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LongText Report for: 7arg-pdb

Name Class
7arg-pdb
HEADER    SIGNALING PROTEIN                       24-OCT-20   7ARG              
TITLE     NOTUM IN COMPLEX WITH ARUK3002704                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HNOTUM;                                                     
COMPND   5 EC: 3.1.1.98;                                                        
COMPND   6 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: NOTUM, OK/SW-CL.30;                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    NOTUM INHIBITOR, SIGNALING PROTEIN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHAO,E.Y.JONES                                                      
REVDAT   1   04-AUG-21 7ARG    0                                                
JRNL        AUTH   Y.ZHAO,F.SVENSSON,D.STEADMAN,S.FREW,A.MONAGHAN,M.BICTASH,    
JRNL        AUTH 2 T.MOREIRA,R.CHALK,W.LU,P.V.FISH,E.Y.JONES                    
JRNL        TITL   STRUCTURAL INSIGHTS INTO NOTUM COVALENT INHIBITION.          
JRNL        REF    J.MED.CHEM.                                2021              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   34292747                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.1C00701                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 95315                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4759                            
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 52.8200 -  3.8500    1.00     3308   134  0.1772 0.1907        
REMARK   3     2  3.8500 -  3.0600    1.00     3113   161  0.1747 0.1883        
REMARK   3     3  3.0600 -  2.6700    1.00     3089   157  0.1834 0.2032        
REMARK   3     4  2.6700 -  2.4300    1.00     3092   153  0.1880 0.2111        
REMARK   3     5  2.4300 -  2.2500    1.00     3070   132  0.1789 0.1935        
REMARK   3     6  2.2500 -  2.1200    1.00     3055   141  0.1699 0.1836        
REMARK   3     7  2.1200 -  2.0100    1.00     3057   168  0.1731 0.1778        
REMARK   3     8  2.0100 -  1.9300    1.00     2990   169  0.1692 0.1926        
REMARK   3     9  1.9300 -  1.8500    1.00     3044   155  0.1731 0.1930        
REMARK   3    10  1.8500 -  1.7900    1.00     3010   159  0.1699 0.1926        
REMARK   3    11  1.7900 -  1.7300    1.00     3039   156  0.1665 0.2001        
REMARK   3    12  1.7300 -  1.6800    1.00     3019   167  0.1737 0.2018        
REMARK   3    13  1.6800 -  1.6400    1.00     2973   183  0.1736 0.1810        
REMARK   3    14  1.6400 -  1.6000    1.00     3027   153  0.1713 0.2324        
REMARK   3    15  1.6000 -  1.5600    1.00     2998   142  0.1754 0.1762        
REMARK   3    16  1.5600 -  1.5300    1.00     3020   135  0.1710 0.1840        
REMARK   3    17  1.5300 -  1.5000    1.00     2995   170  0.1825 0.1938        
REMARK   3    18  1.5000 -  1.4700    1.00     2968   177  0.1824 0.2223        
REMARK   3    19  1.4700 -  1.4400    1.00     2992   161  0.1915 0.2267        
REMARK   3    20  1.4400 -  1.4200    1.00     2979   166  0.1931 0.1981        
REMARK   3    21  1.4200 -  1.4000    1.00     2965   170  0.2130 0.2551        
REMARK   3    22  1.4000 -  1.3800    1.00     2998   155  0.2187 0.2532        
REMARK   3    23  1.3800 -  1.3500    1.00     2959   169  0.2197 0.2420        
REMARK   3    24  1.3500 -  1.3400    0.99     3012   145  0.2217 0.2350        
REMARK   3    25  1.3400 -  1.3200    1.00     2953   182  0.2223 0.2488        
REMARK   3    26  1.3200 -  1.3000    0.99     2963   154  0.2367 0.2645        
REMARK   3    27  1.3000 -  1.2800    0.99     2979   170  0.2381 0.2535        
REMARK   3    28  1.2800 -  1.2700    1.00     2971   157  0.2497 0.2541        
REMARK   3    29  1.2700 -  1.2500    0.99     2931   176  0.2612 0.2743        
REMARK   3    30  1.2500 -  1.2400    0.99     2987   142  0.2796 0.3074        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.120            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 224 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4437 -10.2862  -0.5936              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2009 T22:   0.1459                                     
REMARK   3      T33:   0.1972 T12:   0.0010                                     
REMARK   3      T13:   0.0114 T23:  -0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9837 L22:   1.1993                                     
REMARK   3      L33:   2.0303 L12:   0.1313                                     
REMARK   3      L13:  -0.0533 L23:  -0.1156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0244 S12:   0.0157 S13:  -0.1195                       
REMARK   3      S21:   0.0437 S22:   0.0233 S23:   0.0129                       
REMARK   3      S31:   0.2470 S32:   0.0239 S33:  -0.0209                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 225 THROUGH 286 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2681   1.9562  -1.9730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1432 T22:   0.1430                                     
REMARK   3      T33:   0.1358 T12:  -0.0004                                     
REMARK   3      T13:  -0.0113 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4478 L22:   3.3241                                     
REMARK   3      L33:   1.5894 L12:   0.1375                                     
REMARK   3      L13:   0.2598 L23:   1.5859                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0124 S12:  -0.0500 S13:  -0.0156                       
REMARK   3      S21:   0.2713 S22:   0.0043 S23:  -0.1155                       
REMARK   3      S31:   0.2229 S32:   0.0697 S33:  -0.0598                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 287 THROUGH 320 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5914   1.9462   4.5829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1464 T22:   0.2700                                     
REMARK   3      T33:   0.1901 T12:  -0.0116                                     
REMARK   3      T13:  -0.0413 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1459 L22:   5.2242                                     
REMARK   3      L33:   2.6573 L12:   2.5589                                     
REMARK   3      L13:  -0.4464 L23:  -2.7582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1769 S12:  -0.6292 S13:  -0.2027                       
REMARK   3      S21:   0.1552 S22:  -0.3754 S23:  -0.3560                       
REMARK   3      S31:   0.0033 S32:   0.2078 S33:   0.1676                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 451 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8587  14.1835  -6.2460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1517 T22:   0.1571                                     
REMARK   3      T33:   0.1722 T12:  -0.0054                                     
REMARK   3      T13:  -0.0023 T23:   0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9022 L22:   1.1097                                     
REMARK   3      L33:   0.9339 L12:  -0.1497                                     
REMARK   3      L13:   0.3256 L23:   0.4714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0279 S12:  -0.0317 S13:   0.0955                       
REMARK   3      S21:  -0.0567 S22:   0.0055 S23:   0.0867                       
REMARK   3      S31:  -0.0791 S32:  -0.0513 S33:   0.0375                       
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 7ARG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-OCT-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292111972.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9762                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95627                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 39.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 6TV4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM     
REMARK 280  CITRIC, PH4.6, EVAPORATION, TEMPERATURE 296K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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       29.86500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.01000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.89000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.01000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.86500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.89000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
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 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     GLU A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     GLY A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     GLN A    83                                                      
REMARK 465     GLN A    84                                                      
REMARK 465     LEU A    85                                                      
REMARK 465     ASN A    86                                                      
REMARK 465     GLU A    87                                                      
REMARK 465     THR A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     GLN A   354                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     LYS A   423                                                      
REMARK 465     ALA A   424                                                      
REMARK 465     SER A   425                                                      
REMARK 465     LYS A   426                                                      
REMARK 465     GLY A   452                                                      
REMARK 465     THR A   453                                                      
REMARK 465     LYS A   454                                                      
REMARK 465     HIS A   455                                                      
REMARK 465     HIS A   456                                                      
REMARK 465     HIS A   457                                                      
REMARK 465     HIS A   458                                                      
REMARK 465     HIS A   459                                                      
REMARK 465     HIS A   460                                                      
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   OD1  ASN A   366     NH2  ARG A   369              1.85            
REMARK 500   OE1  GLU A   113     NH1  ARG A   115              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 432   CB  -  CA  -  C   ANGL. DEV. =   7.4 DEGREES          
REMARK 500    CYS A 432   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
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    TRP A 128     -136.27     58.63                                   
REMARK 500    MET A 143       44.21   -141.23                                   
REMARK 500    ALA A 191       52.26   -144.28                                   
REMARK 500    SER A 232     -122.53     58.53                                   
REMARK 500    ASP A 278       44.19    -98.33                                   
REMARK 500    CYS A 279     -120.92     40.28                                   
REMARK 500    VAL A 280      -71.09     68.78                                   
REMARK 500    GLN A 311     -179.51     69.32                                   
REMARK 500    SER A 388     -164.61   -166.59                                   
REMARK 500    HIS A 389      119.45   -167.75                                   
REMARK 500    GLU A 390      164.76     65.78                                   
REMARK 500    ILE A 391      -43.18   -153.74                                   
REMARK 500    ASP A 420       88.51    -50.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7ARG A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 7ARG GLU A   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG THR A   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG GLY A   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
SEQADV 7ARG GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7ARG HIS A  460  UNP  Q6P988              EXPRESSION TAG                 
SEQRES   1 A  383  GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG          
SEQRES   2 A  383  LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP          
SEQRES   3 A  383  GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY          
SEQRES   4 A  383  SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR          
SEQRES   5 A  383  CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR          
SEQRES   6 A  383  MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR          
SEQRES   7 A  383  ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU          
SEQRES   8 A  383  ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO          
SEQRES   9 A  383  TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS          
SEQRES  10 A  383  SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE          
SEQRES  11 A  383  ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU          
SEQRES  12 A  383  SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER SER ALA          
SEQRES  13 A  383  GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA          
SEQRES  14 A  383  GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL          
SEQRES  15 A  383  ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS          
SEQRES  16 A  383  GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS          
SEQRES  17 A  383  ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP          
SEQRES  18 A  383  ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN          
SEQRES  19 A  383  GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL          
SEQRES  20 A  383  TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP          
SEQRES  21 A  383  LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS          
SEQRES  22 A  383  LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR          
SEQRES  23 A  383  ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS          
SEQRES  24 A  383  ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS          
SEQRES  25 A  383  GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL          
SEQRES  26 A  383  LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP          
SEQRES  27 A  383  ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO          
SEQRES  28 A  383  LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO          
SEQRES  29 A  383  TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS          
SEQRES  30 A  383  HIS HIS HIS HIS HIS HIS                                      
HET    NAG  A 501      14                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    DMS  A 506       4                                                       
HET    EDO  A 507       4                                                       
HET    EDO  A 508       4                                                       
HET    SO4  A 509       5                                                       
HET    SO4  A 510       5                                                       
HET    EDO  A 511       4                                                       
HET    EDO  A 512       4                                                       
HET    EDO  A 513      10                                                       
HET    RW8  A 514      15                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     RW8 METHYL 4-(2,3-DIHYDROINDOL-1-YL)-4-OXIDANYLIDENE-                
HETNAM   2 RW8  BUTANOATE                                                       
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   7  DMS    C2 H6 O S                                                    
FORMUL   8  EDO    5(C2 H6 O2)                                                  
FORMUL  15  RW8    C13 H15 N O3                                                 
FORMUL  16  HOH   *130(H2 O)                                                    
HELIX    1 AA1 ASN A  132  MET A  143  1                                  12    
HELIX    2 AA2 ARG A  144  MET A  147  5                                   4    
HELIX    3 AA3 THR A  159  SER A  163  5                                   5    
HELIX    4 AA4 MET A  203  GLY A  217  1                                  15    
HELIX    5 AA5 ARG A  218  ALA A  223  5                                   6    
HELIX    6 AA6 SER A  232  LEU A  252  1                                  21    
HELIX    7 AA7 ALA A  286  ASN A  299  1                                  14    
HELIX    8 AA8 PRO A  303  GLN A  311  1                                   9    
HELIX    9 AA9 GLU A  314  PHE A  319  5                                   6    
HELIX   10 AB1 PHE A  320  TYR A  325  1                                   6    
HELIX   11 AB2 PRO A  326  LEU A  328  5                                   3    
HELIX   12 AB3 GLU A  341  ASP A  347  1                                   7    
HELIX   13 AB4 GLN A  357  LYS A  376  1                                  20    
HELIX   14 AB5 LEU A  407  LEU A  418  1                                  12    
SHEET    1 AA110 THR A 155  ARG A 156  0                                        
SHEET    2 AA110 LEU A  89  LEU A  93 -1  N  LEU A  89   O  ARG A 156           
SHEET    3 AA110 GLY A 108  LYS A 112 -1  O  TYR A 109   N  HIS A  92           
SHEET    4 AA110 ASN A 176  ILE A 180 -1  O  PHE A 179   N  TYR A 110           
SHEET    5 AA110 ARG A 119  LEU A 124  1  N  PHE A 123   O  ILE A 180           
SHEET    6 AA110 VAL A 225  SER A 231  1  O  ALA A 229   N  LEU A 124           
SHEET    7 AA110 GLN A 258  ASP A 264  1  O  ARG A 260   N  LEU A 228           
SHEET    8 AA110 VAL A 332  VAL A 335  1  O  VAL A 335   N  ALA A 263           
SHEET    9 AA110 SER A 381  ALA A 383  1  O  PHE A 382   N  VAL A 334           
SHEET   10 AA110 HIS A 435  VAL A 437  1  O  LEU A 436   N  ALA A 383           
SHEET    1 AA2 2 PHE A 339  ASP A 340  0                                        
SHEET    2 AA2 2 LEU A 387  SER A 388  1  O  SER A 388   N  PHE A 339           
SHEET    1 AA3 2 GLN A 401  VAL A 402  0                                        
SHEET    2 AA3 2 THR A 405  SER A 406 -1  O  THR A 405   N  VAL A 402           
SSBOND   1 CYS A  101    CYS A  183                          1555   1555  2.08  
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.02  
SSBOND   3 CYS A  279    CYS A  285                          1555   1555  2.02  
SSBOND   4 CYS A  306    CYS A  318                          1555   1555  2.12  
SSBOND   5 CYS A  386    CYS A  449                          1555   1555  2.03  
SSBOND   6 CYS A  413    CYS A  432                          1555   1555  2.05  
SSBOND   7 CYS A  440    CYS A  445                          1555   1555  2.02  
LINK         ND2 ASN A  96                 C1  NAG A 501     1555   1555  1.43  
LINK         OG  SER A 232                 C03 RW8 A 514     1555   1555  1.37  
CRYST1   59.730   71.780   78.020  90.00  90.00  90.00 P 21 21 21    4          
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      0.016742  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013931  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012817        0.00000                         
TER    2870      THR A 451                                                      
MASTER      376    0   14   14   14    0    0    6 3064    1  105   30          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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