GenomeNet

Database: PDB
Entry: 4DM9
LinkDB: 4DM9
Original site: 4DM9 
HEADER    HYDROLASE, LIGASE/INHIBITOR             07-FEB-12   4DM9              
TITLE     THE CRYSTAL STRUCTURE OF UBIQUITIN CARBOXY-TERMINAL HYDROLASE L1      
TITLE    2 (UCHL1) BOUND TO A TRIPEPTIDE FLUOROMETHYL KETONE Z-VAE(OME)-FMK     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L1;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: UCH-L1, NEURON CYTOPLASMIC PROTEIN 9.5, PGP 9.5, PGP9.5,    
COMPND   5 UBIQUITIN THIOESTERASE L1;                                           
COMPND   6 EC: 3.4.19.12, 6.-.-.-;                                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: TRIPEPTIDE FLUOROMETHYL KETONE INHIBITOR Z-VAE(OME)-FMK;   
COMPND  10 CHAIN: X, Y;                                                         
COMPND  11 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: UCHL1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    UBIQUITIN HYDROLASE, LIGASE, HYDROLASE, LIGASE-INHIBITOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.W.DAVIES,J.CHANEY,G.KORBEL,D.RINGE,G.A.PETSKO,H.PLOEGH,C.DAS        
REVDAT   2   13-JUN-12 4DM9    1       JRNL                                     
REVDAT   1   23-MAY-12 4DM9    0                                                
JRNL        AUTH   C.W.DAVIES,J.CHANEY,G.KORBEL,D.RINGE,G.A.PETSKO,H.PLOEGH,    
JRNL        AUTH 2 C.DAS                                                        
JRNL        TITL   THE CO-CRYSTAL STRUCTURE OF UBIQUITIN CARBOXY-TERMINAL       
JRNL        TITL 2 HYDROLASE L1 (UCHL1) WITH A TRIPEPTIDE FLUOROMETHYL KETONE   
JRNL        TITL 3 (Z-VAE(OME)-FMK).                                            
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  3900 2012              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   22617491                                                     
JRNL        DOI    10.1016/J.BMCL.2012.04.124                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20267                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1037                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.8766 -  4.4932    0.99     2978   138  0.1788 0.2368        
REMARK   3     2  4.4932 -  3.5675    1.00     2842   132  0.1517 0.1803        
REMARK   3     3  3.5675 -  3.1169    1.00     2777   168  0.2139 0.2458        
REMARK   3     4  3.1169 -  2.8321    1.00     2753   162  0.2403 0.3503        
REMARK   3     5  2.8321 -  2.6291    1.00     2747   165  0.2586 0.3077        
REMARK   3     6  2.6291 -  2.4742    0.98     2696   138  0.2801 0.3371        
REMARK   3     7  2.4742 -  2.3503    0.89     2437   134  0.3369 0.3832        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.36                                          
REMARK   3   B_SOL              : 61.66                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.91500                                              
REMARK   3    B22 (A**2) : 8.91500                                              
REMARK   3    B33 (A**2) : -17.83010                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3611                                  
REMARK   3   ANGLE     :  1.048           4856                                  
REMARK   3   CHIRALITY :  0.088            530                                  
REMARK   3   PLANARITY :  0.004            643                                  
REMARK   3   DIHEDRAL  : 16.536           1361                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:136)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1751  16.6399  14.5648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2131 T22:   0.3525                                     
REMARK   3      T33:   0.2420 T12:   0.0259                                     
REMARK   3      T13:   0.0212 T23:   0.0842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5907 L22:   5.6719                                     
REMARK   3      L33:   3.8446 L12:  -0.4424                                     
REMARK   3      L13:   0.8571 L23:   1.2130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1107 S12:  -0.0529 S13:  -0.0454                       
REMARK   3      S21:   0.0049 S22:   0.2731 S23:   0.2469                       
REMARK   3      S31:  -0.1560 S32:  -0.4633 S33:  -0.1397                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 137:159)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4842  11.0402  23.1044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5280 T22:   0.5180                                     
REMARK   3      T33:   0.4218 T12:   0.1397                                     
REMARK   3      T13:   0.0035 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5915 L22:   1.5880                                     
REMARK   3      L33:   9.0049 L12:   3.0473                                     
REMARK   3      L13:  -6.6302 L23:  -3.5284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8111 S12:  -0.5419 S13:  -0.8537                       
REMARK   3      S21:  -0.0751 S22:   0.4172 S23:  -0.2754                       
REMARK   3      S31:   0.8797 S32:   0.6685 S33:   0.3267                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 160:207)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0017  13.3556   3.4491              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3822 T22:   0.4472                                     
REMARK   3      T33:   0.2619 T12:   0.0236                                     
REMARK   3      T13:   0.0059 T23:   0.0383                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0015 L22:   8.0962                                     
REMARK   3      L33:   7.4248 L12:  -1.4749                                     
REMARK   3      L13:   5.4123 L23:  -2.0489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0420 S12:   0.5642 S13:  -0.2451                       
REMARK   3      S21:  -0.7443 S22:   0.1874 S23:   0.4170                       
REMARK   3      S31:   0.1659 S32:  -0.2229 S33:  -0.2159                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 208:223)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9014   3.8756   9.5624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4350 T22:   0.5138                                     
REMARK   3      T33:   0.5501 T12:  -0.1347                                     
REMARK   3      T13:   0.0280 T23:   0.0346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5202 L22:   8.1477                                     
REMARK   3      L33:   4.8391 L12:  -5.2664                                     
REMARK   3      L13:  -2.7472 L23:   4.9500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1862 S12:   0.2716 S13:   0.0443                       
REMARK   3      S21:  -0.1999 S22:   0.5389 S23:  -0.2362                       
REMARK   3      S31:   0.0577 S32:  -0.1825 S33:  -0.2875                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 1:45)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  54.8744  22.0824  44.8497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4388 T22:   0.4528                                     
REMARK   3      T33:   0.4536 T12:   0.0288                                     
REMARK   3      T13:   0.1567 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5730 L22:   6.4432                                     
REMARK   3      L33:   7.8430 L12:  -0.9465                                     
REMARK   3      L13:   2.9828 L23:   2.4268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1544 S12:   0.2524 S13:   0.4820                       
REMARK   3      S21:  -0.4520 S22:   0.2010 S23:  -0.9860                       
REMARK   3      S31:  -0.8570 S32:   0.6289 S33:  -0.3269                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 46:69)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  44.4992  15.6694  61.6965              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4745 T22:   0.7314                                     
REMARK   3      T33:   0.3201 T12:  -0.0556                                     
REMARK   3      T13:   0.0121 T23:  -0.0587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2654 L22:   8.2477                                     
REMARK   3      L33:   4.1422 L12:   1.4365                                     
REMARK   3      L13:  -0.4841 L23:  -0.2635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2031 S12:  -0.5834 S13:  -0.4085                       
REMARK   3      S21:   1.0916 S22:  -0.1353 S23:   0.3504                       
REMARK   3      S31:  -0.0759 S32:  -1.3217 S33:  -0.0368                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 70:136)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5733  26.7631  47.3766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6049 T22:   0.6702                                     
REMARK   3      T33:   0.4736 T12:   0.2618                                     
REMARK   3      T13:  -0.0808 T23:  -0.0306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0121 L22:   4.8274                                     
REMARK   3      L33:   4.9971 L12:  -0.2953                                     
REMARK   3      L13:  -0.7897 L23:   2.9375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1364 S12:   0.2842 S13:   0.5280                       
REMARK   3      S21:  -0.5247 S22:  -0.1766 S23:   0.4168                       
REMARK   3      S31:  -1.2450 S32:  -1.0133 S33:   0.0176                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 137:159)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  46.7575  10.6179  40.4082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6567 T22:   0.5312                                     
REMARK   3      T33:   0.4898 T12:   0.2428                                     
REMARK   3      T13:   0.1002 T23:  -0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1641 L22:   3.0443                                     
REMARK   3      L33:   4.1343 L12:   3.9454                                     
REMARK   3      L13:  -4.6078 L23:  -3.4781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0984 S12:   0.1664 S13:  -0.8112                       
REMARK   3      S21:  -0.6641 S22:  -0.5297 S23:  -0.0365                       
REMARK   3      S31:   0.3441 S32:   0.2036 S33:   0.5282                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 160:189)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  45.1064  25.5604  58.7128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5241 T22:   0.4365                                     
REMARK   3      T33:   0.3941 T12:   0.0657                                     
REMARK   3      T13:  -0.0564 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1196 L22:   3.5896                                     
REMARK   3      L33:   8.0553 L12:  -4.5360                                     
REMARK   3      L13:  -0.6193 L23:   2.4615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0316 S12:  -0.1922 S13:   0.7677                       
REMARK   3      S21:   0.6923 S22:  -0.1819 S23:   0.0167                       
REMARK   3      S31:  -0.7578 S32:  -0.5968 S33:   0.1190                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 190:207)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  55.2659  24.7432  62.7919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5265 T22:   0.6773                                     
REMARK   3      T33:   0.6273 T12:   0.0300                                     
REMARK   3      T13:  -0.0594 T23:  -0.1117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8676 L22:   2.9590                                     
REMARK   3      L33:   7.4628 L12:   2.3223                                     
REMARK   3      L13:   1.6934 L23:  -0.7324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3846 S12:  -0.9621 S13:   0.3042                       
REMARK   3      S21:   1.6720 S22:   0.2097 S23:  -0.2050                       
REMARK   3      S31:   0.1403 S32:  -0.0337 S33:  -0.4778                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 208:223)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6024  17.7255  53.7477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3839 T22:   0.5043                                     
REMARK   3      T33:   0.4467 T12:  -0.0803                                     
REMARK   3      T13:  -0.0738 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5371 L22:   4.1077                                     
REMARK   3      L33:   9.0101 L12:  -5.7101                                     
REMARK   3      L13:   3.9145 L23:  -1.0637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:  -0.5052 S13:  -0.0865                       
REMARK   3      S21:   0.5219 S22:   0.3936 S23:  -0.5478                       
REMARK   3      S31:  -0.6031 S32:   0.3883 S33:  -0.3503                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4DM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070506.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
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                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20326                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 12.900                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 48.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2ETL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M AMMONIUM SULFATE, 0.1M HEPES, PH    
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z                                          
REMARK 290       4555   Y+1/2,-X+1/2,Z                                          
REMARK 290       5555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       6555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       55.00550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       55.00550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       55.00550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       55.00550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       55.00550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.00550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       55.00550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.00550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
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        0.00000            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Y                                  
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 A 308  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     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     LEU B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
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    LYS A  71       -3.02     69.40                                   
REMARK 500    CYS A 152      120.24    107.76                                   
REMARK 500    ASP A 155      -69.25     46.72                                   
REMARK 500    CYS B 152      121.72    110.21                                   
REMARK 500    VAL B 154       -4.06     81.65                                   
REMARK 500    LYS B 157       33.48    -63.01                                   
REMARK 500    ALA B 222      118.67    -37.96                                   
REMARK 500    ALA Y   3      -60.99     54.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    CYS A 152        18.4      L          L   OUTSIDE RANGE           
REMARK 500    CYS B 152        19.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL Y   2        22.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN X OF TRIPEPTIDE             
REMARK 800  FLUOROMETHYL KETONE INHIBITOR Z-VAE(OME)-FMK                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN Y OF TRIPEPTIDE             
REMARK 800  FLUOROMETHYL KETONE INHIBITOR Z-VAE(OME)-FMK                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ETL   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITHOUT FLUOROMETHYL KETONE INHBITOR                
DBREF  4DM9 A    1   223  UNP    P09936   UCHL1_HUMAN      1    223             
DBREF  4DM9 B    1   223  UNP    P09936   UCHL1_HUMAN      1    223             
DBREF  4DM9 X    1     5  PDB    4DM9     4DM9             1      5             
DBREF  4DM9 Y    1     5  PDB    4DM9     4DM9             1      5             
SEQADV 4DM9 GLY A   -4  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 PRO A   -3  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 LEU A   -2  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 GLY A   -1  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 SER A    0  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 GLY B   -4  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 PRO B   -3  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 LEU B   -2  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 GLY B   -1  UNP  P09936              EXPRESSION TAG                 
SEQADV 4DM9 SER B    0  UNP  P09936              EXPRESSION TAG                 
SEQRES   1 A  228  GLY PRO LEU GLY SER MET GLN LEU LYS PRO MET GLU ILE          
SEQRES   2 A  228  ASN PRO GLU MET LEU ASN LYS VAL LEU SER ARG LEU GLY          
SEQRES   3 A  228  VAL ALA GLY GLN TRP ARG PHE VAL ASP VAL LEU GLY LEU          
SEQRES   4 A  228  GLU GLU GLU SER LEU GLY SER VAL PRO ALA PRO ALA CYS          
SEQRES   5 A  228  ALA LEU LEU LEU LEU PHE PRO LEU THR ALA GLN HIS GLU          
SEQRES   6 A  228  ASN PHE ARG LYS LYS GLN ILE GLU GLU LEU LYS GLY GLN          
SEQRES   7 A  228  GLU VAL SER PRO LYS VAL TYR PHE MET LYS GLN THR ILE          
SEQRES   8 A  228  GLY ASN SER CYS GLY THR ILE GLY LEU ILE HIS ALA VAL          
SEQRES   9 A  228  ALA ASN ASN GLN ASP LYS LEU GLY PHE GLU ASP GLY SER          
SEQRES  10 A  228  VAL LEU LYS GLN PHE LEU SER GLU THR GLU LYS MET SER          
SEQRES  11 A  228  PRO GLU ASP ARG ALA LYS CYS PHE GLU LYS ASN GLU ALA          
SEQRES  12 A  228  ILE GLN ALA ALA HIS ASP ALA VAL ALA GLN GLU GLY GLN          
SEQRES  13 A  228  CYS ARG VAL ASP ASP LYS VAL ASN PHE HIS PHE ILE LEU          
SEQRES  14 A  228  PHE ASN ASN VAL ASP GLY HIS LEU TYR GLU LEU ASP GLY          
SEQRES  15 A  228  ARG MET PRO PHE PRO VAL ASN HIS GLY ALA SER SER GLU          
SEQRES  16 A  228  ASP THR LEU LEU LYS ASP ALA ALA LYS VAL CYS ARG GLU          
SEQRES  17 A  228  PHE THR GLU ARG GLU GLN GLY GLU VAL ARG PHE SER ALA          
SEQRES  18 A  228  VAL ALA LEU CYS LYS ALA ALA                                  
SEQRES   1 B  228  GLY PRO LEU GLY SER MET GLN LEU LYS PRO MET GLU ILE          
SEQRES   2 B  228  ASN PRO GLU MET LEU ASN LYS VAL LEU SER ARG LEU GLY          
SEQRES   3 B  228  VAL ALA GLY GLN TRP ARG PHE VAL ASP VAL LEU GLY LEU          
SEQRES   4 B  228  GLU GLU GLU SER LEU GLY SER VAL PRO ALA PRO ALA CYS          
SEQRES   5 B  228  ALA LEU LEU LEU LEU PHE PRO LEU THR ALA GLN HIS GLU          
SEQRES   6 B  228  ASN PHE ARG LYS LYS GLN ILE GLU GLU LEU LYS GLY GLN          
SEQRES   7 B  228  GLU VAL SER PRO LYS VAL TYR PHE MET LYS GLN THR ILE          
SEQRES   8 B  228  GLY ASN SER CYS GLY THR ILE GLY LEU ILE HIS ALA VAL          
SEQRES   9 B  228  ALA ASN ASN GLN ASP LYS LEU GLY PHE GLU ASP GLY SER          
SEQRES  10 B  228  VAL LEU LYS GLN PHE LEU SER GLU THR GLU LYS MET SER          
SEQRES  11 B  228  PRO GLU ASP ARG ALA LYS CYS PHE GLU LYS ASN GLU ALA          
SEQRES  12 B  228  ILE GLN ALA ALA HIS ASP ALA VAL ALA GLN GLU GLY GLN          
SEQRES  13 B  228  CYS ARG VAL ASP ASP LYS VAL ASN PHE HIS PHE ILE LEU          
SEQRES  14 B  228  PHE ASN ASN VAL ASP GLY HIS LEU TYR GLU LEU ASP GLY          
SEQRES  15 B  228  ARG MET PRO PHE PRO VAL ASN HIS GLY ALA SER SER GLU          
SEQRES  16 B  228  ASP THR LEU LEU LYS ASP ALA ALA LYS VAL CYS ARG GLU          
SEQRES  17 B  228  PHE THR GLU ARG GLU GLN GLY GLU VAL ARG PHE SER ALA          
SEQRES  18 B  228  VAL ALA LEU CYS LYS ALA ALA                                  
SEQRES   1 X    5  PHQ VAL ALA GME CF0                                          
SEQRES   1 Y    5  PHQ VAL ALA GME CF0                                          
MODRES 4DM9 GME X    4  GLU  5-O-METHYL-GLUTAMIC ACID                           
MODRES 4DM9 GME Y    4  GLU  5-O-METHYL-GLUTAMIC ACID                           
HET    PHQ  X   1      10                                                       
HET    GME  X   4      10                                                       
HET    CF0  X   5       1                                                       
HET    PHQ  Y   1      10                                                       
HET    GME  Y   4      10                                                       
HET    CF0  Y   5       1                                                       
HETNAM     PHQ BENZYL CHLOROCARBONATE                                           
HETNAM     GME 5-O-METHYL-GLUTAMIC ACID                                         
HETNAM     CF0 FLUOROMETHANE                                                    
HETSYN     GME (2S)-2-AMINO-5-METHOXY-5-OXOPENTANOIC ACID                       
HETSYN     CF0 FLUORO METHYL GROUP                                              
FORMUL   3  PHQ    2(C8 H7 CL O2)                                               
FORMUL   3  GME    2(C6 H11 N O4)                                               
FORMUL   3  CF0    2(C H3 F)                                                    
FORMUL   5  HOH   *42(H2 O)                                                     
HELIX    1   1 ASN A    9  LEU A   20  1                                  12    
HELIX    2   2 GLU A   35  SER A   41  1                                   7    
HELIX    3   3 THR A   56  LYS A   71  1                                  16    
HELIX    4   4 SER A   89  ASN A  101  1                                  13    
HELIX    5   5 SER A  112  THR A  121  1                                  10    
HELIX    6   6 SER A  125  LYS A  135  1                                  11    
HELIX    7   7 ASN A  136  GLN A  148  1                                  13    
HELIX    8   8 SER A  189  ASP A  191  5                                   3    
HELIX    9   9 THR A  192  GLU A  208  1                                  17    
HELIX   10  10 ASN B    9  LEU B   20  1                                  12    
HELIX   11  11 GLU B   35  SER B   41  1                                   7    
HELIX   12  12 THR B   56  LEU B   70  1                                  15    
HELIX   13  13 SER B   89  ASN B  101  1                                  13    
HELIX   14  14 SER B  112  THR B  121  1                                  10    
HELIX   15  15 SER B  125  LYS B  135  1                                  11    
HELIX   16  16 ASN B  136  GLN B  148  1                                  13    
HELIX   17  17 SER B  189  ASP B  191  5                                   3    
HELIX   18  18 THR B  192  GLU B  208  1                                  17    
SHEET    1   A 6 TRP A  26  VAL A  31  0                                        
SHEET    2   A 6 SER A 215  LYS A 221 -1  O  CYS A 220   N  ARG A  27           
SHEET    3   A 6 ALA A  46  PRO A  54 -1  N  LEU A  52   O  SER A 215           
SHEET    4   A 6 PHE A 160  VAL A 168 -1  O  ILE A 163   N  LEU A  51           
SHEET    5   A 6 HIS A 171  LEU A 175 -1  O  TYR A 173   N  ASN A 166           
SHEET    6   A 6 VAL A 183  ALA A 187 -1  O  HIS A 185   N  LEU A 172           
SHEET    1   B 6 TRP B  26  VAL B  31  0                                        
SHEET    2   B 6 SER B 215  LYS B 221 -1  O  CYS B 220   N  ARG B  27           
SHEET    3   B 6 ALA B  46  PRO B  54 -1  N  LEU B  52   O  SER B 215           
SHEET    4   B 6 PHE B 160  VAL B 168 -1  O  ILE B 163   N  LEU B  51           
SHEET    5   B 6 HIS B 171  LEU B 175 -1  O  TYR B 173   N  ASN B 166           
SHEET    6   B 6 VAL B 183  ALA B 187 -1  O  HIS B 185   N  LEU B 172           
LINK         C1  PHQ X   1                 N   VAL X   2     1555   1555  1.43  
LINK         C   ALA X   3                 N   GME X   4     1555   1555  1.33  
LINK         C   GME X   4                 C1  CF0 X   5     1555   1555  1.54  
LINK         C1  PHQ Y   1                 N   VAL Y   2     1555   1555  1.43  
LINK         C   ALA Y   3                 N   GME Y   4     1555   1555  1.33  
LINK         C   GME Y   4                 C1  CF0 Y   5     1555   1555  1.54  
LINK         SG  CYS A  90                 C1  CF0 X   5     1555   1555  1.80  
LINK         SG  CYS B  90                 C1  CF0 Y   5     1555   1555  1.80  
CISPEP   1 ALA A   44    PRO A   45          0        -2.35                     
CISPEP   2 ALA B   44    PRO B   45          0        -2.39                     
SITE     1 AC1 18 MET A   6  VAL A  31  LEU A  32  GLY A  33                    
SITE     2 AC1 18 LEU A  34  GLN A  84  GLY A  87  ASN A  88                    
SITE     3 AC1 18 SER A  89  CYS A  90  ARG A 153  ASN A 159                    
SITE     4 AC1 18 PHE A 160  ARG A 178  PHE A 214  SER A 215                    
SITE     5 AC1 18 ALA A 216  HOH X 101                                          
SITE     1 AC2 17 VAL B  31  LEU B  32  GLY B  33  LEU B  34                    
SITE     2 AC2 17 GLN B  84  GLY B  87  ASN B  88  SER B  89                    
SITE     3 AC2 17 CYS B  90  ARG B 153  LYS B 157  VAL B 158                    
SITE     4 AC2 17 ASN B 159  PHE B 160  ARG B 178  PHE B 214                    
SITE     5 AC2 17 HOH Y 101                                                     
CRYST1  110.011  110.011   78.745  90.00  90.00  90.00 P 4 21 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      0.009090  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009090  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012699        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system