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LongText Report for: 1W52-pdb

Name Class
1W52-pdb
HEADER    LIPASE                                  02-AUG-04   1W52              
TITLE     CRYSTAL STRUCTURE OF A PROTEOLYZED FORM OF PANCREATIC                 
TITLE    2 LIPASE RELATED PROTEIN 2 FROM HORSE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PANCREATIC LIPASE RELATED PROTEIN 2;                       
COMPND   3 CHAIN: X                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   3 ORGANISM_COMMON: HORSE;                                              
SOURCE   4 ORGAN: PANCREAS                                                      
KEYWDS    PANCREATIC LIPASE RELATED PROTEINS, DETERGENT, CLEAVED FLAP,          
KEYWDS   2 LIPASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MANCHENO,S.JAYNE,B.KERFELEC,C.CHAPUS,I.CRENON,J.A.HERMOSO           
REVDAT   1   12-JUL-06 1W52    0                                                
JRNL        AUTH   J.M.MANCHENO,S.JAYNE,B.KERFELEC,C.CHAPUS,I.CRENON,           
JRNL        AUTH 2 J.A.HERMOSO                                                  
JRNL        TITL   CRYSTALIZATION OF A PROTEOLYZED FORM OF THE HORSE            
JRNL        TITL 2 PANCREATIC LIPASE-RELATED PROTEIN 2: STRUCTURAL              
JRNL        TITL 3 BASIS FOR THE SPECIFIC DETERGENT REQUIREMENT.                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  60  2107 2004              
JRNL        REFN   ASTM ABCRE6  DK ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.99 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3   REFINEMENT TARGET : MAXIMUM LIKELIHOOD                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.97                          
REMARK   3   NUMBER OF REFLECTIONS             : 15958                          
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) : 0.23445                         
REMARK   3   R VALUE            (WORKING SET) : 0.23138                         
REMARK   3   FREE R VALUE                     : 0.29378                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  5.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 847                             
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) : 2.990                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.067                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1155                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.342                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 65                           
REMARK   3   BIN FREE R VALUE                    : 0.421                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3494                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) :  52.087                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) :     0.02                                             
REMARK   3    B22 (A**2) :     0.02                                             
REMARK   3    B33 (A**2) :    -0.03                                             
REMARK   3    B12 (A**2) :     0.01                                             
REMARK   3    B13 (A**2) :     0.00                                             
REMARK   3    B23 (A**2) :     0.00                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A):   0.968       
REMARK   3   ESU BASED ON FREE R VALUE                       (A):   0.420       
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A):   0.313       
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2):  17.505       
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.892                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.838                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A):  3611 ; 0.020 ; 0.021          
REMARK   3   BOND LENGTHS OTHERS            (A):  3129 ; 0.002 ; 0.020          
REMARK   3   BOND ANGLES REFINED      (DEGREES):  4891 ; 1.993 ; 1.951          
REMARK   3   BOND ANGLES OTHERS       (DEGREES):  7337 ; 1.368 ; 3.000          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):   446 ; 7.549 ; 5.000          
REMARK   3   TORSION ANGLES, PERIOD 2 (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   TORSION ANGLES, PERIOD 3 (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   TORSION ANGLES, PERIOD 4 (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):   515 ; 0.097 ; 0.200          
REMARK   3   GENERAL PLANES REFINED         (A):  4045 ; 0.007 ; 0.020          
REMARK   3   GENERAL PLANES OTHERS          (A):   729 ; 0.004 ; 0.020          
REMARK   3   NON-BONDED CONTACTS REFINED    (A):  1012 ; 0.266 ; 0.200          
REMARK   3   NON-BONDED CONTACTS OTHERS     (A):  4070 ; 0.262 ; 0.200          
REMARK   3   NON-BONDED TORSION OTHERS      (A):  2082 ; 0.093 ; 0.200          
REMARK   3   H-BOND (X...Y) REFINED         (A):    91 ; 0.194 ; 0.200          
REMARK   3   POTENTIAL METAL-ION REFINED    (A):     1 ; 0.173 ; 0.200          
REMARK   3   SYMMETRY VDW REFINED           (A):     7 ; 0.369 ; 0.200          
REMARK   3   SYMMETRY VDW OTHERS            (A):    44 ; 0.329 ; 0.200          
REMARK   3   SYMMETRY H-BOND REFINED        (A):     1 ; 0.281 ; 0.200          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT  RMS   WEIGHT            
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2):  2222 ; 1.765 ; 1.500            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2):  3576 ; 3.487 ; 2.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2):  1389 ; 3.502 ; 3.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2):  1315 ; 6.163 ; 4.500            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   :1.40                                           
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3    RIDING POSITIONS.                                                 
REMARK   3    CHAINS FROM SEVERAL SEQUENCE REGIONS FROM THE C-TERMINAL          
REMARK   3    DOMAIN ARE NOT DEFINED IN THE ELECTRON DENSITY MAP                
REMARK   3    THE FOLLOWING REGIONS ARE NOT DEFINED IN ELECTRON DENSITY         
REMARK   3    MAP, 346-354,363-368,379-386,398-402,407-424,433-452 B-           
REMARK   3    FACTORS OF THESE RESIDUES HAVE BEEN CHANGED TOP 100.00            
REMARK   4                                                                      
REMARK   4 1W52 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 18-AUG-2004.                
REMARK 100 THE EBI ID CODE IS EBI-20635.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-2004                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF BEAMLINE ID14-EH2             
REMARK 200  BEAMLINE                       : ID14-EH2                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALE                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16857                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.99                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.6                               
REMARK 200  R MERGE                    (I) : 0.13                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.40                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.2                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.60                               
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: PDB ENTRY 1BU8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3                                            
REMARK 290       3555   Y-X,-X,Z+1/3                                            
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,1/3-Z                                            
REMARK 290       6555   -X,Y-X,2/3-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 -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       57.21200            
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       28.60600            
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       28.60600            
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       57.21200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF   1 CHAIN(S). SEE REMARK 350 FOR                   
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300                                                                      
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC                       
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: X                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 X   243                                                      
REMARK 465     PHE X   244                                                      
REMARK 465     SER X   245                                                      
REMARK 465     THR X   246                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL                
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 500 NUMBER; I=INSERTION CODE).                                           
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)           
REMARK 500                                                                      
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991                               
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO X 213  CB     PRO X 213  CG       0.255                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                                                                      
REMARK 500   O    ASP X    57     OG1  THR X    60               2.11           
REMARK 500   O    ILE X    61     OG   SER X    64               2.12           
REMARK 500   O    ARG X   363     O    GLY X   367               2.19           
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 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500                                                                      
REMARK 500    SER X 154     -117.39     56.87                                   
REMARK 500    VAL X 404      155.02    124.25                                   
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 LEU X 212    PRO X 213                  230.00                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM CA    CA X 602  THE COORDINATION ANGLES ARE:          
REMARK 600  1 ASP   194X  OD1                                                   
REMARK 600  2 ASP   197X  OD1        85.7                                       
REMARK 600  3 GLU   189X  O         101.9 145.2                                 
REMARK 600  4 ASP   197X  OD2        80.0  51.1 163.3                           
REMARK 600                             1     2     3                            
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: DDQ BINDING SITE FOR CHAIN X                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: DDQ BINDING SITE FOR CHAIN X                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN X                        
DBREF  1W52 X    1   452  UNP    Q95KP4   Q95KP4           1    452             
SEQRES   1 X  452  LYS GLU VAL CYS TYR THR PRO LEU GLY CYS PHE SER ASP          
SEQRES   2 X  452  ASP LYS PRO TRP ALA GLY THR LEU GLN ARG PRO LEU LYS          
SEQRES   3 X  452  SER LEU PRO TRP SER PRO GLU GLU VAL ASN THR ARG PHE          
SEQRES   4 X  452  LEU LEU TYR THR ASN LYS ASN PRO ASP SER TYR GLN LEU          
SEQRES   5 X  452  ILE THR ALA ARG ASP VAL ALA THR ILE LYS SER SER ASN          
SEQRES   6 X  452  PHE GLN SER SER ARG LYS THR HIS PHE VAL ILE HIS GLY          
SEQRES   7 X  452  PHE ARG ASP ARG GLY GLU ASP SER TRP PRO SER ASP MET          
SEQRES   8 X  452  CYS LYS LYS ILE LEU GLN VAL GLU THR THR ASN CYS ILE          
SEQRES   9 X  452  SER VAL ASP TRP SER SER GLY ALA LYS ALA GLU TYR THR          
SEQRES  10 X  452  GLN ALA VAL GLN ASN ILE ARG ILE VAL GLY ALA GLU THR          
SEQRES  11 X  452  ALA TYR LEU ILE GLN GLN LEU LEU THR GLU LEU SER TYR          
SEQRES  12 X  452  ASN PRO GLU ASN VAL HIS ILE ILE GLY HIS SER LEU GLY          
SEQRES  13 X  452  ALA HIS THR ALA GLY GLU ALA GLY ARG ARG LEU GLU GLY          
SEQRES  14 X  452  ARG VAL GLY ARG VAL THR GLY LEU ASP PRO ALA GLU PRO          
SEQRES  15 X  452  CYS PHE GLN ASP ALA SER GLU GLU VAL ARG LEU ASP PRO          
SEQRES  16 X  452  SER ASP ALA GLN PHE VAL ASP VAL ILE HIS THR ASP ALA          
SEQRES  17 X  452  SER PRO MET LEU PRO SER LEU GLY PHE GLY MET SER GLN          
SEQRES  18 X  452  LYS VAL GLY HIS MET ASP PHE PHE PRO ASN GLY GLY LYS          
SEQRES  19 X  452  GLN MET PRO GLY CYS LYS ARG SER SER PHE SER THR PHE          
SEQRES  20 X  452  ILE ASP ILE ASN GLY ILE TRP GLN GLY ALA GLN ASP TYR          
SEQRES  21 X  452  LEU ALA CYS ASN HIS LEU LYS SER PHE GLU TYR TYR SER          
SEQRES  22 X  452  SER SER ILE LEU ASN PRO ASP GLY PHE LEU ALA TYR PRO          
SEQRES  23 X  452  CYS ASP SER TYR ASP LYS PHE GLN GLU ASN GLY CYS PHE          
SEQRES  24 X  452  PRO CYS PRO ALA GLY GLY CYS PRO LYS MET GLY HIS TYR          
SEQRES  25 X  452  ALA ASP GLN TYR LYS GLU LYS THR SER ALA VAL GLU GLN          
SEQRES  26 X  452  THR PHE PHE LEU ASN THR GLY GLU SER GLY ASP TYR THR          
SEQRES  27 X  452  SER TRP ARG TYR ARG VAL SER ILE THR LEU ALA GLY SER          
SEQRES  28 X  452  GLY LYS ALA ASN GLY TYR LEU LYS VAL THR LEU ARG GLY          
SEQRES  29 X  452  SER ASN GLY ASN SER LYS GLN TYR GLU ILE PHE LYS GLY          
SEQRES  30 X  452  SER LEU GLN PRO ASP SER SER TYR THR LEU ASP VAL ASP          
SEQRES  31 X  452  VAL ASN PHE ILE ILE GLY LYS ILE GLN GLU VAL LYS PHE          
SEQRES  32 X  452  VAL TRP ASN LYS THR VAL LEU ASN LEU SER LYS PRO GLN          
SEQRES  33 X  452  LEU GLY ALA SER ARG ILE THR VAL GLN SER GLY ALA ASP          
SEQRES  34 X  452  GLY THR GLU TYR LYS PHE CYS GLY SER GLY THR VAL GLN          
SEQRES  35 X  452  ASP ASN VAL GLU GLN SER LEU TYR PRO CYS                      
HET    DDQ  X 501      14                                                       
HET    DDQ  X 502      14                                                       
HET     CA  X 601       1                                                       
HET     CA  X 602       1                                                       
HETNAM     DDQ DECYLAMINE-N,N-DIMETHYL-N-OXIDE                                  
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  DDQ    2(C12 H27 N1 O1)                                             
FORMUL   3   CA    2(CA1 2+)                                                    
HELIX    1   1 SER X   31  ASN X   36  1                                   6    
HELIX    2   2 VAL X   58  SER X   63  1                                   6    
HELIX    3   3 SER X   86  GLN X   97  1                                  12    
HELIX    4   4 TRP X  108  LYS X  113  1                                   6    
HELIX    5   5 GLU X  115  SER X  142  1                                  28    
HELIX    6   6 ASN X  144  GLU X  146  5                                   3    
HELIX    7   7 SER X  154  LEU X  167  1                                  14    
HELIX    8   8 ASP X  194  ALA X  198  5                                   5    
HELIX    9   9 GLY X  232  LYS X  234  5                                   3    
HELIX   10  10 ASP X  249  ILE X  253  5                                   5    
HELIX   11  11 GLY X  256  ASN X  278  1                                  23    
HELIX   12  12 PRO X  279  PHE X  282  5                                   4    
HELIX   13  13 SER X  289  GLU X  295  1                                   7    
HELIX   14  14 GLY X  310  TYR X  316  5                                   7    
SHEET    1  XA 2 VAL X   3  TYR X   5  0                                        
SHEET    2  XA 2 GLY X   9  PHE X  11 -1  O  GLY X   9   N  TYR X   5           
SHEET    1  XB10 ASN X  46  ILE X  53  0                                        
SHEET    2  XB10 ARG X  38  THR X  43 -1  O  PHE X  39   N  ILE X  53           
SHEET    3  XB10 ASN X 102  ASP X 107 -1  O  CYS X 103   N  TYR X  42           
SHEET    4  XB10 THR X  72  ILE X  76  1  O  HIS X  73   N  ILE X 104           
SHEET    5  XB10 VAL X 148  HIS X 153  1  O  HIS X 149   N  PHE X  74           
SHEET    6  XB10 ARG X 173  LEU X 177  1  O  ARG X 173   N  ILE X 150           
SHEET    7  XB10 VAL X 201  ILE X 204  1  O  ASP X 202   N  GLY X 176           
SHEET    8  XB10 MET X 226  PRO X 230  1  O  MET X 226   N  VAL X 203           
SHEET    9  XB10 GLN X 325  LEU X 329  1  O  GLN X 325   N  ASP X 227           
SHEET   10  XB10 TYR X 285  PRO X 286 -1  O  TYR X 285   N  PHE X 328           
SHEET    1  XC 2 TRP X 340  VAL X 344  0                                        
SHEET    2  XC 2 LEU X 387  VAL X 391 -1  O  LEU X 387   N  VAL X 344           
SHEET    1  XD 2 ASN X 355  GLY X 356  0                                        
SHEET    2  XD 2 GLY X 377  SER X 378 -1  O  GLY X 377   N  GLY X 356           
SHEET    1  XE 2 PHE X 435  CYS X 436  0                                        
SHEET    2  XE 2 TYR X 450  PRO X 451 -1  O  TYR X 450   N  CYS X 436           
SSBOND   1 CYS X    4    CYS X   10                          1555   1555        
SSBOND   2 CYS X   92    CYS X  103                          1555   1555        
SSBOND   3 CYS X  239    CYS X  263                          1555   1555        
SSBOND   4 CYS X  287    CYS X  298                          1555   1555        
SSBOND   5 CYS X  301    CYS X  306                          1555   1555        
SSBOND   6 CYS X  436    CYS X  452                          1555   1555        
LINK        CA    CA X 601                 OD2 ASP X 314     1555   1555        
LINK        CA    CA X 602                 OD2 ASP X 197     1555   1555        
LINK        CA    CA X 602                 OD1 ASP X 197     1555   1555        
LINK        CA    CA X 602                 O   GLU X 189     1555   1555        
LINK        CA    CA X 602                 OD1 ASP X 194     1555   1555        
CISPEP   1 LYS X   15    PRO X   16          0       -10.03                     
CISPEP   2 PHE X  299    PRO X  300          0        -4.74                     
SITE     1 AC1  3 MET X 211  LEU X 215  TRP X 254                               
SITE     1 AC2  4 ARG X  80  ASP X  81  TYR X 116  HIS X 265                    
SITE     1 AC4  4 GLU X 189  ARG X 192  ASP X 194  ASP X 197                    
CRYST1  128.426  128.426   85.818  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007787  0.004496  0.000000        0.00000                         
SCALE2      0.000000  0.008991  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011653        0.00000                         
TER    3495      CYS X 452                                                      
MASTER      312    0    4   14   18    0    3    6 3524    1   47   35          
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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