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Database: PDB
Entry: 2PIU
LinkDB: 2PIU
Original site: 2PIU 
HEADER    HORMONE RECEPTOR                        13-APR-07   2PIU              
TITLE     ANDROGEN RECEPTOR LBD WITH SMALL MOLECULE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANDROGEN RECEPTOR;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LIGAND-BINDING DOMAIN (RESIDUES 669-919);                  
COMPND   5 SYNONYM: DIHYDROTESTOSTERONE RECEPTOR;                               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AR, DHTR, NR3C4;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ANDROGEN RECEPTOR INHIBITORS COACTIVATOR BINDING AF-2, HORMONE        
KEYWDS   2 RECEPTOR                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ESTEBANEZ-PERPINA,A.A.ARNOLD,J.D.BAXTER,P.WEBB,R.K.GUY,             
AUTHOR   2 K.R.FLETTERICK                                                       
REVDAT   5   18-OCT-17 2PIU    1       REMARK                                   
REVDAT   4   07-APR-09 2PIU    1       REMARK                                   
REVDAT   3   24-FEB-09 2PIU    1       VERSN                                    
REVDAT   2   27-MAY-08 2PIU    1       JRNL                                     
REVDAT   1   25-SEP-07 2PIU    0                                                
JRNL        AUTH   E.ESTEBANEZ-PERPINA,L.A.ARNOLD,A.A.ARNOLD,P.NGUYEN,          
JRNL        AUTH 2 E.D.RODRIGUES,E.MAR,R.BATEMAN,P.PALLAI,K.M.SHOKAT,           
JRNL        AUTH 3 J.D.BAXTER,R.K.GUY,P.WEBB,R.J.FLETTERICK                     
JRNL        TITL   A SURFACE ON THE ANDROGEN RECEPTOR THAT ALLOSTERICALLY       
JRNL        TITL 2 REGULATES COACTIVATOR BINDING.                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 104 16074 2007              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17911242                                                     
JRNL        DOI    10.1073/PNAS.0708036104                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
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             : 15599                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 2028                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 160                                     
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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 2PIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042421.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ELVES                              
REMARK 200  DATA SCALING SOFTWARE          : ELVES                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15599                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10600                            
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) : 2.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 298K                                                    
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       28.09000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.37500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.03500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.37500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.09000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.03500            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     CYS A   669                                                      
REMARK 465     GLN A   670                                                      
REMARK 465     GLN A   919                                                      
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 726       -9.89    -59.34                                   
REMARK 500    ASP A 819       31.65    -87.90                                   
REMARK 500    CYS A 844       59.85    -97.10                                   
REMARK 500    LYS A 845      -57.13    176.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHT A 931                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4HY A 932                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4HY A 933                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PIN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PIX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PKL   RELATED DB: PDB                                   
DBREF  2PIU A  669   919  UNP    P10275   ANDR_HUMAN     669    919             
SEQRES   1 A  251  CYS GLN PRO ILE PHE LEU ASN VAL LEU GLU ALA ILE GLU          
SEQRES   2 A  251  PRO GLY VAL VAL CYS ALA GLY HIS ASP ASN ASN GLN PRO          
SEQRES   3 A  251  ASP SER PHE ALA ALA LEU LEU SER SER LEU ASN GLU LEU          
SEQRES   4 A  251  GLY GLU ARG GLN LEU VAL HIS VAL VAL LYS TRP ALA LYS          
SEQRES   5 A  251  ALA LEU PRO GLY PHE ARG ASN LEU HIS VAL ASP ASP GLN          
SEQRES   6 A  251  MET ALA VAL ILE GLN TYR SER TRP MET GLY LEU MET VAL          
SEQRES   7 A  251  PHE ALA MET GLY TRP ARG SER PHE THR ASN VAL ASN SER          
SEQRES   8 A  251  ARG MET LEU TYR PHE ALA PRO ASP LEU VAL PHE ASN GLU          
SEQRES   9 A  251  TYR ARG MET HIS LYS SER ARG MET TYR SER GLN CYS VAL          
SEQRES  10 A  251  ARG MET ARG HIS LEU SER GLN GLU PHE GLY TRP LEU GLN          
SEQRES  11 A  251  ILE THR PRO GLN GLU PHE LEU CYS MET LYS ALA LEU LEU          
SEQRES  12 A  251  LEU PHE SER ILE ILE PRO VAL ASP GLY LEU LYS ASN GLN          
SEQRES  13 A  251  LYS PHE PHE ASP GLU LEU ARG MET ASN TYR ILE LYS GLU          
SEQRES  14 A  251  LEU ASP ARG ILE ILE ALA CYS LYS ARG LYS ASN PRO THR          
SEQRES  15 A  251  SER CYS SER ARG ARG PHE TYR GLN LEU THR LYS LEU LEU          
SEQRES  16 A  251  ASP SER VAL GLN PRO ILE ALA ARG GLU LEU HIS GLN PHE          
SEQRES  17 A  251  THR PHE ASP LEU LEU ILE LYS SER HIS MET VAL SER VAL          
SEQRES  18 A  251  ASP PHE PRO GLU MET MET ALA GLU ILE ILE SER VAL GLN          
SEQRES  19 A  251  VAL PRO LYS ILE LEU SER GLY LYS VAL LYS PRO ILE TYR          
SEQRES  20 A  251  PHE HIS THR GLN                                              
HET    DHT  A 931      21                                                       
HET    4HY  A 932      21                                                       
HET    4HY  A 933      21                                                       
HETNAM     DHT 5-ALPHA-DIHYDROTESTOSTERONE                                      
HETNAM     4HY [4-(4-HYDROXY-3-IODO-PHENOXY)-3,5-DIIODO-PHENYL]-ACETIC          
HETNAM   2 4HY  ACID                                                            
FORMUL   2  DHT    C19 H30 O2                                                   
FORMUL   3  4HY    2(C14 H9 I3 O4)                                              
FORMUL   5  HOH   *160(H2 O)                                                    
HELIX    1   1 PRO A  671  GLU A  681  1                                  11    
HELIX    2   2 SER A  696  LYS A  720  1                                  25    
HELIX    3   3 GLY A  724  LEU A  728  5                                   5    
HELIX    4   4 HIS A  729  ASN A  758  1                                  30    
HELIX    5   5 ASN A  771  SER A  778  1                                   8    
HELIX    6   6 MET A  780  LEU A  797  1                                  18    
HELIX    7   7 THR A  800  LEU A  812  1                                  13    
HELIX    8   8 ASN A  823  CYS A  844  1                                  22    
HELIX    9   9 ASN A  848  LYS A  883  1                                  36    
HELIX   10  10 PRO A  892  GLN A  902  1                                  11    
HELIX   11  11 GLN A  902  SER A  908  1                                   7    
SHEET    1   A 2 LEU A 762  ALA A 765  0                                        
SHEET    2   A 2 LEU A 768  PHE A 770 -1  O  PHE A 770   N  LEU A 762           
SHEET    1   B 2 ILE A 815  PRO A 817  0                                        
SHEET    2   B 2 VAL A 911  PRO A 913 -1  O  LYS A 912   N  ILE A 816           
SITE     1 AC1  7 LEU A 704  ASN A 705  GLN A 711  MET A 749                    
SITE     2 AC1  7 ARG A 752  PHE A 764  THR A 877                               
SITE     1 AC2  8 LYS A 717  LYS A 720  MET A 734  ILE A 737                    
SITE     2 AC2  8 MET A 894  ILE A 898  HOH A1079  HOH A1085                    
SITE     1 AC3 10 GLY A 724  PHE A 826  ASN A 833  TYR A 834                    
SITE     2 AC3 10 GLU A 837  ASP A 879  ILE A 882  HOH A1046                    
SITE     3 AC3 10 HOH A1084  HOH A1086                                          
CRYST1   56.180   66.070   72.750  90.00  90.00  90.00 P 21 21 21    4          
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      0.017800  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015135  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013746        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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