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Database: PDB
Entry: 6PE8
LinkDB: 6PE8
Original site: 6PE8 
HEADER    IMMUNE SYSTEM                           20-JUN-19   6PE8              
TITLE     CRYSTAL STRUCTURE OF CD40/ABBV-323 FAB COMPLEX                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAB HEAVY CHAIN;                                           
COMPND   3 CHAIN: A, H;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: FAB LIGHT CHAIN;                                           
COMPND   7 CHAIN: B, L;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 5;       
COMPND  11 CHAIN: T, U;                                                         
COMPND  12 SYNONYM: B-CELL SURFACE ANTIGEN CD40,BP50,CD40L RECEPTOR,CDW40;      
COMPND  13 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: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: CD40, TNFRSF5;                                                 
SOURCE  18 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  19 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    CD40, FAB, COMPLEX, IMMUNE SYSTEM                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.ARGIRIADI                                                         
REVDAT   1   14-AUG-19 6PE8    0                                                
JRNL        AUTH   M.A.ARGIRIADI,L.BENATUIL,I.DUBROVSKA,D.A.EGAN,L.GAO,         
JRNL        AUTH 2 A.GREISCHAR,J.HARDMAN,J.HARLAN,R.B.IYER,R.A.JUDGE,M.LAKE,    
JRNL        AUTH 3 D.C.PERRON,R.SADHUKHAN,B.SIELAFF,S.SOUSA,R.WANG,B.L.MCRAE    
JRNL        TITL   CD40/ANTI-CD40 ANTIBODY COMPLEXES WHICH ILLUSTRATE AGONIST   
JRNL        TITL 2 AND ANTAGONIST STRUCTURAL SWITCHES.                          
JRNL        REF    BMC MOL CELL BIOL             V.  20    29 2019              
JRNL        REFN                   ISSN 2661-8850                               
JRNL        PMID   31382872                                                     
JRNL        DOI    10.1186/S12860-019-0213-4                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.900                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 40063                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1925                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.9829 -  6.8325    1.00     2927   135  0.2443 0.2810        
REMARK   3     2  6.8325 -  5.4282    1.00     2787   128  0.2104 0.2770        
REMARK   3     3  5.4282 -  4.7435    1.00     2731   160  0.1683 0.2057        
REMARK   3     4  4.7435 -  4.3105    1.00     2749   136  0.1513 0.1989        
REMARK   3     5  4.3105 -  4.0019    1.00     2710   139  0.1632 0.1989        
REMARK   3     6  4.0019 -  3.7662    1.00     2721   133  0.1821 0.2498        
REMARK   3     7  3.7662 -  3.5777    1.00     2733   119  0.1950 0.2592        
REMARK   3     8  3.5777 -  3.4221    1.00     2680   145  0.2019 0.2977        
REMARK   3     9  3.4221 -  3.2904    1.00     2679   125  0.2319 0.3141        
REMARK   3    10  3.2904 -  3.1769    1.00     2698   159  0.2326 0.3279        
REMARK   3    11  3.1769 -  3.0776    1.00     2662   154  0.2373 0.3224        
REMARK   3    12  3.0776 -  2.9897    1.00     2686   142  0.2526 0.3739        
REMARK   3    13  2.9897 -  2.9110    1.00     2671   135  0.2776 0.3516        
REMARK   3    14  2.9110 -  2.8400    1.00     2704   115  0.3135 0.4420        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.690           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           9243                                  
REMARK   3   ANGLE     :  1.125          12591                                  
REMARK   3   CHIRALITY :  0.056           1405                                  
REMARK   3   PLANARITY :  0.006           1616                                  
REMARK   3   DIHEDRAL  :  3.323           6279                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6PE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000242275.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40335                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 173.200                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6PE7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M PHOSPHATE      
REMARK 280  -CITRATE PH 4.2, VAPOR DIFFUSION, TEMPERATURE 296.15K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       86.65400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.97950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.65400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.97950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, U                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, T                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     SER A   133                                                      
REMARK 465     THR A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     GLY A   136                                                      
REMARK 465     ASP A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     THR A   222                                                      
REMARK 465     HIS A   223                                                      
REMARK 465     SER H   131                                                      
REMARK 465     LYS H   132                                                      
REMARK 465     SER H   133                                                      
REMARK 465     THR H   134                                                      
REMARK 465     SER H   135                                                      
REMARK 465     GLY H   136                                                      
REMARK 465     CYS H   219                                                      
REMARK 465     ASP H   220                                                      
REMARK 465     LYS H   221                                                      
REMARK 465     THR H   222                                                      
REMARK 465     HIS H   223                                                      
REMARK 465     CYS L   220                                                      
REMARK 465     GLU T    21                                                      
REMARK 465     PRO T    22                                                      
REMARK 465     PRO T    23                                                      
REMARK 465     ALA T   177                                                      
REMARK 465     GLY T   178                                                      
REMARK 465     THR T   179                                                      
REMARK 465     ASN T   180                                                      
REMARK 465     GLY T   187                                                      
REMARK 465     PRO T   188                                                      
REMARK 465     GLN T   189                                                      
REMARK 465     ASP T   190                                                      
REMARK 465     ARG T   191                                                      
REMARK 465     LEU T   192                                                      
REMARK 465     ARG T   193                                                      
REMARK 465     GLU U    21                                                      
REMARK 465     PRO U    22                                                      
REMARK 465     ALA U   177                                                      
REMARK 465     GLY U   178                                                      
REMARK 465     THR U   179                                                      
REMARK 465     ASN U   180                                                      
REMARK 465     GLY U   187                                                      
REMARK 465     PRO U   188                                                      
REMARK 465     GLN U   189                                                      
REMARK 465     ASP U   190                                                      
REMARK 465     ARG U   191                                                      
REMARK 465     LEU U   192                                                      
REMARK 465     ARG U   193                                                      
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     LYS H 217    CG   CD   CE   NZ                                   
REMARK 470     PHE T 150    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU T 159    CG   CD   OE1  OE2                                  
REMARK 470     LYS T 160    CG   CD   CE   NZ                                   
REMARK 470     TRP T 164    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP T 164    CZ3  CH2                                            
REMARK 470     GLU T 168    CG   CD   OE1  OE2                                  
REMARK 470     LYS T 170    CG   CD   CE   NZ                                   
REMARK 470     ASP T 171    CG   OD1  OD2                                       
REMARK 470     LEU T 172    CG   CD1  CD2                                       
REMARK 470     VAL T 173    CG1  CG2                                            
REMARK 470     VAL T 174    CG1  CG2                                            
REMARK 470     GLN T 175    CG   CD   OE1  NE2                                  
REMARK 470     GLN T 176    CG   CD   OE1  NE2                                  
REMARK 470     LYS T 181    CG   CD   CE   NZ                                   
REMARK 470     LYS U 170    CG   CD   CE   NZ                                   
REMARK 470     ASP U 171    CG   OD1  OD2                                       
REMARK 470     LEU U 172    CG   CD1  CD2                                       
REMARK 470     VAL U 173    CG1  CG2                                            
REMARK 470     VAL U 174    CG1  CG2                                            
REMARK 470     GLN U 175    CG   CD   OE1  NE2                                  
REMARK 470     GLN U 176    CG   CD   OE1  NE2                                  
REMARK 470     LYS U 181    CG   CD   CE   NZ                                   
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    LYS A  43     -169.20   -113.28                                   
REMARK 500    ASP A 147       66.27     61.55                                   
REMARK 500    ASN A 158       41.77     38.85                                   
REMARK 500    SER A 176       -9.59    -57.09                                   
REMARK 500    LEU A 192      -33.31   -135.77                                   
REMARK 500    PRO B  46      122.06    -39.71                                   
REMARK 500    ALA B  57      -20.93     70.78                                   
REMARK 500    ASN B 144       72.66     62.93                                   
REMARK 500    LYS B 175      -61.57   -101.77                                   
REMARK 500    THR H 138      118.81   -160.86                                   
REMARK 500    ASN L  34       15.77   -142.80                                   
REMARK 500    GLN L  35       18.64     59.60                                   
REMARK 500    ALA L  57      -24.94     70.76                                   
REMARK 500    SER L  58      -10.76   -140.49                                   
REMARK 500    ALA L  90     -178.01   -178.03                                   
REMARK 500    ASN L 144       73.22     57.67                                   
REMARK 500    THR T  52     -169.60   -103.58                                   
REMARK 500    GLN T 133      115.37   -160.17                                   
REMARK 500    VAL T 138        3.05   -172.43                                   
REMARK 500    PHE T 158      -31.28   -131.67                                   
REMARK 500    CYS T 167     -157.49   -151.71                                   
REMARK 500    SER U  35      -13.20     74.14                                   
REMARK 500    THR U  52     -168.23   -104.54                                   
REMARK 500    ARG U  73       30.75   -141.24                                   
REMARK 500    PHE U 158      -32.49   -130.59                                   
REMARK 500    GLU U 168      -62.01    -93.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 T 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 T 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 U 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 U 202                 
DBREF  6PE8 A    1   223  PDB    6PE8     6PE8             1    223             
DBREF  6PE8 B    1   220  PDB    6PE8     6PE8             1    220             
DBREF  6PE8 H    1   223  PDB    6PE8     6PE8             1    223             
DBREF  6PE8 L    1   220  PDB    6PE8     6PE8             1    220             
DBREF  6PE8 T   21   193  UNP    P25942   TNR5_HUMAN      21    193             
DBREF  6PE8 U   21   193  UNP    P25942   TNR5_HUMAN      21    193             
SEQRES   1 A  223  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS          
SEQRES   2 A  223  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 A  223  PHE THR PHE SER ASP TYR GLY MET ASN TRP VAL ARG GLN          
SEQRES   4 A  223  ALA PRO GLY LYS GLY LEU GLU TRP ILE ALA TYR ILE SER          
SEQRES   5 A  223  SER GLY ARG GLY ASN ILE TYR TYR ALA ASP THR VAL LYS          
SEQRES   6 A  223  GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER          
SEQRES   7 A  223  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 A  223  ALA VAL TYR TYR CYS ALA ARG SER TRP GLY TYR PHE ASP          
SEQRES   9 A  223  VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA          
SEQRES  10 A  223  SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER          
SEQRES  11 A  223  SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS          
SEQRES  12 A  223  LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER          
SEQRES  13 A  223  TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE          
SEQRES  14 A  223  PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER          
SEQRES  15 A  223  SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN          
SEQRES  16 A  223  THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR          
SEQRES  17 A  223  LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS          
SEQRES  18 A  223  THR HIS                                                      
SEQRES   1 B  220  ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL          
SEQRES   2 B  220  SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER          
SEQRES   3 B  220  GLN SER LEU LEU ASN ARG GLY ASN GLN LYS ASN TYR LEU          
SEQRES   4 B  220  THR TRP PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU          
SEQRES   5 B  220  LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO          
SEQRES   6 B  220  ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR          
SEQRES   7 B  220  LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL          
SEQRES   8 B  220  TYR TYR CYS GLN ASN ASP TYR THR TYR PRO LEU THR PHE          
SEQRES   9 B  220  GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA          
SEQRES  10 B  220  ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN          
SEQRES  11 B  220  LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN          
SEQRES  12 B  220  ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL          
SEQRES  13 B  220  ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL          
SEQRES  14 B  220  THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER          
SEQRES  15 B  220  SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS          
SEQRES  16 B  220  LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER          
SEQRES  17 B  220  SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS              
SEQRES   1 H  223  GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS          
SEQRES   2 H  223  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  223  PHE THR PHE SER ASP TYR GLY MET ASN TRP VAL ARG GLN          
SEQRES   4 H  223  ALA PRO GLY LYS GLY LEU GLU TRP ILE ALA TYR ILE SER          
SEQRES   5 H  223  SER GLY ARG GLY ASN ILE TYR TYR ALA ASP THR VAL LYS          
SEQRES   6 H  223  GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER          
SEQRES   7 H  223  LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR          
SEQRES   8 H  223  ALA VAL TYR TYR CYS ALA ARG SER TRP GLY TYR PHE ASP          
SEQRES   9 H  223  VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA          
SEQRES  10 H  223  SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER          
SEQRES  11 H  223  SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS          
SEQRES  12 H  223  LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER          
SEQRES  13 H  223  TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE          
SEQRES  14 H  223  PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER          
SEQRES  15 H  223  SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN          
SEQRES  16 H  223  THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR          
SEQRES  17 H  223  LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS          
SEQRES  18 H  223  THR HIS                                                      
SEQRES   1 L  220  ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL          
SEQRES   2 L  220  SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER          
SEQRES   3 L  220  GLN SER LEU LEU ASN ARG GLY ASN GLN LYS ASN TYR LEU          
SEQRES   4 L  220  THR TRP PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU          
SEQRES   5 L  220  LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO          
SEQRES   6 L  220  ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR          
SEQRES   7 L  220  LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL          
SEQRES   8 L  220  TYR TYR CYS GLN ASN ASP TYR THR TYR PRO LEU THR PHE          
SEQRES   9 L  220  GLY GLN GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA          
SEQRES  10 L  220  ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN          
SEQRES  11 L  220  LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN          
SEQRES  12 L  220  ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL          
SEQRES  13 L  220  ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL          
SEQRES  14 L  220  THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER          
SEQRES  15 L  220  SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS          
SEQRES  16 L  220  LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER          
SEQRES  17 L  220  SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS              
SEQRES   1 T  173  GLU PRO PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE          
SEQRES   2 T  173  ASN SER GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS          
SEQRES   3 T  173  LEU VAL SER ASP CYS THR GLU PHE THR GLU THR GLU CYS          
SEQRES   4 T  173  LEU PRO CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN          
SEQRES   5 T  173  ARG GLU THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO          
SEQRES   6 T  173  ASN LEU GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU          
SEQRES   7 T  173  THR ASP THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS          
SEQRES   8 T  173  THR SER GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER          
SEQRES   9 T  173  CYS SER PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY          
SEQRES  10 T  173  VAL SER ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE          
SEQRES  11 T  173  PHE SER ASN VAL SER SER ALA PHE GLU LYS CYS HIS PRO          
SEQRES  12 T  173  TRP THR SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN          
SEQRES  13 T  173  ALA GLY THR ASN LYS THR ASP VAL VAL CYS GLY PRO GLN          
SEQRES  14 T  173  ASP ARG LEU ARG                                              
SEQRES   1 U  173  GLU PRO PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE          
SEQRES   2 U  173  ASN SER GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS          
SEQRES   3 U  173  LEU VAL SER ASP CYS THR GLU PHE THR GLU THR GLU CYS          
SEQRES   4 U  173  LEU PRO CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN          
SEQRES   5 U  173  ARG GLU THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO          
SEQRES   6 U  173  ASN LEU GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU          
SEQRES   7 U  173  THR ASP THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS          
SEQRES   8 U  173  THR SER GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER          
SEQRES   9 U  173  CYS SER PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY          
SEQRES  10 U  173  VAL SER ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE          
SEQRES  11 U  173  PHE SER ASN VAL SER SER ALA PHE GLU LYS CYS HIS PRO          
SEQRES  12 U  173  TRP THR SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN          
SEQRES  13 U  173  ALA GLY THR ASN LYS THR ASP VAL VAL CYS GLY PRO GLN          
SEQRES  14 U  173  ASP ARG LEU ARG                                              
HET    SO4  T 201       5                                                       
HET    SO4  T 202       5                                                       
HET    SO4  U 201       5                                                       
HET    SO4  U 202       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   7  SO4    4(O4 S 2-)                                                   
FORMUL  11  HOH   *151(H2 O)                                                    
HELIX    1 AA1 THR A   28  TYR A   32  5                                   5    
HELIX    2 AA2 ASP A   62  LYS A   65  5                                   4    
HELIX    3 AA3 ARG A   87  THR A   91  5                                   5    
HELIX    4 AA4 SER A  159  ALA A  161  5                                   3    
HELIX    5 AA5 LYS A  204  SER A  206  5                                   3    
HELIX    6 AA6 GLN B   85  VAL B   89  5                                   5    
HELIX    7 AA7 SER B  127  SER B  133  1                                   7    
HELIX    8 AA8 LYS B  189  HIS B  195  1                                   7    
HELIX    9 AA9 THR H   28  TYR H   32  5                                   5    
HELIX   10 AB1 ASP H   62  LYS H   65  5                                   4    
HELIX   11 AB2 ARG H   87  THR H   91  5                                   5    
HELIX   12 AB3 SER H  159  ALA H  161  5                                   3    
HELIX   13 AB4 PRO H  188  THR H  194  5                                   7    
HELIX   14 AB5 LYS H  204  SER H  206  5                                   3    
HELIX   15 AB6 GLN L   85  VAL L   89  5                                   5    
HELIX   16 AB7 SER L  127  SER L  133  1                                   7    
HELIX   17 AB8 LYS L  189  LYS L  194  1                                   6    
HELIX   18 AB9 ASP T   84  LEU T   87  5                                   4    
HELIX   19 AC1 ASP U   84  LEU U   87  5                                   4    
SHEET    1 AA1 4 GLN A   3  SER A   7  0                                        
SHEET    2 AA1 4 LEU A  18  SER A  25 -1  O  SER A  25   N  GLN A   3           
SHEET    3 AA1 4 SER A  78  MET A  83 -1  O  MET A  83   N  LEU A  18           
SHEET    4 AA1 4 PHE A  68  ASP A  73 -1  N  THR A  69   O  GLN A  82           
SHEET    1 AA2 6 GLY A  10  VAL A  12  0                                        
SHEET    2 AA2 6 THR A 110  VAL A 114  1  O  THR A 113   N  GLY A  10           
SHEET    3 AA2 6 ALA A  92  SER A  99 -1  N  TYR A  94   O  THR A 110           
SHEET    4 AA2 6 GLY A  33  GLN A  39 -1  N  VAL A  37   O  TYR A  95           
SHEET    5 AA2 6 LEU A  45  ILE A  51 -1  O  ILE A  51   N  MET A  34           
SHEET    6 AA2 6 ILE A  58  TYR A  60 -1  O  TYR A  59   N  TYR A  50           
SHEET    1 AA3 4 GLY A  10  VAL A  12  0                                        
SHEET    2 AA3 4 THR A 110  VAL A 114  1  O  THR A 113   N  GLY A  10           
SHEET    3 AA3 4 ALA A  92  SER A  99 -1  N  TYR A  94   O  THR A 110           
SHEET    4 AA3 4 PHE A 103  TRP A 106 -1  O  VAL A 105   N  ARG A  98           
SHEET    1 AA4 4 SER A 123  LEU A 127  0                                        
SHEET    2 AA4 4 THR A 138  TYR A 148 -1  O  LEU A 144   N  PHE A 125           
SHEET    3 AA4 4 TYR A 179  PRO A 188 -1  O  VAL A 187   N  ALA A 139           
SHEET    4 AA4 4 HIS A 167  THR A 168 -1  N  HIS A 167   O  VAL A 184           
SHEET    1 AA5 4 SER A 123  LEU A 127  0                                        
SHEET    2 AA5 4 THR A 138  TYR A 148 -1  O  LEU A 144   N  PHE A 125           
SHEET    3 AA5 4 TYR A 179  PRO A 188 -1  O  VAL A 187   N  ALA A 139           
SHEET    4 AA5 4 VAL A 172  LEU A 173 -1  N  VAL A 172   O  SER A 180           
SHEET    1 AA6 6 THR A 154  TRP A 157  0                                        
SHEET    2 AA6 6 TYR A 197  HIS A 203 -1  O  ASN A 200   N  SER A 156           
SHEET    3 AA6 6 THR A 208  VAL A 214 -1  O  VAL A 210   N  VAL A 201           
SHEET    4 AA6 6 THR H 208  VAL H 214 -1  O  LYS H 209   N  ASP A 211           
SHEET    5 AA6 6 TYR H 197  HIS H 203 -1  N  TYR H 197   O  VAL H 214           
SHEET    6 AA6 6 THR H 154  TRP H 157 -1  N  SER H 156   O  ASN H 200           
SHEET    1 AA7 4 MET B   4  SER B   7  0                                        
SHEET    2 AA7 4 ALA B  19  SER B  25 -1  O  ASN B  22   N  SER B   7           
SHEET    3 AA7 4 ASP B  76  ILE B  81 -1  O  LEU B  79   N  ILE B  21           
SHEET    4 AA7 4 PHE B  68  SER B  73 -1  N  SER B  69   O  THR B  80           
SHEET    1 AA8 6 SER B  10  SER B  14  0                                        
SHEET    2 AA8 6 THR B 108  LYS B 113  1  O  GLU B 111   N  LEU B  11           
SHEET    3 AA8 6 ALA B  90  ASN B  96 -1  N  ALA B  90   O  LEU B 110           
SHEET    4 AA8 6 LEU B  39  GLN B  44 -1  N  GLN B  44   O  VAL B  91           
SHEET    5 AA8 6 LYS B  51  TYR B  55 -1  O  LEU B  53   N  TRP B  41           
SHEET    6 AA8 6 THR B  59  ARG B  60 -1  O  THR B  59   N  TYR B  55           
SHEET    1 AA9 2 LEU B  30  ASN B  31  0                                        
SHEET    2 AA9 2 LYS B  36  ASN B  37 -1  O  LYS B  36   N  ASN B  31           
SHEET    1 AB1 4 SER B 120  PHE B 124  0                                        
SHEET    2 AB1 4 THR B 135  PHE B 145 -1  O  ASN B 143   N  SER B 120           
SHEET    3 AB1 4 TYR B 179  SER B 188 -1  O  LEU B 187   N  ALA B 136           
SHEET    4 AB1 4 SER B 165  VAL B 169 -1  N  SER B 168   O  SER B 182           
SHEET    1 AB2 4 ALA B 159  LEU B 160  0                                        
SHEET    2 AB2 4 ALA B 150  VAL B 156 -1  N  VAL B 156   O  ALA B 159           
SHEET    3 AB2 4 VAL B 197  HIS B 204 -1  O  GLU B 201   N  GLN B 153           
SHEET    4 AB2 4 VAL B 211  ASN B 216 -1  O  VAL B 211   N  VAL B 202           
SHEET    1 AB3 4 GLN H   3  SER H   7  0                                        
SHEET    2 AB3 4 LEU H  18  SER H  25 -1  O  SER H  21   N  SER H   7           
SHEET    3 AB3 4 SER H  78  MET H  83 -1  O  LEU H  79   N  CYS H  22           
SHEET    4 AB3 4 PHE H  68  ASP H  73 -1  N  ASP H  73   O  SER H  78           
SHEET    1 AB4 6 GLY H  10  VAL H  12  0                                        
SHEET    2 AB4 6 THR H 110  VAL H 114  1  O  THR H 113   N  VAL H  12           
SHEET    3 AB4 6 ALA H  92  SER H  99 -1  N  TYR H  94   O  THR H 110           
SHEET    4 AB4 6 GLY H  33  GLN H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5 AB4 6 LEU H  45  ILE H  51 -1  O  ILE H  51   N  MET H  34           
SHEET    6 AB4 6 ILE H  58  TYR H  60 -1  O  TYR H  59   N  TYR H  50           
SHEET    1 AB5 4 GLY H  10  VAL H  12  0                                        
SHEET    2 AB5 4 THR H 110  VAL H 114  1  O  THR H 113   N  VAL H  12           
SHEET    3 AB5 4 ALA H  92  SER H  99 -1  N  TYR H  94   O  THR H 110           
SHEET    4 AB5 4 PHE H 103  TRP H 106 -1  O  VAL H 105   N  ARG H  98           
SHEET    1 AB6 4 SER H 123  LEU H 127  0                                        
SHEET    2 AB6 4 ALA H 140  TYR H 148 -1  O  LEU H 144   N  PHE H 125           
SHEET    3 AB6 4 TYR H 179  THR H 186 -1  O  TYR H 179   N  TYR H 148           
SHEET    4 AB6 4 HIS H 167  THR H 168 -1  N  HIS H 167   O  VAL H 184           
SHEET    1 AB7 4 SER H 123  LEU H 127  0                                        
SHEET    2 AB7 4 ALA H 140  TYR H 148 -1  O  LEU H 144   N  PHE H 125           
SHEET    3 AB7 4 TYR H 179  THR H 186 -1  O  TYR H 179   N  TYR H 148           
SHEET    4 AB7 4 VAL H 172  LEU H 173 -1  N  VAL H 172   O  SER H 180           
SHEET    1 AB8 4 MET L   4  SER L   7  0                                        
SHEET    2 AB8 4 ALA L  19  SER L  25 -1  O  LYS L  24   N  THR L   5           
SHEET    3 AB8 4 ASP L  76  ILE L  81 -1  O  LEU L  79   N  ILE L  21           
SHEET    4 AB8 4 PHE L  68  SER L  73 -1  N  SER L  69   O  THR L  80           
SHEET    1 AB9 6 SER L  10  SER L  14  0                                        
SHEET    2 AB9 6 THR L 108  LYS L 113  1  O  GLU L 111   N  LEU L  11           
SHEET    3 AB9 6 VAL L  91  ASN L  96 -1  N  TYR L  92   O  THR L 108           
SHEET    4 AB9 6 LEU L  39  GLN L  44 -1  N  THR L  40   O  GLN L  95           
SHEET    5 AB9 6 LYS L  51  TYR L  55 -1  O  LYS L  51   N  GLN L  43           
SHEET    6 AB9 6 THR L  59  ARG L  60 -1  O  THR L  59   N  TYR L  55           
SHEET    1 AC1 4 SER L 120  PHE L 124  0                                        
SHEET    2 AC1 4 THR L 135  PHE L 145 -1  O  LEU L 141   N  PHE L 122           
SHEET    3 AC1 4 TYR L 179  SER L 188 -1  O  LEU L 187   N  ALA L 136           
SHEET    4 AC1 4 SER L 165  VAL L 169 -1  N  GLN L 166   O  THR L 184           
SHEET    1 AC2 4 ALA L 159  LEU L 160  0                                        
SHEET    2 AC2 4 LYS L 151  VAL L 156 -1  N  VAL L 156   O  ALA L 159           
SHEET    3 AC2 4 VAL L 197  THR L 203 -1  O  GLU L 201   N  GLN L 153           
SHEET    4 AC2 4 VAL L 211  ASN L 216 -1  O  PHE L 215   N  TYR L 198           
SHEET    1 AC3 2 GLN T  30  ILE T  33  0                                        
SHEET    2 AC3 2 GLN T  36  SER T  39 -1  O  CYS T  38   N  TYR T  31           
SHEET    1 AC4 2 GLN T  45  SER T  49  0                                        
SHEET    2 AC4 2 GLU T  58  PRO T  61 -1  O  GLU T  58   N  VAL T  48           
SHEET    1 AC5 2 GLU T  66  PHE T  67  0                                        
SHEET    2 AC5 2 HIS T  78  GLN T  79 -1  O  HIS T  78   N  PHE T  67           
SHEET    1 AC6 2 LEU T  89  GLN T  93  0                                        
SHEET    2 AC6 2 ILE T 102  CYS T 105 -1  O  THR T 104   N  ARG T  90           
SHEET    1 AC7 2 HIS T 110  CYS T 111  0                                        
SHEET    2 AC7 2 CYS T 119  VAL T 120 -1  O  VAL T 120   N  HIS T 110           
SHEET    1 AC8 2 PHE T 129  GLN T 133  0                                        
SHEET    2 AC8 2 ILE T 142  PRO T 145 -1  O  GLU T 144   N  GLY T 130           
SHEET    1 AC9 2 PHE T 150  PHE T 151  0                                        
SHEET    2 AC9 2 HIS T 162  PRO T 163 -1  O  HIS T 162   N  PHE T 151           
SHEET    1 AD1 2 GLN U  30  ILE U  33  0                                        
SHEET    2 AD1 2 GLN U  36  SER U  39 -1  O  CYS U  38   N  TYR U  31           
SHEET    1 AD2 2 GLN U  45  SER U  49  0                                        
SHEET    2 AD2 2 GLU U  58  PRO U  61 -1  O  LEU U  60   N  LYS U  46           
SHEET    1 AD3 2 GLU U  66  PHE U  67  0                                        
SHEET    2 AD3 2 HIS U  78  GLN U  79 -1  O  HIS U  78   N  PHE U  67           
SHEET    1 AD4 2 LEU U  89  GLN U  93  0                                        
SHEET    2 AD4 2 ILE U 102  CYS U 105 -1  O  THR U 104   N  ARG U  90           
SHEET    1 AD5 2 HIS U 110  CYS U 111  0                                        
SHEET    2 AD5 2 CYS U 119  VAL U 120 -1  O  VAL U 120   N  HIS U 110           
SHEET    1 AD6 2 PHE U 129  GLN U 133  0                                        
SHEET    2 AD6 2 ILE U 142  PRO U 145 -1  O  ILE U 142   N  LYS U 132           
SHEET    1 AD7 2 PHE U 150  PHE U 151  0                                        
SHEET    2 AD7 2 HIS U 162  PRO U 163 -1  O  HIS U 162   N  PHE U 151           
SSBOND   1 CYS A   22    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A  143    CYS A  199                          1555   1555  2.02  
SSBOND   3 CYS A  219    CYS B  220                          1555   1555  2.04  
SSBOND   4 CYS B   23    CYS B   94                          1555   1555  2.06  
SSBOND   5 CYS B  140    CYS B  200                          1555   1555  2.02  
SSBOND   6 CYS H   22    CYS H   96                          1555   1555  2.05  
SSBOND   7 CYS H  143    CYS H  199                          1555   1555  2.03  
SSBOND   8 CYS L   23    CYS L   94                          1555   1555  2.05  
SSBOND   9 CYS L  140    CYS L  200                          1555   1555  2.05  
SSBOND  10 CYS T   26    CYS T   37                          1555   1555  2.05  
SSBOND  11 CYS T   38    CYS T   51                          1555   1555  2.07  
SSBOND  12 CYS T   41    CYS T   59                          1555   1555  2.04  
SSBOND  13 CYS T   62    CYS T   77                          1555   1555  2.02  
SSBOND  14 CYS T   83    CYS T  103                          1555   1555  2.05  
SSBOND  15 CYS T  105    CYS T  119                          1555   1555  2.04  
SSBOND  16 CYS T  111    CYS T  116                          1555   1555  2.04  
SSBOND  17 CYS T  125    CYS T  143                          1555   1555  2.11  
SSBOND  18 CYS T  146    CYS T  161                          1555   1555  2.05  
SSBOND  19 CYS T  167    CYS T  186                          1555   1555  2.03  
SSBOND  20 CYS U   26    CYS U   37                          1555   1555  2.14  
SSBOND  21 CYS U   38    CYS U   51                          1555   1555  2.09  
SSBOND  22 CYS U   41    CYS U   59                          1555   1555  2.06  
SSBOND  23 CYS U   62    CYS U   77                          1555   1555  2.06  
SSBOND  24 CYS U   83    CYS U  103                          1555   1555  2.05  
SSBOND  25 CYS U  105    CYS U  119                          1555   1555  2.03  
SSBOND  26 CYS U  111    CYS U  116                          1555   1555  2.04  
SSBOND  27 CYS U  125    CYS U  143                          1555   1555  2.05  
SSBOND  28 CYS U  146    CYS U  161                          1555   1555  2.07  
SSBOND  29 CYS U  167    CYS U  186                          1555   1555  2.05  
CISPEP   1 PHE A  149    PRO A  150          0        -2.19                     
CISPEP   2 GLU A  151    PRO A  152          0         1.18                     
CISPEP   3 SER B    7    PRO B    8          0        -1.02                     
CISPEP   4 TYR B  100    PRO B  101          0         0.35                     
CISPEP   5 TYR B  146    PRO B  147          0        -0.25                     
CISPEP   6 PHE H  149    PRO H  150          0        -2.98                     
CISPEP   7 GLU H  151    PRO H  152          0         1.11                     
CISPEP   8 SER L    7    PRO L    8          0        -0.02                     
CISPEP   9 TYR L  100    PRO L  101          0         5.53                     
CISPEP  10 TYR L  146    PRO L  147          0         1.44                     
CISPEP  11 VAL U  148    GLY U  149          0       -15.90                     
SITE     1 AC1  6 VAL T 120  LEU T 121  HIS T 122  VAL U 120                    
SITE     2 AC1  6 LEU U 121  HIS U 122                                          
SITE     1 AC2  4 GLU B 149  LYS B 151  ARG T 123  ASP T 140                    
SITE     1 AC3  6 LEU T  68  ASP T  69  THR T  70  GLU T  74                    
SITE     2 AC3  6 HIS T  78  ARG U  73                                          
SITE     1 AC4  6 ARG T  73  LEU U  68  ASP U  69  THR U  70                    
SITE     2 AC4  6 GLU U  74  HIS U  78                                          
CRYST1  173.308   75.959  126.093  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005770  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013165  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007931        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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