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Database: PDB
Entry: 4CGH
LinkDB: 4CGH
Original site: 4CGH 
HEADER    TRANSFERASE                             25-NOV-13   4CGH              
TITLE     INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL CHALLENGE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRASE;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 50-212;                         
COMPND   5 EC: 2.7.7.7;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET                                        
KEYWDS    TRANSFERASE, HIV INTEGRASE, STRUCTURE BASED DRUG DESIGN               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.S.PEAT                                                              
REVDAT   4   20-DEC-23 4CGH    1       JRNL   REMARK                            
REVDAT   3   25-JUN-14 4CGH    1       JRNL                                     
REVDAT   2   26-FEB-14 4CGH    1       JRNL                                     
REVDAT   1   04-DEC-13 4CGH    0                                                
JRNL        AUTH   T.S.PEAT,O.DOLEZAL,J.NEWMAN,D.MOBLEY,J.J.DEADMAN             
JRNL        TITL   INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL 
JRNL        TITL 2 CHALLENGE.                                                   
JRNL        REF    J.COMPUT.AIDED MOL.DES.       V.  28   347 2014              
JRNL        REFN                   ISSN 0920-654X                               
JRNL        PMID   24532034                                                     
JRNL        DOI    10.1007/S10822-014-9721-7                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35721                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1903                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.76                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2650                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 151                          
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2318                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 101                                     
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
REMARK   3    B12 (A**2) : -0.02000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.111         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.075         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2607 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2503 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3568 ; 1.310 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5790 ; 0.754 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   334 ; 5.159 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   110 ;31.646 ;25.455       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   454 ;14.764 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;10.695 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   401 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2997 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   587 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1245 ; 1.774 ; 3.882       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1242 ; 1.773 ; 3.878       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1563 ; 3.041 ; 6.507       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1362 ; 1.983 ; 4.291       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4CGH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290059069.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37651                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRY 3ZSQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN WAS CONCENTRATED TO 5.5      
REMARK 280  MG/ML IN 40 MM TRIS PH 8.0, 250 MM NACL, 30 MM MGCL2, 5 MM DTT      
REMARK 280  AND SET UP IN A 1:1 RATIO WITH 1.6 TO 2.0 M AMMONIUM SULFATE,       
REMARK 280  100 MM SODIUM ACETATE BUFFER PH 5.0 TO 5.5., PH 5.5                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       22.27000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.54000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.4 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     HIS A    37                                                      
REMARK 465     HIS A    38                                                      
REMARK 465     HIS A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     SER A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     LEU A    43                                                      
REMARK 465     VAL A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     ARG A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     SER A    48                                                      
REMARK 465     HIS A    49                                                      
REMARK 465     MET A    50                                                      
REMARK 465     HIS A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     GLN A    53                                                      
REMARK 465     VAL A    54                                                      
REMARK 465     ASP A    55                                                      
REMARK 465     SER A    56                                                      
REMARK 465     GLY A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     ILE A   191                                                      
REMARK 465     GLY A   192                                                      
REMARK 465     THR A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     MET B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     HIS B    35                                                      
REMARK 465     HIS B    36                                                      
REMARK 465     HIS B    37                                                      
REMARK 465     HIS B    38                                                      
REMARK 465     HIS B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     SER B    41                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     LEU B    43                                                      
REMARK 465     VAL B    44                                                      
REMARK 465     PRO B    45                                                      
REMARK 465     ARG B    46                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     SER B    48                                                      
REMARK 465     HIS B    49                                                      
REMARK 465     MET B    50                                                      
REMARK 465     HIS B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     GLN B    53                                                      
REMARK 465     VAL B    54                                                      
REMARK 465     ASP B    55                                                      
REMARK 465     SER B    56                                                      
REMARK 465     GLY B   189                                                      
REMARK 465     GLY B   190                                                      
REMARK 465     ILE B   191                                                      
REMARK 465     GLY B   192                                                      
REMARK 465     THR B   210                                                      
REMARK 465     LYS B   211                                                      
REMARK 465     GLU B   212                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    GLU A    92     O3   SO4 A  1213              2.13            
REMARK 500   OE1  GLU B    87     O    ACY A  1214              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LOZ B 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LOZ A 1216                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CGD   RELATED DB: PDB                                   
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL         
REMARK 900 CHALLENGE                                                            
REMARK 900 RELATED ID: 4CGF   RELATED DB: PDB                                   
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL         
REMARK 900 CHALLENGE                                                            
REMARK 900 RELATED ID: 4CGG   RELATED DB: PDB                                   
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL         
REMARK 900 CHALLENGE                                                            
REMARK 900 RELATED ID: 4CGI   RELATED DB: PDB                                   
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL         
REMARK 900 CHALLENGE                                                            
REMARK 900 RELATED ID: 4CGJ   RELATED DB: PDB                                   
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL         
REMARK 900 CHALLENGE                                                            
DBREF  4CGH A   50   212  UNP    Q76353   Q76353_9HIV1    50    212             
DBREF  4CGH B   50   212  UNP    Q76353   Q76353_9HIV1    50    212             
SEQADV 4CGH MET A   30  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH GLY A   31  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER A   32  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER A   33  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS A   34  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS A   35  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS A   36  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS A   37  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS A   38  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS A   39  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER A   40  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER A   41  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH GLY A   42  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH LEU A   43  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH VAL A   44  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH PRO A   45  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH ARG A   46  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH GLY A   47  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER A   48  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS A   49  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER A   56  UNP  Q76353    CYS    56 ENGINEERED MUTATION            
SEQADV 4CGH ASP A  139  UNP  Q76353    PHE   139 ENGINEERED MUTATION            
SEQADV 4CGH HIS A  185  UNP  Q76353    PHE   185 ENGINEERED MUTATION            
SEQADV 4CGH MET B   30  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH GLY B   31  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER B   32  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER B   33  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS B   34  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS B   35  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS B   36  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS B   37  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS B   38  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS B   39  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER B   40  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER B   41  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH GLY B   42  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH LEU B   43  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH VAL B   44  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH PRO B   45  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH ARG B   46  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH GLY B   47  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER B   48  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH HIS B   49  UNP  Q76353              EXPRESSION TAG                 
SEQADV 4CGH SER B   56  UNP  Q76353    CYS    56 ENGINEERED MUTATION            
SEQADV 4CGH ASP B  139  UNP  Q76353    PHE   139 ENGINEERED MUTATION            
SEQADV 4CGH HIS B  185  UNP  Q76353    PHE   185 ENGINEERED MUTATION            
SEQRES   1 A  183  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  183  LEU VAL PRO ARG GLY SER HIS MET HIS GLY GLN VAL ASP          
SEQRES   3 A  183  SER SER PRO GLY ILE TRP GLN LEU ASP CYS THR HIS LEU          
SEQRES   4 A  183  GLU GLY LYS VAL ILE LEU VAL ALA VAL HIS VAL ALA SER          
SEQRES   5 A  183  GLY TYR ILE GLU ALA GLU VAL ILE PRO ALA GLU THR GLY          
SEQRES   6 A  183  GLN GLU THR ALA TYR PHE LEU LEU LYS LEU ALA GLY ARG          
SEQRES   7 A  183  TRP PRO VAL LYS THR VAL HIS THR ASP ASN GLY SER ASN          
SEQRES   8 A  183  PHE THR SER THR THR VAL LYS ALA ALA CYS TRP TRP ALA          
SEQRES   9 A  183  GLY ILE LYS GLN GLU ASP GLY ILE PRO TYR ASN PRO GLN          
SEQRES  10 A  183  SER GLN GLY VAL ILE GLU SER MET ASN LYS GLU LEU LYS          
SEQRES  11 A  183  LYS ILE ILE GLY GLN VAL ARG ASP GLN ALA GLU HIS LEU          
SEQRES  12 A  183  LYS THR ALA VAL GLN MET ALA VAL PHE ILE HIS ASN HIS          
SEQRES  13 A  183  LYS ARG LYS GLY GLY ILE GLY GLY TYR SER ALA GLY GLU          
SEQRES  14 A  183  ARG ILE VAL ASP ILE ILE ALA THR ASP ILE GLN THR LYS          
SEQRES  15 A  183  GLU                                                          
SEQRES   1 B  183  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  183  LEU VAL PRO ARG GLY SER HIS MET HIS GLY GLN VAL ASP          
SEQRES   3 B  183  SER SER PRO GLY ILE TRP GLN LEU ASP CYS THR HIS LEU          
SEQRES   4 B  183  GLU GLY LYS VAL ILE LEU VAL ALA VAL HIS VAL ALA SER          
SEQRES   5 B  183  GLY TYR ILE GLU ALA GLU VAL ILE PRO ALA GLU THR GLY          
SEQRES   6 B  183  GLN GLU THR ALA TYR PHE LEU LEU LYS LEU ALA GLY ARG          
SEQRES   7 B  183  TRP PRO VAL LYS THR VAL HIS THR ASP ASN GLY SER ASN          
SEQRES   8 B  183  PHE THR SER THR THR VAL LYS ALA ALA CYS TRP TRP ALA          
SEQRES   9 B  183  GLY ILE LYS GLN GLU ASP GLY ILE PRO TYR ASN PRO GLN          
SEQRES  10 B  183  SER GLN GLY VAL ILE GLU SER MET ASN LYS GLU LEU LYS          
SEQRES  11 B  183  LYS ILE ILE GLY GLN VAL ARG ASP GLN ALA GLU HIS LEU          
SEQRES  12 B  183  LYS THR ALA VAL GLN MET ALA VAL PHE ILE HIS ASN HIS          
SEQRES  13 B  183  LYS ARG LYS GLY GLY ILE GLY GLY TYR SER ALA GLY GLU          
SEQRES  14 B  183  ARG ILE VAL ASP ILE ILE ALA THR ASP ILE GLN THR LYS          
SEQRES  15 B  183  GLU                                                          
HET    SO4  A1210       5                                                       
HET    SO4  A1211       5                                                       
HET    SO4  A1212       5                                                       
HET    SO4  A1213       5                                                       
HET    ACY  A1214       4                                                       
HET    ACY  A1215       4                                                       
HET    LOZ  A1216      29                                                       
HET    SO4  B1210       5                                                       
HET    SO4  B1211       5                                                       
HET    SO4  B1212       5                                                       
HET    LOZ  B1213      29                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACY ACETIC ACID                                                      
HETNAM     LOZ 5-[[(1S,2R)-2-(4-AZANYLBUTANOYLAMINO)-2,3-DIHYDRO-1H-            
HETNAM   2 LOZ  INDEN-1-YL]METHYL]-1,3-BENZODIOXOLE-4-CARBOXYLIC ACID           
FORMUL   3  SO4    7(O4 S 2-)                                                   
FORMUL   7  ACY    2(C2 H4 O2)                                                  
FORMUL   9  LOZ    2(C22 H24 N2 O5)                                             
FORMUL  14  HOH   *121(H2 O)                                                    
HELIX    1   1 THR A   93  TRP A  108  1                                  16    
HELIX    2   2 ASN A  117  SER A  123  1                                   7    
HELIX    3   3 SER A  123  GLY A  134  1                                  12    
HELIX    4   4 PRO A  145  ARG A  166  1                                  22    
HELIX    5   5 ASP A  167  ALA A  169  5                                   3    
HELIX    6   6 HIS A  171  LYS A  186  1                                  16    
HELIX    7   7 SER A  195  GLN A  209  1                                  15    
HELIX    8   8 THR B   93  TRP B  108  1                                  16    
HELIX    9   9 ASN B  117  SER B  123  1                                   7    
HELIX   10  10 SER B  123  GLY B  134  1                                  12    
HELIX   11  11 PRO B  145  ARG B  166  1                                  22    
HELIX   12  12 ASP B  167  ALA B  169  5                                   3    
HELIX   13  13 HIS B  171  LYS B  186  1                                  16    
HELIX   14  14 SER B  195  GLN B  209  1                                  15    
SHEET    1  AA 5 ILE A  84  ILE A  89  0                                        
SHEET    2  AA 5 LYS A  71  HIS A  78 -1  O  VAL A  72   N  ILE A  89           
SHEET    3  AA 5 ILE A  60  LEU A  68 -1  O  GLN A  62   N  VAL A  77           
SHEET    4  AA 5 THR A 112  HIS A 114  1  O  THR A 112   N  TRP A  61           
SHEET    5  AA 5 LYS A 136  GLU A 138  1  O  LYS A 136   N  VAL A 113           
SHEET    1  BA 5 ILE B  84  ILE B  89  0                                        
SHEET    2  BA 5 LYS B  71  HIS B  78 -1  O  VAL B  72   N  ILE B  89           
SHEET    3  BA 5 ILE B  60  LEU B  68 -1  O  GLN B  62   N  VAL B  77           
SHEET    4  BA 5 THR B 112  HIS B 114  1  O  THR B 112   N  TRP B  61           
SHEET    5  BA 5 LYS B 136  GLU B 138  1  O  LYS B 136   N  VAL B 113           
SITE     1 AC1  6 THR B  66  HIS B  67  LYS B 111  LYS B 136                    
SITE     2 AC1  6 LYS B 159  HOH B2038                                          
SITE     1 AC2  5 THR A  66  HIS A  67  LYS A 111  LYS A 159                    
SITE     2 AC2  5 HOH A2044                                                     
SITE     1 AC3  5 LYS B  71  ARG B 166  HIS B 171  LEU B 172                    
SITE     2 AC3  5 HOH B2045                                                     
SITE     1 AC4  5 LYS A  71  ARG A 166  HIS A 171  LEU A 172                    
SITE     2 AC4  5 HOH A2051                                                     
SITE     1 AC5  6 GLY B  94  SER B 123  THR B 124  THR B 125                    
SITE     2 AC5  6 HOH B2017  HOH B2031                                          
SITE     1 AC6  7 GLY A  94  GLN A  95  SER A 123  THR A 124                    
SITE     2 AC6  7 THR A 125  HOH A2020  HOH A2037                               
SITE     1 AC7  5 HIS A  67  VAL A  72  ALA A  91  GLU A  92                    
SITE     2 AC7  5 ARG B 187                                                     
SITE     1 AC8  6 TYR A  99  LYS A 103  ACY A1215  HOH A2025                    
SITE     2 AC8  6 HOH A2065  HOH B2046                                          
SITE     1 AC9  6 ACY A1214  HOH A2012  HOH A2013  HOH A2052                    
SITE     2 AC9  6 TYR B  99  LYS B 103                                          
SITE     1 BC1 12 GLN A  95  TYR A  99  LEU A 102  THR A 125                    
SITE     2 BC1 12 ALA A 129  TRP A 132  HOH A2021  GLN B 168                    
SITE     3 BC1 12 GLU B 170  HIS B 171  THR B 174  MET B 178                    
SITE     1 BC2 10 GLN A 168  GLU A 170  HIS A 171  THR A 174                    
SITE     2 BC2 10 MET A 178  GLN B  95  TYR B  99  THR B 125                    
SITE     3 BC2 10 ALA B 129  TRP B 132                                          
CRYST1   71.500   71.500   66.810  90.00  90.00 120.00 P 31          6          
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      0.013986  0.008075  0.000000        0.00000                         
SCALE2      0.000000  0.016150  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014968        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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