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Database: PDB
Entry: 3GMH
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Original site: 3GMH 
HEADER    CELL CYCLE                              13-MAR-09   3GMH              
TITLE     CRYSTAL STRUCTURE OF THE MAD2 DIMER                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A;         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: MAD2-LIKE 1, HSMAD2;                                        
COMPND   5 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: MAD2, MAD2A, MAD2L1;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE-30                                    
KEYWDS    CELL CYCLE, MITOTIC SPINDLE ASSEMBLY CHECKPOINT, CELL DIVISION,       
KEYWDS   2 MITOSIS, NUCLEUS                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.OZKAN,X.LUO,M.MACHIUS,H.YU,J.DEISENHOFER                            
REVDAT   3   07-OCT-15 3GMH    1       JRNL                                     
REVDAT   2   02-SEP-15 3GMH    1       JRNL   VERSN                             
REVDAT   1   17-NOV-10 3GMH    0                                                
JRNL        AUTH   M.HARA,E.OZKAN,H.SUN,H.YU,X.LUO                              
JRNL        TITL   STRUCTURE OF AN INTERMEDIATE CONFORMER OF THE SPINDLE        
JRNL        TITL 2 CHECKPOINT PROTEIN MAD2.                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112 11252 2015              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   26305957                                                     
JRNL        DOI    10.1073/PNAS.1512197112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 2009_02_15_2320_3)            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 35601                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1771                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.7388 -  9.2693    1.00     2694   144  0.2143 0.2382        
REMARK   3     2  9.2693 -  7.3650    1.00     2627   146  0.1795 0.2217        
REMARK   3     3  7.3650 -  6.4362    1.00     2630   145  0.2040 0.2354        
REMARK   3     4  6.4362 -  5.8487    1.00     2590   151  0.2122 0.2370        
REMARK   3     5  5.8487 -  5.4301    1.00     2596   137  0.2060 0.2365        
REMARK   3     6  5.4301 -  5.1103    1.00     2604   151  0.1939 0.2250        
REMARK   3     7  5.1103 -  4.8546    1.00     2613   140  0.1864 0.2151        
REMARK   3     8  4.8546 -  4.6434    1.00     2594   125  0.1969 0.2168        
REMARK   3     9  4.6434 -  4.4648    1.00     2606   139  0.1953 0.2410        
REMARK   3    10  4.4648 -  4.3108    1.00     2602   123  0.2082 0.2420        
REMARK   3    11  4.3108 -  4.1761    1.00     2587   134  0.2233 0.2598        
REMARK   3    12  4.1761 -  4.0568    1.00     2613   119  0.2406 0.2531        
REMARK   3    13  4.0568 -  3.9500    0.95     2474   117  0.2774 0.3218        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 113.14                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : -0.000           
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 116.12                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 156.85                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.79900                                              
REMARK   3    B22 (A**2) : 33.17000                                             
REMARK   3    B33 (A**2) : -34.96900                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 19.57200                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          18620                                  
REMARK   3   ANGLE     :  1.023          25239                                  
REMARK   3   CHIRALITY :  0.068           3014                                  
REMARK   3   PLANARITY :  0.004           3118                                  
REMARK   3   DIHEDRAL  : 17.096           6775                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain L                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  93.9151 -13.0727  55.3166              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8443 T22:   0.7762                                     
REMARK   3      T33:   1.1296 T12:   0.0678                                     
REMARK   3      T13:  -0.3905 T23:  -0.2433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5900 L22:   4.0035                                     
REMARK   3      L33:   3.3847 L12:   1.2705                                     
REMARK   3      L13:  -0.6918 L23:  -1.2002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1201 S12:   0.0356 S13:  -0.4951                       
REMARK   3      S21:  -0.1738 S22:   0.0396 S23:  -0.2835                       
REMARK   3      S31:   0.3580 S32:  -0.2116 S33:  -0.1079                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 3                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 10:202)                 
REMARK   3     SELECTION          : chain C and (resseq 10:44 or resseq 46:     
REMARK   3                          204)                                        
REMARK   3     ATOM PAIRS NUMBER  : 1550                                        
REMARK   3     RMSD               : 0.028                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 10:202)                 
REMARK   3     SELECTION          : chain E and (resseq 10:204)                 
REMARK   3     ATOM PAIRS NUMBER  : 1507                                        
REMARK   3     RMSD               : 0.039                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 10:202)                 
REMARK   3     SELECTION          : chain G and (resseq 10:203)                 
REMARK   3     ATOM PAIRS NUMBER  : 1518                                        
REMARK   3     RMSD               : 0.033                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 10:202)                 
REMARK   3     SELECTION          : chain I and (resseq 10:32 or resseq 44:     
REMARK   3                          135 or resseq 143:203)                      
REMARK   3     ATOM PAIRS NUMBER  : 1370                                        
REMARK   3     RMSD               : 0.040                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 10:202)                 
REMARK   3     SELECTION          : chain K and (resseq 10:203)                 
REMARK   3     ATOM PAIRS NUMBER  : 1518                                        
REMARK   3     RMSD               : 0.036                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain B                                     
REMARK   3     SELECTION          : chain D                                     
REMARK   3     ATOM PAIRS NUMBER  : 1495                                        
REMARK   3     RMSD               : 0.030                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain B                                     
REMARK   3     SELECTION          : chain F and (resseq 10:46 or resseq 51:     
REMARK   3                          198)                                        
REMARK   3     ATOM PAIRS NUMBER  : 1414                                        
REMARK   3     RMSD               : 0.042                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain B                                     
REMARK   3     SELECTION          : chain H and (resseq 10:157 or resseq 176:   
REMARK   3                          203)                                        
REMARK   3     ATOM PAIRS NUMBER  : 1342                                        
REMARK   3     RMSD               : 0.036                                       
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: chain B                                     
REMARK   3     SELECTION          : chain J and not (resseq 165 and (name CB    
REMARK   3                          or name CG or name CD or name OE*))         
REMARK   3     ATOM PAIRS NUMBER  : 1490                                        
REMARK   3     RMSD               : 0.038                                       
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: chain B                                     
REMARK   3     SELECTION          : chain L and (resseq 10:157 or resseq 176:   
REMARK   3                          198)                                        
REMARK   3     ATOM PAIRS NUMBER  : 1299                                        
REMARK   3     RMSD               : 0.043                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain H and (resseq 163:172)                
REMARK   3     SELECTION          : chain L and (resseq 163:172)                
REMARK   3     ATOM PAIRS NUMBER  : 81                                          
REMARK   3     RMSD               : 0.017                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3GMH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052044.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : CUSTOM                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35718                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.16500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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: 2V64                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 0.1M HEPES, PH    
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.45900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: 2590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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: 2530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
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: 2330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
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: 6                                                       
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: 2310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
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     MET A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     VAL A   203                                                      
REMARK 465     ASN A   204                                                      
REMARK 465     ASP A   205                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     ALA B   110                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     ASP B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     ALA B   115                                                      
REMARK 465     PRO B   116                                                      
REMARK 465     ARG B   117                                                      
REMARK 465     GLU B   118                                                      
REMARK 465     LYS B   119                                                      
REMARK 465     ASN B   204                                                      
REMARK 465     ASP B   205                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     ARG C     0                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     ASP C   205                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     ARG D     0                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     ALA D   110                                                      
REMARK 465     LYS D   111                                                      
REMARK 465     ASP D   112                                                      
REMARK 465     ASP D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     ALA D   115                                                      
REMARK 465     PRO D   116                                                      
REMARK 465     ARG D   117                                                      
REMARK 465     GLU D   118                                                      
REMARK 465     LYS D   119                                                      
REMARK 465     ASN D   204                                                      
REMARK 465     ASP D   205                                                      
REMARK 465     MET E    -1                                                      
REMARK 465     ARG E     0                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     HIS E     3                                                      
REMARK 465     HIS E     4                                                      
REMARK 465     HIS E     5                                                      
REMARK 465     HIS E     6                                                      
REMARK 465     HIS E     7                                                      
REMARK 465     HIS E     8                                                      
REMARK 465     GLY E     9                                                      
REMARK 465     LYS E   111                                                      
REMARK 465     ASP E   112                                                      
REMARK 465     ASP E   113                                                      
REMARK 465     SER E   114                                                      
REMARK 465     ALA E   115                                                      
REMARK 465     PRO E   116                                                      
REMARK 465     ARG E   117                                                      
REMARK 465     ASP E   205                                                      
REMARK 465     MET F    -1                                                      
REMARK 465     ARG F     0                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     HIS F     3                                                      
REMARK 465     HIS F     4                                                      
REMARK 465     HIS F     5                                                      
REMARK 465     HIS F     6                                                      
REMARK 465     HIS F     7                                                      
REMARK 465     HIS F     8                                                      
REMARK 465     ALA F   110                                                      
REMARK 465     LYS F   111                                                      
REMARK 465     ASP F   112                                                      
REMARK 465     ASP F   113                                                      
REMARK 465     SER F   114                                                      
REMARK 465     ALA F   115                                                      
REMARK 465     PRO F   116                                                      
REMARK 465     ARG F   117                                                      
REMARK 465     GLU F   118                                                      
REMARK 465     LYS F   119                                                      
REMARK 465     ASN F   204                                                      
REMARK 465     ASP F   205                                                      
REMARK 465     MET G    -1                                                      
REMARK 465     ARG G     0                                                      
REMARK 465     GLY G     1                                                      
REMARK 465     SER G     2                                                      
REMARK 465     HIS G     3                                                      
REMARK 465     HIS G     4                                                      
REMARK 465     HIS G     5                                                      
REMARK 465     HIS G     6                                                      
REMARK 465     HIS G     7                                                      
REMARK 465     HIS G     8                                                      
REMARK 465     GLY G     9                                                      
REMARK 465     LYS G   111                                                      
REMARK 465     ASP G   112                                                      
REMARK 465     ASP G   113                                                      
REMARK 465     SER G   114                                                      
REMARK 465     ALA G   115                                                      
REMARK 465     PRO G   116                                                      
REMARK 465     VAL G   203                                                      
REMARK 465     ASN G   204                                                      
REMARK 465     ASP G   205                                                      
REMARK 465     MET H    -1                                                      
REMARK 465     ARG H     0                                                      
REMARK 465     GLY H     1                                                      
REMARK 465     SER H     2                                                      
REMARK 465     HIS H     3                                                      
REMARK 465     HIS H     4                                                      
REMARK 465     HIS H     5                                                      
REMARK 465     HIS H     6                                                      
REMARK 465     HIS H     7                                                      
REMARK 465     ALA H   110                                                      
REMARK 465     LYS H   111                                                      
REMARK 465     ASP H   112                                                      
REMARK 465     ASP H   113                                                      
REMARK 465     SER H   114                                                      
REMARK 465     ALA H   115                                                      
REMARK 465     PRO H   116                                                      
REMARK 465     ARG H   117                                                      
REMARK 465     GLU H   118                                                      
REMARK 465     LYS H   119                                                      
REMARK 465     ASN H   204                                                      
REMARK 465     ASP H   205                                                      
REMARK 465     MET I    -1                                                      
REMARK 465     ARG I     0                                                      
REMARK 465     GLY I     1                                                      
REMARK 465     SER I     2                                                      
REMARK 465     HIS I     3                                                      
REMARK 465     HIS I     4                                                      
REMARK 465     HIS I     5                                                      
REMARK 465     HIS I     6                                                      
REMARK 465     HIS I     7                                                      
REMARK 465     HIS I     8                                                      
REMARK 465     GLY I     9                                                      
REMARK 465     LYS I   111                                                      
REMARK 465     ASP I   112                                                      
REMARK 465     ASP I   113                                                      
REMARK 465     SER I   114                                                      
REMARK 465     ALA I   115                                                      
REMARK 465     PRO I   116                                                      
REMARK 465     ASN I   204                                                      
REMARK 465     ASP I   205                                                      
REMARK 465     MET J    -1                                                      
REMARK 465     ARG J     0                                                      
REMARK 465     GLY J     1                                                      
REMARK 465     SER J     2                                                      
REMARK 465     HIS J     3                                                      
REMARK 465     HIS J     4                                                      
REMARK 465     HIS J     5                                                      
REMARK 465     HIS J     6                                                      
REMARK 465     HIS J     7                                                      
REMARK 465     HIS J     8                                                      
REMARK 465     ALA J   110                                                      
REMARK 465     LYS J   111                                                      
REMARK 465     ASP J   112                                                      
REMARK 465     ASP J   113                                                      
REMARK 465     SER J   114                                                      
REMARK 465     ALA J   115                                                      
REMARK 465     PRO J   116                                                      
REMARK 465     ARG J   117                                                      
REMARK 465     GLU J   118                                                      
REMARK 465     LYS J   119                                                      
REMARK 465     ASN J   204                                                      
REMARK 465     ASP J   205                                                      
REMARK 465     MET K    -1                                                      
REMARK 465     ARG K     0                                                      
REMARK 465     GLY K     1                                                      
REMARK 465     SER K     2                                                      
REMARK 465     HIS K     3                                                      
REMARK 465     HIS K     4                                                      
REMARK 465     HIS K     5                                                      
REMARK 465     HIS K     6                                                      
REMARK 465     HIS K     7                                                      
REMARK 465     HIS K     8                                                      
REMARK 465     GLY K     9                                                      
REMARK 465     LYS K   111                                                      
REMARK 465     ASP K   112                                                      
REMARK 465     ASP K   113                                                      
REMARK 465     SER K   114                                                      
REMARK 465     ALA K   115                                                      
REMARK 465     PRO K   116                                                      
REMARK 465     ASN K   204                                                      
REMARK 465     ASP K   205                                                      
REMARK 465     MET L    -1                                                      
REMARK 465     ARG L     0                                                      
REMARK 465     GLY L     1                                                      
REMARK 465     SER L     2                                                      
REMARK 465     HIS L     3                                                      
REMARK 465     HIS L     4                                                      
REMARK 465     HIS L     5                                                      
REMARK 465     HIS L     6                                                      
REMARK 465     HIS L     7                                                      
REMARK 465     HIS L     8                                                      
REMARK 465     ASP L   112                                                      
REMARK 465     ASP L   113                                                      
REMARK 465     SER L   114                                                      
REMARK 465     ALA L   115                                                      
REMARK 465     PRO L   116                                                      
REMARK 465     ARG L   117                                                      
REMARK 465     GLU L   118                                                      
REMARK 465     LYS L   119                                                      
REMARK 465     ASN L   204                                                      
REMARK 465     ASP L   205                                                      
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    GLU A  95      151.07    -48.56                                   
REMARK 500    ALA A 110      -33.16   -142.24                                   
REMARK 500    ASP A 112       67.99   -107.47                                   
REMARK 500    LYS A 119      115.13   -176.47                                   
REMARK 500    ASP A 160       36.31    -82.26                                   
REMARK 500    PRO A 164      151.55    -41.40                                   
REMARK 500    THR A 176      -71.21    -31.74                                   
REMARK 500    THR A 189      -11.94     72.32                                   
REMARK 500    SER B  16     -176.05    -67.85                                   
REMARK 500    PRO B  39     -175.60    -62.98                                   
REMARK 500    TYR B  77       -5.56    -55.53                                   
REMARK 500    GLU B  98      148.58   -176.62                                   
REMARK 500    VAL B 139      -17.55    -47.84                                   
REMARK 500    GLU B 146       -0.55   -151.34                                   
REMARK 500    LEU B 161      149.93   -175.30                                   
REMARK 500    GLU B 169      -74.78     79.15                                   
REMARK 500    GLU B 180       -6.95     79.93                                   
REMARK 500    ASN B 194     -166.28     52.57                                   
REMARK 500    ILE B 201       48.97   -146.45                                   
REMARK 500    GLU C  95      150.97    -49.40                                   
REMARK 500    ALA C 110      -33.21   -141.70                                   
REMARK 500    ASP C 112       67.87   -107.31                                   
REMARK 500    LYS C 119      116.08   -175.68                                   
REMARK 500    ASP C 160       36.09    -82.07                                   
REMARK 500    PRO C 164      151.75    -41.71                                   
REMARK 500    THR C 176      -72.03    -31.07                                   
REMARK 500    THR C 189      -13.02     72.67                                   
REMARK 500    PRO D  39     -175.58    -61.40                                   
REMARK 500    TYR D  77       -5.48    -55.88                                   
REMARK 500    GLU D  98      149.21   -177.60                                   
REMARK 500    VAL D 139      -18.06    -47.57                                   
REMARK 500    GLU D 146       -1.87   -150.00                                   
REMARK 500    LEU D 161      149.54   -173.98                                   
REMARK 500    VAL D 162        3.36    -68.11                                   
REMARK 500    GLU D 169      -75.38     77.73                                   
REMARK 500    GLU D 180       -6.77     79.59                                   
REMARK 500    ASN D 194     -166.17     53.09                                   
REMARK 500    ILE D 201       49.72   -147.18                                   
REMARK 500    GLU E  95      150.27    -47.46                                   
REMARK 500    LYS E 119      116.93   -176.23                                   
REMARK 500    ASP E 160       36.26    -82.29                                   
REMARK 500    PRO E 164      151.13    -40.60                                   
REMARK 500    THR E 176      -73.60    -32.06                                   
REMARK 500    THR E 189      -12.36     70.36                                   
REMARK 500    PRO F  39     -177.43    -60.03                                   
REMARK 500    TYR F  77       -5.85    -56.10                                   
REMARK 500    GLU F  98      148.61   -174.92                                   
REMARK 500    VAL F 139      -18.96    -47.01                                   
REMARK 500    GLU F 146       -1.17   -150.37                                   
REMARK 500    VAL F 162        3.36    -68.86                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     108 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 H 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 206                 
DBREF  3GMH A   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH B   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH C   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH D   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH E   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH F   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH G   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH H   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH I   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH J   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH K   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
DBREF  3GMH L   11   205  UNP    Q13257   MD2L1_HUMAN     11    205             
SEQADV 3GMH MET A   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG A    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY A    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER A    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS A    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS A    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS A    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS A    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS A    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS A    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY A    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER A   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET B   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG B    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY B    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER B    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS B    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS B    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS B    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS B    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS B    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS B    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY B    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER B   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET C   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG C    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY C    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER C    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS C    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS C    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS C    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS C    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS C    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS C    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY C    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER C   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET D   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG D    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY D    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER D    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS D    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS D    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS D    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS D    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS D    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS D    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY D    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER D   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET E   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG E    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY E    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER E    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS E    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS E    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS E    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS E    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS E    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS E    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY E    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER E   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET F   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG F    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY F    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER F    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS F    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS F    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS F    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS F    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS F    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS F    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY F    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER F   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET G   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG G    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY G    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER G    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS G    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS G    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS G    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS G    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS G    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS G    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY G    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER G   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET H   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG H    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY H    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER H    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS H    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS H    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS H    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS H    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS H    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS H    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY H    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER H   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET I   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG I    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY I    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER I    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS I    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS I    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS I    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS I    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS I    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS I    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY I    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER I   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET J   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG J    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY J    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER J    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS J    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS J    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS J    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS J    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS J    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS J    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY J    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER J   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET K   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG K    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY K    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER K    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS K    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS K    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS K    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS K    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS K    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS K    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY K    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER K   10  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH MET L   -1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH ARG L    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY L    1  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER L    2  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS L    3  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS L    4  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS L    5  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS L    6  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS L    7  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH HIS L    8  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH GLY L    9  UNP  Q13257              EXPRESSION TAG                 
SEQADV 3GMH SER L   10  UNP  Q13257              EXPRESSION TAG                 
SEQRES   1 A  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 A  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 A  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 A  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 A  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 A  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 A  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 A  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 A  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 A  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 A  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 A  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 A  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 A  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 A  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 A  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 B  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 B  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 B  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 B  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 B  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 B  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 B  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 B  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 B  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 B  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 B  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 B  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 B  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 B  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 B  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 B  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 C  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 C  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 C  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 C  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 C  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 C  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 C  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 C  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 C  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 C  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 C  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 C  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 C  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 C  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 C  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 C  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 D  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 D  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 D  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 D  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 D  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 D  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 D  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 D  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 D  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 D  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 D  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 D  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 D  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 D  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 D  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 D  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 E  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 E  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 E  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 E  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 E  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 E  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 E  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 E  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 E  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 E  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 E  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 E  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 E  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 E  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 E  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 E  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 F  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 F  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 F  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 F  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 F  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 F  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 F  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 F  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 F  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 F  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 F  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 F  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 F  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 F  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 F  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 F  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 G  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 G  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 G  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 G  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 G  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 G  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 G  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 G  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 G  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 G  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 G  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 G  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 G  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 G  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 G  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 G  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 H  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 H  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 H  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 H  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 H  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 H  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 H  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 H  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 H  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 H  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 H  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 H  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 H  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 H  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 H  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 H  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 I  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 I  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 I  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 I  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 I  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 I  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 I  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 I  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 I  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 I  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 I  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 I  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 I  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 I  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 I  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 I  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 J  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 J  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 J  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 J  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 J  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 J  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 J  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 J  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 J  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 J  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 J  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 J  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 J  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 J  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 J  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 J  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 K  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 K  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 K  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 K  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 K  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 K  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 K  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 K  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 K  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 K  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 K  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 K  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 K  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 K  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 K  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 K  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 L  207  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE          
SEQRES   2 L  207  THR LEU ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE          
SEQRES   3 L  207  SER PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE          
SEQRES   4 L  207  TYR PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY          
SEQRES   5 L  207  LEU THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS          
SEQRES   6 L  207  TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU          
SEQRES   7 L  207  TYR LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER          
SEQRES   8 L  207  ASN ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE          
SEQRES   9 L  207  ASP ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA          
SEQRES  10 L  207  PRO ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 L  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 L  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 L  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 L  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 L  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 L  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
HET    SO4  H 206       5                                                       
HET    SO4  L 206       5                                                       
HET    SO4  D 206       5                                                       
HET    SO4  B 206       5                                                       
HET    SO4  A 206       5                                                       
HET    SO4  C 206       5                                                       
HET    SO4  C 207       5                                                       
HET    SO4  A 207       5                                                       
HET    SO4  I 206       5                                                       
HET    SO4  E 206       5                                                       
HET    SO4  K 206       5                                                       
HET    SO4  G 206       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL  13  SO4    12(O4 S 2-)                                                  
HELIX    1   1 THR A   12  GLN A   34  1                                  23    
HELIX    2   2 PRO A   39  GLU A   41  5                                   3    
HELIX    3   3 ASP A   58  CYS A   79  1                                  22    
HELIX    4   4 SER A  120  THR A  138  1                                  19    
HELIX    5   5 SER B   16  ARG B   35  1                                  20    
HELIX    6   6 ASP B   58  TYR B   77  1                                  20    
HELIX    7   7 SER B  120  THR B  140  1                                  21    
HELIX    8   8 PRO B  164  GLU B  168  5                                   5    
HELIX    9   9 THR C   12  GLN C   34  1                                  23    
HELIX   10  10 PRO C   39  GLU C   41  5                                   3    
HELIX   11  11 ASP C   58  CYS C   79  1                                  22    
HELIX   12  12 SER C  120  THR C  138  1                                  19    
HELIX   13  13 SER D   16  ARG D   35  1                                  20    
HELIX   14  14 ASP D   58  TYR D   77  1                                  20    
HELIX   15  15 SER D  120  THR D  140  1                                  21    
HELIX   16  16 PRO D  164  GLU D  168  5                                   5    
HELIX   17  17 THR E   12  GLN E   34  1                                  23    
HELIX   18  18 PRO E   39  GLU E   41  5                                   3    
HELIX   19  19 ASP E   58  CYS E   79  1                                  22    
HELIX   20  20 SER E  120  THR E  138  1                                  19    
HELIX   21  21 SER F   16  ARG F   35  1                                  20    
HELIX   22  22 ASP F   58  TYR F   77  1                                  20    
HELIX   23  23 SER F  120  THR F  140  1                                  21    
HELIX   24  24 PRO F  164  GLU F  168  5                                   5    
HELIX   25  25 THR G   12  GLN G   34  1                                  23    
HELIX   26  26 PRO G   39  GLU G   41  5                                   3    
HELIX   27  27 ASP G   58  CYS G   79  1                                  22    
HELIX   28  28 SER G  120  THR G  138  1                                  19    
HELIX   29  29 VAL G  139  PHE G  141  5                                   3    
HELIX   30  30 SER H   16  ARG H   35  1                                  20    
HELIX   31  31 ASP H   58  TYR H   77  1                                  20    
HELIX   32  32 SER H  120  THR H  140  1                                  21    
HELIX   33  33 PRO H  164  GLU H  168  5                                   5    
HELIX   34  34 THR I   12  ILE I   37  1                                  26    
HELIX   35  35 PRO I   39  GLU I   41  5                                   3    
HELIX   36  36 ASP I   58  CYS I   79  1                                  22    
HELIX   37  37 SER I  120  LEU I  142  1                                  23    
HELIX   38  38 SER J   16  ARG J   35  1                                  20    
HELIX   39  39 ASP J   58  TYR J   77  1                                  20    
HELIX   40  40 SER J  120  THR J  140  1                                  21    
HELIX   41  41 PRO J  164  GLU J  168  5                                   5    
HELIX   42  42 THR K   12  GLN K   34  1                                  23    
HELIX   43  43 PRO K   39  GLU K   41  5                                   3    
HELIX   44  44 ASP K   58  CYS K   79  1                                  22    
HELIX   45  45 SER K  120  THR K  138  1                                  19    
HELIX   46  46 SER L   16  ARG L   35  1                                  20    
HELIX   47  47 ASP L   58  TYR L   77  1                                  20    
HELIX   48  48 SER L  120  THR L  140  1                                  21    
HELIX   49  49 PRO L  164  GLU L  168  5                                   5    
SHEET    1   A 2 PHE A  43  LYS A  48  0                                        
SHEET    2   A 2 LEU A  51  THR A  56 -1  O  VAL A  55   N  THR A  44           
SHEET    1   B 6 SER A 178  THR A 187  0                                        
SHEET    2   B 6 HIS A 191  LYS A 200 -1  O  VAL A 193   N  PHE A 186           
SHEET    3   B 6 VAL A  96  CYS A 106 -1  N  GLU A 105   O  LYS A 192           
SHEET    4   B 6 VAL A  81  ASN A  90 -1  N  VAL A  86   O  TRP A 100           
SHEET    5   B 6 CYS A 149  THR A 157 -1  O  ASP A 152   N  VAL A  87           
SHEET    6   B 6 VAL D 197  TYR D 199 -1  O  VAL D 197   N  THR A 157           
SHEET    1   C 6 ILE B  11  GLY B  15  0                                        
SHEET    2   C 6 VAL B  96  CYS B 106  1  O  ASP B 103   N  LEU B  13           
SHEET    3   C 6 VAL B  81  ASN B  90 -1  N  LEU B  84   O  PHE B 102           
SHEET    4   C 6 CYS B 149  THR B 157 -1  O  SER B 150   N  SER B  89           
SHEET    5   C 6 LEU B 183  LYS B 192  1  O  HIS B 191   N  ILE B 155           
SHEET    6   C 6 GLN B 173  ILE B 175 -1  N  PHE B 174   O  PHE B 186           
SHEET    1   D 4 LEU B  51  THR B  56  0                                        
SHEET    2   D 4 PHE B  43  LYS B  48 -1  N  VAL B  46   O  LEU B  53           
SHEET    3   D 4 PHE H  43  LYS H  48 -1  O  GLN H  47   N  ARG B  45           
SHEET    4   D 4 LEU H  51  THR H  56 -1  O  LEU H  53   N  VAL H  46           
SHEET    1   E 6 VAL B 197  TYR B 199  0                                        
SHEET    2   E 6 CYS C 149  THR C 157 -1  O  THR C 157   N  VAL B 197           
SHEET    3   E 6 VAL C  81  ASN C  90 -1  N  VAL C  87   O  ASP C 152           
SHEET    4   E 6 VAL C  96  CYS C 106 -1  O  TRP C 100   N  VAL C  86           
SHEET    5   E 6 HIS C 191  LYS C 200 -1  O  LYS C 192   N  GLU C 105           
SHEET    6   E 6 SER C 178  THR C 187 -1  N  PHE C 186   O  VAL C 193           
SHEET    1   F 2 PHE C  43  LYS C  48  0                                        
SHEET    2   F 2 LEU C  51  THR C  56 -1  O  VAL C  55   N  THR C  44           
SHEET    1   G 6 ILE D  11  GLY D  15  0                                        
SHEET    2   G 6 VAL D  96  CYS D 106  1  O  ASP D 103   N  LEU D  13           
SHEET    3   G 6 VAL D  81  ASN D  90 -1  N  LEU D  84   O  PHE D 102           
SHEET    4   G 6 CYS D 149  THR D 157 -1  O  SER D 150   N  SER D  89           
SHEET    5   G 6 LEU D 183  LYS D 192  1  O  HIS D 191   N  ILE D 155           
SHEET    6   G 6 GLN D 173  ILE D 175 -1  N  PHE D 174   O  PHE D 186           
SHEET    1   H 4 LEU D  51  THR D  56  0                                        
SHEET    2   H 4 PHE D  43  LYS D  48 -1  N  VAL D  46   O  LEU D  53           
SHEET    3   H 4 PHE L  43  LYS L  48 -1  O  GLN L  47   N  ARG D  45           
SHEET    4   H 4 LEU L  51  THR L  56 -1  O  LEU L  53   N  VAL L  46           
SHEET    1   I 2 PHE E  43  LYS E  48  0                                        
SHEET    2   I 2 LEU E  51  THR E  56 -1  O  VAL E  55   N  THR E  44           
SHEET    1   J 5 CYS E 149  THR E 157  0                                        
SHEET    2   J 5 VAL E  81  ASN E  90 -1  N  VAL E  87   O  ASP E 152           
SHEET    3   J 5 VAL E  96  CYS E 106 -1  O  PHE E 102   N  LEU E  84           
SHEET    4   J 5 HIS E 191  LYS E 200 -1  O  LYS E 192   N  GLU E 105           
SHEET    5   J 5 SER E 178  THR E 187 -1  N  PHE E 186   O  VAL E 193           
SHEET    1   K 6 ILE F  11  GLY F  15  0                                        
SHEET    2   K 6 VAL F  96  CYS F 106  1  O  ASP F 103   N  LEU F  13           
SHEET    3   K 6 VAL F  81  ASN F  90 -1  N  LEU F  84   O  PHE F 102           
SHEET    4   K 6 CYS F 149  THR F 157 -1  O  SER F 150   N  SER F  89           
SHEET    5   K 6 LEU F 183  LYS F 192  1  O  SER F 185   N  PHE F 151           
SHEET    6   K 6 GLN F 173  ILE F 175 -1  N  PHE F 174   O  PHE F 186           
SHEET    1   L 2 PHE F  43  LYS F  48  0                                        
SHEET    2   L 2 LEU F  51  THR F  56 -1  O  LEU F  53   N  VAL F  46           
SHEET    1   M 2 PHE G  43  LYS G  48  0                                        
SHEET    2   M 2 LEU G  51  THR G  56 -1  O  VAL G  55   N  THR G  44           
SHEET    1   N 6 SER G 178  THR G 187  0                                        
SHEET    2   N 6 HIS G 191  LYS G 200 -1  O  VAL G 193   N  PHE G 186           
SHEET    3   N 6 VAL G  96  CYS G 106 -1  N  GLU G 105   O  LYS G 192           
SHEET    4   N 6 VAL G  81  ASN G  90 -1  N  LEU G  84   O  PHE G 102           
SHEET    5   N 6 CYS G 149  THR G 157 -1  O  ASP G 152   N  VAL G  87           
SHEET    6   N 6 VAL J 197  ALA J 198 -1  O  VAL J 197   N  THR G 157           
SHEET    1   O 6 ILE H  11  GLY H  15  0                                        
SHEET    2   O 6 VAL H  96  CYS H 106  1  O  ASP H 103   N  LEU H  13           
SHEET    3   O 6 VAL H  81  ASN H  90 -1  N  LEU H  84   O  PHE H 102           
SHEET    4   O 6 CYS H 149  THR H 157 -1  O  SER H 150   N  SER H  89           
SHEET    5   O 6 LEU H 183  LYS H 192  1  O  HIS H 191   N  ILE H 155           
SHEET    6   O 6 GLN H 173  ILE H 175 -1  N  PHE H 174   O  PHE H 186           
SHEET    1   P 6 VAL H 197  TYR H 199  0                                        
SHEET    2   P 6 CYS I 149  THR I 157 -1  O  ILE I 155   N  TYR H 199           
SHEET    3   P 6 VAL I  81  ASN I  90 -1  N  VAL I  87   O  ASP I 152           
SHEET    4   P 6 VAL I  96  CYS I 106 -1  O  TRP I 100   N  VAL I  86           
SHEET    5   P 6 HIS I 191  LYS I 200 -1  O  LYS I 192   N  GLU I 105           
SHEET    6   P 6 SER I 178  THR I 187 -1  N  PHE I 186   O  VAL I 193           
SHEET    1   Q 2 PHE I  43  LYS I  48  0                                        
SHEET    2   Q 2 LEU I  51  THR I  56 -1  O  LEU I  53   N  VAL I  46           
SHEET    1   R 6 ILE J  11  GLY J  15  0                                        
SHEET    2   R 6 VAL J  96  CYS J 106  1  O  ASP J 103   N  LEU J  13           
SHEET    3   R 6 VAL J  81  ASN J  90 -1  N  LEU J  84   O  PHE J 102           
SHEET    4   R 6 CYS J 149  THR J 157 -1  O  SER J 150   N  SER J  89           
SHEET    5   R 6 LEU J 183  LYS J 192  1  O  HIS J 191   N  ILE J 155           
SHEET    6   R 6 GLN J 173  ILE J 175 -1  N  PHE J 174   O  PHE J 186           
SHEET    1   S 2 PHE J  43  LYS J  48  0                                        
SHEET    2   S 2 LEU J  51  THR J  56 -1  O  LEU J  53   N  VAL J  46           
SHEET    1   T 2 PHE K  43  LYS K  48  0                                        
SHEET    2   T 2 LEU K  51  THR K  56 -1  O  VAL K  55   N  THR K  44           
SHEET    1   U 5 CYS K 149  THR K 157  0                                        
SHEET    2   U 5 VAL K  81  ASN K  90 -1  N  VAL K  87   O  ASP K 152           
SHEET    3   U 5 VAL K  96  CYS K 106 -1  O  PHE K 102   N  LEU K  84           
SHEET    4   U 5 HIS K 191  LYS K 200 -1  O  LYS K 192   N  GLU K 105           
SHEET    5   U 5 SER K 178  THR K 187 -1  N  PHE K 186   O  VAL K 193           
SHEET    1   V 6 ILE L  11  GLY L  15  0                                        
SHEET    2   V 6 VAL L  96  CYS L 106  1  O  ASP L 103   N  LEU L  13           
SHEET    3   V 6 VAL L  81  ASN L  90 -1  N  LEU L  84   O  PHE L 102           
SHEET    4   V 6 CYS L 149  THR L 157 -1  O  SER L 150   N  SER L  89           
SHEET    5   V 6 LEU L 183  LYS L 192  1  O  HIS L 191   N  ILE L 155           
SHEET    6   V 6 GLN L 173  ILE L 175 -1  N  PHE L 174   O  PHE L 186           
SSBOND   1 CYS A   79    CYS A  106                          1555   1555  2.05  
SSBOND   2 CYS B   79    CYS B  106                          1555   1555  2.04  
SSBOND   3 CYS C   79    CYS C  106                          1555   1555  2.05  
SSBOND   4 CYS D   79    CYS D  106                          1555   1555  2.04  
SSBOND   5 CYS E   79    CYS E  106                          1555   1555  2.04  
SSBOND   6 CYS F   79    CYS F  106                          1555   1555  2.04  
SSBOND   7 CYS G   79    CYS G  106                          1555   1555  2.04  
SSBOND   8 CYS H   79    CYS H  106                          1555   1555  2.04  
SSBOND   9 CYS I   79    CYS I  106                          1555   1555  2.04  
SSBOND  10 CYS J   79    CYS J  106                          1555   1555  2.04  
SSBOND  11 CYS K   79    CYS K  106                          1555   1555  2.04  
SSBOND  12 CYS L   79    CYS L  106                          1555   1555  2.04  
SITE     1 AC1  5 TYR A  33  ARG A  45  ARG B  45  TYR H  49                    
SITE     2 AC1  5 GLY H  50                                                     
SITE     1 AC2  4 TYR C  33  LYS L  48  TYR L  49  GLY L  50                    
SITE     1 AC3  6 LYS D  48  TYR D  49  GLY D  50  TYR K  33                    
SITE     2 AC3  6 ARG K  45  ARG L  45                                          
SITE     1 AC4  6 LYS B  48  TYR B  49  GLY B  50  TYR G  33                    
SITE     2 AC4  6 ARG G  45  ARG H  45                                          
SITE     1 AC5  3 ARG A 182  SER A 185  LYS A 192                               
SITE     1 AC6  3 ARG C 129  ARG C 133  ARG D 182                               
SITE     1 AC7  3 ARG C 182  SER C 185  LYS C 192                               
SITE     1 AC8  4 ARG A 129  ARG A 133  GLY B  36  ARG B 182                    
SITE     1 AC9  4 ARG I 129  ARG I 133  GLY J  36  ARG J 182                    
SITE     1 BC1  4 ARG E 129  ARG E 133  GLY F  36  ARG F 182                    
SITE     1 BC2  5 ARG K 129  ARG K 133  GLY L  36  LEU L 145                    
SITE     2 BC2  5 ARG L 182                                                     
SITE     1 BC3  4 ARG G 129  ARG G 133  GLY H  36  ARG H 182                    
CRYST1  124.829  104.918  157.746  90.00  97.57  90.00 P 1 21 1     24          
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      0.008011  0.000000  0.001065        0.00000                         
SCALE2      0.000000  0.009531  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006395        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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