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Database: PDB
Entry: 1P5Q
LinkDB: 1P5Q
Original site: 1P5Q 
HEADER    ISOMERASE                               28-APR-03   1P5Q              
TITLE     CRYSTAL STRUCTURE OF FKBP52 C-TERMINAL DOMAIN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FK506-BINDING PROTEIN 4;                                   
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: FKBP52 C-TERMINAL DOMAIN;                                  
COMPND   5 SYNONYM: FKBP52;                                                     
COMPND   6 EC: 5.2.1.8;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ISOMERASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.WU,P.LI,Z.LOU,C.SHU,Y.DING,B.SHEN,Z.RAO                             
REVDAT   3   13-JUL-11 1P5Q    1       VERSN                                    
REVDAT   2   24-FEB-09 1P5Q    1       VERSN                                    
REVDAT   1   22-JUN-04 1P5Q    0                                                
JRNL        AUTH   B.WU,P.LI,Y.LIU,Z.LOU,Y.DING,C.SHU,S.YE,M.BARTLAM,B.SHEN,    
JRNL        AUTH 2 Z.RAO                                                        
JRNL        TITL   3D STRUCTURE OF HUMAN FK506-BINDING PROTEIN 52: IMPLICATIONS 
JRNL        TITL 2 FOR THE ASSEMBLY OF THE GLUCOCORTICOID                       
JRNL        TITL 3 RECEPTOR/HSP90/IMMUNOPHILIN HETEROCOMPLEX                    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101  8348 2004              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   15159550                                                     
JRNL        DOI    10.1073/PNAS.0305969101                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -2.000                         
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 291337                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3164                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6876                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 527                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.04                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.19                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.23                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1P5Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-MAY-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019040.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798, 0.9800, 0.9000             
REMARK 200  MONOCHROMATOR                  : MELTING SILICOM + FUZED QUARTZ     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 291337                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS, ETHANOL, PH      
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.44850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.44850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       57.13700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.46350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       57.13700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.46350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.44850            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       57.13700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       71.46350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.44850            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       57.13700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       71.46350            
REMARK 290   SMTRY3   8  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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 81040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -304.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -85.44850            
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   124                                                      
REMARK 465     GLY A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     SER A   127                                                      
REMARK 465     HIS A   128                                                      
REMARK 465     HIS A   129                                                      
REMARK 465     HIS A   130                                                      
REMARK 465     HIS A   131                                                      
REMARK 465     HIS A   132                                                      
REMARK 465     HIS A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     GLY A   136                                                      
REMARK 465     LEU A   137                                                      
REMARK 465     VAL A   138                                                      
REMARK 465     PRO A   139                                                      
REMARK 465     ARG A   140                                                      
REMARK 465     GLY A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     HIS A   143                                                      
REMARK 465     MET A   144                                                      
REMARK 465     GLU A   428                                                      
REMARK 465     ALA A   429                                                      
REMARK 465     SER A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     GLY A   432                                                      
REMARK 465     ASP A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     PRO A   435                                                      
REMARK 465     THR A   436                                                      
REMARK 465     ASP A   437                                                      
REMARK 465     THR A   438                                                      
REMARK 465     GLU A   439                                                      
REMARK 465     MET A   440                                                      
REMARK 465     LYS A   441                                                      
REMARK 465     GLU A   442                                                      
REMARK 465     GLU A   443                                                      
REMARK 465     GLN A   444                                                      
REMARK 465     LYS A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     ASN A   447                                                      
REMARK 465     THR A   448                                                      
REMARK 465     ALA A   449                                                      
REMARK 465     GLY A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     GLN A   452                                                      
REMARK 465     SER A   453                                                      
REMARK 465     GLN A   454                                                      
REMARK 465     VAL A   455                                                      
REMARK 465     GLU A   456                                                      
REMARK 465     THR A   457                                                      
REMARK 465     GLU A   458                                                      
REMARK 465     ALA A   459                                                      
REMARK 465     MET B   124                                                      
REMARK 465     GLY B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     SER B   127                                                      
REMARK 465     HIS B   128                                                      
REMARK 465     HIS B   129                                                      
REMARK 465     HIS B   130                                                      
REMARK 465     HIS B   131                                                      
REMARK 465     HIS B   132                                                      
REMARK 465     HIS B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     SER B   135                                                      
REMARK 465     GLY B   136                                                      
REMARK 465     LEU B   137                                                      
REMARK 465     VAL B   138                                                      
REMARK 465     PRO B   139                                                      
REMARK 465     ARG B   140                                                      
REMARK 465     GLY B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     HIS B   143                                                      
REMARK 465     MET B   144                                                      
REMARK 465     GLU B   428                                                      
REMARK 465     ALA B   429                                                      
REMARK 465     SER B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 465     GLY B   432                                                      
REMARK 465     ASP B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     PRO B   435                                                      
REMARK 465     THR B   436                                                      
REMARK 465     ASP B   437                                                      
REMARK 465     THR B   438                                                      
REMARK 465     GLU B   439                                                      
REMARK 465     MET B   440                                                      
REMARK 465     LYS B   441                                                      
REMARK 465     GLU B   442                                                      
REMARK 465     GLU B   443                                                      
REMARK 465     GLN B   444                                                      
REMARK 465     LYS B   445                                                      
REMARK 465     SER B   446                                                      
REMARK 465     ASN B   447                                                      
REMARK 465     THR B   448                                                      
REMARK 465     ALA B   449                                                      
REMARK 465     GLY B   450                                                      
REMARK 465     SER B   451                                                      
REMARK 465     GLN B   452                                                      
REMARK 465     SER B   453                                                      
REMARK 465     GLN B   454                                                      
REMARK 465     VAL B   455                                                      
REMARK 465     GLU B   456                                                      
REMARK 465     THR B   457                                                      
REMARK 465     GLU B   458                                                      
REMARK 465     ALA B   459                                                      
REMARK 465     MET C   124                                                      
REMARK 465     GLY C   125                                                      
REMARK 465     SER C   126                                                      
REMARK 465     SER C   127                                                      
REMARK 465     HIS C   128                                                      
REMARK 465     HIS C   129                                                      
REMARK 465     HIS C   130                                                      
REMARK 465     HIS C   131                                                      
REMARK 465     HIS C   132                                                      
REMARK 465     HIS C   133                                                      
REMARK 465     SER C   134                                                      
REMARK 465     SER C   135                                                      
REMARK 465     GLY C   136                                                      
REMARK 465     LEU C   137                                                      
REMARK 465     VAL C   138                                                      
REMARK 465     PRO C   139                                                      
REMARK 465     ARG C   140                                                      
REMARK 465     GLY C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     HIS C   143                                                      
REMARK 465     MET C   144                                                      
REMARK 465     GLU C   428                                                      
REMARK 465     ALA C   429                                                      
REMARK 465     SER C   430                                                      
REMARK 465     SER C   431                                                      
REMARK 465     GLY C   432                                                      
REMARK 465     ASP C   433                                                      
REMARK 465     HIS C   434                                                      
REMARK 465     PRO C   435                                                      
REMARK 465     THR C   436                                                      
REMARK 465     ASP C   437                                                      
REMARK 465     THR C   438                                                      
REMARK 465     GLU C   439                                                      
REMARK 465     MET C   440                                                      
REMARK 465     LYS C   441                                                      
REMARK 465     GLU C   442                                                      
REMARK 465     GLU C   443                                                      
REMARK 465     GLN C   444                                                      
REMARK 465     LYS C   445                                                      
REMARK 465     SER C   446                                                      
REMARK 465     ASN C   447                                                      
REMARK 465     THR C   448                                                      
REMARK 465     ALA C   449                                                      
REMARK 465     GLY C   450                                                      
REMARK 465     SER C   451                                                      
REMARK 465     GLN C   452                                                      
REMARK 465     SER C   453                                                      
REMARK 465     GLN C   454                                                      
REMARK 465     VAL C   455                                                      
REMARK 465     GLU C   456                                                      
REMARK 465     THR C   457                                                      
REMARK 465     GLU C   458                                                      
REMARK 465     ALA C   459                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 275    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 275    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLU C   283     OE1  GLU C   283     4565     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG C 318   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 157      159.15    -45.37                                   
REMARK 500    LYS A 179       60.57     60.16                                   
REMARK 500    ASP A 180       -1.98     51.46                                   
REMARK 500    GLN A 185      115.50   -166.61                                   
REMARK 500    ALA A 226     -136.42   -102.52                                   
REMARK 500    GLN A 236       11.38     50.49                                   
REMARK 500    GLU A 246       76.14   -114.05                                   
REMARK 500    SER A 258      -56.19    -19.26                                   
REMARK 500    LEU A 300       20.59    -79.00                                   
REMARK 500    GLU A 301      -71.24    -84.97                                   
REMARK 500    SER A 307       21.53    -61.14                                   
REMARK 500    ASN A 308      -24.45     70.34                                   
REMARK 500    GLU A 309      -60.48    -95.87                                   
REMARK 500    ALA A 334       62.13   -115.74                                   
REMARK 500    ALA A 425       17.24    -65.30                                   
REMARK 500    LYS A 426       63.46   -114.66                                   
REMARK 500    GLU B 159      167.20    167.58                                   
REMARK 500    ASP B 184      119.38   -171.82                                   
REMARK 500    ALA B 226     -131.03    -83.87                                   
REMARK 500    LYS B 232      114.33   -164.65                                   
REMARK 500    ASN B 240       84.38     45.87                                   
REMARK 500    LYS B 250      -70.45    -76.56                                   
REMARK 500    PHE B 252      163.64    175.92                                   
REMARK 500    SER B 258      -47.50    -25.44                                   
REMARK 500    LYS B 285       43.52    -76.16                                   
REMARK 500    TYR B 286      -52.06    -28.28                                   
REMARK 500    SER B 298      -75.51    -59.04                                   
REMARK 500    TRP B 299      -32.41    -36.29                                   
REMARK 500    GLU B 301      -93.62    -56.97                                   
REMARK 500    SER B 305       30.44    -76.91                                   
REMARK 500    SER B 307       79.61   -114.75                                   
REMARK 500    ASN B 308      -83.58     43.48                                   
REMARK 500    ALA B 334       68.34   -107.47                                   
REMARK 500    ASP B 349       88.72   -168.24                                   
REMARK 500    SER B 350        0.66    -66.67                                   
REMARK 500    ASN B 352      106.75    -46.84                                   
REMARK 500    PHE B 369      -51.59    -28.52                                   
REMARK 500    ALA B 425       36.18    -99.95                                   
REMARK 500    GLU C 146       27.55     81.66                                   
REMARK 500    ASP C 147       72.68   -155.24                                   
REMARK 500    THR C 156      114.85   -161.77                                   
REMARK 500    GLU C 159       74.13    175.13                                   
REMARK 500    TYR C 161       16.66     41.25                                   
REMARK 500    ASP C 180       10.83     57.37                                   
REMARK 500    ILE C 192      108.78    -56.33                                   
REMARK 500    GLN C 209        2.20    -68.70                                   
REMARK 500    LYS C 213      146.90    -34.80                                   
REMARK 500    PRO C 223      -70.71    -12.43                                   
REMARK 500    SER C 224        0.98    -61.87                                   
REMARK 500    ALA C 226     -119.72    -93.68                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      71 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR C 225         0.07    SIDE CHAIN                              
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 A1108        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A1115        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A1139        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH A1171        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A1179        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH B1086        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH B1121        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH B1142        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B1176        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH C1118        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH C1125        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C1132        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH C1151        DISTANCE =  5.81 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1009                
DBREF  1P5Q A  146   459  UNP    Q02790   FKBP4_HUMAN    145    458             
DBREF  1P5Q B  146   459  UNP    Q02790   FKBP4_HUMAN    145    458             
DBREF  1P5Q C  146   459  UNP    Q02790   FKBP4_HUMAN    145    458             
SEQADV 1P5Q MET A  124  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY A  125  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER A  126  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER A  127  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS A  128  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS A  129  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS A  130  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS A  131  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS A  132  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS A  133  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER A  134  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER A  135  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY A  136  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q LEU A  137  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q VAL A  138  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q PRO A  139  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q ARG A  140  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY A  141  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER A  142  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS A  143  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q MET A  144  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLU A  145  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q MSE A  211  UNP  Q02790    MET   210 MODIFIED RESIDUE               
SEQADV 1P5Q MSE A  261  UNP  Q02790    MET   260 MODIFIED RESIDUE               
SEQADV 1P5Q SER A  357  UNP  Q02790    PHE   356 CONFLICT                       
SEQADV 1P5Q MET B  124  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY B  125  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER B  126  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER B  127  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS B  128  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS B  129  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS B  130  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS B  131  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS B  132  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS B  133  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER B  134  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER B  135  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY B  136  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q LEU B  137  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q VAL B  138  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q PRO B  139  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q ARG B  140  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY B  141  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER B  142  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS B  143  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q MET B  144  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLU B  145  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q MSE B  211  UNP  Q02790    MET   210 MODIFIED RESIDUE               
SEQADV 1P5Q MSE B  261  UNP  Q02790    MET   260 MODIFIED RESIDUE               
SEQADV 1P5Q SER B  357  UNP  Q02790    PHE   356 CONFLICT                       
SEQADV 1P5Q MET C  124  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY C  125  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER C  126  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER C  127  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS C  128  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS C  129  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS C  130  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS C  131  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS C  132  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS C  133  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER C  134  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER C  135  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY C  136  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q LEU C  137  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q VAL C  138  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q PRO C  139  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q ARG C  140  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLY C  141  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q SER C  142  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q HIS C  143  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q MET C  144  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q GLU C  145  UNP  Q02790              EXPRESSION TAG                 
SEQADV 1P5Q MSE C  211  UNP  Q02790    MET   210 MODIFIED RESIDUE               
SEQADV 1P5Q MSE C  261  UNP  Q02790    MET   260 MODIFIED RESIDUE               
SEQADV 1P5Q SER C  357  UNP  Q02790    PHE   356 CONFLICT                       
SEQRES   1 A  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  336  LEU VAL PRO ARG GLY SER HIS MET GLU GLU ASP GLY GLY          
SEQRES   3 A  336  ILE ILE ARG ARG ILE GLN THR ARG GLY GLU GLY TYR ALA          
SEQRES   4 A  336  LYS PRO ASN GLU GLY ALA ILE VAL GLU VAL ALA LEU GLU          
SEQRES   5 A  336  GLY TYR TYR LYS ASP LYS LEU PHE ASP GLN ARG GLU LEU          
SEQRES   6 A  336  ARG PHE GLU ILE GLY GLU GLY GLU ASN LEU ASP LEU PRO          
SEQRES   7 A  336  TYR GLY LEU GLU ARG ALA ILE GLN ARG MSE GLU LYS GLY          
SEQRES   8 A  336  GLU HIS SER ILE VAL TYR LEU LYS PRO SER TYR ALA PHE          
SEQRES   9 A  336  GLY SER VAL GLY LYS GLU LYS PHE GLN ILE PRO PRO ASN          
SEQRES  10 A  336  ALA GLU LEU LYS TYR GLU LEU HIS LEU LYS SER PHE GLU          
SEQRES  11 A  336  LYS ALA LYS GLU SER TRP GLU MSE ASN SER GLU GLU LYS          
SEQRES  12 A  336  LEU GLU GLN SER THR ILE VAL LYS GLU ARG GLY THR VAL          
SEQRES  13 A  336  TYR PHE LYS GLU GLY LYS TYR LYS GLN ALA LEU LEU GLN          
SEQRES  14 A  336  TYR LYS LYS ILE VAL SER TRP LEU GLU TYR GLU SER SER          
SEQRES  15 A  336  PHE SER ASN GLU GLU ALA GLN LYS ALA GLN ALA LEU ARG          
SEQRES  16 A  336  LEU ALA SER HIS LEU ASN LEU ALA MET CYS HIS LEU LYS          
SEQRES  17 A  336  LEU GLN ALA PHE SER ALA ALA ILE GLU SER CYS ASN LYS          
SEQRES  18 A  336  ALA LEU GLU LEU ASP SER ASN ASN GLU LYS GLY LEU SER          
SEQRES  19 A  336  ARG ARG GLY GLU ALA HIS LEU ALA VAL ASN ASP PHE GLU          
SEQRES  20 A  336  LEU ALA ARG ALA ASP PHE GLN LYS VAL LEU GLN LEU TYR          
SEQRES  21 A  336  PRO ASN ASN LYS ALA ALA LYS THR GLN LEU ALA VAL CYS          
SEQRES  22 A  336  GLN GLN ARG ILE ARG ARG GLN LEU ALA ARG GLU LYS LYS          
SEQRES  23 A  336  LEU TYR ALA ASN MET PHE GLU ARG LEU ALA GLU GLU GLU          
SEQRES  24 A  336  ASN LYS ALA LYS ALA GLU ALA SER SER GLY ASP HIS PRO          
SEQRES  25 A  336  THR ASP THR GLU MET LYS GLU GLU GLN LYS SER ASN THR          
SEQRES  26 A  336  ALA GLY SER GLN SER GLN VAL GLU THR GLU ALA                  
SEQRES   1 B  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  336  LEU VAL PRO ARG GLY SER HIS MET GLU GLU ASP GLY GLY          
SEQRES   3 B  336  ILE ILE ARG ARG ILE GLN THR ARG GLY GLU GLY TYR ALA          
SEQRES   4 B  336  LYS PRO ASN GLU GLY ALA ILE VAL GLU VAL ALA LEU GLU          
SEQRES   5 B  336  GLY TYR TYR LYS ASP LYS LEU PHE ASP GLN ARG GLU LEU          
SEQRES   6 B  336  ARG PHE GLU ILE GLY GLU GLY GLU ASN LEU ASP LEU PRO          
SEQRES   7 B  336  TYR GLY LEU GLU ARG ALA ILE GLN ARG MSE GLU LYS GLY          
SEQRES   8 B  336  GLU HIS SER ILE VAL TYR LEU LYS PRO SER TYR ALA PHE          
SEQRES   9 B  336  GLY SER VAL GLY LYS GLU LYS PHE GLN ILE PRO PRO ASN          
SEQRES  10 B  336  ALA GLU LEU LYS TYR GLU LEU HIS LEU LYS SER PHE GLU          
SEQRES  11 B  336  LYS ALA LYS GLU SER TRP GLU MSE ASN SER GLU GLU LYS          
SEQRES  12 B  336  LEU GLU GLN SER THR ILE VAL LYS GLU ARG GLY THR VAL          
SEQRES  13 B  336  TYR PHE LYS GLU GLY LYS TYR LYS GLN ALA LEU LEU GLN          
SEQRES  14 B  336  TYR LYS LYS ILE VAL SER TRP LEU GLU TYR GLU SER SER          
SEQRES  15 B  336  PHE SER ASN GLU GLU ALA GLN LYS ALA GLN ALA LEU ARG          
SEQRES  16 B  336  LEU ALA SER HIS LEU ASN LEU ALA MET CYS HIS LEU LYS          
SEQRES  17 B  336  LEU GLN ALA PHE SER ALA ALA ILE GLU SER CYS ASN LYS          
SEQRES  18 B  336  ALA LEU GLU LEU ASP SER ASN ASN GLU LYS GLY LEU SER          
SEQRES  19 B  336  ARG ARG GLY GLU ALA HIS LEU ALA VAL ASN ASP PHE GLU          
SEQRES  20 B  336  LEU ALA ARG ALA ASP PHE GLN LYS VAL LEU GLN LEU TYR          
SEQRES  21 B  336  PRO ASN ASN LYS ALA ALA LYS THR GLN LEU ALA VAL CYS          
SEQRES  22 B  336  GLN GLN ARG ILE ARG ARG GLN LEU ALA ARG GLU LYS LYS          
SEQRES  23 B  336  LEU TYR ALA ASN MET PHE GLU ARG LEU ALA GLU GLU GLU          
SEQRES  24 B  336  ASN LYS ALA LYS ALA GLU ALA SER SER GLY ASP HIS PRO          
SEQRES  25 B  336  THR ASP THR GLU MET LYS GLU GLU GLN LYS SER ASN THR          
SEQRES  26 B  336  ALA GLY SER GLN SER GLN VAL GLU THR GLU ALA                  
SEQRES   1 C  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  336  LEU VAL PRO ARG GLY SER HIS MET GLU GLU ASP GLY GLY          
SEQRES   3 C  336  ILE ILE ARG ARG ILE GLN THR ARG GLY GLU GLY TYR ALA          
SEQRES   4 C  336  LYS PRO ASN GLU GLY ALA ILE VAL GLU VAL ALA LEU GLU          
SEQRES   5 C  336  GLY TYR TYR LYS ASP LYS LEU PHE ASP GLN ARG GLU LEU          
SEQRES   6 C  336  ARG PHE GLU ILE GLY GLU GLY GLU ASN LEU ASP LEU PRO          
SEQRES   7 C  336  TYR GLY LEU GLU ARG ALA ILE GLN ARG MSE GLU LYS GLY          
SEQRES   8 C  336  GLU HIS SER ILE VAL TYR LEU LYS PRO SER TYR ALA PHE          
SEQRES   9 C  336  GLY SER VAL GLY LYS GLU LYS PHE GLN ILE PRO PRO ASN          
SEQRES  10 C  336  ALA GLU LEU LYS TYR GLU LEU HIS LEU LYS SER PHE GLU          
SEQRES  11 C  336  LYS ALA LYS GLU SER TRP GLU MSE ASN SER GLU GLU LYS          
SEQRES  12 C  336  LEU GLU GLN SER THR ILE VAL LYS GLU ARG GLY THR VAL          
SEQRES  13 C  336  TYR PHE LYS GLU GLY LYS TYR LYS GLN ALA LEU LEU GLN          
SEQRES  14 C  336  TYR LYS LYS ILE VAL SER TRP LEU GLU TYR GLU SER SER          
SEQRES  15 C  336  PHE SER ASN GLU GLU ALA GLN LYS ALA GLN ALA LEU ARG          
SEQRES  16 C  336  LEU ALA SER HIS LEU ASN LEU ALA MET CYS HIS LEU LYS          
SEQRES  17 C  336  LEU GLN ALA PHE SER ALA ALA ILE GLU SER CYS ASN LYS          
SEQRES  18 C  336  ALA LEU GLU LEU ASP SER ASN ASN GLU LYS GLY LEU SER          
SEQRES  19 C  336  ARG ARG GLY GLU ALA HIS LEU ALA VAL ASN ASP PHE GLU          
SEQRES  20 C  336  LEU ALA ARG ALA ASP PHE GLN LYS VAL LEU GLN LEU TYR          
SEQRES  21 C  336  PRO ASN ASN LYS ALA ALA LYS THR GLN LEU ALA VAL CYS          
SEQRES  22 C  336  GLN GLN ARG ILE ARG ARG GLN LEU ALA ARG GLU LYS LYS          
SEQRES  23 C  336  LEU TYR ALA ASN MET PHE GLU ARG LEU ALA GLU GLU GLU          
SEQRES  24 C  336  ASN LYS ALA LYS ALA GLU ALA SER SER GLY ASP HIS PRO          
SEQRES  25 C  336  THR ASP THR GLU MET LYS GLU GLU GLN LYS SER ASN THR          
SEQRES  26 C  336  ALA GLY SER GLN SER GLN VAL GLU THR GLU ALA                  
MODRES 1P5Q MSE A  211  MET  SELENOMETHIONINE                                   
MODRES 1P5Q MSE A  261  MET  SELENOMETHIONINE                                   
MODRES 1P5Q MSE B  211  MET  SELENOMETHIONINE                                   
MODRES 1P5Q MSE B  261  MET  SELENOMETHIONINE                                   
MODRES 1P5Q MSE C  211  MET  SELENOMETHIONINE                                   
MODRES 1P5Q MSE C  261  MET  SELENOMETHIONINE                                   
HET    MSE  A 211       8                                                       
HET    MSE  A 261       8                                                       
HET    MSE  B 211       8                                                       
HET    MSE  B 261       8                                                       
HET    MSE  C 211       8                                                       
HET    MSE  C 261       8                                                       
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    SO4  A1003       5                                                       
HET    SO4  A1004       5                                                       
HET    SO4  B1005       5                                                       
HET    SO4  B1006       5                                                       
HET    SO4  C1007       5                                                       
HET    SO4  C1008       5                                                       
HET    SO4  C1009       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   4  SO4    9(O4 S 2-)                                                   
FORMUL  13  HOH   *527(H2 O)                                                    
HELIX    1   1 GLU A  194  ASP A  199  5                                   6    
HELIX    2   2 PRO A  201  GLN A  209  1                                   9    
HELIX    3   3 LYS A  232  GLN A  236  5                                   5    
HELIX    4   4 GLU A  257  MSE A  261  5                                   5    
HELIX    5   5 ASN A  262  GLY A  284  1                                  23    
HELIX    6   6 LYS A  285  LEU A  300  1                                  16    
HELIX    7   7 ASN A  308  LEU A  332  1                                  25    
HELIX    8   8 ALA A  334  ASP A  349  1                                  16    
HELIX    9   9 ASN A  352  VAL A  366  1                                  15    
HELIX   10  10 ASP A  368  TYR A  383  1                                  16    
HELIX   11  11 ASN A  386  ALA A  425  1                                  40    
HELIX   12  12 GLU B  194  ASP B  199  5                                   6    
HELIX   13  13 PRO B  201  GLN B  209  1                                   9    
HELIX   14  14 PRO B  223  ALA B  226  5                                   4    
HELIX   15  15 ASN B  262  GLU B  283  1                                  22    
HELIX   16  16 LYS B  285  GLU B  301  1                                  17    
HELIX   17  17 ASN B  308  LEU B  332  1                                  25    
HELIX   18  18 ALA B  334  GLU B  347  1                                  14    
HELIX   19  19 ASN B  352  VAL B  366  1                                  15    
HELIX   20  20 ASP B  368  TYR B  383  1                                  16    
HELIX   21  21 ASN B  386  ALA B  425  1                                  40    
HELIX   22  22 GLU C  194  ASP C  199  5                                   6    
HELIX   23  23 PRO C  201  GLN C  209  1                                   9    
HELIX   24  24 PRO C  223  ALA C  226  5                                   4    
HELIX   25  25 LYS C  232  GLN C  236  5                                   5    
HELIX   26  26 ASN C  262  GLU C  283  1                                  22    
HELIX   27  27 LYS C  285  LEU C  300  1                                  16    
HELIX   28  28 ASN C  308  LEU C  332  1                                  25    
HELIX   29  29 ALA C  334  GLU C  347  1                                  14    
HELIX   30  30 ASN C  352  VAL C  366  1                                  15    
HELIX   31  31 ASP C  368  GLN C  381  1                                  14    
HELIX   32  32 ASN C  386  ALA C  425  1                                  40    
SHEET    1   A 5 ILE A 150  THR A 156  0                                        
SHEET    2   A 5 HIS A 216  LEU A 221 -1  O  TYR A 220   N  ILE A 151           
SHEET    3   A 5 LEU A 243  GLU A 253 -1  O  LEU A 243   N  LEU A 221           
SHEET    4   A 5 ILE A 169  TYR A 178 -1  N  TYR A 177   O  LYS A 244           
SHEET    5   A 5 LYS A 181  GLU A 191 -1  O  ASP A 184   N  GLY A 176           
SHEET    1   B 5 ILE B 150  THR B 156  0                                        
SHEET    2   B 5 HIS B 216  LEU B 221 -1  O  TYR B 220   N  ILE B 151           
SHEET    3   B 5 LEU B 243  GLU B 253 -1  O  TYR B 245   N  VAL B 219           
SHEET    4   B 5 ILE B 169  TYR B 178 -1  N  TYR B 177   O  LYS B 244           
SHEET    5   B 5 LYS B 181  GLU B 191 -1  O  ASP B 184   N  GLY B 176           
SHEET    1   C 5 ILE C 150  THR C 156  0                                        
SHEET    2   C 5 GLU C 215  LEU C 221 -1  O  ILE C 218   N  ARG C 153           
SHEET    3   C 5 LEU C 243  TYR C 245 -1  O  LEU C 243   N  LEU C 221           
SHEET    4   C 5 ILE C 169  TYR C 178 -1  N  TYR C 177   O  LYS C 244           
SHEET    5   C 5 LYS C 181  GLU C 191 -1  O  ARG C 186   N  LEU C 174           
SHEET    1   D 5 ILE C 150  THR C 156  0                                        
SHEET    2   D 5 GLU C 215  LEU C 221 -1  O  ILE C 218   N  ARG C 153           
SHEET    3   D 5 HIS C 248  SER C 251 -1  O  LEU C 249   N  GLU C 215           
SHEET    4   D 5 ILE C 169  TYR C 178 -1  N  GLU C 171   O  SER C 251           
SHEET    5   D 5 LYS C 181  GLU C 191 -1  O  ARG C 186   N  LEU C 174           
LINK         C   ARG A 210                 N   MSE A 211     1555   1555  1.33  
LINK         C   MSE A 211                 N   GLU A 212     1555   1555  1.33  
LINK         C   GLU A 260                 N   MSE A 261     1555   1555  1.33  
LINK         C   MSE A 261                 N   ASN A 262     1555   1555  1.33  
LINK         C   ARG B 210                 N   MSE B 211     1555   1555  1.33  
LINK         C   MSE B 211                 N   GLU B 212     1555   1555  1.34  
LINK         C   GLU B 260                 N   MSE B 261     1555   1555  1.33  
LINK         C   MSE B 261                 N   ASN B 262     1555   1555  1.33  
LINK         C   ARG C 210                 N   MSE C 211     1555   1555  1.32  
LINK         C   MSE C 211                 N   GLU C 212     1555   1555  1.34  
LINK         C   GLU C 260                 N   MSE C 261     1555   1555  1.33  
LINK         C   MSE C 261                 N   ASN C 262     1555   1555  1.33  
SITE     1 AC1  4 ARG A 152  ARG A 210  ASN C 367  ARG C 399                    
SITE     1 AC2  7 LYS A 232  GLU A 233  LYS A 234  HOH A1026                    
SITE     2 AC2  7 HOH A1055  HOH A1175  LYS B 179                               
SITE     1 AC3  3 TYR A 383  PRO A 384  ASN A 385                               
SITE     1 AC4  4 ASN A 367  ARG A 399  ARG B 152  ARG B 210                    
SITE     1 AC5  4 LYS B 232  GLU B 233  LYS B 234  LYS C 179                    
SITE     1 AC6  5 TYR B 383  PRO B 384  ASN B 385  HOH B1112                    
SITE     2 AC6  5 HOH B1175                                                     
SITE     1 AC7  4 LYS A 179  LYS C 232  GLU C 233  LYS C 234                    
SITE     1 AC8  5 ASP C 349  ASN C 351  ASN C 352  TYR C 383                    
SITE     2 AC8  5 HOH C1019                                                     
SITE     1 AC9  4 TYR C 383  PRO C 384  ASN C 385  HOH C1184                    
CRYST1  114.274  142.927  170.897  90.00  90.00  90.00 C 2 2 21     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      0.008751  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006997  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005851        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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