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Database: PDB
Entry: 5M36
LinkDB: 5M36
Original site: 5M36 
HEADER    HYDROLASE                               14-OCT-16   5M36              
TITLE     THE MOLECULAR TWEEZER CLR01 STABILIZES A DISORDERED PROTEIN-PROTEIN   
TITLE    2 INTERFACE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 14-3-3 PROTEIN ZETA/DELTA;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1,KCIP-1;                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: M-PHASE INDUCER PHOSPHATASE 3;                             
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 SYNONYM: DUAL SPECIFICITY PHOSPHATASE CDC25C;                        
COMPND  10 EC: 3.1.3.48;                                                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: YWHAZ;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    STABILIZATION, 14-3-3, DISORDERED PPI INTERFACE, CDC25C, HYDROLASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BIER,C.OTTMANN                                                      
REVDAT   3   12-DEC-18 5M36    1       LINK                                     
REVDAT   2   22-NOV-17 5M36    1       JRNL                                     
REVDAT   1   15-NOV-17 5M36    0                                                
SPRSDE     15-NOV-17 5M36      5JIV                                             
JRNL        AUTH   D.BIER,S.MITTAL,K.BRAVO-RODRIGUEZ,A.SOWISLOK,X.GUILLORY,     
JRNL        AUTH 2 J.BRIELS,C.HEID,M.BARTEL,B.WETTIG,L.BRUNSVELD,               
JRNL        AUTH 3 E.SANCHEZ-GARCIA,T.SCHRADER,C.OTTMANN                        
JRNL        TITL   THE MOLECULAR TWEEZER CLR01 STABILIZES A DISORDERED          
JRNL        TITL 2 PROTEIN-PROTEIN INTERFACE.                                   
JRNL        REF    J. AM. CHEM. SOC.             V. 139 16256 2017              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   29039919                                                     
JRNL        DOI    10.1021/JACS.7B07939                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 29554                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1555                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2147                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 112                          
REMARK   3   BIN FREE R VALUE                    : 0.4270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3679                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 244                                     
REMARK   3   SOLVENT ATOMS            : 67                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.40000                                             
REMARK   3    B22 (A**2) : 8.89000                                              
REMARK   3    B33 (A**2) : -2.49000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.304         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.251         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.267         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.025        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4039 ; 0.009 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3561 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5527 ; 1.376 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8263 ; 1.214 ; 3.010       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   464 ; 5.711 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;35.922 ;24.809       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   670 ;15.346 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;17.045 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   602 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4390 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   797 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5M36 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001822.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.989                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31166                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.06                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.6800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.01                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.92300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.3.0, PHASER                                  
REMARK 200 STARTING MODEL: 3NKX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM ACETATE; 0.085 M         
REMARK 280  SODIUM CITRATE PH 5.6; 25.5% (W/V) PEG 4000; 15% (V/V) GLYCEROL,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       35.76000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.41000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.18000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.41000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.76000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.18000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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     GLU A    70                                                      
REMARK 465     GLY A    71                                                      
REMARK 465     ALA A    72                                                      
REMARK 465     THR A   205                                                      
REMARK 465     LEU A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     GLU A   208                                                      
REMARK 465     GLU A   209                                                      
REMARK 465     LYS B    68                                                      
REMARK 465     THR B    69                                                      
REMARK 465     GLU B    70                                                      
REMARK 465     THR B   205                                                      
REMARK 465     LEU B   206                                                      
REMARK 465     SER B   207                                                      
REMARK 465     GLU B   208                                                      
REMARK 465     GLU B   209                                                      
REMARK 465     SER B   210                                                      
REMARK 465     SER B   230                                                      
REMARK 465     LEU C   226                                                      
REMARK 465     LYS C   227                                                      
REMARK 465     GLN C   228                                                      
REMARK 465     VAL C   229                                                      
REMARK 465     GLU C   230                                                      
REMARK 465     LYS C   231                                                      
REMARK 465     PHE C   232                                                      
REMARK 465     LYS C   233                                                      
REMARK 465     ASP C   234                                                      
REMARK 465     ASN C   235                                                      
REMARK 465     THR C   236                                                      
REMARK 465     ILE C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     ASP C   239                                                      
REMARK 465     LYS C   240                                                      
REMARK 465     VAL C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     LYS C   243                                                      
REMARK 465     LYS C   244                                                      
REMARK 465     SER D   207                                                      
REMARK 465     ARG D   208                                                      
REMARK 465     SER D   209                                                      
REMARK 465     GLY D   210                                                      
REMARK 465     LEU D   211                                                      
REMARK 465     LEU D   221                                                      
REMARK 465     ASN D   222                                                      
REMARK 465     ARG D   223                                                      
REMARK 465     PRO D   224                                                      
REMARK 465     ARG D   225                                                      
REMARK 465     LEU D   226                                                      
REMARK 465     LYS D   227                                                      
REMARK 465     GLN D   228                                                      
REMARK 465     VAL D   229                                                      
REMARK 465     GLU D   230                                                      
REMARK 465     LYS D   231                                                      
REMARK 465     PHE D   232                                                      
REMARK 465     LYS D   233                                                      
REMARK 465     ASP D   234                                                      
REMARK 465     ASN D   235                                                      
REMARK 465     THR D   236                                                      
REMARK 465     ILE D   237                                                      
REMARK 465     PRO D   238                                                      
REMARK 465     ASP D   239                                                      
REMARK 465     LYS D   240                                                      
REMARK 465     VAL D   241                                                      
REMARK 465     LYS D   242                                                      
REMARK 465     LYS D   243                                                      
REMARK 465     LYS D   244                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A   2    CG   OD1  OD2                                       
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     LYS A  49    CD   CE   NZ                                        
REMARK 470     THR A  69    OG1  CG2                                            
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     LYS A  75    CG   CD   CE   NZ                                   
REMARK 470     GLN A  76    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     ASP A 136    CG   OD1  OD2                                       
REMARK 470     LYS A 139    CG   CD   CE   NZ                                   
REMARK 470     LYS A 157    CE   NZ                                             
REMARK 470     LYS A 158    CG   CD   CE   NZ                                   
REMARK 470     ASP A 204    CG   OD1  OD2                                       
REMARK 470     LYS A 212    CG   CD   CE   NZ                                   
REMARK 470     SER A 230    OG                                                  
REMARK 470     GLU B  73    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  74    CG   CD   CE   NZ                                   
REMARK 470     LYS B  75    CG   CD   CE   NZ                                   
REMARK 470     ARG B  80    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B  81    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     ALA B 134    CB                                                  
REMARK 470     LYS B 139    CG   CD   CE   NZ                                   
REMARK 470     SER C 207    CB   OG                                             
REMARK 470     LEU C 211    CG   CD1  CD2                                       
REMARK 470     TYR D 212    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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    PHE A 104      -61.06   -134.13                                   
REMARK 500    ASN A 183       56.06   -108.33                                   
REMARK 500    PHE B 104      -53.83   -132.48                                   
REMARK 500    SER B 184       71.08   -112.54                                   
REMARK 500    GLU B 202       46.97   -102.58                                   
REMARK 500    SER C 209     -165.97   -120.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 425        DISTANCE =  6.37 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9SZ A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9SZ A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9SZ B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9SZ C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues BEZ A 303 and BEZ B      
REMARK 800  302                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EWZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5EXA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JDD   RELATED DB: PDB                                   
DBREF  5M36 A    2   230  UNP    P63104   1433Z_HUMAN      2    230             
DBREF  5M36 B    2   230  UNP    P63104   1433Z_HUMAN      2    230             
DBREF  5M36 C  207   244  UNP    P30307   MPIP3_HUMAN    207    244             
DBREF  5M36 D  207   244  UNP    P30307   MPIP3_HUMAN    207    244             
SEQRES   1 A  229  ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA GLU          
SEQRES   2 A  229  GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CSO MET LYS          
SEQRES   3 A  229  SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU GLU          
SEQRES   4 A  229  ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL GLY          
SEQRES   5 A  229  ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE GLU          
SEQRES   6 A  229  GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET ALA          
SEQRES   7 A  229  ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG ASP          
SEQRES   8 A  229  ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE LEU          
SEQRES   9 A  229  ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE TYR          
SEQRES  10 A  229  LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA GLU          
SEQRES  11 A  229  VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP GLN          
SEQRES  12 A  229  SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER LYS          
SEQRES  13 A  229  LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY LEU          
SEQRES  14 A  229  ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU ASN          
SEQRES  15 A  229  SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA PHE          
SEQRES  16 A  229  ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU GLU          
SEQRES  17 A  229  SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU ARG          
SEQRES  18 A  229  ASP ASN LEU THR LEU TRP THR SER                              
SEQRES   1 B  229  ASP LYS ASN GLU LEU VAL GLN LYS ALA LYS LEU ALA GLU          
SEQRES   2 B  229  GLN ALA GLU ARG TYR ASP ASP MET ALA ALA CSO MET LYS          
SEQRES   3 B  229  SER VAL THR GLU GLN GLY ALA GLU LEU SER ASN GLU GLU          
SEQRES   4 B  229  ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL GLY          
SEQRES   5 B  229  ALA ARG ARG SER SER TRP ARG VAL VAL SER SER ILE GLU          
SEQRES   6 B  229  GLN LYS THR GLU GLY ALA GLU LYS LYS GLN GLN MET ALA          
SEQRES   7 B  229  ARG GLU TYR ARG GLU LYS ILE GLU THR GLU LEU ARG ASP          
SEQRES   8 B  229  ILE CYS ASN ASP VAL LEU SER LEU LEU GLU LYS PHE LEU          
SEQRES   9 B  229  ILE PRO ASN ALA SER GLN ALA GLU SER LYS VAL PHE TYR          
SEQRES  10 B  229  LEU LYS MET LYS GLY ASP TYR TYR ARG TYR LEU ALA GLU          
SEQRES  11 B  229  VAL ALA ALA GLY ASP ASP LYS LYS GLY ILE VAL ASP GLN          
SEQRES  12 B  229  SER GLN GLN ALA TYR GLN GLU ALA PHE GLU ILE SER LYS          
SEQRES  13 B  229  LYS GLU MET GLN PRO THR HIS PRO ILE ARG LEU GLY LEU          
SEQRES  14 B  229  ALA LEU ASN PHE SER VAL PHE TYR TYR GLU ILE LEU ASN          
SEQRES  15 B  229  SER PRO GLU LYS ALA CYS SER LEU ALA LYS THR ALA PHE          
SEQRES  16 B  229  ASP GLU ALA ILE ALA GLU LEU ASP THR LEU SER GLU GLU          
SEQRES  17 B  229  SER TYR LYS ASP SER THR LEU ILE MET GLN LEU LEU ARG          
SEQRES  18 B  229  ASP ASN LEU THR LEU TRP THR SER                              
SEQRES   1 C   38  SER ARG SER GLY LEU TYR ARG SER PRO SEP MET PRO GLU          
SEQRES   2 C   38  ASN LEU ASN ARG PRO ARG LEU LYS GLN VAL GLU LYS PHE          
SEQRES   3 C   38  LYS ASP ASN THR ILE PRO ASP LYS VAL LYS LYS LYS              
SEQRES   1 D   38  SER ARG SER GLY LEU TYR ARG SER PRO SEP MET PRO GLU          
SEQRES   2 D   38  ASN LEU ASN ARG PRO ARG LEU LYS GLN VAL GLU LYS PHE          
SEQRES   3 D   38  LYS ASP ASN THR ILE PRO ASP LYS VAL LYS LYS LYS              
MODRES 5M36 CSO A   25  CYS  MODIFIED RESIDUE                                   
MODRES 5M36 CSO B   25  CYS  MODIFIED RESIDUE                                   
MODRES 5M36 SEP C  216  SER  MODIFIED RESIDUE                                   
MODRES 5M36 SEP D  216  SER  MODIFIED RESIDUE                                   
HET    CSO  A  25       7                                                       
HET    CSO  B  25       7                                                       
HET    SEP  C 216      10                                                       
HET    SEP  D 216      10                                                       
HET    9SZ  A 301      52                                                       
HET    9SZ  A 302      52                                                       
HET    BEZ  A 303       9                                                       
HET    GOL  A 304       6                                                       
HET    GOL  A 305       6                                                       
HET    9SZ  B 301      52                                                       
HET    BEZ  B 302       9                                                       
HET    GOL  B 303       6                                                       
HET    9SZ  C 301      52                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     9SZ C42 H32 O8 P2                                                    
HETNAM     BEZ BENZOIC ACID                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CSO    2(C3 H7 N O3 S)                                              
FORMUL   3  SEP    2(C3 H8 N O6 P)                                              
FORMUL   5  9SZ    4(C42 H32 O8 P2)                                             
FORMUL   7  BEZ    2(C7 H6 O2)                                                  
FORMUL   8  GOL    3(C3 H8 O3)                                                  
FORMUL  14  HOH   *67(H2 O)                                                     
HELIX    1 AA1 ASP A    2  GLU A   17  1                                  16    
HELIX    2 AA2 ARG A   18  GLN A   32  1                                  15    
HELIX    3 AA3 SER A   37  THR A   69  1                                  33    
HELIX    4 AA4 LYS A   74  PHE A  104  1                                  31    
HELIX    5 AA5 PHE A  104  ALA A  109  1                                   6    
HELIX    6 AA6 GLN A  111  VAL A  132  1                                  22    
HELIX    7 AA7 ALA A  134  MET A  160  1                                  27    
HELIX    8 AA8 HIS A  164  ILE A  181  1                                  18    
HELIX    9 AA9 SER A  184  ASP A  204  1                                  21    
HELIX   10 AB1 LYS A  212  THR A  229  1                                  18    
HELIX   11 AB2 LYS B    3  ALA B   16  1                                  14    
HELIX   12 AB3 ARG B   18  GLN B   32  1                                  15    
HELIX   13 AB4 SER B   37  GLN B   67  1                                  31    
HELIX   14 AB5 GLU B   73  PHE B  104  1                                  32    
HELIX   15 AB6 PHE B  104  ALA B  109  1                                   6    
HELIX   16 AB7 GLN B  111  GLU B  131  1                                  21    
HELIX   17 AB8 ASP B  137  MET B  160  1                                  24    
HELIX   18 AB9 HIS B  164  LEU B  182  1                                  19    
HELIX   19 AC1 SER B  184  GLU B  202  1                                  19    
HELIX   20 AC2 LYS B  212  THR B  229  1                                  18    
LINK         C   ALA A  24                 N   CSO A  25     1555   1555  1.33  
LINK         C   CSO A  25                 N   MET A  26     1555   1555  1.33  
LINK         C   ALA B  24                 N   CSO B  25     1555   1555  1.33  
LINK         C   CSO B  25                 N   MET B  26     1555   1555  1.33  
LINK         C   PRO C 215                 N   SEP C 216     1555   1555  1.33  
LINK         C   SEP C 216                 N   MET C 217     1555   1555  1.34  
LINK         C   PRO D 215                 N   SEP D 216     1555   1555  1.34  
LINK         C   SEP D 216                 N   MET D 217     1555   1555  1.34  
SITE     1 AC1  5 ARG A  60  SER A  64  GLN A  67  TYR A 179                    
SITE     2 AC1  5 9SZ A 302                                                     
SITE     1 AC2  6 ASN A 183  9SZ A 301  HOH A 401  GLN B 150                    
SITE     2 AC2  6 TYR B 178  SER B 190                                          
SITE     1 AC3  2 LYS A 193  ASP A 197                                          
SITE     1 AC4  6 GLN A 150  TYR A 178  LYS A 187  ASN B 183                    
SITE     2 AC4  6 HOH B 411  9SZ C 301                                          
SITE     1 AC5  2 TYR B  82  LYS B  85                                          
SITE     1 AC6  9 ARG B  60  GLN B  67  TYR B 179  GLU B 180                    
SITE     2 AC6  9 9SZ B 301  ARG C 208  SER C 209  TYR C 212                    
SITE     3 AC6  9 HOH C 408                                                     
SITE     1 AC7 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AC7 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AC7 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AC7 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AC8 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AC8 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AC8 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AC8 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AC9 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AC9 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AC9 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AC9 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD1 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD1 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD1 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD1 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD2 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD2 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD2 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD2 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD3 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD3 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD3 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD3 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD4 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD4 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD4 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD4 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD5 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD5 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD5 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD5 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD6 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD6 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD6 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD6 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD7 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD7 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD7 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD7 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD8 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD8 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD8 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD8 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AD9 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AD9 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AD9 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AD9 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AE1 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AE1 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AE1 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AE1 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AE2 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AE2 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AE2 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AE2 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AE3 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AE3 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AE3 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AE3 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AE4 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AE4 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AE4 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AE4 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AE5 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AE5 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AE5 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AE5 15 MET B 218  GLN B 219  ARG B 222                               
SITE     1 AE6 15 ASN A 183  MET A 218  GLN A 219  ARG A 222                    
SITE     2 AE6 15 9SZ A 301  HOH A 401  TYR B  82  LYS B  85                    
SITE     3 AE6 15 GLN B 150  TYR B 178  SER B 190  PHE B 196                    
SITE     4 AE6 15 MET B 218  GLN B 219  ARG B 222                               
CRYST1   71.520  102.360  112.820  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013982  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009769  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008864        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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