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LongText Report for: 4ZRD-pdb

Name Class
4ZRD-pdb
HEADER    HYDROLASE                               12-MAY-15   4ZRD              
TITLE     CRYSTAL STRUCTURE OF SMG1 F278N MUTANT                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIP1, SECRETORY LIPASE (FAMILY 3);                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 20-304;                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MALASSEZIA GLOBOSA (STRAIN ATCC MYA-4612 / CBS  
SOURCE   3 7966);                                                               
SOURCE   4 ORGANISM_COMMON: DANDRUFF-ASSOCIATED FUNGUS;                         
SOURCE   5 ORGANISM_TAXID: 425265;                                              
SOURCE   6 STRAIN: ATCC MYA-4612 / CBS 7966;                                    
SOURCE   7 GENE: MGL_0797;                                                      
SOURCE   8 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: X33                                        
KEYWDS    MONO- AND DIACYLGLYCEROL LIPASE, SECRETORY LIPASE (FAMILY 3),         
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.XU,H.XU,S.HOU,J.LIU                                                 
REVDAT   1   23-SEP-15 4ZRD    0                                                
JRNL        AUTH   S.GUO,J.XU,I.V.PAVLIDIS,D.LAN,U.T.BORNSCHEUER,J.LIU,Y.WANG   
JRNL        TITL   STRUCTURE OF PRODUCT-BOUND SMG1 LIPASE: ACTIVE SITE GATING   
JRNL        TITL 2 IMPLICATIONS                                                 
JRNL        REF    FEBS J.                                    2015              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        DOI    10.1111/FEBS.13513                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15253                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2184                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 67                                      
REMARK   3   SOLVENT ATOMS            : 40                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.78                          
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    27        A   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4969  16.2191   0.0679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0157 T22:   0.0061                                     
REMARK   3      T33:   0.2472 T12:   0.0031                                     
REMARK   3      T13:  -0.0269 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8463 L22:   3.9954                                     
REMARK   3      L33:   3.5384 L12:   0.2564                                     
REMARK   3      L13:   0.3698 L23:   1.4925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0782 S12:   0.0530 S13:  -0.1698                       
REMARK   3      S21:   0.1329 S22:   0.1416 S23:  -0.1030                       
REMARK   3      S31:   0.1665 S32:   0.0737 S33:  -0.0635                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4ZRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209753.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.3                                
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) : 0.9952                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.2.8                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16070                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.300                              
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: 3UUE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH6.3, 28%PEG3350, PH      
REMARK 280  5.3, EVAPORATION, TEMPERATURE 277K                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       30.53000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       45.79500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       15.26500            
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 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     SER A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ILE A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ARG A    25                                                      
REMARK 465     GLY A    26                                                      
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    GLU A  77        5.58   -152.26                                   
REMARK 500    TYR A  79      -58.95   -126.51                                   
REMARK 500    ASN A 161       54.26     37.58                                   
REMARK 500    SER A 171     -130.31     61.19                                   
REMARK 500    TYR A 193      -67.53    -92.43                                   
REMARK 500    ASP A 228      125.87    -38.13                                   
REMARK 500    ASP A 245      131.32     76.47                                   
REMARK 500    ASN A 253       -7.01     74.29                                   
REMARK 500    PHE A 276       53.25   -108.55                                   
REMARK 500    GLN A 282       45.02   -103.14                                   
REMARK 500    ILE A 290       72.88   -113.18                                   
REMARK 500    ALA A 292     -143.52     74.32                                   
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 GOL A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide MAN A 505 bound   
REMARK 800  to THR A 32                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  501 through MAN A 504 bound to ASN A 253                            
DBREF  4ZRD A   20   304  UNP    A8PUY1   A8PUY1_MALGO    20    304             
SEQADV 4ZRD ASN A  278  UNP  A8PUY1    PHE   278 ENGINEERED MUTATION            
SEQRES   1 A  285  SER SER ILE TYR ALA ARG GLY ARG GLY GLY SER SER THR          
SEQRES   2 A  285  ASP GLN PRO VAL ALA ASN PRO TYR ASN THR LYS GLU ILE          
SEQRES   3 A  285  SER LEU ALA ALA GLY LEU VAL GLN GLN THR TYR CYS ASP          
SEQRES   4 A  285  SER THR GLU ASN GLY LEU LYS ILE GLY ASP SER GLU LEU          
SEQRES   5 A  285  LEU TYR THR MET GLY GLU GLY TYR ALA ARG GLN ARG VAL          
SEQRES   6 A  285  ASN ILE TYR HIS SER PRO SER LEU GLY ILE ALA VAL ALA          
SEQRES   7 A  285  ILE GLU GLY THR ASN LEU PHE SER LEU ASN SER ASP LEU          
SEQRES   8 A  285  HIS ASP ALA LYS PHE TRP GLN GLU ASP PRO ASN GLU ARG          
SEQRES   9 A  285  TYR ILE GLN TYR TYR PRO LYS GLY THR LYS LEU MET HIS          
SEQRES  10 A  285  GLY PHE GLN GLN ALA TYR ASN ASP LEU MET ASP ASP ILE          
SEQRES  11 A  285  PHE THR ALA VAL LYS LYS TYR LYS LYS GLU LYS ASN GLU          
SEQRES  12 A  285  LYS ARG VAL THR VAL ILE GLY HIS SER LEU GLY ALA ALA          
SEQRES  13 A  285  MET GLY LEU LEU CYS ALA MET ASP ILE GLU LEU ARG MET          
SEQRES  14 A  285  ASP GLY GLY LEU TYR LYS THR TYR LEU PHE GLY LEU PRO          
SEQRES  15 A  285  ARG LEU GLY ASN PRO THR PHE ALA SER PHE VAL ASP GLN          
SEQRES  16 A  285  LYS ILE GLY ASP LYS PHE HIS SER ILE ILE ASN GLY ARG          
SEQRES  17 A  285  ASP TRP VAL PRO THR VAL PRO PRO ARG ALA LEU GLY TYR          
SEQRES  18 A  285  GLN HIS PRO SER ASP TYR VAL TRP ILE TYR PRO GLY ASN          
SEQRES  19 A  285  SER THR SER ALA LYS LEU TYR PRO GLY GLN GLU ASN VAL          
SEQRES  20 A  285  HIS GLY ILE LEU THR VAL ALA ARG GLU PHE ASN ASN ASP          
SEQRES  21 A  285  ASP HIS GLN GLY ILE TYR PHE HIS THR GLN ILE GLY ALA          
SEQRES  22 A  285  VAL MET GLY GLU CYS PRO ALA GLN VAL GLY ALA HIS              
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    BMA  A 503      11                                                       
HET    MAN  A 504      11                                                       
HET    MAN  A 505      11                                                       
HET    GOL  A 506       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   2  BMA    C6 H12 O6                                                    
FORMUL   2  MAN    2(C6 H12 O6)                                                 
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *40(H2 O)                                                     
HELIX    1 AA1 ASN A   41  GLN A   54  1                                  14    
HELIX    2 AA2 THR A   55  CYS A   57  5                                   3    
HELIX    3 AA3 ASP A  112  PHE A  115  5                                   4    
HELIX    4 AA4 TYR A  124  TYR A  128  5                                   5    
HELIX    5 AA5 HIS A  136  ASP A  144  1                                   9    
HELIX    6 AA6 LEU A  145  LYS A  160  1                                  16    
HELIX    7 AA7 SER A  171  MET A  188  1                                  18    
HELIX    8 AA8 ASN A  205  GLY A  217  1                                  13    
HELIX    9 AA9 TRP A  229  VAL A  233  5                                   5    
HELIX   10 AB1 PRO A  235  GLY A  239  5                                   5    
HELIX   11 AB2 GLY A  268  VAL A  272  5                                   5    
HELIX   12 AB3 GLY A  291  GLY A  295  5                                   5    
SHEET    1 AA110 VAL A  36  ALA A  37  0                                        
SHEET    2 AA110 ALA A 257  GLN A 263 -1  O  LEU A 259   N  VAL A  36           
SHEET    3 AA110 SER A 244  ILE A 249 -1  N  TYR A 246   O  TYR A 260           
SHEET    4 AA110 PHE A 220  ASN A 225  1  N  ILE A 224   O  ILE A 249           
SHEET    5 AA110 LYS A 194  PHE A 198  1  N  LEU A 197   O  ILE A 223           
SHEET    6 AA110 VAL A 165  HIS A 170  1  N  GLY A 169   O  PHE A 198           
SHEET    7 AA110 GLY A  93  ILE A  98  1  N  VAL A  96   O  THR A 166           
SHEET    8 AA110 VAL A  84  SER A  89 -1  N  ASN A  85   O  ALA A  97           
SHEET    9 AA110 SER A  69  MET A  75 -1  N  LEU A  72   O  ILE A  86           
SHEET   10 AA110 LYS A  65  ILE A  66 -1  N  ILE A  66   O  SER A  69           
SHEET    1 AA2 2 GLN A 117  GLU A 118  0                                        
SHEET    2 AA2 2 LEU A 134  MET A 135 -1  O  LEU A 134   N  GLU A 118           
SHEET    1 AA3 2 ILE A 284  TYR A 285  0                                        
SHEET    2 AA3 2 THR A 288  GLN A 289 -1  O  THR A 288   N  TYR A 285           
SSBOND   1 CYS A   57    CYS A  297                          1555   1555  2.06  
LINK         OG1 THR A  32                 C1  MAN A 505     1555   1555  1.45  
LINK         ND2 ASN A 253                 C1  NAG A 501     1555   1555  1.43  
LINK         O4  NAG A 501                 C1  NAG A 502     1555   1555  1.44  
LINK         O4  NAG A 502                 C1  BMA A 503     1555   1555  1.44  
LINK         O6  BMA A 503                 C1  MAN A 504     1555   1555  1.45  
CISPEP   1 VAL A  233    PRO A  234          0        -9.49                     
CISPEP   2 TYR A  250    PRO A  251          0         2.94                     
CISPEP   3 CYS A  297    PRO A  298          0        -0.36                     
SITE     1 AC1  6 GLY A 100  SER A 105  LEU A 106  SER A 171                    
SITE     2 AC1  6 LEU A 172  ASN A 278                                          
SITE     1 AC2  1 THR A  32                                                     
SITE     1 AC3  7 ASN A 253  ASP A 279  ASP A 280  GLN A 282                    
SITE     2 AC3  7 GLY A 283  GLN A 289  HOH A 626                               
CRYST1   77.310   77.310   61.060  90.00  90.00  90.00 P 43          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      0.012935  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012935  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016377        0.00000                         
TER    2185      HIS A 304                                                      
MASTER      308    0    6   12   14    0    5    6 2291    1   71   22          
END                                                                             

Send your questions or comments to :
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:
ESTHER Home Page and ACEDB Home Page
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