GenomeNet

Database: PDB
Entry: 2R9N
LinkDB: 2R9N
Original site: 2R9N 
HEADER    HYDROLASE                               13-SEP-07   2R9N              
TITLE     CATHEPSIN S COMPLEXED WITH COMPOUND 26                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATHEPSIN S;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.22.27;                                                       
COMPND   5 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: CTSS;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, CATHEPSIN, PROTEASE, GLYCOPROTEIN, LYSOSOME, POLYMORPHISM, 
KEYWDS   2 THIOL PROTEASE, ZYMOGEN                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.D.WARD,M.J.EMMANUEL,D.S.THOMSON,W.LIU,Y.BEKKALI,L.L.FRYE,           
AUTHOR   2 M.GIRARDOT,T.MORWICK,E.R.R.YOUNG,R.ZINDELL,M.HRAPCHAK,M.DETURI,      
AUTHOR   3 A.WHITE,K.M.CRANE,D.M.WHITE,Y.WANG,M.-H.HAO,C.A.GRYGON,M.E.LABADIA,  
AUTHOR   4 J.WILDESON,D.FREEMAN,R.NELSON,A.CAPOLINO,J.D.PETERSON,E.L.RAYMOND,   
AUTHOR   5 M.L.BROWN,D.M.SPERO                                                  
REVDAT   4   30-AUG-23 2R9N    1       SEQADV                                   
REVDAT   3   24-JUL-19 2R9N    1       REMARK                                   
REVDAT   2   24-FEB-09 2R9N    1       VERSN                                    
REVDAT   1   18-DEC-07 2R9N    0                                                
JRNL        AUTH   Y.D.WARD,M.J.EMMANUEL,D.S.THOMSON,W.LIU,Y.BEKKALI,L.L.FRYE,  
JRNL        AUTH 2 M.GIRARDOT,T.MORWICK,E.R.R.YOUNG,R.ZINDELL,M.HRAPCHAK,       
JRNL        AUTH 3 M.DETURI,A.WHITE,K.M.CRANE,D.M.WHITE,Y.WANG,M.-H.HAO,        
JRNL        AUTH 4 C.A.GRYGON,M.E.LABADIA,J.WILDESON,D.FREEMAN,R.NELSON,        
JRNL        AUTH 5 A.CAPOLINO,J.D.PETERSON,E.L.RAYMOND,M.L.BROWN,D.M.SPERO      
JRNL        TITL   DESIGN AND SYNTHESIS OF REVERSIBLE INHIBITORS OF CATHEPSIN   
JRNL        TITL 2 S: ALPHA,ALPHA-DISUBSTITUTION AT THE P1 RESIDUE PROVIDES     
JRNL        TITL 3 POTENT INHIBITORS IN CELLULAR ASSAYS AND IN VIVO MODELS OF   
JRNL        TITL 4 ANTIGEN PRESENTATION                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 98.1                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
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             : 38137                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1965                            
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            : 3364                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 312                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.16                          
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.790                           
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  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 2R9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044598.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC FOCUSSING MIRRORS            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38189                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1MS6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NAOAC, 18-35% PEG MME (500         
REMARK 280  -8000), 2 M (NH4)2SO4 WITH OR WITHOUT 15% GLYCEROL, PH 4.6,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+3/4                                              
REMARK 290       8555   -Y,-X,-Z+1/4                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.98050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.49025            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.47075            
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        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.98050            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      112.47075            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       37.49025            
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                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 376  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 390  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 433  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   218                                                      
REMARK 465     HIS A   219                                                      
REMARK 465     HIS A   220                                                      
REMARK 465     HIS A   221                                                      
REMARK 465     HIS A   222                                                      
REMARK 465     HIS B   218                                                      
REMARK 465     HIS B   219                                                      
REMARK 465     HIS B   220                                                      
REMARK 465     HIS B   221                                                      
REMARK 465     HIS B   222                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 149    CG   CD   NE   CZ   NH1  NH2                        
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   SG   CYS B    25     C32  Y14 B   281              1.91            
REMARK 500   SG   CYS A    25     C32  Y14 A   281              1.93            
REMARK 500   O    HOH A   324     O    HOH A   343              2.17            
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    THR A  58     -125.31   -110.00                                   
REMARK 500    ASN A 163       -1.94   -145.97                                   
REMARK 500    THR B  58     -131.18   -109.41                                   
REMARK 500    ARG B 141       47.11    -82.94                                   
REMARK 500    ASN B 163        1.11   -151.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R9M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2R9O   RELATED DB: PDB                                   
DBREF  2R9N A    1   217  UNP    P25774   CATS_HUMAN     115    331             
DBREF  2R9N B    1   217  UNP    P25774   CATS_HUMAN     115    331             
SEQADV 2R9N HIS A  218  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS A  219  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS A  220  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS A  221  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS A  222  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS B  218  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS B  219  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS B  220  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS B  221  UNP  P25774              EXPRESSION TAG                 
SEQADV 2R9N HIS B  222  UNP  P25774              EXPRESSION TAG                 
SEQRES   1 A  222  LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS VAL          
SEQRES   2 A  222  THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA CYS TRP          
SEQRES   3 A  222  ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU LYS          
SEQRES   4 A  222  LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN ASN          
SEQRES   5 A  222  LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS GLY          
SEQRES   6 A  222  CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR ILE          
SEQRES   7 A  222  ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR PRO          
SEQRES   8 A  222  TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER LYS          
SEQRES   9 A  222  TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU PRO          
SEQRES  10 A  222  TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA ASN          
SEQRES  11 A  222  LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS PRO          
SEQRES  12 A  222  SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU PRO          
SEQRES  13 A  222  SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL VAL          
SEQRES  14 A  222  GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU VAL          
SEQRES  15 A  222  LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY TYR          
SEQRES  16 A  222  ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY ILE          
SEQRES  17 A  222  ALA SER PHE PRO SER TYR PRO GLU ILE HIS HIS HIS HIS          
SEQRES  18 A  222  HIS                                                          
SEQRES   1 B  222  LEU PRO ASP SER VAL ASP TRP ARG GLU LYS GLY CYS VAL          
SEQRES   2 B  222  THR GLU VAL LYS TYR GLN GLY SER CYS GLY ALA CYS TRP          
SEQRES   3 B  222  ALA PHE SER ALA VAL GLY ALA LEU GLU ALA GLN LEU LYS          
SEQRES   4 B  222  LEU LYS THR GLY LYS LEU VAL SER LEU SER ALA GLN ASN          
SEQRES   5 B  222  LEU VAL ASP CYS SER THR GLU LYS TYR GLY ASN LYS GLY          
SEQRES   6 B  222  CYS ASN GLY GLY PHE MET THR THR ALA PHE GLN TYR ILE          
SEQRES   7 B  222  ILE ASP ASN LYS GLY ILE ASP SER ASP ALA SER TYR PRO          
SEQRES   8 B  222  TYR LYS ALA MET ASP GLN LYS CYS GLN TYR ASP SER LYS          
SEQRES   9 B  222  TYR ARG ALA ALA THR CYS SER LYS TYR THR GLU LEU PRO          
SEQRES  10 B  222  TYR GLY ARG GLU ASP VAL LEU LYS GLU ALA VAL ALA ASN          
SEQRES  11 B  222  LYS GLY PRO VAL SER VAL GLY VAL ASP ALA ARG HIS PRO          
SEQRES  12 B  222  SER PHE PHE LEU TYR ARG SER GLY VAL TYR TYR GLU PRO          
SEQRES  13 B  222  SER CYS THR GLN ASN VAL ASN HIS GLY VAL LEU VAL VAL          
SEQRES  14 B  222  GLY TYR GLY ASP LEU ASN GLY LYS GLU TYR TRP LEU VAL          
SEQRES  15 B  222  LYS ASN SER TRP GLY HIS ASN PHE GLY GLU GLU GLY TYR          
SEQRES  16 B  222  ILE ARG MET ALA ARG ASN LYS GLY ASN HIS CYS GLY ILE          
SEQRES  17 B  222  ALA SER PHE PRO SER TYR PRO GLU ILE HIS HIS HIS HIS          
SEQRES  18 B  222  HIS                                                          
HET    Y14  A 281      34                                                       
HET    Y14  B 281      34                                                       
HETNAM     Y14 N-[(1S)-2-{[(3S)-1-BENZYL-3-CYANOPYRROLIDIN-3-                   
HETNAM   2 Y14  YL]AMINO}-1-(CYCLOHEXYLMETHYL)-2-OXOETHYL]MORPHOLINE-           
HETNAM   3 Y14  4-CARBOXAMIDE                                                   
FORMUL   3  Y14    2(C26 H37 N5 O3)                                             
FORMUL   5  HOH   *312(H2 O)                                                    
HELIX    1   1 ARG A    8  GLY A   11  5                                   4    
HELIX    2   2 ALA A   24  GLY A   43  1                                  20    
HELIX    3   3 SER A   49  SER A   57  1                                   9    
HELIX    4   4 THR A   58  GLY A   62  5                                   5    
HELIX    5   5 LYS A   64  GLY A   68  5                                   5    
HELIX    6   6 PHE A   70  LYS A   82  1                                  13    
HELIX    7   7 ASP A  102  LYS A  104  5                                   3    
HELIX    8   8 ARG A  120  LYS A  131  1                                  12    
HELIX    9   9 HIS A  142  LEU A  147  1                                   6    
HELIX   10  10 ASN A  204  ILE A  208  5                                   5    
HELIX   11  11 ARG B    8  GLY B   11  5                                   4    
HELIX   12  12 ALA B   24  GLY B   43  1                                  20    
HELIX   13  13 SER B   49  SER B   57  1                                   9    
HELIX   14  14 THR B   58  GLY B   62  5                                   5    
HELIX   15  15 LYS B   64  GLY B   68  5                                   5    
HELIX   16  16 PHE B   70  LYS B   82  1                                  13    
HELIX   17  17 ASP B  102  LYS B  104  5                                   3    
HELIX   18  18 ARG B  120  LYS B  131  1                                  12    
HELIX   19  19 HIS B  142  TYR B  148  1                                   7    
HELIX   20  20 ASN B  204  ILE B  208  5                                   5    
SHEET    1   A 3 VAL A   5  ASP A   6  0                                        
SHEET    2   A 3 HIS A 164  LEU A 174 -1  O  TYR A 171   N  VAL A   5           
SHEET    3   A 3 VAL A 134  VAL A 138 -1  N  VAL A 136   O  VAL A 166           
SHEET    1   B 4 VAL A   5  ASP A   6  0                                        
SHEET    2   B 4 HIS A 164  LEU A 174 -1  O  TYR A 171   N  VAL A   5           
SHEET    3   B 4 LYS A 177  LYS A 183 -1  O  LYS A 183   N  LEU A 167           
SHEET    4   B 4 TYR A 195  ALA A 199 -1  O  ILE A 196   N  VAL A 182           
SHEET    1   C 2 ILE A  84  ASP A  85  0                                        
SHEET    2   C 2 ARG A 106  ALA A 108 -1  O  ALA A 107   N  ILE A  84           
SHEET    1   D 2 LYS A 112  GLU A 115  0                                        
SHEET    2   D 2 SER A 213  GLU A 216 -1  O  TYR A 214   N  THR A 114           
SHEET    1   E 3 VAL B   5  ASP B   6  0                                        
SHEET    2   E 3 HIS B 164  LEU B 174 -1  O  TYR B 171   N  VAL B   5           
SHEET    3   E 3 VAL B 134  VAL B 138 -1  N  VAL B 136   O  VAL B 166           
SHEET    1   F 5 VAL B   5  ASP B   6  0                                        
SHEET    2   F 5 HIS B 164  LEU B 174 -1  O  TYR B 171   N  VAL B   5           
SHEET    3   F 5 LYS B 177  LYS B 183 -1  O  LYS B 183   N  LEU B 167           
SHEET    4   F 5 TYR B 195  ALA B 199 -1  O  MET B 198   N  TRP B 180           
SHEET    5   F 5 VAL B 152  TYR B 153  1  N  TYR B 153   O  ARG B 197           
SHEET    1   G 2 ILE B  84  ASP B  85  0                                        
SHEET    2   G 2 ARG B 106  ALA B 108 -1  O  ALA B 107   N  ILE B  84           
SHEET    1   H 2 LYS B 112  GLU B 115  0                                        
SHEET    2   H 2 SER B 213  GLU B 216 -1  O  TYR B 214   N  THR B 114           
SSBOND   1 CYS A   22    CYS A   66                          1555   1555  2.05  
SSBOND   2 CYS A   56    CYS A   99                          1555   1555  2.04  
SSBOND   3 CYS A  158    CYS A  206                          1555   1555  2.04  
SSBOND   4 CYS B   22    CYS B   66                          1555   1555  2.03  
SSBOND   5 CYS B   56    CYS B   99                          1555   1555  2.04  
SSBOND   6 CYS B  158    CYS B  206                          1555   1555  2.04  
CRYST1   85.296   85.296  149.961  90.00  90.00  90.00 P 41 2 2     16          
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      0.011724  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011724  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006668        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system