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Database: PDB
Entry: 5A0A
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HEADER    HYDROLASE                               17-APR-15   5A0A              
TITLE     CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A      
TITLE    2 DIHYDROPYRIMIDONE INHIBITOR                                          
CAVEAT     5A0A    NAG E 1247 HAS LONG BOND BETWEEN C1 AND C4 OF E1245          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUTROPHIL ELASTASE;                                       
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: BONE MARROW SERINE PROTEASE, ELASTASE-2, HUMAN LEUKOCYTE EL 
COMPND   5 ASTASE, HLE, MEDULLASIN, PMN ELASTASE, ELASTASE, HLE, MEDULIASIN, PMN
COMPND   6 ELASTASE;                                                            
COMPND   7 EC: 3.4.21.37                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRYPSIN FAMILY FOLD, PROTEASE, HYDROLASE, HYDROLASE- INHIBITOR        
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.VONNUSSBAUM,V.M.-J.LI,S.ALLERHEILIGEN,S.ANLAUF,L.BAERFACKER,        
AUTHOR   2 M.BECHEM,M.DELBECK,M.F.FITZGERALD,M.GERISCH,H.GIELEN-HAERTWIG,       
AUTHOR   3 H.HANING,D.KARTHAUS,D.LANG,K.LUSTIG,D.MEIBOM,J.MITTENDORF,           
AUTHOR   4 U.ROSENTRETER,M.SCHAEFER,S.SCHAEFER,J.SCHAMBERGER,L.A.TELAN,         
AUTHOR   5 A.TERSTEEGEN                                                         
REVDAT   2   22-MAR-17 5A0A    1       JRNL                                     
REVDAT   1   19-AUG-15 5A0A    0                                                
JRNL        AUTH   F.VON NUSSBAUM,V.M.LI,S.ALLERHEILIGEN,S.ANLAUF,L.BARFACKER,  
JRNL        AUTH 2 M.BECHEM,M.DELBECK,M.F.FITZGERALD,M.GERISCH,                 
JRNL        AUTH 3 H.GIELEN-HAERTWIG,H.HANING,D.KARTHAUS,D.LANG,K.LUSTIG,       
JRNL        AUTH 4 D.MEIBOM,J.MITTENDORF,U.ROSENTRETER,M.SCHAFER,S.SCHAFER,     
JRNL        AUTH 5 J.SCHAMBERGER,L.A.TELAN,A.TERSTEEGEN                         
JRNL        TITL   FREEZING THE BIOACTIVE CONFORMATION TO BOOST POTENCY: THE    
JRNL        TITL 2 IDENTIFICATION OF BAY 85-8501, A SELECTIVE AND POTENT        
JRNL        TITL 3 INHIBITOR OF HUMAN NEUTROPHIL ELASTASE FOR PULMONARY         
JRNL        TITL 4 DISEASES.                                                    
JRNL        REF    CHEMMEDCHEM                   V.  10  1163 2015              
JRNL        REFN                   ESSN 1860-7187                               
JRNL        PMID   26083237                                                     
JRNL        DOI    10.1002/CMDC.201500131                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 18923                          
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 + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 817                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.78                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1208                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 46                           
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1617                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 106                                     
REMARK   3   SOLVENT ATOMS            : 182                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.47000                                             
REMARK   3    B12 (A**2) : 0.16000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.127         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.896         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1762 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2405 ; 1.520 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   214 ; 6.402 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   282 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1308 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   797 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   139 ; 0.125 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    55 ; 0.194 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.315 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1064 ; 0.864 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1701 ; 1.504 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   698 ; 2.376 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   704 ; 3.862 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 5A0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-63626.                                       
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                             : NULL                               
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          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54179                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH MAR IP                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 1.000                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.88000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1PPG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28%PEG4000,0.1MTRIS/HCL AT PH            
REMARK 280  8.2,0.7MLICL                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       34.79150            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       34.79150            
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       34.79150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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 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     ASN E   147                                                      
REMARK 465     ARG E   148                                                      
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   O4   NAG E  1245     C1   NAG E  1247              2.01            
REMARK 500   NH1  ARG E   128     O    HOH E  2103              2.04            
REMARK 500   O    HOH E  2033     O    HOH E  2052              2.07            
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    ARG E  36       56.20     25.32                                   
REMARK 500    HIS E  71      -59.34   -136.57                                   
REMARK 500    ASN E  92       45.85   -140.97                                   
REMARK 500    SER E 195      126.96    -36.02                                   
REMARK 500    LEU E 223      -65.95   -129.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG E 1247                                                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  7-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "EB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JJS E 1244                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 1247                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE E 1250                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  E1248 through FUC E1249 bound to ASN E 109                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  E1245 through FUC E1246 bound to ASN E 159                          
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5A09   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A     
REMARK 900 DIHYDROPYRIMIDONE INHIBITOR                                          
REMARK 900 RELATED ID: 5A0B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A     
REMARK 900 DIHYDROPYRIMIDONE INHIBITOR                                          
REMARK 900 RELATED ID: 5A0C   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NEUTROPHIL ELASTASE IN COMPLEX WITH A     
REMARK 900 DIHYDROPYRIMIDONE INHIBITOR                                          
DBREF  5A0A E   16   243  UNP    P08246   ELNE_HUMAN      30    247             
SEQRES   1 E  218  ILE VAL GLY GLY ARG ARG ALA ARG PRO HIS ALA TRP PRO          
SEQRES   2 E  218  PHE MET VAL SER LEU GLN LEU ARG GLY GLY HIS PHE CYS          
SEQRES   3 E  218  GLY ALA THR LEU ILE ALA PRO ASN PHE VAL MET SER ALA          
SEQRES   4 E  218  ALA HIS CYS VAL ALA ASN VAL ASN VAL ARG ALA VAL ARG          
SEQRES   5 E  218  VAL VAL LEU GLY ALA HIS ASN LEU SER ARG ARG GLU PRO          
SEQRES   6 E  218  THR ARG GLN VAL PHE ALA VAL GLN ARG ILE PHE GLU ASN          
SEQRES   7 E  218  GLY TYR ASP PRO VAL ASN LEU LEU ASN ASP ILE VAL ILE          
SEQRES   8 E  218  LEU GLN LEU ASN GLY SER ALA THR ILE ASN ALA ASN VAL          
SEQRES   9 E  218  GLN VAL ALA GLN LEU PRO ALA GLN GLY ARG ARG LEU GLY          
SEQRES  10 E  218  ASN GLY VAL GLN CYS LEU ALA MET GLY TRP GLY LEU LEU          
SEQRES  11 E  218  GLY ARG ASN ARG GLY ILE ALA SER VAL LEU GLN GLU LEU          
SEQRES  12 E  218  ASN VAL THR VAL VAL THR SER LEU CYS ARG ARG SER ASN          
SEQRES  13 E  218  VAL CYS THR LEU VAL ARG GLY ARG GLN ALA GLY VAL CYS          
SEQRES  14 E  218  PHE GLY ASP SER GLY SER PRO LEU VAL CYS ASN GLY LEU          
SEQRES  15 E  218  ILE HIS GLY ILE ALA SER PHE VAL ARG GLY GLY CYS ALA          
SEQRES  16 E  218  SER GLY LEU TYR PRO ASP ALA PHE ALA PRO VAL ALA GLN          
SEQRES  17 E  218  PHE VAL ASN TRP ILE ASP SER ILE ILE GLN                      
MODRES 5A0A ASN E  109  ASN  GLYCOSYLATION SITE                                 
MODRES 5A0A ASN E  159  ASN  GLYCOSYLATION SITE                                 
HET    JJS  E1244      29                                                       
HET    NAG  E1245      14                                                       
HET    FUC  E1246      10                                                       
HET    NAG  E1247      14                                                       
HET    NAG  E1248      14                                                       
HET    FUC  E1249      10                                                       
HET    EPE  E1250      15                                                       
HETNAM     JJS 5-[(6R)-5-ETHANOYL-4-METHYL-2-OXIDANYLIDENE-3-[3-                
HETNAM   2 JJS  (TRIFLUOROMETHYL)PHENYL]-1,6-DIHYDROPYRIMIDIN-6-                
HETNAM   3 JJS  YL]PYRIDINE-2-CARBONITRILE                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EPE HEPES                                                            
FORMUL   2  JJS    C20 H15 F3 N4 O2                                             
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   6  EPE    C8 H18 N2 O4 S                                               
FORMUL   7  HOH   *182(H2 O)                                                    
HELIX    1   1 ALA E   55  VAL E   59  5                                   5    
HELIX    2   2 ASN E   63  ALA E   63C 5                                   4    
HELIX    3   3 PHE E  234  GLN E  243  1                                  10    
SHEET    1  EA 8 ARG E  20  ARG E  21  0                                        
SHEET    2  EA 8 GLN E 156  VAL E 163 -1  O  GLU E 157   N  ARG E  20           
SHEET    3  EA 8 VAL E 181  LEU E 184 -1  O  CYS E 182   N  VAL E 163           
SHEET    4  EA 8 ASP E 226  PRO E 230 -1  O  ASP E 226   N  THR E 183           
SHEET    5  EA 8 LEU E 208  PHE E 215 -1  O  ILE E 212   N  ALA E 229           
SHEET    6  EA 8 PRO E 198  CYS E 201 -1  O  LEU E 199   N  HIS E 210           
SHEET    7  EA 8 GLN E 135  GLY E 140 -1  O  LEU E 137   N  VAL E 200           
SHEET    8  EA 8 ARG E  20  ARG E  21  0                                        
SHEET    1  EB 7 MET E  30  LEU E  35  0                                        
SHEET    2  EB 7 GLY E  39  ALA E  48 -1  O  GLY E  39   N  LEU E  35           
SHEET    3  EB 7 PHE E  51  SER E  54 -1  O  PHE E  51   N  ILE E  47           
SHEET    4  EB 7 VAL E 104  LEU E 108 -1  O  VAL E 104   N  SER E  54           
SHEET    5  EB 7 GLN E  81  GLU E  90 -1  N  GLN E  86   O  GLN E 107           
SHEET    6  EB 7 ARG E  65  LEU E  68 -1  O  VAL E  66   N  PHE E  83           
SHEET    7  EB 7 MET E  30  LEU E  35 -1  O  SER E  32   N  VAL E  67           
SSBOND   1 CYS E   42    CYS E   58                          1555   1555  2.05  
SSBOND   2 CYS E  136    CYS E  201                          1555   1555  2.05  
SSBOND   3 CYS E  168    CYS E  182                          1555   1555  2.01  
SSBOND   4 CYS E  191    CYS E  220                          1555   1555  2.04  
LINK         ND2 ASN E 109                 C1  NAG E1248     1555   1555  1.46  
LINK         ND2 ASN E 159                 C1  NAG E1245     1555   1555  1.45  
LINK         O6  NAG E1245                 C1  FUC E1246     1555   1555  1.46  
LINK         O6  NAG E1248                 C1  FUC E1249     1555   1555  1.46  
SITE     1 AC1 17 HIS E  57  TYR E  94  LEU E  99  ASP E 102                    
SITE     2 AC1 17 VAL E 190  CYS E 191  PHE E 192  ASP E 194                    
SITE     3 AC1 17 SER E 195  ALA E 213  SER E 214  PHE E 215                    
SITE     4 AC1 17 VAL E 216  TYR E 224  HOH E2079  HOH E2156                    
SITE     5 AC1 17 HOH E2174                                                     
SITE     1 AC2  4 NAG E1245  FUC E1246  HOH E2178  HOH E2179                    
SITE     1 AC3 11 VAL E 120  GLN E 122  ARG E 128  LEU E 130                    
SITE     2 AC3 11 ASN E 202  LEU E 208  HIS E 210  HOH E2089                    
SITE     3 AC3 11 HOH E2094  HOH E2103  HOH E2104                               
SITE     1 AC4  8 ARG E  63B VAL E  64  ARG E  65  ALA E  84                    
SITE     2 AC4  8 ASN E 109  HOH E2180  HOH E2181  HOH E2182                    
SITE     1 AC5 13 TRP E  27  GLU E  90  GLN E 135  LEU E 137                    
SITE     2 AC5 13 ASN E 159  VAL E 200  CYS E 201  ASN E 202                    
SITE     3 AC5 13 GLY E 207  NAG E1247  HOH E2116  HOH E2117                    
SITE     4 AC5 13 HOH E2177                                                     
CRYST1   72.712   72.712   69.583  90.00  90.00 120.00 P 63          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      0.013753  0.007940  0.000000        0.00000                         
SCALE2      0.000000  0.015880  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014371        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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