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Database: PDB
Entry: 1SG1
LinkDB: 1SG1
Original site: 1SG1 
HEADER    HORMONE/GROWTH FACTOR/MEMBRANE PROTEIN  22-FEB-04   1SG1              
TITLE     CRYSTAL STRUCTURE OF THE RECEPTOR-LIGAND COMPLEX BETWEEN              
TITLE    2 NERVE GROWTH FACTOR AND THE COMMON NEUROTROPHIN RECEPTOR             
TITLE    3 P75                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-NERVE GROWTH FACTOR;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: BETA-NGF;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY                 
COMPND   8 MEMBER 16;                                                           
COMPND   9 CHAIN: X;                                                            
COMPND  10 SYNONYM: LOW- AFFINITY NERVE GROWTH FACTOR RECEPTOR, NGF             
COMPND  11 RECEPTOR, GP80-LNGFR, P75 ICD, LOW AFFINITY NEUROTROPHIN             
COMPND  12 RECEPTOR P75NTR;                                                     
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NGFB;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  12 ORGANISM_TAXID: 10116;                                               
SOURCE  13 GENE: P75;                                                           
SOURCE  14 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: TN5;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PACGP67A                                  
KEYWDS    NERVE GROWTH FACTOR, NGF, P75, NEUROTROPHIN, COMMON                   
KEYWDS   2 NEUROTROPHIN RECEPTOR, CRYSTAL STRUCTURE, GROWTH FACTOR              
KEYWDS   3 RECEPTOR, RECEPTOR/LIGAND COMPLEX, HORMONE/GROWTH                    
KEYWDS   4 FACTOR/MEMBRANE PROTEIN COMPLEX                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.L.HE,K.C.GARCIA                                                     
REVDAT   3   24-FEB-09 1SG1    1       VERSN                                    
REVDAT   2   12-APR-05 1SG1    1       JRNL                                     
REVDAT   1   01-JUN-04 1SG1    0                                                
JRNL        AUTH   X.L.HE,K.C.GARCIA                                            
JRNL        TITL   STRUCTURE OF NERVE GROWTH FACTOR COMPLEXED WITH              
JRNL        TITL 2 THE SHARED NEUROTROPHIN RECEPTOR P75                         
JRNL        REF    SCIENCE                       V. 304   870 2004              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   15131306                                                     
JRNL        DOI    10.1126/SCIENCE.1095190                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
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)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 16891                          
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) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 803                             
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4000                       
REMARK   3   BIN FREE R VALUE                    : 0.4110                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 85                           
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            : 2763                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 375                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.40                          
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) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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 1SG1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021679.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0597                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16891                              
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     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
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) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: PART OF THE STRUCTURE STARTS FROM PDB ENTRY 1WWW     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, ISOPROPONAL, SODIUM            
REMARK 280  CHLORIDE, CITRATE, PH 6.3, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 295K                                                    
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       24.84600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.00500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.89800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.00500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.84600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.89800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X                               
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     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PRO A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     VAL A    64                                                      
REMARK 465     ASP A    65                                                      
REMARK 465     SER A    66                                                      
REMARK 465     ALA A   116                                                      
REMARK 465     VAL A   117                                                      
REMARK 465     ARG A   118                                                      
REMARK 465     ARG A   119                                                      
REMARK 465     ALA A   120                                                      
REMARK 465     SER B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     PHE B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     PRO B    61                                                      
REMARK 465     ASN B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     VAL B    64                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     VAL B   117                                                      
REMARK 465     ARG B   118                                                      
REMARK 465     ARG B   119                                                      
REMARK 465     ALA B   120                                                      
REMARK 465     LYS X     1                                                      
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    THR A  26      -76.47   -107.43                                   
REMARK 500    ASN A  45       57.59   -159.76                                   
REMARK 500    MET A  92       65.82   -103.68                                   
REMARK 500    ASP A  93       88.14    -51.77                                   
REMARK 500    LYS A  95      -84.58    -68.43                                   
REMARK 500    ASP B  30     -176.56    -63.71                                   
REMARK 500    ASN B  45       55.16     75.46                                   
REMARK 500    ASN B  46       -4.34     72.51                                   
REMARK 500    ARG B  59       57.34   -148.49                                   
REMARK 500    HIS B  75      -39.17   -138.61                                   
REMARK 500    THR B  85     -163.51   -105.45                                   
REMARK 500    LYS B  95     -106.12    -68.45                                   
REMARK 500    SER X   5        5.22    -59.11                                   
REMARK 500    HIS X  11       -8.03    -54.22                                   
REMARK 500    ASN X  20     -168.33    -56.50                                   
REMARK 500    GLN X  33      -83.62    -40.83                                   
REMARK 500    THR X  34      132.16    172.36                                   
REMARK 500    ASN X  42       -9.07     75.31                                   
REMARK 500    THR X  52       -8.40   -148.71                                   
REMARK 500    ALA X  82      167.33    -47.30                                   
REMARK 500    GLU X 101      172.79    -58.30                                   
REMARK 500    VAL X 107      -51.80   -123.29                                   
REMARK 500    ASP X 112     -102.08     34.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 558        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH A 564        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH X 177        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH B 146        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH X 189        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH B 159        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A 592        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH X 203        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 167        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH B 168        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH B 169        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH B 170        DISTANCE =  9.07 ANGSTROMS                       
REMARK 525    HOH B 171        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH B 172        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH B 174        DISTANCE =  9.30 ANGSTROMS                       
REMARK 525    HOH X 219        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH B 179        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A 613        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH B 182        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A 616        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH X 227        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A 621        DISTANCE =  8.59 ANGSTROMS                       
REMARK 525    HOH A 623        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH A 624        DISTANCE =  7.89 ANGSTROMS                       
REMARK 525    HOH X 235        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH A 626        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH A 627        DISTANCE =  9.30 ANGSTROMS                       
REMARK 525    HOH B 196        DISTANCE =  8.82 ANGSTROMS                       
REMARK 525    HOH B 197        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH A 630        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A 632        DISTANCE =  7.98 ANGSTROMS                       
REMARK 525    HOH X 244        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH A 637        DISTANCE =  9.55 ANGSTROMS                       
REMARK 525    HOH X 247        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH X 250        DISTANCE = 11.42 ANGSTROMS                       
REMARK 525    HOH A 641        DISTANCE = 13.65 ANGSTROMS                       
REMARK 525    HOH B 210        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH X 252        DISTANCE =  8.25 ANGSTROMS                       
REMARK 525    HOH X 253        DISTANCE = 12.04 ANGSTROMS                       
REMARK 525    HOH A 644        DISTANCE =  9.35 ANGSTROMS                       
REMARK 525    HOH X 254        DISTANCE =  7.39 ANGSTROMS                       
REMARK 525    HOH A 645        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH X 258        DISTANCE =  8.22 ANGSTROMS                       
REMARK 525    HOH X 259        DISTANCE =  8.04 ANGSTROMS                       
REMARK 525    HOH X 260        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH X 261        DISTANCE =  9.24 ANGSTROMS                       
REMARK 525    HOH A 653        DISTANCE =  9.20 ANGSTROMS                       
REMARK 525    HOH A 655        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH X 268        DISTANCE =  9.21 ANGSTROMS                       
REMARK 525    HOH A 660        DISTANCE =  8.26 ANGSTROMS                       
REMARK 525    HOH A 665        DISTANCE =  8.90 ANGSTROMS                       
REMARK 525    HOH A 669        DISTANCE = 10.25 ANGSTROMS                       
REMARK 525    HOH A 671        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH X 285        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A 677        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH X 287        DISTANCE =  9.89 ANGSTROMS                       
REMARK 525    HOH A 679        DISTANCE =  8.54 ANGSTROMS                       
REMARK 525    HOH A 680        DISTANCE =  7.67 ANGSTROMS                       
REMARK 525    HOH X 290        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A 681        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH X 291        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH X 299        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH X 302        DISTANCE =  7.26 ANGSTROMS                       
REMARK 525    HOH X 311        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH X 312        DISTANCE =  8.27 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 551                  
DBREF  1SG1 A    1   120  UNP    P01138   NGF_HUMAN      122    241             
DBREF  1SG1 B    1   120  UNP    P01138   NGF_HUMAN      122    241             
DBREF  1SG1 X    1   161  UNP    P07174   TNR16_RAT       30    190             
SEQRES   1 A  120  SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER          
SEQRES   2 A  120  VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR          
SEQRES   3 A  120  THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU          
SEQRES   4 A  120  GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR          
SEQRES   5 A  120  PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP          
SEQRES   6 A  120  SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER          
SEQRES   7 A  120  TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR          
SEQRES   8 A  120  MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE          
SEQRES   9 A  120  ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL          
SEQRES  10 A  120  ARG ARG ALA                                                  
SEQRES   1 B  120  SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER          
SEQRES   2 B  120  VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR          
SEQRES   3 B  120  THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU          
SEQRES   4 B  120  GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR          
SEQRES   5 B  120  PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP          
SEQRES   6 B  120  SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER          
SEQRES   7 B  120  TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR          
SEQRES   8 B  120  MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE          
SEQRES   9 B  120  ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL          
SEQRES  10 B  120  ARG ARG ALA                                                  
SEQRES   1 X  161  LYS GLU THR CYS SER THR GLY LEU TYR THR HIS SER GLY          
SEQRES   2 X  161  GLU CYS CYS LYS ALA CYS ASN LEU GLY GLU GLY VAL ALA          
SEQRES   3 X  161  GLN PRO CYS GLY ALA ASN GLN THR VAL CYS GLU PRO CYS          
SEQRES   4 X  161  LEU ASP ASN VAL THR PHE SER ASP VAL VAL SER ALA THR          
SEQRES   5 X  161  GLU PRO CYS LYS PRO CYS THR GLU CYS LEU GLY LEU GLN          
SEQRES   6 X  161  SER MET SER ALA PRO CYS VAL GLU ALA ASP ASP ALA VAL          
SEQRES   7 X  161  CYS ARG CYS ALA TYR GLY TYR TYR GLN ASP GLU GLU THR          
SEQRES   8 X  161  GLY HIS CYS GLU ALA CYS SER VAL CYS GLU VAL GLY SER          
SEQRES   9 X  161  GLY LEU VAL PHE SER CYS GLN ASP LYS GLN ASN THR VAL          
SEQRES  10 X  161  CYS GLU GLU CYS PRO GLU GLY THR TYR SER ASP GLU ALA          
SEQRES  11 X  161  ASN HIS VAL ASP PRO CYS LEU PRO CYS THR VAL CYS GLU          
SEQRES  12 X  161  ASP THR GLU ARG GLN LEU ARG GLU CYS THR PRO TRP ALA          
SEQRES  13 X  161  ASP ALA GLU CYS GLU                                          
HET     CL  A 551       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  HOH   *375(H2 O)                                                    
SHEET    1   A 5 PHE A  12  SER A  13  0                                        
SHEET    2   A 5 ALA B  97  ARG B 114 -1  O  LEU B 112   N  PHE A  12           
SHEET    3   A 5 TRP B  76  MET B  92 -1  N  ASN B  77   O  SER B 113           
SHEET    4   A 5 GLU B  35  VAL B  38 -1  N  MET B  37   O  MET B  92           
SHEET    5   A 5 THR B  27  THR B  29 -1  N  ALA B  28   O  VAL B  36           
SHEET    1   B 2 SER A  17  VAL A  22  0                                        
SHEET    2   B 2 PHE A  53  CYS A  58 -1  O  GLU A  55   N  VAL A  20           
SHEET    1   C 2 THR A  27  THR A  29  0                                        
SHEET    2   C 2 GLU A  35  MET A  37 -1  O  VAL A  36   N  ALA A  28           
SHEET    1   D 2 GLU A  41  ASN A  43  0                                        
SHEET    2   D 2 VAL A  48  LYS A  50 -1  O  PHE A  49   N  VAL A  42           
SHEET    1   E 3 TRP A  76  THR A  91  0                                        
SHEET    2   E 3 ALA A  98  ARG A 114 -1  O  ALA A  98   N  THR A  91           
SHEET    3   E 3 PHE B  12  SER B  13 -1  O  PHE B  12   N  LEU A 112           
SHEET    1   F 2 VAL B  18  VAL B  22  0                                        
SHEET    2   F 2 PHE B  53  LYS B  57 -1  O  PHE B  53   N  VAL B  22           
SHEET    1   G 2 VAL B  42  ASN B  43  0                                        
SHEET    2   G 2 VAL B  48  PHE B  49 -1  O  PHE B  49   N  VAL B  42           
SHEET    1   H 2 GLU X  23  GLN X  27  0                                        
SHEET    2   H 2 VAL X  35  PRO X  38 -1  O  VAL X  35   N  ALA X  26           
SHEET    1   I 2 THR X  44  PHE X  45  0                                        
SHEET    2   I 2 LYS X  56  PRO X  57 -1  O  LYS X  56   N  PHE X  45           
SHEET    1   J 2 GLN X  65  ALA X  69  0                                        
SHEET    2   J 2 VAL X  78  CYS X  81 -1  O  ARG X  80   N  SER X  66           
SHEET    1   K 2 TYR X  85  GLN X  87  0                                        
SHEET    2   K 2 CYS X  94  ALA X  96 -1  O  GLU X  95   N  TYR X  86           
SHEET    1   L 2 SER X 104  PHE X 108  0                                        
SHEET    2   L 2 VAL X 117  GLU X 120 -1  O  GLU X 119   N  GLY X 105           
SHEET    1   M 2 THR X 125  TYR X 126  0                                        
SHEET    2   M 2 LEU X 137  PRO X 138 -1  O  LEU X 137   N  TYR X 126           
SSBOND   1 CYS A   15    CYS A   80                          1555   1555  2.02  
SSBOND   2 CYS A   58    CYS A  108                          1555   1555  2.03  
SSBOND   3 CYS A   68    CYS A  110                          1555   1555  2.04  
SSBOND   4 CYS B   15    CYS B   80                          1555   1555  2.03  
SSBOND   5 CYS B   58    CYS B  108                          1555   1555  2.04  
SSBOND   6 CYS B   68    CYS B  110                          1555   1555  2.03  
SSBOND   7 CYS X    4    CYS X   15                          1555   1555  2.03  
SSBOND   8 CYS X   16    CYS X   29                          1555   1555  2.03  
SSBOND   9 CYS X   19    CYS X   36                          1555   1555  2.03  
SSBOND  10 CYS X   39    CYS X   55                          1555   1555  2.04  
SSBOND  11 CYS X   58    CYS X   71                          1555   1555  2.03  
SSBOND  12 CYS X   61    CYS X   79                          1555   1555  2.03  
SSBOND  13 CYS X   81    CYS X   94                          1555   1555  2.03  
SSBOND  14 CYS X   97    CYS X  110                          1555   1555  2.02  
SSBOND  15 CYS X  100    CYS X  118                          1555   1555  2.04  
SSBOND  16 CYS X  121    CYS X  136                          1555   1555  2.04  
SSBOND  17 CYS X  139    CYS X  152                          1555   1555  2.03  
SSBOND  18 CYS X  142    CYS X  160                          1555   1555  2.04  
SITE     1 AC1  3 VAL A 109  CYS A 110  CYS B 110                               
CRYST1   49.692   91.796   92.010  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020124  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010894  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010868        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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