GenomeNet

Database: PDB
Entry: 2JXR
LinkDB: 2JXR
Original site: 2JXR 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           24-APR-97   2JXR              
TITLE     STRUCTURE OF YEAST PROTEINASE A                                       
CAVEAT     2JXR    THR A 16 HAS WRONG CHIRALITY AT ATOM CB ASN A 43 HAS WRONG   
CAVEAT   2 2JXR    CHIRALITY AT ATOM CA SER A 63 HAS WRONG CHIRALITY AT ATOM    
CAVEAT   3 2JXR    CA ASN A 161 HAS WRONG CHIRALITY AT ATOM CA TRP A 241 HAS    
CAVEAT   4 2JXR    WRONG CHIRALITY AT ATOM CA MAN B 5 HAS WRONG CHIRALITY AT    
CAVEAT   5 2JXR    ATOM C1 MAN B 5 HAS WRONG CHIRALITY AT ATOM C2 MAN B 5 HAS   
CAVEAT   6 2JXR    WRONG CHIRALITY AT ATOM C5 NAG A 337 HAS WRONG CHIRALITY AT  
CAVEAT   7 2JXR    ATOM C1 NAG A 337 HAS WRONG CHIRALITY AT ATOM C2             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEINASE A;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SACCHAROPEPSIN, YEAST ENDOPEPTIDASE A;                      
COMPND   5 EC: 3.4.23.25;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932                                                 
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX, ASPARTYL PROTEASE,             
KEYWDS   2 GLYCOPROTEIN, ZYMOGEN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.F.AGUILAR,M.BADASSO,T.DREYER,N.B.CRONIN,M.P.NEWMAN,J.B.COOPER,      
AUTHOR   2 D.J.HOOVER,S.P.WOOD,M.S.JOHNSON,T.L.BLUNDELL                         
REVDAT   5   03-NOV-21 2JXR    1       SEQADV HETSYN                            
REVDAT   4   29-JUL-20 2JXR    1       CAVEAT COMPND REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   13-JUL-11 2JXR    1       VERSN                                    
REVDAT   2   24-FEB-09 2JXR    1       VERSN                                    
REVDAT   1   29-OCT-97 2JXR    0                                                
SPRSDE     29-OCT-97 2JXR      1JXR                                             
JRNL        AUTH   C.F.AGUILAR,N.B.CRONIN,M.BADASSO,T.DREYER,M.P.NEWMAN,        
JRNL        AUTH 2 J.B.COOPER,D.J.HOOVER,S.P.WOOD,M.S.JOHNSON,T.L.BLUNDELL      
JRNL        TITL   THE THREE-DIMENSIONAL STRUCTURE AT 2.4 A RESOLUTION OF       
JRNL        TITL 2 GLYCOSYLATED PROTEINASE A FROM THE LYSOSOME-LIKE VACUOLE OF  
JRNL        TITL 3 SACCHAROMYCES CEREVISIAE.                                    
JRNL        REF    J.MOL.BIOL.                   V. 267   899 1997              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9135120                                                      
JRNL        DOI    10.1006/JMBI.1996.0880                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : RESTRAIN                                             
REMARK   3   AUTHORS     : MOSS,DRIESSEN,HANEEF,HOWLIN,HARRIS                   
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 18013                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2528                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 121                                     
REMARK   3   SOLVENT ATOMS            : 119                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.01                          
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: LOOP RESIDUES A 140 - A 142 WERE          
REMARK   3  MODELED STEREOCHEMICALLY.                                           
REMARK   4                                                                      
REMARK   4 2JXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178279.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NOV-93                             
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               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
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                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AGROVATA, WEIS                     
REMARK 200  DATA SCALING SOFTWARE          : AGROVATA                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18325                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07000                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
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   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-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       73.60000            
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       36.80000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.80000            
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       73.60000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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, 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: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 25.0 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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       73.60000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 260   CZ    PHE A 260   CE2     0.120                       
REMARK 500    VAL A 301   CB    VAL A 301   CG1    -0.128                       
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    HIS A   2   CA  -  CB  -  CG  ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ASP A   3   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    VAL A   4   CA  -  CB  -  CG2 ANGL. DEV. =  22.9 DEGREES          
REMARK 500    TYR A  14   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TYR A  15   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ASP A  17   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ILE A  30   CB  -  CG1 -  CD1 ANGL. DEV. =  17.6 DEGREES          
REMARK 500    SER A  35   C   -  N   -  CA  ANGL. DEV. =  24.4 DEGREES          
REMARK 500    LEU A  38   CB  -  CG  -  CD1 ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ASN A  43   N   -  CA  -  CB  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    TYR A  56   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP A  57   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ALA A  60   O   -  C   -  N   ANGL. DEV. =  12.6 DEGREES          
REMARK 500    SER A  63   N   -  CA  -  CB  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    LEU A  80   CA  -  CB  -  CG  ANGL. DEV. =  20.0 DEGREES          
REMARK 500    ILE A  91   CA  -  C   -  N   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    GLY A  92   C   -  N   -  CA  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASP A  93   CB  -  CG  -  OD1 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    LEU A  94   CB  -  CG  -  CD2 ANGL. DEV. = -14.1 DEGREES          
REMARK 500    PRO A 108   C   -  N   -  CA  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    PRO A 108   C   -  N   -  CD  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU A 121   CB  -  CG  -  CD2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    GLY A 122   C   -  N   -  CA  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASP A 126   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ILE A 128   CB  -  CG1 -  CD1 ANGL. DEV. = -19.9 DEGREES          
REMARK 500    ASP A 131   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    LYS A 132   CD  -  CE  -  NZ  ANGL. DEV. =  20.6 DEGREES          
REMARK 500    VAL A 133   CA  -  CB  -  CG1 ANGL. DEV. = -10.9 DEGREES          
REMARK 500    VAL A 134   CG1 -  CB  -  CG2 ANGL. DEV. = -11.9 DEGREES          
REMARK 500    LEU A 145   CB  -  CG  -  CD2 ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG A 150   CB  -  CG  -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ARG A 150   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    PHE A 153   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    TYR A 154   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ASP A 159B  CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASN A 161   N   -  CA  -  CB  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    ASP A 171   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    PHE A 175   CG  -  CD1 -  CE1 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PHE A 175   CD1 -  CE1 -  CZ  ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    LYS A 176   CA  -  CB  -  CG  ANGL. DEV. =  23.9 DEGREES          
REMARK 500    THR A 180   O   -  C   -  N   ANGL. DEV. =   9.9 DEGREES          
REMARK 500    VAL A 184   CA  -  CB  -  CG1 ANGL. DEV. =  11.8 DEGREES          
REMARK 500    ARG A 186   CA  -  CB  -  CG  ANGL. DEV. =  22.8 DEGREES          
REMARK 500    ARG A 186   CG  -  CD  -  NE  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    LYS A 187   CD  -  CE  -  NZ  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    LYS A 193   CA  -  CB  -  CG  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    LYS A 193   CG  -  CD  -  CE  ANGL. DEV. =  20.5 DEGREES          
REMARK 500    TYR A 203   CB  -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ASP A 215   CB  -  CG  -  OD1 ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ASP A 215   CB  -  CG  -  OD2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      73 ANGLE DEVIATIONS.                             
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    ASN A  67      -30.13   -155.39                                   
REMARK 500    ASP A  87      176.76    174.40                                   
REMARK 500    ASP A 159B    -151.12   -114.46                                   
REMARK 500    THR A 159C     -85.97   -172.63                                   
REMARK 500    ASN A 161       99.40    -48.82                                   
REMARK 500    ALA A 188      -59.45   -148.40                                   
REMARK 500    LEU A 220     -150.97   -112.37                                   
REMARK 500    LYS A 239       99.06    -63.63                                   
REMARK 500    TRP A 241      -85.17     -3.06                                   
REMARK 500    ASN A 263        8.06     58.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR                                
REMARK 630 MOLECULE NAME: N-(MORPHOLIN-4-YLCARBONYL)-L-PHENYLALANYL-N-[(1R)-1-  
REMARK 630 (CYCLOHEXYLMETHYL)-3,3-DIFLUORO-2,2-DIHYDROXY-4-(METHYLAMINO)-4-     
REMARK 630 OXOBUTYL]-L-NORLEUCINAMIDE                                           
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     2Z3 A   327                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    MOR PHE NLE CHF NME                                      
REMARK 630 DETAILS: NULL                                                        
DBREF  2JXR A    0   326  UNP    P07267   CARP_YEAST      77    405             
SEQADV 2JXR ILE A  315  UNP  P07267    LEU   394 ENGINEERED MUTATION            
SEQRES   1 A  329  GLY GLY HIS ASP VAL PRO LEU THR ASN TYR LEU ASN ALA          
SEQRES   2 A  329  GLN TYR TYR THR ASP ILE THR LEU GLY THR PRO PRO GLN          
SEQRES   3 A  329  ASN PHE LYS VAL ILE LEU ASP THR GLY SER SER ASN LEU          
SEQRES   4 A  329  TRP VAL PRO SER ASN GLU CYS GLY SER LEU ALA CYS PHE          
SEQRES   5 A  329  LEU HIS SER LYS TYR ASP HIS GLU ALA SER SER SER TYR          
SEQRES   6 A  329  LYS ALA ASN GLY THR GLU PHE ALA ILE GLN TYR GLY THR          
SEQRES   7 A  329  GLY SER LEU GLU GLY TYR ILE SER GLN ASP THR LEU SER          
SEQRES   8 A  329  ILE GLY ASP LEU THR ILE PRO LYS GLN ASP PHE ALA GLU          
SEQRES   9 A  329  ALA THR SER GLU PRO GLY LEU THR PHE ALA PHE GLY LYS          
SEQRES  10 A  329  PHE ASP GLY ILE LEU GLY LEU GLY TYR ASP THR ILE SER          
SEQRES  11 A  329  VAL ASP LYS VAL VAL PRO PRO PHE TYR ASN ALA ILE GLN          
SEQRES  12 A  329  GLN ASP LEU LEU ASP GLU LYS ARG PHE ALA PHE TYR LEU          
SEQRES  13 A  329  GLY ASP THR SER LYS ASP THR GLU ASN GLY GLY GLU ALA          
SEQRES  14 A  329  THR PHE GLY GLY ILE ASP GLU SER LYS PHE LYS GLY ASP          
SEQRES  15 A  329  ILE THR TRP LEU PRO VAL ARG ARG LYS ALA TYR TRP GLU          
SEQRES  16 A  329  VAL LYS PHE GLU GLY ILE GLY LEU GLY ASP GLU TYR ALA          
SEQRES  17 A  329  GLU LEU GLU SER HIS GLY ALA ALA ILE ASP THR GLY THR          
SEQRES  18 A  329  SER LEU ILE THR LEU PRO SER GLY LEU ALA GLU MET ILE          
SEQRES  19 A  329  ASN ALA GLU ILE GLY ALA LYS LYS GLY TRP THR GLY GLN          
SEQRES  20 A  329  TYR THR LEU ASP CYS ASN THR ARG ASP ASN LEU PRO ASP          
SEQRES  21 A  329  LEU ILE PHE ASN PHE ASN GLY TYR ASN PHE THR ILE GLY          
SEQRES  22 A  329  PRO TYR ASP TYR THR LEU GLU VAL SER GLY SER CYS ILE          
SEQRES  23 A  329  SER ALA ILE THR PRO MET ASP PHE PRO GLU PRO VAL GLY          
SEQRES  24 A  329  PRO LEU ALA ILE VAL GLY ASP ALA PHE LEU ARG LYS TYR          
SEQRES  25 A  329  TYR SER ILE TYR ASP ILE GLY ASN ASN ALA VAL GLY LEU          
SEQRES  26 A  329  ALA LYS ALA ILE                                              
MODRES 2JXR ASN A   67  ASN  GLYCOSYLATION SITE                                 
MODRES 2JXR ASN A  266  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    BMA  B   3      11                                                       
HET    BMA  B   4      11                                                       
HET    MAN  B   5      11                                                       
HET    2Z3  A 327      46                                                       
HET    NAG  A 337      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     2Z3 N-(MORPHOLIN-4-YLCARBONYL)-L-PHENYLALANYL-N-[(1R)-1-             
HETNAM   2 2Z3  (CYCLOHEXYLMETHYL)-3,3-DIFLUORO-2,2-DIHYDROXY-4-                
HETNAM   3 2Z3  (METHYLAMINO)-4-OXOBUTYL]-L-NORLEUCINAMIDE                      
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE                               
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
HETSYN     2Z3 CP-81,282                                                        
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   2  BMA    2(C6 H12 O6)                                                 
FORMUL   2  MAN    C6 H12 O6                                                    
FORMUL   3  2Z3    C32 H49 F2 N5 O7                                             
FORMUL   5  HOH   *119(H2 O)                                                    
HELIX    1   A SER A   47  HIS A   53  1                                   7    
HELIX    2  H2 ASP A   57  SER A   61  1                                   5    
HELIX    3  H3 SER A  129  VAL A  133  1                                   5    
HELIX    4  H4 PRO A  135  GLN A  143  1                                   9    
HELIX    5  H5 PRO A  224  ILE A  235  1                                  12    
HELIX    6  H6 ASP A  248  LEU A  255  1                                   8    
HELIX    7  H7 GLY A  302  LYS A  308  1                                   7    
SHEET    1   A 6 HIS A   2  PRO A   5  0                                        
SHEET    2   A 6 GLY A 163  PHE A 167 -1  N  PHE A 167   O  HIS A   2           
SHEET    3   A 6 ARG A 150  LEU A 155 -1  N  TYR A 154   O  GLU A 164           
SHEET    4   A 6 TYR A 309  ASP A 314 -1  N  TYR A 313   O  PHE A 151           
SHEET    5   A 6 ALA A 319  LYS A 324 -1  N  ALA A 323   O  TYR A 310           
SHEET    6   A 6 THR A 180  PRO A 183 -1  N  LEU A 182   O  VAL A 320           
SHEET    1   B 4 THR A   7  TYR A   9  0                                        
SHEET    2   B 4 GLN A  13  THR A  19 -1  N  TYR A  15   O  THR A   7           
SHEET    3   B 4 ASN A  26  ASP A  32 -1  N  VAL A  29   O  THR A  16           
SHEET    4   B 4 GLY A 119  GLY A 122  1  N  GLY A 119   O  ILE A  30           
SHEET    1   C 4 TRP A  39  PRO A  41  0                                        
SHEET    2   C 4 PHE A 101  SER A 106  1  N  ALA A 102   O  VAL A  40           
SHEET    3   C 4 SER A  79  SER A  85 -1  N  SER A  85   O  PHE A 101           
SHEET    4   C 4 GLU A  70  GLN A  74 -1  N  ILE A  73   O  LEU A  80           
SHEET    1   D 2 LEU A  89  ILE A  91  0                                        
SHEET    2   D 2 LEU A  94  ILE A  96 -1  N  ILE A  96   O  LEU A  89           
SHEET    1   E 3 GLU A 191  LYS A 193  0                                        
SHEET    2   E 3 GLY A 210  ILE A 214 -1  N  ALA A 212   O  VAL A 192           
SHEET    3   E 3 LEU A 298  VAL A 301  1  N  ALA A 299   O  GLY A 210           
SHEET    1   F 4 GLU A 202  GLU A 205  0                                        
SHEET    2   F 4 PHE A 194  LEU A 199 -1  N  LEU A 199   O  GLU A 202           
SHEET    3   F 4 LEU A 258  PHE A 262 -1  N  ASN A 261   O  GLU A 195           
SHEET    4   F 4 TYR A 265  ILE A 269 -1  N  ILE A 269   O  LEU A 258           
SHEET    1   G 2 ILE A 221  LEU A 223  0                                        
SHEET    2   G 2 ILE A 286  PRO A 288  1  N  THR A 287   O  ILE A 221           
SHEET    1   H 2 THR A 275  VAL A 278  0                                        
SHEET    2   H 2 SER A 281  SER A 284 -1  N  ILE A 283   O  LEU A 276           
SSBOND   1 CYS A   45    CYS A   50                          1555   1555  1.96  
SSBOND   2 CYS A  249    CYS A  282                          1555   1555  1.96  
LINK         ND2 ASN A  67                 C1  NAG B   1     1555   1555  1.40  
LINK         ND2 ASN A 266                 C1  NAG A 337     1555   1555  1.49  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.41  
LINK         O4  NAG B   2                 C1  BMA B   3     1555   1555  1.45  
LINK         O3  BMA B   3                 C1  BMA B   4     1555   1555  1.41  
LINK         O2  BMA B   4                 C1  MAN B   5     1555   1555  1.46  
CISPEP   1 THR A   22    PRO A   23          0        -1.06                     
CISPEP   2 GLU A  293    PRO A  294          0         7.77                     
CISPEP   3 GLY A  296    PRO A  297          0        -1.19                     
CRYST1   86.700   86.700  110.400  90.00  90.00 120.00 P 32 2 1      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      0.011534  0.006659  0.000000        0.00000                         
SCALE2      0.000000  0.013318  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009058        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system