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Entry: 1AGF
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HEADER    HISTOCOMPATIBILITY COMPLEX              24-MAR-97   1AGF              
TITLE     ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL CHANGES IN            
TITLE    2 HLA B8-HIV-1 GAG PEPTIDE (GGKKRYKL-5R MUTATION)                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: B*0801;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR;                                             
COMPND   5 SYNONYM: B8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BETA-2 MICROGLOBULIN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: EXTRACELLULAR;                                             
COMPND  11 SYNONYM: B2M;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: HIV-1 GAG PEPTIDE (GGKKRYKL - 5R MUTATION);                
COMPND  15 CHAIN: C;                                                            
COMPND  16 FRAGMENT: EXTRACELLULAR;                                             
COMPND  17 SYNONYM: PEPTIDE;                                                    
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: XA90;                                                     
SOURCE   6 GENE: GAG;                                                           
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)PLYSS;                         
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGMT7;                                    
SOURCE  11 EXPRESSION_SYSTEM_GENE: GAG;                                         
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 CELL_LINE: XA90;                                                     
SOURCE  17 GENE: GAG;                                                           
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: XA90;                                   
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PHN1;                                     
SOURCE  22 EXPRESSION_SYSTEM_GENE: GAG;                                         
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE  25 ORGANISM_TAXID: 11676                                                
KEYWDS    HLA B8, HIV, MHC CLASS I, HISTOCOMPATIBILITY COMPLEX                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.W.REID,S.MCADAM,K.J.SMITH,P.KLENERMAN,C.A.O'CALLAGHAN,              
AUTHOR   2 K.HARLOS,B.K.JAKOBSEN,A.J.MCMICHAEL,J.BELL,D.I.STUART,               
AUTHOR   3 E.Y.JONES                                                            
REVDAT   3   24-FEB-09 1AGF    1       VERSN                                    
REVDAT   2   01-APR-03 1AGF    1       JRNL                                     
REVDAT   1   16-JUN-97 1AGF    0                                                
JRNL        AUTH   S.W.REID,S.MCADAM,K.J.SMITH,P.KLENERMAN,                     
JRNL        AUTH 2 C.A.O'CALLAGHAN,K.HARLOS,B.K.JAKOBSEN,                       
JRNL        AUTH 3 A.J.MCMICHAEL,J.I.BELL,D.I.STUART,E.Y.JONES                  
JRNL        TITL   ANTAGONIST HIV-1 GAG PEPTIDES INDUCE STRUCTURAL              
JRNL        TITL 2 CHANGES IN HLA B8.                                           
JRNL        REF    J.EXP.MED.                    V. 184  2279 1996              
JRNL        REFN                   ISSN 0022-1007                               
JRNL        PMID   8976183                                                      
JRNL        DOI    10.1084/JEM.184.6.2279                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
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) : 14.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 26227                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3148                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 302                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.90                          
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) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
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) : 3.300 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.900 ; 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  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AGF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 187                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.76                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 26227                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
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) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: HLA B27                                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000 0.1M SODIUM CITRATE,        
REMARK 280  PH 6.5 0.03M AMMONIUM ACETATE                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.30000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.05000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.05000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  268   CB    CG    CD    CE    NZ                          
REMARK 480     LYS B   58   CB    CG    CD    CE    NZ                          
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    SER A   2      -15.05   -150.89                                   
REMARK 500    ARG A  14       79.54   -150.86                                   
REMARK 500    ASP A  29     -126.65     52.94                                   
REMARK 500    ARG A 111      148.58   -173.56                                   
REMARK 500    ASN A 114       88.03   -162.56                                   
REMARK 500    GLN A 224       45.54   -108.32                                   
REMARK 500    ARG A 239      -21.87     94.10                                   
REMARK 500    TRP B  60       -1.67     76.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 116         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 296        DISTANCE =  7.57 ANGSTROMS                       
REMARK 525    HOH A 297        DISTANCE = 10.45 ANGSTROMS                       
REMARK 525    HOH A 298        DISTANCE = 11.68 ANGSTROMS                       
REMARK 525    HOH B 160        DISTANCE =  9.60 ANGSTROMS                       
REMARK 525    HOH A 402        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A 436        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH A 441        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A 491        DISTANCE =  5.48 ANGSTROMS                       
DBREF  1AGF A    1   276  UNP    P30460   1B08_HUMAN      25    300             
DBREF  1AGF B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  1AGF C    1     8  PDB    1AGF     1AGF             1      8             
SEQRES   1 A  276  GLY SER HIS SER MET ARG TYR PHE ASP THR ALA MET SER          
SEQRES   2 A  276  ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE SER VAL GLY          
SEQRES   3 A  276  TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  276  ALA ALA SER PRO ARG GLU GLU PRO ARG ALA PRO TRP ILE          
SEQRES   5 A  276  GLU GLN GLU GLY PRO GLU TYR TRP ASP ARG ASN THR GLN          
SEQRES   6 A  276  ILE PHE LYS THR ASN THR GLN THR ASP ARG GLU SER LEU          
SEQRES   7 A  276  ARG ASN LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY          
SEQRES   8 A  276  SER HIS THR LEU GLN SER MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  276  PRO ASP GLY ARG LEU LEU ARG GLY HIS ASN GLN TYR ALA          
SEQRES  10 A  276  TYR ASP GLY LYS ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  276  ARG SER TRP THR ALA ALA ASP THR ALA ALA GLN ILE THR          
SEQRES  12 A  276  GLN ARG LYS TRP GLU ALA ALA ARG VAL ALA GLU GLN ASP          
SEQRES  13 A  276  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG          
SEQRES  14 A  276  ARG TYR LEU GLU ASN GLY LYS ASP THR LEU GLU ARG ALA          
SEQRES  15 A  276  ASP PRO PRO LYS THR HIS VAL THR HIS HIS PRO ILE SER          
SEQRES  16 A  276  ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  276  TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY          
SEQRES  18 A  276  GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG          
SEQRES  19 A  276  PRO ALA GLY ASP ARG THR PHE GLN LYS TRP ALA ALA VAL          
SEQRES  20 A  276  VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS HIS          
SEQRES  21 A  276  VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG          
SEQRES  22 A  276  TRP GLU PRO                                                  
SEQRES   1 B   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 B   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 B   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 B   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 B   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 C    8  GLY GLY LYS LYS ARG TYR LYS LEU                              
FORMUL   4  HOH   *302(H2 O)                                                    
HELIX    1   1 PRO A   50  ILE A   52  5                                   3    
HELIX    2   2 PRO A   57  TYR A   84  1                                  28    
HELIX    3   3 ALA A  140  ALA A  149  1                                  10    
HELIX    4   4 VAL A  152  GLU A  161  1                                  10    
HELIX    5   5 THR A  163  ASN A  174  1                                  12    
HELIX    6   6 LYS A  176  LEU A  179  1                                   4    
HELIX    7   7 THR A  225  ASP A  227  5                                   3    
HELIX    8   8 GLU A  254  ARG A  256  5                                   3    
SHEET    1   A 7 THR A  31  ASP A  37  0                                        
SHEET    2   A 7 ARG A  21  VAL A  28 -1  N  VAL A  28   O  THR A  31           
SHEET    3   A 7 HIS A   3  MET A  12 -1  N  MET A  12   O  ARG A  21           
SHEET    4   A 7 THR A  94  VAL A 103 -1  N  VAL A 103   O  HIS A   3           
SHEET    5   A 7 LEU A 109  TYR A 118 -1  N  ALA A 117   O  GLN A  96           
SHEET    6   A 7 LYS A 121  LEU A 126 -1  N  ILE A 124   O  TYR A 116           
SHEET    7   A 7 TRP A 133  ALA A 135 -1  N  THR A 134   O  ALA A 125           
SHEET    1   B 4 LYS A 186  PRO A 193  0                                        
SHEET    2   B 4 GLU A 198  PHE A 208 -1  N  LEU A 206   O  LYS A 186           
SHEET    3   B 4 PHE A 241  PRO A 250 -1  N  VAL A 249   O  ALA A 199           
SHEET    4   B 4 THR A 228  LEU A 230 -1  N  GLU A 229   O  ALA A 246           
SHEET    1   C 3 THR A 214  ARG A 219  0                                        
SHEET    2   C 3 TYR A 257  GLN A 262 -1  N  GLN A 262   O  THR A 214           
SHEET    3   C 3 LEU A 270  LEU A 272 -1  N  LEU A 272   O  CYS A 259           
SHEET    1   D 3 LYS B   6  SER B  11  0                                        
SHEET    2   D 3 SER B  20  PHE B  30 -1  N  SER B  28   O  LYS B   6           
SHEET    3   D 3 PHE B  62  THR B  71 -1  N  PHE B  70   O  ASN B  21           
SHEET    1   E 3 GLU B  36  LYS B  41  0                                        
SHEET    2   E 3 TYR B  78  ASN B  83 -1  N  ASN B  83   O  GLU B  36           
SHEET    3   E 3 LYS B  91  LYS B  94 -1  N  VAL B  93   O  CYS B  80           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.41  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.25  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.29  
CISPEP   1 TYR A  209    PRO A  210          0         1.17                     
CISPEP   2 HIS B   31    PRO B   32          0        -0.83                     
CRYST1   50.600   81.300  110.100  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019763  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012300  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009083        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system