GenomeNet

Database: PDB
Entry: 2G1Y
LinkDB: 2G1Y
Original site: 2G1Y 
HEADER    HYDROLASE                               15-FEB-06   2G1Y              
TITLE     KETOPIPERAZINE-BASED RENIN INHIBITORS: OPTIMIZATION OF THE "C" RING   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RENIN;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ANGIOTENSINOGENASE;                                         
COMPND   5 EC: 3.4.23.15;                                                       
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: REN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN-LIGAND COMPLEXES, HYDROLASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.D.HOLSWORTH,M.JALAIEA,E.ZHANGA,P.MCCONNELLA                         
REVDAT   4   29-JUL-20 2G1Y    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   13-JUL-11 2G1Y    1       VERSN                                    
REVDAT   2   24-FEB-09 2G1Y    1       VERSN                                    
REVDAT   1   13-JUN-06 2G1Y    0                                                
JRNL        AUTH   D.D.HOLSWORTH,C.CAI,X.M.CHENG,W.L.CODY,D.M.DOWNING,N.ERASGA, 
JRNL        AUTH 2 C.LEE,N.A.POWELL,J.J.EDNUNDS,M.STIER,M.JALAIE,E.ZHANG,       
JRNL        AUTH 3 P.MCCONNELL,M.J.RYAN,J.BRYANT,T.LI,A.KASANI,E.HALL,R.SUBEDI, 
JRNL        AUTH 4 M.RAHIM,S.MAITI                                              
JRNL        TITL   KETOPIPERAZINE-BASED RENIN INHIBITORS: OPTIMIZATION OF THE   
JRNL        TITL 2 "C" RING                                                     
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  2500 2006              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   16480874                                                     
JRNL        DOI    10.1016/J.BMCL.2006.01.084                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 32307                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3231                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5144                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 322                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2G1Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000036586.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32307                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 1.0                                
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 1.0                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+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       70.51900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.51900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.51900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.51900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.51900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.51900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       70.51900            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       70.51900            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       70.51900            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       70.51900            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       70.51900            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       70.51900            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       70.51900            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       70.51900            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       70.51900            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       70.51900            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       70.51900            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       70.51900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22730 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 350   BIOMT1   2  0.000000  0.000000 -1.000000      141.03800            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       70.51900            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000      211.55700            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -70.51900            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000      211.55700            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000      141.03800            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2  0.000000  0.000000 -1.000000      141.03800            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       70.51900            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000      211.55700            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -70.51900            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000      211.55700            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000      141.03800            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 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 350   BIOMT1   2  0.000000  0.000000 -1.000000      141.03800            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       70.51900            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000      211.55700            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000      -70.51900            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000      211.55700            
REMARK 350   BIOMT3   3 -1.000000  0.000000  0.000000      141.03800            
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  70      -54.08   -156.23                                   
REMARK 500    ASP A 160      161.76    -47.08                                   
REMARK 500    SER A 164      105.97    -49.65                                   
REMARK 500    GLN A 165      -16.39    179.59                                   
REMARK 500    SER A 208      106.84    166.35                                   
REMARK 500    THR A 209       80.23    -67.41                                   
REMARK 500    CYS A 212       46.89     37.94                                   
REMARK 500    ASP A 214       -4.40     61.64                                   
REMARK 500    TYR A 226     -165.53   -127.38                                   
REMARK 500    SER A 230      153.72    -46.91                                   
REMARK 500    ARG A 246     -161.36   -101.65                                   
REMARK 500    GLN A 282       85.92    -66.56                                   
REMARK 500    ALA A 294       24.36    -79.69                                   
REMARK 500    ASP B  12       -1.05     66.91                                   
REMARK 500    TYR B  50       96.59    -65.78                                   
REMARK 500    SER B  62        5.69    -69.80                                   
REMARK 500    HIS B  69      152.26    -49.86                                   
REMARK 500    ASN B  70       71.40    174.90                                   
REMARK 500    THR B  80      -84.76   -103.74                                   
REMARK 500    SER B 207       12.36   -141.21                                   
REMARK 500    THR B 209       77.68    -68.61                                   
REMARK 500    ARG B 246      -87.33    -60.62                                   
REMARK 500    LEU B 247      -49.25   -133.72                                   
REMARK 500    ALA B 294       32.40    -96.62                                   
REMARK 500    MET B 298       99.84   -163.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2G1N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G1R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G1O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G1S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G20   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G21   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G22   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G24   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G26   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G27   RELATED DB: PDB                                   
DBREF  2G1Y A    3   335  UNP    P00797   RENI_HUMAN      74    406             
DBREF  2G1Y B    3   335  UNP    P00797   RENI_HUMAN      74    406             
SEQRES   1 A  333  SER SER VAL ILE LEU THR ASN TYR MET ASP THR GLN TYR          
SEQRES   2 A  333  TYR GLY GLU ILE GLY ILE GLY THR PRO PRO GLN THR PHE          
SEQRES   3 A  333  LYS VAL VAL PHE ASP THR GLY SER SER ASN VAL TRP VAL          
SEQRES   4 A  333  PRO SER SER LYS CYS SER ARG LEU TYR THR ALA CYS VAL          
SEQRES   5 A  333  TYR HIS LYS LEU PHE ASP ALA SER ASP SER SER SER TYR          
SEQRES   6 A  333  LYS HIS ASN GLY THR GLU LEU THR LEU ARG TYR SER THR          
SEQRES   7 A  333  GLY THR VAL SER GLY PHE LEU SER GLN ASP ILE ILE THR          
SEQRES   8 A  333  VAL GLY GLY ILE THR VAL THR GLN MET PHE GLY GLU VAL          
SEQRES   9 A  333  THR GLU MET PRO ALA LEU PRO PHE MET LEU ALA GLU PHE          
SEQRES  10 A  333  ASP GLY VAL VAL GLY MET GLY PHE ILE GLU GLN ALA ILE          
SEQRES  11 A  333  GLY ARG VAL THR PRO ILE PHE ASP ASN ILE ILE SER GLN          
SEQRES  12 A  333  GLY VAL LEU LYS GLU ASP VAL PHE SER PHE TYR TYR ASN          
SEQRES  13 A  333  ARG ASP SER GLU ASN SER GLN SER LEU GLY GLY GLN ILE          
SEQRES  14 A  333  VAL LEU GLY GLY SER ASP PRO GLN HIS TYR GLU GLY ASN          
SEQRES  15 A  333  PHE HIS TYR ILE ASN LEU ILE LYS THR GLY VAL TRP GLN          
SEQRES  16 A  333  ILE GLN MET LYS GLY VAL SER VAL GLY SER SER THR LEU          
SEQRES  17 A  333  LEU CYS GLU ASP GLY CYS LEU ALA LEU VAL ASP THR GLY          
SEQRES  18 A  333  ALA SER TYR ILE SER GLY SER THR SER SER ILE GLU LYS          
SEQRES  19 A  333  LEU MET GLU ALA LEU GLY ALA LYS LYS ARG LEU PHE ASP          
SEQRES  20 A  333  TYR VAL VAL LYS CYS ASN GLU GLY PRO THR LEU PRO ASP          
SEQRES  21 A  333  ILE SER PHE HIS LEU GLY GLY LYS GLU TYR THR LEU THR          
SEQRES  22 A  333  SER ALA ASP TYR VAL PHE GLN GLU SER TYR SER SER LYS          
SEQRES  23 A  333  LYS LEU CYS THR LEU ALA ILE HIS ALA MET ASP ILE PRO          
SEQRES  24 A  333  PRO PRO THR GLY PRO THR TRP ALA LEU GLY ALA THR PHE          
SEQRES  25 A  333  ILE ARG LYS PHE TYR THR GLU PHE ASP ARG ARG ASN ASN          
SEQRES  26 A  333  ARG ILE GLY PHE ALA LEU ALA ARG                              
SEQRES   1 B  333  SER SER VAL ILE LEU THR ASN TYR MET ASP THR GLN TYR          
SEQRES   2 B  333  TYR GLY GLU ILE GLY ILE GLY THR PRO PRO GLN THR PHE          
SEQRES   3 B  333  LYS VAL VAL PHE ASP THR GLY SER SER ASN VAL TRP VAL          
SEQRES   4 B  333  PRO SER SER LYS CYS SER ARG LEU TYR THR ALA CYS VAL          
SEQRES   5 B  333  TYR HIS LYS LEU PHE ASP ALA SER ASP SER SER SER TYR          
SEQRES   6 B  333  LYS HIS ASN GLY THR GLU LEU THR LEU ARG TYR SER THR          
SEQRES   7 B  333  GLY THR VAL SER GLY PHE LEU SER GLN ASP ILE ILE THR          
SEQRES   8 B  333  VAL GLY GLY ILE THR VAL THR GLN MET PHE GLY GLU VAL          
SEQRES   9 B  333  THR GLU MET PRO ALA LEU PRO PHE MET LEU ALA GLU PHE          
SEQRES  10 B  333  ASP GLY VAL VAL GLY MET GLY PHE ILE GLU GLN ALA ILE          
SEQRES  11 B  333  GLY ARG VAL THR PRO ILE PHE ASP ASN ILE ILE SER GLN          
SEQRES  12 B  333  GLY VAL LEU LYS GLU ASP VAL PHE SER PHE TYR TYR ASN          
SEQRES  13 B  333  ARG ASP SER GLU ASN SER GLN SER LEU GLY GLY GLN ILE          
SEQRES  14 B  333  VAL LEU GLY GLY SER ASP PRO GLN HIS TYR GLU GLY ASN          
SEQRES  15 B  333  PHE HIS TYR ILE ASN LEU ILE LYS THR GLY VAL TRP GLN          
SEQRES  16 B  333  ILE GLN MET LYS GLY VAL SER VAL GLY SER SER THR LEU          
SEQRES  17 B  333  LEU CYS GLU ASP GLY CYS LEU ALA LEU VAL ASP THR GLY          
SEQRES  18 B  333  ALA SER TYR ILE SER GLY SER THR SER SER ILE GLU LYS          
SEQRES  19 B  333  LEU MET GLU ALA LEU GLY ALA LYS LYS ARG LEU PHE ASP          
SEQRES  20 B  333  TYR VAL VAL LYS CYS ASN GLU GLY PRO THR LEU PRO ASP          
SEQRES  21 B  333  ILE SER PHE HIS LEU GLY GLY LYS GLU TYR THR LEU THR          
SEQRES  22 B  333  SER ALA ASP TYR VAL PHE GLN GLU SER TYR SER SER LYS          
SEQRES  23 B  333  LYS LEU CYS THR LEU ALA ILE HIS ALA MET ASP ILE PRO          
SEQRES  24 B  333  PRO PRO THR GLY PRO THR TRP ALA LEU GLY ALA THR PHE          
SEQRES  25 B  333  ILE ARG LYS PHE TYR THR GLU PHE ASP ARG ARG ASN ASN          
SEQRES  26 B  333  ARG ILE GLY PHE ALA LEU ALA ARG                              
MODRES 2G1Y ASN A   70  ASN  GLYCOSYLATION SITE                                 
MODRES 2G1Y ASN B   70  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 985      14                                                       
HET    5IG  A 885      28                                                       
HET    NAG  B 986      14                                                       
HET    5IG  B 886      28                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     5IG 6-(2,4-DIAMINO-6-ETHYLPYRIMIDIN-5-YL)-4-(3-                      
HETNAM   2 5IG  METHOXYPROPYL)-2,2-DIMETHYL-2H-1,4-BENZOXAZIN-3(4H)-            
HETNAM   3 5IG  ONE                                                             
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  5IG    2(C20 H27 N5 O3)                                             
FORMUL   7  HOH   *322(H2 O)                                                    
HELIX    1   1 TYR A   50  TYR A   55  1                                   6    
HELIX    2   2 ASP A   60  SER A   64  5                                   5    
HELIX    3   3 PRO A  110  MET A  115  1                                   6    
HELIX    4   4 PHE A  127  VAL A  135  5                                   9    
HELIX    5   5 PRO A  137  GLN A  145  1                                   9    
HELIX    6   6 ASP A  177  GLN A  179  5                                   3    
HELIX    7   7 SER A  230  GLY A  242  1                                  13    
HELIX    8   8 ASN A  255  LEU A  260  5                                   6    
HELIX    9   9 THR A  275  VAL A  280  1                                   6    
HELIX   10  10 GLY A  311  ARG A  316  1                                   6    
HELIX   11  11 TYR B   50  TYR B   55  1                                   6    
HELIX   12  12 ASP B   60  SER B   64  5                                   5    
HELIX   13  13 PRO B  110  MET B  115  1                                   6    
HELIX   14  14 PRO B  137  GLN B  145  1                                   9    
HELIX   15  15 ASP B  177  GLN B  179  5                                   3    
HELIX   16  16 SER B  230  GLY B  242  1                                  13    
HELIX   17  17 ASN B  255  LEU B  260  5                                   6    
HELIX   18  18 THR B  275  VAL B  280  1                                   6    
HELIX   19  19 GLY B  311  LYS B  317  1                                   7    
SHEET    1   A 9 LYS A  68  TYR A  78  0                                        
SHEET    2   A 9 GLY A  81  VAL A  94 -1  O  VAL A  83   N  LEU A  76           
SHEET    3   A 9 GLN A  14  ILE A  21 -1  N  GLY A  20   O  THR A  93           
SHEET    4   A 9 SER A   4  TYR A  10 -1  N  TYR A  10   O  GLN A  14           
SHEET    5   A 9 GLY A 169  LEU A 173 -1  O  GLY A 169   N  LEU A   7           
SHEET    6   A 9 VAL A 152  TYR A 157 -1  N  TYR A 156   O  GLN A 170           
SHEET    7   A 9 PHE A 318  ASP A 323 -1  O  THR A 320   N  PHE A 155           
SHEET    8   A 9 ARG A 328  ALA A 334 -1  O  GLY A 330   N  GLU A 321           
SHEET    9   A 9 TYR A 181  ASN A 189 -1  N  ILE A 188   O  ILE A 329           
SHEET    1   B13 LYS A  68  TYR A  78  0                                        
SHEET    2   B13 GLY A  81  VAL A  94 -1  O  VAL A  83   N  LEU A  76           
SHEET    3   B13 ILE A  97  GLU A 108 -1  O  VAL A  99   N  ILE A  92           
SHEET    4   B13 VAL A  39  PRO A  42  1  N  VAL A  39   O  GLY A 104           
SHEET    5   B13 GLY A 121  GLY A 124 -1  O  VAL A 122   N  TRP A  40           
SHEET    6   B13 GLN A  26  ASP A  33  1  N  VAL A  31   O  VAL A 123           
SHEET    7   B13 GLN A  14  ILE A  21 -1  N  GLY A  17   O  VAL A  30           
SHEET    8   B13 SER A   4  TYR A  10 -1  N  TYR A  10   O  GLN A  14           
SHEET    9   B13 GLY A 169  LEU A 173 -1  O  GLY A 169   N  LEU A   7           
SHEET   10   B13 VAL A 152  TYR A 157 -1  N  TYR A 156   O  GLN A 170           
SHEET   11   B13 PHE A 318  ASP A 323 -1  O  THR A 320   N  PHE A 155           
SHEET   12   B13 ARG A 328  ALA A 334 -1  O  GLY A 330   N  GLU A 321           
SHEET   13   B13 TYR A 181  ASN A 189 -1  N  ILE A 188   O  ILE A 329           
SHEET    1   C 7 LYS A 270  LEU A 274  0                                        
SHEET    2   C 7 ILE A 263  LEU A 267 -1  N  ILE A 263   O  LEU A 274           
SHEET    3   C 7 GLN A 197  VAL A 205 -1  N  GLY A 202   O  HIS A 266           
SHEET    4   C 7 CYS A 216  VAL A 220 -1  O  CYS A 216   N  MET A 200           
SHEET    5   C 7 TRP A 308  LEU A 310  1  O  LEU A 310   N  LEU A 219           
SHEET    6   C 7 ILE A 227  GLY A 229 -1  N  SER A 228   O  ALA A 309           
SHEET    7   C 7 ILE A 295  ALA A 297  1  O  HIS A 296   N  ILE A 227           
SHEET    1   D 3 LYS A 244  LYS A 245  0                                        
SHEET    2   D 3 TYR A 250  LYS A 253 -1  O  VAL A 251   N  LYS A 244           
SHEET    3   D 3 LEU A 290  THR A 292 -1  O  CYS A 291   N  VAL A 252           
SHEET    1   E 9 LYS B  68  ARG B  77  0                                        
SHEET    2   E 9 THR B  82  VAL B  94 -1  O  LEU B  87   N  THR B  72           
SHEET    3   E 9 GLN B  14  ILE B  21 -1  N  GLY B  20   O  THR B  93           
SHEET    4   E 9 SER B   4  TYR B  10 -1  N  THR B   8   O  TYR B  16           
SHEET    5   E 9 GLY B 169  LEU B 173 -1  O  GLY B 169   N  LEU B   7           
SHEET    6   E 9 VAL B 152  TYR B 157 -1  N  SER B 154   O  VAL B 172           
SHEET    7   E 9 PHE B 318  ASP B 323 -1  O  PHE B 322   N  PHE B 153           
SHEET    8   E 9 ARG B 328  ALA B 334 -1  O  GLY B 330   N  GLU B 321           
SHEET    9   E 9 TYR B 181  ASN B 189 -1  N  GLU B 182   O  LEU B 333           
SHEET    1   F13 LYS B  68  ARG B  77  0                                        
SHEET    2   F13 THR B  82  VAL B  94 -1  O  LEU B  87   N  THR B  72           
SHEET    3   F13 ILE B  97  GLU B 108 -1  O  ILE B  97   N  VAL B  94           
SHEET    4   F13 VAL B  39  PRO B  42  1  N  VAL B  41   O  VAL B 106           
SHEET    5   F13 GLY B 121  GLY B 124 -1  O  VAL B 122   N  TRP B  40           
SHEET    6   F13 GLN B  26  ASP B  33  1  N  VAL B  31   O  VAL B 123           
SHEET    7   F13 GLN B  14  ILE B  21 -1  N  GLY B  17   O  VAL B  30           
SHEET    8   F13 SER B   4  TYR B  10 -1  N  THR B   8   O  TYR B  16           
SHEET    9   F13 GLY B 169  LEU B 173 -1  O  GLY B 169   N  LEU B   7           
SHEET   10   F13 VAL B 152  TYR B 157 -1  N  SER B 154   O  VAL B 172           
SHEET   11   F13 PHE B 318  ASP B 323 -1  O  PHE B 322   N  PHE B 153           
SHEET   12   F13 ARG B 328  ALA B 334 -1  O  GLY B 330   N  GLU B 321           
SHEET   13   F13 TYR B 181  ASN B 189 -1  N  GLU B 182   O  LEU B 333           
SHEET    1   G 5 GLN B 197  MET B 200  0                                        
SHEET    2   G 5 CYS B 216  VAL B 220 -1  O  ALA B 218   N  ILE B 198           
SHEET    3   G 5 TRP B 308  LEU B 310  1  O  LEU B 310   N  LEU B 219           
SHEET    4   G 5 ILE B 227  GLY B 229 -1  N  SER B 228   O  ALA B 309           
SHEET    5   G 5 ILE B 295  ALA B 297  1  O  HIS B 296   N  ILE B 227           
SHEET    1   H 4 SER B 208  LEU B 211  0                                        
SHEET    2   H 4 VAL B 203  VAL B 205 -1  N  VAL B 203   O  LEU B 211           
SHEET    3   H 4 ILE B 263  LEU B 267 -1  O  SER B 264   N  SER B 204           
SHEET    4   H 4 LYS B 270  LEU B 274 -1  O  TYR B 272   N  PHE B 265           
SHEET    1   I 3 LYS B 244  LYS B 245  0                                        
SHEET    2   I 3 TYR B 250  LYS B 253 -1  O  VAL B 251   N  LYS B 244           
SHEET    3   I 3 LEU B 290  THR B 292 -1  O  CYS B 291   N  VAL B 252           
SSBOND   1 CYS A   46    CYS A   53                          1555   1555  2.03  
SSBOND   2 CYS A  212    CYS A  216                          1555   1555  2.03  
SSBOND   3 CYS A  254    CYS A  291                          1555   1555  2.03  
SSBOND   4 CYS B   46    CYS B   53                          1555   1555  2.03  
SSBOND   5 CYS B  212    CYS B  216                          1555   1555  2.03  
SSBOND   6 CYS B  254    CYS B  291                          1555   1555  2.03  
LINK         ND2 ASN A  70                 C1  NAG A 985     1555   1555  1.45  
LINK         ND2 ASN B  70                 C1  NAG B 986     1555   1555  1.45  
CISPEP   1 THR A   23    PRO A   24          0        -0.24                     
CISPEP   2 LEU A  112    PRO A  113          0         0.60                     
CISPEP   3 PRO A  302    PRO A  303          0         0.01                     
CISPEP   4 GLY A  305    PRO A  306          0         0.05                     
CISPEP   5 THR B   23    PRO B   24          0        -0.08                     
CISPEP   6 LEU B  112    PRO B  113          0         0.08                     
CISPEP   7 PRO B  302    PRO B  303          0         0.17                     
CISPEP   8 GLY B  305    PRO B  306          0        -0.23                     
CRYST1  141.038  141.038  141.038  90.00  90.00  90.00 P 21 3       24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007046  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007046  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007046        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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