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Database: PDB
Entry: 4D3C
LinkDB: 4D3C
Original site: 4D3C 
HEADER    PROTEIN BINDING                         21-OCT-14   4D3C              
TITLE     CRYSTAL STRUCTURE OF THE NK1 DOMAIN OF HGF IN COMPLEX WITH ANTI-HGF   
TITLE    2 MONOCLONAL ANTIBODY SFN68.                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOCYTE GROWTH FACTOR;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 23-210;                                           
COMPND   5 SYNONYM: HEPATOPOIETIN-A, SCATTER FACTOR, SF, NK1;                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SFN68 FAB;                                                 
COMPND  10 CHAIN: H;                                                            
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: SFN68 FAB;                                                 
COMPND  13 CHAIN: L                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   9 ORGANISM_COMMON: RABBIT;                                             
SOURCE  10 ORGANISM_TAXID: 9986;                                                
SOURCE  11 OTHER_DETAILS: RABBIT/HUMAN CHIMERIC ANTIBODY;                       
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE  14 ORGANISM_COMMON: RABBIT;                                             
SOURCE  15 ORGANISM_TAXID: 9986;                                                
SOURCE  16 OTHER_DETAILS: RABBIT/HUMAN CHIMERIC ANTIBODY                        
KEYWDS    PROTEIN BINDING                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.J.KANG,K.L.KIM,H.S.CHO,J.H.CHUNG                                    
REVDAT   2   29-AUG-18 4D3C    1       JRNL                                     
REVDAT   1   13-JAN-16 4D3C    0                                                
JRNL        AUTH   Y.J.KANG,K.L.KIM,H.S.CHO,J.H.CHUNG                           
JRNL        TITL   A MECHANISTIC BASIS FOR CONVERTING A RECEPTOR TYROSINE       
JRNL        TITL 2 KINASE AGONIST TO AN ANTAGONIST.                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25541                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.269                           
REMARK   3   R VALUE            (WORKING SET) : 0.268                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1347                            
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) : 2.62                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1586                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 92                           
REMARK   3   BIN FREE R VALUE                    : 0.4260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4225                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 22                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 85.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.12000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : -1.11000                                             
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): 0.511         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.328         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.318         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.560        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4329 ; 0.012 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3967 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5882 ; 1.456 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9161 ; 0.835 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   549 ; 6.150 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;34.490 ;24.360       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   691 ;15.563 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;15.611 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   655 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4910 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   977 ; 0.002 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4D3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290061983.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 93.15                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
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          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25541                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.620                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRIES 1JPT, 1NK1.                              
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       35.35650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.35650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.35150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      148.84600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.35150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      148.84600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       35.35650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.35150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      148.84600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       35.35650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.35150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      148.84600            
REMARK 290   SMTRY3   8  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     MET A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     HIS A    26                                                      
REMARK 465     HIS A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     GLN A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     LYS A    34                                                      
REMARK 465     ARG A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     THR A    49                                                      
REMARK 465     LEU A    50                                                      
REMARK 465     ILE A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     ILE A    53                                                      
REMARK 465     ASP A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     LEU A    57                                                      
REMARK 465     LYS A    58                                                      
REMARK 465     ILE A    59                                                      
REMARK 465     LYS A    60                                                      
REMARK 465     THR A    61                                                      
REMARK 465     LYS A    62                                                      
REMARK 465     LYS A    63                                                      
REMARK 465     VAL A    64                                                      
REMARK 465     ASN A    65                                                      
REMARK 465     THR A    66                                                      
REMARK 465     ASP A    90                                                      
REMARK 465     LYS A    91                                                      
REMARK 465     ALA A    92                                                      
REMARK 465     ARG A    93                                                      
REMARK 465     LYS A    94                                                      
REMARK 465     GLN A    95                                                      
REMARK 465     SER A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     VAL A   108                                                      
REMARK 465     LYS A   109                                                      
REMARK 465     LYS A   110                                                      
REMARK 465     GLU A   111                                                      
REMARK 465     PHE A   112                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     HIS A   114                                                      
REMARK 465     GLU A   115                                                      
REMARK 465     PHE A   116                                                      
REMARK 465     VAL A   209                                                      
REMARK 465     GLU A   210                                                      
REMARK 465     SER H   131                                                      
REMARK 465     ARG H   132                                                      
REMARK 465     SER H   133                                                      
REMARK 465     THR H   134                                                      
REMARK 465     SER H   135                                                      
REMARK 465     GLU H   136                                                      
REMARK 465     LYS H   217                                                      
REMARK 465     TYR H   218                                                      
REMARK 465     PHE L   210                                                      
REMARK 465     ASN L   211                                                      
REMARK 465     ARG L   212                                                      
REMARK 465     GLY L   213                                                      
REMARK 465     GLU L   214                                                      
REMARK 465     CYS L   215                                                      
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    LEU L    33     O    GLY L    50              1.83            
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    TYR H 148   CG    TYR H 148   CD1    -0.118                       
REMARK 500    CYS H 199   CB    CYS H 199   SG     -0.102                       
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    GLY L  77   N   -  CA  -  C   ANGL. DEV. = -17.8 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    PRO A 100       39.54    -92.15                                   
REMARK 500    ASN A 127       34.38    -85.09                                   
REMARK 500    LYS A 137       22.87   -150.21                                   
REMARK 500    SER A 141       37.42   -142.24                                   
REMARK 500    SER A 161       72.06   -105.93                                   
REMARK 500    ASP A 171       78.09     58.03                                   
REMARK 500    GLU A 174     -137.14     50.57                                   
REMARK 500    SER H  30      -48.64   -134.51                                   
REMARK 500    THR H  31       -5.45     91.82                                   
REMARK 500    VAL H  64      -31.70   -141.76                                   
REMARK 500    LEU H 100      -60.70   -124.90                                   
REMARK 500    THR H 194      -62.31    -98.06                                   
REMARK 500    SER L  30       72.03     60.95                                   
REMARK 500    ASN L  31       13.35     51.67                                   
REMARK 500    LEU L  47      -63.08   -103.69                                   
REMARK 500    ALA L  83      105.46    -57.93                                   
REMARK 500    SER L  94      143.83   -171.62                                   
REMARK 500    ALA L  97      135.92   -175.79                                   
REMARK 500    ASN L 139       78.86     51.13                                   
REMARK 500    ASP L 152       53.14     32.83                                   
REMARK 500    ASN L 153       24.40   -155.89                                   
REMARK 500    LEU L 155       25.33     45.94                                   
REMARK 500    GLN L 156      105.77    -55.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4D3C A   32   210  UNP    P14210   HGF_HUMAN       32    210             
DBREF  4D3C H    1   218  PDB    4D3C     4D3C             1    218             
DBREF  4D3C L    1   215  PDB    4D3C     4D3C             1    215             
SEQADV 4D3C MET A   18  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C GLY A   19  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C SER A   20  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C SER A   21  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C HIS A   22  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C HIS A   23  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C HIS A   24  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C HIS A   25  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C HIS A   26  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C HIS A   27  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C SER A   28  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C GLN A   29  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C ASP A   30  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C PRO A   31  UNP  P14210              EXPRESSION TAG                 
SEQADV 4D3C GLY A  134  UNP  P14210    ARG   134 ENGINEERED MUTATION            
SEQRES   1 A  193  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  193  PRO GLN ARG LYS ARG ARG ASN THR ILE HIS GLU PHE LYS          
SEQRES   3 A  193  LYS SER ALA LYS THR THR LEU ILE LYS ILE ASP PRO ALA          
SEQRES   4 A  193  LEU LYS ILE LYS THR LYS LYS VAL ASN THR ALA ASP GLN          
SEQRES   5 A  193  CYS ALA ASN ARG CYS THR ARG ASN LYS GLY LEU PRO PHE          
SEQRES   6 A  193  THR CYS LYS ALA PHE VAL PHE ASP LYS ALA ARG LYS GLN          
SEQRES   7 A  193  CYS LEU TRP PHE PRO PHE ASN SER MET SER SER GLY VAL          
SEQRES   8 A  193  LYS LYS GLU PHE GLY HIS GLU PHE ASP LEU TYR GLU ASN          
SEQRES   9 A  193  LYS ASP TYR ILE ARG ASN CYS ILE ILE GLY LYS GLY GLY          
SEQRES  10 A  193  SER TYR LYS GLY THR VAL SER ILE THR LYS SER GLY ILE          
SEQRES  11 A  193  LYS CYS GLN PRO TRP SER SER MET ILE PRO HIS GLU HIS          
SEQRES  12 A  193  SER PHE LEU PRO SER SER TYR ARG GLY LYS ASP LEU GLN          
SEQRES  13 A  193  GLU ASN TYR CYS ARG ASN PRO ARG GLY GLU GLU GLY GLY          
SEQRES  14 A  193  PRO TRP CYS PHE THR SER ASN PRO GLU VAL ARG TYR GLU          
SEQRES  15 A  193  VAL CYS ASP ILE PRO GLN CYS SER GLU VAL GLU                  
SEQRES   1 H  218  GLN GLN GLN LEU VAL GLU SER GLY GLY ARG LEU VAL ASN          
SEQRES   2 H  218  PRO GLY GLU SER LEU THR LEU THR CYS LYS ALA SER GLY          
SEQRES   3 H  218  PHE THR PHE SER THR TYR TYR MET SER TRP VAL ARG GLN          
SEQRES   4 H  218  ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE GLY          
SEQRES   5 H  218  THR SER SER GLY THR THR TYR TYR ALA ASN SER VAL LYS          
SEQRES   6 H  218  GLY ARG PHE THR ILE SER SER ASP ASN ALA GLN ASN THR          
SEQRES   7 H  218  VAL PHE LEU GLN MET THR SER LEU THR ASP SER ASP THR          
SEQRES   8 H  218  ALA THR TYR PHE CYS ALA ARG GLY LEU GLY ARG ILE ASN          
SEQRES   9 H  218  LEU TRP GLY PRO GLY THR LEU VAL THR VAL SER SER ALA          
SEQRES  10 H  218  SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO CYS          
SEQRES  11 H  218  SER ARG SER THR SER GLU SER THR ALA ALA LEU GLY CYS          
SEQRES  12 H  218  LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER          
SEQRES  13 H  218  TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE          
SEQRES  14 H  218  PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER          
SEQRES  15 H  218  SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR LYS          
SEQRES  16 H  218  THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER ASN THR          
SEQRES  17 H  218  LYS VAL ASP LYS ARG VAL GLU SER LYS TYR                      
SEQRES   1 L  215  GLU LEU ASP LEU THR GLN THR PRO SER SER VAL SER ALA          
SEQRES   2 L  215  ALA VAL GLY GLY THR VAL THR ILE ASN CYS GLN ALA SER          
SEQRES   3 L  215  GLN SER VAL SER ASN LEU LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  215  PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR GLY ALA SER          
SEQRES   5 L  215  ASN LEU GLU SER GLY VAL PRO SER ARG PHE ARG GLY SER          
SEQRES   6 L  215  GLY SER GLY THR GLU PHE THR LEU THR ILE SER GLY MET          
SEQRES   7 L  215  LYS ALA GLU ASP ALA ALA THR TYR TYR CYS GLN SER GLY          
SEQRES   8 L  215  TYR TYR SER ALA GLY ALA THR PHE GLY ALA GLY THR ASN          
SEQRES   9 L  215  VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE          
SEQRES  10 L  215  ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR          
SEQRES  11 L  215  ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG          
SEQRES  12 L  215  GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN          
SEQRES  13 L  215  SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER          
SEQRES  14 L  215  LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU          
SEQRES  15 L  215  SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS          
SEQRES  16 L  215  GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS          
SEQRES  17 L  215  SER PHE ASN ARG GLY GLU CYS                                  
FORMUL   4  HOH   *22(H2 O)                                                     
HELIX    1   1 ALA A   67  ARG A   76  1                                  10    
HELIX    2   2 ASP A  123  ILE A  125  5                                   3    
HELIX    3   3 ASN H   74  GLN H   76  5                                   3    
HELIX    4   4 THR H   87  THR H   91  5                                   5    
HELIX    5   5 SER H  159  ALA H  161  5                                   3    
HELIX    6   6 SER H  190  GLY H  193  5                                   4    
HELIX    7   7 LYS L   79  ALA L   83  5                                   5    
HELIX    8   8 SER L  122  SER L  128  1                                   7    
HELIX    9   9 LYS L  184  HIS L  190  1                                   7    
SHEET    1  AA 4 PHE A  42  SER A  45  0                                        
SHEET    2  AA 4 LEU A 118  ASN A 121 -1  O  LEU A 118   N  SER A  45           
SHEET    3  AA 4 ALA A  86  VAL A  88 -1  O  PHE A  87   N  TYR A 119           
SHEET    4  AA 4 LEU A  97  PHE A  99 -1  O  LEU A  97   N  VAL A  88           
SHEET    1  AB 2 TRP A 188  PHE A 190  0                                        
SHEET    2  AB 2 TYR A 198  VAL A 200 -1  O  GLU A 199   N  CYS A 189           
SHEET    1  HA 4 GLN H   3  SER H   7  0                                        
SHEET    2  HA 4 LEU H  18  SER H  25 -1  O  THR H  21   N  SER H   7           
SHEET    3  HA 4 THR H  78  MET H  83 -1  O  VAL H  79   N  CYS H  22           
SHEET    4  HA 4 PHE H  68  ASP H  73 -1  O  THR H  69   N  GLN H  82           
SHEET    1  HB 4 LEU H  11  VAL H  12  0                                        
SHEET    2  HB 4 THR H 110  VAL H 114  1  O  THR H 113   N  VAL H  12           
SHEET    3  HB 4 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 112           
SHEET    4  HB 4 LEU H 105  TRP H 106 -1  O  LEU H 105   N  ARG H  98           
SHEET    1  HC 6 LEU H  11  VAL H  12  0                                        
SHEET    2  HC 6 THR H 110  VAL H 114  1  O  THR H 113   N  VAL H  12           
SHEET    3  HC 6 ALA H  92  ARG H  98 -1  O  ALA H  92   N  VAL H 112           
SHEET    4  HC 6 TYR H  33  GLN H  39 -1  O  SER H  35   N  ALA H  97           
SHEET    5  HC 6 LEU H  45  GLY H  52 -1  O  GLU H  46   N  ARG H  38           
SHEET    6  HC 6 THR H  58  TYR H  60 -1  O  TYR H  59   N  TYR H  50           
SHEET    1  HD 2 LEU H 105  TRP H 106  0                                        
SHEET    2  HD 2 ALA H  92  ARG H  98 -1  O  ARG H  98   N  LEU H 105           
SHEET    1  HE 4 SER H 123  LEU H 127  0                                        
SHEET    2  HE 4 THR H 138  TYR H 148 -1  O  GLY H 142   N  LEU H 127           
SHEET    3  HE 4 TYR H 179  PRO H 188 -1  O  TYR H 179   N  TYR H 148           
SHEET    4  HE 4 VAL H 172  LEU H 173  1  O  VAL H 172   N  SER H 180           
SHEET    1  HF 4 SER H 123  LEU H 127  0                                        
SHEET    2  HF 4 THR H 138  TYR H 148 -1  O  GLY H 142   N  LEU H 127           
SHEET    3  HF 4 TYR H 179  PRO H 188 -1  O  TYR H 179   N  TYR H 148           
SHEET    4  HF 4 VAL H 166  THR H 168 -1  O  HIS H 167   N  VAL H 184           
SHEET    1  HG 2 VAL H 172  LEU H 173  0                                        
SHEET    2  HG 2 TYR H 179  PRO H 188  1  O  SER H 180   N  VAL H 172           
SHEET    1  HH 3 VAL H 153  TRP H 157  0                                        
SHEET    2  HH 3 THR H 198  HIS H 203 -1  O  ASN H 200   N  SER H 156           
SHEET    3  HH 3 THR H 208  ARG H 213 -1  O  THR H 208   N  HIS H 203           
SHEET    1  LA 4 LEU L   4  THR L   7  0                                        
SHEET    2  LA 4 VAL L  19  ALA L  25 -1  O  ASN L  22   N  THR L   7           
SHEET    3  LA 4 GLU L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4  LA 4 PHE L  62  SER L  67 -1  O  ARG L  63   N  THR L  74           
SHEET    1  LB 4 SER L  10  ALA L  13  0                                        
SHEET    2  LB 4 THR L 103  ILE L 107  1  O  ASN L 104   N  VAL L  11           
SHEET    3  LB 4 THR L  85  GLY L  91 -1  O  TYR L  86   N  THR L 103           
SHEET    4  LB 4 ALA L  97  PHE L  99 -1  O  THR L  98   N  SER L  90           
SHEET    1  LC 6 SER L  10  ALA L  13  0                                        
SHEET    2  LC 6 THR L 103  ILE L 107  1  O  ASN L 104   N  VAL L  11           
SHEET    3  LC 6 THR L  85  GLY L  91 -1  O  TYR L  86   N  THR L 103           
SHEET    4  LC 6 ALA L  34  GLN L  38 -1  O  ALA L  34   N  GLN L  89           
SHEET    5  LC 6 LYS L  45  TYR L  49 -1  O  LYS L  45   N  GLN L  37           
SHEET    6  LC 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  LD 2 ALA L  97  PHE L  99  0                                        
SHEET    2  LD 2 THR L  85  GLY L  91 -1  O  SER L  90   N  THR L  98           
SHEET    1  LE 4 SER L 115  ILE L 118  0                                        
SHEET    2  LE 4 THR L 130  PHE L 140 -1  O  LEU L 136   N  PHE L 117           
SHEET    3  LE 4 TYR L 174  SER L 183 -1  O  TYR L 174   N  PHE L 140           
SHEET    4  LE 4 SER L 160  VAL L 164 -1  O  GLN L 161   N  THR L 179           
SHEET    1  LF 3 LYS L 146  LYS L 150  0                                        
SHEET    2  LF 3 ALA L 194  THR L 198 -1  O  ALA L 194   N  LYS L 150           
SHEET    3  LF 3 VAL L 206  LYS L 208 -1  O  VAL L 206   N  VAL L 197           
SSBOND   1 CYS A   70    CYS A   96                          1555   1555  2.13  
SSBOND   2 CYS A   74    CYS A   84                          1555   1555  2.07  
SSBOND   3 CYS A  128    CYS A  206                          1555   1555  2.07  
SSBOND   4 CYS A  149    CYS A  189                          1555   1555  2.02  
SSBOND   5 CYS A  177    CYS A  201                          1555   1555  2.05  
SSBOND   6 CYS H   22    CYS H   96                          1555   1555  2.07  
SSBOND   7 CYS H  143    CYS H  199                          1555   1555  2.06  
SSBOND   8 CYS L   23    CYS L   88                          1555   1555  2.09  
SSBOND   9 CYS L  135    CYS L  195                          1555   1555  2.01  
CISPEP   1 ILE A  156    PRO A  157          0        -1.23                     
CISPEP   2 PHE H   29    SER H   30          0        -7.74                     
CISPEP   3 SER H   30    THR H   31          0       -17.42                     
CISPEP   4 PHE H  149    PRO H  150          0        -6.08                     
CISPEP   5 GLU H  151    PRO H  152          0        -2.73                     
CISPEP   6 THR L    7    PRO L    8          0        -2.24                     
CISPEP   7 SER L   94    ALA L   95          0         4.79                     
CISPEP   8 TYR L  141    PRO L  142          0        -2.23                     
CISPEP   9 ASP L  152    ASN L  153          0         1.88                     
CRYST1   86.703  297.692   70.713  90.00  90.00  90.00 C 2 2 21      8          
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      0.011534  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003359  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014142        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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