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Database: PDB
Entry: 1G82
LinkDB: 1G82
Original site: 1G82 
HEADER    HORMONE/GROWTH FACTOR                   16-NOV-00   1G82              
TITLE     STRUCTURE OF FIBROBLAST GROWTH FACTOR 9                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR 9;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 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: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBACPAK9                                  
KEYWDS    FIBROBLAST GROWTH FACTOR, HORMONE-GROWTH FACTOR COMPLEX               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.J.HECHT,R.ADAR,B.HOFMANN,O.BOGIN,H.WEICH,A.YAYON                    
REVDAT   3   13-JUL-11 1G82    1       VERSN                                    
REVDAT   2   24-FEB-09 1G82    1       VERSN                                    
REVDAT   1   07-MAR-01 1G82    0                                                
JRNL        AUTH   H.J.HECHT,R.ADAR,B.HOFMANN,O.BOGIN,H.WEICH,A.YAYON           
JRNL        TITL   STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 SHOWS A SYMMETRIC    
JRNL        TITL 2 DIMER WITH UNIQUE RECEPTOR- AND HEPARIN-BINDING INTERFACES.  
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  57   378 2001              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   11223514                                                     
JRNL        DOI    10.1107/S0907444900020813                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38917                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2058                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5145                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 188                                     
REMARK   3   SOLVENT ATOMS            : 147                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.00000                                             
REMARK   3    B22 (A**2) : -0.00000                                             
REMARK   3    B33 (A**2) : 1.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.034 ; 0.021               
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.389 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.558 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.728 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.009 ; 4.500                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1G82 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB012350.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-DEC-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07                               
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40985                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2AFG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES, TRIS, PH 5.2,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       75.97350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       75.97350            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.61500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       75.97350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.30750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       75.97350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       87.92250            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       75.97350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       75.97350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.61500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       75.97350            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       87.92250            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       75.97350            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       29.30750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER. THE ASYMMETRIC UNIT      
REMARK 300 CONTAINS TWO DIMERS. THE DIMERS ARE FORMED BY MOLECULE A AND D, AND  
REMARK 300 B AND C.                                                             
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000      227.92050            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -29.30750            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C                            
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     PRO A    49                                                      
REMARK 465     ALA A    50                                                      
REMARK 465     VAL A    51                                                      
REMARK 465     PRO B    49                                                      
REMARK 465     ALA B    50                                                      
REMARK 465     SER B   208                                                      
REMARK 465     PRO C    49                                                      
REMARK 465     ALA C    50                                                      
REMARK 465     VAL C    51                                                      
REMARK 465     GLN C   207                                                      
REMARK 465     SER C   208                                                      
REMARK 465     ILE D   204                                                      
REMARK 465     LEU D   205                                                      
REMARK 465     SER D   206                                                      
REMARK 465     GLN D   207                                                      
REMARK 465     SER D   208                                                      
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    ASN D   119     N    GLY D   122              2.05            
REMARK 500   OG1  THR A   158     O    HOH A   709              2.14            
REMARK 500   O    HOH A   690     O    HOH A   699              2.17            
REMARK 500   NH2  ARG A   161     O4   SO4 A   294              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 123   CD    GLU A 123   OE1     0.068                       
REMARK 500    GLU A 128   CD    GLU A 128   OE1     0.066                       
REMARK 500    TRP A 144   CB    TRP A 144   CG     -0.124                       
REMARK 500    VAL A 156   CB    VAL A 156   CG1    -0.146                       
REMARK 500    ARG A 160   CB    ARG A 160   CG     -0.205                       
REMARK 500    TYR A 162   CD1   TYR A 162   CE1    -0.098                       
REMARK 500    TYR A 162   CE2   TYR A 162   CD2    -0.121                       
REMARK 500    PRO A 172   C     PRO A 172   O      -0.131                       
REMARK 500    ARG A 173   C     ARG A 173   O       0.114                       
REMARK 500    LYS A 179   CD    LYS A 179   CE      0.179                       
REMARK 500    LYS A 179   CE    LYS A 179   NZ      0.203                       
REMARK 500    ARG A 190   CD    ARG A 190   NE     -0.104                       
REMARK 500    ASP A 195   CB    ASP A 195   CG      0.173                       
REMARK 500    TYR B 153   CE2   TYR B 153   CD2    -0.110                       
REMARK 500    TYR C  67   CD1   TYR C  67   CE1    -0.102                       
REMARK 500    GLU C 120   CD    GLU C 120   OE2     0.097                       
REMARK 500    ARG D  64   CD    ARG D  64   NE     -0.124                       
REMARK 500    PHE D  72   CG    PHE D  72   CD1    -0.105                       
REMARK 500    SER D  90   CA    SER D  90   CB     -0.092                       
REMARK 500    GLU D  96   CD    GLU D  96   OE1    -0.072                       
REMARK 500    GLU D 123   CG    GLU D 123   CD      0.095                       
REMARK 500    GLU D 123   CD    GLU D 123   OE1     0.085                       
REMARK 500    GLU D 128   CG    GLU D 128   CD      0.098                       
REMARK 500    TYR D 153   CG    TYR D 153   CD2    -0.085                       
REMARK 500    ARG D 161   CG    ARG D 161   CD     -0.150                       
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    ARG A  62   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A  63   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A  69   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    LEU A  74   CB  -  CG  -  CD1 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    LEU A 130   CB  -  CG  -  CD2 ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 173   CG  -  CD  -  NE  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    ARG A 190   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 190   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 195   CB  -  CG  -  OD2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ASP B  55   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 157   CB  -  CG  -  OD2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ASP B 169   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 193   CB  -  CG  -  OD2 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    LEU B 200   CB  -  CG  -  CD2 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ASP C  88   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C 157   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG C 190   CG  -  CD  -  NE  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    TYR C 201   CB  -  CA  -  C   ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ILE C 204   CG1 -  CB  -  CG2 ANGL. DEV. = -16.4 DEGREES          
REMARK 500    LEU C 205   CA  -  CB  -  CG  ANGL. DEV. =  19.2 DEGREES          
REMARK 500    ASP D  55   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG D  62   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG D  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG D  64   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ILE D  82   CG1 -  CB  -  CG2 ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ASP D 111   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    LEU D 152   CB  -  CG  -  CD2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ARG D 190   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP D 195   CB  -  CG  -  OD2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP D 203   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 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    ALA A 101     -178.20   -174.27                                   
REMARK 500    GLU A 141      -56.75   -124.78                                   
REMARK 500    GLU A 142      131.04   -172.85                                   
REMARK 500    TRP A 144       -2.37     74.24                                   
REMARK 500    ARG A 177       50.61   -118.58                                   
REMARK 500    VAL A 197       77.43   -114.48                                   
REMARK 500    THR B  52      115.01    -39.03                                   
REMARK 500    ASP B  53      149.17    -34.53                                   
REMARK 500    ASN B  79        8.65    -69.02                                   
REMARK 500    ALA B 101      175.88    174.54                                   
REMARK 500    GLU B 141      -82.54   -103.40                                   
REMARK 500    ASN B 143       50.22     35.19                                   
REMARK 500    LEU B 152      -78.45   -104.25                                   
REMARK 500    LYS B 168       -5.44    -58.48                                   
REMARK 500    ARG B 177       33.79    -90.60                                   
REMARK 500    LYS B 183      -41.59    -28.60                                   
REMARK 500    GLU B 199       55.09   -100.17                                   
REMARK 500    LEU B 200      -32.68   -135.03                                   
REMARK 500    ALA C 101      178.59    177.06                                   
REMARK 500    GLU C 141      -77.16   -132.46                                   
REMARK 500    GLU C 142     -110.41    -97.03                                   
REMARK 500    ASN C 143       73.75   -116.86                                   
REMARK 500    TRP C 144       -9.56     83.42                                   
REMARK 500    LEU C 200      -29.22    -33.57                                   
REMARK 500    LYS C 202        2.30   -168.28                                   
REMARK 500    LEU C 205       10.83    -61.73                                   
REMARK 500    GLU D 141      -58.91   -124.74                                   
REMARK 500    VAL D 197       58.73   -152.40                                   
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    SER C 206        20.8      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 NAG A 651                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 652                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 653                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 651                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 651                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 652                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC C 653                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 651                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 652                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC D 653                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 292                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 293                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 294                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 295                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 296                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 297                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 298                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 299                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301                 
DBREF  1G82 A   49   208  PIR    A48137   A48137          49    208             
DBREF  1G82 B   49   208  PIR    A48137   A48137          49    208             
DBREF  1G82 C   49   208  PIR    A48137   A48137          49    208             
DBREF  1G82 D   49   208  PIR    A48137   A48137          49    208             
SEQRES   1 A  160  PRO ALA VAL THR ASP LEU ASP HIS LEU LYS GLY ILE LEU          
SEQRES   2 A  160  ARG ARG ARG GLN LEU TYR CYS ARG THR GLY PHE HIS LEU          
SEQRES   3 A  160  GLU ILE PHE PRO ASN GLY THR ILE GLN GLY THR ARG LYS          
SEQRES   4 A  160  ASP HIS SER ARG PHE GLY ILE LEU GLU PHE ILE SER ILE          
SEQRES   5 A  160  ALA VAL GLY LEU VAL SER ILE ARG GLY VAL ASP SER GLY          
SEQRES   6 A  160  LEU TYR LEU GLY MET ASN GLU LYS GLY GLU LEU TYR GLY          
SEQRES   7 A  160  SER GLU LYS LEU THR GLN GLU CYS VAL PHE ARG GLU GLN          
SEQRES   8 A  160  PHE GLU GLU ASN TRP TYR ASN THR TYR SER SER ASN LEU          
SEQRES   9 A  160  TYR LYS HIS VAL ASP THR GLY ARG ARG TYR TYR VAL ALA          
SEQRES  10 A  160  LEU ASN LYS ASP GLY THR PRO ARG GLU GLY THR ARG THR          
SEQRES  11 A  160  LYS ARG HIS GLN LYS PHE THR HIS PHE LEU PRO ARG PRO          
SEQRES  12 A  160  VAL ASP PRO ASP LYS VAL PRO GLU LEU TYR LYS ASP ILE          
SEQRES  13 A  160  LEU SER GLN SER                                              
SEQRES   1 B  160  PRO ALA VAL THR ASP LEU ASP HIS LEU LYS GLY ILE LEU          
SEQRES   2 B  160  ARG ARG ARG GLN LEU TYR CYS ARG THR GLY PHE HIS LEU          
SEQRES   3 B  160  GLU ILE PHE PRO ASN GLY THR ILE GLN GLY THR ARG LYS          
SEQRES   4 B  160  ASP HIS SER ARG PHE GLY ILE LEU GLU PHE ILE SER ILE          
SEQRES   5 B  160  ALA VAL GLY LEU VAL SER ILE ARG GLY VAL ASP SER GLY          
SEQRES   6 B  160  LEU TYR LEU GLY MET ASN GLU LYS GLY GLU LEU TYR GLY          
SEQRES   7 B  160  SER GLU LYS LEU THR GLN GLU CYS VAL PHE ARG GLU GLN          
SEQRES   8 B  160  PHE GLU GLU ASN TRP TYR ASN THR TYR SER SER ASN LEU          
SEQRES   9 B  160  TYR LYS HIS VAL ASP THR GLY ARG ARG TYR TYR VAL ALA          
SEQRES  10 B  160  LEU ASN LYS ASP GLY THR PRO ARG GLU GLY THR ARG THR          
SEQRES  11 B  160  LYS ARG HIS GLN LYS PHE THR HIS PHE LEU PRO ARG PRO          
SEQRES  12 B  160  VAL ASP PRO ASP LYS VAL PRO GLU LEU TYR LYS ASP ILE          
SEQRES  13 B  160  LEU SER GLN SER                                              
SEQRES   1 C  160  PRO ALA VAL THR ASP LEU ASP HIS LEU LYS GLY ILE LEU          
SEQRES   2 C  160  ARG ARG ARG GLN LEU TYR CYS ARG THR GLY PHE HIS LEU          
SEQRES   3 C  160  GLU ILE PHE PRO ASN GLY THR ILE GLN GLY THR ARG LYS          
SEQRES   4 C  160  ASP HIS SER ARG PHE GLY ILE LEU GLU PHE ILE SER ILE          
SEQRES   5 C  160  ALA VAL GLY LEU VAL SER ILE ARG GLY VAL ASP SER GLY          
SEQRES   6 C  160  LEU TYR LEU GLY MET ASN GLU LYS GLY GLU LEU TYR GLY          
SEQRES   7 C  160  SER GLU LYS LEU THR GLN GLU CYS VAL PHE ARG GLU GLN          
SEQRES   8 C  160  PHE GLU GLU ASN TRP TYR ASN THR TYR SER SER ASN LEU          
SEQRES   9 C  160  TYR LYS HIS VAL ASP THR GLY ARG ARG TYR TYR VAL ALA          
SEQRES  10 C  160  LEU ASN LYS ASP GLY THR PRO ARG GLU GLY THR ARG THR          
SEQRES  11 C  160  LYS ARG HIS GLN LYS PHE THR HIS PHE LEU PRO ARG PRO          
SEQRES  12 C  160  VAL ASP PRO ASP LYS VAL PRO GLU LEU TYR LYS ASP ILE          
SEQRES  13 C  160  LEU SER GLN SER                                              
SEQRES   1 D  160  PRO ALA VAL THR ASP LEU ASP HIS LEU LYS GLY ILE LEU          
SEQRES   2 D  160  ARG ARG ARG GLN LEU TYR CYS ARG THR GLY PHE HIS LEU          
SEQRES   3 D  160  GLU ILE PHE PRO ASN GLY THR ILE GLN GLY THR ARG LYS          
SEQRES   4 D  160  ASP HIS SER ARG PHE GLY ILE LEU GLU PHE ILE SER ILE          
SEQRES   5 D  160  ALA VAL GLY LEU VAL SER ILE ARG GLY VAL ASP SER GLY          
SEQRES   6 D  160  LEU TYR LEU GLY MET ASN GLU LYS GLY GLU LEU TYR GLY          
SEQRES   7 D  160  SER GLU LYS LEU THR GLN GLU CYS VAL PHE ARG GLU GLN          
SEQRES   8 D  160  PHE GLU GLU ASN TRP TYR ASN THR TYR SER SER ASN LEU          
SEQRES   9 D  160  TYR LYS HIS VAL ASP THR GLY ARG ARG TYR TYR VAL ALA          
SEQRES  10 D  160  LEU ASN LYS ASP GLY THR PRO ARG GLU GLY THR ARG THR          
SEQRES  11 D  160  LYS ARG HIS GLN LYS PHE THR HIS PHE LEU PRO ARG PRO          
SEQRES  12 D  160  VAL ASP PRO ASP LYS VAL PRO GLU LEU TYR LYS ASP ILE          
SEQRES  13 D  160  LEU SER GLN SER                                              
MODRES 1G82 ASN A   79  ASN  GLYCOSYLATION SITE                                 
MODRES 1G82 ASN B   79  ASN  GLYCOSYLATION SITE                                 
MODRES 1G82 ASN C   79  ASN  GLYCOSYLATION SITE                                 
MODRES 1G82 ASN D   79  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 651      14                                                       
HET    NAG  A 652      14                                                       
HET    FUC  A 653      10                                                       
HET    NAG  B 651      14                                                       
HET    NAG  C 651      14                                                       
HET    NAG  C 652      14                                                       
HET    FUC  C 653      10                                                       
HET    NAG  D 651      14                                                       
HET    NAG  D 652      14                                                       
HET    FUC  D 653      10                                                       
HET    SO4  A 290       5                                                       
HET    SO4  B 291       5                                                       
HET    SO4  C 292       5                                                       
HET    SO4  D 293       5                                                       
HET    SO4  A 294       5                                                       
HET    SO4  B 295       5                                                       
HET    SO4  C 296       5                                                       
HET    SO4  D 297       5                                                       
HET    SO4  C 298       5                                                       
HET    SO4  A 299       5                                                       
HET    SO4  D 300       5                                                       
HET    SO4  C 301       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  NAG    7(C8 H15 N O6)                                               
FORMUL   5  FUC    3(C6 H12 O5)                                                 
FORMUL   9  SO4    12(O4 S 2-)                                                  
FORMUL  21  HOH   *147(H2 O)                                                    
HELIX    1   1 THR A   52  LEU A   61  1                                  10    
HELIX    2   2 THR A  131  CYS A  134  5                                   4    
HELIX    3   3 GLN A  182  THR A  185  5                                   4    
HELIX    4   4 ASP A  193  VAL A  197  5                                   5    
HELIX    5   5 GLU A  199  ILE A  204  5                                   6    
HELIX    6   6 ASP B   53  LEU B   61  1                                   9    
HELIX    7   7 SER B   90  GLY B   93  5                                   4    
HELIX    8   8 THR B  131  CYS B  134  5                                   4    
HELIX    9   9 GLU B  174  THR B  178  5                                   5    
HELIX   10  10 GLN B  182  THR B  185  5                                   4    
HELIX   11  11 LEU B  200  LEU B  205  1                                   6    
HELIX   12  12 ASP C   53  ARG C   62  1                                  10    
HELIX   13  13 SER C   90  GLY C   93  5                                   4    
HELIX   14  14 THR C  131  CYS C  134  5                                   4    
HELIX   15  15 GLU C  174  THR C  178  5                                   5    
HELIX   16  16 GLN C  182  THR C  185  5                                   4    
HELIX   17  17 ASP C  193  VAL C  197  5                                   5    
HELIX   18  18 VAL C  197  TYR C  201  5                                   5    
HELIX   19  19 PRO D   49  LEU D   61  1                                  13    
HELIX   20  20 SER D   90  GLY D   93  5                                   4    
HELIX   21  21 THR D  131  CYS D  134  5                                   4    
HELIX   22  22 GLU D  174  THR D  178  5                                   5    
HELIX   23  23 GLN D  182  THR D  185  5                                   4    
HELIX   24  24 ASP D  193  VAL D  197  5                                   5    
HELIX   25  25 VAL D  197  LYS D  202  5                                   6    
SHEET    1   A 8 ARG A 161  TYR A 163  0                                        
SHEET    2   A 8 TYR A 145  LYS A 154 -1  N  SER A 150   O  TYR A 162           
SHEET    3   A 8 PHE A 187  ARG A 190 -1  N  PHE A 187   O  ASN A 146           
SHEET    4   A 8 ARG A  63  CYS A  68 -1  O  GLN A  65   N  ARG A 190           
SHEET    5   A 8 LEU A  95  ALA A 101 -1  N  LEU A  95   O  ARG A  64           
SHEET    6   A 8 LEU A 104  GLY A 109 -1  O  LEU A 104   N  ILE A 100           
SHEET    7   A 8 PHE A 136  GLU A 142 -1  O  PHE A 136   N  VAL A 105           
SHEET    8   A 8 TYR A 145  LYS A 154 -1  O  TYR A 145   N  GLU A 141           
SHEET    1   B 2 HIS A  73  ILE A  76  0                                        
SHEET    2   B 2 ILE A  82  THR A  85 -1  O  GLN A  83   N  GLU A  75           
SHEET    1   C 2 TYR A 115  MET A 118  0                                        
SHEET    2   C 2 LEU A 124  SER A 127 -1  O  TYR A 125   N  GLY A 117           
SHEET    1   D11 ILE B  82  THR B  85  0                                        
SHEET    2   D11 PHE B  72  ILE B  76 -1  N  HIS B  73   O  THR B  85           
SHEET    3   D11 ARG B  63  CYS B  68 -1  O  LEU B  66   N  LEU B  74           
SHEET    4   D11 LEU B  95  ALA B 101 -1  N  LEU B  95   O  ARG B  64           
SHEET    5   D11 LEU B 104  GLY B 109 -1  N  LEU B 104   O  ALA B 101           
SHEET    6   D11 PHE B 136  GLU B 142 -1  N  PHE B 136   O  VAL B 105           
SHEET    7   D11 TYR B 145  LYS B 154 -1  N  TYR B 145   O  GLU B 142           
SHEET    8   D11 ARG B 161  TYR B 163 -1  O  TYR B 162   N  SER B 150           
SHEET    9   D11 TYR B 145  LYS B 154 -1  N  SER B 150   O  TYR B 162           
SHEET   10   D11 PHE B 187  ARG B 190 -1  O  PHE B 187   N  ASN B 146           
SHEET   11   D11 ARG B  63  CYS B  68 -1  O  GLN B  65   N  ARG B 190           
SHEET    1   E 2 TYR B 115  MET B 118  0                                        
SHEET    2   E 2 LEU B 124  SER B 127 -1  O  TYR B 125   N  GLY B 117           
SHEET    1   F11 ILE C  82  THR C  85  0                                        
SHEET    2   F11 PHE C  72  ILE C  76 -1  N  HIS C  73   O  THR C  85           
SHEET    3   F11 ARG C  63  CYS C  68 -1  O  LEU C  66   N  LEU C  74           
SHEET    4   F11 LEU C  95  ALA C 101 -1  O  LEU C  95   N  ARG C  64           
SHEET    5   F11 LEU C 104  GLY C 109 -1  N  LEU C 104   O  ALA C 101           
SHEET    6   F11 PHE C 136  PHE C 140 -1  N  PHE C 136   O  VAL C 105           
SHEET    7   F11 ASN C 146  LYS C 154 -1  N  THR C 147   O  GLN C 139           
SHEET    8   F11 ARG C 161  TYR C 163 -1  O  TYR C 162   N  SER C 150           
SHEET    9   F11 ASN C 146  LYS C 154 -1  N  SER C 150   O  TYR C 162           
SHEET   10   F11 PHE C 187  ARG C 190 -1  N  PHE C 187   O  ASN C 146           
SHEET   11   F11 ARG C  63  CYS C  68 -1  O  GLN C  65   N  ARG C 190           
SHEET    1   G 2 TYR C 115  MET C 118  0                                        
SHEET    2   G 2 LEU C 124  SER C 127 -1  O  TYR C 125   N  GLY C 117           
SHEET    1   H 8 ARG D 161  TYR D 163  0                                        
SHEET    2   H 8 TYR D 145  LYS D 154 -1  N  SER D 150   O  TYR D 162           
SHEET    3   H 8 PHE D 187  ARG D 190 -1  O  PHE D 187   N  ASN D 146           
SHEET    4   H 8 ARG D  63  CYS D  68 -1  O  GLN D  65   N  ARG D 190           
SHEET    5   H 8 LEU D  95  ALA D 101 -1  N  LEU D  95   O  ARG D  64           
SHEET    6   H 8 LEU D 104  GLY D 109 -1  N  LEU D 104   O  ALA D 101           
SHEET    7   H 8 PHE D 136  GLU D 142 -1  N  PHE D 136   O  VAL D 105           
SHEET    8   H 8 TYR D 145  LYS D 154 -1  N  TYR D 145   O  GLU D 142           
SHEET    1   I 2 HIS D  73  ILE D  76  0                                        
SHEET    2   I 2 ILE D  82  THR D  85 -1  O  GLN D  83   N  GLU D  75           
SHEET    1   J 2 TYR D 115  MET D 118  0                                        
SHEET    2   J 2 LEU D 124  SER D 127 -1  O  TYR D 125   N  GLY D 117           
LINK         C1  NAG A 651                 ND2 ASN A  79     1555   1555  1.42  
LINK         C1  NAG B 651                 ND2 ASN B  79     1555   1555  1.46  
LINK         C1  NAG C 651                 ND2 ASN C  79     1555   1555  1.46  
LINK         C1  NAG D 651                 ND2 ASN D  79     1555   1555  1.45  
LINK         O6  NAG A 651                 C1  FUC A 653     1555   1555  1.46  
LINK         O6  NAG C 651                 C1  FUC C 653     1555   1555  1.43  
LINK         O6  NAG D 651                 C1  FUC D 653     1555   1555  1.44  
LINK         O4  NAG A 651                 C1  NAG A 652     1555   1555  1.50  
LINK         O4  NAG C 651                 C1  NAG C 652     1555   1555  1.47  
LINK         O4  NAG D 651                 C1  NAG D 652     1555   1555  1.47  
LINK         ND2 ASN A  79                 C2  NAG A 651     1555   1555  2.03  
SITE     1 AC1  4 ASN A  79  NAG A 652  FUC A 653  HOH A 708                    
SITE     1 AC2  1 NAG A 651                                                     
SITE     1 AC3  4 PRO A  78  PHE A  92  NAG A 651  FUC C 653                    
SITE     1 AC4  1 ASN B  79                                                     
SITE     1 AC5  4 PHE C  77  ASN C  79  NAG C 652  FUC C 653                    
SITE     1 AC6  2 NAG C 651  FUC C 653                                          
SITE     1 AC7  4 FUC A 653  PHE C  92  NAG C 651  NAG C 652                    
SITE     1 AC8  8 THR A 158  GLY A 159  PHE D  77  ASN D  79                    
SITE     2 AC8  8 THR D  81  NAG D 652  FUC D 653  HOH D 701                    
SITE     1 AC9  3 PHE D  77  NAG D 651  FUC D 653                               
SITE     1 BC1  4 PHE D  92  NAG D 651  NAG D 652  HOH D 662                    
SITE     1 BC2  4 ARG A 160  ARG A 161  TYR A 163  ARG A 180                    
SITE     1 BC3  5 GLY B 159  ARG B 160  ARG B 161  TYR B 163                    
SITE     2 BC3  5 ARG B 180                                                     
SITE     1 BC4  5 ARG C 160  ARG C 161  TYR C 163  ARG C 180                    
SITE     2 BC4  5 HOH C 674                                                     
SITE     1 BC5  6 ARG D 160  ARG D 161  TYR D 163  ARG D 180                    
SITE     2 BC5  6 HOH D 660  HOH D 700                                          
SITE     1 BC6  3 ARG A 137  LYS A 154  ARG A 161                               
SITE     1 BC7  3 ARG B 137  LYS B 154  ARG B 161                               
SITE     1 BC8  3 ARG C 137  LYS C 154  ARG C 161                               
SITE     1 BC9  4 ARG D 137  LYS D 154  ARG D 161  HOH D 673                    
SITE     1 CC1  2 ARG C 160  LYS C 179                                          
SITE     1 CC2  2 ARG A 173  ARG A 177                                          
SITE     1 CC3  2 ARG D 173  ARG D 177                                          
SITE     1 CC4  2 ARG C 173  ARG C 177                                          
CRYST1  151.947  151.947  117.230  90.00  90.00  90.00 I 41         32          
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      0.006581  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006581  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008530        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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