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Database: PDB
Entry: 3HN4
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Original site: 3HN4 
HEADER    HORMONE                                 29-MAY-09   3HN4              
TITLE     CRYSTAL STRUCTURE OF THE NK2 FRAGMENT (28-289) OF HUMAN HEPATOCYTE    
TITLE    2 GROWTH FACTOR/SCATTER FACTOR                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPATOCYTE GROWTH FACTOR;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 28-289;                                       
COMPND   5 SYNONYM: SCATTER FACTOR, SF, HEPATOPOEITIN-A, HEPATOCYTE GROWTH      
COMPND   6 FACTOR ALPHA CHAIN, HEPATOCYTE GROWTH FACTOR BETA CHAIN;             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: 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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B(DE);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-DUET1/TRX/DSBC                        
KEYWDS    HGF/SF, HORMONE/GROWTH FACTOR, DISULFIDE BOND, GLYCOPROTEIN, GROWTH   
KEYWDS   2 FACTOR, KRINGLE, SERINE PROTEASE HOMOLOG, HORMONE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.D.TOLBERT                                                           
REVDAT   3   01-NOV-17 3HN4    1       REMARK                                   
REVDAT   2   01-SEP-10 3HN4    1       JRNL                                     
REVDAT   1   09-JUN-10 3HN4    0                                                
JRNL        AUTH   W.D.TOLBERT,J.DAUGHERTY-HOLTROP,E.GHERARDI,G.VANDE WOUDE,    
JRNL        AUTH 2 H.E.XU                                                       
JRNL        TITL   STRUCTURAL BASIS FOR AGONISM AND ANTAGONISM OF HEPATOCYTE    
JRNL        TITL 2 GROWTH FACTOR.                                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 13264 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20624990                                                     
JRNL        DOI    10.1073/PNAS.1005183107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 10223                          
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) : 0.270                           
REMARK   3   R VALUE            (WORKING SET) : 0.263                           
REMARK   3   FREE R VALUE                     : 0.333                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1028                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 603                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.4550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2089                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 106                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.18000                                              
REMARK   3    B22 (A**2) : 0.18000                                              
REMARK   3    B33 (A**2) : -0.27000                                             
REMARK   3    B12 (A**2) : 0.09000                                              
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): 2.923         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.446         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.312         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.594        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.883                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.824                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2227 ; 0.005 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3016 ; 0.867 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   261 ; 4.580 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   111 ;33.406 ;23.243       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   382 ;15.433 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;13.820 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   291 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1714 ; 0.004 ; 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):  1299 ; 0.199 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2110 ; 0.367 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   928 ; 0.301 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   906 ; 0.542 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3HN4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053337.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-08; 17-DEC-08; 05-MAR-09;   
REMARK 200                                   30-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100; 100; 100                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y; Y                         
REMARK 200  RADIATION SOURCE               : APS; APS; APS; APS                 
REMARK 200  BEAMLINE                       : 21-ID-D; 21-ID-D; 21-ID-G; 21-ID   
REMARK 200                                   -D                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL; NULL             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M; M                         
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12700; 1.12700; 0.97860;         
REMARK 200                                   1.07800                            
REMARK 200  MONOCHROMATOR                  : SI(111); SI(111); SI(111);         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL; NULL; NULL; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD; CCD; CCD                 
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD; MARMOSAIC    
REMARK 200                                   300 MM CCD; MARMOSAIC 300 MM CCD;  
REMARK 200                                   MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, MOSFLM                   
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000, SCALA                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.13400                            
REMARK 200  R SYM                      (I) : 0.13400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; SINGLE   
REMARK 200                       WAVELENGTH; SINGLE WAVELENGTH                  
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1NK1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM SULFATE, 17-23% PEG       
REMARK 280  2000 OR 4000, 100 MM HEPES PH 8.0, 5% 2-METHYL-2,4-PENTANEDIOL,     
REMARK 280  0.5 MM BETA-OCTYL GLUCOSIDE, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      307.78200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      153.89100            
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      230.83650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       76.94550            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      384.72750            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      307.78200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      153.89100            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       76.94550            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      230.83650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      384.72750            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     TYR A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     ARG A    33                                                      
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    LEU A  57       93.23     66.50                                   
REMARK 500    PRO A  81       21.50    -69.16                                   
REMARK 500    ARG A 126      -76.28      3.67                                   
REMARK 500    ASN A 127      -19.80     62.82                                   
REMARK 500    LYS A 137       36.94   -142.40                                   
REMARK 500    GLU A 174     -126.70     50.63                                   
REMARK 500    SER A 207       32.50    -82.17                                   
REMARK 500    GLU A 208      -60.20    -91.99                                   
REMARK 500    GLU A 210       95.39    -65.91                                   
REMARK 500    ALA A 214     -125.94     56.73                                   
REMARK 500    ALA A 214     -126.25     56.73                                   
REMARK 500    ASP A 252       -6.49     76.20                                   
REMARK 500    ASP A 257     -123.62     43.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NK1   RELATED DB: PDB                                   
REMARK 900 NK1 STRUCTURE                                                        
REMARK 900 RELATED ID: 1GP9   RELATED DB: PDB                                   
REMARK 900 NK1 STRUCTURE                                                        
REMARK 900 RELATED ID: 1GMN   RELATED DB: PDB                                   
REMARK 900 NK1-HEPARIN COMPLEXES                                                
REMARK 900 RELATED ID: 1GMO   RELATED DB: PDB                                   
REMARK 900 NK1-HEPARIN COMPLEXES                                                
REMARK 900 RELATED ID: 1BHT   RELATED DB: PDB                                   
REMARK 900 NK1 STRUCTURE                                                        
REMARK 900 RELATED ID: 2HGF   RELATED DB: PDB                                   
REMARK 900 NMR N-TERMINAL DOMAIN STRUCTURE                                      
REMARK 900 RELATED ID: 2QJ2   RELATED DB: PDB                                   
REMARK 900 NK1 STRUCTURE                                                        
REMARK 900 RELATED ID: 2QJ4   RELATED DB: PDB                                   
REMARK 900 MOUSE NK1 STRUCTURE                                                  
REMARK 900 RELATED ID: 3HMR   RELATED DB: PDB                                   
REMARK 900 MOUSE NK2 N-TERMINAL DOMAIN STRUCTURE                                
REMARK 900 RELATED ID: 3HMS   RELATED DB: PDB                                   
REMARK 900 NK2 N-TERMINAL DOMAIN STRUCTURE                                      
REMARK 900 RELATED ID: 3HMT   RELATED DB: PDB                                   
REMARK 900 NK2 N-TERMINAL DOMAIN STRUCTURE                                      
DBREF  3HN4 A   28   289  UNP    P14210   HGF_HUMAN       28    289             
SEQADV 3HN4 GLY A   26  UNP  P14210              EXPRESSION TAG                 
SEQADV 3HN4 SER A   27  UNP  P14210              EXPRESSION TAG                 
SEQADV 3HN4 GLU A  132  UNP  P14210    LYS   132 ENGINEERED                     
SEQADV 3HN4 GLU A  134  UNP  P14210    ARG   134 ENGINEERED                     
SEQADV 3HN4 ALA A  214  UNP  P14210    CYS   214 ENGINEERED                     
SEQRES   1 A  264  GLY SER TYR ALA GLU GLY GLN ARG LYS ARG ARG ASN THR          
SEQRES   2 A  264  ILE HIS GLU PHE LYS LYS SER ALA LYS THR THR LEU ILE          
SEQRES   3 A  264  LYS ILE ASP PRO ALA LEU LYS ILE LYS THR LYS LYS VAL          
SEQRES   4 A  264  ASN THR ALA ASP GLN CYS ALA ASN ARG CYS THR ARG ASN          
SEQRES   5 A  264  LYS GLY LEU PRO PHE THR CYS LYS ALA PHE VAL PHE ASP          
SEQRES   6 A  264  LYS ALA ARG LYS GLN CYS LEU TRP PHE PRO PHE ASN SER          
SEQRES   7 A  264  MET SER SER GLY VAL LYS LYS GLU PHE GLY HIS GLU PHE          
SEQRES   8 A  264  ASP LEU TYR GLU ASN LYS ASP TYR ILE ARG ASN CYS ILE          
SEQRES   9 A  264  ILE GLY GLU GLY GLU SER TYR LYS GLY THR VAL SER ILE          
SEQRES  10 A  264  THR LYS SER GLY ILE LYS CYS GLN PRO TRP SER SER MET          
SEQRES  11 A  264  ILE PRO HIS GLU HIS SER PHE LEU PRO SER SER TYR ARG          
SEQRES  12 A  264  GLY LYS ASP LEU GLN GLU ASN TYR CYS ARG ASN PRO ARG          
SEQRES  13 A  264  GLY GLU GLU GLY GLY PRO TRP CYS PHE THR SER ASN PRO          
SEQRES  14 A  264  GLU VAL ARG TYR GLU VAL CYS ASP ILE PRO GLN CYS SER          
SEQRES  15 A  264  GLU VAL GLU CYS MET THR ALA ASN GLY GLU SER TYR ARG          
SEQRES  16 A  264  GLY LEU MET ASP HIS THR GLU SER GLY LYS ILE CYS GLN          
SEQRES  17 A  264  ARG TRP ASP HIS GLN THR PRO HIS ARG HIS LYS PHE LEU          
SEQRES  18 A  264  PRO GLU ARG TYR PRO ASP LYS GLY PHE ASP ASP ASN TYR          
SEQRES  19 A  264  CYS ARG ASN PRO ASP GLY GLN PRO ARG PRO TRP CYS TYR          
SEQRES  20 A  264  THR LEU ASP PRO HIS THR ARG TRP GLU TYR CYS ALA ILE          
SEQRES  21 A  264  LYS THR CYS ALA                                              
HET    EPE  A1001      15                                                       
HET    MPD  A1002       8                                                       
HET    MPD  A1003       8                                                       
HET    SO4  A2001       5                                                       
HET    SO4  A2002       5                                                       
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     SO4 SULFATE ION                                                      
HETSYN     EPE HEPES                                                            
FORMUL   2  EPE    C8 H18 N2 O4 S                                               
FORMUL   3  MPD    2(C6 H14 O2)                                                 
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *106(H2 O)                                                    
HELIX    1   1 THR A   38  HIS A   40  5                                   3    
HELIX    2   2 THR A   66  ARG A   76  1                                  11    
HELIX    3   3 ASP A  123  ILE A  125  5                                   3    
SHEET    1   A 5 PHE A  42  LYS A  52  0                                        
SHEET    2   A 5 VAL A 108  ASN A 121 -1  O  LYS A 109   N  ILE A  51           
SHEET    3   A 5 ALA A  86  ASP A  90 -1  N  PHE A  87   O  TYR A 119           
SHEET    4   A 5 GLN A  95  PHE A  99 -1  O  PHE A  99   N  ALA A  86           
SHEET    5   A 5 LYS A  60  LYS A  63 -1  N  LYS A  60   O  TRP A  98           
SHEET    1   B 2 TRP A 188  PHE A 190  0                                        
SHEET    2   B 2 TYR A 198  VAL A 200 -1  O  GLU A 199   N  CYS A 189           
SHEET    1   C 2 CYS A 211  MET A 212  0                                        
SHEET    2   C 2 LYS A 286  THR A 287  1  O  LYS A 286   N  MET A 212           
SHEET    1   D 2 TRP A 270  TYR A 272  0                                        
SHEET    2   D 2 TRP A 280  TYR A 282 -1  O  GLU A 281   N  CYS A 271           
SSBOND   1 CYS A   70    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A   74    CYS A   84                          1555   1555  2.04  
SSBOND   3 CYS A  128    CYS A  206                          1555   1555  2.04  
SSBOND   4 CYS A  149    CYS A  189                          1555   1555  2.03  
SSBOND   5 CYS A  177    CYS A  201                          1555   1555  2.03  
SSBOND   6 CYS A  211    CYS A  288                          1555   1555  2.03  
SSBOND   7 CYS A  232    CYS A  271                          1555   1555  2.03  
SSBOND   8 CYS A  260    CYS A  283                          1555   1555  2.03  
CISPEP   1 ILE A  156    PRO A  157          0         0.98                     
CISPEP   2 THR A  239    PRO A  240          0        -2.17                     
SITE     1 AC1 10 SER A 161  GLU A 183  GLY A 185  GLY A 186                    
SITE     2 AC1 10 TRP A 188  PHE A 190  ARG A 197  TYR A 198                    
SITE     3 AC1 10 VAL A 200  HOH A3005                                          
SITE     1 AC2  2 LYS A  60  ARG A  73                                          
SITE     1 AC3  1 ILE A 231                                                     
SITE     1 AC4  4 ARG A  93  HIS A 241  ARG A 242  ARG A 279                    
SITE     1 AC5  6 THR A  83  GLY A 169  LYS A 170  ASP A 171                    
SITE     2 AC5  6 GLN A 173  HOH A3054                                          
CRYST1   48.150   48.150  461.673  90.00  90.00 120.00 P 65 2 2     12          
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      0.020768  0.011991  0.000000        0.00000                         
SCALE2      0.000000  0.023981  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002166        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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