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Database: PDB
Entry: 1F3U
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Original site: 1F3U 
HEADER    TRANSCRIPTION                           06-JUN-00   1F3U              
TITLE     CRYSTAL STRUCTURE OF THE RAP30/74 INTERACTION DOMAINS OF              
TITLE    2 HUMAN TFIIF                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION INITIATION FACTOR IIF, BETA                  
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, C, E, G;                                                   
COMPND   5 FRAGMENT: RESIDUES 2-119;                                            
COMPND   6 SYNONYM: TRANSCRIPTION INITIATION FACTOR RAP30;                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: TRANSCRIPTION INITIATION FACTOR IIF, ALPHA                 
COMPND  10 SUBUNIT;                                                             
COMPND  11 CHAIN: B, D, F, H;                                                   
COMPND  12 FRAGMENT: RESIDUES 2-172;                                            
COMPND  13 SYNONYM: TRANSCRIPTION INITIATION FACTOR RAP74;                      
COMPND  14 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 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    GENERAL TRANSCRIPTION INITIATION AND ELONGATION FACTOR, RNA           
KEYWDS   2 POLYMERASE II, NOVEL DIMERIZATION FOLD, BETA BARREL                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.GAISER,S.TAN,T.J.RICHMOND                                           
REVDAT   4   24-FEB-09 1F3U    1       VERSN                                    
REVDAT   3   01-APR-03 1F3U    1       JRNL                                     
REVDAT   2   07-NOV-00 1F3U    1       SHEET  REMARK                            
REVDAT   1   11-OCT-00 1F3U    0                                                
JRNL        AUTH   F.GAISER,S.TAN,T.J.RICHMOND                                  
JRNL        TITL   NOVEL DIMERIZATION FOLD OF RAP30/RAP74 IN HUMAN              
JRNL        TITL 2 TFIIF AT 1.7 A RESOLUTION.                                   
JRNL        REF    J.MOL.BIOL.                   V. 302  1119 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11183778                                                     
JRNL        DOI    10.1006/JMBI.2000.4110                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.Q.WANG,L.LEI,Z.F.BURTON                                    
REMARK   1  TITL   IMPORTANCE OF CODON PREFERENCE FOR PRODUCTION OF             
REMARK   1  TITL 2 HUMAN RAP74 AND RECONSTITUTION OF THE RAP30/74               
REMARK   1  TITL 3 COMPLEX                                                      
REMARK   1  REF    PROTEIN EXPR.PURIF.           V.   5   476 1994              
REMARK   1  REFN                   ISSN 1046-5928                               
REMARK   1  DOI    10.1006/PREP.1994.1067                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9A                                             
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1277208.220                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 105675                         
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) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3596                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9154                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 388                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8236                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 692                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.77000                                             
REMARK   3    B22 (A**2) : -1.64000                                             
REMARK   3    B33 (A**2) : 2.41000                                              
REMARK   3    B12 (A**2) : 2.79000                                              
REMARK   3    B13 (A**2) : 3.74000                                              
REMARK   3    B23 (A**2) : -1.22000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
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) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.38                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.23                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.77                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.270 ; 3.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.770 ; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.570 ; 5.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.420 ; 6.000                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.68                                                 
REMARK   3   BSOL        : 113.40                                               
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE VALUES WERE CALCULATED WITH ALL       
REMARK   3  ATOMS AT ZERO OCCUPANCY DELETED. REFMAC WAS ALSO USED FOR PART      
REMARK   3  OF THE REFINEMENT PROCESS. ALTERNATE POSITION INDICATORS            
REMARK   3  REPRESENT TWO COMPLETELY DIFFERENT CHAIN TRACES THAT ARE            
REMARK   3  INDUCED BY A CRYSTAL CONTACT. IF THE CORRESPONDING                  
REMARK   3  CONFORMATION B IS MISSING, THIS INDICATES THAT THIS BRANCH OF       
REMARK   3  THE CHAIN IS NOT OBSERVED.                                          
REMARK   4                                                                      
REMARK   4 1F3U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011209.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-NOV-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
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                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9330                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108916                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19400                            
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: NULL                         
REMARK 200 SOFTWARE USED: CNS 0.5                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1500, LITHIUM NITRATE, BIS-          
REMARK 280  TRIS, DTT, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  278K                                                                
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, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 4490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 4470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     SER B    65                                                      
REMARK 465     GLY B    66                                                      
REMARK 465     ALA B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     GLU B    70                                                      
REMARK 465     PHE B    71                                                      
REMARK 465     ASN B    72                                                      
REMARK 465     THR B   154                                                      
REMARK 465     LEU B   155                                                      
REMARK 465     THR B   156                                                      
REMARK 465     ALA B   157                                                      
REMARK 465     GLU B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ALA B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     GLU B   162                                                      
REMARK 465     GLU B   163                                                      
REMARK 465     TRP B   164                                                      
REMARK 465     GLU B   165                                                      
REMARK 465     ARG B   166                                                      
REMARK 465     ARG B   167                                                      
REMARK 465     ASN B   168                                                      
REMARK 465     LYS B   169                                                      
REMARK 465     VAL B   170                                                      
REMARK 465     LEU B   171                                                      
REMARK 465     ASN B   172                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     PRO D     6                                                      
REMARK 465     GLU D    64                                                      
REMARK 465     SER D    65                                                      
REMARK 465     GLY D    66                                                      
REMARK 465     ALA D    67                                                      
REMARK 465     GLY D    68                                                      
REMARK 465     SER D    69                                                      
REMARK 465     GLU D    70                                                      
REMARK 465     PHE D    71                                                      
REMARK 465     ASN D    72                                                      
REMARK 465     LYS D   169                                                      
REMARK 465     VAL D   170                                                      
REMARK 465     LEU D   171                                                      
REMARK 465     ASN D   172                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     LEU F     4                                                      
REMARK 465     PRO F    63                                                      
REMARK 465     GLU F    64                                                      
REMARK 465     SER F    65                                                      
REMARK 465     GLY F    66                                                      
REMARK 465     ALA F    67                                                      
REMARK 465     GLY F    68                                                      
REMARK 465     SER F    69                                                      
REMARK 465     GLU F    70                                                      
REMARK 465     PHE F    71                                                      
REMARK 465     ASN F    72                                                      
REMARK 465     LYS F   169                                                      
REMARK 465     VAL F   170                                                      
REMARK 465     LEU F   171                                                      
REMARK 465     ASN F   172                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     ALA H     3                                                      
REMARK 465     LEU H     4                                                      
REMARK 465     GLY H     5                                                      
REMARK 465     PRO H     6                                                      
REMARK 465     PRO H    63                                                      
REMARK 465     GLU H    64                                                      
REMARK 465     SER H    65                                                      
REMARK 465     GLY H    66                                                      
REMARK 465     ALA H    67                                                      
REMARK 465     GLY H    68                                                      
REMARK 465     SER H    69                                                      
REMARK 465     GLU H    70                                                      
REMARK 465     PHE H    71                                                      
REMARK 465     ASN H    72                                                      
REMARK 465     THR H   154                                                      
REMARK 465     LEU H   155                                                      
REMARK 465     THR H   156                                                      
REMARK 465     ALA H   157                                                      
REMARK 465     GLU H   158                                                      
REMARK 465     GLU H   159                                                      
REMARK 465     ALA H   160                                                      
REMARK 465     GLU H   161                                                      
REMARK 465     GLU H   162                                                      
REMARK 465     GLU H   163                                                      
REMARK 465     TRP H   164                                                      
REMARK 465     GLU H   165                                                      
REMARK 465     ARG H   166                                                      
REMARK 465     ARG H   167                                                      
REMARK 465     ASN H   168                                                      
REMARK 465     LYS H   169                                                      
REMARK 465     VAL H   170                                                      
REMARK 465     LEU H   171                                                      
REMARK 465     ASN H   172                                                      
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     SER C  76    OG                                                  
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     GLY B  116                                                       
REMARK 475     GLY B  117                                                       
REMARK 475     VAL B  118                                                       
REMARK 475     THR B  119                                                       
REMARK 475     VAL D  118                                                       
REMARK 475     THR D  119                                                       
REMARK 475     GLU F   77                                                       
REMARK 475     GLU F   78                                                       
REMARK 475     ALA F   79                                                       
REMARK 475     THR F  119                                                       
REMARK 475     THR F  154                                                       
REMARK 475     LEU F  155                                                       
REMARK 475     THR F  156                                                       
REMARK 475     ALA F  157                                                       
REMARK 475     GLU F  158                                                       
REMARK 475     GLY H  116                                                       
REMARK 475     GLY H  117                                                       
REMARK 475     VAL H  118                                                       
REMARK 475     THR H  119                                                       
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   71   CB    CG    CD    CE    NZ                          
REMARK 480     PRO A   72   CB    CG    CD                                      
REMARK 480     ALA A   73   CB                                                  
REMARK 480     SER A   74   CB    OG                                            
REMARK 480     VAL A   75   CB    CG1   CG2                                     
REMARK 480     SER A   76   CB    OG                                            
REMARK 480     LYS C   13   CB    CG    CD    CE    NZ                          
REMARK 480     LYS C   71   CB    CG    CD    CE    NZ                          
REMARK 480     PRO C   72   CB    CG    CD                                      
REMARK 480     ALA C   73   CB                                                  
REMARK 480     SER C   74   CB    OG                                            
REMARK 480     VAL C   75   CB    CG1   CG2                                     
REMARK 480     SER C   76   CB                                                  
REMARK 480     ALA C   77   CB                                                  
REMARK 480     ASN F   21   CB    CG    OD1   ND2                               
REMARK 480     ARG F   76   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG F   81   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     VAL F  118   CB    CG1   CG2                                     
REMARK 480     GLU F  159   CB    CG    CD    OE1   OE2                         
REMARK 480     LYS G   13   CB    CG    CD    CE    NZ                          
REMARK 480     SER H    8   CB    OG                                            
REMARK 480     ASN H   21   CB    CG    OD1   ND2                               
REMARK 480     THR H   22   OG1   CG2                                           
REMARK 480     THR H   23   OG1   CG2                                           
REMARK 480     LYS H   55   CB    CG    CD    CE    NZ                          
REMARK 480     ARG H   76   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS H   89   CG    CD    CE    NZ                                
REMARK 480     GLU H  120   CB    CG    CD    OE1   OE2                         
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    THR A  48     -166.70   -122.50                                   
REMARK 500    ILE A  68       96.74    -54.62                                   
REMARK 500    LYS A  71      149.84     50.72                                   
REMARK 500    PRO A  72     -114.24    -89.24                                   
REMARK 500    SER A  74      -38.88     62.44                                   
REMARK 500    SER A  76     -125.91    -13.22                                   
REMARK 500    GLN A  91      148.74    176.83                                   
REMARK 500    LYS B  36       69.57     34.09                                   
REMARK 500    LYS B  89      163.27    -45.86                                   
REMARK 500    THR B 119      161.25     15.43                                   
REMARK 500    GLU B 120     -111.39   -147.38                                   
REMARK 500    ARG C   4      152.61    -42.07                                   
REMARK 500    ASP C   8      100.40    -53.05                                   
REMARK 500    SER C  35     -144.15   -141.39                                   
REMARK 500    ILE C  68      123.55    -24.52                                   
REMARK 500    LYS C  71      124.31    -32.55                                   
REMARK 500    SER C  76      -88.85   -166.21                                   
REMARK 500    ARG C  79      126.73    -16.81                                   
REMARK 500    ASP C 102       11.85    108.10                                   
REMARK 500    THR D  22      130.18    170.40                                   
REMARK 500    LYS D  36       77.63     37.23                                   
REMARK 500    ASN D  43      -37.56   -137.52                                   
REMARK 500    ASN D  53       57.84   -104.87                                   
REMARK 500    ASN D 103       60.38     62.30                                   
REMARK 500    GLU D 120     -155.19   -108.16                                   
REMARK 500    ASP E 102       16.81     57.35                                   
REMARK 500    LYS F  36       72.28     39.17                                   
REMARK 500    ASN F  53       73.21   -104.28                                   
REMARK 500    ARG F  76      105.58    -55.83                                   
REMARK 500    GLU F  77      143.61    -16.37                                   
REMARK 500    ALA F  79       22.84     15.45                                   
REMARK 500    ARG F  80        9.41   -167.05                                   
REMARK 500    VAL F 118      115.63    118.01                                   
REMARK 500    THR F 154      -91.05   -148.26                                   
REMARK 500    LEU F 155       62.58      6.64                                   
REMARK 500    GLU F 159      -30.70   -134.83                                   
REMARK 500    ASN H  10     -163.59   -108.44                                   
REMARK 500    VAL H  11      173.45    159.82                                   
REMARK 500    LYS H  36       60.85     35.89                                   
REMARK 500    ILE H  56      164.29    -49.62                                   
REMARK 500    TYR H  57       95.16   -178.67                                   
REMARK 500    GLU H  59      170.12    -58.60                                   
REMARK 500    GLU H  60      126.91    176.69                                   
REMARK 500    ASN H 103       79.93     62.12                                   
REMARK 500    GLU H 120      -98.50   -160.70                                   
REMARK 500    ASP H 132        0.09    -69.82                                   
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 D 320        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH A 212        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A 213        DISTANCE = 19.41 ANGSTROMS                       
DBREF  1F3U A    2   119  UNP    P13984   T2FB_HUMAN       2    119             
DBREF  1F3U C    2   119  UNP    P13984   T2FB_HUMAN       2    119             
DBREF  1F3U E    2   119  UNP    P13984   T2FB_HUMAN       2    119             
DBREF  1F3U G    2   119  UNP    P13984   T2FB_HUMAN       2    119             
DBREF  1F3U B    2   172  UNP    P35269   T2FA_HUMAN       2    172             
DBREF  1F3U D    2   172  UNP    P35269   T2FA_HUMAN       2    172             
DBREF  1F3U F    2   172  UNP    P35269   T2FA_HUMAN       2    172             
DBREF  1F3U H    2   172  UNP    P35269   T2FA_HUMAN       2    172             
SEQRES   1 A  118  ALA GLU ARG GLY GLU LEU ASP LEU THR GLY ALA LYS GLN          
SEQRES   2 A  118  ASN THR GLY VAL TRP LEU VAL LYS VAL PRO LYS TYR LEU          
SEQRES   3 A  118  SER GLN GLN TRP ALA LYS ALA SER GLY ARG GLY GLU VAL          
SEQRES   4 A  118  GLY LYS LEU ARG ILE ALA LYS THR GLN GLY ARG THR GLU          
SEQRES   5 A  118  VAL SER PHE THR LEU ASN GLU ASP LEU ALA ASN ILE HIS          
SEQRES   6 A  118  ASP ILE GLY GLY LYS PRO ALA SER VAL SER ALA PRO ARG          
SEQRES   7 A  118  GLU HIS PRO PHE VAL LEU GLN SER VAL GLY GLY GLN THR          
SEQRES   8 A  118  LEU THR VAL PHE THR GLU SER SER SER ASP LYS LEU SER          
SEQRES   9 A  118  LEU GLU GLY ILE VAL VAL GLN ARG ALA GLU CYS ARG PRO          
SEQRES  10 A  118  ALA                                                          
SEQRES   1 B  171  ALA ALA LEU GLY PRO SER SER GLN ASN VAL THR GLU TYR          
SEQRES   2 B  171  VAL VAL ARG VAL PRO LYS ASN THR THR LYS LYS TYR ASN          
SEQRES   3 B  171  ILE MET ALA PHE ASN ALA ALA ASP LYS VAL ASN PHE ALA          
SEQRES   4 B  171  THR TRP ASN GLN ALA ARG LEU GLU ARG ASP LEU SER ASN          
SEQRES   5 B  171  LYS LYS ILE TYR GLN GLU GLU GLU MET PRO GLU SER GLY          
SEQRES   6 B  171  ALA GLY SER GLU PHE ASN ARG LYS LEU ARG GLU GLU ALA          
SEQRES   7 B  171  ARG ARG LYS LYS TYR GLY ILE VAL LEU LYS GLU PHE ARG          
SEQRES   8 B  171  PRO GLU ASP GLN PRO TRP LEU LEU ARG VAL ASN GLY LYS          
SEQRES   9 B  171  SER GLY ARG LYS PHE LYS GLY ILE LYS LYS GLY GLY VAL          
SEQRES  10 B  171  THR GLU ASN THR SER TYR TYR ILE PHE THR GLN CYS PRO          
SEQRES  11 B  171  ASP GLY ALA PHE GLU ALA PHE PRO VAL HIS ASN TRP TYR          
SEQRES  12 B  171  ASN PHE THR PRO LEU ALA ARG HIS ARG THR LEU THR ALA          
SEQRES  13 B  171  GLU GLU ALA GLU GLU GLU TRP GLU ARG ARG ASN LYS VAL          
SEQRES  14 B  171  LEU ASN                                                      
SEQRES   1 C  118  ALA GLU ARG GLY GLU LEU ASP LEU THR GLY ALA LYS GLN          
SEQRES   2 C  118  ASN THR GLY VAL TRP LEU VAL LYS VAL PRO LYS TYR LEU          
SEQRES   3 C  118  SER GLN GLN TRP ALA LYS ALA SER GLY ARG GLY GLU VAL          
SEQRES   4 C  118  GLY LYS LEU ARG ILE ALA LYS THR GLN GLY ARG THR GLU          
SEQRES   5 C  118  VAL SER PHE THR LEU ASN GLU ASP LEU ALA ASN ILE HIS          
SEQRES   6 C  118  ASP ILE GLY GLY LYS PRO ALA SER VAL SER ALA PRO ARG          
SEQRES   7 C  118  GLU HIS PRO PHE VAL LEU GLN SER VAL GLY GLY GLN THR          
SEQRES   8 C  118  LEU THR VAL PHE THR GLU SER SER SER ASP LYS LEU SER          
SEQRES   9 C  118  LEU GLU GLY ILE VAL VAL GLN ARG ALA GLU CYS ARG PRO          
SEQRES  10 C  118  ALA                                                          
SEQRES   1 D  171  ALA ALA LEU GLY PRO SER SER GLN ASN VAL THR GLU TYR          
SEQRES   2 D  171  VAL VAL ARG VAL PRO LYS ASN THR THR LYS LYS TYR ASN          
SEQRES   3 D  171  ILE MET ALA PHE ASN ALA ALA ASP LYS VAL ASN PHE ALA          
SEQRES   4 D  171  THR TRP ASN GLN ALA ARG LEU GLU ARG ASP LEU SER ASN          
SEQRES   5 D  171  LYS LYS ILE TYR GLN GLU GLU GLU MET PRO GLU SER GLY          
SEQRES   6 D  171  ALA GLY SER GLU PHE ASN ARG LYS LEU ARG GLU GLU ALA          
SEQRES   7 D  171  ARG ARG LYS LYS TYR GLY ILE VAL LEU LYS GLU PHE ARG          
SEQRES   8 D  171  PRO GLU ASP GLN PRO TRP LEU LEU ARG VAL ASN GLY LYS          
SEQRES   9 D  171  SER GLY ARG LYS PHE LYS GLY ILE LYS LYS GLY GLY VAL          
SEQRES  10 D  171  THR GLU ASN THR SER TYR TYR ILE PHE THR GLN CYS PRO          
SEQRES  11 D  171  ASP GLY ALA PHE GLU ALA PHE PRO VAL HIS ASN TRP TYR          
SEQRES  12 D  171  ASN PHE THR PRO LEU ALA ARG HIS ARG THR LEU THR ALA          
SEQRES  13 D  171  GLU GLU ALA GLU GLU GLU TRP GLU ARG ARG ASN LYS VAL          
SEQRES  14 D  171  LEU ASN                                                      
SEQRES   1 E  118  ALA GLU ARG GLY GLU LEU ASP LEU THR GLY ALA LYS GLN          
SEQRES   2 E  118  ASN THR GLY VAL TRP LEU VAL LYS VAL PRO LYS TYR LEU          
SEQRES   3 E  118  SER GLN GLN TRP ALA LYS ALA SER GLY ARG GLY GLU VAL          
SEQRES   4 E  118  GLY LYS LEU ARG ILE ALA LYS THR GLN GLY ARG THR GLU          
SEQRES   5 E  118  VAL SER PHE THR LEU ASN GLU ASP LEU ALA ASN ILE HIS          
SEQRES   6 E  118  ASP ILE GLY GLY LYS PRO ALA SER VAL SER ALA PRO ARG          
SEQRES   7 E  118  GLU HIS PRO PHE VAL LEU GLN SER VAL GLY GLY GLN THR          
SEQRES   8 E  118  LEU THR VAL PHE THR GLU SER SER SER ASP LYS LEU SER          
SEQRES   9 E  118  LEU GLU GLY ILE VAL VAL GLN ARG ALA GLU CYS ARG PRO          
SEQRES  10 E  118  ALA                                                          
SEQRES   1 F  171  ALA ALA LEU GLY PRO SER SER GLN ASN VAL THR GLU TYR          
SEQRES   2 F  171  VAL VAL ARG VAL PRO LYS ASN THR THR LYS LYS TYR ASN          
SEQRES   3 F  171  ILE MET ALA PHE ASN ALA ALA ASP LYS VAL ASN PHE ALA          
SEQRES   4 F  171  THR TRP ASN GLN ALA ARG LEU GLU ARG ASP LEU SER ASN          
SEQRES   5 F  171  LYS LYS ILE TYR GLN GLU GLU GLU MET PRO GLU SER GLY          
SEQRES   6 F  171  ALA GLY SER GLU PHE ASN ARG LYS LEU ARG GLU GLU ALA          
SEQRES   7 F  171  ARG ARG LYS LYS TYR GLY ILE VAL LEU LYS GLU PHE ARG          
SEQRES   8 F  171  PRO GLU ASP GLN PRO TRP LEU LEU ARG VAL ASN GLY LYS          
SEQRES   9 F  171  SER GLY ARG LYS PHE LYS GLY ILE LYS LYS GLY GLY VAL          
SEQRES  10 F  171  THR GLU ASN THR SER TYR TYR ILE PHE THR GLN CYS PRO          
SEQRES  11 F  171  ASP GLY ALA PHE GLU ALA PHE PRO VAL HIS ASN TRP TYR          
SEQRES  12 F  171  ASN PHE THR PRO LEU ALA ARG HIS ARG THR LEU THR ALA          
SEQRES  13 F  171  GLU GLU ALA GLU GLU GLU TRP GLU ARG ARG ASN LYS VAL          
SEQRES  14 F  171  LEU ASN                                                      
SEQRES   1 G  118  ALA GLU ARG GLY GLU LEU ASP LEU THR GLY ALA LYS GLN          
SEQRES   2 G  118  ASN THR GLY VAL TRP LEU VAL LYS VAL PRO LYS TYR LEU          
SEQRES   3 G  118  SER GLN GLN TRP ALA LYS ALA SER GLY ARG GLY GLU VAL          
SEQRES   4 G  118  GLY LYS LEU ARG ILE ALA LYS THR GLN GLY ARG THR GLU          
SEQRES   5 G  118  VAL SER PHE THR LEU ASN GLU ASP LEU ALA ASN ILE HIS          
SEQRES   6 G  118  ASP ILE GLY GLY LYS PRO ALA SER VAL SER ALA PRO ARG          
SEQRES   7 G  118  GLU HIS PRO PHE VAL LEU GLN SER VAL GLY GLY GLN THR          
SEQRES   8 G  118  LEU THR VAL PHE THR GLU SER SER SER ASP LYS LEU SER          
SEQRES   9 G  118  LEU GLU GLY ILE VAL VAL GLN ARG ALA GLU CYS ARG PRO          
SEQRES  10 G  118  ALA                                                          
SEQRES   1 H  171  ALA ALA LEU GLY PRO SER SER GLN ASN VAL THR GLU TYR          
SEQRES   2 H  171  VAL VAL ARG VAL PRO LYS ASN THR THR LYS LYS TYR ASN          
SEQRES   3 H  171  ILE MET ALA PHE ASN ALA ALA ASP LYS VAL ASN PHE ALA          
SEQRES   4 H  171  THR TRP ASN GLN ALA ARG LEU GLU ARG ASP LEU SER ASN          
SEQRES   5 H  171  LYS LYS ILE TYR GLN GLU GLU GLU MET PRO GLU SER GLY          
SEQRES   6 H  171  ALA GLY SER GLU PHE ASN ARG LYS LEU ARG GLU GLU ALA          
SEQRES   7 H  171  ARG ARG LYS LYS TYR GLY ILE VAL LEU LYS GLU PHE ARG          
SEQRES   8 H  171  PRO GLU ASP GLN PRO TRP LEU LEU ARG VAL ASN GLY LYS          
SEQRES   9 H  171  SER GLY ARG LYS PHE LYS GLY ILE LYS LYS GLY GLY VAL          
SEQRES  10 H  171  THR GLU ASN THR SER TYR TYR ILE PHE THR GLN CYS PRO          
SEQRES  11 H  171  ASP GLY ALA PHE GLU ALA PHE PRO VAL HIS ASN TRP TYR          
SEQRES  12 H  171  ASN PHE THR PRO LEU ALA ARG HIS ARG THR LEU THR ALA          
SEQRES  13 H  171  GLU GLU ALA GLU GLU GLU TRP GLU ARG ARG ASN LYS VAL          
SEQRES  14 H  171  LEU ASN                                                      
FORMUL   9  HOH   *692(H2 O)                                                    
HELIX    1   1 LEU A    9  GLN A   14  1                                   6    
HELIX    2   2 LYS A   25  ALA A   32  1                                   8    
HELIX    3   3 ASP A   61  ASN A   64  1                                   4    
HELIX    4   1 LEU C    9  GLN C   14  1                                   6    
HELIX    5   2 LYS C   25  ALA C   32  1                                   8    
HELIX    6   3 GLU C   60  ASN C   64  1                                   5    
HELIX    7   4 ALA D  157  ASN D  168  1                                  12    
HELIX    8   1 LEU E    9  GLN E   14  1                                   6    
HELIX    9   2 LYS E   25  ALA E   32  1                                   8    
HELIX   10   3 GLU E   60  ASN E   64  1                                   5    
HELIX   11   4 GLU F  159  ASN F  168  1                                  10    
HELIX   12   1 LEU G    9  GLN G   14  1                                   6    
HELIX   13   2 LYS G   25  ALA G   32  1                                   8    
HELIX   14   3 GLU G   60  ASN G   64  1                                   5    
SHEET    1   A 8 GLU A   6  ASP A   8  0                                        
SHEET    2   A 8 LEU A 104  VAL A 110  1                                        
SHEET    3   A 8 GLN A  91  SER A  99 -1  N  SER A 105   O  THR A  97           
SHEET    4   A 8 LYS B  24  ASN B  32 -1  N  GLU A  98   O  LYS B  25           
SHEET    5   A 8 VAL B 140  PRO B 148  1  N  ILE B  28   O  ASN B 142           
SHEET    6   A 8 LYS B 109  LYS B 114 -1  N  ASN B 145   O  ILE B 113           
SHEET    7   A 8 TRP B  98  VAL B 102 -1  N  GLY B 112   O  TRP B  98           
SHEET    8   A 8 ALA B  45  ARG B  49 -1  N  LEU B  99   O  GLU B  48           
SHEET    1   B 8 GLY A  17  PRO A  24  0                                        
SHEET    2   B 8 THR B 122  GLN B 129 -1  N  VAL A  21   O  TYR B 125           
SHEET    3   B 8 PHE B 135  PRO B 139 -1  N  ILE B 126   O  PHE B 138           
SHEET    4   B 8 ASN B  10  ARG B  17  1  N  ALA B 137   O  ARG B  17           
SHEET    5   B 8 GLU A  39  THR A  48 -1  N  VAL B  16   O  GLY A  41           
SHEET    6   B 8 ARG A  51  LEU A  58 -1  N  LYS A  42   O  THR A  57           
SHEET    7   B 8 GLU A  80  GLN A  86 -1  N  PHE A  56   O  HIS A  81           
SHEET    8   B 8 VAL A 111  CYS A 116 -1  N  VAL A  84   O  GLU A 115           
SHEET    1   C 2 GLN B  58  GLU B  61  0                                        
SHEET    2   C 2 TYR B  84  VAL B  87 -1  N  GLN B  58   O  VAL B  87           
SHEET    1   D 8 GLU C   6  ASP C   8  0                                        
SHEET    2   D 8 LEU C 104  VAL C 110  1                                        
SHEET    3   D 8 GLN C  91  SER C  99 -1  N  SER C 105   O  THR C  97           
SHEET    4   D 8 LYS D  24  ASN D  32 -1  N  GLU C  98   O  LYS D  25           
SHEET    5   D 8 ASN D 142  PRO D 148  1  N  ILE D  28   O  ASN D 142           
SHEET    6   D 8 LYS D 109  LYS D 114 -1  N  ASN D 145   O  ILE D 113           
SHEET    7   D 8 TRP D  98  VAL D 102 -1  N  GLY D 112   O  TRP D  98           
SHEET    8   D 8 ALA D  45  ARG D  49 -1  N  LEU D  99   O  GLU D  48           
SHEET    1   E 8 GLY C  17  PRO C  24  0                                        
SHEET    2   E 8 THR D 122  GLN D 129 -1  N  VAL C  21   O  TYR D 125           
SHEET    3   E 8 PHE D 135  PRO D 139 -1  N  ILE D 126   O  PHE D 138           
SHEET    4   E 8 ASN D  10  ARG D  17  1  N  ALA D 137   O  ARG D  17           
SHEET    5   E 8 GLU C  39  THR C  48 -1  N  VAL D  16   O  GLY C  41           
SHEET    6   E 8 ARG C  51  LEU C  58 -1  N  LYS C  42   O  THR C  57           
SHEET    7   E 8 GLU C  80  GLN C  86 -1  N  PHE C  56   O  HIS C  81           
SHEET    8   E 8 VAL C 111  CYS C 116 -1  N  VAL C  84   O  GLU C 115           
SHEET    1   F 2 LYS D  55  GLU D  61  0                                        
SHEET    2   F 2 TYR D  84  GLU D  90 -1  N  GLN D  58   O  VAL D  87           
SHEET    1   G 8 GLU E   6  ASP E   8  0                                        
SHEET    2   G 8 LEU E 104  VAL E 110  1                                        
SHEET    3   G 8 GLN E  91  SER E  99 -1  N  SER E 105   O  THR E  97           
SHEET    4   G 8 LYS F  24  ASN F  32 -1  N  GLU E  98   O  LYS F  25           
SHEET    5   G 8 VAL F 140  PRO F 148  1  N  ILE F  28   O  ASN F 142           
SHEET    6   G 8 LYS F 109  LYS F 114 -1  N  ASN F 145   O  ILE F 113           
SHEET    7   G 8 TRP F  98  VAL F 102 -1  N  GLY F 112   O  TRP F  98           
SHEET    8   G 8 ALA F  45  ARG F  49 -1  N  LEU F  99   O  GLU F  48           
SHEET    1   H 8 GLY E  17  PRO E  24  0                                        
SHEET    2   H 8 THR F 122  GLN F 129 -1  N  VAL E  21   O  TYR F 125           
SHEET    3   H 8 PHE F 135  PRO F 139 -1  N  ILE F 126   O  PHE F 138           
SHEET    4   H 8 THR F  12  ARG F  17  1  N  ALA F 137   O  ARG F  17           
SHEET    5   H 8 GLU E  39  THR E  48 -1  N  VAL F  16   O  GLY E  41           
SHEET    6   H 8 ARG E  51  LEU E  58 -1  N  LYS E  42   O  THR E  57           
SHEET    7   H 8 GLU E  80  GLN E  86 -1  N  PHE E  56   O  HIS E  81           
SHEET    8   H 8 VAL E 111  CYS E 116 -1  N  VAL E  84   O  GLU E 115           
SHEET    1   I 2 LYS F  55  GLU F  61  0                                        
SHEET    2   I 2 TYR F  84  GLU F  90 -1  N  GLN F  58   O  VAL F  87           
SHEET    1   J 8 GLU G   6  ASP G   8  0                                        
SHEET    2   J 8 LEU G 104  VAL G 110  1                                        
SHEET    3   J 8 GLN G  91  SER G  99 -1  N  SER G 105   O  THR G  97           
SHEET    4   J 8 LYS H  25  ASN H  32 -1  N  GLU G  98   O  LYS H  25           
SHEET    5   J 8 VAL H 140  PRO H 148  1  N  ILE H  28   O  ASN H 142           
SHEET    6   J 8 LYS H 109  LYS H 114 -1  N  ASN H 145   O  ILE H 113           
SHEET    7   J 8 TRP H  98  VAL H 102 -1  N  GLY H 112   O  TRP H  98           
SHEET    8   J 8 ALA H  45  ARG H  49 -1  N  LEU H  99   O  GLU H  48           
SHEET    1   K 8 GLY G  17  PRO G  24  0                                        
SHEET    2   K 8 THR H 122  GLN H 129 -1  N  VAL G  21   O  TYR H 125           
SHEET    3   K 8 PHE H 135  PRO H 139 -1  N  ILE H 126   O  PHE H 138           
SHEET    4   K 8 THR H  12  ARG H  17  1  N  ALA H 137   O  ARG H  17           
SHEET    5   K 8 GLU G  39  THR G  48 -1  N  VAL H  16   O  GLY G  41           
SHEET    6   K 8 ARG G  51  LEU G  58 -1  N  LYS G  42   O  THR G  57           
SHEET    7   K 8 GLU G  80  GLN G  86 -1  N  PHE G  56   O  HIS G  81           
SHEET    8   K 8 VAL G 111  CYS G 116 -1  N  VAL G  84   O  GLU G 115           
SHEET    1   L 2 GLN H  58  GLU H  61  0                                        
SHEET    2   L 2 TYR H  84  VAL H  87 -1  N  GLN H  58   O  VAL H  87           
CRYST1   48.015   72.290   82.266 104.51  93.32 104.32 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020830  0.005320  0.002770        0.00000                         
SCALE2      0.000000  0.014280  0.004060        0.00000                         
SCALE3      0.000000  0.000000  0.012660        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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