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LongText Report for: 3UUF-pdb

Name Class
3UUF-pdb
HEADER    HYDROLASE                               28-NOV-11   3UUF              
TITLE     CRYSTAL STRUCTURE OF MONO- AND DIACYLGLYCEROL LIPASE FROM MALASSEZIA  
TITLE    2 GLOBOSA                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIP1, SECRETORY LIPASE (FAMILY 3);                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 26-304;                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MALASSEZIA GLOBOSA;                             
SOURCE   3 ORGANISM_COMMON: DANDRUFF-ASSOCIATED FUNGUS;                         
SOURCE   4 ORGANISM_TAXID: 425265;                                              
SOURCE   5 STRAIN: ATCC MYA-4612 / CBS 7966;                                    
SOURCE   6 GENE: MGL_0797;                                                      
SOURCE   7 EXPRESSION_SYSTEM: KOMAGATAELLA PHAFFII;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 460519                                      
KEYWDS    LID-DOMAIN, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.XU,J.XU,S.HOU,J.LIU                                                 
REVDAT   1   25-APR-12 3UUF    0                                                
JRNL        AUTH   T.XU,L.LIU,S.HOU,J.XU,B.YANG,Y.WANG,J.LIU                    
JRNL        TITL   CRYSTAL STRUCTURE OF A MONO- AND DIACYLGLYCEROL LIPASE FROM  
JRNL        TITL 2 MALASSEZIA GLOBOSA REVEALS A NOVEL LID CONFORMATION AND      
JRNL        TITL 3 INSIGHTS INTO THE SUBSTRATE SPECIFICITY.                     
JRNL        REF    J.STRUCT.BIOL.                             2012              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   22484238                                                     
JRNL        DOI    10.1016/J.JSB.2012.03.006                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 10455                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 531                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 741                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 22                           
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2187                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 12                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.93000                                             
REMARK   3    B22 (A**2) : -0.93000                                             
REMARK   3    B33 (A**2) : 1.87000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.611         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.292         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.379        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2287 ; 0.014 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3105 ; 1.840 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   277 ; 8.047 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;33.505 ;24.404       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   361 ;17.631 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;18.855 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   331 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1768 ; 0.009 ; 0.021       
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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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                                                           
REMARK   4                                                                      
REMARK   4 3UUF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB069221.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION ENHANCE ULTRA   
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11015                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.952                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11400                            
REMARK 200   FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.50200                            
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX MR_ROSSETA                                     
REMARK 200 STARTING MODEL: 3NGM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 20% PEGMME 5000,   
REMARK 280  VAPOR DIFFUSION, 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       29.88650            
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       44.82975            
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       14.94325            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 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 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   OG1  THR A    32     C2   MAN A   504              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A 116   CE2   TRP A 116   CD2     0.077                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  33      146.54    -38.29                                   
REMARK 500    GLU A  61       90.25    -54.08                                   
REMARK 500    ASP A  68        5.25    -67.63                                   
REMARK 500    GLU A  77        1.53   -163.31                                   
REMARK 500    LEU A 110        0.11    -64.70                                   
REMARK 500    SER A 171     -130.22     62.29                                   
REMARK 500    PRO A 231        1.72    -62.27                                   
REMARK 500    PRO A 243     -171.15    -60.62                                   
REMARK 500    ASP A 245      131.10     76.02                                   
REMARK 500    ASN A 253       -3.42     74.17                                   
REMARK 500    PHE A 276       45.28   -109.94                                   
REMARK 500    ASP A 279      -72.17    -68.46                                   
REMARK 500    PHE A 286       69.47     38.17                                   
REMARK 500    ALA A 292     -146.08     75.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 THR A   60     GLU A   61                  147.42                    
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 MAN A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LINKED RESIDUES A 501-502         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UUE   RELATED DB: PDB                                   
DBREF  3UUF A   27   304  UNP    A8PUY1   A8PUY1_MALGO    27    304             
SEQRES   1 A  278  ARG GLY GLY SER SER THR ASP GLN PRO VAL ALA ASN PRO          
SEQRES   2 A  278  TYR ASN THR LYS GLU ILE SER LEU ALA ALA GLY LEU VAL          
SEQRES   3 A  278  GLN GLN THR TYR CYS ASP SER THR GLU ASN GLY LEU LYS          
SEQRES   4 A  278  ILE GLY ASP SER GLU LEU LEU TYR THR MET GLY GLU GLY          
SEQRES   5 A  278  TYR ALA ARG GLN ARG VAL ASN ILE TYR HIS SER PRO SER          
SEQRES   6 A  278  LEU GLY ILE ALA VAL ALA ILE GLU GLY THR ASN LEU PHE          
SEQRES   7 A  278  SER LEU ASN SER ASP LEU HIS ASP ALA LYS PHE TRP GLN          
SEQRES   8 A  278  GLU ASP PRO ASN GLU ARG TYR ILE GLN TYR TYR PRO LYS          
SEQRES   9 A  278  GLY THR LYS LEU MET HIS GLY PHE GLN GLN ALA TYR ASN          
SEQRES  10 A  278  ASP LEU MET ASP ASP ILE PHE THR ALA VAL LYS LYS TYR          
SEQRES  11 A  278  LYS LYS GLU LYS ASN GLU LYS ARG VAL THR VAL ILE GLY          
SEQRES  12 A  278  HIS SER LEU GLY ALA ALA MET GLY LEU LEU CYS ALA MET          
SEQRES  13 A  278  ASP ILE GLU LEU ARG MET ASP GLY GLY LEU TYR LYS THR          
SEQRES  14 A  278  TYR LEU PHE GLY LEU PRO ARG LEU GLY ASN PRO THR PHE          
SEQRES  15 A  278  ALA SER PHE VAL ASP GLN LYS ILE GLY ASP LYS PHE HIS          
SEQRES  16 A  278  SER ILE ILE ASN GLY ARG ASP TRP VAL PRO THR VAL PRO          
SEQRES  17 A  278  PRO ARG ALA LEU GLY TYR GLN HIS PRO SER ASP TYR VAL          
SEQRES  18 A  278  TRP ILE TYR PRO GLY ASN SER THR SER ALA LYS LEU TYR          
SEQRES  19 A  278  PRO GLY GLN GLU ASN VAL HIS GLY ILE LEU THR VAL ALA          
SEQRES  20 A  278  ARG GLU PHE ASN PHE ASP ASP HIS GLN GLY ILE TYR PHE          
SEQRES  21 A  278  HIS THR GLN ILE GLY ALA VAL MET GLY GLU CYS PRO ALA          
SEQRES  22 A  278  GLN VAL GLY ALA HIS                                          
MODRES 3UUF ASN A  253  ASN  GLYCOSYLATION SITE                                 
MODRES 3UUF THR A   32  THR  GLYCOSYLATION SITE                                 
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    MAN  A 504      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   3  MAN    C6 H12 O6                                                    
FORMUL   4  HOH   *12(H2 O)                                                     
HELIX    1   1 ASN A   41  GLN A   54  1                                  14    
HELIX    2   2 THR A   55  CYS A   57  5                                   3    
HELIX    3   3 ASP A  112  PHE A  115  5                                   4    
HELIX    4   4 TYR A  124  TYR A  128  5                                   5    
HELIX    5   5 HIS A  136  ASP A  144  1                                   9    
HELIX    6   6 LEU A  145  ASN A  161  1                                  17    
HELIX    7   7 SER A  171  MET A  188  1                                  18    
HELIX    8   8 ASN A  205  GLY A  217  1                                  13    
HELIX    9   9 TRP A  229  VAL A  233  5                                   5    
HELIX   10  10 PRO A  235  GLY A  239  5                                   5    
HELIX   11  11 GLY A  268  VAL A  272  5                                   5    
HELIX   12  12 ASP A  279  GLN A  282  5                                   4    
HELIX   13  13 GLY A  291  GLY A  295  5                                   5    
SHEET    1   A10 VAL A  36  ALA A  37  0                                        
SHEET    2   A10 ALA A 257  GLN A 263 -1  O  LEU A 259   N  VAL A  36           
SHEET    3   A10 SER A 244  ILE A 249 -1  N  TYR A 246   O  TYR A 260           
SHEET    4   A10 PHE A 220  ASN A 225  1  N  ILE A 224   O  ILE A 249           
SHEET    5   A10 LYS A 194  PHE A 198  1  N  LEU A 197   O  ILE A 223           
SHEET    6   A10 VAL A 165  HIS A 170  1  N  GLY A 169   O  PHE A 198           
SHEET    7   A10 GLY A  93  ILE A  98  1  N  VAL A  96   O  ILE A 168           
SHEET    8   A10 VAL A  84  SER A  89 -1  N  ASN A  85   O  ALA A  97           
SHEET    9   A10 SER A  69  MET A  75 -1  N  LEU A  72   O  ILE A  86           
SHEET   10   A10 LYS A  65  ILE A  66 -1  N  ILE A  66   O  SER A  69           
SHEET    1   B 2 GLN A 117  GLU A 118  0                                        
SHEET    2   B 2 LEU A 134  MET A 135 -1  O  LEU A 134   N  GLU A 118           
SHEET    1   C 2 ILE A 284  TYR A 285  0                                        
SHEET    2   C 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  2.02  
LINK         ND2 ASN A 253                 C1  NAG A 501     1555   1555  1.44  
LINK         O4  NAG A 501                 C1  NAG A 502     1555   1555  1.46  
LINK         OG1 THR A  32                 C1  MAN A 504     1555   1555  1.47  
CISPEP   1 VAL A  233    PRO A  234          0        -6.13                     
CISPEP   2 TYR A  250    PRO A  251          0        -1.86                     
CISPEP   3 CYS A  297    PRO A  298          0        -0.35                     
SITE     1 AC1  2 THR A  32  ASP A  33                                          
SITE     1 AC2  6 ASN A 253  ASP A 279  ASP A 280  GLN A 282                    
SITE     2 AC2  6 GLY A 283  GLN A 289                                          
CRYST1   77.507   77.507   59.773  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      0.012902  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012902  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016730        0.00000                         
TER    2188      HIS A 304                                                      
MASTER      314    0    3   13   14    0    3    6 2238    1   43   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:
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