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LongText Report for: 4N8S-pdb

Name Class
4N8S-pdb
HEADER    HYDROLASE                               18-OCT-13   4N8S              
TITLE     CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF LIPASE FROM THERMOMYCES   
TITLE    2 LANUGINOSA WITH ETHYLACETOACETATE AND P-NITROBENZALDEHYDE AT 2.3 A   
TITLE    3 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TRIACYLGLYCEROL LIPASE;                                     
COMPND   5 EC: 3.1.1.3                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOMYCES LANUGINOSUS;                        
SOURCE   3 ORGANISM_TAXID: 5541                                                 
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.KUMAR,J.MUKHERJEE,M.N.GUPTA,M.SINHA,P.KAUR,S.SHARMA,T.P.SINGH       
REVDAT   1   06-NOV-13 4N8S    0                                                
JRNL        AUTH   M.KUMAR,J.MUKHERJEE,M.N.GUPTA,M.SINHA,P.KAUR,S.SHARMA,       
JRNL        AUTH 2 T.P.SINGH                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF LIPASE FROM      
JRNL        TITL 2 THERMOMYCES LANUGINOSA WITH ETHYLACETOACETATE AND            
JRNL        TITL 3 P-NITROBENZALDEHYDE AT 2.3 A RESOLUTION                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 37933                          
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2051                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2620                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 136                          
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4142                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 163                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 23.01000                                             
REMARK   3    B22 (A**2) : 23.01000                                             
REMARK   3    B33 (A**2) : -46.01000                                            
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): 0.051         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.045         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.254         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.521        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4321 ; 0.020 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2842 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5883 ; 2.081 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6854 ; 1.090 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   536 ; 7.979 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   210 ;38.777 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   622 ;17.227 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;18.940 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   637 ; 0.120 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4960 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   940 ; 0.002 ; 0.020       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.829                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : K, H, -L                                        
REMARK   3      TWIN FRACTION : 0.171                                           
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4N8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082895.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40215                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 121.670                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200   FOR THE DATA SET  : 41.5000                            
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) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30500                            
REMARK 200   FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 4DYH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 0.1M NACL, 1.6M AMMONIUM     
REMARK 280  SULPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       26.76300            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       53.52600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.14450            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.90750            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       13.38150            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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    ASN A  25       41.03   -147.79                                   
REMARK 500    CYS A  41       58.95   -153.44                                   
REMARK 500    LYS A  74       62.31     62.40                                   
REMARK 500    SER A 146     -110.25     67.49                                   
REMARK 500    THR A 199     -119.72     32.53                                   
REMARK 500    ASP A 242       40.99     35.04                                   
REMARK 500    PRO A 250       30.81    -89.85                                   
REMARK 500    LYS B  24       53.04    -91.29                                   
REMARK 500    ASN B  26     -123.70     46.16                                   
REMARK 500    CYS B  41       57.98   -140.61                                   
REMARK 500    ASP B  62       62.75     17.47                                   
REMARK 500    LYS B  74       60.07     64.53                                   
REMARK 500    ASN B  92       30.05    -89.59                                   
REMARK 500    HIS B 110      117.27    -20.87                                   
REMARK 500    SER B 146     -116.56     62.16                                   
REMARK 500    VAL B 154      -60.63   -106.27                                   
REMARK 500    GLN B 188      134.37    -37.68                                   
REMARK 500    THR B 199     -123.01     30.39                                   
REMARK 500    ASP B 201      140.34    -26.02                                   
REMARK 500    ARG B 209      -19.84    103.19                                   
REMARK 500    LEU B 227       23.15     49.89                                   
REMARK 500    ASP B 242       24.16     45.09                                   
REMARK 500    PHE B 262       -2.37     60.79                                   
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 B  244     GLY B  245                 -148.82                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 175         0.12    SIDE CHAIN                              
REMARK 500    ARG A 232         0.10    SIDE CHAIN                              
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 XXH A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EAC A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XXH B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EAC B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 301 BOUND   
REMARK 800  TO ASN A 33                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 301 BOUND   
REMARK 800  TO ASN B 33                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DYH   RELATED DB: PDB                                   
REMARK 900 MODEL PDB                                                            
DBREF  4N8S A    1   269  UNP    O59952   LIP_THELA       23    291             
DBREF  4N8S B    1   269  UNP    O59952   LIP_THELA       23    291             
SEQRES   1 A  269  GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE          
SEQRES   2 A  269  ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN          
SEQRES   3 A  269  ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN          
SEQRES   4 A  269  ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU          
SEQRES   5 A  269  TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY          
SEQRES   6 A  269  PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU          
SEQRES   7 A  269  SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY          
SEQRES   8 A  269  ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS          
SEQRES   9 A  269  SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP          
SEQRES  10 A  269  ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP          
SEQRES  11 A  269  ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR          
SEQRES  12 A  269  GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY          
SEQRES  13 A  269  ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE          
SEQRES  14 A  269  SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA          
SEQRES  15 A  269  GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG          
SEQRES  16 A  269  ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO          
SEQRES  17 A  269  ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP          
SEQRES  18 A  269  ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP          
SEQRES  19 A  269  ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN          
SEQRES  20 A  269  ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP          
SEQRES  21 A  269  TYR PHE GLY LEU ILE GLY THR CYS LEU                          
SEQRES   1 B  269  GLU VAL SER GLN ASP LEU PHE ASN GLN PHE ASN LEU PHE          
SEQRES   2 B  269  ALA GLN TYR SER ALA ALA ALA TYR CYS GLY LYS ASN ASN          
SEQRES   3 B  269  ASP ALA PRO ALA GLY THR ASN ILE THR CYS THR GLY ASN          
SEQRES   4 B  269  ALA CYS PRO GLU VAL GLU LYS ALA ASP ALA THR PHE LEU          
SEQRES   5 B  269  TYR SER PHE GLU ASP SER GLY VAL GLY ASP VAL THR GLY          
SEQRES   6 B  269  PHE LEU ALA LEU ASP ASN THR ASN LYS LEU ILE VAL LEU          
SEQRES   7 B  269  SER PHE ARG GLY SER ARG SER ILE GLU ASN TRP ILE GLY          
SEQRES   8 B  269  ASN LEU ASN PHE ASP LEU LYS GLU ILE ASN ASP ILE CYS          
SEQRES   9 B  269  SER GLY CYS ARG GLY HIS ASP GLY PHE THR SER SER TRP          
SEQRES  10 B  269  ARG SER VAL ALA ASP THR LEU ARG GLN LYS VAL GLU ASP          
SEQRES  11 B  269  ALA VAL ARG GLU HIS PRO ASP TYR ARG VAL VAL PHE THR          
SEQRES  12 B  269  GLY HIS SER LEU GLY GLY ALA LEU ALA THR VAL ALA GLY          
SEQRES  13 B  269  ALA ASP LEU ARG GLY ASN GLY TYR ASP ILE ASP VAL PHE          
SEQRES  14 B  269  SER TYR GLY ALA PRO ARG VAL GLY ASN ARG ALA PHE ALA          
SEQRES  15 B  269  GLU PHE LEU THR VAL GLN THR GLY GLY THR LEU TYR ARG          
SEQRES  16 B  269  ILE THR HIS THR ASN ASP ILE VAL PRO ARG LEU PRO PRO          
SEQRES  17 B  269  ARG GLU PHE GLY TYR SER HIS SER SER PRO GLU TYR TRP          
SEQRES  18 B  269  ILE LYS SER GLY THR LEU VAL PRO VAL THR ARG ASN ASP          
SEQRES  19 B  269  ILE VAL LYS ILE GLU GLY ILE ASP ALA THR GLY GLY ASN          
SEQRES  20 B  269  ASN GLN PRO ASN ILE PRO ASP ILE PRO ALA HIS LEU TRP          
SEQRES  21 B  269  TYR PHE GLY LEU ILE GLY THR CYS LEU                          
MODRES 4N8S ASN A   33  ASN  GLYCOSYLATION SITE                                 
MODRES 4N8S ASN B   33  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 301      14                                                       
HET    XXH  A 302      11                                                       
HET    EAC  A 303       9                                                       
HET    NAG  B 301      14                                                       
HET    XXH  B 302      11                                                       
HET    EAC  B 303       9                                                       
HET    GOL  B 304       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     XXH 4-NITROBENZALDEHYDE                                              
HETNAM     EAC ETHYL 3-OXOBUTANOATE                                             
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  XXH    2(C7 H5 N O3)                                                
FORMUL   5  EAC    2(C6 H10 O3)                                                 
FORMUL   9  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *163(H2 O)                                                    
HELIX    1   1 SER A    3  GLY A   23  1                                  21    
HELIX    2   2 CYS A   41  ALA A   47  1                                   7    
HELIX    3   3 SER A   85  ASN A   92  1                                   8    
HELIX    4   4 ASP A  111  HIS A  135  1                                  25    
HELIX    5   5 SER A  146  ARG A  160  1                                  15    
HELIX    6   6 ARG A  179  GLN A  188  1                                  10    
HELIX    7   7 ILE A  202  LEU A  206  5                                   5    
HELIX    8   8 PRO A  208  PHE A  211  5                                   4    
HELIX    9   9 THR A  231  ASN A  233  5                                   3    
HELIX   10  10 ILE A  255  TRP A  260  5                                   6    
HELIX   11  11 SER B    3  GLY B   23  1                                  21    
HELIX   12  12 CYS B   41  ALA B   47  1                                   7    
HELIX   13  13 SER B   85  ASN B   92  1                                   8    
HELIX   14  14 HIS B  110  HIS B  135  1                                  26    
HELIX   15  15 SER B  146  ARG B  160  1                                  15    
HELIX   16  16 ASN B  178  GLN B  188  1                                  11    
HELIX   17  17 ILE B  202  LEU B  206  5                                   5    
HELIX   18  18 THR B  231  ASN B  233  5                                   3    
HELIX   19  19 ILE B  255  TRP B  260  5                                   6    
SHEET    1   A 8 ALA A  49  SER A  58  0                                        
SHEET    2   A 8 VAL A  63  ASP A  70 -1  O  LEU A  67   N  LEU A  52           
SHEET    3   A 8 LEU A  75  PHE A  80 -1  O  LEU A  75   N  ASP A  70           
SHEET    4   A 8 ARG A 139  HIS A 145  1  O  THR A 143   N  LEU A  78           
SHEET    5   A 8 ILE A 166  TYR A 171  1  O  ASP A 167   N  PHE A 142           
SHEET    6   A 8 LEU A 193  HIS A 198  1  O  TYR A 194   N  VAL A 168           
SHEET    7   A 8 GLU A 219  ILE A 222  1  O  ILE A 222   N  THR A 197           
SHEET    8   A 8 ILE A 235  ILE A 238 -1  O  VAL A 236   N  TRP A 221           
SHEET    1   B 2 LEU A  97  ILE A 100  0                                        
SHEET    2   B 2 CYS A 107  HIS A 110 -1  O  GLY A 109   N  LYS A  98           
SHEET    1   C 2 GLY A 177  ASN A 178  0                                        
SHEET    2   C 2 TYR A 213  SER A 214 -1  O  SER A 214   N  GLY A 177           
SHEET    1   D 8 ALA B  49  SER B  58  0                                        
SHEET    2   D 8 VAL B  63  ASP B  70 -1  O  LEU B  67   N  LEU B  52           
SHEET    3   D 8 LEU B  75  PHE B  80 -1  O  SER B  79   N  PHE B  66           
SHEET    4   D 8 ARG B 139  HIS B 145  1  O  THR B 143   N  LEU B  78           
SHEET    5   D 8 ILE B 166  TYR B 171  1  O  TYR B 171   N  GLY B 144           
SHEET    6   D 8 LEU B 193  HIS B 198  1  O  TYR B 194   N  VAL B 168           
SHEET    7   D 8 GLU B 219  ILE B 222  1  O  ILE B 222   N  THR B 197           
SHEET    8   D 8 ILE B 235  ILE B 238 -1  O  ILE B 238   N  GLU B 219           
SSBOND   1 CYS A   22    CYS A  268                          1555   1555  2.05  
SSBOND   2 CYS A   36    CYS A   41                          1555   1555  2.07  
SSBOND   3 CYS A  104    CYS A  107                          1555   1555  2.06  
SSBOND   4 CYS B   22    CYS B  268                          1555   1555  2.05  
SSBOND   5 CYS B   36    CYS B   41                          1555   1555  2.04  
SSBOND   6 CYS B  104    CYS B  107                          1555   1555  1.91  
LINK         ND2 ASN A  33                 C1  NAG A 301     1555   1555  1.48  
LINK         ND2 ASN B  33                 C1  NAG B 301     1555   1555  1.48  
CISPEP   1 LEU A  206    PRO A  207          0        -5.04                     
CISPEP   2 SER A  217    PRO A  218          0        -8.17                     
CISPEP   3 LEU B  206    PRO B  207          0        -1.38                     
CISPEP   4 SER B  217    PRO B  218          0        -0.66                     
SITE     1 AC1  9 ALA A  14  GLN A  15  ASN A  39  ALA A  40                    
SITE     2 AC1  9 TYR A 261  GLY A 263  LEU A 264  HOH A 431                    
SITE     3 AC1  9 LEU B 227                                                     
SITE     1 AC2  5 ARG A  81  GLY A  82  SER A  83  ARG A  84                    
SITE     2 AC2  5 SER A  85                                                     
SITE     1 AC3  9 SER A   3  ASP A   5  ASP B   5  GLN B   9                    
SITE     2 AC3  9 LEU B  12  GLU B  43  ASN B  73  HOH B 421                    
SITE     3 AC3  9 HOH B 488                                                     
SITE     1 AC4  4 SER B  83  ARG B  84  SER B  85  TRP B  89                    
SITE     1 AC5  6 LEU A 227  PRO A 229  TRP A 260  LEU B 227                    
SITE     2 AC5  6 PRO B 229  TRP B 260                                          
SITE     1 AC6  2 ASN A  33  ASP A  48                                          
SITE     1 AC7  2 ASN B  33  HOH B 414                                          
CRYST1  140.461  140.461   80.289  90.00  90.00 120.00 P 61         12          
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      0.007119  0.004110  0.000000        0.00000                         
SCALE2      0.000000  0.008221  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012455        0.00000                         
TER    2072      LEU A 269                                                      
TER    4144      LEU B 269                                                      
MASTER      359    0    7   19   20    0   13    6 4379    2   88   42          
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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