GenomeNet

Database: PDB
Entry: 1M27
LinkDB: 1M27
Original site: 1M27 
HEADER    SIGNALING PROTEIN, TRANSFERASE          21-JUN-02   1M27              
TITLE     CRYSTAL STRUCTURE OF SAP/FYNSH3/SLAM TERNARY COMPLEX                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SH2 DOMAIN PROTEIN 1A;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: XLP GENE PRODUCT, SAP, SLAM-ASSOCIATED PROTEIN, T           
COMPND   5 CELL SIGNAL TRANSDUCTION MOLECULE SAP, DUNCAN'S DISEASE              
COMPND   6 SH2-PROTEIN;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE;                 
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: SLAM PEPTIDE (RESIDUES 276-286);                           
COMPND  12 SYNONYM: SLAM, IPO-3, CD150 ANTIGEN, CDW150;                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FYN;                
COMPND  16 CHAIN: C;                                                            
COMPND  17 FRAGMENT: SH3 DOMAIN (RESIDUES 82-143);                              
COMPND  18 SYNONYM: FYN, P59-FYN, SYN, SLK;                                     
COMPND  19 EC: 2.7.1.112;                                                       
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
SOURCE  10 THIS SEQUENCE WAS CHEMICALLY SYNTHESIZED.;                           
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SH2-SH3 INTERACTION, SIGNALING PROTEIN, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.CHAN,J.GRIESBACH,H.K.SONG,F.POY,C.TERHORST,M.J.ECK                  
REVDAT   2   24-FEB-09 1M27    1       VERSN                                    
REVDAT   1   06-MAY-03 1M27    0                                                
JRNL        AUTH   B.CHAN,A.LANYI,H.K.SONG,J.GRIESBACH,                         
JRNL        AUTH 2 M.SIMARRO-GRANDE,F.POY,D.HOWIE,J.SUMEGI,C.TERHORST,          
JRNL        AUTH 3 M.J.ECK                                                      
JRNL        TITL   SAP COUPLES FYN TO SLAM IMMUNE RECEPTORS.                    
JRNL        REF    NAT.CELL BIOL.                V.   5   155 2003              
JRNL        REFN                   ISSN 1465-7392                               
JRNL        PMID   12545174                                                     
JRNL        DOI    10.1038/NCB920                                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 8291                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 967                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 20.00                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 967                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1407                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 86                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.26                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1M27 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016505.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 160                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRROR                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62846                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TARTRATE, PH 5.6, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 297K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.53950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       26.45450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       26.45450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       45.76975            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       26.45450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       26.45450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      137.30925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       26.45450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       26.45450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       45.76975            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       26.45450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       26.45450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      137.30925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       91.53950            
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 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 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  36       -2.36   -154.69                                   
REMARK 500    THR C  85      -50.79   -138.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 323        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH C 173        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH C 174        DISTANCE =  5.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLC A 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D4T   RELATED DB: PDB                                   
REMARK 900 SAP/SLAM COMPLEX                                                     
DBREF  1M27 A    1   104  UNP    O60880   SH21A_HUMAN      1    104             
DBREF  1M27 C   84   144  UNP    P06241   FYN_HUMAN       83    143             
DBREF  1M27 B  276   286  UNP    Q13291   SLAF1_HUMAN    276    286             
SEQRES   1 A  104  MET ASP ALA VAL ALA VAL TYR HIS GLY LYS ILE SER ARG          
SEQRES   2 A  104  GLU THR GLY GLU LYS LEU LEU LEU ALA THR GLY LEU ASP          
SEQRES   3 A  104  GLY SER TYR LEU LEU ARG ASP SER GLU SER VAL PRO GLY          
SEQRES   4 A  104  VAL TYR CYS LEU CYS VAL LEU TYR HIS GLY TYR ILE TYR          
SEQRES   5 A  104  THR TYR ARG VAL SER GLN THR GLU THR GLY SER TRP SER          
SEQRES   6 A  104  ALA GLU THR ALA PRO GLY VAL HIS LYS ARG TYR PHE ARG          
SEQRES   7 A  104  LYS ILE LYS ASN LEU ILE SER ALA PHE GLN LYS PRO ASP          
SEQRES   8 A  104  GLN GLY ILE VAL ILE PRO LEU GLN TYR PRO VAL GLU LYS          
SEQRES   1 B   11  LYS SER LEU THR ILE TYR ALA GLN VAL GLN LYS                  
SEQRES   1 C   61  VAL THR LEU PHE VAL ALA LEU TYR ASP TYR GLU ALA ARG          
SEQRES   2 C   61  THR GLU ASP ASP LEU SER PHE HIS LYS GLY GLU LYS PHE          
SEQRES   3 C   61  GLN ILE LEU ASN SER SER GLU GLY ASP TRP TRP GLU ALA          
SEQRES   4 C   61  ARG SER LEU THR THR GLY GLU THR GLY TYR ILE PRO SER          
SEQRES   5 C   61  ASN TYR VAL ALA PRO VAL ASP SER ILE                          
HET    FLC  A 300      13                                                       
HETNAM     FLC CITRATE ANION                                                    
FORMUL   4  FLC    C6 H5 O7 3-                                                  
FORMUL   5  HOH   *86(H2 O)                                                     
HELIX    1   1 SER A   12  GLY A   24  1                                  13    
HELIX    2   2 LYS A   79  PHE A   87  1                                   9    
SHEET    1   A 5 TYR A 100  PRO A 101  0                                        
SHEET    2   A 5 SER A  28  ASP A  33  1  N  TYR A  29   O  TYR A 100           
SHEET    3   A 5 VAL A  40  TYR A  47 -1  O  CYS A  44   N  LEU A  30           
SHEET    4   A 5 TYR A  50  GLN A  58 -1  O  VAL A  56   N  TYR A  41           
SHEET    5   A 5 TRP A  64  ALA A  66 -1  O  SER A  65   N  SER A  57           
SHEET    1   B 5 TYR A 100  PRO A 101  0                                        
SHEET    2   B 5 SER A  28  ASP A  33  1  N  TYR A  29   O  TYR A 100           
SHEET    3   B 5 VAL A  40  TYR A  47 -1  O  CYS A  44   N  LEU A  30           
SHEET    4   B 5 TYR A  50  GLN A  58 -1  O  VAL A  56   N  TYR A  41           
SHEET    5   B 5 THR B 279  ALA B 282  1  O  ILE B 280   N  THR A  53           
SHEET    1   C 5 THR C 130  PRO C 134  0                                        
SHEET    2   C 5 TRP C 119  SER C 124 -1  N  ALA C 122   O  GLY C 131           
SHEET    3   C 5 LYS C 108  ASN C 113 -1  N  GLN C 110   O  ARG C 123           
SHEET    4   C 5 LEU C  86  ALA C  89 -1  N  PHE C  87   O  PHE C 109           
SHEET    5   C 5 VAL C 138  PRO C 140 -1  O  ALA C 139   N  VAL C  88           
SITE     1 AC1  8 ARG A  32  SER A  34  GLU A  35  SER A  36                    
SITE     2 AC1  8 CYS A  42  ARG A  55  HOH A 322  TYR B 281                    
CRYST1   52.909   52.909  183.079  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018900  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005462        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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