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Database: PDB
Entry: 4NBI
LinkDB: 4NBI
Original site: 4NBI 
HEADER    HYDROLASE                               23-OCT-13   4NBI              
TITLE     D-AMINOACYL-TRNA DEACYLASE (DTD) FROM PLASMODIUM FALCIPARUM IN COMPLEX
TITLE    2 WITH D-TYROSYL-3'-AMINOADENOSINE AT 1.86 ANGSTROM RESOLUTION         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-TYROSYL-TRNA(TYR) DEACYLASE;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.-.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_TAXID: 36329;                                               
SOURCE   4 STRAIN: 3D7;                                                         
SOURCE   5 GENE: DTD, PF11_0095;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-21B                                   
KEYWDS    DTD, DEACYLASE, DTD-LIKE, HYDROLASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.AHMAD,S.B.ROUTH,V.KAMARTHAPU,R.SANKARANARAYANAN                     
REVDAT   3   08-NOV-23 4NBI    1       REMARK                                   
REVDAT   2   15-NOV-17 4NBI    1       REMARK                                   
REVDAT   1   18-DEC-13 4NBI    0                                                
JRNL        AUTH   S.AHMAD,S.B.ROUTH,V.KAMARTHAPU,J.CHALISSERY,S.MUTHUKUMAR,    
JRNL        AUTH 2 T.HUSSAIN,S.P.KRUPARANI,M.V.DESHMUKH,R.SANKARANARAYANAN      
JRNL        TITL   MECHANISM OF CHIRAL PROOFREADING DURING TRANSLATION OF THE   
JRNL        TITL 2 GENETIC CODE.                                                
JRNL        REF    ELIFE                         V.   2 01519 2013              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   24302572                                                     
JRNL        DOI    10.7554/ELIFE.01519                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 25154                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1276                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.86                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1619                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2593                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 250                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.71000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -1.77000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.58000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.155         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.082         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.651         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2693 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3633 ; 1.093 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   311 ; 5.891 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   129 ;45.213 ;25.504       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   501 ;12.881 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;12.760 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   402 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1992 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES                                                  
REMARK   4                                                                      
REMARK   4 4NBI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082993.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, PHASER                                        
REMARK 200 STARTING MODEL: 3KNF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 3350, 0.6M SODIUM CHLORIDE,      
REMARK 280  0.1M HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       41.06700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.87150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       41.06700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       32.87150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 3790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14440 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 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     LYS A   164                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     ILE B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     ASN B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     LYS B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     ASN B   161                                                      
REMARK 465     LEU B   162                                                      
REMARK 465     ASN B   163                                                      
REMARK 465     LYS B   164                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   28   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU A   32   CD   OE1  OE2                                       
REMARK 480     LYS A   34   CE   NZ                                             
REMARK 480     LYS A   45   CE   NZ                                             
REMARK 480     ASN A   69   CB   CG   OD1  ND2                                  
REMARK 480     ASN B   94   CG   OD1  ND2                                       
REMARK 480     LYS B   97   CD   CE   NZ                                        
REMARK 480     ASP B  102   CB   CG   OD1  OD2                                  
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    GLU A  32   CG    GLU A  32   CD     -0.109                       
REMARK 500    ASN A  69   CA    ASN A  69   CB      0.182                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASN A  69   N   -  CA  -  CB  ANGL. DEV. = -27.7 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    LYS A  34     -135.58    -94.08                                   
REMARK 500    ASN A  67     -113.13    -92.46                                   
REMARK 500    TYR A 127     -109.41   -117.47                                   
REMARK 500    LYS B  34     -134.63    -94.71                                   
REMARK 500    PHE B  92       65.31   -110.12                                   
REMARK 500    PHE B 103       42.05    -97.04                                   
REMARK 500    TYR B 127     -113.51   -114.51                                   
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 D3Y A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D3Y B 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4NBJ   RELATED DB: PDB                                   
DBREF  4NBI A    1   164  UNP    Q8IIS0   Q8IIS0_PLAF7     1    164             
DBREF  4NBI B    1   164  UNP    Q8IIS0   Q8IIS0_PLAF7     1    164             
SEQRES   1 A  164  MET ARG VAL VAL ILE GLN ARG VAL LYS GLY ALA ILE LEU          
SEQRES   2 A  164  SER VAL ARG LYS GLU ASN ILE GLY GLU ASN GLU LYS GLU          
SEQRES   3 A  164  LEU GLU ILE ILE SER GLU ILE LYS ASN GLY LEU ILE CYS          
SEQRES   4 A  164  PHE LEU GLY ILE HIS LYS ASN ASP THR TRP GLU ASP ALA          
SEQRES   5 A  164  LEU TYR ILE ILE ARG LYS CYS LEU ASN LEU ARG LEU TRP          
SEQRES   6 A  164  ASN ASN ASP ASN LYS THR TRP ASP LYS ASN VAL LYS ASP          
SEQRES   7 A  164  LEU ASN TYR GLU LEU LEU ILE VAL SER GLN PHE THR LEU          
SEQRES   8 A  164  PHE GLY ASN THR LYS LYS GLY ASN LYS PRO ASP PHE HIS          
SEQRES   9 A  164  LEU ALA LYS GLU PRO ASN GLU ALA LEU ILE PHE TYR ASN          
SEQRES  10 A  164  LYS ILE ILE ASP GLU PHE LYS LYS GLN TYR ASN ASP ASP          
SEQRES  11 A  164  LYS ILE LYS ILE GLY LYS PHE GLY ASN TYR MET ASN ILE          
SEQRES  12 A  164  ASP VAL THR ASN ASP GLY PRO VAL THR ILE TYR ILE ASP          
SEQRES  13 A  164  THR HIS ASP ILE ASN LEU ASN LYS                              
SEQRES   1 B  164  MET ARG VAL VAL ILE GLN ARG VAL LYS GLY ALA ILE LEU          
SEQRES   2 B  164  SER VAL ARG LYS GLU ASN ILE GLY GLU ASN GLU LYS GLU          
SEQRES   3 B  164  LEU GLU ILE ILE SER GLU ILE LYS ASN GLY LEU ILE CYS          
SEQRES   4 B  164  PHE LEU GLY ILE HIS LYS ASN ASP THR TRP GLU ASP ALA          
SEQRES   5 B  164  LEU TYR ILE ILE ARG LYS CYS LEU ASN LEU ARG LEU TRP          
SEQRES   6 B  164  ASN ASN ASP ASN LYS THR TRP ASP LYS ASN VAL LYS ASP          
SEQRES   7 B  164  LEU ASN TYR GLU LEU LEU ILE VAL SER GLN PHE THR LEU          
SEQRES   8 B  164  PHE GLY ASN THR LYS LYS GLY ASN LYS PRO ASP PHE HIS          
SEQRES   9 B  164  LEU ALA LYS GLU PRO ASN GLU ALA LEU ILE PHE TYR ASN          
SEQRES  10 B  164  LYS ILE ILE ASP GLU PHE LYS LYS GLN TYR ASN ASP ASP          
SEQRES  11 B  164  LYS ILE LYS ILE GLY LYS PHE GLY ASN TYR MET ASN ILE          
SEQRES  12 B  164  ASP VAL THR ASN ASP GLY PRO VAL THR ILE TYR ILE ASP          
SEQRES  13 B  164  THR HIS ASP ILE ASN LEU ASN LYS                              
HET    D3Y  A 201      31                                                       
HET    PGE  A 502      10                                                       
HET    D3Y  B 201      31                                                       
HETNAM     D3Y 3'-DEOXY-3'-(D-TYROSYLAMINO)ADENOSINE                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   3  D3Y    2(C19 H23 N7 O5)                                             
FORMUL   4  PGE    C6 H14 O4                                                    
FORMUL   6  HOH   *250(H2 O)                                                    
HELIX    1   1 THR A   48  LEU A   62  1                                  15    
HELIX    2   2 PHE A   89  GLY A   93  5                                   5    
HELIX    3   3 GLU A  108  TYR A  127  1                                  20    
HELIX    4   4 ASN A  128  ASP A  130  5                                   3    
HELIX    5   5 HIS A  158  ILE A  160  5                                   3    
HELIX    6   6 THR B   48  LEU B   62  1                                  15    
HELIX    7   7 PHE B   89  GLY B   93  5                                   5    
HELIX    8   8 GLU B  108  TYR B  127  1                                  20    
HELIX    9   9 ASN B  128  ASP B  130  5                                   3    
SHEET    1   A 6 LEU A  27  ILE A  33  0                                        
SHEET    2   A 6 ARG A   2  ARG A  16 -1  N  LEU A  13   O  SER A  31           
SHEET    3   A 6 MET A 141  ASP A 156 -1  O  ASN A 142   N  SER A  14           
SHEET    4   A 6 MET B 141  ASP B 156 -1  O  ILE B 143   N  ASN A 147           
SHEET    5   A 6 ARG B   2  VAL B  15 -1  N  ILE B   5   O  ILE B 153           
SHEET    6   A 6 GLU B  28  ILE B  33 -1  O  SER B  31   N  LEU B  13           
SHEET    1   B10 ILE A 132  ILE A 134  0                                        
SHEET    2   B10 GLU A  82  SER A  87  1  N  LEU A  83   O  LYS A 133           
SHEET    3   B10 GLY A  36  GLY A  42  1  N  CYS A  39   O  LEU A  84           
SHEET    4   B10 ARG A   2  ARG A  16 -1  N  ARG A   2   O  GLY A  42           
SHEET    5   B10 MET A 141  ASP A 156 -1  O  ASN A 142   N  SER A  14           
SHEET    6   B10 MET B 141  ASP B 156 -1  O  ILE B 143   N  ASN A 147           
SHEET    7   B10 ARG B   2  VAL B  15 -1  N  ILE B   5   O  ILE B 153           
SHEET    8   B10 GLY B  36  GLY B  42 -1  O  GLY B  42   N  ARG B   2           
SHEET    9   B10 GLU B  82  SER B  87  1  O  VAL B  86   N  CYS B  39           
SHEET   10   B10 ILE B 132  ILE B 134  1  O  LYS B 133   N  LEU B  83           
CISPEP   1 GLY A  149    PRO A  150          0        -9.78                     
CISPEP   2 GLY B  149    PRO B  150          0       -11.02                     
SITE     1 AC1 14 LEU A  41  ILE A  43  SER A  87  GLN A  88                    
SITE     2 AC1 14 PHE A  89  LYS A 107  ALA A 112  PHE A 137                    
SITE     3 AC1 14 GLY A 138  ASN A 139  HOH A 648  HOH A 705                    
SITE     4 AC1 14 GLY B 149  PRO B 150                                          
SITE     1 AC2  5 ASP A 144  THR A 146  GLY B  10  ILE B  12                    
SITE     2 AC2  5 THR B 146                                                     
SITE     1 AC3 15 GLY A 149  PRO A 150  LEU B  41  ILE B  43                    
SITE     2 AC3 15 SER B  87  GLN B  88  PHE B  89  LYS B 107                    
SITE     3 AC3 15 PHE B 137  GLY B 138  ASN B 139  HOH B 343                    
SITE     4 AC3 15 HOH B 345  HOH B 368  HOH B 393                               
CRYST1   82.134   65.743   56.917  90.00  93.30  90.00 C 1 2 1       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      0.012175  0.000000  0.000702        0.00000                         
SCALE2      0.000000  0.015211  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017599        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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