
REMARK 500    ASP U  22       71.58   -156.04                                   
REMARK 500    GLU U  34     -127.95     33.40                                   
REMARK 500    SER U  44      168.00    176.30                                   
REMARK 500    CYS U  45      163.19    -45.69                                   
REMARK 500    THR U  54      -62.43   -126.09                                   
REMARK 500    LEU U  55      122.83     50.97                                   
REMARK 500    ASP U  74       97.07    -45.88                                   
REMARK 500    LEU U  75      104.65     66.42                                   
REMARK 500    CYS U  76       -2.51   -153.65                                   
REMARK 500    GLN U  78      124.03    -27.79                                   
REMARK 500    SER U  81     -179.13    -57.59                                   
REMARK 500    THR U  86      112.80    159.23                                   
REMARK 500    TYR U  92     -120.52   -110.94                                   
REMARK 500    MET U 103        5.99     59.06                                   
REMARK 500    GLN U 131     -102.54   -172.55                                   
REMARK 500    GLU U 135       44.07    178.78                                   
REMARK 500    ARG U 137      166.04     71.91                                   
REMARK 500    PRO U 138      148.39    -33.04                                   
REMARK 500    CYS U 153      -74.12   -118.98                                   
REMARK 500    PRO U 154      125.10    -34.20                                   
REMARK 500    ASN U 162      -34.46    -39.62                                   
REMARK 500    ASP U 163       26.10   -143.26                                   
REMARK 500    CYS U 170      106.03   -167.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU U   16     CYS U   17                 -137.00                    
REMARK 500 GLU U  185     ASN U  186                 -146.32                    
REMARK 500 GLU U  230     PRO U  231                 -120.32                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR U  54        21.1      L          L   OUTSIDE RANGE           
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 NAG U 1052                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 1172                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN U 1202                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FD6   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF UROKINASE RECEPTOR IN COMPLEX WITH UROKINASE            
REMARK 900 RELATED ID: 3BT2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX WITH FAB FRAGMENTS                          
DBREF  3BT1 A    1   133  UNP    P00749   UROK_HUMAN      21    153             
DBREF  3BT1 B    2    41  UNP    P04004   VTNC_HUMAN      21     60             
DBREF  3BT1 U    1   281  UNP    Q03405   UPAR_HUMAN      23    303             
SEQADV 3BT1 ARG A   -1  UNP  P00749              EXPRESSION TAG                 
SEQADV 3BT1 SER A    0  UNP  P00749              EXPRESSION TAG                 
SEQADV 3BT1 ARG U   -1  UNP  Q03405              EXPRESSION TAG                 
SEQADV 3BT1 SER U    0  UNP  Q03405              EXPRESSION TAG                 
SEQRES   1 A  135  ARG SER SER ASN GLU LEU HIS GLN VAL PRO SER ASN CYS          
SEQRES   2 A  135  ASP CYS LEU ASN GLY GLY THR CYS VAL SER ASN LYS TYR          
SEQRES   3 A  135  PHE SER ASN ILE HIS TRP CYS ASN CYS PRO LYS LYS PHE          
SEQRES   4 A  135  GLY GLY GLN HIS CYS GLU ILE ASP LYS SER LYS THR CYS          
SEQRES   5 A  135  TYR GLU GLY ASN GLY HIS PHE TYR ARG GLY LYS ALA SER          
SEQRES   6 A  135  THR ASP THR MET GLY ARG PRO CYS LEU PRO TRP ASN SER          
SEQRES   7 A  135  ALA THR VAL LEU GLN GLN THR TYR HIS ALA HIS ARG SER          
SEQRES   8 A  135  ASP ALA LEU GLN LEU GLY LEU GLY LYS HIS ASN TYR CYS          
SEQRES   9 A  135  ARG ASN PRO ASP ASN ARG ARG ARG PRO TRP CYS TYR VAL          
SEQRES  10 A  135  GLN VAL GLY LEU LYS PRO LEU VAL GLN GLU CYS MET VAL          
SEQRES  11 A  135  HIS ASP CYS ALA ASP                                          
SEQRES   1 B   40  GLN GLU SER CYS LYS GLY ARG CYS THR GLU GLY PHE ASN          
SEQRES   2 B   40  VAL ASP LYS LYS CYS GLN CYS ASP GLU LEU CYS SER TYR          
SEQRES   3 B   40  TYR GLN SER CYS CYS THR ASP TYR THR ALA GLU CYS LYS          
SEQRES   4 B   40  PRO                                                          
SEQRES   1 U  283  ARG SER LEU ARG CYS MET GLN CYS LYS THR ASN GLY ASP          
SEQRES   2 U  283  CYS ARG VAL GLU GLU CYS ALA LEU GLY GLN ASP LEU CYS          
SEQRES   3 U  283  ARG THR THR ILE VAL ARG LEU TRP GLU GLU GLY GLU GLU          
SEQRES   4 U  283  LEU GLU LEU VAL GLU LYS SER CYS THR HIS SER GLU LYS          
SEQRES   5 U  283  THR ASN ARG THR LEU SER TYR ARG THR GLY LEU LYS ILE          
SEQRES   6 U  283  THR SER LEU THR GLU VAL VAL CYS GLY LEU ASP LEU CYS          
SEQRES   7 U  283  ASN GLN GLY ASN SER GLY ARG ALA VAL THR TYR SER ARG          
SEQRES   8 U  283  SER ARG TYR LEU GLU CYS ILE SER CYS GLY SER SER ASP          
SEQRES   9 U  283  MET SER CYS GLU ARG GLY ARG HIS GLN SER LEU GLN CYS          
SEQRES  10 U  283  ARG SER PRO GLU GLU GLN CYS LEU ASP VAL VAL THR HIS          
SEQRES  11 U  283  TRP ILE GLN GLU GLY GLU GLU GLY ARG PRO LYS ASP ASP          
SEQRES  12 U  283  ARG HIS LEU ARG GLY CYS GLY TYR LEU PRO GLY CYS PRO          
SEQRES  13 U  283  GLY SER ASN GLY PHE HIS ASN ASN ASP THR PHE HIS PHE          
SEQRES  14 U  283  LEU LYS CYS CYS ASN THR THR LYS CYS ASN GLU GLY PRO          
SEQRES  15 U  283  ILE LEU GLU LEU GLU ASN LEU PRO GLN ASN GLY ARG GLN          
SEQRES  16 U  283  CYS TYR SER CYS LYS GLY ASN SER THR HIS GLY CYS SER          
SEQRES  17 U  283  SER GLU GLU THR PHE LEU ILE ASP CYS ARG GLY PRO MET          
SEQRES  18 U  283  ASN GLN CYS LEU VAL ALA THR GLY THR HIS GLU PRO LYS          
SEQRES  19 U  283  ASN GLN SER TYR MET VAL ARG GLY CYS ALA THR ALA SER          
SEQRES  20 U  283  MET CYS GLN HIS ALA HIS LEU GLY ASP ALA PHE SER MET          
SEQRES  21 U  283  ASN HIS ILE ASP VAL SER CYS CYS THR LYS SER GLY CYS          
SEQRES  22 U  283  ASN HIS PRO ASP LEU ASP VAL GLN TYR ARG                      
MODRES 3BT1 ASN U   52  ASN  GLYCOSYLATION SITE                                 
MODRES 3BT1 ASN U  172  ASN  GLYCOSYLATION SITE                                 
MODRES 3BT1 ASN U  200  ASN  GLYCOSYLATION SITE                                 
HET    NAG  U1052      14                                                       
HET    NAG  U1172      14                                                       
HET    NAG  U1200      14                                                       
HET    NAG  U1201      14                                                       
HET    MAN  U1202      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   6  MAN    C6 H12 O6                                                    
HELIX    1   1 THR A   78  GLN A   82  5                                   5    
HELIX    2   2 ARG A   88  GLN A   93  5                                   6    
HELIX    3   3 LEU B   24  GLN B   29  1                                   6    
HELIX    4   4 ASP B   34  CYS B   39  1                                   6    
HELIX    5   5 SER U  101  MET U  103  5                                   3    
HELIX    6   6 SER U  206  THR U  210  5                                   5    
HELIX    7   7 HIS U  251  PHE U  256  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  TRP A  30   N  VAL A  20           
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 115  0                                        
SHEET    2   D 2 LEU A 122  GLU A 125 -1  O  GLN A 124   N  CYS A 113           
SHEET    1   E 2 ARG U   2  CYS U   6  0                                        
SHEET    2   E 2 CYS U  12  GLU U  16 -1  O  GLU U  15   N  CYS U   3           
SHEET    1   F 4 GLU U  36  THR U  46  0                                        
SHEET    2   F 4 LEU U  23  GLU U  33 -1  N  GLU U  33   O  GLU U  36           
SHEET    3   F 4 LYS U  62  CYS U  71 -1  O  THR U  67   N  ILE U  28           
SHEET    4   F 4 SER U  56  THR U  59 -1  N  TYR U  57   O  THR U  64           
SHEET    1   G 9 GLN U 111  GLN U 114  0                                        
SHEET    2   G 9 GLU U  94  GLY U  99 -1  N  CYS U  95   O  LEU U 113           
SHEET    3   G 9 HIS U 143  GLY U 148 -1  O  ARG U 145   N  CYS U  98           
SHEET    4   G 9 GLN U 121  TRP U 129 -1  N  GLN U 121   O  GLY U 148           
SHEET    5   G 9 THR U 164  CYS U 171 -1  O  PHE U 165   N  HIS U 128           
SHEET    6   G 9 GLY U 155  ASN U 161 -1  N  ASN U 157   O  LEU U 168           
SHEET    7   G 9 MET U 237  ALA U 242 -1  O  CYS U 241   N  HIS U 160           
SHEET    8   G 9 GLN U 221  HIS U 229 -1  N  GLN U 221   O  ALA U 242           
SHEET    9   G 9 MET U 258  CYS U 266 -1  O  CYS U 266   N  CYS U 222           
SHEET    1   H 2 GLN U 189  SER U 196  0                                        
SHEET    2   H 2 PHE U 211  ARG U 216 -1  O  ILE U 213   N  CYS U 194           
SSBOND   1 CYS A   11    CYS A   19                          1555   1555  2.01  
SSBOND   2 CYS A   13    CYS A   31                          1555   1555  2.03  
SSBOND   3 CYS A   33    CYS A   42                          1555   1555  2.02  
SSBOND   4 CYS A   50    CYS A  131                          1555   1555  2.04  
SSBOND   5 CYS A   71    CYS A  113                          1555   1555  2.03  
SSBOND   6 CYS A  102    CYS A  126                          1555   1555  2.04  
SSBOND   7 CYS B    5    CYS B   21                          1555   1555  2.03  
SSBOND   8 CYS B    5    CYS B   32                          1555   1555  2.13  
SSBOND   9 CYS B    9    CYS B   39                          1555   1555  2.01  
SSBOND  10 CYS B   19    CYS B   32                          1555   1555  2.08  
SSBOND  11 CYS B   25    CYS B   31                          1555   1555  2.01  
SSBOND  12 CYS U    3    CYS U   24                          1555   1555  2.06  
SSBOND  13 CYS U    3    CYS U   17                          1555   1555  2.11  
SSBOND  14 CYS U    6    CYS U   12                          1555   1555  2.02  
SSBOND  15 CYS U   17    CYS U   45                          1555   1555  2.04  
SSBOND  16 CYS U   71    CYS U   76                          1555   1555  2.05  
SSBOND  17 CYS U   95    CYS U  122                          1555   1555  1.98  
SSBOND  18 CYS U   98    CYS U  105                          1555   1555  2.04  
SSBOND  19 CYS U  115    CYS U  147                          1555   1555  2.08  
SSBOND  20 CYS U  153    CYS U  170                          1555   1555  2.00  
SSBOND  21 CYS U  171    CYS U  176                          1555   1555  2.04  
SSBOND  22 CYS U  194    CYS U  222                          1555   1555  1.97  
SSBOND  23 CYS U  197    CYS U  205                          1555   1555  2.08  
SSBOND  24 CYS U  215    CYS U  241                          1555   1555  2.01  
SSBOND  25 CYS U  247    CYS U  265                          1555   1555  2.03  
SSBOND  26 CYS U  266    CYS U  271                          1555   1555  2.04  
LINK         ND2 ASN U  52                 C1  NAG U1052     1555   1555  1.55  
LINK         ND2 ASN U 172                 C1  NAG U1172     1555   1555  1.33  
LINK         ND2 ASN U 200                 C1  NAG U1200     1555   1555  1.47  
LINK         O4  NAG U1200                 C1  NAG U1201     1555   1555  1.47  
LINK         O4  NAG U1201                 C1  MAN U1202     1555   1555  1.48  
SITE     1 AC1  1 ASN U  52                                                     
SITE     1 AC2  3 MET A  67  MET A 127  ASN U 172                               
SITE     1 AC3  3 ASN U 200  THR U 202  HIS U 203                               
SITE     1 AC4  1 HIS U 203                                                     
SITE     1 AC5  1 GLU B  23                                                     
CRYST1   97.353  105.187   55.360  90.00  90.00  90.00 P 21 21 2     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      0.010272  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009507  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018064        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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