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Database: PDB
Entry: 5TYS
LinkDB: 5TYS
Original site: 5TYS 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           21-NOV-16   5TYS              
TITLE     X-RAY CRYSTAL STRUCTURE OF WILD TYPE HIV-1 PROTEASE IN COMPLEX WITH   
TITLE    2 GRL-142                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASE;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: 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: 562                                         
KEYWDS    GRL-142, HIV-1 PROTEASE, PROTEASE-INHIBITOR, DARUNAVIR, PYRAN, FURAN, 
KEYWDS   2 NONPEPTIDIC, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.S.YEDIDI,H.HAYASHI,M.AOKI,D.DAS,A.K.GHOSH,H.MITSUYA                 
REVDAT   4   04-OCT-23 5TYS    1       REMARK                                   
REVDAT   3   04-DEC-19 5TYS    1       REMARK                                   
REVDAT   2   01-NOV-17 5TYS    1       JRNL                                     
REVDAT   1   18-OCT-17 5TYS    0                                                
JRNL        AUTH   M.AOKI,H.HAYASHI,K.V.RAO,D.DAS,N.HIGASHI-KUWATA,H.BULUT,     
JRNL        AUTH 2 H.AOKI-OGATA,Y.TAKAMATSU,R.S.YEDIDI,D.A.DAVIS,S.I.HATTORI,   
JRNL        AUTH 3 N.NISHIDA,K.HASEGAWA,N.TAKAMUNE,P.R.NYALAPATLA,H.L.OSSWALD,  
JRNL        AUTH 4 H.JONO,H.SAITO,R.YARCHOAN,S.MISUMI,A.K.GHOSH,H.MITSUYA       
JRNL        TITL   A NOVEL CENTRAL NERVOUS SYSTEM-PENETRATING PROTEASE          
JRNL        TITL 2 INHIBITOR OVERCOMES HUMAN IMMUNODEFICIENCY VIRUS 1           
JRNL        TITL 3 RESISTANCE WITH UNPRECEDENTED AM TO PM POTENCY.              
JRNL        REF    ELIFE                         V.   6       2017              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   29039736                                                     
JRNL        DOI    10.7554/ELIFE.28020                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.710                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 12421                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 598                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  0.0000 -  3.1855    1.00     2989   151  0.1805 0.2147        
REMARK   3     2  3.1855 -  2.5287    1.00     2947   146  0.2124 0.2498        
REMARK   3     3  2.5287 -  2.2092    1.00     2978   140  0.2114 0.2663        
REMARK   3     4  2.2092 -  2.0072    0.99     2909   161  0.1992 0.2632        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.880           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           1650                                  
REMARK   3   ANGLE     :  1.022           2252                                  
REMARK   3   CHIRALITY :  0.065            266                                  
REMARK   3   PLANARITY :  0.005            268                                  
REMARK   3   DIHEDRAL  : 10.557            950                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000225026.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12475                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.20                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 4HLA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM/POTASSIUM PHOSPHATE (PH     
REMARK 280  6.2), 20% (W/V) POLYETHYLENE GLYCOL 1000, 0.2 M SODIUM CHLORIDE,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
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       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       27.40967            
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       54.81933            
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       41.11450            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       68.52417            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       13.70483            
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: 4020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 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   O    HOH A   516     O    HOH B   144              1.92            
REMARK 500   O    HOH B   112     O    HOH B   137              1.94            
REMARK 500   O    HOH B   122     O    HOH B   144              1.97            
REMARK 500   O    HOH B   142     O    HOH B   145              2.01            
REMARK 500   O    HOH B   125     O    HOH B   147              2.11            
REMARK 500   O    HOH A   516     O    HOH A   534              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   541     O    HOH B   114     6555     1.85            
REMARK 500   O    HOH A   515     O    HOH B   141     6555     2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  87   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B  87   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  61       57.42     39.12                                   
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 7OA A 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HLA   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH DARUNAVIR                               
REMARK 900 RELATED ID: 5TYR   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH GRL121                                  
DBREF  5TYS A    1    99  UNP    C8B467   C8B467_9HIV1     1     99             
DBREF  5TYS B    1    99  UNP    C8B467   C8B467_9HIV1     1     99             
SEQRES   1 A   99  PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE          
SEQRES   2 A   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 A   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO          
SEQRES   4 A   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 A   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU          
SEQRES   6 A   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 A   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 A   99  GLN ILE GLY CYS THR LEU ASN PHE                              
SEQRES   1 B   99  PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE          
SEQRES   2 B   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 B   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO          
SEQRES   4 B   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 B   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU          
SEQRES   6 B   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 B   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 B   99  GLN ILE GLY CYS THR LEU ASN PHE                              
HET    7OA  A 400      96                                                       
HETNAM     7OA (3S,3AR,5R,7AS,8S)-HEXAHYDRO-4H-3,5-METHANOFURO[2,3-             
HETNAM   2 7OA  B]PYRAN-8-YL [(2S,3R)-4-[{[2-(CYCLOPROPYLAMINO)-1,3-            
HETNAM   3 7OA  BENZOTHIAZOL-6-YL]SULFONYL}(2-METHYLPROPYL)AMINO]-1-            
HETNAM   4 7OA  (3,5-DIFLUOROPHENYL)-3-HYDROXYBUTAN-2-YL]CARBAMATE              
FORMUL   3  7OA    C33 H40 F2 N4 O7 S2                                          
FORMUL   4  HOH   *90(H2 O)                                                     
HELIX    1 AA1 GLY A   86  THR A   91  1                                   6    
HELIX    2 AA2 GLN A   92  GLY A   94  5                                   3    
HELIX    3 AA3 GLY B   86  THR B   91  1                                   6    
SHEET    1 AA1 4 GLN A   2  THR A   4  0                                        
SHEET    2 AA1 4 THR B  96  ASN B  98 -1  O  LEU B  97   N  ILE A   3           
SHEET    3 AA1 4 THR A  96  ASN A  98 -1  N  THR A  96   O  ASN B  98           
SHEET    4 AA1 4 GLN B   2  ILE B   3 -1  O  ILE B   3   N  LEU A  97           
SHEET    1 AA2 8 LYS A  43  GLY A  49  0                                        
SHEET    2 AA2 8 GLY A  52  ILE A  66 -1  O  GLY A  52   N  GLY A  49           
SHEET    3 AA2 8 HIS A  69  VAL A  77 -1  O  HIS A  69   N  ILE A  66           
SHEET    4 AA2 8 THR A  31  LEU A  33  1  N  LEU A  33   O  LEU A  76           
SHEET    5 AA2 8 ILE A  84  ILE A  85 -1  O  ILE A  84   N  VAL A  32           
SHEET    6 AA2 8 GLN A  18  LEU A  24  1  N  LEU A  23   O  ILE A  85           
SHEET    7 AA2 8 LEU A  10  ILE A  15 -1  N  ILE A  13   O  LYS A  20           
SHEET    8 AA2 8 GLY A  52  ILE A  66 -1  O  GLU A  65   N  LYS A  14           
SHEET    1 AA3 8 LYS B  43  GLY B  49  0                                        
SHEET    2 AA3 8 GLY B  52  ILE B  66 -1  O  VAL B  56   N  LYS B  45           
SHEET    3 AA3 8 HIS B  69  VAL B  77 -1  O  HIS B  69   N  ILE B  66           
SHEET    4 AA3 8 THR B  31  LEU B  33  1  N  LEU B  33   O  LEU B  76           
SHEET    5 AA3 8 ILE B  84  ILE B  85 -1  O  ILE B  84   N  VAL B  32           
SHEET    6 AA3 8 GLN B  18  LEU B  24  1  N  LEU B  23   O  ILE B  85           
SHEET    7 AA3 8 LEU B  10  ILE B  15 -1  N  ILE B  13   O  LYS B  20           
SHEET    8 AA3 8 GLY B  52  ILE B  66 -1  O  GLU B  65   N  LYS B  14           
SITE     1 AC1 26 ARG A   8  ASP A  25  GLY A  27  ALA A  28                    
SITE     2 AC1 26 ASP A  29  ASP A  30  ILE A  47  GLY A  48                    
SITE     3 AC1 26 GLY A  49  ILE A  50  PRO A  81  VAL A  82                    
SITE     4 AC1 26 ILE A  84  HOH A 503  ARG B   8  ASP B  25                    
SITE     5 AC1 26 GLY B  27  ALA B  28  ASP B  29  ASP B  30                    
SITE     6 AC1 26 GLY B  48  GLY B  49  ILE B  50  PRO B  81                    
SITE     7 AC1 26 VAL B  82  ILE B  84                                          
CRYST1   63.131   63.131   82.229  90.00  90.00 120.00 P 61         12          
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      0.015840  0.009145  0.000000        0.00000                         
SCALE2      0.000000  0.018291  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012161        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system