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Database: PDB
Entry: 4K3J
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Original site: 4K3J 
HEADER    TRANSFERASE/IMMUNE SYSTEM/GROWTH FACTOR 10-APR-13   4K3J              
TITLE     CRYSTAL STRUCTURE OF ONARTUZUMAB FAB IN COMPLEX WITH MET AND HGF-BETA 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOCYTE GROWTH FACTOR;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 495-721;                                      
COMPND   5 SYNONYM: HEPATOPOIETIN-A, SCATTER FACTOR, SF, HEPATOCYTE GROWTH      
COMPND   6 FACTOR ALPHA CHAIN, HEPATOCYTE GROWTH FACTOR BETA CHAIN;             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: HEPATOCYTE GROWTH FACTOR BETA CHAIN;                       
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: SEMA AND PSI DOMAIN, UNP RESIDUES 39-564;                  
COMPND  13 SYNONYM: HGF RECEPTOR, HGF/SF RECEPTOR, PROTO-ONCOGENE C-MET, SCATTER
COMPND  14 FACTOR RECEPTOR, SF RECEPTOR, TYROSINE-PROTEIN KINASE MET;           
COMPND  15 EC: 2.7.10.1;                                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: ONARTUZUMAB FAB HEAVY CHAIN;                               
COMPND  19 CHAIN: H;                                                            
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 4;                                                           
COMPND  22 MOLECULE: ONARTUZUMAB FAB LIGHT CHAIN;                               
COMPND  23 CHAIN: L;                                                            
COMPND  24 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: HGF, HPTA;                                                     
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: MET;                                                           
SOURCE  13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE  17 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE  22 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ANTIBODY, GLYCOSYLATION, TRANSFERASE-IMMUNE SYSTEM-GROWTH FACTOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.MA,M.A.STAROVASNIK                                                  
REVDAT   3   20-AUG-14 4K3J    1       SOURCE                                   
REVDAT   2   21-MAY-14 4K3J    1       SOURCE                                   
REVDAT   1   28-AUG-13 4K3J    0                                                
JRNL        AUTH   M.MERCHANT,X.MA,H.R.MAUN,Z.ZHENG,J.PENG,M.ROMERO,A.HUANG,    
JRNL        AUTH 2 N.Y.YANG,M.NISHIMURA,J.GREVE,L.SANTELL,Y.W.ZHANG,Y.SU,       
JRNL        AUTH 3 D.W.KAUFMAN,K.L.BILLECI,E.MAI,B.MOFFAT,A.LIM,E.T.DUENAS,     
JRNL        AUTH 4 H.S.PHILLIPS,H.XIANG,J.C.YOUNG,G.F.VANDE WOUDE,M.S.DENNIS,   
JRNL        AUTH 5 D.E.REILLY,R.H.SCHWALL,M.A.STAROVASNIK,R.A.LAZARUS,          
JRNL        AUTH 6 D.G.YANSURA                                                  
JRNL        TITL   MONOVALENT ANTIBODY DESIGN AND MECHANISM OF ACTION OF        
JRNL        TITL 2 ONARTUZUMAB, A MET ANTAGONIST WITH ANTI-TUMOR ACTIVITY AS A  
JRNL        TITL 3 THERAPEUTIC AGENT.                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 E2987 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   23882082                                                     
JRNL        DOI    10.1073/PNAS.1302725110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38286                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2027                            
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) : 2739                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9084                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 183                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.20000                                              
REMARK   3    B22 (A**2) : -1.04000                                             
REMARK   3    B33 (A**2) : 0.83000                                              
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): 1.704         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.356         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.266         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.924        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9343 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12708 ; 1.050 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1157 ; 5.957 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   405 ;34.189 ;24.099       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1517 ;15.059 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    43 ;14.299 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1408 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7081 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5795 ; 0.449 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9404 ; 0.858 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3548 ; 0.982 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3304 ; 1.735 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   495        A   636                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9814  82.4719  10.1408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0842 T22:   0.0492                                     
REMARK   3      T33:   0.0850 T12:  -0.0188                                     
REMARK   3      T13:  -0.0552 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3001 L22:   3.9964                                     
REMARK   3      L33:   3.0652 L12:  -1.5194                                     
REMARK   3      L13:   1.0763 L23:  -0.3864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1140 S12:  -0.1038 S13:   0.3572                       
REMARK   3      S21:   0.3418 S22:  -0.0400 S23:  -0.5482                       
REMARK   3      S31:  -0.2103 S32:   0.3009 S33:   0.1540                       
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   637        A   661                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2122  73.3223  15.6565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5929 T22:   1.0656                                     
REMARK   3      T33:   0.9751 T12:  -0.1016                                     
REMARK   3      T13:   0.2945 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2790 L22:  10.3734                                     
REMARK   3      L33:  10.5692 L12:  -5.3119                                     
REMARK   3      L13:   5.7907 L23:   3.0046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5461 S12:  -0.8315 S13:  -1.6168                       
REMARK   3      S21:   0.6523 S22:  -1.1727 S23:   2.8729                       
REMARK   3      S31:   1.1968 S32:  -2.4249 S33:   0.6265                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   662        A   721                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.2057  77.9900  15.9030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2268 T22:   0.0954                                     
REMARK   3      T33:   0.0357 T12:   0.0009                                     
REMARK   3      T13:   0.0329 T23:  -0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3856 L22:   5.9175                                     
REMARK   3      L33:   3.9426 L12:  -3.0075                                     
REMARK   3      L13:  -0.0850 L23:  -0.5018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2614 S12:  -0.5505 S13:   0.1758                       
REMARK   3      S21:   0.8095 S22:   0.2384 S23:   0.0330                       
REMARK   3      S31:  -0.0685 S32:  -0.1070 S33:   0.0230                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    39        B   212                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4744  75.1304 -15.4946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1524 T22:   0.1255                                     
REMARK   3      T33:   0.2325 T12:  -0.0427                                     
REMARK   3      T13:  -0.0573 T23:   0.1269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4786 L22:   3.1355                                     
REMARK   3      L33:   3.2651 L12:   0.0389                                     
REMARK   3      L13:   1.4652 L23:   0.5177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1271 S12:   0.2620 S13:   0.7261                       
REMARK   3      S21:  -0.3077 S22:   0.1274 S23:   0.4358                       
REMARK   3      S31:  -0.4500 S32:  -0.1391 S33:  -0.0003                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   213        B   454                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4165  53.9394 -18.5801              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2086 T22:   0.1519                                     
REMARK   3      T33:   0.0849 T12:  -0.0271                                     
REMARK   3      T13:  -0.0196 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4827 L22:   2.8430                                     
REMARK   3      L33:   1.8266 L12:   0.3188                                     
REMARK   3      L13:   0.1294 L23:  -0.4131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0073 S12:   0.2113 S13:  -0.2474                       
REMARK   3      S21:  -0.4832 S22:   0.0487 S23:  -0.2436                       
REMARK   3      S31:   0.2747 S32:   0.2416 S33:  -0.0560                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   455        B   564                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5896  45.7405 -13.1449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4114 T22:   0.4140                                     
REMARK   3      T33:   0.5215 T12:  -0.1708                                     
REMARK   3      T13:  -0.1246 T23:   0.1382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3845 L22:   1.5216                                     
REMARK   3      L33:   0.3162 L12:   1.8694                                     
REMARK   3      L13:  -0.5272 L23:   0.0451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0481 S12:  -0.0984 S13:   0.2233                       
REMARK   3      S21:   0.1201 S22:  -0.1384 S23:   0.4562                       
REMARK   3      S31:   0.0825 S32:  -0.0494 S33:   0.1865                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   215                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1314  16.1525   7.2439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2697 T22:   0.3416                                     
REMARK   3      T33:   0.2542 T12:  -0.0196                                     
REMARK   3      T13:   0.0037 T23:   0.1154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5383 L22:   3.0625                                     
REMARK   3      L33:   1.7614 L12:  -1.0060                                     
REMARK   3      L13:   0.8158 L23:  -1.9125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2276 S12:   0.1774 S13:  -0.0158                       
REMARK   3      S21:  -0.2288 S22:  -0.3869 S23:  -0.1839                       
REMARK   3      S31:   0.1784 S32:   0.4709 S33:   0.1592                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0357  20.0800  23.7848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2632 T22:   0.2692                                     
REMARK   3      T33:   0.2412 T12:  -0.0614                                     
REMARK   3      T13:  -0.0671 T23:   0.0950                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1596 L22:   1.5618                                     
REMARK   3      L33:   1.5934 L12:  -0.9034                                     
REMARK   3      L13:   0.8713 L23:  -1.1307                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0223 S12:  -0.0798 S13:  -0.0512                       
REMARK   3      S21:   0.3284 S22:  -0.0193 S23:  -0.1078                       
REMARK   3      S31:  -0.1908 S32:   0.1812 S33:   0.0415                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4K3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078845.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40382                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5600                            
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     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.880                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SHY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE PH 6.2, 20%      
REMARK 280  (W/V) PEG 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K     
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       64.09550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       96.11400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       64.09550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       96.11400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L                            
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     HIS A   722                                                      
REMARK 465     HIS A   723                                                      
REMARK 465     HIS A   724                                                      
REMARK 465     HIS A   725                                                      
REMARK 465     HIS A   726                                                      
REMARK 465     HIS A   727                                                      
REMARK 465     GLU B   302                                                      
REMARK 465     LYS B   303                                                      
REMARK 465     ARG B   304                                                      
REMARK 465     LYS B   305                                                      
REMARK 465     LYS B   306                                                      
REMARK 465     ARG B   307                                                      
REMARK 465     SER B   308                                                      
REMARK 465     THR B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     PHE B   398                                                      
REMARK 465     ASN B   399                                                      
REMARK 465     ARG B   400                                                      
REMARK 465     THR B   401                                                      
REMARK 465     LEU B   402                                                      
REMARK 465     LEU B   403                                                      
REMARK 465     ARG B   404                                                      
REMARK 465     ASN B   405                                                      
REMARK 465     SER B   406                                                      
REMARK 465     SER B   407                                                      
REMARK 465     GLY B   408                                                      
REMARK 465     CYS B   409                                                      
REMARK 465     GLU B   410                                                      
REMARK 465     ALA B   411                                                      
REMARK 465     ARG B   412                                                      
REMARK 465     ARG B   413                                                      
REMARK 465     ASP B   414                                                      
REMARK 465     GLN B   498                                                      
REMARK 465     HIS B   565                                                      
REMARK 465     HIS B   566                                                      
REMARK 465     HIS B   567                                                      
REMARK 465     HIS B   568                                                      
REMARK 465     HIS B   569                                                      
REMARK 465     HIS B   570                                                      
REMARK 465     HIS B   571                                                      
REMARK 465     HIS B   572                                                      
REMARK 465     CYS H   216                                                      
REMARK 465     ASP H   217                                                      
REMARK 465     LYS H   218                                                      
REMARK 465     GLY L   212                                                      
REMARK 465     GLU L   213                                                      
REMARK 465     CYS L   214                                                      
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   O    THR B   495     O    ASN B   499              1.91            
REMARK 500   NH2  ARG A   647     ND1  HIS B   148              1.92            
REMARK 500   O    GLU A   608     O    ILE A   636              2.03            
REMARK 500   O    CYS B   282     O    HOH B   908              2.13            
REMARK 500   OD1  ASN B    68     C    GLY B    87              2.15            
REMARK 500   O    ARG H    66     ND2  ASN H    82A             2.18            
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    GLU A 559      -57.75   -123.03                                   
REMARK 500    ASP A 578       16.40     53.72                                   
REMARK 500    HIS A 682     -157.61    -93.42                                   
REMARK 500    ASN B  68       -4.17     69.77                                   
REMARK 500    LYS B 104       65.75   -113.20                                   
REMARK 500    THR B 151       36.35    -93.59                                   
REMARK 500    ALA B 152       11.70   -144.38                                   
REMARK 500    GLU B 167     -160.49    -76.85                                   
REMARK 500    ASN B 202     -158.83   -115.37                                   
REMARK 500    SER B 255      143.55   -172.93                                   
REMARK 500    VAL B 378     -123.56     72.27                                   
REMARK 500    LEU B 386      109.87    -57.44                                   
REMARK 500    ASN B 393       49.42   -100.41                                   
REMARK 500    TYR B 416      113.08   -170.46                                   
REMARK 500    HIS B 542      -42.02    -27.36                                   
REMARK 500    GLN B 559      -31.79   -131.24                                   
REMARK 500    PRO H  41      124.38    -39.23                                   
REMARK 500    PRO H  61      -25.96    -37.37                                   
REMARK 500    PRO H 100A    -101.28    -73.04                                   
REMARK 500    LEU H 124       77.68   -109.11                                   
REMARK 500    THR H 131      113.23    -39.71                                   
REMARK 500    ASP H 144       74.96     61.22                                   
REMARK 500    THR H 160      -30.35   -138.05                                   
REMARK 500    ALA L  51      -39.17     65.42                                   
REMARK 500    SER L  77       56.50     39.67                                   
REMARK 500    ALA L  84     -175.58    176.85                                   
REMARK 500    GLU L 143      108.84    -58.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 818        DISTANCE =  7.43 ANGSTROMS                       
REMARK 525    HOH A 822        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A 849        DISTANCE =  7.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 801                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SHY   RELATED DB: PDB                                   
DBREF  4K3J A  495   721  UNP    P14210   HGF_HUMAN      495    721             
DBREF  4K3J B   39   564  UNP    P08581   MET_HUMAN       39    564             
DBREF  4K3J H    1   218  PDB    4K3J     4K3J             1    218             
DBREF  4K3J L    1   214  PDB    4K3J     4K3J             1    214             
SEQADV 4K3J SER A  604  UNP  P14210    CYS   604 ENGINEERED MUTATION            
SEQADV 4K3J HIS A  722  UNP  P14210              EXPRESSION TAG                 
SEQADV 4K3J HIS A  723  UNP  P14210              EXPRESSION TAG                 
SEQADV 4K3J HIS A  724  UNP  P14210              EXPRESSION TAG                 
SEQADV 4K3J HIS A  725  UNP  P14210              EXPRESSION TAG                 
SEQADV 4K3J HIS A  726  UNP  P14210              EXPRESSION TAG                 
SEQADV 4K3J HIS A  727  UNP  P14210              EXPRESSION TAG                 
SEQADV 4K3J HIS B  565  UNP  P08581              EXPRESSION TAG                 
SEQADV 4K3J HIS B  566  UNP  P08581              EXPRESSION TAG                 
SEQADV 4K3J HIS B  567  UNP  P08581              EXPRESSION TAG                 
SEQADV 4K3J HIS B  568  UNP  P08581              EXPRESSION TAG                 
SEQADV 4K3J HIS B  569  UNP  P08581              EXPRESSION TAG                 
SEQADV 4K3J HIS B  570  UNP  P08581              EXPRESSION TAG                 
SEQADV 4K3J HIS B  571  UNP  P08581              EXPRESSION TAG                 
SEQADV 4K3J HIS B  572  UNP  P08581              EXPRESSION TAG                 
SEQRES   1 A  233  VAL VAL ASN GLY ILE PRO THR ARG THR ASN ILE GLY TRP          
SEQRES   2 A  233  MET VAL SER LEU ARG TYR ARG ASN LYS HIS ILE CYS GLY          
SEQRES   3 A  233  GLY SER LEU ILE LYS GLU SER TRP VAL LEU THR ALA ARG          
SEQRES   4 A  233  GLN CYS PHE PRO SER ARG ASP LEU LYS ASP TYR GLU ALA          
SEQRES   5 A  233  TRP LEU GLY ILE HIS ASP VAL HIS GLY ARG GLY ASP GLU          
SEQRES   6 A  233  LYS CYS LYS GLN VAL LEU ASN VAL SER GLN LEU VAL TYR          
SEQRES   7 A  233  GLY PRO GLU GLY SER ASP LEU VAL LEU MET LYS LEU ALA          
SEQRES   8 A  233  ARG PRO ALA VAL LEU ASP ASP PHE VAL SER THR ILE ASP          
SEQRES   9 A  233  LEU PRO ASN TYR GLY SER THR ILE PRO GLU LYS THR SER          
SEQRES  10 A  233  CYS SER VAL TYR GLY TRP GLY TYR THR GLY LEU ILE ASN          
SEQRES  11 A  233  TYR ASP GLY LEU LEU ARG VAL ALA HIS LEU TYR ILE MET          
SEQRES  12 A  233  GLY ASN GLU LYS CYS SER GLN HIS HIS ARG GLY LYS VAL          
SEQRES  13 A  233  THR LEU ASN GLU SER GLU ILE CYS ALA GLY ALA GLU LYS          
SEQRES  14 A  233  ILE GLY SER GLY PRO CYS GLU GLY ASP TYR GLY GLY PRO          
SEQRES  15 A  233  LEU VAL CYS GLU GLN HIS LYS MET ARG MET VAL LEU GLY          
SEQRES  16 A  233  VAL ILE VAL PRO GLY ARG GLY CYS ALA ILE PRO ASN ARG          
SEQRES  17 A  233  PRO GLY ILE PHE VAL ARG VAL ALA TYR TYR ALA LYS TRP          
SEQRES  18 A  233  ILE HIS LYS ILE ILE LEU HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  534  MET LYS TYR GLN LEU PRO ASN PHE THR ALA GLU THR PRO          
SEQRES   2 B  534  ILE GLN ASN VAL ILE LEU HIS GLU HIS HIS ILE PHE LEU          
SEQRES   3 B  534  GLY ALA THR ASN TYR ILE TYR VAL LEU ASN GLU GLU ASP          
SEQRES   4 B  534  LEU GLN LYS VAL ALA GLU TYR LYS THR GLY PRO VAL LEU          
SEQRES   5 B  534  GLU HIS PRO ASP CYS PHE PRO CYS GLN ASP CYS SER SER          
SEQRES   6 B  534  LYS ALA ASN LEU SER GLY GLY VAL TRP LYS ASP ASN ILE          
SEQRES   7 B  534  ASN MET ALA LEU VAL VAL ASP THR TYR TYR ASP ASP GLN          
SEQRES   8 B  534  LEU ILE SER CYS GLY SER VAL ASN ARG GLY THR CYS GLN          
SEQRES   9 B  534  ARG HIS VAL PHE PRO HIS ASN HIS THR ALA ASP ILE GLN          
SEQRES  10 B  534  SER GLU VAL HIS CYS ILE PHE SER PRO GLN ILE GLU GLU          
SEQRES  11 B  534  PRO SER GLN CYS PRO ASP CYS VAL VAL SER ALA LEU GLY          
SEQRES  12 B  534  ALA LYS VAL LEU SER SER VAL LYS ASP ARG PHE ILE ASN          
SEQRES  13 B  534  PHE PHE VAL GLY ASN THR ILE ASN SER SER TYR PHE PRO          
SEQRES  14 B  534  ASP HIS PRO LEU HIS SER ILE SER VAL ARG ARG LEU LYS          
SEQRES  15 B  534  GLU THR LYS ASP GLY PHE MET PHE LEU THR ASP GLN SER          
SEQRES  16 B  534  TYR ILE ASP VAL LEU PRO GLU PHE ARG ASP SER TYR PRO          
SEQRES  17 B  534  ILE LYS TYR VAL HIS ALA PHE GLU SER ASN ASN PHE ILE          
SEQRES  18 B  534  TYR PHE LEU THR VAL GLN ARG GLU THR LEU ASP ALA GLN          
SEQRES  19 B  534  THR PHE HIS THR ARG ILE ILE ARG PHE CYS SER ILE ASN          
SEQRES  20 B  534  SER GLY LEU HIS SER TYR MET GLU MET PRO LEU GLU CYS          
SEQRES  21 B  534  ILE LEU THR GLU LYS ARG LYS LYS ARG SER THR LYS LYS          
SEQRES  22 B  534  GLU VAL PHE ASN ILE LEU GLN ALA ALA TYR VAL SER LYS          
SEQRES  23 B  534  PRO GLY ALA GLN LEU ALA ARG GLN ILE GLY ALA SER LEU          
SEQRES  24 B  534  ASN ASP ASP ILE LEU PHE GLY VAL PHE ALA GLN SER LYS          
SEQRES  25 B  534  PRO ASP SER ALA GLU PRO MET ASP ARG SER ALA MET CYS          
SEQRES  26 B  534  ALA PHE PRO ILE LYS TYR VAL ASN ASP PHE PHE ASN LYS          
SEQRES  27 B  534  ILE VAL ASN LYS ASN ASN VAL ARG CYS LEU GLN HIS PHE          
SEQRES  28 B  534  TYR GLY PRO ASN HIS GLU HIS CYS PHE ASN ARG THR LEU          
SEQRES  29 B  534  LEU ARG ASN SER SER GLY CYS GLU ALA ARG ARG ASP GLU          
SEQRES  30 B  534  TYR ARG THR GLU PHE THR THR ALA LEU GLN ARG VAL ASP          
SEQRES  31 B  534  LEU PHE MET GLY GLN PHE SER GLU VAL LEU LEU THR SER          
SEQRES  32 B  534  ILE SER THR PHE ILE LYS GLY ASP LEU THR ILE ALA ASN          
SEQRES  33 B  534  LEU GLY THR SER GLU GLY ARG PHE MET GLN VAL VAL VAL          
SEQRES  34 B  534  SER ARG SER GLY PRO SER THR PRO HIS VAL ASN PHE LEU          
SEQRES  35 B  534  LEU ASP SER HIS PRO VAL SER PRO GLU VAL ILE VAL GLU          
SEQRES  36 B  534  HIS THR LEU ASN GLN ASN GLY TYR THR LEU VAL ILE THR          
SEQRES  37 B  534  GLY LYS LYS ILE THR LYS ILE PRO LEU ASN GLY LEU GLY          
SEQRES  38 B  534  CYS ARG HIS PHE GLN SER CYS SER GLN CYS LEU SER ALA          
SEQRES  39 B  534  PRO PRO PHE VAL GLN CYS GLY TRP CYS HIS ASP LYS CYS          
SEQRES  40 B  534  VAL ARG SER GLU GLU CYS LEU SER GLY THR TRP THR GLN          
SEQRES  41 B  534  GLN ILE CYS LEU PRO ALA HIS HIS HIS HIS HIS HIS HIS          
SEQRES  42 B  534  HIS                                                          
SEQRES   1 H  224  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  224  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  224  TYR THR PHE THR SER TYR TRP LEU HIS TRP VAL ARG GLN          
SEQRES   4 H  224  ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY MET ILE ASP          
SEQRES   5 H  224  PRO SER ASN SER ASP THR ARG PHE ASN PRO ASN PHE LYS          
SEQRES   6 H  224  ASP ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR          
SEQRES   7 H  224  ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 H  224  ALA VAL TYR TYR CYS ALA THR TYR ARG SER TYR VAL THR          
SEQRES   9 H  224  PRO LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL          
SEQRES  10 H  224  SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU          
SEQRES  11 H  224  ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA          
SEQRES  12 H  224  LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  224  THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL          
SEQRES  14 H  224  HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR          
SEQRES  15 H  224  SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU          
SEQRES  16 H  224  GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO          
SEQRES  17 H  224  SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER          
SEQRES  18 H  224  CYS ASP LYS                                                  
SEQRES   1 L  220  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  220  SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS SER SER          
SEQRES   3 L  220  GLN SER LEU LEU TYR THR SER SER GLN LYS ASN TYR LEU          
SEQRES   4 L  220  ALA TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU          
SEQRES   5 L  220  LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO          
SEQRES   6 L  220  SER ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR          
SEQRES   7 L  220  LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE ALA THR          
SEQRES   8 L  220  TYR TYR CYS GLN GLN TYR TYR ALA TYR PRO TRP THR PHE          
SEQRES   9 L  220  GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA          
SEQRES  10 L  220  ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN          
SEQRES  11 L  220  LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN          
SEQRES  12 L  220  ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL          
SEQRES  13 L  220  ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL          
SEQRES  14 L  220  THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER          
SEQRES  15 L  220  SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS          
SEQRES  16 L  220  LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER          
SEQRES  17 L  220  SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS              
MODRES 4K3J ASN B   45  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B 801      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  NAG    C8 H15 N O6                                                  
FORMUL   6  HOH   *183(H2 O)                                                    
HELIX    1   1 GLN A  534  PHE A  536  5                                   3    
HELIX    2   2 ASP A  540  LYS A  542  5                                   3    
HELIX    3   3 GLY A  638  HIS A  646  1                                   9    
HELIX    4   4 TYR A  712  LEU A  721  1                                  10    
HELIX    5   5 VAL B  136  GLY B  139  5                                   4    
HELIX    6   6 LEU B  238  ARG B  242  5                                   5    
HELIX    7   7 GLY B  326  GLY B  334  1                                   9    
HELIX    8   8 ILE B  367  LYS B  376  1                                  10    
HELIX    9   9 ASN B  379  ASN B  381  5                                   3    
HELIX   10  10 GLY B  517  HIS B  522  1                                   6    
HELIX   11  11 SER B  525  SER B  531  1                                   7    
HELIX   12  12 ALA B  532  VAL B  536  5                                   5    
HELIX   13  13 GLU B  549  CYS B  551  5                                   3    
HELIX   14  14 THR H   28  TYR H   32  5                                   5    
HELIX   15  15 THR H   73  LYS H   75  5                                   3    
HELIX   16  16 ARG H   83  THR H   87  5                                   5    
HELIX   17  17 SER H  187  LEU H  189  5                                   3    
HELIX   18  18 GLN L   79  PHE L   83  5                                   5    
HELIX   19  19 SER L  121  LYS L  126  1                                   6    
HELIX   20  20 LYS L  183  LYS L  188  1                                   6    
SHEET    1   A 8 ILE A 499  PRO A 500  0                                        
SHEET    2   A 8 ARG A 630  MET A 637 -1  O  VAL A 631   N  ILE A 499           
SHEET    3   A 8 GLU A 656  GLY A 660 -1  O  CYS A 658   N  MET A 637           
SHEET    4   A 8 GLY A 704  ARG A 708 -1  O  GLY A 704   N  ALA A 659           
SHEET    5   A 8 MET A 686  ILE A 691 -1  N  VAL A 690   O  VAL A 707           
SHEET    6   A 8 PRO A 676  CYS A 679 -1  N  LEU A 677   O  GLY A 689           
SHEET    7   A 8 SER A 611  GLY A 616 -1  N  SER A 613   O  VAL A 678           
SHEET    8   A 8 ARG A 630  MET A 637 -1  O  LEU A 634   N  CYS A 612           
SHEET    1   B 7 MET A 508  TYR A 513  0                                        
SHEET    2   B 7 LYS A 516  LYS A 525 -1  O  ILE A 518   N  LEU A 511           
SHEET    3   B 7 TRP A 528  ALA A 532 -1  O  LEU A 530   N  SER A 522           
SHEET    4   B 7 LEU A 579  LEU A 584 -1  O  MET A 582   N  VAL A 529           
SHEET    5   B 7 GLN A 563  TYR A 572 -1  N  SER A 568   O  LYS A 583           
SHEET    6   B 7 TYR A 544  LEU A 548 -1  N  ALA A 546   O  LEU A 565           
SHEET    7   B 7 MET A 508  TYR A 513 -1  N  ARG A 512   O  GLU A 545           
SHEET    1   C 4 ASN B  45  THR B  47  0                                        
SHEET    2   C 4 LYS B 509  PRO B 514 -1  O  ILE B 510   N  PHE B  46           
SHEET    3   C 4 TYR B 501  THR B 506 -1  N  VAL B 504   O  THR B 511           
SHEET    4   C 4 ILE B 491  GLU B 493 -1  N  GLU B 493   O  TYR B 501           
SHEET    1   D 4 ILE B  52  HIS B  58  0                                        
SHEET    2   D 4 HIS B  61  ALA B  66 -1  O  GLY B  65   N  ASN B  54           
SHEET    3   D 4 TYR B  69  ASN B  74 -1  O  LEU B  73   N  ILE B  62           
SHEET    4   D 4 LYS B  80  LYS B  85 -1  O  VAL B  81   N  VAL B  72           
SHEET    1   E 2 VAL B  89  GLU B  91  0                                        
SHEET    2   E 2 VAL B 111  LYS B 113 -1  O  LYS B 113   N  VAL B  89           
SHEET    1   F 4 ASN B 117  ASP B 123  0                                        
SHEET    2   F 4 GLN B 129  GLY B 134 -1  O  ILE B 131   N  VAL B 121           
SHEET    3   F 4 CYS B 141  VAL B 145 -1  O  HIS B 144   N  LEU B 130           
SHEET    4   F 4 VAL B 158  CYS B 160 -1  O  HIS B 159   N  ARG B 143           
SHEET    1   G 4 ALA B 182  LYS B 189  0                                        
SHEET    2   G 4 PHE B 192  ASN B 199 -1  O  PHE B 196   N  LEU B 185           
SHEET    3   G 4 ILE B 214  LEU B 219 -1  O  ARG B 217   N  PHE B 195           
SHEET    4   G 4 PHE B 226  MET B 227 -1  O  MET B 227   N  ARG B 218           
SHEET    1   H 4 ALA B 182  LYS B 189  0                                        
SHEET    2   H 4 PHE B 192  ASN B 199 -1  O  PHE B 196   N  LEU B 185           
SHEET    3   H 4 ILE B 214  LEU B 219 -1  O  ARG B 217   N  PHE B 195           
SHEET    4   H 4 TYR B 234  ILE B 235 -1  O  ILE B 235   N  ILE B 214           
SHEET    1   I 6 LYS B 248  SER B 255  0                                        
SHEET    2   I 6 PHE B 258  ARG B 266 -1  O  TYR B 260   N  PHE B 253           
SHEET    3   I 6 PHE B 274  CYS B 282 -1  O  ILE B 279   N  PHE B 261           
SHEET    4   I 6 HIS B 289  LEU B 300 -1  O  MET B 294   N  ILE B 278           
SHEET    5   I 6 THR B 418  PHE B 420  1  O  PHE B 420   N  GLU B 293           
SHEET    6   I 6 VAL B 383  CYS B 385 -1  N  ARG B 384   O  GLU B 419           
SHEET    1   J 3 GLU B 312  PHE B 314  0                                        
SHEET    2   J 3 HIS B 289  LEU B 300 -1  N  CYS B 298   O  PHE B 314           
SHEET    3   J 3 LEU B 424  VAL B 427  1  O  LEU B 424   N  PRO B 295           
SHEET    1   K 3 ILE B 316  SER B 323  0                                        
SHEET    2   K 3 ILE B 341  SER B 349 -1  O  VAL B 345   N  GLN B 318           
SHEET    3   K 3 PRO B 356  PRO B 366 -1  O  ALA B 361   N  PHE B 346           
SHEET    1   L 4 LEU B 439  LYS B 447  0                                        
SHEET    2   L 4 LEU B 450  THR B 457 -1  O  ILE B 452   N  PHE B 445           
SHEET    3   L 4 ARG B 461  VAL B 466 -1  O  MET B 463   N  LEU B 455           
SHEET    4   L 4 VAL B 477  LEU B 480 -1  O  PHE B 479   N  PHE B 462           
SHEET    1   M 3 LYS B 544  ARG B 547  0                                        
SHEET    2   M 3 CYS B 538  CYS B 541 -1  N  CYS B 541   O  LYS B 544           
SHEET    3   M 3 TRP B 556  THR B 557 -1  O  THR B 557   N  TRP B 540           
SHEET    1   N 4 GLN H   3  SER H   7  0                                        
SHEET    2   N 4 LEU H  18  SER H  25 -1  O  SER H  21   N  SER H   7           
SHEET    3   N 4 THR H  77  MET H  82 -1  O  LEU H  80   N  LEU H  20           
SHEET    4   N 4 PHE H  67  ASP H  72 -1  N  THR H  68   O  GLN H  81           
SHEET    1   O 6 GLY H  10  VAL H  12  0                                        
SHEET    2   O 6 THR H 107  VAL H 111  1  O  THR H 110   N  GLY H  10           
SHEET    3   O 6 ALA H  88  THR H  94 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   O 6 LEU H  34  GLN H  39 -1  N  VAL H  37   O  TYR H  91           
SHEET    5   O 6 LEU H  45  ILE H  51 -1  O  GLU H  46   N  ARG H  38           
SHEET    6   O 6 THR H  57  PHE H  59 -1  O  ARG H  58   N  MET H  50           
SHEET    1   P 4 GLY H  10  VAL H  12  0                                        
SHEET    2   P 4 THR H 107  VAL H 111  1  O  THR H 110   N  GLY H  10           
SHEET    3   P 4 ALA H  88  THR H  94 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   P 4 TYR H 102  TRP H 103 -1  O  TYR H 102   N  THR H  94           
SHEET    1   Q 4 SER H 120  LEU H 124  0                                        
SHEET    2   Q 4 THR H 135  TYR H 145 -1  O  LEU H 141   N  PHE H 122           
SHEET    3   Q 4 TYR H 176  PRO H 185 -1  O  VAL H 184   N  ALA H 136           
SHEET    4   Q 4 VAL H 163  THR H 165 -1  N  HIS H 164   O  VAL H 181           
SHEET    1   R 4 SER H 120  LEU H 124  0                                        
SHEET    2   R 4 THR H 135  TYR H 145 -1  O  LEU H 141   N  PHE H 122           
SHEET    3   R 4 TYR H 176  PRO H 185 -1  O  VAL H 184   N  ALA H 136           
SHEET    4   R 4 VAL H 169  LEU H 170 -1  N  VAL H 169   O  SER H 177           
SHEET    1   S 3 THR H 151  TRP H 154  0                                        
SHEET    2   S 3 TYR H 194  HIS H 200 -1  O  ASN H 197   N  SER H 153           
SHEET    3   S 3 THR H 205  VAL H 211 -1  O  VAL H 207   N  VAL H 198           
SHEET    1   T 4 MET L   4  SER L   7  0                                        
SHEET    2   T 4 VAL L  19  SER L  25 -1  O  THR L  22   N  SER L   7           
SHEET    3   T 4 ASP L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4   T 4 PHE L  62  SER L  67 -1  N  SER L  65   O  THR L  72           
SHEET    1   U 6 SER L  10  SER L  14  0                                        
SHEET    2   U 6 THR L 102  LYS L 107  1  O  GLU L 105   N  LEU L  11           
SHEET    3   U 6 ALA L  84  GLN L  90 -1  N  ALA L  84   O  VAL L 104           
SHEET    4   U 6 LEU L  33  GLN L  38 -1  N  TYR L  36   O  TYR L  87           
SHEET    5   U 6 LYS L  45  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6   U 6 THR L  53  ARG L  54 -1  O  THR L  53   N  TYR L  49           
SHEET    1   V 4 SER L  10  SER L  14  0                                        
SHEET    2   V 4 THR L 102  LYS L 107  1  O  GLU L 105   N  LEU L  11           
SHEET    3   V 4 ALA L  84  GLN L  90 -1  N  ALA L  84   O  VAL L 104           
SHEET    4   V 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   W 2 LEU L  27C TYR L  27D 0                                        
SHEET    2   W 2 LYS L  30  ASN L  31 -1  O  LYS L  30   N  TYR L  27D          
SHEET    1   X 4 SER L 114  PHE L 118  0                                        
SHEET    2   X 4 THR L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3   X 4 TYR L 173  SER L 182 -1  O  LEU L 179   N  VAL L 132           
SHEET    4   X 4 SER L 159  VAL L 163 -1  N  GLN L 160   O  THR L 178           
SHEET    1   Y 4 ALA L 153  LEU L 154  0                                        
SHEET    2   Y 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3   Y 4 VAL L 191  THR L 197 -1  O  ALA L 193   N  LYS L 149           
SHEET    4   Y 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SSBOND   1 CYS A  519    CYS A  535                          1555   1555  2.03  
SSBOND   2 CYS A  612    CYS A  679                          1555   1555  2.06  
SSBOND   3 CYS A  642    CYS A  658                          1555   1555  2.02  
SSBOND   4 CYS A  669    CYS A  697                          1555   1555  2.06  
SSBOND   5 CYS B   95    CYS B  101                          1555   1555  1.99  
SSBOND   6 CYS B   98    CYS B  160                          1555   1555  1.99  
SSBOND   7 CYS B  133    CYS B  141                          1555   1555  2.03  
SSBOND   8 CYS B  172    CYS B  175                          1555   1555  2.04  
SSBOND   9 CYS B  298    CYS B  363                          1555   1555  2.05  
SSBOND  10 CYS B  385    CYS B  397                          1555   1555  2.04  
SSBOND  11 CYS B  520    CYS B  538                          1555   1555  2.06  
SSBOND  12 CYS B  526    CYS B  561                          1555   1555  2.02  
SSBOND  13 CYS B  529    CYS B  545                          1555   1555  2.05  
SSBOND  14 CYS B  541    CYS B  551                          1555   1555  2.08  
SSBOND  15 CYS H   22    CYS H   92                          1555   1555  2.05  
SSBOND  16 CYS H  140    CYS H  196                          1555   1555  2.03  
SSBOND  17 CYS L   23    CYS L   88                          1555   1555  2.06  
SSBOND  18 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         ND2 ASN B  45                 C1  NAG B 801     1555   1555  1.44  
CISPEP   1 GLY B   87    PRO B   88          0         2.48                     
CISPEP   2 PHE H  146    PRO H  147          0        -5.74                     
CISPEP   3 GLU H  148    PRO H  149          0         0.70                     
CISPEP   4 SER L    7    PRO L    8          0        -2.04                     
CISPEP   5 TYR L   94    PRO L   95          0        -0.44                     
CISPEP   6 TYR L  140    PRO L  141          0        -0.70                     
SITE     1 AC1  4 GLN B  42  LEU B  43  ASN B  45  HOH B 957                    
CRYST1  128.191  192.228   65.585  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      0.007801  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005202  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015247        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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