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Database: PDB
Entry: 5DFV
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HEADER    IMMUNE SYSTEM                           27-AUG-15   5DFV              
TITLE     CRYSTAL STRUCTURE OF HUMAN CD81 LARGE EXTRACELLULAR LOOP IN COMPLEX   
TITLE    2 WITH MURINE FAB FRAGMENT K04                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CD81 ANTIGEN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 26 KDA CELL SURFACE PROTEIN TAPA-1,TARGET OF THE            
COMPND   5 ANTIPROLIFERATIVE ANTIBODY 1,TETRASPANIN-28,TSPAN-28;                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: FAB HEAVY CHAIN;                                           
COMPND   9 CHAIN: C, E;                                                         
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: FAB LIGHT CHAIN;                                           
COMPND  12 CHAIN: D, F                                                          
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 CELL_LINE: MURINE HYBRIDOMA;                                         
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  15 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  16 ORGANISM_TAXID: 10090;                                               
SOURCE  17 CELL_LINE: MURINE HYBRIDOMA                                          
KEYWDS    HELICAL BUNDLE, CELL ADHESION, ANTIBODY-ANTIGEN COMPLEX, IMMUNE       
KEYWDS   2 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.F.HARRIS,A.WONG,A.KUGLSTATTER                                       
REVDAT   2   02-MAR-16 5DFV    1       JRNL                                     
REVDAT   1   16-DEC-15 5DFV    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.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 29086                          
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) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1583                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1250                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.3860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7926                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 4                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11000                                              
REMARK   3    B22 (A**2) : -0.07000                                             
REMARK   3    B33 (A**2) : -0.35000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.64000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.442         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.332         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.241        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.889                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.830                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8109 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5428 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11014 ; 1.052 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13300 ; 0.785 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1026 ; 6.084 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   321 ;35.818 ;24.798       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1347 ;17.532 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;19.023 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1248 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8961 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1555 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1747 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5512 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3865 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4509 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   178 ; 0.127 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    13 ; 0.247 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    18 ; 0.192 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.090 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6596 ; 0.365 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2084 ; 0.030 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8336 ; 0.404 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3530 ; 0.413 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2678 ; 0.677 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5DFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213158.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
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   : 30682                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
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     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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   (%): 56.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAOAC, 20% PEG 10000, PH 4.0,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.24150            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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     GLY A   178                                                      
REMARK 465     SER A   179                                                      
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     HIS A   208                                                      
REMARK 465     GLY B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     GLY B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     ASN B   180                                                      
REMARK 465     ILE B   181                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     CYS C  1014                                                      
REMARK 465     GLY C  1015                                                      
REMARK 465     GLY C  1016                                                      
REMARK 465     THR C  1017                                                      
REMARK 465     THR C  1018                                                      
REMARK 465     GLY C  1019                                                      
REMARK 465     VAL C  1100                                                      
REMARK 465     PRO C  1101                                                      
REMARK 465     CYS D  2106                                                      
REMARK 465     CYS E  1014                                                      
REMARK 465     GLY E  1015                                                      
REMARK 465     GLY E  1016                                                      
REMARK 465     THR E  1017                                                      
REMARK 465     THR E  1018                                                      
REMARK 465     GLY E  1019                                                      
REMARK 465     VAL E  1100                                                      
REMARK 465     PRO E  1101                                                      
REMARK 465     CYS F  2106                                                      
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     PHE B 113    N    CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ASP B 138    CG   OD1  OD2                                       
REMARK 470     VAL C1011    CG1  CG2                                            
REMARK 470     VAL E1011    CG1  CG2                                            
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     PHE B  113   CB                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE B 113   CA    PHE B 113   CB     -0.154                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP A 138       82.25    -64.22                                   
REMARK 500    ASP A 139       80.73     28.79                                   
REMARK 500    ASP A 155       85.75     49.71                                   
REMARK 500    ASN A 173       62.00     62.63                                   
REMARK 500    PRO A 176       98.79    -68.35                                   
REMARK 500    ILE A 182     -114.84     18.25                                   
REMARK 500    ASN A 184     -104.62     55.31                                   
REMARK 500    LEU A 185      -54.57     -4.03                                   
REMARK 500    LYS A 201     -128.33   -112.21                                   
REMARK 500    ALA B 140       80.68    -45.85                                   
REMARK 500    ASP B 155       77.06     62.71                                   
REMARK 500    LEU B 162       56.80   -146.91                                   
REMARK 500    LEU C 395       61.76    -69.53                                   
REMARK 500    PRO C1012     -170.11    -69.89                                   
REMARK 500    PRO C1033     -154.48    -85.18                                   
REMARK 500    SER C1058       72.39     56.19                                   
REMARK 500    VAL C1069      -83.10   -101.54                                   
REMARK 500    THR C1070      -33.57   -169.07                                   
REMARK 500    SER C1071      -46.29     96.83                                   
REMARK 500    GLU C1097      149.17   -174.00                                   
REMARK 500    LEU D 515       96.01    -65.15                                   
REMARK 500    GLN D 517      134.49    160.79                                   
REMARK 500    VAL D 562       31.89    -90.86                                   
REMARK 500    THR D 581     -167.76   -102.94                                   
REMARK 500    SER D 596      112.57   -174.51                                   
REMARK 500    TYR D 597      -11.87     88.72                                   
REMARK 500    ALA D 694      -55.69     83.06                                   
REMARK 500    HIS D 722      119.22   -164.30                                   
REMARK 500    GLU D 726      -63.64    -24.88                                   
REMARK 500    ALA D2001     -132.64    -65.38                                   
REMARK 500    SER D2019       58.06    -90.23                                   
REMARK 500    GLN D2048       62.10   -107.96                                   
REMARK 500    GLU D2079       34.09    -82.24                                   
REMARK 500    ASN D2082       49.11    -99.83                                   
REMARK 500    SER D2083      116.10   -175.34                                   
REMARK 500    ASN D2104       68.79   -169.42                                   
REMARK 500    ASP E 288       17.06   -149.81                                   
REMARK 500    ALA E 326      162.67    169.42                                   
REMARK 500    THR E 354     -161.57    -71.10                                   
REMARK 500    ASP E 394      -33.09    -36.86                                   
REMARK 500    SER E1042       69.56     33.04                                   
REMARK 500    SER E1046      -38.80   -137.24                                   
REMARK 500    VAL E1069     -167.66   -111.76                                   
REMARK 500    THR E1070      123.97   -170.23                                   
REMARK 500    SER E1071       -7.02   -171.84                                   
REMARK 500    ASN E1072      -36.21     64.81                                   
REMARK 500    ALA F 694      -52.84     80.69                                   
REMARK 500    ASN F2049       61.75    -68.02                                   
REMARK 500    ASN F2104       53.45     77.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER D  596     TYR D  597                   33.00                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5DFV A  112   202  UNP    P60033   CD81_HUMAN     112    202             
DBREF  5DFV B  112   202  UNP    P60033   CD81_HUMAN     112    202             
DBREF  5DFV C  101  1101  PDB    5DFV     5DFV           101   1101             
DBREF  5DFV D  501  2106  PDB    5DFV     5DFV           501   2106             
DBREF  5DFV E  101  1101  PDB    5DFV     5DFV           101   1101             
DBREF  5DFV F  501  2106  PDB    5DFV     5DFV           501   2106             
SEQADV 5DFV GLY A  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV SER A  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS A  202  UNP  P60033    LEU   202 CONFLICT                       
SEQADV 5DFV HIS A  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS A  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS A  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS A  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS A  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS A  208  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV GLY B  110  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV SER B  111  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS B  202  UNP  P60033    LEU   202 CONFLICT                       
SEQADV 5DFV HIS B  203  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS B  204  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS B  205  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS B  206  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS B  207  UNP  P60033              EXPRESSION TAG                 
SEQADV 5DFV HIS B  208  UNP  P60033              EXPRESSION TAG                 
SEQRES   1 A   99  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 A   99  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 A   99  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 A   99  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 A   99  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 A   99  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 A   99  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 A   99  LYS HIS HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B   99  GLY SER GLY PHE VAL ASN LYS ASP GLN ILE ALA LYS ASP          
SEQRES   2 B   99  VAL LYS GLN PHE TYR ASP GLN ALA LEU GLN GLN ALA VAL          
SEQRES   3 B   99  VAL ASP ASP ASP ALA ASN ASN ALA LYS ALA VAL VAL LYS          
SEQRES   4 B   99  THR PHE HIS GLU THR LEU ASP CYS CYS GLY SER SER THR          
SEQRES   5 B   99  LEU THR ALA LEU THR THR SER VAL LEU LYS ASN ASN LEU          
SEQRES   6 B   99  CYS PRO SER GLY SER ASN ILE ILE SER ASN LEU PHE LYS          
SEQRES   7 B   99  GLU ASP CYS HIS GLN LYS ILE ASP ASP LEU PHE SER GLY          
SEQRES   8 B   99  LYS HIS HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  222  GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS          
SEQRES   2 C  222  PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY          
SEQRES   3 C  222  TYR THR PHE SER SER SER TRP MET ASN TRP VAL LYS GLN          
SEQRES   4 C  222  ARG PRO GLY LYS GLY LEU GLU TRP ILE GLY ARG ILE TYR          
SEQRES   5 C  222  SER GLY ASP GLY ASP ALA ILE TYR ASN GLY LYS PHE LYS          
SEQRES   6 C  222  GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR          
SEQRES   7 C  222  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 C  222  ALA VAL TYR PHE CYS ALA ARG GLU GLY LYS THR GLY ASP          
SEQRES   9 C  222  LEU LEU LEU ARG SER TRP GLY GLN GLY SER ALA LEU THR          
SEQRES  10 C  222  VAL SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO          
SEQRES  11 C  222  LEU VAL PRO VAL CYS GLY GLY THR THR GLY SER SER VAL          
SEQRES  12 C  222  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO          
SEQRES  13 C  222  VAL THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY          
SEQRES  14 C  222  VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR          
SEQRES  15 C  222  THR LEU SER SER SER VAL THR VAL THR SER ASN THR TRP          
SEQRES  16 C  222  PRO SER GLN THR ILE THR CYS ASN VAL ALA HIS PRO ALA          
SEQRES  17 C  222  SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG VAL          
SEQRES  18 C  222  PRO                                                          
SEQRES   1 D  218  ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SER VAL          
SEQRES   2 D  218  SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER          
SEQRES   3 D  218  LYS SER VAL SER THR SER ILE TYR SER TYR MET HIS TRP          
SEQRES   4 D  218  TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE          
SEQRES   5 D  218  LYS TYR ALA SER TYR LEU GLU SER GLY VAL PRO ALA ARG          
SEQRES   6 D  218  PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN          
SEQRES   7 D  218  ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR          
SEQRES   8 D  218  CYS GLU HIS SER ARG GLU PHE PRO PHE THR PHE GLY THR          
SEQRES   9 D  218  GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO          
SEQRES  10 D  218  THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR          
SEQRES  11 D  218  SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE          
SEQRES  12 D  218  TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY          
SEQRES  13 D  218  SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP          
SEQRES  14 D  218  GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR          
SEQRES  15 D  218  LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER          
SEQRES  16 D  218  TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO          
SEQRES  17 D  218  ILE VAL LYS SER PHE ASN ARG ASN GLU CYS                      
SEQRES   1 E  222  GLN VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS          
SEQRES   2 E  222  PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY          
SEQRES   3 E  222  TYR THR PHE SER SER SER TRP MET ASN TRP VAL LYS GLN          
SEQRES   4 E  222  ARG PRO GLY LYS GLY LEU GLU TRP ILE GLY ARG ILE TYR          
SEQRES   5 E  222  SER GLY ASP GLY ASP ALA ILE TYR ASN GLY LYS PHE LYS          
SEQRES   6 E  222  GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR          
SEQRES   7 E  222  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 E  222  ALA VAL TYR PHE CYS ALA ARG GLU GLY LYS THR GLY ASP          
SEQRES   9 E  222  LEU LEU LEU ARG SER TRP GLY GLN GLY SER ALA LEU THR          
SEQRES  10 E  222  VAL SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO          
SEQRES  11 E  222  LEU VAL PRO VAL CYS GLY GLY THR THR GLY SER SER VAL          
SEQRES  12 E  222  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO          
SEQRES  13 E  222  VAL THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY          
SEQRES  14 E  222  VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR          
SEQRES  15 E  222  THR LEU SER SER SER VAL THR VAL THR SER ASN THR TRP          
SEQRES  16 E  222  PRO SER GLN THR ILE THR CYS ASN VAL ALA HIS PRO ALA          
SEQRES  17 E  222  SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG VAL          
SEQRES  18 E  222  PRO                                                          
SEQRES   1 F  218  ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU SER VAL          
SEQRES   2 F  218  SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER          
SEQRES   3 F  218  LYS SER VAL SER THR SER ILE TYR SER TYR MET HIS TRP          
SEQRES   4 F  218  TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE          
SEQRES   5 F  218  LYS TYR ALA SER TYR LEU GLU SER GLY VAL PRO ALA ARG          
SEQRES   6 F  218  PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN          
SEQRES   7 F  218  ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR          
SEQRES   8 F  218  CYS GLU HIS SER ARG GLU PHE PRO PHE THR PHE GLY THR          
SEQRES   9 F  218  GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO          
SEQRES  10 F  218  THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR          
SEQRES  11 F  218  SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE          
SEQRES  12 F  218  TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY          
SEQRES  13 F  218  SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP          
SEQRES  14 F  218  GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR          
SEQRES  15 F  218  LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER          
SEQRES  16 F  218  TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO          
SEQRES  17 F  218  ILE VAL LYS SER PHE ASN ARG ASN GLU CYS                      
FORMUL   7  HOH   *4(H2 O)                                                      
HELIX    1 AA1 ASN A  115  ASP A  137  1                                  23    
HELIX    2 AA2 ALA A  140  ASP A  155  1                                  16    
HELIX    3 AA3 LEU A  162  ASN A  172  1                                  11    
HELIX    4 AA4 ASN A  184  GLU A  188  5                                   5    
HELIX    5 AA5 ASP A  189  SER A  199  1                                  11    
HELIX    6 AA6 ASN B  115  ASP B  137  1                                  23    
HELIX    7 AA7 ALA B  140  ASP B  155  1                                  16    
HELIX    8 AA8 SER B  159  THR B  161  5                                   3    
HELIX    9 AA9 LEU B  162  ASN B  172  1                                  11    
HELIX   10 AB1 ILE B  182  GLU B  188  5                                   7    
HELIX   11 AB2 ASP B  189  GLY B  200  1                                  12    
HELIX   12 AB3 THR C  153  SER C  156  5                                   4    
HELIX   13 AB4 THR C  321  SER C  325  5                                   5    
HELIX   14 AB5 SER C 1042  SER C 1044  5                                   3    
HELIX   15 AB6 PRO C 1086  SER C 1089  5                                   4    
HELIX   16 AB7 GLU D  725  ALA D  729  5                                   5    
HELIX   17 AB8 SER D 2013  SER D 2019  1                                   7    
HELIX   18 AB9 THR D 2074  GLU D 2079  1                                   6    
HELIX   19 AC1 THR E  153  SER E  156  5                                   4    
HELIX   20 AC2 GLY E  295  LYS E  298  5                                   4    
HELIX   21 AC3 THR E  321  SER E  325  5                                   5    
HELIX   22 AC4 PRO E 1086  SER E 1089  5                                   4    
HELIX   23 AC5 GLU F  725  ALA F  729  5                                   5    
HELIX   24 AC6 SER F 2013  SER F 2019  1                                   7    
HELIX   25 AC7 LYS F 2075  HIS F 2081  1                                   7    
SHEET    1 AA1 4 GLN C 103  GLN C 106  0                                        
SHEET    2 AA1 4 VAL C 118  SER C 125 -1  O  LYS C 123   N  GLN C 105           
SHEET    3 AA1 4 THR C 312  LEU C 317 -1  O  MET C 315   N  ILE C 120           
SHEET    4 AA1 4 ALA C 302  ASP C 307 -1  N  ASP C 307   O  THR C 312           
SHEET    1 AA2 6 GLU C 110  VAL C 112  0                                        
SHEET    2 AA2 6 SER C 405  VAL C 409  1  O  ALA C 406   N  GLU C 110           
SHEET    3 AA2 6 ALA C 326  ARG C 332 -1  N  TYR C 328   O  SER C 405           
SHEET    4 AA2 6 TRP C 197  GLN C 204 -1  N  ASN C 199   O  ALA C 331           
SHEET    5 AA2 6 GLU C 211  TYR C 253 -1  O  ILE C 213   N  TRP C 201           
SHEET    6 AA2 6 ALA C 291  TYR C 293 -1  O  ILE C 292   N  ARG C 251           
SHEET    1 AA3 4 GLU C 110  VAL C 112  0                                        
SHEET    2 AA3 4 SER C 405  VAL C 409  1  O  ALA C 406   N  GLU C 110           
SHEET    3 AA3 4 ALA C 326  ARG C 332 -1  N  TYR C 328   O  SER C 405           
SHEET    4 AA3 4 SER C 399  TRP C 401 -1  O  SER C 399   N  ARG C 332           
SHEET    1 AA4 4 SER C1006  LEU C1010  0                                        
SHEET    2 AA4 4 THR C1023  TYR C1031 -1  O  GLY C1025   N  LEU C1010           
SHEET    3 AA4 4 TYR C1061  THR C1068 -1  O  TYR C1061   N  TYR C1031           
SHEET    4 AA4 4 VAL C1049  THR C1051 -1  N  HIS C1050   O  SER C1066           
SHEET    1 AA5 4 SER C1006  LEU C1010  0                                        
SHEET    2 AA5 4 THR C1023  TYR C1031 -1  O  GLY C1025   N  LEU C1010           
SHEET    3 AA5 4 TYR C1061  THR C1068 -1  O  TYR C1061   N  TYR C1031           
SHEET    4 AA5 4 LEU C1055  LEU C1056 -1  N  LEU C1055   O  THR C1062           
SHEET    1 AA6 3 THR C1037  TRP C1040  0                                        
SHEET    2 AA6 3 THR C1080  HIS C1085 -1  O  ASN C1082   N  THR C1039           
SHEET    3 AA6 3 THR C1090  LYS C1095 -1  O  THR C1090   N  HIS C1085           
SHEET    1 AA7 4 LEU D 504  SER D 507  0                                        
SHEET    2 AA7 4 ALA D 519  ALA D 552 -1  O  SER D 522   N  SER D 507           
SHEET    3 AA7 4 ASP D 716  ILE D 721 -1  O  ILE D 721   N  ALA D 519           
SHEET    4 AA7 4 PHE D 706  SER D 711 -1  N  SER D 709   O  THR D 718           
SHEET    1 AA8 6 SER D 510  VAL D 513  0                                        
SHEET    2 AA8 6 THR D 805  ILE D 809  1  O  GLU D 808   N  LEU D 511           
SHEET    3 AA8 6 THR D 731  HIS D 752 -1  N  TYR D 732   O  THR D 805           
SHEET    4 AA8 6 MET D 598  GLN D 604 -1  N  TYR D 602   O  TYR D 733           
SHEET    5 AA8 6 LYS D 611  LYS D 615 -1  O  LYS D 611   N  GLN D 603           
SHEET    6 AA8 6 TYR D 696  LEU D 697 -1  O  TYR D 696   N  LYS D 615           
SHEET    1 AA9 4 THR D2006  PHE D2010  0                                        
SHEET    2 AA9 4 ALA D2022  PHE D2031 -1  O  VAL D2025   N  PHE D2010           
SHEET    3 AA9 4 TYR D2065  LEU D2073 -1  O  MET D2067   N  LEU D2028           
SHEET    4 AA9 4 VAL D2051  ASN D2053 -1  N  LEU D2052   O  THR D2070           
SHEET    1 AB1 3 ASN D2037  ILE D2042  0                                        
SHEET    2 AB1 3 TYR D2084  THR D2089 -1  O  GLU D2087   N  LYS D2039           
SHEET    3 AB1 3 SER D2100  PHE D2101 -1  O  PHE D2101   N  TYR D2084           
SHEET    1 AB2 4 GLN E 103  GLN E 106  0                                        
SHEET    2 AB2 4 VAL E 118  SER E 125 -1  O  LYS E 123   N  GLN E 105           
SHEET    3 AB2 4 THR E 312  LEU E 317 -1  O  ALA E 313   N  CYS E 122           
SHEET    4 AB2 4 ALA E 302  ASP E 307 -1  N  THR E 305   O  TYR E 314           
SHEET    1 AB3 6 GLU E 110  VAL E 112  0                                        
SHEET    2 AB3 6 SER E 405  VAL E 409  1  O  ALA E 406   N  GLU E 110           
SHEET    3 AB3 6 ALA E 326  ARG E 332 -1  N  ALA E 326   O  LEU E 407           
SHEET    4 AB3 6 TRP E 197  GLN E 204 -1  N  ASN E 199   O  ALA E 331           
SHEET    5 AB3 6 GLU E 211  TYR E 253 -1  O  GLU E 211   N  LYS E 203           
SHEET    6 AB3 6 ALA E 291  TYR E 293 -1  O  ILE E 292   N  ARG E 251           
SHEET    1 AB4 4 GLU E 110  VAL E 112  0                                        
SHEET    2 AB4 4 SER E 405  VAL E 409  1  O  ALA E 406   N  GLU E 110           
SHEET    3 AB4 4 ALA E 326  ARG E 332 -1  N  ALA E 326   O  LEU E 407           
SHEET    4 AB4 4 SER E 399  TRP E 401 -1  O  SER E 399   N  ARG E 332           
SHEET    1 AB5 4 SER E1006  LEU E1010  0                                        
SHEET    2 AB5 4 VAL E1022  TYR E1031 -1  O  LEU E1027   N  TYR E1008           
SHEET    3 AB5 4 LEU E1060  VAL E1069 -1  O  TYR E1061   N  TYR E1031           
SHEET    4 AB5 4 VAL E1049  THR E1051 -1  N  HIS E1050   O  SER E1066           
SHEET    1 AB6 4 SER E1006  LEU E1010  0                                        
SHEET    2 AB6 4 VAL E1022  TYR E1031 -1  O  LEU E1027   N  TYR E1008           
SHEET    3 AB6 4 LEU E1060  VAL E1069 -1  O  TYR E1061   N  TYR E1031           
SHEET    4 AB6 4 LEU E1055  GLN E1057 -1  N  LEU E1055   O  THR E1062           
SHEET    1 AB7 3 THR E1037  TRP E1040  0                                        
SHEET    2 AB7 3 THR E1080  HIS E1085 -1  O  ASN E1082   N  THR E1039           
SHEET    3 AB7 3 THR E1090  LYS E1095 -1  O  LYS E1094   N  CYS E1081           
SHEET    1 AB8 4 LEU F 504  SER F 507  0                                        
SHEET    2 AB8 4 ALA F 519  ALA F 552 -1  O  ARG F 551   N  THR F 505           
SHEET    3 AB8 4 ASP F 716  ILE F 721 -1  O  PHE F 717   N  CYS F 523           
SHEET    4 AB8 4 PHE F 706  SER F 711 -1  N  SER F 709   O  THR F 718           
SHEET    1 AB9 6 SER F 510  SER F 514  0                                        
SHEET    2 AB9 6 THR F 805  LYS F 810  1  O  GLU F 808   N  LEU F 511           
SHEET    3 AB9 6 ALA F 730  HIS F 752 -1  N  TYR F 732   O  THR F 805           
SHEET    4 AB9 6 MET F 598  GLN F 604 -1  N  TYR F 602   O  TYR F 733           
SHEET    5 AB9 6 LYS F 611  LYS F 615 -1  O  LEU F 613   N  TRP F 601           
SHEET    6 AB9 6 TYR F 696  LEU F 697 -1  O  TYR F 696   N  LYS F 615           
SHEET    1 AC1 4 SER F 510  SER F 514  0                                        
SHEET    2 AC1 4 THR F 805  LYS F 810  1  O  GLU F 808   N  LEU F 511           
SHEET    3 AC1 4 ALA F 730  HIS F 752 -1  N  TYR F 732   O  THR F 805           
SHEET    4 AC1 4 THR F 799  PHE F 801 -1  O  THR F 799   N  HIS F 752           
SHEET    1 AC2 4 SER F2008  PHE F2010  0                                        
SHEET    2 AC2 4 GLY F2021  PHE F2031 -1  O  VAL F2025   N  PHE F2010           
SHEET    3 AC2 4 TYR F2065  THR F2074 -1  O  MET F2067   N  LEU F2028           
SHEET    4 AC2 4 VAL F2051  TRP F2055 -1  N  SER F2054   O  SER F2068           
SHEET    1 AC3 4 SER F2045  GLU F2046  0                                        
SHEET    2 AC3 4 ILE F2036  ILE F2042 -1  N  ILE F2042   O  SER F2045           
SHEET    3 AC3 4 SER F2083  HIS F2090 -1  O  THR F2085   N  LYS F2041           
SHEET    4 AC3 4 ILE F2097  ASN F2102 -1  O  ILE F2097   N  ALA F2088           
SSBOND   1 CYS A  156    CYS A  190                          1555   1555  2.03  
SSBOND   2 CYS A  157    CYS A  175                          1555   1555  2.04  
SSBOND   3 CYS B  156    CYS B  190                          1555   1555  2.04  
SSBOND   4 CYS B  157    CYS B  175                          1555   1555  2.04  
SSBOND   5 CYS C  122    CYS C  330                          1555   1555  2.03  
SSBOND   6 CYS C 1026    CYS C 1081                          1555   1555  2.05  
SSBOND   7 CYS D  523    CYS D  734                          1555   1555  2.80  
SSBOND   8 CYS D 2026    CYS D 2086                          1555   1555  2.03  
SSBOND   9 CYS E  122    CYS E  330                          1555   1555  2.05  
SSBOND  10 CYS E 1026    CYS E 1081                          1555   1555  2.03  
SSBOND  11 CYS F  523    CYS F  734                          1555   1555  2.04  
SSBOND  12 CYS F 2026    CYS F 2086                          1555   1555  2.04  
CISPEP   1 SER A  183    ASN A  184          0       -13.30                     
CISPEP   2 PHE C 1032    PRO C 1033          0         1.43                     
CISPEP   3 GLU C 1034    PRO C 1035          0         1.51                     
CISPEP   4 TRP C 1074    PRO C 1075          0        -7.68                     
CISPEP   5 SER D  507    PRO D  508          0        -0.14                     
CISPEP   6 GLY D  516    GLN D  517          0       -21.66                     
CISPEP   7 HIS D  722    PRO D  723          0         1.11                     
CISPEP   8 PHE D  796    PRO D  797          0        -7.11                     
CISPEP   9 TYR D 2032    PRO D 2033          0        -1.70                     
CISPEP  10 PHE E 1032    PRO E 1033          0        -4.60                     
CISPEP  11 GLU E 1034    PRO E 1035          0         0.74                     
CISPEP  12 THR E 1070    SER E 1071          0        -7.30                     
CISPEP  13 SER E 1071    ASN E 1072          0        17.42                     
CISPEP  14 TRP E 1074    PRO E 1075          0         0.28                     
CISPEP  15 SER F  507    PRO F  508          0        -1.85                     
CISPEP  16 HIS F  722    PRO F  723          0         1.79                     
CISPEP  17 PHE F  796    PRO F  797          0        -1.50                     
CISPEP  18 TYR F 2032    PRO F 2033          0        -0.24                     
CRYST1   77.631   94.483   94.114  90.00 104.14  90.00 P 1 21 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      0.012881  0.000000  0.003245        0.00000                         
SCALE2      0.000000  0.010584  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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