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Entry: 3BT2
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HEADER    IMMUNE SYSTEM                           27-DEC-07   3BT2              
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: ANTI-UPAR ANTIBODY, LIGHT CHAIN;                           
COMPND  16 CHAIN: L;                                                            
COMPND  17 FRAGMENT: FAB FRAGMENT, LIGHT CHAIN;                                 
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: ANTI-UPAR ANTIBODY, HEAVY CHAIN;                           
COMPND  21 CHAIN: H;                                                            
COMPND  22 FRAGMENT: FAB FRAGMENT, HEAVY CHAIN;                                 
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: UROKINASE PLASMINOGEN ACTIVATOR SURFACE RECEPTOR;          
COMPND  26 CHAIN: U;                                                            
COMPND  27 SYNONYM: UPAR, U-PAR, MONOCYTE ACTIVATION ANTIGEN MO3, CD87 ANTIGEN; 
COMPND  28 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: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMT/BIP;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: VTN;                                                           
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 MOL_ID: 3;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  23 ORGANISM_TAXID: 10090;                                               
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  26 MOL_ID: 4;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  28 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  29 ORGANISM_TAXID: 10090;                                               
SOURCE  30 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  32 MOL_ID: 5;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  34 ORGANISM_COMMON: HUMAN;                                              
SOURCE  35 ORGANISM_TAXID: 9606;                                                
SOURCE  36 GENE: PLAUR, MO3, UPAR;                                              
SOURCE  37 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  38 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  39 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  40 EXPRESSION_SYSTEM_STRAIN: S2 CELLS;                                  
SOURCE  41 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  42 EXPRESSION_SYSTEM_PLASMID: PMT/BIP                                   
KEYWDS    PROTEIN-PROTEIN INTERACTION, 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 3BT2    1       VERSN                                    
REVDAT   3   24-FEB-09 3BT2    1       VERSN                                    
REVDAT   2   22-APR-08 3BT2    1       JRNL                                     
REVDAT   1   25-MAR-08 3BT2    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 37032                          
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) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1191                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2593                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6527                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 57                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 42.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : 1.50000                                              
REMARK   3    B33 (A**2) : -1.47000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.70000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.463         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.292         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.316         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.105        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.917                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6782 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4587 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9213 ; 1.740 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11097 ; 1.110 ; 3.010       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   835 ; 7.848 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   293 ;37.001 ;24.403       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1097 ;18.315 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;19.280 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1003 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7496 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1321 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1296 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4541 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3036 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3667 ; 0.096 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   181 ; 0.236 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.417 ; 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):    10 ; 0.135 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    48 ; 0.184 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.121 ; 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):  5317 ; 1.039 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1721 ; 0.166 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6778 ; 1.264 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3050 ; 2.001 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2435 ; 2.926 ; 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  : 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 :   B     2        B    41                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.0350 -46.9060  42.1430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4389 T22:   0.8800                                     
REMARK   3      T33:   0.2227 T12:   0.1835                                     
REMARK   3      T13:  -0.0199 T23:  -0.1026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.7256 L22:  26.5061                                     
REMARK   3      L33:   7.8644 L12:  -0.4411                                     
REMARK   3      L13:  -4.6959 L23:  -3.4339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7767 S12:   1.8843 S13:  -0.7720                       
REMARK   3      S21:  -1.9615 S22:   0.3062 S23:  -3.7408                       
REMARK   3      S31:   2.5648 S32:   1.0052 S33:   0.4705                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    41        A   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.2840 -40.5410  78.7630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0711 T22:   0.0780                                     
REMARK   3      T33:  -0.2841 T12:  -0.0007                                     
REMARK   3      T13:  -0.0029 T23:   0.4202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8112 L22:   8.7012                                     
REMARK   3      L33:   4.6745 L12:  -1.2009                                     
REMARK   3      L13:  -1.6517 L23:   5.1144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5181 S12:   0.2417 S13:   0.8900                       
REMARK   3      S21:  -0.3670 S22:  -0.3248 S23:  -1.2106                       
REMARK   3      S31:  -0.6866 S32:   0.8789 S33:  -0.1934                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   U     1        U    80                          
REMARK   3    RESIDUE RANGE :   A     9        A    40                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4850 -38.1400  60.3870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0382 T22:  -0.1934                                     
REMARK   3      T33:  -0.5517 T12:   0.0749                                     
REMARK   3      T13:  -0.1130 T23:   0.2814                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1447 L22:   5.9408                                     
REMARK   3      L33:   6.0103 L12:   2.0134                                     
REMARK   3      L13:   0.3447 L23:  -2.6643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0910 S12:  -0.1513 S13:  -0.1966                       
REMARK   3      S21:   0.1904 S22:   0.0273 S23:  -0.0426                       
REMARK   3      S31:  -0.0607 S32:   0.2014 S33:   0.0637                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   212                          
REMARK   3    RESIDUE RANGE :   H     1        H   208                          
REMARK   3    RESIDUE RANGE :   U    87        U   185                          
REMARK   3    RESIDUE RANGE :   U   186        U   275                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8100  -7.0670  18.9510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4237 T22:  -0.3873                                     
REMARK   3      T33:  -0.4443 T12:  -0.0247                                     
REMARK   3      T13:   0.0117 T23:  -0.0373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7195 L22:   1.7667                                     
REMARK   3      L33:   2.1140 L12:   0.0287                                     
REMARK   3      L13:   0.3308 L23:  -1.4249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0931 S12:  -0.0707 S13:   0.1554                       
REMARK   3      S21:   0.1367 S22:  -0.2159 S23:  -0.0153                       
REMARK   3      S31:   0.0124 S32:   0.2226 S33:   0.1228                       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3BT2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB045933.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; NSLS                          
REMARK 200  BEAMLINE                       : 24-ID-C; X12C                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 1.0                           
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC QUANTUM     
REMARK 200                                   210                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38381                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : 0.07700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; 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   (%): 57.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, 2.5% ETHANOL, 0.05%         
REMARK 280  SODIUM AZIDE, 50MM CACODYLATE PH 6.5, PH 7.5, MICRODIALYSIS,        
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       43.60250            
REMARK 290   SMTRY3   2  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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, H, 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: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H, 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     PRO A     8                                                      
REMARK 465     ASP A   133                                                      
REMARK 465     CYS L   213                                                      
REMARK 465     GLY H   127                                                      
REMARK 465     GLY H   209                                                      
REMARK 465     ARG U     0                                                      
REMARK 465     SER U    81                                                      
REMARK 465     GLY U    82                                                      
REMARK 465     ARG U    83                                                      
REMARK 465     ALA U    84                                                      
REMARK 465     VAL U    85                                                      
REMARK 465     THR U    86                                                      
REMARK 465     GLN U   131                                                      
REMARK 465     GLU U   132                                                      
REMARK 465     GLY U   133                                                      
REMARK 465     GLU U   134                                                      
REMARK 465     GLU U   135                                                      
REMARK 465     GLY U   136                                                      
REMARK 465     ARG U   137                                                      
REMARK 465     PRO U   138                                                      
REMARK 465     HIS U   249                                                      
REMARK 465     ALA U   250                                                      
REMARK 465     HIS U   251                                                      
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   OE1  GLU L   105     OH   TYR L   172              1.83            
REMARK 500   NE2  HIS U   128     OE2  GLU U   183              1.92            
REMARK 500   NE2  HIS U   143     OE2  GLU U   183              1.96            
REMARK 500   O    HIS U   273     N    ASP U   275              1.99            
REMARK 500   O    ALA L    25     OG1  THR L    69              2.00            
REMARK 500   O    TYR L    93     N    PHE L    96              2.01            
REMARK 500   OH   TYR A    58     O    LYS A    61              2.01            
REMARK 500   OD2  ASP A    12     NE2  HIS A    41              2.03            
REMARK 500   CG1  VAL H   131     O    VAL H   178              2.12            
REMARK 500   OD2  ASP A    12     NE2  HIS A    29              2.13            
REMARK 500   O    TYR L    93     CD2  PHE L    96              2.19            
REMARK 500   OE2  GLU L    50     ND1  HIS H    98              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    GLY A  38   C     GLY A  38   O       0.132                       
REMARK 500    HIS A  41   CG    HIS A  41   CD2     0.073                       
REMARK 500    CYS L 193   CB    CYS L 193   SG     -0.128                       
REMARK 500    LYS U   7   C     LYS U   7   O       0.193                       
REMARK 500    GLU U 183   CB    GLU U 183   CG      0.263                       
REMARK 500    GLU U 183   CD    GLU U 183   OE2     0.077                       
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    ARG A  88   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LYS B  40   N   -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    TYR L  93   CB  -  CG  -  CD2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    TYR L  93   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    PRO L  94   C   -  N   -  CA  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ARG L 187   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG L 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ASP H 101   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG U 192   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG U 192   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 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    ASN A  10     -124.30    -70.15                                   
REMARK 500    CYS A  11       74.86     57.51                                   
REMARK 500    ASP A  12        1.55    -68.05                                   
REMARK 500    ASN A  15     -131.98     66.58                                   
REMARK 500    GLU A  52     -140.82    -84.63                                   
REMARK 500    LYS A  61     -141.47    -90.12                                   
REMARK 500    ALA A  62      101.01     79.80                                   
REMARK 500    THR A  66      -36.93    -35.28                                   
REMARK 500    ASN A 104       57.40   -162.21                                   
REMARK 500    VAL A 128      124.58    -30.58                                   
REMARK 500    LYS B   6      -49.50    177.51                                   
REMARK 500    ARG B   8      -34.90     84.02                                   
REMARK 500    THR B  10       48.80   -150.93                                   
REMARK 500    CYS B  19      136.57     58.17                                   
REMARK 500    GLU B  38      -90.13    -87.88                                   
REMARK 500    LYS B  40      -99.16    -76.49                                   
REMARK 500    ILE L   2      108.08    -10.69                                   
REMARK 500    SER L  26      -29.40    -35.63                                   
REMARK 500    TRP L  47      -57.54   -123.41                                   
REMARK 500    GLU L  50       47.80     33.62                                   
REMARK 500    ILE L  51      -52.64     90.41                                   
REMARK 500    ALA L  84     -179.98   -175.63                                   
REMARK 500    TYR L  93      -93.08    -17.74                                   
REMARK 500    PRO L  94      -10.62    -36.89                                   
REMARK 500    PHE L  96       32.97     38.65                                   
REMARK 500    HIS H  52A     -59.16     75.28                                   
REMARK 500    SER H  82B      60.31     60.11                                   
REMARK 500    SER H 129      -41.49     38.70                                   
REMARK 500    MET H 130        8.82   -168.60                                   
REMARK 500    VAL H 131       89.30     73.02                                   
REMARK 500    SER H 155      -46.59   -140.69                                   
REMARK 500    GLU U  34     -127.80     45.46                                   
REMARK 500    ASP U  74      111.60    125.35                                   
REMARK 500    SER U  88       83.50     79.65                                   
REMARK 500    ARG U  89      -72.87   -130.06                                   
REMARK 500    TYR U  92     -107.74   -113.37                                   
REMARK 500    CYS U 153      -70.72    -79.45                                   
REMARK 500    PRO U 154      102.81    -49.71                                   
REMARK 500    ASN U 161     -158.68   -149.06                                   
REMARK 500    GLU U 230      173.60     67.57                                   
REMARK 500    PRO U 231      -83.56    -38.80                                   
REMARK 500    LYS U 232     -169.77    -67.07                                   
REMARK 500    ASN U 233       49.83    -84.44                                   
REMARK 500    ASN U 259      -86.74   -131.63                                   
REMARK 500    ASN U 272      -22.23    -25.11                                   
REMARK 500    PRO U 274       33.34    -38.84                                   
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 LYS A   61     ALA A   62                 -138.66                    
REMARK 500 MET H  130     VAL H  131                  143.58                    
REMARK 500 CYS U  271     ASN U  272                  144.37                    
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    LYS B  40         3.3      L          L   EXPECTING SP3           
REMARK 500    SER H 129        23.7      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 1172                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG U 1200                
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: 3BT1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX WITHOUT FAB FRAGMENTS                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS COORDINATES IN CHAINS L AND H ARE USED NON-SEQUENTIAL           
REMARK 999 RESIDUE NUMBERING. IT IS DUE TO KABAT-WU NUMBERING, WHICH IS         
REMARK 999 TYPICAL FOR ANTIBODY.                                                
DBREF  3BT2 A    1   133  UNP    P00749   UROK_HUMAN      21    153             
DBREF  3BT2 B    2    41  UNP    P04004   VTNC_HUMAN      21     60             
DBREF  3BT2 L    1   213  PDB    3BT2     3BT2             1    212             
DBREF  3BT2 H    1   209  PDB    3BT2     3BT2             1    214             
DBREF  3BT2 U    1   281  UNP    Q03405   UPAR_HUMAN      23    303             
SEQADV 3BT2 ARG A   -1  UNP  P00749              EXPRESSION TAG                 
SEQADV 3BT2 SER A    0  UNP  P00749              EXPRESSION TAG                 
SEQADV 3BT2 ARG U    0  UNP  Q03405              EXPRESSION TAG                 
SEQADV 3BT2 SER U    1A 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 L  212  ASP ILE VAL LEU THR GLN SER PRO ASP ILE THR ALA ALA          
SEQRES   2 L  212  SER LEU GLY GLN LYS VAL THR ILE THR CYS SER ALA SER          
SEQRES   3 L  212  SER SER VAL SER TYR MET HIS TRP TYR GLN GLN LYS SER          
SEQRES   4 L  212  GLY THR SER PRO LYS PRO TRP ILE PHE GLU ILE SER LYS          
SEQRES   5 L  212  LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY          
SEQRES   6 L  212  SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU          
SEQRES   7 L  212  ALA GLU ASP ALA ALA ILE TYR TYR CYS GLN GLN TRP ASN          
SEQRES   8 L  212  TYR PRO PHE THR PHE GLY GLY GLY THR LYS LEU GLU ILE          
SEQRES   9 L  212  LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO          
SEQRES  10 L  212  PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL          
SEQRES  11 L  212  VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN          
SEQRES  12 L  212  VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY          
SEQRES  13 L  212  VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER          
SEQRES  14 L  212  THR TYR SER MET SER SER THR LEU THR LEU THR LYS ASP          
SEQRES  15 L  212  GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR          
SEQRES  16 L  212  HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN          
SEQRES  17 L  212  ARG ASN GLU CYS                                              
SEQRES   1 H  214  GLY VAL LYS LEU GLN GLN SER GLY PRO GLU VAL VAL LYS          
SEQRES   2 H  214  PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY          
SEQRES   3 H  214  TYR SER PHE THR ASN PHE TYR ILE HIS TRP VAL LYS GLN          
SEQRES   4 H  214  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE PHE          
SEQRES   5 H  214  HIS GLY SER ASP ASN THR GLU TYR ASN GLU LYS PHE LYS          
SEQRES   6 H  214  ASP LYS ALA THR LEU THR ALA ASP THR SER SER SER THR          
SEQRES   7 H  214  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 H  214  ALA VAL TYR PHE CYS ALA ARG TRP GLY PRO HIS TRP TYR          
SEQRES   9 H  214  PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL SER          
SEQRES  10 H  214  SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 H  214  PRO GLY ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS          
SEQRES  12 H  214  GLY TYR PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER          
SEQRES  13 H  214  GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL          
SEQRES  14 H  214  LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR          
SEQRES  15 H  214  VAL PRO SER SER THR TRP PRO SER GLU THR VAL THR CYS          
SEQRES  16 H  214  ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS          
SEQRES  17 H  214  LYS ILE ALA ALA ALA GLY                                      
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 3BT2 ASN U   52  ASN  GLYCOSYLATION SITE                                 
MODRES 3BT2 ASN U  172  ASN  GLYCOSYLATION SITE                                 
MODRES 3BT2 ASN U  200  ASN  GLYCOSYLATION SITE                                 
HET    NAG  U1052      14                                                       
HET    NAG  U1172      14                                                       
HET    NAG  U1173      14                                                       
HET    NAG  U1200      14                                                       
HET    NAG  U1201      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   6  NAG    5(C8 H15 N O6)                                               
FORMUL   9  HOH   *57(H2 O)                                                     
HELIX    1   1 LYS A   23  SER A   26  5                                   4    
HELIX    2   2 THR A   78  GLN A   82  5                                   5    
HELIX    3   3 ASP A   90  GLY A   95  1                                   6    
HELIX    4   4 THR B   33  GLU B   38  1                                   6    
HELIX    5   5 GLU L   79  ALA L   83  5                                   5    
HELIX    6   6 SER L  120  SER L  126  1                                   7    
HELIX    7   7 LYS L  182  ARG L  187  1                                   6    
HELIX    8   8 SER H   28  PHE H   32  5                                   5    
HELIX    9   9 GLU H   61  LYS H   64  5                                   4    
HELIX   10  10 THR H   73  SER H   75  5                                   3    
HELIX   11  11 THR H   83  SER H   87  5                                   5    
HELIX   12  12 SER H  151  SER H  153  5                                   3    
HELIX   13  13 PRO H  195  SER H  198  5                                   4    
HELIX   14  14 LEU U   75  GLY U   79  5                                   5    
HELIX   15  15 SER U  101  MET U  103  5                                   3    
HELIX   16  16 GLU U  183  LEU U  187  5                                   5    
HELIX   17  17 ALA U  244  GLN U  248  5                                   5    
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 TRP A 112  VAL A 117  0                                        
SHEET    2   C 2 LYS A 120  GLU A 125 -1  O  LEU A 122   N  VAL A 115           
SHEET    1   D 4 LEU L   4  SER L   7  0                                        
SHEET    2   D 4 VAL L  19  ALA L  25 -1  O  SER L  24   N  THR L   5           
SHEET    3   D 4 SER L  70  ILE L  75 -1  O  TYR L  71   N  CYS L  23           
SHEET    4   D 4 PHE L  62  SER L  67 -1  N  SER L  65   O  SER L  72           
SHEET    1   E 6 ILE L  10  ALA L  13  0                                        
SHEET    2   E 6 THR L 102  ILE L 106  1  O  GLU L 105   N  ALA L  13           
SHEET    3   E 6 ALA L  84  GLN L  90 -1  N  ALA L  84   O  LEU L 104           
SHEET    4   E 6 MET L  33  GLN L  38 -1  N  GLN L  38   O  ILE L  85           
SHEET    5   E 6 LYS L  45  PHE L  49 -1  O  ILE L  48   N  TRP L  35           
SHEET    6   E 6 LYS L  53  LEU L  54 -1  O  LYS L  53   N  PHE L  49           
SHEET    1   F 4 THR L 113  PHE L 117  0                                        
SHEET    2   F 4 GLY L 128  PHE L 138 -1  O  ASN L 136   N  THR L 113           
SHEET    3   F 4 TYR L 172  THR L 181 -1  O  LEU L 178   N  VAL L 131           
SHEET    4   F 4 VAL L 158  TRP L 162 -1  N  LEU L 159   O  THR L 177           
SHEET    1   G 4 SER L 152  ARG L 154  0                                        
SHEET    2   G 4 ASN L 144  ILE L 149 -1  N  TRP L 147   O  ARG L 154           
SHEET    3   G 4 SER L 190  THR L 196 -1  O  THR L 196   N  ASN L 144           
SHEET    4   G 4 ILE L 204  ASN L 209 -1  O  ILE L 204   N  ALA L 195           
SHEET    1   H 4 LYS H   3  GLN H   6  0                                        
SHEET    2   H 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  GLN H   5           
SHEET    3   H 4 THR H  77  LEU H  82 -1  O  LEU H  82   N  VAL H  18           
SHEET    4   H 4 ALA H  67  ASP H  72 -1  N  THR H  70   O  TYR H  79           
SHEET    1   I 6 GLU H  10  VAL H  12  0                                        
SHEET    2   I 6 THR H 107  VAL H 111  1  O  THR H 108   N  GLU H  10           
SHEET    3   I 6 ALA H  88  TRP H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4   I 6 ILE H  34  GLN H  39 -1  N  VAL H  37   O  PHE H  91           
SHEET    5   I 6 GLU H  46  ILE H  51 -1  O  ILE H  48   N  TRP H  36           
SHEET    6   I 6 THR H  57  TYR H  59 -1  O  GLU H  58   N  TRP H  50           
SHEET    1   J 4 GLU H  10  VAL H  12  0                                        
SHEET    2   J 4 THR H 107  VAL H 111  1  O  THR H 108   N  GLU H  10           
SHEET    3   J 4 ALA H  88  TRP H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4   J 4 PHE H 100A TRP H 103 -1  O  VAL H 102   N  ARG H  94           
SHEET    1   K 4 SER H 120  LEU H 124  0                                        
SHEET    2   K 4 THR H 132  TYR H 140 -1  O  LEU H 136   N  TYR H 122           
SHEET    3   K 4 LEU H 169  THR H 177 -1  O  VAL H 176   N  LEU H 133           
SHEET    4   K 4 VAL H 158  THR H 160 -1  N  HIS H 159   O  SER H 175           
SHEET    1   L 4 SER H 120  LEU H 124  0                                        
SHEET    2   L 4 THR H 132  TYR H 140 -1  O  LEU H 136   N  TYR H 122           
SHEET    3   L 4 LEU H 169  THR H 177 -1  O  VAL H 176   N  LEU H 133           
SHEET    4   L 4 VAL H 164  GLN H 166 -1  N  GLN H 166   O  LEU H 169           
SHEET    1   M 3 THR H 146  TRP H 149  0                                        
SHEET    2   M 3 THR H 189  HIS H 194 -1  O  ALA H 193   N  THR H 146           
SHEET    3   M 3 THR H 199  LYS H 204 -1  O  VAL H 201   N  VAL H 192           
SHEET    1   N 2 ARG U   2  CYS U   6  0                                        
SHEET    2   N 2 CYS U  12  GLU U  16 -1  O  ARG U  13   N  GLN U   5           
SHEET    1   O11 GLU U  36  THR U  46  0                                        
SHEET    2   O11 LEU U  23  GLU U  33 -1  N  LEU U  31   O  LEU U  38           
SHEET    3   O11 LYS U  62  CYS U  71 -1  O  THR U  67   N  ILE U  28           
SHEET    4   O11 ARG U  53  THR U  59 -1  N  LEU U  55   O  LEU U  66           
SHEET    5   O11 HIS U 143  TYR U 149 -1  O  CYS U 147   N  SER U  56           
SHEET    6   O11 GLN U 121  TRP U 129 -1  N  GLN U 121   O  GLY U 148           
SHEET    7   O11 THR U 164  CYS U 171 -1  O  PHE U 167   N  VAL U 126           
SHEET    8   O11 GLY U 155  ASN U 161 -1  N  ASN U 157   O  LEU U 168           
SHEET    9   O11 GLN U 234  ALA U 242 -1  O  CYS U 241   N  HIS U 160           
SHEET   10   O11 GLN U 189  GLY U 199 -1  N  CYS U 197   O  ARG U 239           
SHEET   11   O11 PHE U 211  ARG U 216 -1  O  ILE U 213   N  CYS U 194           
SHEET    1   P 9 GLN U 111  GLN U 114  0                                        
SHEET    2   P 9 GLU U  94  GLY U  99 -1  N  SER U  97   O  GLN U 111           
SHEET    3   P 9 HIS U 143  TYR U 149 -1  O  ARG U 145   N  CYS U  98           
SHEET    4   P 9 GLN U 121  TRP U 129 -1  N  GLN U 121   O  GLY U 148           
SHEET    5   P 9 THR U 164  CYS U 171 -1  O  PHE U 167   N  VAL U 126           
SHEET    6   P 9 GLY U 155  ASN U 161 -1  N  ASN U 157   O  LEU U 168           
SHEET    7   P 9 GLN U 234  ALA U 242 -1  O  CYS U 241   N  HIS U 160           
SHEET    8   P 9 GLN U 221  HIS U 229 -1  N  GLY U 227   O  TYR U 236           
SHEET    9   P 9 ASP U 262  CYS U 266 -1  O  CYS U 266   N  CYS U 222           
SSBOND   1 CYS A   11    CYS A   19                          1555   1555  2.07  
SSBOND   2 CYS A   13    CYS A   31                          1555   1555  2.02  
SSBOND   3 CYS A   33    CYS A   42                          1555   1555  2.04  
SSBOND   4 CYS A   50    CYS A  131                          1555   1555  2.02  
SSBOND   5 CYS A   71    CYS A  113                          1555   1555  2.04  
SSBOND   6 CYS A  102    CYS A  126                          1555   1555  2.03  
SSBOND   7 CYS B    5    CYS B   21                          1555   1555  2.03  
SSBOND   8 CYS B    9    CYS B   39                          1555   1555  2.04  
SSBOND   9 CYS B   19    CYS B   32                          1555   1555  2.03  
SSBOND  10 CYS B   25    CYS B   31                          1555   1555  2.04  
SSBOND  11 CYS L   23    CYS L   88                          1555   1555  2.13  
SSBOND  12 CYS L  133    CYS L  193                          1555   1555  2.06  
SSBOND  13 CYS H   22    CYS H   92                          1555   1555  2.14  
SSBOND  14 CYS H  135    CYS H  190                          1555   1555  2.07  
SSBOND  15 CYS U    3    CYS U   24                          1555   1555  2.01  
SSBOND  16 CYS U    6    CYS U   12                          1555   1555  2.06  
SSBOND  17 CYS U   17    CYS U   45                          1555   1555  2.04  
SSBOND  18 CYS U   71    CYS U   76                          1555   1555  2.02  
SSBOND  19 CYS U   95    CYS U  122                          1555   1555  2.02  
SSBOND  20 CYS U   98    CYS U  105                          1555   1555  2.08  
SSBOND  21 CYS U  115    CYS U  147                          1555   1555  2.07  
SSBOND  22 CYS U  153    CYS U  170                          1555   1555  2.06  
SSBOND  23 CYS U  171    CYS U  176                          1555   1555  2.05  
SSBOND  24 CYS U  194    CYS U  222                          1555   1555  2.04  
SSBOND  25 CYS U  197    CYS U  205                          1555   1555  2.10  
SSBOND  26 CYS U  215    CYS U  241                          1555   1555  2.06  
SSBOND  27 CYS U  247    CYS U  265                          1555   1555  2.03  
SSBOND  28 CYS U  266    CYS U  271                          1555   1555  2.02  
LINK         ND2 ASN U  52                 C1  NAG U1052     1555   1555  1.46  
LINK         ND2 ASN U 172                 C1  NAG U1172     1555   1555  1.44  
LINK         ND2 ASN U 200                 C1  NAG U1200     1555   1555  1.45  
LINK         O4  NAG U1172                 C1  NAG U1173     1555   1555  1.44  
LINK         O4  NAG U1200                 C1  NAG U1201     1555   1555  1.47  
CISPEP   1 SER L    7    PRO L    8          0        -1.97                     
CISPEP   2 TYR L  139    PRO L  140          0        -4.12                     
CISPEP   3 PHE H  141    PRO H  142          0        -2.15                     
CISPEP   4 GLU H  143    PRO H  144          0         2.71                     
CISPEP   5 TRP H  183    PRO H  184          0         0.60                     
SITE     1 AC1  1 ASN U 172                                                     
SITE     1 AC2  2 ASN U 200  HIS U 203                                          
CRYST1   52.096   87.205  124.274  90.00  94.31  90.00 P 1 21 1      2          
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      0.019195  0.000000  0.001447        0.00000                         
SCALE2      0.000000  0.011467  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008070        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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