GenomeNet

Database: PDB
Entry: 1BND
LinkDB: 1BND
Original site: 1BND 
HEADER    COMPLEX (GROWTH FACTOR/GROWTH FACTOR)   12-DEC-94   1BND              
TITLE     STRUCTURE OF THE BRAIN-DERIVED NEUROTROPHIC FACTOR(SLASH)NEUROTROPHIN 
TITLE    2 3 HETERODIMER                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BRAIN DERIVED NEUROTROPHIC FACTOR;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BDNF;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NEUROTROPHIN 3;                                            
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: NT3;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: HETERODIMER                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 OTHER_DETAILS: SUPPLIED BY REGENERON PHARM.;                         
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 ORGAN: BRAIN;                                                        
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 OTHER_DETAILS: SUPPLIED BY REGENERON PHARM.;                         
KEYWDS    NEUROTROPHIN, COMPLEX (GROWTH FACTOR-GROWTH FACTOR) COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.ROBINSON,C.RADZIEJEWSKI,D.I.STUART,E.Y.JONES                      
REVDAT   4   13-JUL-11 1BND    1       VERSN                                    
REVDAT   3   24-FEB-09 1BND    1       VERSN                                    
REVDAT   2   01-APR-03 1BND    1       JRNL                                     
REVDAT   1   04-APR-96 1BND    0                                                
JRNL        AUTH   R.C.ROBINSON,C.RADZIEJEWSKI,D.I.STUART,E.Y.JONES             
JRNL        TITL   STRUCTURE OF THE BRAIN-DERIVED NEUROTROPHIC                  
JRNL        TITL 2 FACTOR/NEUROTROPHIN 3 HETERODIMER.                           
JRNL        REF    BIOCHEMISTRY                  V.  34  4139 1995              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   7703225                                                      
JRNL        DOI    10.1021/BI00013A001                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.RADZIEJEWSKI,R.C.ROBINSON                                  
REMARK   1  TITL   HETERODIMERS OF THE NEUROTROPHIC FACTORS: FORMATION,         
REMARK   1  TITL 2 ISOLATION, AND DIFFERENTIAL STABILITY                        
REMARK   1  REF    BIOCHEMISTRY                  V.  32 13350 1993              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 11691                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1722                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 70                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.89                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.350 ; 4.350                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.650 ; 6.650                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.350 ; 4.350                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.650 ; 6.650                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BND COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JAN-94                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
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) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11771                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08200                            
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       49.20000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       49.20000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.55000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       66.16200            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       59.87246            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ARG A   117                                                      
REMARK 465     GLY A   118                                                      
REMARK 465     ARG A   119                                                      
REMARK 465     TYR B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     ILE B   117                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     ARG B   119                                                      
REMARK 465     THR B   120                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  61   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    HIS B  74   N   -  CA  -  CB  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    HIS B  74   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  26      -69.22     81.26                                   
REMARK 500    MET A  31        0.78    -67.51                                   
REMARK 500    VAL A  44     -163.60   -116.76                                   
REMARK 500    LYS A  46      -70.41    -62.79                                   
REMARK 500    THR A  64       39.58    -78.18                                   
REMARK 500    ASP A  72       81.29    -66.42                                   
REMARK 500    GLN A  79      137.53   -172.85                                   
REMARK 500    GLN B  44        0.94     86.24                                   
REMARK 500    ASN B  45       74.55     40.19                                   
REMARK 500    SER B  46      -72.93   -102.00                                   
REMARK 500    ASP B  71       74.95   -101.00                                   
REMARK 500    HIS B  74       36.49   -156.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS B  74        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 500                 
DBREF  1BND A    1   119  UNP    P23560   BDNF_HUMAN     129    247             
DBREF  1BND B    1   120  UNP    P20783   NT3_HUMAN      139    257             
SEQADV 1BND GLN A    9  UNP  P23560    GLU   137 CONFLICT                       
SEQADV 1BND VAL B   11  UNP  P20783    TYR   149 CONFLICT                       
SEQADV 1BND GLN B   44  UNP  P20783    GLY   182 CONFLICT                       
SEQRES   1 A  119  HIS SER ASP PRO ALA ARG ARG GLY GLN LEU SER VAL CYS          
SEQRES   2 A  119  ASP SER ILE SER GLU TRP VAL THR ALA ALA ASP LYS LYS          
SEQRES   3 A  119  THR ALA VAL ASP MET SER GLY GLY THR VAL THR VAL LEU          
SEQRES   4 A  119  GLU LYS VAL PRO VAL SER LYS GLY GLN LEU LYS GLN TYR          
SEQRES   5 A  119  PHE TYR GLU THR LYS CYS ASN PRO MET GLY TYR THR LYS          
SEQRES   6 A  119  GLU GLY CYS ARG GLY ILE ASP LYS ARG HIS TRP ASN SER          
SEQRES   7 A  119  GLN CYS ARG THR THR GLN SER TYR VAL ARG ALA LEU THR          
SEQRES   8 A  119  MET ASP SER LYS LYS ARG ILE GLY TRP ARG PHE ILE ARG          
SEQRES   9 A  119  ILE ASP THR SER CYS VAL CYS THR LEU THR ILE LYS ARG          
SEQRES  10 A  119  GLY ARG                                                      
SEQRES   1 B  119  TYR ALA GLU HIS LYS SER HIS ARG GLY GLU VAL SER VAL          
SEQRES   2 B  119  CYS ASP SER GLU SER LEU TRP VAL THR ASP LYS SER SER          
SEQRES   3 B  119  ALA ILE ASP ILE ARG GLY HIS GLN VAL THR VAL LEU GLY          
SEQRES   4 B  119  GLU ILE LYS THR GLN ASN SER PRO VAL LYS GLN TYR PHE          
SEQRES   5 B  119  TYR GLU THR ARG CYS LYS GLU ALA ARG PRO VAL LYS ASN          
SEQRES   6 B  119  GLY CYS ARG GLY ILE ASP ASP LYS HIS TRP ASN SER GLN          
SEQRES   7 B  119  CYS LYS THR SER GLN THR TYR VAL ARG ALA LEU THR SER          
SEQRES   8 B  119  GLU ASN ASN LYS LEU VAL GLY TRP ARG TRP ILE ARG ILE          
SEQRES   9 B  119  ASP THR SER CYS VAL CYS ALA LEU SER ARG LYS ILE GLY          
SEQRES  10 B  119  ARG THR                                                      
HET    IPA  A 500       5                                                       
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   3  IPA    C3 H8 O                                                      
FORMUL   4  HOH   *70(H2 O)                                                     
HELIX    1   1 ALA A   22  LYS A   25  1                                   4    
HELIX    2   2 TYR A   63  LYS A   65  5                                   3    
SHEET    1   A 2 SER A  15  THR A  21  0                                        
SHEET    2   A 2 TYR A  52  CYS A  58 -1  N  LYS A  57   O  ILE A  16           
SHEET    1   B 2 THR A  27  VAL A  29  0                                        
SHEET    2   B 2 THR A  35  THR A  37 -1  N  VAL A  36   O  ALA A  28           
SHEET    1   C 2 LYS A  41  PRO A  43  0                                        
SHEET    2   C 2 GLN A  48  LYS A  50 -1  N  LEU A  49   O  VAL A  42           
SHEET    1   D 3 GLU B  10  SER B  12  0                                        
SHEET    2   D 3 ILE A  98  ILE A 115 -1  N  LEU A 113   O  VAL B  11           
SHEET    3   D 3 TRP A  76  MET A  92 -1  N  THR A  91   O  GLY A  99           
SHEET    1   E 2 SER B  16  VAL B  21  0                                        
SHEET    2   E 2 PHE B  52  CYS B  57 -1  N  ARG B  56   O  GLU B  17           
SHEET    1   F 2 SER B  26  ILE B  28  0                                        
SHEET    2   F 2 GLN B  34  THR B  36 -1  N  VAL B  35   O  ALA B  27           
SHEET    1   G 2 ASN B  76  THR B  90  0                                        
SHEET    2   G 2 GLY B  98  SER B 113 -1  N  SER B 113   O  ASN B  76           
SSBOND   1 CYS A   13    CYS A   80                          1555   1555  2.01  
SSBOND   2 CYS A   58    CYS A  109                          1555   1555  2.01  
SSBOND   3 CYS A   68    CYS A  111                          1555   1555  2.03  
SSBOND   4 CYS B   14    CYS B   79                          1555   1555  2.02  
SSBOND   5 CYS B   57    CYS B  108                          1555   1555  2.02  
SSBOND   6 CYS B   67    CYS B  110                          1555   1555  2.04  
CISPEP   1 SER B   46    PRO B   47          0        -0.44                     
SITE     1 AC1  7 VAL A  29  ASP A  30  GLY A  33  TYR A  86                    
SITE     2 AC1  7 ARG A 104  VAL B  11  ARG B  68                               
CRYST1   98.400   45.100   68.000  90.00 118.30  90.00 C 1 2 1       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      0.010163  0.000000  0.005472        0.00000                         
SCALE2      0.000000  0.022173  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016702        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system