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LongText Report for: 7b3i-pdb

Name Class
7b3i-pdb
HEADER    HYDROLASE                               01-DEC-20   7B3I              
TITLE     NOTUM COMPLEX WITH ARUK3003776                                        
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_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    NOTUM INHIBITOR, HYDROLASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHAO,E.Y.JONES,P.FISH                                               
REVDAT   1   08-DEC-21 7B3I    0                                                
JRNL        AUTH   P.FISH,E.Y.JONES                                             
JRNL        TITL   NOTUM INHIBITOR                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.34 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) : 1.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 76393                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3865                            
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 46.0000 -  4.0700    1.00     2795   153  0.2010 0.1896        
REMARK   3     2  4.0700 -  3.2300    1.00     2688   142  0.1875 0.1742        
REMARK   3     3  3.2300 -  2.8200    1.00     2653   132  0.1940 0.1887        
REMARK   3     4  2.8200 -  2.5600    1.00     2633   147  0.1953 0.1851        
REMARK   3     5  2.5600 -  2.3800    1.00     2597   150  0.1912 0.1935        
REMARK   3     6  2.3800 -  2.2400    1.00     2622   127  0.1864 0.2058        
REMARK   3     7  2.2400 -  2.1300    1.00     2580   150  0.1748 0.1723        
REMARK   3     8  2.1300 -  2.0300    1.00     2568   175  0.1744 0.2009        
REMARK   3     9  2.0300 -  1.9600    1.00     2598   133  0.1762 0.1765        
REMARK   3    10  1.9600 -  1.8900    1.00     2618   120  0.1750 0.1906        
REMARK   3    11  1.8900 -  1.8300    1.00     2573   139  0.1810 0.1862        
REMARK   3    12  1.8300 -  1.7800    1.00     2576   137  0.1748 0.1873        
REMARK   3    13  1.7800 -  1.7300    1.00     2600   139  0.1751 0.1725        
REMARK   3    14  1.7300 -  1.6900    1.00     2562   136  0.1731 0.2101        
REMARK   3    15  1.6900 -  1.6500    1.00     2573   118  0.1858 0.1850        
REMARK   3    16  1.6500 -  1.6100    1.00     2574   138  0.1850 0.2481        
REMARK   3    17  1.6100 -  1.5800    1.00     2592   124  0.1866 0.2056        
REMARK   3    18  1.5800 -  1.5500    1.00     2593   136  0.1904 0.1850        
REMARK   3    19  1.5500 -  1.5200    1.00     2558   128  0.1996 0.2323        
REMARK   3    20  1.5200 -  1.5000    1.00     2563   139  0.2212 0.2505        
REMARK   3    21  1.5000 -  1.4700    1.00     2569   135  0.2350 0.2926        
REMARK   3    22  1.4700 -  1.4500    1.00     2536   137  0.2508 0.2729        
REMARK   3    23  1.4500 -  1.4300    1.00     2614   130  0.2656 0.2549        
REMARK   3    24  1.4300 -  1.4100    1.00     2534   150  0.2958 0.3156        
REMARK   3    25  1.4100 -  1.3900    1.00     2533   149  0.3202 0.3583        
REMARK   3    26  1.3900 -  1.3700    1.00     2579   125  0.3386 0.3598        
REMARK   3    27  1.3700 -  1.3600    1.00     2533   136  0.3506 0.3672        
REMARK   3    28  1.3600 -  1.3400    0.99     2514   140  0.3840 0.3698        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.740           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.87                          
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  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1527  71.0125  80.9992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1599 T22:   0.1651                                     
REMARK   3      T33:   0.1577 T12:   0.0015                                     
REMARK   3      T13:  -0.0046 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6914 L22:   1.1333                                     
REMARK   3      L33:   0.7845 L12:  -0.0931                                     
REMARK   3      L13:  -0.0641 L23:  -0.0010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0170 S12:   0.0276 S13:   0.0273                       
REMARK   3      S21:  -0.0180 S22:   0.0086 S23:  -0.0239                       
REMARK   3      S31:  -0.0737 S32:   0.0101 S33:   0.0097                       
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 7B3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292112581.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.2                                
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) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 XE 16M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76523                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 39.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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: MOLREP                                                
REMARK 200 STARTING MODEL: 7ARG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULPHATE 0.1 M SODIUM     
REMARK 280  CITRATE, PH 4.2, 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       29.76400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.05450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.23350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.05450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.76400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.23350            
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: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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     HIS A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     ASP A   278                                                      
REMARK 465     CYS A   279                                                      
REMARK 465     VAL A   280                                                      
REMARK 465     ASP A   281                                                      
REMARK 465     THR A   282                                                      
REMARK 465     ILE A   283                                                      
REMARK 465     THR A   284                                                      
REMARK 465     CYS A   285                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     THR A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     GLN A   354                                                      
REMARK 465     ASP A   420                                                      
REMARK 465     SER A   421                                                      
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     THR A   427                                                      
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 115    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 134    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 312    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 391    CG1  CG2  CD1                                       
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    ASP A  88   OD1 -  CG  -  OD2 ANGL. DEV. = -34.3 DEGREES          
REMARK 500    ASP A  88   CB  -  CG  -  OD1 ANGL. DEV. =  38.6 DEGREES          
REMARK 500    ASP A  88   CB  -  CG  -  OD2 ANGL. DEV. = -30.2 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     -139.24     60.15                                   
REMARK 500    SER A 232     -125.62     65.28                                   
REMARK 500    TYR A 254       64.57   -119.78                                   
REMARK 500    GLN A 311     -176.59     68.17                                   
REMARK 500    SER A 388     -168.80   -164.03                                   
REMARK 500    GLU A 390      158.32     67.43                                   
REMARK 500    ILE A 391      -41.54   -149.73                                   
REMARK 500    LYS A 430      109.06    -59.04                                   
REMARK 500    HIS A 444       19.84     93.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ASP A  88         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7B3I A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 7B3I GLU A   78  UNP  Q6P988              CLONING ARTIFACT               
SEQADV 7B3I THR A   79  UNP  Q6P988              CLONING ARTIFACT               
SEQADV 7B3I GLY A   80  UNP  Q6P988              CLONING ARTIFACT               
SEQADV 7B3I SER A  330  UNP  Q6P988    CYS   330 ENGINEERED MUTATION            
SEQADV 7B3I GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 7B3I 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    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    DMS  A 504       4                                                       
HET    EDO  A 505       4                                                       
HET    EDO  A 506       4                                                       
HET    EDO  A 507       4                                                       
HET    STK  A 508      18                                                       
HET    DMS  A 509       4                                                       
HET    DMS  A 510       4                                                       
HET    SO4  A 511       5                                                       
HET    SO4  A 512       5                                                       
HET    SO4  A 513       5                                                       
HET    SO4  A 514       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     STK 3-(3-CHLOROPHENYL)SULFANYL-1$L^{4},2,7,8-                        
HETNAM   2 STK  TETRAZABICYCLO[4.3.0]NONA-1(6),2,4,7-TETRAEN-9-ONE              
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  SO4    7(O4 S 2-)                                                   
FORMUL   5  DMS    3(C2 H6 O S)                                                 
FORMUL   6  EDO    3(C2 H6 O2)                                                  
FORMUL   9  STK    C11 H7 CL N4 O S                                             
FORMUL  16  HOH   *90(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  GLY A  253  1                                  22    
HELIX    7 AA7 PRO A  287  ASN A  299  1                                  13    
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  LEU A  375  1                                  19    
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  LEU A 227   N  TRP A 120           
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  2.05  
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.04  
SSBOND   3 CYS A  306    CYS A  318                          1555   1555  2.06  
SSBOND   4 CYS A  386    CYS A  449                          1555   1555  2.03  
SSBOND   5 CYS A  413    CYS A  432                          1555   1555  2.04  
SSBOND   6 CYS A  440    CYS A  445                          1555   1555  2.01  
CRYST1   59.528   72.467   78.109  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      0.016799  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013799  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012803        0.00000                         
TER    2741      THR A 451                                                      
MASTER      357    0   14   14   14    0    0    6 2891    1   89   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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