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Database: PDB
Entry: 1FLR
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Original site: 1FLR 
HEADER    IMMUNOGLOBULIN                          19-JAN-95   1FLR              
TITLE     4-4-20 FAB FRAGMENT                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-4-20 (IG*G2A=KAPPA=) FAB FRAGMENT;                       
COMPND   3 CHAIN: L;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 4-4-20 (IG*G2A=KAPPA=) FAB FRAGMENT;                       
COMPND   6 CHAIN: H                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 STRAIN: BALB/C;                                                      
SOURCE   6 VARIANT: BALB/CV;                                                    
SOURCE   7 CELL_LINE: 4-4-20 MURINE-MURINE HYBRIDOMA;                           
SOURCE   8 ORGAN: SPLEEN;                                                       
SOURCE   9 CELL: LYMPHOCYTE-PLASMA CELL;                                        
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 STRAIN: BALB/C;                                                      
SOURCE  15 VARIANT: BALB/CV;                                                    
SOURCE  16 CELL_LINE: 4-4-20 MURINE-MURINE HYBRIDOMA;                           
SOURCE  17 ORGAN: SPLEEN;                                                       
SOURCE  18 CELL: LYMPHOCYTE-PLASMA CELL                                         
KEYWDS    IMMUNOGLOBULIN                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WHITLOW                                                             
REVDAT   4   13-JUL-11 1FLR    1       VERSN                                    
REVDAT   3   24-FEB-09 1FLR    1       VERSN                                    
REVDAT   2   01-APR-03 1FLR    1       JRNL                                     
REVDAT   1   15-SEP-95 1FLR    0                                                
JRNL        AUTH   M.WHITLOW,A.J.HOWARD,J.F.WOOD,E.W.VOSS JR.,K.D.HARDMAN       
JRNL        TITL   1.85 A STRUCTURE OF ANTI-FLUORESCEIN 4-4-20 FAB.             
JRNL        REF    PROTEIN ENG.                  V.   8   749 1995              
JRNL        REFN                   ISSN 0269-2139                               
JRNL        PMID   8637844                                                      
JRNL        DOI    10.1093/PROTEIN/8.8.749                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.N.HERRON,X.HE,M.L.MASON,E.W.VOSS JUNIOR,A.B.EDMUNDSON      
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF A FLUORESCEIN-FAB COMPLEX     
REMARK   1  TITL 2 CRYSTALLIZED IN 2-METHYL-2,4-PENTANEDIOL                     
REMARK   1  REF    PROTEINS                      V.   5   271 1989              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.L.GIBSON,J.N.HERRON,X.-M.HE,V.A.PATRICK,M.L.MASON,         
REMARK   1  AUTH 2 J.-N.LIN,D.M.KRANZ,E.W.VOSS JUNIOR,A.B.EDMUNDSON             
REMARK   1  TITL   DIFFERENCES IN CRYSTAL PROPERTIES AND LIGAND AFFINITIES OF   
REMARK   1  TITL 2 AN ANTIFLUORESCYL FAB (4-4-20) IN TWO SOLVENT SYSTEMS        
REMARK   1  REF    PROTEINS                      V.   3   155 1988              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   W.D.BEDZYK,L.S.JOHNSON,G.S.RIORDON,E.W.VOSS                  
REMARK   1  TITL   COMPARISON OF VARIABLE REGION PRIMARY STRUCTURES WITHIN AN   
REMARK   1  TITL 2 ANTI-FLUORESCEIN IDIOTYPE FAMILY                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  1565 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 26328                          
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 + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3350                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 290                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.017 ; 0.015               
REMARK   3    ANGLE DISTANCE                  (A) : 0.037 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.047 ; 0.040               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.015 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.191 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.191 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.271 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.305 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.600 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 21.400; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 16.871; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 17.107; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 19.144; 1.500               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 20.506; 2.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  RESIDUES CYS H 133 TO GLY H 138 ARE IN WEAK ELECTRON                
REMARK   3  DENSITY.  THERE IS A DISCONTINUITY IN THE ELECTION DENSITY          
REMARK   3  MAP BETWEEN RESIDUES VAL H 132 AND CYS H 133.  THE                  
REMARK   3  RESULTING COORDINATES, AS PRESENTED IN THIS ENTRY, CONTAIN          
REMARK   3  TWO POSITIONS FOR N CYS H 133, ONE OF WHICH IS PROPERLY             
REMARK   3  CONNECTED TO C VAL H 132 BUT QUITE DISTANT (5.58 ANGSTROMS)         
REMARK   3  FROM CA CYS H 133.  THE OTHER POSITION FOR N CYS H 133 IS           
REMARK   3  PROPERLY CONNECTED TO CA H 133 BUT QUITE DISTANT (4.51              
REMARK   3  ANGSTROMS) FROM C VAL H 132.                                        
REMARK   4                                                                      
REMARK   4 1FLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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        : 21-OCT-88                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS-NICOLET X100               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29963                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 70.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04100                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER H    77                                                      
REMARK 465     LYS H    78                                                      
REMARK 465     GLY H   219                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG L  24    CZ   NH1  NH2                                       
REMARK 470     ASP H 135    CG   OD1  OD2                                       
REMARK 470     THR H 136    OG1  CG2                                            
REMARK 470     THR H 137    OG1  CG2                                            
REMARK 470     GLY H 138    O                                                   
REMARK 470     GLU H 153    OE1  OE2                                            
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 H 682        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH H 736        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH H 737        DISTANCE =  7.50 ANGSTROMS                       
REMARK 525    HOH H 774        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH H 775        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH H 776        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH H 784        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH H 790        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH H 792        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH H 793        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH H 794        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH H 804        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH H 805        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH H 806        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH H 808        DISTANCE =  9.22 ANGSTROMS                       
REMARK 525    HOH H 815        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH H 820        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH H 825        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH H 837        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH H 856        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH L 623        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH L 712        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH L 721        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH L 747        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH L 748        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH L 770        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH L 773        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH L 841        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH L 842        DISTANCE =  7.57 ANGSTROMS                       
REMARK 525    HOH L 863        DISTANCE =  9.36 ANGSTROMS                       
REMARK 525    HOH L 882        DISTANCE = 13.72 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLU L 600                 
DBREF  1FLR L    1   219  GB     1589925  AAB09710         1    219             
DBREF  1FLR H  119   219  UNP    P01865   GCAM_MOUSE       1    101             
SEQADV 1FLR VAL L    2  GB   1589925   ILE     2 CONFLICT                       
SEQADV 1FLR THR L    7  GB   1589925   SER     7 CONFLICT                       
SEQADV 1FLR LEU L   29  GB   1589925   VAL    29 CONFLICT                       
SEQADV 1FLR ARG L   39  GB   1589925   GLU    39 CONFLICT                       
SEQADV 1FLR TYR L   41  GB   1589925   PHE    41 CONFLICT                       
SEQADV 1FLR VAL L   51  GB   1589925   LEU    51 CONFLICT                       
SEQADV 1FLR PHE L   92  GB   1589925   TYR    92 CONFLICT                       
SEQADV 1FLR SER L   94  GB   1589925   PHE    94 CONFLICT                       
SEQADV 1FLR SER L   96  GB   1589925   ALA    96 CONFLICT                       
SEQADV 1FLR THR L   97  GB   1589925   SER    97 CONFLICT                       
SEQADV 1FLR ASN L  217  GB   1589925   GLY   217 CONFLICT                       
SEQRES   1 L  219  ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL          
SEQRES   2 L  219  SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER          
SEQRES   3 L  219  GLN SER LEU VAL HIS SER ASN GLY ASN THR TYR LEU ARG          
SEQRES   4 L  219  TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS VAL LEU          
SEQRES   5 L  219  ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP          
SEQRES   6 L  219  ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU          
SEQRES   7 L  219  LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR          
SEQRES   8 L  219  PHE CYS SER GLN SER THR HIS VAL PRO TRP THR PHE GLY          
SEQRES   9 L  219  GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA          
SEQRES  10 L  219  PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU          
SEQRES  11 L  219  THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN          
SEQRES  12 L  219  PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP          
SEQRES  13 L  219  GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR          
SEQRES  14 L  219  ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER          
SEQRES  15 L  219  THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN          
SEQRES  16 L  219  SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER          
SEQRES  17 L  219  PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS                  
SEQRES   1 H  219  GLU VAL LYS LEU ASP GLU THR GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  219  PRO GLY ARG PRO MET LYS LEU SER CYS VAL ALA SER GLY          
SEQRES   3 H  219  PHE THR PHE SER ASP TYR TRP MET ASN TRP VAL ARG GLN          
SEQRES   4 H  219  SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLN ILE ARG          
SEQRES   5 H  219  ASN LYS PRO TYR ASN TYR GLU THR TYR TYR SER ASP SER          
SEQRES   6 H  219  VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS          
SEQRES   7 H  219  SER SER VAL TYR LEU GLN MET ASN ASN LEU ARG VAL GLU          
SEQRES   8 H  219  ASP MET GLY ILE TYR TYR CYS THR GLY SER TYR TYR GLY          
SEQRES   9 H  219  MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER          
SEQRES  10 H  219  SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA          
SEQRES  11 H  219  PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU          
SEQRES  12 H  219  GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 H  219  LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS          
SEQRES  14 H  219  THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU          
SEQRES  15 H  219  SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER          
SEQRES  16 H  219  GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER          
SEQRES  17 H  219  THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY                  
HET    FLU  L 600      25                                                       
HETNAM     FLU 2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-BENZOIC ACID                 
HETSYN     FLU FLUORESCEIN                                                      
FORMUL   3  FLU    C20 H12 O5                                                   
FORMUL   4  HOH   *290(H2 O)                                                    
HELIX    1   1 ALA L   85  ASP L   87  5                                   3    
HELIX    2   2 SER L  127  SER L  132  1                                   6    
HELIX    3   3 LYS L  188  ARG L  193  1                                   6    
HELIX    4   4 PHE H   29  ASP H   31  5                                   3    
HELIX    5   5 LYS H   54  TYR H   56  5                                   3    
HELIX    6   6 ASP H   64  VAL H   66  5                                   3    
HELIX    7   7 VAL H   90  ASP H   92  5                                   3    
HELIX    8   8 ASN H  160  GLY H  162  5                                   3    
HELIX    9   9 PRO H  205  SER H  207  5                                   3    
SHEET    1   A 4 THR L   5  THR L   7  0                                        
SHEET    2   A 4 ALA L  19  ARG L  24 -1  N  ARG L  24   O  THR L   5           
SHEET    3   A 4 ASP L  75  ILE L  80 -1  N  ILE L  80   O  ALA L  19           
SHEET    4   A 4 PHE L  67  SER L  72 -1  N  SER L  72   O  ASP L  75           
SHEET    1   B 5 SER L  10  VAL L  13  0                                        
SHEET    2   B 5 THR L 107  ILE L 111  1  N  LYS L 108   O  LEU L  11           
SHEET    3   B 5 GLY L  89  GLN L  95 -1  N  TYR L  91   O  THR L 107           
SHEET    4   B 5 LEU L  38  GLN L  43 -1  N  GLN L  43   O  VAL L  90           
SHEET    5   B 5 LYS L  50  ILE L  53 -1  N  ILE L  53   O  TRP L  40           
SHEET    1   C 4 THR L 119  PHE L 123  0                                        
SHEET    2   C 4 GLY L 134  ASN L 142 -1  N  ASN L 142   O  THR L 119           
SHEET    3   C 4 MET L 180  THR L 187 -1  N  LEU L 186   O  ALA L 135           
SHEET    4   C 4 VAL L 164  TRP L 168 -1  N  SER L 167   O  SER L 181           
SHEET    1   D 3 ASN L 150  ILE L 155  0                                        
SHEET    2   D 3 SER L 196  THR L 202 -1  N  THR L 202   O  ASN L 150           
SHEET    3   D 3 ILE L 210  ASN L 215 -1  N  PHE L 214   O  TYR L 197           
SHEET    1   E 3 MET H  18  VAL H  23  0                                        
SHEET    2   E 3 SER H  80  MET H  85 -1  N  MET H  85   O  MET H  18           
SHEET    3   E 3 PHE H  70  ASP H  75 -1  N  ASP H  75   O  SER H  80           
SHEET    1   F 5 THR H 112  VAL H 114  0                                        
SHEET    2   F 5 GLY H  94  SER H 101 -1  N  TYR H  96   O  THR H 112           
SHEET    3   F 5 TRP H  33  GLN H  39 -1  N  GLN H  39   O  ILE H  95           
SHEET    4   F 5 LEU H  45  ILE H  51 -1  N  ILE H  51   O  MET H  34           
SHEET    5   F 5 THR H  60  TYR H  62 -1  N  TYR H  61   O  GLN H  50           
SHEET    1   G 2 THR H  99  TYR H 102  0                                        
SHEET    2   G 2 MET H 105  TRP H 108 -1  N  TYR H 107   O  GLY H 100           
SHEET    1   H 4 SER H 125  LEU H 129  0                                        
SHEET    2   H 4 THR H 142  LYS H 148 -1  N  LYS H 148   O  SER H 125           
SHEET    3   H 4 LEU H 182  THR H 187 -1  N  VAL H 186   O  LEU H 143           
SHEET    4   H 4 VAL H 168  PHE H 171 -1  N  PHE H 171   O  SER H 183           
SHEET    1   I 3 THR H 156  TRP H 159  0                                        
SHEET    2   I 3 ILE H 198  HIS H 204 -1  N  ALA H 203   O  THR H 156           
SHEET    3   I 3 THR H 209  ILE H 215 -1  N  ILE H 215   O  ILE H 198           
SHEET    1   J 2 VAL H 174  GLN H 176  0                                        
SHEET    2   J 2 LEU H 179  THR H 181 -1  N  THR H 181   O  VAL H 174           
SSBOND   1 CYS L   23    CYS L   93                          1555   1555  1.96  
SSBOND   2 CYS L  139    CYS L  199                          1555   1555  1.95  
SSBOND   3 CYS L  219    CYS H  133                          1555   1555  2.07  
SSBOND   4 CYS H   22    CYS H   98                          1555   1555  2.02  
SSBOND   5 CYS H  145    CYS H  200                          1555   1555  2.02  
CISPEP   1 THR L    7    PRO L    8          0        -1.93                     
CISPEP   2 VAL L   99    PRO L  100          0         0.90                     
CISPEP   3 TYR L  145    PRO L  146          0         2.36                     
CISPEP   4 PHE H  151    PRO H  152          0         1.20                     
CISPEP   5 TRP H  193    PRO H  194          0         0.57                     
SITE     1 AC1 11 TRP H  33  TYR H  56  TYR H 102  TYR H 103                    
SITE     2 AC1 11 GLY H 104  HOH H 677  HIS L  31  TYR L  37                    
SITE     3 AC1 11 ARG L  39  SER L  96  TRP L 101                               
CRYST1   42.750   43.870   58.170  95.15  86.85  98.01 P 1           1          
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      0.023392  0.003292 -0.001018        0.00000                         
SCALE2      0.000000  0.023019  0.001918        0.00000                         
SCALE3      0.000000  0.000000  0.017277        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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