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Database: PDB
Entry: 5LR1
LinkDB: 5LR1
Original site: 5LR1 
HEADER    CHAPERONE PROTEIN                       18-AUG-16   5LR1              
TITLE     CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH A003498614A.               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HEAT SHOCK 86 KDA,HSP86,LIPOPOLYSACCHARIDE-ASSOCIATED       
COMPND   5 PROTEIN 2,LPS-ASSOCIATED PROTEIN 2,RENAL CARCINOMA ANTIGEN NY-REN-38;
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: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PQE30                                 
KEYWDS    CHAPERONE PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VALLEE,A.DUPUY                                                      
REVDAT   2   12-JUN-19 5LR1    1       AUTHOR JRNL                              
REVDAT   1   23-AUG-17 5LR1    0                                                
JRNL        AUTH   F.VALLEE,A.DUPUY                                             
JRNL        TITL   CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH A003498614A.      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 53714                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.200                          
REMARK   3   R VALUE            (WORKING SET)  : 0.199                          
REMARK   3   FREE R VALUE                      : 0.220                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.940                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2653                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.44                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.48                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.97                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3841                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2190                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3647                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2180                   
REMARK   3   BIN FREE R VALUE                        : 0.2370                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.05                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 194                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1638                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 287                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.06190                                              
REMARK   3    B22 (A**2) : -2.57820                                             
REMARK   3    B33 (A**2) : 1.51630                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.190               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.064               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.064               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.059               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.060               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 1697   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 2292   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 607    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 46     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 265    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 1697   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 231    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2152   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.71                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.24                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5LR1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001197.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53831                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2YJX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 TO 1.4 M SODIUM CITRATE, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.27000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.34000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.11500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.27000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.34000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.11500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.27000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.34000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.11500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.27000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.34000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.11500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 10480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 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    ASN A 105      -52.77   -121.51                                   
REMARK 500    ARG A 182      139.60   -170.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  167     GLY A  168                 -148.32                    
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 72Y A 4000                
DBREF  5LR1 A   18   223  UNP    P07900   HS90A_HUMAN     18    223             
SEQADV 5LR1 HIS A   16  UNP  P07900              EXPRESSION TAG                 
SEQADV 5LR1 MET A   17  UNP  P07900              EXPRESSION TAG                 
SEQRES   1 A  208  HIS MET GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN          
SEQRES   2 A  208  LEU MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS          
SEQRES   3 A  208  GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER SER ASP          
SEQRES   4 A  208  ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO          
SEQRES   5 A  208  SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE ASN LEU          
SEQRES   6 A  208  ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE VAL ASP          
SEQRES   7 A  208  THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN          
SEQRES   8 A  208  LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET          
SEQRES   9 A  208  GLU ALA LEU GLN ALA GLY ALA ASP ILE SER MET ILE GLY          
SEQRES  10 A  208  GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA          
SEQRES  11 A  208  GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP ASP GLU          
SEQRES  12 A  208  GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR          
SEQRES  13 A  208  VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG GLY THR          
SEQRES  14 A  208  LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR          
SEQRES  15 A  208  LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS LYS HIS          
SEQRES  16 A  208  SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE VAL GLU          
HET    72Y  A4000      21                                                       
HETNAM     72Y 4-CHLORANYL-7-[(4-CHLORANYL-3,5-DIMETHYL-PYRIDIN-2-YL)           
HETNAM   2 72Y  METHYL]PYRROLO[2,3-D]PYRIMIDIN-2-AMINE                          
FORMUL   2  72Y    C14 H13 CL2 N5                                               
FORMUL   3  HOH   *287(H2 O)                                                    
HELIX    1 AA1 GLN A   23  THR A   36  1                                  14    
HELIX    2 AA2 GLU A   42  ASP A   66  1                                  25    
HELIX    3 AA3 PRO A   67  ASP A   71  5                                   5    
HELIX    4 AA4 THR A   99  ASN A  105  1                                   7    
HELIX    5 AA5 ASN A  105  ALA A  124  1                                  20    
HELIX    6 AA6 ASP A  127  GLY A  135  5                                   9    
HELIX    7 AA7 VAL A  136  LEU A  143  5                                   8    
HELIX    8 AA8 GLU A  192  LEU A  198  5                                   7    
HELIX    9 AA9 GLU A  199  SER A  211  1                                  13    
SHEET    1 AA1 8 GLU A  18  ALA A  21  0                                        
SHEET    2 AA1 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3 AA1 8 TYR A 160  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4 AA1 8 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5 AA1 8 GLY A 183  LEU A 190 -1  O  ILE A 187   N  THR A 149           
SHEET    6 AA1 8 THR A  88  ASP A  93 -1  N  LEU A  89   O  LEU A 188           
SHEET    7 AA1 8 ILE A  78  ASN A  83 -1  N  ILE A  81   O  THR A  90           
SHEET    8 AA1 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
SITE     1 AC1 14 ASN A  51  ALA A  55  ASP A  93  ILE A  96                    
SITE     2 AC1 14 GLY A  97  MET A  98  LEU A 107  PHE A 138                    
SITE     3 AC1 14 TYR A 139  TRP A 162  THR A 184  HOH A4179                    
SITE     4 AC1 14 HOH A4196  HOH A4281                                          
CRYST1   66.540   90.680   98.230  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015029  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011028  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010180        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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