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Database: PDB
Entry: 5LYH
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HEADER    TRANSFERASE                             28-SEP-16   5LYH              
TITLE     HUMAN PARP14 (ARTD8), CATALYTIC FRAGMENT IN COMPLEX WITH INHIBITOR H10
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE 14;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PARP-14,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 8,     
COMPND   5 ARTD8,B AGGRESSIVE LYMPHOMA PROTEIN 2;                               
COMPND   6 EC: 2.4.2.30;                                                        
COMPND   7 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: PARP14, BAL2, KIAA1268;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE;                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    ADP-RIBOSYLATION, INHIBITOR COMPLEX, TRANSFERASE DOMAIN, TRANSFERASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KARLBERG,A.G.THORSELL,H.SCHULER                                     
REVDAT   4   17-JAN-24 5LYH    1       REMARK                                   
REVDAT   3   24-JAN-18 5LYH    1       SOURCE REMARK                            
REVDAT   2   11-JAN-17 5LYH    1       JRNL                                     
REVDAT   1   21-DEC-16 5LYH    0                                                
JRNL        AUTH   B.PENG,A.G.THORSELL,T.KARLBERG,H.SCHULER,S.Q.YAO             
JRNL        TITL   SMALL MOLECULE MICROARRAY BASED DISCOVERY OF PARP14          
JRNL        TITL 2 INHIBITORS.                                                  
JRNL        REF    ANGEW. CHEM. INT. ED. ENGL.   V.  56   248 2017              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   27918638                                                     
JRNL        DOI    10.1002/ANIE.201609655                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24403                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2004                            
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) : 2.17                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.22                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1711                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 138                          
REMARK   3   BIN FREE R VALUE                    : 0.4320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2987                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 19                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -31.74000                                            
REMARK   3    B22 (A**2) : -31.74000                                            
REMARK   3    B33 (A**2) : 63.49000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.046         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.036         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.206         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3161 ; 0.015 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2833 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4297 ; 1.751 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6498 ; 1.271 ; 3.007       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   365 ; 7.753 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   168 ;33.279 ;24.226       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   481 ;16.829 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;23.782 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   435 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3664 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   824 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1466 ; 5.162 ; 5.944       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1465 ; 5.157 ; 5.943       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1826 ; 7.377 ; 8.902       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1827 ; 7.375 ; 8.903       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1692 ; 4.945 ; 6.366       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1693 ; 4.944 ; 6.364       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2469 ; 7.341 ; 9.433       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3404 ;10.628 ;47.368       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3404 ;10.627 ;47.365       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A  1613   1801       B  1613   1801   20500  0.10  0.05     
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.658                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : -H,-K,L                                         
REMARK   3      TWIN FRACTION : 0.342                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 5LYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001597.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P13 (MX1)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97999                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26408                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.170                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 9.500                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.13000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4F1L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG3350, 0.225M SODIUM MALONATE,   
REMARK 280  PH 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.69333            
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       81.38667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       81.38667            
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       40.69333            
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 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     SER A  1609                                                      
REMARK 465     MET A  1610                                                      
REMARK 465     ASP A  1611                                                      
REMARK 465     TYR A  1701                                                      
REMARK 465     ALA A  1702                                                      
REMARK 465     GLY A  1703                                                      
REMARK 465     LYS A  1704                                                      
REMARK 465     ASN A  1705                                                      
REMARK 465     SER B  1609                                                      
REMARK 465     MET B  1610                                                      
REMARK 465     ASP B  1611                                                      
REMARK 465     MET B  1612                                                      
REMARK 465     ALA B  1702                                                      
REMARK 465     GLY B  1703                                                      
REMARK 465     LYS B  1704                                                      
REMARK 465     ASN B  1705                                                      
REMARK 465     ALA B  1706                                                      
REMARK 465     VAL B  1707                                                      
REMARK 465     ALA B  1708                                                      
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 A1613      145.55     84.51                                   
REMARK 500    ASN A1698      137.75     -3.56                                   
REMARK 500    LYS A1711       72.73   -102.39                                   
REMARK 500    TYR A1727      -65.95   -103.97                                   
REMARK 500    PRO A1793       69.09    -69.87                                   
REMARK 500    GLN B1614      -49.06     81.20                                   
REMARK 500    GLN B1614      -47.64     80.47                                   
REMARK 500    ASN B1698     -168.05    -71.60                                   
REMARK 500    ARG B1699     -105.76     54.93                                   
REMARK 500    LYS B1711       70.46   -102.61                                   
REMARK 500    TYR B1727      -66.03   -104.31                                   
REMARK 500    ASN B1752      -94.89   -130.25                                   
REMARK 500    HIS B1753      -43.58    168.99                                   
REMARK 500    ASN B1776      108.56   -160.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A 1612     LYS A 1613                 -136.10                    
REMARK 500 ARG B 1699     SER B 1700                  -30.41                    
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 residue 7B8 A 1901                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7B8 B 1901                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5LXP   RELATED DB: PDB                                   
REMARK 900 5LXP CONTAINS THE SAME PROTEIN COMPLEXED WITH INHIBITOR H5           
DBREF  5LYH A 1611  1801  UNP    Q460N5   PAR14_HUMAN   1530   1720             
DBREF  5LYH B 1611  1801  UNP    Q460N5   PAR14_HUMAN   1530   1720             
SEQADV 5LYH SER A 1609  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 5LYH MET A 1610  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 5LYH SER B 1609  UNP  Q460N5              EXPRESSION TAG                 
SEQADV 5LYH MET B 1610  UNP  Q460N5              EXPRESSION TAG                 
SEQRES   1 A  193  SER MET ASP MET LYS GLN GLN ASN PHE CYS VAL VAL GLU          
SEQRES   2 A  193  LEU LEU PRO SER ASP PRO GLU TYR ASN THR VAL ALA SER          
SEQRES   3 A  193  LYS PHE ASN GLN THR CYS SER HIS PHE ARG ILE GLU LYS          
SEQRES   4 A  193  ILE GLU ARG ILE GLN ASN PRO ASP LEU TRP ASN SER TYR          
SEQRES   5 A  193  GLN ALA LYS LYS LYS THR MET ASP ALA LYS ASN GLY GLN          
SEQRES   6 A  193  THR MET ASN GLU LYS GLN LEU PHE HIS GLY THR ASP ALA          
SEQRES   7 A  193  GLY SER VAL PRO HIS VAL ASN ARG ASN GLY PHE ASN ARG          
SEQRES   8 A  193  SER TYR ALA GLY LYS ASN ALA VAL ALA TYR GLY LYS GLY          
SEQRES   9 A  193  THR TYR PHE ALA VAL ASN ALA ASN TYR SER ALA ASN ASP          
SEQRES  10 A  193  THR TYR SER ARG PRO ASP ALA ASN GLY ARG LYS HIS VAL          
SEQRES  11 A  193  TYR TYR VAL ARG VAL LEU THR GLY ILE TYR THR HIS GLY          
SEQRES  12 A  193  ASN HIS SER LEU ILE VAL PRO PRO SER LYS ASN PRO GLN          
SEQRES  13 A  193  ASN PRO THR ASP LEU TYR ASP THR VAL THR ASP ASN VAL          
SEQRES  14 A  193  HIS HIS PRO SER LEU PHE VAL ALA PHE TYR ASP TYR GLN          
SEQRES  15 A  193  ALA TYR PRO GLU TYR LEU ILE THR PHE ARG LYS                  
SEQRES   1 B  193  SER MET ASP MET LYS GLN GLN ASN PHE CYS VAL VAL GLU          
SEQRES   2 B  193  LEU LEU PRO SER ASP PRO GLU TYR ASN THR VAL ALA SER          
SEQRES   3 B  193  LYS PHE ASN GLN THR CYS SER HIS PHE ARG ILE GLU LYS          
SEQRES   4 B  193  ILE GLU ARG ILE GLN ASN PRO ASP LEU TRP ASN SER TYR          
SEQRES   5 B  193  GLN ALA LYS LYS LYS THR MET ASP ALA LYS ASN GLY GLN          
SEQRES   6 B  193  THR MET ASN GLU LYS GLN LEU PHE HIS GLY THR ASP ALA          
SEQRES   7 B  193  GLY SER VAL PRO HIS VAL ASN ARG ASN GLY PHE ASN ARG          
SEQRES   8 B  193  SER TYR ALA GLY LYS ASN ALA VAL ALA TYR GLY LYS GLY          
SEQRES   9 B  193  THR TYR PHE ALA VAL ASN ALA ASN TYR SER ALA ASN ASP          
SEQRES  10 B  193  THR TYR SER ARG PRO ASP ALA ASN GLY ARG LYS HIS VAL          
SEQRES  11 B  193  TYR TYR VAL ARG VAL LEU THR GLY ILE TYR THR HIS GLY          
SEQRES  12 B  193  ASN HIS SER LEU ILE VAL PRO PRO SER LYS ASN PRO GLN          
SEQRES  13 B  193  ASN PRO THR ASP LEU TYR ASP THR VAL THR ASP ASN VAL          
SEQRES  14 B  193  HIS HIS PRO SER LEU PHE VAL ALA PHE TYR ASP TYR GLN          
SEQRES  15 B  193  ALA TYR PRO GLU TYR LEU ILE THR PHE ARG LYS                  
HET    7B8  A1901      39                                                       
HET    7B8  B1901      39                                                       
HETNAM     7B8 3-[2-[4-[2-[[4-[(3-AMINOCARBONYLPHENYL)AMINO]-4-                 
HETNAM   2 7B8  OXIDANYLIDENE-BUTANOYL]AMINO]ETHYL]-1,2,3-TRIAZOL-1-            
HETNAM   3 7B8  YL]ETHYLSULFAMOYL]BENZOIC ACID                                  
FORMUL   3  7B8    2(C24 H27 N7 O7 S)                                           
FORMUL   5  HOH   *19(H2 O)                                                     
HELIX    1 AA1 ASP A 1626  SER A 1641  1                                  16    
HELIX    2 AA2 ASN A 1653  GLY A 1672  1                                  20    
HELIX    3 AA3 SER A 1688  GLY A 1696  1                                   9    
HELIX    4 AA4 ASN A 1718  ASN A 1724  1                                   7    
HELIX    5 AA5 ASP B 1626  SER B 1641  1                                  16    
HELIX    6 AA6 ASN B 1653  GLY B 1672  1                                  20    
HELIX    7 AA7 SER B 1688  GLY B 1696  1                                   9    
HELIX    8 AA8 ASN B 1718  ASN B 1724  1                                   7    
SHEET    1 AA1 5 CYS A1618  GLU A1621  0                                        
SHEET    2 AA1 5 ARG A1644  GLN A1652 -1  O  ARG A1650   N  VAL A1620           
SHEET    3 AA1 5 ALA A1791  ARG A1800 -1  O  ARG A1800   N  ARG A1644           
SHEET    4 AA1 5 LYS A1736  LEU A1744 -1  N  VAL A1738   O  ILE A1797           
SHEET    5 AA1 5 GLU A1677  THR A1684 -1  N  LEU A1680   O  VAL A1741           
SHEET    1 AA2 4 THR A1713  ALA A1716  0                                        
SHEET    2 AA2 4 LEU A1782  ALA A1785 -1  O  ALA A1785   N  THR A1713           
SHEET    3 AA2 4 THR A1772  THR A1774 -1  N  VAL A1773   O  VAL A1784           
SHEET    4 AA2 4 TYR A1748  HIS A1750  1  N  THR A1749   O  THR A1774           
SHEET    1 AA3 5 CYS B1618  GLU B1621  0                                        
SHEET    2 AA3 5 ARG B1644  GLN B1652 -1  O  GLN B1652   N  CYS B1618           
SHEET    3 AA3 5 ALA B1791  ARG B1800 -1  O  GLU B1794   N  ILE B1651           
SHEET    4 AA3 5 LYS B1736  LEU B1744 -1  N  VAL B1738   O  ILE B1797           
SHEET    5 AA3 5 GLU B1677  THR B1684 -1  N  LEU B1680   O  VAL B1741           
SHEET    1 AA4 4 THR B1713  ALA B1716  0                                        
SHEET    2 AA4 4 LEU B1782  ALA B1785 -1  O  ALA B1785   N  THR B1713           
SHEET    3 AA4 4 THR B1772  THR B1774 -1  N  VAL B1773   O  VAL B1784           
SHEET    4 AA4 4 TYR B1748  THR B1749  1  N  THR B1749   O  THR B1774           
SSBOND   1 CYS A 1618    CYS A 1618                          1555   6765  2.19  
SSBOND   2 CYS B 1618    CYS B 1618                          1555   6765  2.07  
SITE     1 AC1 18 HIS A1682  GLY A1683  THR A1684  SER A1688                    
SITE     2 AC1 18 HIS A1691  PHE A1697  ASN A1698  SER A1700                    
SITE     3 AC1 18 VAL A1707  GLY A1712  THR A1713  TYR A1714                    
SITE     4 AC1 18 PHE A1715  ALA A1716  TYR A1721  SER A1722                    
SITE     5 AC1 18 TYR A1727  ASN B1724                                          
SITE     1 AC2 15 ASN A1724  HOH A2007  HIS B1682  GLY B1683                    
SITE     2 AC2 15 THR B1684  SER B1688  HIS B1691  VAL B1692                    
SITE     3 AC2 15 SER B1700  GLY B1712  TYR B1714  TYR B1721                    
SITE     4 AC2 15 SER B1722  TYR B1727  HOH B2002                               
CRYST1   83.032   83.032  122.080  90.00  90.00 120.00 P 31 2 1     12          
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      0.012044  0.006953  0.000000        0.00000                         
SCALE2      0.000000  0.013907  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008191        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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