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Database: PDB
Entry: 5IHL
LinkDB: 5IHL
Original site: 5IHL 
HEADER    IMMUNE SYSTEM/SIGNALING PROTEIN         29-FEB-16   5IHL              
TITLE     STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE CD40 IN COMPLEX WITH     
TITLE    2 3H56-5 DAB                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 5;       
COMPND   3 CHAIN: A, D, F, H;                                                   
COMPND   4 FRAGMENT: EXTRA CELLULAR DOMAIN (UNP RESIDUES 23-193);               
COMPND   5 SYNONYM: B-CELL SURFACE ANTIGEN CD40,BP50,CD40L RECEPTOR,CDW40;      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 3H56-5 DOMAIN ANTIBODY (DAB);                              
COMPND  10 CHAIN: B, E, G, I;                                                   
COMPND  11 FRAGMENT: 3H56-5 DAB;                                                
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CD40, TNFRSF5;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HEK293;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: HB2151;                                    
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PDOM13                                    
KEYWDS    CELL SURFACE RECEPTOR; DOMAIN ANTIBODY; ANTITUMOR; PROTEIN/PROTEIN    
KEYWDS   2 INTERACTION;, IMMUNE SYSTEM-SIGNALING PROTEIN COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHERIFF                                                             
REVDAT   3   20-JUL-16 5IHL    1       JRNL                                     
REVDAT   2   08-JUN-16 5IHL    1       JRNL                                     
REVDAT   1   01-JUN-16 5IHL    0                                                
JRNL        AUTH   A.P.YAMNIUK,A.SURI,S.R.KRYSTEK,J.TAMURA,V.RAMAMURTHY,R.KUHN, 
JRNL        AUTH 2 K.CARROLL,C.FLEENER,R.RYSECK,L.CHENG,Y.AN,P.DREW,S.GRANT,    
JRNL        AUTH 3 S.J.SUCHARD,S.G.NADLER,J.W.BRYSON,S.SHERIFF                  
JRNL        TITL   FUNCTIONAL ANTAGONISM OF HUMAN CD40 ACHIEVED BY TARGETING A  
JRNL        TITL 2 UNIQUE SPECIES-SPECIFIC EPITOPE.                             
JRNL        REF    J.MOL.BIOL.                   V. 428  2860 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   27216500                                                     
JRNL        DOI    10.1016/J.JMB.2016.05.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34308                          
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)  : 0.269                          
REMARK   3   R VALUE            (WORKING SET)  : 0.268                          
REMARK   3   FREE R VALUE                      : 0.298                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 2.780                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 953                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.40                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 90.80                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3158                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.3366                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3076                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.3337                   
REMARK   3   BIN FREE R VALUE                        : 0.4540                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.60                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 82                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8271                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.11                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.36560                                             
REMARK   3    B22 (A**2) : -7.67200                                             
REMARK   3    B33 (A**2) : 9.03750                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.550               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 2.045               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.486               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 2.443               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.496               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.880                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.836                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8512   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11633  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2697   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 197    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1280   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8512   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1149   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9756   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.43                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.40                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 23.92                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.3542   11.5121  105.6680           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0327 T22:    0.3450                                    
REMARK   3     T33:    0.0243 T12:   -0.1790                                    
REMARK   3     T13:   -0.0102 T23:   -0.3040                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2172 L22:    0.4319                                    
REMARK   3     L33:    1.4118 L12:    1.1025                                    
REMARK   3     L13:    2.6576 L23:    0.8031                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0822 S12:   -0.1475 S13:   -0.0456                     
REMARK   3     S21:   -0.0173 S22:    0.0291 S23:   -0.0641                     
REMARK   3     S31:    0.1074 S32:   -0.3965 S33:    0.0531                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.3888   37.2118  112.6440           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1530 T22:    0.0521                                    
REMARK   3     T33:   -0.1679 T12:    0.0248                                    
REMARK   3     T13:   -0.3040 T23:   -0.2212                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0588 L22:    4.4318                                    
REMARK   3     L33:    6.3966 L12:    0.6133                                    
REMARK   3     L13:   -0.3141 L23:   -1.3836                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0018 S12:    0.3420 S13:    0.3745                     
REMARK   3     S21:   -0.0605 S22:   -0.3345 S23:    0.1465                     
REMARK   3     S31:   -1.0885 S32:   -0.0064 S33:    0.3327                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -59.8421  -19.3939  101.1940           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1019 T22:    0.2390                                    
REMARK   3     T33:   -0.0149 T12:   -0.1562                                    
REMARK   3     T13:    0.1970 T23:    0.0176                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9090 L22:    0.0000                                    
REMARK   3     L33:    4.4043 L12:    2.4003                                    
REMARK   3     L13:   -2.9913 L23:   -1.9426                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1083 S12:   -0.1320 S13:    0.3717                     
REMARK   3     S21:    0.3284 S22:    0.0663 S23:    0.0540                     
REMARK   3     S31:    0.0931 S32:   -0.3241 S33:   -0.1747                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -72.7810  -46.6857  112.3280           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2601 T22:    0.4384                                    
REMARK   3     T33:   -0.4390 T12:   -0.1730                                    
REMARK   3     T13:    0.0616 T23:    0.1563                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.4141 L22:    4.9467                                    
REMARK   3     L33:    9.6070 L12:    1.5650                                    
REMARK   3     L13:   -0.1081 L23:    0.6483                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1100 S12:   -0.0876 S13:   -0.2645                     
REMARK   3     S21:   -0.2527 S22:   -0.2545 S23:   -0.3154                     
REMARK   3     S31:    0.3172 S32:    0.4550 S33:    0.1444                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.9530   12.0194   45.9209           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1411 T22:    0.4384                                    
REMARK   3     T33:   -0.0523 T12:   -0.2906                                    
REMARK   3     T13:    0.0506 T23:    0.1756                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2398 L22:    1.8463                                    
REMARK   3     L33:    3.5119 L12:    2.4670                                    
REMARK   3     L13:   -2.0070 L23:   -4.4364                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0973 S12:   -0.0181 S13:    0.0407                     
REMARK   3     S21:   -0.3535 S22:   -0.0293 S23:    0.3531                     
REMARK   3     S31:    0.2665 S32:    0.0949 S33:    0.1266                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { G|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    2.1545   29.6506   38.0689           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0302 T22:    0.2423                                    
REMARK   3     T33:   -0.2734 T12:    0.0139                                    
REMARK   3     T13:    0.0035 T23:    0.2612                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6785 L22:    3.2989                                    
REMARK   3     L33:   11.8301 L12:    1.5076                                    
REMARK   3     L13:    2.2289 L23:   -1.9650                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.3051 S12:    0.1209 S13:   -0.2720                     
REMARK   3     S21:    0.0666 S22:    0.1448 S23:   -0.5144                     
REMARK   3     S31:    0.6424 S32:    0.2969 S33:    0.1603                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { H|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -52.7840  -26.2256   49.0339           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0579 T22:    0.3336                                    
REMARK   3     T33:   -0.0749 T12:   -0.3040                                    
REMARK   3     T13:   -0.2595 T23:   -0.1853                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0330 L22:    1.3199                                    
REMARK   3     L33:    5.3508 L12:    2.2790                                    
REMARK   3     L13:    2.3746 L23:    2.6618                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0828 S12:    0.1317 S13:    0.0152                     
REMARK   3     S21:   -0.3581 S22:    0.1101 S23:   -0.0536                     
REMARK   3     S31:    0.5537 S32:   -0.1560 S33:   -0.0273                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { I|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -80.2172  -38.6651   38.0997           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1778 T22:    0.0640                                    
REMARK   3     T33:   -0.2461 T12:   -0.2024                                    
REMARK   3     T13:   -0.3040 T23:   -0.3038                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.0073 L22:    3.7121                                    
REMARK   3     L33:    7.3325 L12:    1.8698                                    
REMARK   3     L13:   -1.3412 L23:   -0.0608                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0986 S12:   -0.1995 S13:    0.2559                     
REMARK   3     S21:    0.1855 S22:   -0.2533 S23:    0.2236                     
REMARK   3     S31:   -1.0885 S32:    0.4375 S33:    0.3519                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5IHL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218840.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 3.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MICROMAX CONFOCAL                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 92                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37772                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 42.50                              
REMARK 200  R MERGE                    (I) : 0.13700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 43.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.43900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 12.50                              
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: CD40 ENSEMBLE FROM 1JMA, 2UWI, 2AW2, 1NCF            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 80MM TRIS-HCL, PH 8.5, 1.6M AMMONIUM     
REMARK 280  DIHYDROGEN PHOSPHATE, 20% (V/V) GLYCEROL, PH 3.5, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       78.30000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       79.15000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      100.35000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       78.30000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       79.15000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      100.35000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       78.30000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       79.15000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      100.35000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       78.30000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       79.15000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      100.35000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I                                  
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     ARG A   191                                                      
REMARK 465     LEU A   192                                                      
REMARK 465     ARG A   193                                                      
REMARK 465     ASP A   194                                                      
REMARK 465     PRO A   195                                                      
REMARK 465     GLY A   196                                                      
REMARK 465     GLY A   197                                                      
REMARK 465     GLY A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     ARG A   201                                                      
REMARK 465     LEU A   202                                                      
REMARK 465     VAL A   203                                                      
REMARK 465     PRO A   204                                                      
REMARK 465     ARG A   205                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ALA B   114                                                      
REMARK 465     ALA B   115                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     GLN D   189                                                      
REMARK 465     ASP D   190                                                      
REMARK 465     ARG D   191                                                      
REMARK 465     LEU D   192                                                      
REMARK 465     ARG D   193                                                      
REMARK 465     ASP D   194                                                      
REMARK 465     PRO D   195                                                      
REMARK 465     GLY D   196                                                      
REMARK 465     GLY D   197                                                      
REMARK 465     GLY D   198                                                      
REMARK 465     GLY D   199                                                      
REMARK 465     GLY D   200                                                      
REMARK 465     ARG D   201                                                      
REMARK 465     LEU D   202                                                      
REMARK 465     VAL D   203                                                      
REMARK 465     PRO D   204                                                      
REMARK 465     ARG D   205                                                      
REMARK 465     ALA E   114                                                      
REMARK 465     ALA E   115                                                      
REMARK 465     ALA E   116                                                      
REMARK 465     PRO F    23                                                      
REMARK 465     GLN F   189                                                      
REMARK 465     ASP F   190                                                      
REMARK 465     ARG F   191                                                      
REMARK 465     LEU F   192                                                      
REMARK 465     ARG F   193                                                      
REMARK 465     ASP F   194                                                      
REMARK 465     PRO F   195                                                      
REMARK 465     GLY F   196                                                      
REMARK 465     GLY F   197                                                      
REMARK 465     GLY F   198                                                      
REMARK 465     GLY F   199                                                      
REMARK 465     GLY F   200                                                      
REMARK 465     ARG F   201                                                      
REMARK 465     LEU F   202                                                      
REMARK 465     VAL F   203                                                      
REMARK 465     PRO F   204                                                      
REMARK 465     ARG F   205                                                      
REMARK 465     SER G    -2                                                      
REMARK 465     ALA G   114                                                      
REMARK 465     ALA G   115                                                      
REMARK 465     ALA G   116                                                      
REMARK 465     ASP H   190                                                      
REMARK 465     ARG H   191                                                      
REMARK 465     LEU H   192                                                      
REMARK 465     ARG H   193                                                      
REMARK 465     ASP H   194                                                      
REMARK 465     PRO H   195                                                      
REMARK 465     GLY H   196                                                      
REMARK 465     GLY H   197                                                      
REMARK 465     GLY H   198                                                      
REMARK 465     GLY H   199                                                      
REMARK 465     GLY H   200                                                      
REMARK 465     ARG H   201                                                      
REMARK 465     LEU H   202                                                      
REMARK 465     VAL H   203                                                      
REMARK 465     PRO H   204                                                      
REMARK 465     ARG H   205                                                      
REMARK 465     SER I    -2                                                      
REMARK 465     ALA I   114                                                      
REMARK 465     ALA I   115                                                      
REMARK 465     ALA I   116                                                      
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     GLU A  28    CD   OE1  OE2                                       
REMARK 470     LYS A  29    NZ                                                  
REMARK 470     ILE A  33    CG1  CG2  CD1                                       
REMARK 470     ARG A  90    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ILE A 102    CG1  CG2  CD1                                       
REMARK 470     THR A 112    OG1  CG2                                            
REMARK 470     GLU A 114    CG   CD   OE1  OE2                                  
REMARK 470     SER A 118    OG                                                  
REMARK 470     VAL A 120    CG1  CG2                                            
REMARK 470     ILE A 134    CG1  CG2  CD1                                       
REMARK 470     SER A 152    OG                                                  
REMARK 470     LYS A 160    CE   NZ                                             
REMARK 470     LYS A 170    CG   CD   CE   NZ                                   
REMARK 470     LEU A 172    CG   CD1  CD2                                       
REMARK 470     GLN A 176    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 181    CG   CD   CE   NZ                                   
REMARK 470     THR A 182    OG1  CG2                                            
REMARK 470     GLN A 189    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 190    CG   OD1  OD2                                       
REMARK 470     THR B  -1    OG1  CG2                                            
REMARK 470     ARG B  30    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     LYS B  75    CD   CE   NZ                                        
REMARK 470     LYS B  94    CE   NZ                                             
REMARK 470     SER B 112    OG                                                  
REMARK 470     GLU D  28    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  29    CG   CD   CE   NZ                                   
REMARK 470     TYR D  31    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS D  46    CE   NZ                                             
REMARK 470     GLU D  64    CG   CD   OE1  OE2                                  
REMARK 470     SER D  65    OG                                                  
REMARK 470     GLN D  79    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  81    CE   NZ                                             
REMARK 470     ARG D  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  94    CD   CE   NZ                                        
REMARK 470     ILE D 102    CG1  CG2  CD1                                       
REMARK 470     THR D 104    OG1  CG2                                            
REMARK 470     GLU D 106    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 117    CG   CD   OE1  OE2                                  
REMARK 470     SER D 118    OG                                                  
REMARK 470     VAL D 120    CG1  CG2                                            
REMARK 470     SER D 124    OG                                                  
REMARK 470     PHE D 129    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS D 132    CD   CE   NZ                                        
REMARK 470     ILE D 134    CG1  CG2  CD1                                       
REMARK 470     VAL D 148    CG1  CG2                                            
REMARK 470     PHE D 150    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER D 152    OG                                                  
REMARK 470     ASP D 153    CG   OD1  OD2                                       
REMARK 470     VAL D 154    CG1  CG2                                            
REMARK 470     LYS D 160    CG   CD   CE   NZ                                   
REMARK 470     TRP D 164    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 164    CZ3  CH2                                            
REMARK 470     SER D 166    OG                                                  
REMARK 470     GLU D 168    CG   CD   OE1  OE2                                  
REMARK 470     THR D 169    OG1  CG2                                            
REMARK 470     LYS D 170    CG   CD   CE   NZ                                   
REMARK 470     ASP D 171    CG   OD1  OD2                                       
REMARK 470     LEU D 172    CG   CD1  CD2                                       
REMARK 470     VAL D 173    CG1  CG2                                            
REMARK 470     VAL D 174    CG1  CG2                                            
REMARK 470     GLN D 175    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 181    CG   CD   CE   NZ                                   
REMARK 470     THR D 182    OG1  CG2                                            
REMARK 470     VAL D 184    CG1  CG2                                            
REMARK 470     VAL D 185    CG1  CG2                                            
REMARK 470     GLU E   1    CD   OE1  OE2                                       
REMARK 470     GLN E  13    CG   CD   OE1  NE2                                  
REMARK 470     ARG E  30    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  43    CE   NZ                                             
REMARK 470     GLU E  46    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  47    CZ   NH1  NH2                                       
REMARK 470     LYS E  75    CE   NZ                                             
REMARK 470     LYS E  94    CG   CD   CE   NZ                                   
REMARK 470     ARG F  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F  29    NZ                                                  
REMARK 470     LEU F  32    CG   CD1  CD2                                       
REMARK 470     LYS F  46    CG   CD   CE   NZ                                   
REMARK 470     SER F  65    OG                                                  
REMARK 470     ARG F  90    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN F  92    CG   CD   OE1  NE2                                  
REMARK 470     SER F  97    OG                                                  
REMARK 470     ILE F 102    CG1  CG2  CD1                                       
REMARK 470     GLU F 106    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 114    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 117    CG   CD   OE1  OE2                                  
REMARK 470     SER F 118    OG                                                  
REMARK 470     ILE F 134    CG1  CG2  CD1                                       
REMARK 470     GLU F 144    CG   CD   OE1  OE2                                  
REMARK 470     VAL F 148    CG1  CG2                                            
REMARK 470     SER F 152    OG                                                  
REMARK 470     LYS F 160    CD   CE   NZ                                        
REMARK 470     THR F 165    OG1  CG2                                            
REMARK 470     SER F 166    OG                                                  
REMARK 470     LYS F 170    CG   CD   CE   NZ                                   
REMARK 470     ASP F 171    CG   OD1  OD2                                       
REMARK 470     GLN F 175    CD   OE1  NE2                                       
REMARK 470     GLN F 176    CG   CD   OE1  NE2                                  
REMARK 470     ASP F 180    CG   OD1  OD2                                       
REMARK 470     LYS F 181    CG   CD   CE   NZ                                   
REMARK 470     THR F 182    OG1  CG2                                            
REMARK 470     THR G  -1    OG1  CG2                                            
REMARK 470     ARG G  30    NE   CZ   NH1  NH2                                  
REMARK 470     ASP G  31    CG   OD1  OD2                                       
REMARK 470     THR G  55    OG1  CG2                                            
REMARK 470     LYS G  75    CD   CE   NZ                                        
REMARK 470     LYS G  94    CE   NZ                                             
REMARK 470     TYR H  31    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS H  46    CG   CD   CE   NZ                                   
REMARK 470     GLU H  64    CD   OE1  OE2                                       
REMARK 470     ARG H  90    NE   CZ   NH1  NH2                                  
REMARK 470     LYS H  94    CG   CD   CE   NZ                                   
REMARK 470     ILE H 102    CG1  CG2  CD1                                       
REMARK 470     GLU H 114    CD   OE1  OE2                                       
REMARK 470     GLU H 117    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 120    CG1  CG2                                            
REMARK 470     ARG H 123    CZ   NH1  NH2                                       
REMARK 470     SER H 126    OG                                                  
REMARK 470     LYS H 132    CG   CD   CE   NZ                                   
REMARK 470     ASP H 140    CG   OD1  OD2                                       
REMARK 470     VAL H 148    CG1  CG2                                            
REMARK 470     PHE H 150    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER H 152    OG                                                  
REMARK 470     VAL H 154    CG1  CG2                                            
REMARK 470     LYS H 160    NZ                                                  
REMARK 470     TRP H 164    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 164    CZ3  CH2                                            
REMARK 470     THR H 165    OG1  CG2                                            
REMARK 470     SER H 166    OG                                                  
REMARK 470     GLU H 168    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 170    CG   CD   CE   NZ                                   
REMARK 470     ASP H 171    CG   OD1  OD2                                       
REMARK 470     LEU H 172    CG   CD1  CD2                                       
REMARK 470     VAL H 174    CG1  CG2                                            
REMARK 470     GLN H 175    CG   CD   OE1  NE2                                  
REMARK 470     GLN H 176    CG   CD   OE1  NE2                                  
REMARK 470     THR H 179    OG1  CG2                                            
REMARK 470     LYS H 181    CG   CD   CE   NZ                                   
REMARK 470     THR H 182    OG1  CG2                                            
REMARK 470     ASP H 183    CG   OD1  OD2                                       
REMARK 470     VAL H 185    CG1  CG2                                            
REMARK 470     GLN H 189    CG   CD   OE1  NE2                                  
REMARK 470     VAL I  37    CG1  CG2                                            
REMARK 470     GLN I  39    CG   CD   OE1  NE2                                  
REMARK 470     ARG I  47    CZ   NH1  NH2                                       
REMARK 470     LYS I  75    CE   NZ                                             
REMARK 470     LYS I  94    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    SER A 139   C   -  N   -  CA  ANGL. DEV. =  15.7 DEGREES          
REMARK 500    ALA D 157   C   -  N   -  CA  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    PHE H 129   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES          
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    THR A  24     -154.65     55.26                                   
REMARK 500    ALA A  25      -82.06     60.22                                   
REMARK 500    CYS A  26      119.62     68.92                                   
REMARK 500    LYS A  29        7.47     94.28                                   
REMARK 500    LEU A  32      134.93     72.97                                   
REMARK 500    ASN A  34       55.55     33.17                                   
REMARK 500    SER A  35      -33.14     86.87                                   
REMARK 500    THR A  52     -161.69   -109.33                                   
REMARK 500    GLU A  64       37.96    -76.98                                   
REMARK 500    TYR A  82      103.38     80.16                                   
REMARK 500    GLN A  92      -77.52    -90.54                                   
REMARK 500    GLU A 106      -82.02    -27.62                                   
REMARK 500    GLU A 107      -68.31   -168.72                                   
REMARK 500    THR A 112      -13.67    -49.26                                   
REMARK 500    CYS A 125       86.28     45.34                                   
REMARK 500    PRO A 127      -70.23    -17.77                                   
REMARK 500    LYS A 132       26.41   -145.20                                   
REMARK 500    GLN A 133      149.62     65.58                                   
REMARK 500    ALA A 135       -1.16   -147.24                                   
REMARK 500    THR A 136      150.62     56.49                                   
REMARK 500    VAL A 138       44.34    -87.21                                   
REMARK 500    SER A 139        8.33    -41.47                                   
REMARK 500    ILE A 142       90.81     47.08                                   
REMARK 500    VAL A 154      152.16     56.63                                   
REMARK 500    GLU A 168      -51.89    -13.72                                   
REMARK 500    THR A 169       90.61    -54.33                                   
REMARK 500    ASP A 171      161.99    176.73                                   
REMARK 500    ALA A 177      -95.30    -95.26                                   
REMARK 500    THR A 179      -63.74     47.60                                   
REMARK 500    ASP A 183       92.22    -20.29                                   
REMARK 500    VAL A 184       36.95     28.23                                   
REMARK 500    VAL A 185      -85.76     31.77                                   
REMARK 500    CYS A 186      151.85     49.01                                   
REMARK 500    PRO A 188     -159.89   -113.96                                   
REMARK 500    GLN A 189      -26.76   -177.58                                   
REMARK 500    LEU B  45      129.76     43.69                                   
REMARK 500    ALA B  93     -159.99    -99.24                                   
REMARK 500    LYS B  94      119.12   -175.97                                   
REMARK 500    LEU B  95      -59.05    -18.84                                   
REMARK 500    PHE B  97       36.63     80.71                                   
REMARK 500    ASP B 102       17.08    -66.38                                   
REMARK 500    VAL B 111      -64.90   -107.68                                   
REMARK 500    SER B 112     -154.12     50.53                                   
REMARK 500    ARG D  27      118.16    -31.01                                   
REMARK 500    GLU D  28      139.78    -36.60                                   
REMARK 500    LYS D  29      -39.58     65.43                                   
REMARK 500    TYR D  31      117.21    -15.40                                   
REMARK 500    LEU D  32      121.10   -175.85                                   
REMARK 500    ASN D  34       61.03   -162.15                                   
REMARK 500    SER D  35      -37.97     93.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     166 RAMACHANDRAN OUTLIERS.                        
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 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 201                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AUTHOR STATES THAT THE PROTEIN WAS EXPRESSED WITH ASN153 AND     
REMARK 999 ASN180 (AND POST-TRANSLATIONAL CARBOHYDRATE) AND THEN SUBJECTED TO   
REMARK 999 PNGASE F CLEAVAGE WHICH REMOVES THE CARBOHYDRATE AND LEAVES ASP153   
REMARK 999 AND ASP180 RATHER THAN ASN.                                          
DBREF  5IHL A   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5IHL B   -2   116  PDB    5IHL     5IHL            -2    116             
DBREF  5IHL D   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5IHL E   -2   116  PDB    5IHL     5IHL            -2    116             
DBREF  5IHL F   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5IHL G   -2   116  PDB    5IHL     5IHL            -2    116             
DBREF  5IHL H   23   193  UNP    P25942   TNR5_HUMAN      23    193             
DBREF  5IHL I   -2   116  PDB    5IHL     5IHL            -2    116             
SEQADV 5IHL ASP A  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5IHL ASP A  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5IHL ASP A  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO A  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY A  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY A  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY A  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY A  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY A  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG A  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL LEU A  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL VAL A  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO A  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG A  205  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ASP D  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5IHL ASP D  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5IHL ASP D  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO D  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY D  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY D  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY D  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY D  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY D  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG D  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL LEU D  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL VAL D  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO D  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG D  205  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ASP F  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5IHL ASP F  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5IHL ASP F  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO F  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY F  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY F  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY F  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY F  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY F  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG F  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL LEU F  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL VAL F  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO F  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG F  205  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ASP H  153  UNP  P25942    ASN   153 SEE REMARK 999                 
SEQADV 5IHL ASP H  180  UNP  P25942    ASN   180 SEE REMARK 999                 
SEQADV 5IHL ASP H  194  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO H  195  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY H  196  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY H  197  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY H  198  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY H  199  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL GLY H  200  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG H  201  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL LEU H  202  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL VAL H  203  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL PRO H  204  UNP  P25942              EXPRESSION TAG                 
SEQADV 5IHL ARG H  205  UNP  P25942              EXPRESSION TAG                 
SEQRES   1 A  183  PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE ASN SER          
SEQRES   2 A  183  GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS LEU VAL          
SEQRES   3 A  183  SER ASP CYS THR GLU PHE THR GLU THR GLU CYS LEU PRO          
SEQRES   4 A  183  CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN ARG GLU          
SEQRES   5 A  183  THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO ASN LEU          
SEQRES   6 A  183  GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU THR ASP          
SEQRES   7 A  183  THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS THR SER          
SEQRES   8 A  183  GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER CYS SER          
SEQRES   9 A  183  PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY VAL SER          
SEQRES  10 A  183  ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE PHE SER          
SEQRES  11 A  183  ASP VAL SER SER ALA PHE GLU LYS CYS HIS PRO TRP THR          
SEQRES  12 A  183  SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN ALA GLY          
SEQRES  13 A  183  THR ASP LYS THR ASP VAL VAL CYS GLY PRO GLN ASP ARG          
SEQRES  14 A  183  LEU ARG ASP PRO GLY GLY GLY GLY GLY ARG LEU VAL PRO          
SEQRES  15 A  183  ARG                                                          
SEQRES   1 B  121  SER THR GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU          
SEQRES   2 B  121  VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA          
SEQRES   3 B  121  SER GLY PHE THR PHE ARG ASP TYR GLU MET TRP TRP VAL          
SEQRES   4 B  121  ARG GLN ALA PRO GLY LYS GLY LEU GLU ARG VAL SER ALA          
SEQRES   5 B  121  ILE ASN PRO GLN GLY THR ARG THR TYR TYR ALA ASP SER          
SEQRES   6 B  121  VAL MET GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS          
SEQRES   7 B  121  ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU          
SEQRES   8 B  121  ASP THR ALA VAL TYR TYR CYS ALA LYS LEU PRO PHE THR          
SEQRES   9 B  121  PHE ASP ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 B  121  SER ALA ALA ALA                                              
SEQRES   1 D  183  PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE ASN SER          
SEQRES   2 D  183  GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS LEU VAL          
SEQRES   3 D  183  SER ASP CYS THR GLU PHE THR GLU THR GLU CYS LEU PRO          
SEQRES   4 D  183  CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN ARG GLU          
SEQRES   5 D  183  THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO ASN LEU          
SEQRES   6 D  183  GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU THR ASP          
SEQRES   7 D  183  THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS THR SER          
SEQRES   8 D  183  GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER CYS SER          
SEQRES   9 D  183  PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY VAL SER          
SEQRES  10 D  183  ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE PHE SER          
SEQRES  11 D  183  ASP VAL SER SER ALA PHE GLU LYS CYS HIS PRO TRP THR          
SEQRES  12 D  183  SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN ALA GLY          
SEQRES  13 D  183  THR ASP LYS THR ASP VAL VAL CYS GLY PRO GLN ASP ARG          
SEQRES  14 D  183  LEU ARG ASP PRO GLY GLY GLY GLY GLY ARG LEU VAL PRO          
SEQRES  15 D  183  ARG                                                          
SEQRES   1 E  121  SER THR GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU          
SEQRES   2 E  121  VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA          
SEQRES   3 E  121  SER GLY PHE THR PHE ARG ASP TYR GLU MET TRP TRP VAL          
SEQRES   4 E  121  ARG GLN ALA PRO GLY LYS GLY LEU GLU ARG VAL SER ALA          
SEQRES   5 E  121  ILE ASN PRO GLN GLY THR ARG THR TYR TYR ALA ASP SER          
SEQRES   6 E  121  VAL MET GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS          
SEQRES   7 E  121  ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU          
SEQRES   8 E  121  ASP THR ALA VAL TYR TYR CYS ALA LYS LEU PRO PHE THR          
SEQRES   9 E  121  PHE ASP ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 E  121  SER ALA ALA ALA                                              
SEQRES   1 F  183  PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE ASN SER          
SEQRES   2 F  183  GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS LEU VAL          
SEQRES   3 F  183  SER ASP CYS THR GLU PHE THR GLU THR GLU CYS LEU PRO          
SEQRES   4 F  183  CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN ARG GLU          
SEQRES   5 F  183  THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO ASN LEU          
SEQRES   6 F  183  GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU THR ASP          
SEQRES   7 F  183  THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS THR SER          
SEQRES   8 F  183  GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER CYS SER          
SEQRES   9 F  183  PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY VAL SER          
SEQRES  10 F  183  ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE PHE SER          
SEQRES  11 F  183  ASP VAL SER SER ALA PHE GLU LYS CYS HIS PRO TRP THR          
SEQRES  12 F  183  SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN ALA GLY          
SEQRES  13 F  183  THR ASP LYS THR ASP VAL VAL CYS GLY PRO GLN ASP ARG          
SEQRES  14 F  183  LEU ARG ASP PRO GLY GLY GLY GLY GLY ARG LEU VAL PRO          
SEQRES  15 F  183  ARG                                                          
SEQRES   1 G  121  SER THR GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU          
SEQRES   2 G  121  VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA          
SEQRES   3 G  121  SER GLY PHE THR PHE ARG ASP TYR GLU MET TRP TRP VAL          
SEQRES   4 G  121  ARG GLN ALA PRO GLY LYS GLY LEU GLU ARG VAL SER ALA          
SEQRES   5 G  121  ILE ASN PRO GLN GLY THR ARG THR TYR TYR ALA ASP SER          
SEQRES   6 G  121  VAL MET GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS          
SEQRES   7 G  121  ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU          
SEQRES   8 G  121  ASP THR ALA VAL TYR TYR CYS ALA LYS LEU PRO PHE THR          
SEQRES   9 G  121  PHE ASP ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 G  121  SER ALA ALA ALA                                              
SEQRES   1 H  183  PRO THR ALA CYS ARG GLU LYS GLN TYR LEU ILE ASN SER          
SEQRES   2 H  183  GLN CYS CYS SER LEU CYS GLN PRO GLY GLN LYS LEU VAL          
SEQRES   3 H  183  SER ASP CYS THR GLU PHE THR GLU THR GLU CYS LEU PRO          
SEQRES   4 H  183  CYS GLY GLU SER GLU PHE LEU ASP THR TRP ASN ARG GLU          
SEQRES   5 H  183  THR HIS CYS HIS GLN HIS LYS TYR CYS ASP PRO ASN LEU          
SEQRES   6 H  183  GLY LEU ARG VAL GLN GLN LYS GLY THR SER GLU THR ASP          
SEQRES   7 H  183  THR ILE CYS THR CYS GLU GLU GLY TRP HIS CYS THR SER          
SEQRES   8 H  183  GLU ALA CYS GLU SER CYS VAL LEU HIS ARG SER CYS SER          
SEQRES   9 H  183  PRO GLY PHE GLY VAL LYS GLN ILE ALA THR GLY VAL SER          
SEQRES  10 H  183  ASP THR ILE CYS GLU PRO CYS PRO VAL GLY PHE PHE SER          
SEQRES  11 H  183  ASP VAL SER SER ALA PHE GLU LYS CYS HIS PRO TRP THR          
SEQRES  12 H  183  SER CYS GLU THR LYS ASP LEU VAL VAL GLN GLN ALA GLY          
SEQRES  13 H  183  THR ASP LYS THR ASP VAL VAL CYS GLY PRO GLN ASP ARG          
SEQRES  14 H  183  LEU ARG ASP PRO GLY GLY GLY GLY GLY ARG LEU VAL PRO          
SEQRES  15 H  183  ARG                                                          
SEQRES   1 I  121  SER THR GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU          
SEQRES   2 I  121  VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA          
SEQRES   3 I  121  SER GLY PHE THR PHE ARG ASP TYR GLU MET TRP TRP VAL          
SEQRES   4 I  121  ARG GLN ALA PRO GLY LYS GLY LEU GLU ARG VAL SER ALA          
SEQRES   5 I  121  ILE ASN PRO GLN GLY THR ARG THR TYR TYR ALA ASP SER          
SEQRES   6 I  121  VAL MET GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS          
SEQRES   7 I  121  ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU          
SEQRES   8 I  121  ASP THR ALA VAL TYR TYR CYS ALA LYS LEU PRO PHE THR          
SEQRES   9 I  121  PHE ASP ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 I  121  SER ALA ALA ALA                                              
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  B 201       5                                                       
HET    SO4  G 201       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  SO4    4(O4 S 2-)                                                   
HELIX    1 AA1 ASP A   84  LEU A   87  5                                   4    
HELIX    2 AA2 THR B   28  TYR B   32  5                                   5    
HELIX    3 AA3 ASP B   61  MET B   64  5                                   4    
HELIX    4 AA4 ARG B   83  THR B   87  5                                   5    
HELIX    5 AA5 ASP D   84  LEU D   87  5                                   4    
HELIX    6 AA6 THR E   28  TYR E   32  5                                   5    
HELIX    7 AA7 ASP E   61  MET E   64  5                                   4    
HELIX    8 AA8 ARG E   83  THR E   87  5                                   5    
HELIX    9 AA9 ASP F   84  LEU F   87  5                                   4    
HELIX   10 AB1 THR G   28  TYR G   32  5                                   5    
HELIX   11 AB2 ASP G   61  MET G   64  5                                   4    
HELIX   12 AB3 ARG G   83  THR G   87  5                                   5    
HELIX   13 AB4 ASP H   84  LEU H   87  5                                   4    
HELIX   14 AB5 THR I   28  TYR I   32  5                                   5    
HELIX   15 AB6 ASP I   61  MET I   64  5                                   4    
HELIX   16 AB7 ARG I   83  THR I   87  5                                   5    
SHEET    1 AA1 2 GLN A  45  SER A  49  0                                        
SHEET    2 AA1 2 GLU A  58  PRO A  61 -1  O  LEU A  60   N  LYS A  46           
SHEET    1 AA2 2 GLU A  66  PHE A  67  0                                        
SHEET    2 AA2 2 HIS A  78  GLN A  79 -1  O  HIS A  78   N  PHE A  67           
SHEET    1 AA3 2 LEU A  89  GLN A  93  0                                        
SHEET    2 AA3 2 ILE A 102  CYS A 105 -1  O  THR A 104   N  ARG A  90           
SHEET    1 AA4 2 HIS A 110  CYS A 111  0                                        
SHEET    2 AA4 2 CYS A 119  VAL A 120 -1  O  VAL A 120   N  HIS A 110           
SHEET    1 AA5 2 PHE A 129  VAL A 131  0                                        
SHEET    2 AA5 2 CYS A 143  PRO A 145 -1  O  GLU A 144   N  GLY A 130           
SHEET    1 AA6 2 PHE A 150  PHE A 151  0                                        
SHEET    2 AA6 2 HIS A 162  PRO A 163 -1  O  HIS A 162   N  PHE A 151           
SHEET    1 AA7 4 GLN B   3  SER B   7  0                                        
SHEET    2 AA7 4 LEU B  18  SER B  25 -1  O  ALA B  23   N  LEU B   5           
SHEET    3 AA7 4 THR B  77  MET B  82 -1  O  LEU B  78   N  CYS B  22           
SHEET    4 AA7 4 PHE B  67  ASP B  72 -1  N  THR B  68   O  GLN B  81           
SHEET    1 AA8 6 GLY B  10  LEU B  11  0                                        
SHEET    2 AA8 6 THR B 107  THR B 110  1  O  LEU B 108   N  GLY B  10           
SHEET    3 AA8 6 ALA B  88  CYS B  92 -1  N  ALA B  88   O  VAL B 109           
SHEET    4 AA8 6 MET B  34  GLN B  39 -1  N  VAL B  37   O  TYR B  91           
SHEET    5 AA8 6 GLU B  46  ILE B  51 -1  O  GLU B  46   N  ARG B  38           
SHEET    6 AA8 6 THR B  57  TYR B  59 -1  O  TYR B  58   N  ALA B  50           
SHEET    1 AA9 2 GLN D  45  SER D  49  0                                        
SHEET    2 AA9 2 GLU D  58  PRO D  61 -1  O  LEU D  60   N  LYS D  46           
SHEET    1 AB1 2 GLU D  66  PHE D  67  0                                        
SHEET    2 AB1 2 HIS D  78  GLN D  79 -1  O  HIS D  78   N  PHE D  67           
SHEET    1 AB2 2 LEU D  89  GLN D  93  0                                        
SHEET    2 AB2 2 ILE D 102  CYS D 105 -1  O  THR D 104   N  ARG D  90           
SHEET    1 AB3 2 HIS D 110  CYS D 111  0                                        
SHEET    2 AB3 2 CYS D 119  VAL D 120 -1  O  VAL D 120   N  HIS D 110           
SHEET    1 AB4 2 GLY D 130  VAL D 131  0                                        
SHEET    2 AB4 2 CYS D 143  GLU D 144 -1  O  GLU D 144   N  GLY D 130           
SHEET    1 AB5 4 GLN E   3  SER E   7  0                                        
SHEET    2 AB5 4 LEU E  18  SER E  25 -1  O  SER E  25   N  GLN E   3           
SHEET    3 AB5 4 THR E  77  MET E  82 -1  O  LEU E  78   N  CYS E  22           
SHEET    4 AB5 4 PHE E  67  ASP E  72 -1  N  THR E  68   O  GLN E  81           
SHEET    1 AB6 6 GLY E  10  VAL E  12  0                                        
SHEET    2 AB6 6 THR E 107  VAL E 111  1  O  THR E 110   N  GLY E  10           
SHEET    3 AB6 6 ALA E  88  LYS E  94 -1  N  TYR E  90   O  THR E 107           
SHEET    4 AB6 6 MET E  34  GLN E  39 -1  N  VAL E  37   O  TYR E  91           
SHEET    5 AB6 6 GLU E  46  ILE E  51 -1  O  GLU E  46   N  ARG E  38           
SHEET    6 AB6 6 THR E  57  TYR E  59 -1  O  TYR E  58   N  ALA E  50           
SHEET    1 AB7 2 GLN F  45  SER F  49  0                                        
SHEET    2 AB7 2 GLU F  58  PRO F  61 -1  O  LEU F  60   N  LYS F  46           
SHEET    1 AB8 2 GLU F  66  PHE F  67  0                                        
SHEET    2 AB8 2 HIS F  78  GLN F  79 -1  O  HIS F  78   N  PHE F  67           
SHEET    1 AB9 2 LEU F  89  GLN F  93  0                                        
SHEET    2 AB9 2 ILE F 102  CYS F 105 -1  O  THR F 104   N  ARG F  90           
SHEET    1 AC1 2 HIS F 110  CYS F 111  0                                        
SHEET    2 AC1 2 CYS F 119  VAL F 120 -1  O  VAL F 120   N  HIS F 110           
SHEET    1 AC2 2 PHE F 150  PHE F 151  0                                        
SHEET    2 AC2 2 HIS F 162  PRO F 163 -1  O  HIS F 162   N  PHE F 151           
SHEET    1 AC3 4 GLN G   3  SER G   7  0                                        
SHEET    2 AC3 4 LEU G  18  SER G  25 -1  O  ALA G  23   N  LEU G   5           
SHEET    3 AC3 4 THR G  77  MET G  82 -1  O  LEU G  78   N  CYS G  22           
SHEET    4 AC3 4 PHE G  67  ASP G  72 -1  N  THR G  68   O  GLN G  81           
SHEET    1 AC4 6 GLY G  10  LEU G  11  0                                        
SHEET    2 AC4 6 THR G 107  THR G 110  1  O  THR G 110   N  GLY G  10           
SHEET    3 AC4 6 ALA G  88  LYS G  94 -1  N  TYR G  90   O  THR G 107           
SHEET    4 AC4 6 MET G  34  GLN G  39 -1  N  VAL G  37   O  TYR G  91           
SHEET    5 AC4 6 GLU G  46  ILE G  51 -1  O  GLU G  46   N  ARG G  38           
SHEET    6 AC4 6 THR G  57  TYR G  59 -1  O  TYR G  58   N  ALA G  50           
SHEET    1 AC5 2 GLN H  45  SER H  49  0                                        
SHEET    2 AC5 2 GLU H  58  PRO H  61 -1  O  LEU H  60   N  LYS H  46           
SHEET    1 AC6 2 GLU H  66  PHE H  67  0                                        
SHEET    2 AC6 2 HIS H  78  GLN H  79 -1  O  HIS H  78   N  PHE H  67           
SHEET    1 AC7 2 LEU H  89  VAL H  91  0                                        
SHEET    2 AC7 2 CYS H 103  CYS H 105 -1  O  THR H 104   N  ARG H  90           
SHEET    1 AC8 2 HIS H 110  CYS H 111  0                                        
SHEET    2 AC8 2 CYS H 119  VAL H 120 -1  O  VAL H 120   N  HIS H 110           
SHEET    1 AC9 2 GLY H 130  VAL H 131  0                                        
SHEET    2 AC9 2 CYS H 143  GLU H 144 -1  O  GLU H 144   N  GLY H 130           
SHEET    1 AD1 4 GLN I   3  SER I   7  0                                        
SHEET    2 AD1 4 LEU I  18  SER I  25 -1  O  SER I  25   N  GLN I   3           
SHEET    3 AD1 4 THR I  77  MET I  82 -1  O  LEU I  78   N  CYS I  22           
SHEET    4 AD1 4 PHE I  67  ASP I  72 -1  N  THR I  68   O  GLN I  81           
SHEET    1 AD2 6 GLY I  10  VAL I  12  0                                        
SHEET    2 AD2 6 THR I 107  VAL I 111  1  O  THR I 110   N  VAL I  12           
SHEET    3 AD2 6 ALA I  88  LYS I  94 -1  N  TYR I  90   O  THR I 107           
SHEET    4 AD2 6 MET I  34  GLN I  39 -1  N  VAL I  37   O  TYR I  91           
SHEET    5 AD2 6 GLU I  46  ILE I  51 -1  O  GLU I  46   N  ARG I  38           
SHEET    6 AD2 6 THR I  57  TYR I  59 -1  O  TYR I  58   N  ALA I  50           
SSBOND   1 CYS A   26    CYS A   37                          1555   1555  2.05  
SSBOND   2 CYS A   38    CYS A   51                          1555   1555  2.05  
SSBOND   3 CYS A   41    CYS A   59                          1555   1555  2.05  
SSBOND   4 CYS A   62    CYS A   77                          1555   1555  2.05  
SSBOND   5 CYS A   83    CYS A  103                          1555   1555  2.04  
SSBOND   6 CYS A  105    CYS A  119                          1555   1555  2.03  
SSBOND   7 CYS A  111    CYS A  116                          1555   1555  2.02  
SSBOND   8 CYS A  125    CYS A  143                          1555   1555  2.05  
SSBOND   9 CYS A  146    CYS A  161                          1555   1555  2.06  
SSBOND  10 CYS A  167    CYS A  186                          1555   1555  2.03  
SSBOND  11 CYS B   22    CYS B   92                          1555   1555  2.04  
SSBOND  12 CYS D   26    CYS D   37                          1555   1555  2.05  
SSBOND  13 CYS D   38    CYS D   51                          1555   1555  2.04  
SSBOND  14 CYS D   41    CYS D   59                          1555   1555  2.04  
SSBOND  15 CYS D   62    CYS D   77                          1555   1555  2.04  
SSBOND  16 CYS D   83    CYS D  103                          1555   1555  2.04  
SSBOND  17 CYS D  105    CYS D  119                          1555   1555  2.03  
SSBOND  18 CYS D  111    CYS D  116                          1555   1555  2.05  
SSBOND  19 CYS D  125    CYS D  143                          1555   1555  2.03  
SSBOND  20 CYS D  146    CYS D  161                          1555   1555  2.04  
SSBOND  21 CYS D  167    CYS D  186                          1555   1555  2.04  
SSBOND  22 CYS E   22    CYS E   92                          1555   1555  2.04  
SSBOND  23 CYS F   26    CYS F   37                          1555   1555  2.05  
SSBOND  24 CYS F   38    CYS F   51                          1555   1555  2.05  
SSBOND  25 CYS F   41    CYS F   59                          1555   1555  2.04  
SSBOND  26 CYS F   62    CYS F   77                          1555   1555  2.04  
SSBOND  27 CYS F   83    CYS F  103                          1555   1555  2.03  
SSBOND  28 CYS F  105    CYS F  119                          1555   1555  2.03  
SSBOND  29 CYS F  111    CYS F  116                          1555   1555  2.02  
SSBOND  30 CYS F  125    CYS F  143                          1555   1555  2.04  
SSBOND  31 CYS F  146    CYS F  161                          1555   1555  2.04  
SSBOND  32 CYS F  167    CYS F  186                          1555   1555  2.04  
SSBOND  33 CYS G   22    CYS G   92                          1555   1555  2.05  
SSBOND  34 CYS H   26    CYS H   37                          1555   1555  2.05  
SSBOND  35 CYS H   38    CYS H   51                          1555   1555  2.03  
SSBOND  36 CYS H   41    CYS H   59                          1555   1555  2.04  
SSBOND  37 CYS H   62    CYS H   77                          1555   1555  2.04  
SSBOND  38 CYS H   83    CYS H  103                          1555   1555  2.04  
SSBOND  39 CYS H  105    CYS H  119                          1555   1555  2.04  
SSBOND  40 CYS H  111    CYS H  116                          1555   1555  2.05  
SSBOND  41 CYS H  125    CYS H  143                          1555   1555  2.04  
SSBOND  42 CYS H  146    CYS H  161                          1555   1555  2.05  
SSBOND  43 CYS H  167    CYS H  186                          1555   1555  2.04  
SSBOND  44 CYS I   22    CYS I   92                          1555   1555  2.05  
CISPEP   1 THR A  136    GLY A  137          0        -2.28                     
CISPEP   2 CYS A  186    GLY A  187          0        -5.56                     
CISPEP   3 GLY A  187    PRO A  188          0         2.66                     
CISPEP   4 ALA D  115    CYS D  116          0        -0.27                     
CISPEP   5 GLY D  128    PHE D  129          0        10.48                     
CISPEP   6 THR D  136    GLY D  137          0        10.61                     
CISPEP   7 SER D  156    ALA D  157          0        11.32                     
CISPEP   8 LEU E   95    PRO E   96          0        15.19                     
CISPEP   9 PRO E   96    PHE E   97          0        15.15                     
CISPEP  10 SER F   35    GLN F   36          0        -4.42                     
CISPEP  11 ALA F  115    CYS F  116          0        -1.40                     
CISPEP  12 SER F  126    PRO F  127          0         6.81                     
CISPEP  13 GLY F  128    PHE F  129          0         7.73                     
CISPEP  14 THR F  136    GLY F  137          0         2.33                     
CISPEP  15 THR F  182    ASP F  183          0        -2.71                     
CISPEP  16 LEU G   95    PRO G   96          0         7.83                     
CISPEP  17 ALA H  115    CYS H  116          0        -4.32                     
CISPEP  18 GLY H  128    PHE H  129          0         7.20                     
CISPEP  19 PRO H  147    VAL H  148          0        -1.21                     
CISPEP  20 GLY H  149    PHE H  150          0        -3.35                     
CISPEP  21 THR H  182    ASP H  183          0        -1.23                     
CISPEP  22 CYS H  186    GLY H  187          0        -0.63                     
CISPEP  23 LEU I   95    PRO I   96          0         6.11                     
SITE     1 AC1  5 GLU A 159  LYS A 160  HIS A 162  ARG B  56                    
SITE     2 AC1  5 SER I  82B                                                    
SITE     1 AC2  4 GLU A 159  ASN B  52  GLN B  53  ARG B  56                    
SITE     1 AC3  3 PRO B  96  THR B  98  ASP B 102                               
SITE     1 AC4  5 LYS G  94  PRO G  96  THR G  98  ASP G 101                    
SITE     2 AC4  5 ASP G 102                                                     
CRYST1  156.600  158.300  200.700  90.00  90.00  90.00 I 2 2 2      32          
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      0.006386  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006317  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004983        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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