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LongText Report for: 4K6G-pdb

Name Class
4K6G-pdb
HEADER    HYDROLASE                               15-APR-13   4K6G              
TITLE     CRYSTAL STRUCTURE OF CALB FROM CANDIDA ANTARCTICA                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE B;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CALB;                                                       
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CANDIDA ANTARCTICA;                             
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 34362;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA AODE3AI;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    LIPASE, HYDROLASE                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.AN,Y.XIE,Y.FENG,G.WU                                                
REVDAT   1   29-JAN-14 4K6G    0                                                
JRNL        AUTH   Y.XIE,J.AN,G.YANG,G.WU,Y.ZHANG,L.CUI,Y.FENG                  
JRNL        TITL   ENHANCED ENZYME KINETIC STABILITY BY INCREASING RIGIDITY     
JRNL        TITL 2 WITHIN THE ACTIVE SITE                                       
JRNL        REF    J.BIOL.CHEM.                               2014              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        DOI    10.1074/JBC.M113.536045                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 86931                          
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) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4353                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5885                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 318                          
REMARK   3   BIN FREE R VALUE                    : 0.2220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4644                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 402                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09000                                              
REMARK   3    B22 (A**2) : 0.33000                                              
REMARK   3    B33 (A**2) : -0.44000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.10000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.083         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.077         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.046         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.195         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4770 ; 0.005 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6550 ; 1.091 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   631 ; 5.452 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   165 ;33.806 ;25.030       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   679 ;12.171 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;17.091 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   767 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3632 ; 0.005 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4K6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAY-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078950.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 171636                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18900                            
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2M NAAC, 0.1M TRIS-BIS   
REMARK 280  PH6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.82100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   141                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     PRO A   143                                                      
REMARK 465     LEU A   144                                                      
REMARK 465     ASP A   145                                                      
REMARK 465     ALA A   146                                                      
REMARK 465     LEU A   147                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
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 319    CG   CD   OE1  OE2                                  
REMARK 470     ALA B   0    N                                                   
REMARK 470     GLU B 319    CG   CD   OE1  OE2                                  
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    SER A  29       87.07   -154.66                                   
REMARK 500    ASN A  51      -90.38   -146.20                                   
REMARK 500    SER A 105     -127.60     56.18                                   
REMARK 500    ASN A 206       -0.91     74.23                                   
REMARK 500    ALA A 305       36.29   -140.59                                   
REMARK 500    SER B  29       86.22   -156.38                                   
REMARK 500    ASN B  51      -92.47   -144.49                                   
REMARK 500    SER B 105     -127.01     56.38                                   
REMARK 500    ASP B 134       63.83   -102.25                                   
REMARK 500    ASN B 206       -2.31     74.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4K5Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K6H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4K6K   RELATED DB: PDB                                   
DBREF  4K6G A    1   317  UNP    P41365   LIPB_CANAR      26    342             
DBREF  4K6G B    1   317  UNP    P41365   LIPB_CANAR      26    342             
SEQADV 4K6G MET A   -1  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G ALA A    0  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G LEU A  318  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G GLU A  319  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS A  320  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS A  321  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS A  322  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS A  323  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS A  324  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS A  325  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G MET B   -1  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G ALA B    0  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G LEU B  318  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G GLU B  319  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS B  320  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS B  321  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS B  322  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS B  323  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS B  324  UNP  P41365              EXPRESSION TAG                 
SEQADV 4K6G HIS B  325  UNP  P41365              EXPRESSION TAG                 
SEQRES   1 A  327  MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN          
SEQRES   2 A  327  PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY          
SEQRES   3 A  327  ALA SER PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL          
SEQRES   4 A  327  PRO GLY THR GLY THR THR GLY PRO GLN SER PHE ASP SER          
SEQRES   5 A  327  ASN TRP ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO          
SEQRES   6 A  327  CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR          
SEQRES   7 A  327  GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA          
SEQRES   8 A  327  LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU          
SEQRES   9 A  327  THR TRP SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU          
SEQRES  10 A  327  THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU          
SEQRES  11 A  327  MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA          
SEQRES  12 A  327  GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL          
SEQRES  13 A  327  TRP GLN GLN THR THR GLY SER ALA LEU THR THR ALA LEU          
SEQRES  14 A  327  ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR          
SEQRES  15 A  327  ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN          
SEQRES  16 A  327  VAL SER ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN          
SEQRES  17 A  327  GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU          
SEQRES  18 A  327  PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE          
SEQRES  19 A  327  SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER THR THR          
SEQRES  20 A  327  GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS          
SEQRES  21 A  327  ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS          
SEQRES  22 A  327  VAL ALA ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA          
SEQRES  23 A  327  ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU          
SEQRES  24 A  327  MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR          
SEQRES  25 A  327  CYS SER GLY ILE VAL THR PRO LEU GLU HIS HIS HIS HIS          
SEQRES  26 A  327  HIS HIS                                                      
SEQRES   1 B  327  MET ALA LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN          
SEQRES   2 B  327  PRO LYS SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY          
SEQRES   3 B  327  ALA SER PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL          
SEQRES   4 B  327  PRO GLY THR GLY THR THR GLY PRO GLN SER PHE ASP SER          
SEQRES   5 B  327  ASN TRP ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO          
SEQRES   6 B  327  CYS TRP ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR          
SEQRES   7 B  327  GLN VAL ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA          
SEQRES   8 B  327  LEU TYR ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU          
SEQRES   9 B  327  THR TRP SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU          
SEQRES  10 B  327  THR PHE PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU          
SEQRES  11 B  327  MET ALA PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA          
SEQRES  12 B  327  GLY PRO LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL          
SEQRES  13 B  327  TRP GLN GLN THR THR GLY SER ALA LEU THR THR ALA LEU          
SEQRES  14 B  327  ARG ASN ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR          
SEQRES  15 B  327  ASN LEU TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN          
SEQRES  16 B  327  VAL SER ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN          
SEQRES  17 B  327  GLY LYS ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU          
SEQRES  18 B  327  PHE VAL ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE          
SEQRES  19 B  327  SER TYR VAL VAL GLY ARG SER ALA LEU ARG SER THR THR          
SEQRES  20 B  327  GLY GLN ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS          
SEQRES  21 B  327  ASN PRO LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS          
SEQRES  22 B  327  VAL ALA ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA          
SEQRES  23 B  327  ILE VAL ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU          
SEQRES  24 B  327  MET PRO TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR          
SEQRES  25 B  327  CYS SER GLY ILE VAL THR PRO LEU GLU HIS HIS HIS HIS          
SEQRES  26 B  327  HIS HIS                                                      
HET    EDO  A 401       4                                                       
HET    EDO  A 402       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    2(C2 H6 O2)                                                  
FORMUL   5  HOH   *402(H2 O)                                                    
HELIX    1   1 PRO A   12  GLY A   19  1                                   8    
HELIX    2   2 THR A   43  ASP A   49  1                                   7    
HELIX    3   3 ASN A   51  LEU A   59  1                                   9    
HELIX    4   4 ASP A   75  SER A   94  1                                  20    
HELIX    5   5 SER A  105  PHE A  118  1                                  14    
HELIX    6   6 PRO A  119  ARG A  122  5                                   4    
HELIX    7   7 ALA A  151  GLN A  157  1                                   7    
HELIX    8   8 SER A  161  ALA A  170  1                                  10    
HELIX    9   9 ALA A  212  GLY A  217  1                                   6    
HELIX   10  10 ALA A  225  SER A  230  1                                   6    
HELIX   11  11 SER A  230  SER A  243  1                                  14    
HELIX   12  12 ARG A  249  TYR A  253  5                                   5    
HELIX   13  13 GLY A  254  CYS A  258  5                                   5    
HELIX   14  14 THR A  267  ALA A  276  1                                  10    
HELIX   15  15 LEU A  277  GLY A  288  1                                  12    
HELIX   16  16 ALA A  301  ALA A  305  5                                   5    
HELIX   17  17 PRO B   12  GLY B   19  1                                   8    
HELIX   18  18 THR B   43  ASP B   49  1                                   7    
HELIX   19  19 ASN B   51  LEU B   59  1                                   9    
HELIX   20  20 ASP B   75  SER B   94  1                                  20    
HELIX   21  21 SER B  105  PHE B  118  1                                  14    
HELIX   22  22 PRO B  119  ARG B  122  5                                   4    
HELIX   23  23 THR B  138  GLY B  142  5                                   5    
HELIX   24  24 PRO B  143  LEU B  147  5                                   5    
HELIX   25  25 ALA B  151  GLN B  157  1                                   7    
HELIX   26  26 SER B  161  ALA B  170  1                                  10    
HELIX   27  27 ALA B  212  GLY B  217  1                                   6    
HELIX   28  28 ALA B  225  SER B  230  1                                   6    
HELIX   29  29 SER B  230  SER B  243  1                                  14    
HELIX   30  30 ARG B  249  TYR B  253  5                                   5    
HELIX   31  31 GLY B  254  CYS B  258  5                                   5    
HELIX   32  32 THR B  267  ALA B  276  1                                  10    
HELIX   33  33 LEU B  278  GLY B  288  1                                  11    
HELIX   34  34 ALA B  301  ALA B  305  5                                   5    
SHEET    1   A 7 LEU A  20  CYS A  22  0                                        
SHEET    2   A 7 THR A  62  ILE A  66 -1  O  TRP A  65   N  THR A  21           
SHEET    3   A 7 PRO A  33  VAL A  37  1  N  LEU A  36   O  CYS A  64           
SHEET    4   A 7 LEU A  99  TRP A 104  1  O  LEU A 102   N  LEU A  35           
SHEET    5   A 7 VAL A 125  PHE A 131  1  O  MET A 129   N  VAL A 101           
SHEET    6   A 7 THR A 179  TYR A 183  1  O  THR A 180   N  ALA A 130           
SHEET    7   A 7 LYS A 208  GLN A 211  1  O  VAL A 210   N  ASN A 181           
SHEET    1   B 2 ARG A 309  THR A 310  0                                        
SHEET    2   B 2 GLY A 313  ILE A 314 -1  O  GLY A 313   N  THR A 310           
SHEET    1   C 7 LEU B  20  CYS B  22  0                                        
SHEET    2   C 7 THR B  62  ILE B  66 -1  O  TRP B  65   N  THR B  21           
SHEET    3   C 7 PRO B  33  VAL B  37  1  N  LEU B  36   O  CYS B  64           
SHEET    4   C 7 LEU B  99  TRP B 104  1  O  LEU B 102   N  LEU B  35           
SHEET    5   C 7 VAL B 125  PHE B 131  1  O  MET B 129   N  VAL B 101           
SHEET    6   C 7 THR B 179  TYR B 183  1  O  THR B 180   N  ALA B 130           
SHEET    7   C 7 LYS B 208  GLN B 211  1  O  VAL B 210   N  ASN B 181           
SHEET    1   D 2 ARG B 309  THR B 310  0                                        
SHEET    2   D 2 GLY B 313  ILE B 314 -1  O  GLY B 313   N  THR B 310           
SSBOND   1 CYS A   22    CYS A   64                          1555   1555  2.05  
SSBOND   2 CYS A  216    CYS A  258                          1555   1555  2.03  
SSBOND   3 CYS A  293    CYS A  311                          1555   1555  2.04  
SSBOND   4 CYS B   22    CYS B   64                          1555   1555  2.05  
SSBOND   5 CYS B  216    CYS B  258                          1555   1555  2.03  
SSBOND   6 CYS B  293    CYS B  311                          1555   1555  2.04  
CISPEP   1 PRO A   69    PRO A   70          0       -10.35                     
CISPEP   2 GLN A  191    PRO A  192          0         2.57                     
CISPEP   3 PRO B   69    PRO B   70          0        -9.77                     
CISPEP   4 GLN B  191    PRO B  192          0         0.32                     
SITE     1 AC1  5 ASN A 169  PRO A 303  PHE A 304  ALA A 305                    
SITE     2 AC1  5 VAL A 306                                                     
SITE     1 AC2  6 THR A  40  TRP A 104  SER A 105  HIS A 224                    
SITE     2 AC2  6 LEU A 278  ALA A 281                                          
CRYST1   47.699   81.642   71.652  90.00  95.87  90.00 P 1 21 1      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      0.020965  0.000000  0.002154        0.00000                         
SCALE2      0.000000  0.012249  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014030        0.00000                         
TER    2305      GLU A 319                                                      
TER    4646      GLU B 319                                                      
MASTER      313    0    2   34   18    0    4    6 5054    2   20   52          
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.
For technical information about these pages see:
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