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LongText Report for: 7cw1-pdb

Name Class
7cw1-pdb
HEADER    HYDROLASE                               27-AUG-20   7CW1              
TITLE     CRYSTAL STRUCTURE OF A BIODEGRADABLE PLASTIC-DEGRADING CUTINASE-LIKE  
TITLE    2 ENZYME FROM THE PHYLLOSPHERE YEAST, PSEUDOZYMA ANTARCTICA, SOLVED BY 
TITLE    3 GETTING THE PHASE FROM ANOMALOUS SCATTERING OF UNCOVALENTLY          
TITLE    4 COORDINATED ARSENIC (CACODYLATE).                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CUTINASE-LIKE ENZYME;                                      
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOZYMA ANTARCTICA;                          
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 84753                                                
KEYWDS    CUTINASE-LIKE ENZYME, BIODEGRADABLE PLASTIC DEGRADING ENZYME,         
KEYWDS   2 ALPHA/BETA HYDROLASE FOLD, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.SUZUKI                                                              
REVDAT   1   16-SEP-20 7CW1    0                                                
JRNL        AUTH   K.SUZUKI                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A BIODEGRADABLE PLASTIC-DEGRADING       
JRNL        TITL 2 CUTINASE-LIKE ENZYME FROM THE PHYLLOSPHERE YEAST, PSEUDOZYMA 
JRNL        TITL 3 ANTARCTICA, SOLVED BY GETTING THE PHASE FROM ANOMALOUS       
JRNL        TITL 4 SCATTERING OF UNCOVALENTLY COORDINATED ARSENIC (CACODYLATE). 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0258                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31548                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1713                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2239                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 119                          
REMARK   3   BIN FREE R VALUE                    : 0.2450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2846                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 361                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.31                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.27000                                             
REMARK   3    B33 (A**2) : 0.41000                                              
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): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.106         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.064         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.913         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2910 ; 0.012 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  2586 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3962 ; 1.684 ; 1.645       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6014 ; 1.594 ; 1.574       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   392 ; 6.673 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   130 ;31.162 ;23.692       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   422 ;11.061 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;19.603 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   400 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3376 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   580 ; 0.001 ; 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  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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 7CW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300017284.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NUMERICAL LINK TYPE SI(111)        
REMARK 200                                   DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2 0.6.2                         
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.4                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33315                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 12.90                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.48700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CRANK2 2.0.229                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M SODIUM ACETATE TRIHYDRATE,         
REMARK 280  0.085M SODIUM CACODYLATE TRIHYDRATE , 25.5%W/V POLYETHYLENE         
REMARK 280  GLYCOL 8000, 15%W/V POLYETHYLENE GLYCOL 400, PH 6.5, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       22.03250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.19350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.79350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.19350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.03250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.79350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 8400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 8360 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ALA B     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B  30   CG  -  CD  -  NE  ANGL. DEV. = -14.6 DEGREES          
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    THR A  14     -124.83     45.02                                   
REMARK 500    SER A  82     -128.39     60.88                                   
REMARK 500    ASN B  71      106.48   -164.66                                   
REMARK 500    SER B  82     -123.49     64.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7CC4   RELATED DB: PDB                                   
REMARK 900 7CC4 CONTAINS THE SAME PROTEIN THAT WAS SOLVED BY THE MOLECULAR      
REMARK 900 REPLACEMENT METHOD.                                                  
DBREF  7CW1 A    1   198  UNP    S6BC01   S6BC01_PSEA2    27    224             
DBREF  7CW1 B    1   198  UNP    S6BC01   S6BC01_PSEA2    27    224             
SEQRES   1 A  198  ALA GLY CYS SER SER TYR VAL ILE ILE ASN THR ARG GLY          
SEQRES   2 A  198  THR SER GLU PRO GLN GLY PRO SER VAL GLY PHE ARG THR          
SEQRES   3 A  198  MET ASN THR ARG ILE ARG SER ALA VAL SER GLY GLY SER          
SEQRES   4 A  198  GLU TYR ASP THR VAL TYR PRO ALA GLY ILE ASP GLN ASN          
SEQRES   5 A  198  SER ALA GLN GLY THR ALA ASN ILE VAL ALA GLN VAL LYS          
SEQRES   6 A  198  ALA GLY LEU ALA ARG ASN PRO ASN THR CYS PHE LEU LEU          
SEQRES   7 A  198  GLU GLY TYR SER GLN GLY ALA ALA ALA THR CYS ASN ALA          
SEQRES   8 A  198  LEU PRO GLN LEU THR GLY ALA ALA PHE ASP ALA VAL LYS          
SEQRES   9 A  198  GLY VAL ILE LEU ILE GLY ASN PRO GLU HIS LYS PRO ASN          
SEQRES  10 A  198  LEU ALA CYS ASN VAL ASP GLY ASN GLY GLY LYS THR THR          
SEQRES  11 A  198  PHE SER ALA ARG GLY ILE SER ALA ALA PHE THR GLN GLY          
SEQRES  12 A  198  VAL PRO SER ASN TRP VAL SER LYS THR LEU ASP ILE CYS          
SEQRES  13 A  198  ILE TYR GLY ASP GLY VAL CYS ASP VAL SER SER GLY PHE          
SEQRES  14 A  198  GLY ILE THR PRO GLN HIS LEU THR TYR GLY TYR ASN THR          
SEQRES  15 A  198  ASN VAL GLN THR MET GLY ALA ASN PHE GLY ILE LYS ALA          
SEQRES  16 A  198  LEU GLN GLY                                                  
SEQRES   1 B  198  ALA GLY CYS SER SER TYR VAL ILE ILE ASN THR ARG GLY          
SEQRES   2 B  198  THR SER GLU PRO GLN GLY PRO SER VAL GLY PHE ARG THR          
SEQRES   3 B  198  MET ASN THR ARG ILE ARG SER ALA VAL SER GLY GLY SER          
SEQRES   4 B  198  GLU TYR ASP THR VAL TYR PRO ALA GLY ILE ASP GLN ASN          
SEQRES   5 B  198  SER ALA GLN GLY THR ALA ASN ILE VAL ALA GLN VAL LYS          
SEQRES   6 B  198  ALA GLY LEU ALA ARG ASN PRO ASN THR CYS PHE LEU LEU          
SEQRES   7 B  198  GLU GLY TYR SER GLN GLY ALA ALA ALA THR CYS ASN ALA          
SEQRES   8 B  198  LEU PRO GLN LEU THR GLY ALA ALA PHE ASP ALA VAL LYS          
SEQRES   9 B  198  GLY VAL ILE LEU ILE GLY ASN PRO GLU HIS LYS PRO ASN          
SEQRES  10 B  198  LEU ALA CYS ASN VAL ASP GLY ASN GLY GLY LYS THR THR          
SEQRES  11 B  198  PHE SER ALA ARG GLY ILE SER ALA ALA PHE THR GLN GLY          
SEQRES  12 B  198  VAL PRO SER ASN TRP VAL SER LYS THR LEU ASP ILE CYS          
SEQRES  13 B  198  ILE TYR GLY ASP GLY VAL CYS ASP VAL SER SER GLY PHE          
SEQRES  14 B  198  GLY ILE THR PRO GLN HIS LEU THR TYR GLY TYR ASN THR          
SEQRES  15 B  198  ASN VAL GLN THR MET GLY ALA ASN PHE GLY ILE LYS ALA          
SEQRES  16 B  198  LEU GLN GLY                                                  
HET    CAD  A 201       5                                                       
HET     NA  A 202       1                                                       
HET    CAD  B 201       5                                                       
HETNAM     CAD CACODYLIC ACID                                                   
HETNAM      NA SODIUM ION                                                       
HETSYN     CAD HYDROXYDIMETHYLARSINE OXIDE                                      
FORMUL   3  CAD    2(C2 H7 AS O2)                                               
FORMUL   4   NA    NA 1+                                                        
FORMUL   6  HOH   *361(H2 O)                                                    
HELIX    1 AA1 SER A   21  GLY A   23  5                                   3    
HELIX    2 AA2 PHE A   24  VAL A   35  1                                  12    
HELIX    3 AA3 SER A   53  ASN A   71  1                                  19    
HELIX    4 AA4 SER A   82  LEU A   92  1                                  11    
HELIX    5 AA5 PRO A   93  LEU A   95  5                                   3    
HELIX    6 AA6 THR A   96  ALA A  102  1                                   7    
HELIX    7 AA7 SER A  137  THR A  141  5                                   5    
HELIX    8 AA8 PRO A  145  SER A  150  5                                   6    
HELIX    9 AA9 THR A  172  TYR A  180  5                                   9    
HELIX   10 AB1 ASN A  181  GLY A  198  1                                  18    
HELIX   11 AB2 SER B   21  GLY B   23  5                                   3    
HELIX   12 AB3 PHE B   24  VAL B   35  1                                  12    
HELIX   13 AB4 SER B   53  ASN B   71  1                                  19    
HELIX   14 AB5 SER B   82  LEU B   92  1                                  11    
HELIX   15 AB6 PRO B   93  THR B   96  5                                   4    
HELIX   16 AB7 GLY B   97  ALA B  102  1                                   6    
HELIX   17 AB8 SER B  137  THR B  141  5                                   5    
HELIX   18 AB9 PRO B  145  SER B  150  5                                   6    
HELIX   19 AC1 ASP B  164  GLY B  168  5                                   5    
HELIX   20 AC2 THR B  172  TYR B  180  5                                   9    
HELIX   21 AC3 ASN B  181  GLY B  198  1                                  18    
SHEET    1 AA1 6 GLU A  40  ASP A  42  0                                        
SHEET    2 AA1 6 TYR A   6  THR A  11  1  N  ILE A   8   O  TYR A  41           
SHEET    3 AA1 6 CYS A  75  TYR A  81  1  O  LEU A  77   N  ILE A   9           
SHEET    4 AA1 6 VAL A 103  ILE A 109  1  O  ILE A 107   N  LEU A  78           
SHEET    5 AA1 6 THR A 152  ILE A 155  1  O  ILE A 155   N  LEU A 108           
SHEET    6 AA1 6 ASN A 121  VAL A 122  1  N  VAL A 122   O  ASP A 154           
SHEET    1 AA2 6 GLY B  38  ASP B  42  0                                        
SHEET    2 AA2 6 TYR B   6  THR B  11  1  N  ILE B   8   O  SER B  39           
SHEET    3 AA2 6 CYS B  75  TYR B  81  1  O  LEU B  77   N  ILE B   9           
SHEET    4 AA2 6 VAL B 103  ILE B 109  1  O  ILE B 107   N  LEU B  78           
SHEET    5 AA2 6 THR B 152  ILE B 155  1  O  LEU B 153   N  LEU B 108           
SHEET    6 AA2 6 ASN B 121  VAL B 122  1  N  VAL B 122   O  ASP B 154           
SSBOND   1 CYS A    3    CYS A   75                          1555   1555  2.09  
SSBOND   2 CYS A  156    CYS A  163                          1555   1555  2.05  
SSBOND   3 CYS B    3    CYS B   75                          1555   1555  2.14  
SSBOND   4 CYS B  156    CYS B  163                          1555   1555  2.09  
LINK        NA    NA A 202                 O   HOH A 366     1555   1555  3.11  
CRYST1   44.065   61.587  110.387  90.00  90.00  90.00 P 21 21 21    8          
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      0.022694  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016237  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009059        0.00000                         
TER    1424      GLY A 198                                                      
TER    2848      GLY B 198                                                      
MASTER      309    0    3   21   12    0    0    6 3218    2   20   32          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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