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Database: PDB
Entry: 1HCF
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HEADER    TRANSFERASE/HORMONE                     03-MAY-01   1HCF              
TITLE     CRYSTAL STRUCTURE OF TRKB-D5 BOUND TO NEUROTROPHIN-4/5                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROTROPHIN-4;                                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ACTIVE, FRAGMENT. PRO-REGION CLEAVED;                      
COMPND   5 SYNONYM: NEUROTROPHIN-5, NEUROTROPHIN-4/5, NT-4/5;                   
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BDNF/NT-3 GROWTH FACTORS RECEPTOR;                         
COMPND   8 CHAIN: X , Y;                                                        
COMPND   9 FRAGMENT: EXTRACELLULAR DOMAIN 5 (RESIDUES 286 - 383);               
COMPND  10 SYNONYM: TRKB, GP145-TRKB;                                           
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELLULAR_LOCATION: EXTRACELLULAR;                                    
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 CELLULAR_LOCATION: PLASMA MEMBRANE;                                  
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    TRANSFERASE/HORMONE, COMPLEX(TRANSFERASE/GROWTH FACTOR),              
KEYWDS   2 NEUROTROPHIN-4/5, TRKB RECEPTOR, NGF-BETA SUPERFAMILY,               
KEYWDS   3 IMMUNOGLOBULIN DOMAIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.BANFIELD,R.L.NAYLOR,A.G.S.ROBERTSON,S.J.ALLEN,D.DAWBARN,          
AUTHOR   2 R.L.BRADY                                                            
REVDAT   2   24-FEB-09 1HCF    1       VERSN                                    
REVDAT   1   06-DEC-01 1HCF    0                                                
JRNL        AUTH   M.J.BANFIELD,R.L.NAYLOR,A.G.S.ROBERTSON,S.J.ALLEN,           
JRNL        AUTH 2 D.DAWBARN,R.L.BRADY                                          
JRNL        TITL   SPECIFICITY IN TRK-RECEPTOR:NEUROTROPHIN                     
JRNL        TITL 2 INTERACTION: THE CRYSTAL STRUCTURE OF TRKB-D5 IN             
JRNL        TITL 3 COMPLEX WITH NEUROTROPHIN-4/5                                
JRNL        REF    STRUCTURE                     V.   9  1191 2001              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   11738045                                                     
JRNL        DOI    10.1016/S0969-2126(01)00681-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.G.S.ROBERTSON,M.J.BANFIELD,S.J.ALLEN,J.A.DANDO,            
REMARK   1  AUTH 2 G.G.F.MASON,S.J.TYLER,G.S.BENNETT,S.D.BRAIN,                 
REMARK   1  AUTH 3 A.R.CLARKE,R.L.BRADY,D.DAWBARN                               
REMARK   1  TITL   IDENTIFICATION AND STRUCTURE OF THE NERVE GROWTH             
REMARK   1  TITL 2 FACTOR BINDING SITE ON TRKA                                  
REMARK   1  REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 282   131 2001              
REMARK   1  REFN                   ISSN 0006-291X                               
REMARK   1  PMID   11263982                                                     
REMARK   1  DOI    10.1006/BBRC.2001.4462                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.WIESMANN,M.H.ULTSCH,S.H.BASS,A.M.DEVOS                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR IN                  
REMARK   1  TITL 2 COMPLEX WITH THE LIGAND-BINDING DOMAIN OF THE TRKA           
REMARK   1  TITL 3 RECEPTOR                                                     
REMARK   1  REF    NATURE                        V. 401   184 1999              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   10490030                                                     
REMARK   1  DOI    10.1038/43705                                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.H.ULTSCH,C.WIESMANN,L.C.SIMMONS,J.HENRICH,M.YANG,          
REMARK   1  AUTH 2 D.REILLY,S.H.BASS,A.M.DEVOS                                  
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE NEUROTROPHIN BINDING               
REMARK   1  TITL 2 DOMAIN OF TRKA, TRKB AND TRKC                                
REMARK   1  REF    J.MOL.BIOL.                   V. 290   149 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   10388563                                                     
REMARK   1  DOI    10.1006/JMBI.1999.2816                                       
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   R.C.ROBINSON,C.RADZIEJEWSKI,G.SPRAGGON,J.GREENWALD,          
REMARK   1  AUTH 2 M.R.KOSTURA,L.D.BURTNICK,D.I.STUART,S.CHOE,                  
REMARK   1  AUTH 3 E.Y.JONES                                                    
REMARK   1  TITL   THE STRUCTURES OF NEUROTROPHIN 4 HOMODIMER AND THE           
REMARK   1  TITL 2 BRAIN-DERIVED NEUROTROPHIC FACTOR/NEUROTROPHIN 4             
REMARK   1  TITL 3 HETERODIMER REVEAL A COMMON TRK BINDING SITE                 
REMARK   1  REF    PROTEIN SCI.                  V.   8  2589 1999              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1  PMID   10631974                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.7  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MLF                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.7                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 15411                          
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 SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 761                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.7                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.8                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.9                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1430                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.299                        
REMARK   3   BIN FREE R VALUE                    : 0.359                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.5                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 84                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.039                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3419                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 60                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.7                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.7                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.52                                                 
REMARK   3    B22 (A**2) : -7.91                                                
REMARK   3    B33 (A**2) : 7.39                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.4                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.2                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.546 ; 1.5                  
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.997 ; 2.0                  
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.728 ; 2.0                  
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.120 ; 2.5                  
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.328                                                
REMARK   3   BSOL        : 40.14                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : SO4.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HCF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  04-MAY-01.                 
REMARK 100 THE PDBE ID CODE IS EBI-6161.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : CRYSTAL                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15635                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1B98 (NEUROTROPHIN), 1WWB (TRK)                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 46.6                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML COMPLEX IN 20MM TRIS,           
REMARK 280  150MM NACL, PH 7.5, 100MM HEPES PH 7.5, 1.5M LISO4                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       37.18600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.65900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.20300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.65900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.18600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.20300            
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 300                                                                      
REMARK 300 DETAILS:COMPLEX OF HOMODIMERIC NEUROTROPHIN-4 AND                    
REMARK 300 TWO CHAINSOF TRKB                                                    
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X, Y                            
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     ASN A    65                                                      
REMARK 465     ALA A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLU A    68                                                      
REMARK 465     GLY A    69                                                      
REMARK 465     GLY A    70                                                      
REMARK 465     GLY A   128                                                      
REMARK 465     ARG A   129                                                      
REMARK 465     ALA A   130                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     GLY B    49                                                      
REMARK 465     ASN B    65                                                      
REMARK 465     ARG B   129                                                      
REMARK 465     ALA B   130                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A   2    CB   CG1  CG2                                       
REMARK 470     ARG A  28    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A  36    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  62    CD   CE   NZ                                        
REMARK 470     ARG A  83    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 107    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B  53    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B  62    CD   CE   NZ                                        
REMARK 470     GLU X 371    CD   OE1  OE2                                       
REMARK 470     LYS Y 308    CG   CD   CE   NZ                                   
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    CYS X 345   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    CYS X 345   CB  -  CA  -  C   ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    LEU X 346   N   -  CA  -  C   ANGL. DEV. = -20.1 DEGREES          
REMARK 500    CYS Y 345   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500    LEU Y 346   N   -  CA  -  C   ANGL. DEV. = -17.9 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 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    VAL A   2      -84.93    -69.64                                   
REMARK 500    SER A   3      -31.28   -150.49                                   
REMARK 500    ALA A  46     -174.70    -59.63                                   
REMARK 500    SER A  50      155.12    -30.81                                   
REMARK 500    PRO B  45      170.25    -45.19                                   
REMARK 500    PRO B  51     -143.97    -59.92                                   
REMARK 500    LEU B  52      101.89    157.02                                   
REMARK 500    ARG B 126       -2.07   -156.22                                   
REMARK 500    ASP X 298     -132.31   -118.06                                   
REMARK 500    ASN X 338     -125.90    -93.52                                   
REMARK 500    HIS X 339      -78.62    -75.94                                   
REMARK 500    PHE Y 291      124.64   -172.71                                   
REMARK 500    ASP Y 298     -124.92   -118.71                                   
REMARK 500    PRO Y 311     -179.13    -62.67                                   
REMARK 500    ASN Y 338      -94.27    -73.43                                   
REMARK 500    GLU Y 366      -38.06    -37.45                                   
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 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1128                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1129                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1131                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WWB   RELATED DB: PDB                                   
REMARK 900  LIGAND BINDING DOMAIN OF HUMAN TRKB RECEPTOR                        
REMARK 900 RELATED ID: 1B8M   RELATED DB: PDB                                   
REMARK 900  BRAIN DERIVED NEUROTROPHIC FACTOR, NEUROTROPHIN-4                   
REMARK 900 RELATED ID: 1B98   RELATED DB: PDB                                   
REMARK 900  NEUROTROPHIN 4 (HOMODIMER)                                          
REMARK 999                                                                      
REMARK 999 RESIDUES NUMBERED X283, X284, X285 ARE                               
REMARK 999 CLONING ARTEFACTS. THEY ARE DERIVED FROM                             
REMARK 999 THE HIS-TAG SEQUENCE OF THE PET-15B PLASMID,                         
REMARK 999 AND DO NOT CORRESPOND TO THE NATIVE TRKB                             
REMARK 999 RESIDUES 283, 284 AND 285.                                           
REMARK 999                                                                      
REMARK 999 RESIDUES NUMBERED Y283, Y284, Y285 ARE                               
REMARK 999 CLONING ARTEFACTS. THEY ARE DERIVED FROM                             
REMARK 999 THE HIS-TAG SEQUENCE OF THE PET-15B PLASMID,                         
REMARK 999 AND DO NOT CORRESPOND TO THE NATIVE TRKB                             
REMARK 999 RESIDUES 283, 284 AND 285.                                           
DBREF  1HCF A    1   130  UNP    P34130   NT5_HUMAN       81    210             
DBREF  1HCF B    1   130  UNP    P34130   NT5_HUMAN       81    210             
DBREF  1HCF X  283   285  PDB    1HCF     1HCF           283    285             
DBREF  1HCF X  286   383  UNP    Q16620   TRKB_HUMAN     286    383             
DBREF  1HCF Y  283   285  PDB    1HCF     1HCF           283    285             
DBREF  1HCF Y  286   383  UNP    Q16620   TRKB_HUMAN     286    383             
SEQRES   1 A  130  GLY VAL SER GLU THR ALA PRO ALA SER ARG ARG GLY GLU          
SEQRES   2 A  130  LEU ALA VAL CYS ASP ALA VAL SER GLY TRP VAL THR ASP          
SEQRES   3 A  130  ARG ARG THR ALA VAL ASP LEU ARG GLY ARG GLU VAL GLU          
SEQRES   4 A  130  VAL LEU GLY GLU VAL PRO ALA ALA GLY GLY SER PRO LEU          
SEQRES   5 A  130  ARG GLN TYR PHE PHE GLU THR ARG CYS LYS ALA ASP ASN          
SEQRES   6 A  130  ALA GLU GLU GLY GLY PRO GLY ALA GLY GLY GLY GLY CYS          
SEQRES   7 A  130  ARG GLY VAL ASP ARG ARG HIS TRP VAL SER GLU CYS LYS          
SEQRES   8 A  130  ALA LYS GLN SER TYR VAL ARG ALA LEU THR ALA ASP ALA          
SEQRES   9 A  130  GLN GLY ARG VAL GLY TRP ARG TRP ILE ARG ILE ASP THR          
SEQRES  10 A  130  ALA CYS VAL CYS THR LEU LEU SER ARG THR GLY ARG ALA          
SEQRES   1 B  130  GLY VAL SER GLU THR ALA PRO ALA SER ARG ARG GLY GLU          
SEQRES   2 B  130  LEU ALA VAL CYS ASP ALA VAL SER GLY TRP VAL THR ASP          
SEQRES   3 B  130  ARG ARG THR ALA VAL ASP LEU ARG GLY ARG GLU VAL GLU          
SEQRES   4 B  130  VAL LEU GLY GLU VAL PRO ALA ALA GLY GLY SER PRO LEU          
SEQRES   5 B  130  ARG GLN TYR PHE PHE GLU THR ARG CYS LYS ALA ASP ASN          
SEQRES   6 B  130  ALA GLU GLU GLY GLY PRO GLY ALA GLY GLY GLY GLY CYS          
SEQRES   7 B  130  ARG GLY VAL ASP ARG ARG HIS TRP VAL SER GLU CYS LYS          
SEQRES   8 B  130  ALA LYS GLN SER TYR VAL ARG ALA LEU THR ALA ASP ALA          
SEQRES   9 B  130  GLN GLY ARG VAL GLY TRP ARG TRP ILE ARG ILE ASP THR          
SEQRES  10 B  130  ALA CYS VAL CYS THR LEU LEU SER ARG THR GLY ARG ALA          
SEQRES   1 X  101  SER HIS MET ALA PRO THR ILE THR PHE LEU GLU SER PRO          
SEQRES   2 X  101  THR SER ASP HIS HIS TRP CYS ILE PRO PHE THR VAL LYS          
SEQRES   3 X  101  GLY ASN PRO LYS PRO ALA LEU GLN TRP PHE TYR ASN GLY          
SEQRES   4 X  101  ALA ILE LEU ASN GLU SER LYS TYR ILE CYS THR LYS ILE          
SEQRES   5 X  101  HIS VAL THR ASN HIS THR GLU TYR HIS GLY CYS LEU GLN          
SEQRES   6 X  101  LEU ASP ASN PRO THR HIS MET ASN ASN GLY ASP TYR THR          
SEQRES   7 X  101  LEU ILE ALA LYS ASN GLU TYR GLY LYS ASP GLU LYS GLN          
SEQRES   8 X  101  ILE SER ALA HIS PHE MET GLY TRP PRO GLY                      
SEQRES   1 Y  101  SER HIS MET ALA PRO THR ILE THR PHE LEU GLU SER PRO          
SEQRES   2 Y  101  THR SER ASP HIS HIS TRP CYS ILE PRO PHE THR VAL LYS          
SEQRES   3 Y  101  GLY ASN PRO LYS PRO ALA LEU GLN TRP PHE TYR ASN GLY          
SEQRES   4 Y  101  ALA ILE LEU ASN GLU SER LYS TYR ILE CYS THR LYS ILE          
SEQRES   5 Y  101  HIS VAL THR ASN HIS THR GLU TYR HIS GLY CYS LEU GLN          
SEQRES   6 Y  101  LEU ASP ASN PRO THR HIS MET ASN ASN GLY ASP TYR THR          
SEQRES   7 Y  101  LEU ILE ALA LYS ASN GLU TYR GLY LYS ASP GLU LYS GLN          
SEQRES   8 Y  101  ILE SER ALA HIS PHE MET GLY TRP PRO GLY                      
HET    SO4  A1128       5                                                       
HET    SO4  B1129       5                                                       
HET    SO4  B1130       5                                                       
HET    SO4  B1131       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   9  HOH   *60(H2 O1)                                                    
HELIX    1   1 PRO A    7  ARG A   11  5                                   5    
HELIX    1   1 PRO B    7  ARG B   11  5                                   5    
HELIX    2   2 HIS X  353  ASN X  356  5                                   4    
HELIX    3   3 HIS Y  353  ASN Y  356  5                                   4    
SHEET    1  AA 2 ASP A  18  THR A  25  0                                        
SHEET    2  AA 2 PHE A  56  CYS A  61 -1  O  PHE A  56   N  VAL A  24           
SHEET    1  AB 4 ARG A  28  VAL A  31  0                                        
SHEET    2  AB 4 ARG A  36  VAL A  40 -1  O  VAL A  38   N  ALA A  30           
SHEET    3  AB 4 VAL A  87  ALA A 102 -1  O  ALA A 102   N  GLU A  39           
SHEET    4  AB 4 ARG A 107  SER A 125 -1  O  GLY A 109   N  THR A 101           
SHEET    1  AC 2 GLY A  42  ALA A  46  0                                        
SHEET    2  AC 2 SER A  50  ARG A  53 -1  O  LEU A  52   N  VAL A  44           
SHEET    1  BA 2 ASP B  18  THR B  25  0                                        
SHEET    2  BA 2 PHE B  56  CYS B  61 -1  O  PHE B  56   N  VAL B  24           
SHEET    1  BB 4 ARG B  28  VAL B  31  0                                        
SHEET    2  BB 4 ARG B  36  VAL B  40 -1  O  VAL B  38   N  ALA B  30           
SHEET    3  BB 4 VAL B  87  ALA B 102 -1  O  ALA B 102   N  GLU B  39           
SHEET    4  BB 4 ARG B 107  SER B 125 -1  O  GLY B 109   N  THR B 101           
SHEET    1  BC 2 GLY B  42  ALA B  46  0                                        
SHEET    2  BC 2 SER B  50  ARG B  53 -1  O  LEU B  52   N  VAL B  44           
SHEET    1  XX 4 ALA X 322  ASN X 325  0                                        
SHEET    2  XX 4 ALA X 314  TYR X 319 -1  N  TYR X 319   O  ALA X 322           
SHEET    3  XX 4 GLY X 357  LYS X 364 -1  N  LYS X 364   O  ALA X 314           
SHEET    4  XX 4 GLY X 368  HIS X 377 -1  N  ALA X 376   O  GLY X 357           
SHEET    1  XY 4 MET X 285  GLU X 293  0                                        
SHEET    2  XY 4 TRP X 301  GLY X 309 -1  N  LYS X 308   O  THR X 288           
SHEET    3  XY 4 GLU X 341  ASP X 349 -1  N  LEU X 348   O  TRP X 301           
SHEET    4  XY 4 CYS X 331  ASN X 338 -1  N  VAL X 336   O  HIS X 343           
SHEET    1  XZ 4 PRO X 295  SER X 297  0                                        
SHEET    2  XZ 4 TRP X 301  GLY X 309 -1  N  ILE X 303   O  THR X 296           
SHEET    3  XZ 4 GLU X 341  ASP X 349 -1  N  LEU X 348   O  TRP X 301           
SHEET    4  XZ 4 CYS X 331  ASN X 338 -1  N  VAL X 336   O  HIS X 343           
SHEET    1  YX 4 ALA Y 322  ASN Y 325  0                                        
SHEET    2  YX 4 ALA Y 314  TYR Y 319 -1  N  TYR Y 319   O  ALA Y 322           
SHEET    3  YX 4 GLY Y 357  LYS Y 364 -1  N  LYS Y 364   O  ALA Y 314           
SHEET    4  YX 4 GLY Y 368  HIS Y 377 -1  N  ALA Y 376   O  GLY Y 357           
SHEET    1  YY 4 MET Y 285  GLU Y 293  0                                        
SHEET    2  YY 4 TRP Y 301  GLY Y 309 -1  N  LYS Y 308   O  THR Y 288           
SHEET    3  YY 4 GLU Y 341  ASP Y 349 -1  N  LEU Y 348   O  TRP Y 301           
SHEET    4  YY 4 CYS Y 331  ASN Y 338 -1  N  VAL Y 336   O  HIS Y 343           
SHEET    1  YZ 4 PRO Y 295  SER Y 297  0                                        
SHEET    2  YZ 4 TRP Y 301  GLY Y 309 -1  N  ILE Y 303   O  THR Y 296           
SHEET    3  YZ 4 GLU Y 341  ASP Y 349 -1  N  LEU Y 348   O  TRP Y 301           
SHEET    4  YZ 4 CYS Y 331  ASN Y 338 -1  N  VAL Y 336   O  HIS Y 343           
SSBOND   1 CYS A   17    CYS A   90                          1555   1555  2.04  
SSBOND   2 CYS A   61    CYS A  119                          1555   1555  2.04  
SSBOND   3 CYS A   78    CYS A  121                          1555   1555  2.03  
SSBOND   4 CYS B   17    CYS B   90                          1555   1555  2.03  
SSBOND   5 CYS B   61    CYS B  119                          1555   1555  2.04  
SSBOND   6 CYS B   78    CYS B  121                          1555   1555  2.04  
SSBOND   7 CYS X  302    CYS X  345                          1555   1555  2.04  
SSBOND   8 CYS Y  302    CYS Y  345                          1555   1555  2.04  
CISPEP   1 ASN X  310    PRO X  311          0         0.03                     
CISPEP   2 ASN Y  310    PRO Y  311          0        -0.02                     
SITE     1 AC1  1 ARG A  11                                                     
SITE     1 AC2  6 ARG B  34  ARG B  36  HIS B  85  ARG B 111                    
SITE     2 AC2  6 HOH B2007  HOH B2015                                          
SITE     1 AC3  3 ALA B   8  ARG B  11  HOH B2018                               
SITE     1 AC4  3 ARG A  84  ARG B  34  HOH B2019                               
CRYST1   74.372   80.406   91.318  90.00  90.00  90.00 P 21 21 21    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      0.013446  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012437  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010951        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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