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Database: PDB
Entry: 5DFW
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Original site: 5DFW 
HEADER    CELL ADHESION                           27-AUG-15   5DFW              
TITLE     CRYSTAL STRUCTURE OF HUMAN CD81 LARGE EXTRACELLULAR LOOP IN COMPLEX   
TITLE    2 WITH SINGLE CHAIN FV FRAGMENT K13                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD81 ANTIGEN;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 112-201;                                      
COMPND   5 SYNONYM: 26 KDA CELL SURFACE PROTEIN TAPA-1,TARGET OF THE            
COMPND   6 ANTIPROLIFERATIVE ANTIBODY 1,TETRASPANIN-28,TSPAN-28;                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SINGLE CHAIN FV FRAGMENT;                                  
COMPND  10 CHAIN: H;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 101-810;                                      
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD81, TAPA1, TSPAN28;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  11 ORGANISM_TAXID: 10090;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HELICAL BUNDLE, ANTIBODY-ANTIGEN COMPLEX, CELL ADHESION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.F.HARRIS,A.VILLASENOR,A.KUGLSTATTER                                 
REVDAT   2   02-MAR-16 5DFW    1       JRNL                                     
REVDAT   1   16-DEC-15 5DFW    0                                                
JRNL        AUTH   A.BUJOTZEK,F.LIPSMEIER,S.F.HARRIS,J.BENZ,A.KUGLSTATTER,      
JRNL        AUTH 2 G.GEORGES                                                    
JRNL        TITL   VH-VL ORIENTATION PREDICTION FOR ANTIBODY HUMANIZATION       
JRNL        TITL 2 CANDIDATE SELECTION: A CASE STUDY.                           
JRNL        REF    MABS                          V.   8   288 2016              
JRNL        REFN                   ESSN 1942-0870                               
JRNL        PMID   26637054                                                     
JRNL        DOI    10.1080/19420862.2015.1117720                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 68.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 11218                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.194                          
REMARK   3   R VALUE            (WORKING SET)  : 0.190                          
REMARK   3   FREE R VALUE                      : 0.264                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.140                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 577                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.33                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.55                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 923                      
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2458                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 875                      
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2423                   
REMARK   3   BIN FREE R VALUE                        : 0.3100                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.20                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 48                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2418                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 83                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.48680                                              
REMARK   3    B22 (A**2) : -9.47720                                             
REMARK   3    B33 (A**2) : 2.99040                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 11.61740                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.312               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.912                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.864                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2477   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3366   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 825    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 61     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 358    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2477   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 330    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2865   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.22                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.07                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 23.94                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213157.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11229                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 68.2                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 17.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M SODIUM FORMATE,      
REMARK 280  0.1 M SODIUM CITRATE, PH 5.9, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4440 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       28.42289            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       77.60057            
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     GLY A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     HIS A   203                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     GLU H   101                                                      
REMARK 465     GLY H   481                                                      
REMARK 465     GLY H   482                                                      
REMARK 465     GLY H   483                                                      
REMARK 465     GLY H   484                                                      
REMARK 465     SER H   485                                                      
REMARK 465     GLY H   486                                                      
REMARK 465     GLY H   487                                                      
REMARK 465     GLY H   488                                                      
REMARK 465     GLY H   489                                                      
REMARK 465     SER H   490                                                      
REMARK 465     GLY H   491                                                      
REMARK 465     GLY H   492                                                      
REMARK 465     GLY H   493                                                      
REMARK 465     GLY H   494                                                      
REMARK 465     SER H   495                                                      
REMARK 465     GLY H   496                                                      
REMARK 465     GLY H   497                                                      
REMARK 465     GLY H   498                                                      
REMARK 465     GLY H   499                                                      
REMARK 465     SER H   500                                                      
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    CYS A 157      118.07   -162.43                                   
REMARK 500    ARG H 103     -115.48    -91.40                                   
REMARK 500    THR H 124      -85.74    -80.59                                   
REMARK 500    SER H 125      122.99     67.35                                   
REMARK 500    PRO H 295      -37.88    -39.05                                   
REMARK 500    TYR H 353       60.07   -106.52                                   
REMARK 500    GLN H 606      125.33    -32.01                                   
REMARK 500    GLU H 727        6.17    -68.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H 953        DISTANCE =  7.70 ANGSTROMS                       
REMARK 525    HOH H 954        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH H 955        DISTANCE =  8.04 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DFV   RELATED DB: PDB                                   
DBREF  5DFW A  112   201  UNP    P60033   CD81_HUMAN     112    201             
DBREF  5DFW H  101   810  PDB    5DFW     5DFW           101    810             
SEQADV 5DFW GLY A  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFW SER A  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFW HIS A  202  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFW HIS A  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFW HIS A  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFW HIS A  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFW HIS A  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFW HIS A  207  UNP  P60033              EXPRESSION TAG                 
SEQRES   1 A   98  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 A   98  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 A   98  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 A   98  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 A   98  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 A   98  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 A   98  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 A   98  LYS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 H  243  GLU VAL ARG LEU HIS GLN SER ALA ALA GLN LEU VAL GLN          
SEQRES   2 H  243  PRO GLY ALA SER VAL ARG LEU SER CYS THR THR SER GLY          
SEQRES   3 H  243  PHE ASN PHE LYS ASP SER TYR LEU HIS TRP VAL LYS GLN          
SEQRES   4 H  243  ARG PRO ALA GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  243  THR GLY ASN GLY ASN VAL LYS PHE ASP PRO LYS PHE GLN          
SEQRES   6 H  243  ASP LYS ALA THR ILE THR THR ASP ILE PRO SER MET THR          
SEQRES   7 H  243  ALA TYR LEU HIS LEU SER ASN LEU THR SER GLU ASP THR          
SEQRES   8 H  243  ALA VAL TYR TYR CYS VAL PRO TYR GLY TYR GLY PHE HIS          
SEQRES   9 H  243  SER TRP GLY ASP GLY THR THR LEU THR VAL SER SER GLY          
SEQRES  10 H  243  GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  11 H  243  SER GLY GLY GLY GLY SER ASP ILE GLN MET THR GLN SER          
SEQRES  12 H  243  PRO ALA SER LEU SER VAL SER VAL GLY GLU THR VAL THR          
SEQRES  13 H  243  ILE THR CYS ARG ALA SER GLU ASN ILE TYR ARG THR LEU          
SEQRES  14 H  243  ALA TRP TYR LEU GLN LYS GLN GLY LYS SER PRO GLN LEU          
SEQRES  15 H  243  LEU VAL TYR GLY ALA THR THR LEU ALA ASP GLY VAL PRO          
SEQRES  16 H  243  SER ARG PHE SER GLY SER GLY SER GLY THR GLN TYR TYR          
SEQRES  17 H  243  LEU LYS ILE ASN SER LEU GLN SER GLU ASP PHE GLY THR          
SEQRES  18 H  243  TYR HIS CYS GLN HIS PHE TRP GLY THR PRO TRP THR PHE          
SEQRES  19 H  243  GLY GLY GLY THR LYS VAL GLU ILE LYS                          
FORMUL   3  HOH   *83(H2 O)                                                     
HELIX    1 AA1 ASN A  115  VAL A  135  1                                  21    
HELIX    2 AA2 ASN A  141  ASP A  155  1                                  15    
HELIX    3 AA3 SER A  159  ALA A  164  5                                   6    
HELIX    4 AA4 LEU A  165  ASN A  172  1                                   8    
HELIX    5 AA5 ASN A  180  PHE A  186  1                                   7    
HELIX    6 AA6 ASP A  189  GLY A  200  1                                  12    
HELIX    7 AA7 ASN H  153  ASP H  156  5                                   4    
HELIX    8 AA8 PRO H  295  GLN H  298  5                                   4    
HELIX    9 AA9 THR H  321  THR H  325  5                                   5    
HELIX   10 AB1 GLN H  725  PHE H  729  5                                   5    
SHEET    1 AA1 4 HIS H 105  GLN H 106  0                                        
SHEET    2 AA1 4 VAL H 118  THR H 123 -1  O  THR H 123   N  HIS H 105           
SHEET    3 AA1 4 THR H 312  LEU H 317 -1  O  ALA H 313   N  CYS H 122           
SHEET    4 AA1 4 THR H 303  ASP H 307 -1  N  ASP H 307   O  THR H 312           
SHEET    1 AA2 6 GLN H 110  VAL H 112  0                                        
SHEET    2 AA2 6 THR H 405  VAL H 409  1  O  THR H 408   N  VAL H 112           
SHEET    3 AA2 6 ALA H 326  TYR H 351 -1  N  ALA H 326   O  LEU H 407           
SHEET    4 AA2 6 TYR H 197  GLN H 204 -1  N  HIS H 199   O  VAL H 331           
SHEET    5 AA2 6 LEU H 210  ASP H 253 -1  O  GLU H 211   N  LYS H 203           
SHEET    6 AA2 6 VAL H 291  PHE H 293 -1  O  LYS H 292   N  ARG H 251           
SHEET    1 AA3 4 MET H 504  SER H 507  0                                        
SHEET    2 AA3 4 VAL H 519  ALA H 552 -1  O  THR H 522   N  SER H 507           
SHEET    3 AA3 4 GLN H 716  ILE H 721 -1  O  LEU H 719   N  ILE H 521           
SHEET    4 AA3 4 PHE H 706  SER H 711 -1  N  SER H 709   O  TYR H 718           
SHEET    1 AA4 6 SER H 510  SER H 512  0                                        
SHEET    2 AA4 6 THR H 805  GLU H 808  1  O  LYS H 806   N  LEU H 511           
SHEET    3 AA4 6 GLY H 730  HIS H 752 -1  N  GLY H 730   O  VAL H 807           
SHEET    4 AA4 6 LEU H 598  GLN H 604 -1  N  GLN H 604   O  THR H 731           
SHEET    5 AA4 6 GLN H 611  TYR H 615 -1  O  LEU H 613   N  TRP H 601           
SHEET    6 AA4 6 THR H 696  LEU H 697 -1  O  THR H 696   N  TYR H 615           
SSBOND   1 CYS A  156    CYS A  190                          1555   1555  2.03  
SSBOND   2 CYS A  157    CYS A  175                          1555   1555  2.03  
SSBOND   3 CYS H  122    CYS H  330                          1555   1555  2.03  
SSBOND   4 CYS H  523    CYS H  734                          1555   1555  2.04  
CISPEP   1 SER H  507    PRO H  508          0        -1.77                     
CISPEP   2 THR H  796    PRO H  797          0         2.58                     
CRYST1   49.652   49.671   80.452  90.00 105.30  90.00 P 1 2 1       2          
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      0.020140  0.000000  0.005510        0.00000                         
SCALE2      0.000000  0.020132  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012887        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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