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Database: PDB
Entry: 1WWW
LinkDB: 1WWW
Original site: 1WWW 
HEADER    NERVE GROWTH FACTOR/TRKA COMPLEX        12-MAR-99   1WWW              
TITLE     NGF IN COMPLEX WITH DOMAIN 5 OF THE TRKA RECEPTOR                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (NERVE GROWTH FACTOR);                             
COMPND   3 CHAIN: V, W;                                                         
COMPND   4 SYNONYM: BETA-NGF;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROTEIN (TRKA RECEPTOR);                                   
COMPND   8 CHAIN: X, Y;                                                         
COMPND   9 FRAGMENT: DOMAIN 5;                                                  
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    COMPLEX, TRKA RECEPTOR, NERVE GROWTH FACTOR, CYSTEINE KNOT,           
KEYWDS   2 IMMUNOGLOBULIN LIKE DOMAIN, NERVE GROWTH FACTOR/TRKA                 
KEYWDS   3 COMPLEX COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.WIESMANN,M.H.ULTSCH,A.M.DE VOS                                      
REVDAT   3   24-FEB-09 1WWW    1       VERSN                                    
REVDAT   2   01-APR-03 1WWW    1       JRNL                                     
REVDAT   1   15-SEP-99 1WWW    0                                                
JRNL        AUTH   C.WIESMANN,M.H.ULTSCH,S.H.BASS,A.M.DE VOS                    
JRNL        TITL   CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR IN                  
JRNL        TITL 2 COMPLEX WITH THE LIGAND-BINDING DOMAIN OF THE TRKA           
JRNL        TITL 3 RECEPTOR.                                                    
JRNL        REF    NATURE                        V. 401   184 1999              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   10490030                                                     
JRNL        DOI    10.1038/43705                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.200                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 22780                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGOUT                       
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2282                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2391                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE                    : 0.3784                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 259                          
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            : 3283                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 262                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.91                            
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) : 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  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 1WWW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000637.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 160                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23361                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1BET                                                 
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE COLLECTED AT THE ADVANCED LIGHT SOURCE,            
REMARK 200  BERKELEY                                                            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       26.86750            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: V, W, 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     SER V     1                                                      
REMARK 465     PRO V    61                                                      
REMARK 465     ASN V    62                                                      
REMARK 465     PRO V    63                                                      
REMARK 465     VAL V    64                                                      
REMARK 465     ASP V    65                                                      
REMARK 465     SER V    66                                                      
REMARK 465     ALA V   116                                                      
REMARK 465     VAL V   117                                                      
REMARK 465     ARG V   118                                                      
REMARK 465     ARG V   119                                                      
REMARK 465     ALA V   120                                                      
REMARK 465     SER W     1                                                      
REMARK 465     PRO W    61                                                      
REMARK 465     ASN W    62                                                      
REMARK 465     PRO W    63                                                      
REMARK 465     VAL W    64                                                      
REMARK 465     ASP W    65                                                      
REMARK 465     SER W    66                                                      
REMARK 465     VAL W   117                                                      
REMARK 465     ARG W   118                                                      
REMARK 465     ARG W   119                                                      
REMARK 465     ALA W   120                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH W   130     O    HOH W   136              2.15            
REMARK 500   O    HOH V   131     O    HOH Y    86              2.17            
REMARK 500   O    HOH V   130     O    HOH V   178              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS X 345   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    LEU X 346   N   -  CA  -  C   ANGL. DEV. = -21.1 DEGREES          
REMARK 500    LEU Y 346   N   -  CA  -  C   ANGL. DEV. = -20.0 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    ASN V  45       41.54     21.28                                   
REMARK 500    ASN V  46     -130.37   -175.54                                   
REMARK 500    ASP V  93        2.43    -52.91                                   
REMARK 500    LYS V  95      -56.03   -161.26                                   
REMARK 500    THR V 106      -11.46   -140.49                                   
REMARK 500    ASN W  46       -0.13     70.25                                   
REMARK 500    ARG W  59        7.03    -68.51                                   
REMARK 500    MET X 296     -128.32   -120.17                                   
REMARK 500    ASN X 338       76.27     33.13                                   
REMARK 500    GLU X 339      127.99   -172.73                                   
REMARK 500    THR X 352     -166.16   -114.27                                   
REMARK 500    MET X 379      142.88   -172.34                                   
REMARK 500    MET Y 296     -131.70   -112.76                                   
REMARK 500    GLN Y 350       71.11     51.72                                   
REMARK 500    ASN Y 381       71.52   -155.34                                   
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 X  96        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH W 173        DISTANCE =  6.81 ANGSTROMS                       
DBREF  1WWW V    1   120  UNP    P01138   NGF_HUMAN      122    241             
DBREF  1WWW W    1   120  UNP    P01138   NGF_HUMAN      122    241             
DBREF  1WWW X  282   382  UNP    P04629   NTRK1_HUMAN    282    382             
DBREF  1WWW Y  282   382  UNP    P04629   NTRK1_HUMAN    282    382             
SEQRES   1 V  120  SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER          
SEQRES   2 V  120  VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR          
SEQRES   3 V  120  THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU          
SEQRES   4 V  120  GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR          
SEQRES   5 V  120  PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP          
SEQRES   6 V  120  SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER          
SEQRES   7 V  120  TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR          
SEQRES   8 V  120  MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE          
SEQRES   9 V  120  ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL          
SEQRES  10 V  120  ARG ARG ALA                                                  
SEQRES   1 W  120  SER SER SER HIS PRO ILE PHE HIS ARG GLY GLU PHE SER          
SEQRES   2 W  120  VAL CYS ASP SER VAL SER VAL TRP VAL GLY ASP LYS THR          
SEQRES   3 W  120  THR ALA THR ASP ILE LYS GLY LYS GLU VAL MET VAL LEU          
SEQRES   4 W  120  GLY GLU VAL ASN ILE ASN ASN SER VAL PHE LYS GLN TYR          
SEQRES   5 W  120  PHE PHE GLU THR LYS CYS ARG ASP PRO ASN PRO VAL ASP          
SEQRES   6 W  120  SER GLY CYS ARG GLY ILE ASP SER LYS HIS TRP ASN SER          
SEQRES   7 W  120  TYR CYS THR THR THR HIS THR PHE VAL LYS ALA LEU THR          
SEQRES   8 W  120  MET ASP GLY LYS GLN ALA ALA TRP ARG PHE ILE ARG ILE          
SEQRES   9 W  120  ASP THR ALA CYS VAL CYS VAL LEU SER ARG LYS ALA VAL          
SEQRES  10 W  120  ARG ARG ALA                                                  
SEQRES   1 X  101  VAL SER PHE PRO ALA SER VAL GLN LEU HIS THR ALA VAL          
SEQRES   2 X  101  GLU MET HIS HIS TRP CYS ILE PRO PHE SER VAL ASP GLY          
SEQRES   3 X  101  GLN PRO ALA PRO SER LEU ARG TRP LEU PHE ASN GLY SER          
SEQRES   4 X  101  VAL LEU ASN GLU THR SER PHE ILE PHE THR GLU PHE LEU          
SEQRES   5 X  101  GLU PRO ALA ALA ASN GLU THR VAL ARG HIS GLY CYS LEU          
SEQRES   6 X  101  ARG LEU ASN GLN PRO THR HIS VAL ASN ASN GLY ASN TYR          
SEQRES   7 X  101  THR LEU LEU ALA ALA ASN PRO PHE GLY GLN ALA SER ALA          
SEQRES   8 X  101  SER ILE MET ALA ALA PHE MET ASP ASN PRO                      
SEQRES   1 Y  101  VAL SER PHE PRO ALA SER VAL GLN LEU HIS THR ALA VAL          
SEQRES   2 Y  101  GLU MET HIS HIS TRP CYS ILE PRO PHE SER VAL ASP GLY          
SEQRES   3 Y  101  GLN PRO ALA PRO SER LEU ARG TRP LEU PHE ASN GLY SER          
SEQRES   4 Y  101  VAL LEU ASN GLU THR SER PHE ILE PHE THR GLU PHE LEU          
SEQRES   5 Y  101  GLU PRO ALA ALA ASN GLU THR VAL ARG HIS GLY CYS LEU          
SEQRES   6 Y  101  ARG LEU ASN GLN PRO THR HIS VAL ASN ASN GLY ASN TYR          
SEQRES   7 Y  101  THR LEU LEU ALA ALA ASN PRO PHE GLY GLN ALA SER ALA          
SEQRES   8 Y  101  SER ILE MET ALA ALA PHE MET ASP ASN PRO                      
FORMUL   5  HOH   *262(H2 O)                                                    
HELIX    1   1 PRO V    5  ARG V    9  5                                   5    
HELIX    2   2 PRO W    5  ARG W    9  5                                   5    
HELIX    3   3 HIS X  353  ASN X  355  5                                   3    
HELIX    4   4 HIS Y  353  ASN Y  355  5                                   3    
SHEET    1   A 2 SER V  17  VAL V  22  0                                        
SHEET    2   A 2 PHE V  53  CYS V  58 -1  N  LYS V  57   O  VAL V  18           
SHEET    1   B 2 THR V  27  THR V  29  0                                        
SHEET    2   B 2 GLU V  35  MET V  37 -1  N  VAL V  36   O  ALA V  28           
SHEET    1   C 2 GLU V  41  ASN V  43  0                                        
SHEET    2   C 2 VAL V  48  LYS V  50 -1  N  PHE V  49   O  VAL V  42           
SHEET    1   D 2 TRP V  76  MET V  92  0                                        
SHEET    2   D 2 ALA V  97  ARG V 114 -1  N  SER V 113   O  ASN V  77           
SHEET    1   E 2 SER W  17  VAL W  22  0                                        
SHEET    2   E 2 PHE W  53  CYS W  58 -1  N  LYS W  57   O  VAL W  18           
SHEET    1   F 2 THR W  27  THR W  29  0                                        
SHEET    2   F 2 GLU W  35  MET W  37 -1  N  VAL W  36   O  ALA W  28           
SHEET    1   G 2 GLU W  41  ILE W  44  0                                        
SHEET    2   G 2 SER W  47  LYS W  50 -1  N  PHE W  49   O  VAL W  42           
SHEET    1   H 2 TRP W  76  MET W  92  0                                        
SHEET    2   H 2 ALA W  97  ARG W 114 -1  N  SER W 113   O  ASN W  77           
SHEET    1   I 4 SER X 287  LEU X 290  0                                        
SHEET    2   I 4 TRP X 299  ASP X 306 -1  N  ASP X 306   O  SER X 287           
SHEET    3   I 4 ARG X 342  LEU X 348 -1  N  LEU X 348   O  TRP X 299           
SHEET    4   I 4 ILE X 328  PHE X 332 -1  N  GLU X 331   O  CYS X 345           
SHEET    1   J 3 SER X 312  PHE X 317  0                                        
SHEET    2   J 3 GLY X 357  ASN X 365 -1  N  ALA X 364   O  SER X 312           
SHEET    3   J 3 GLY X 368  ALA X 376 -1  N  ALA X 376   O  GLY X 357           
SHEET    1   K 4 SER Y 287  LEU Y 290  0                                        
SHEET    2   K 4 TRP Y 299  ASP Y 306 -1  N  ASP Y 306   O  SER Y 287           
SHEET    3   K 4 ARG Y 342  LEU Y 348 -1  N  LEU Y 348   O  TRP Y 299           
SHEET    4   K 4 ILE Y 328  PHE Y 332 -1  N  GLU Y 331   O  CYS Y 345           
SHEET    1   L 3 SER Y 312  PHE Y 317  0                                        
SHEET    2   L 3 GLY Y 357  ASN Y 365 -1  N  ALA Y 364   O  SER Y 312           
SHEET    3   L 3 GLY Y 368  ALA Y 376 -1  N  ALA Y 376   O  GLY Y 357           
SSBOND   1 CYS V   15    CYS V   80                          1555   1555  2.04  
SSBOND   2 CYS V   58    CYS V  108                          1555   1555  2.03  
SSBOND   3 CYS V   68    CYS V  110                          1555   1555  2.03  
SSBOND   4 CYS W   15    CYS W   80                          1555   1555  2.04  
SSBOND   5 CYS W   58    CYS W  108                          1555   1555  2.04  
SSBOND   6 CYS W   68    CYS W  110                          1555   1555  2.03  
SSBOND   7 CYS X  300    CYS X  345                          1555   1555  2.04  
SSBOND   8 CYS Y  300    CYS Y  345                          1555   1555  2.04  
CISPEP   1 GLN X  308    PRO X  309          0        -0.36                     
CISPEP   2 GLN Y  308    PRO Y  309          0         0.49                     
CRYST1   58.245   53.735   77.101  90.00 107.34  90.00 P 1 21 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      0.017169  0.000000  0.005360        0.00000                         
SCALE2      0.000000  0.018610  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013587        0.00000                         
MTRIX1   1  0.581280 -0.312710 -0.751210       14.78126    1                    
MTRIX2   1 -0.290550 -0.942110  0.167300        0.82210    1                    
MTRIX3   1 -0.760060  0.121000 -0.638490       30.56634    1                    
MTRIX1   2  0.569520 -0.311990 -0.760470       14.76906    1                    
MTRIX2   2 -0.329310 -0.934280  0.136670        2.01039    1                    
MTRIX3   2 -0.753130  0.172590 -0.634830       30.27118    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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