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Database: PDB
Entry: 2PBF
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HEADER    TRANSFERASE                             28-MAR-07   2PBF              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE PROTEIN-L-ISOASPARTATE O-             
TITLE    2 METHYLTRANSFERASE BETA-ASPARTATE METHYLTRANSFERASE (PCMT) FROM       
TITLE    3 PLASMODIUM FALCIPARUM IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE BETA-ASPARTATE  
COMPND   3 METHYLTRANSFERASE;                                                   
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: RESIDUES 15-240;                                           
COMPND   6 EC: 2.1.1.77;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_TAXID: 36329;                                               
SOURCE   4 STRAIN: 3D7;                                                         
SOURCE   5 GENE: PF14_0309;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: P15-LIC                                   
KEYWDS    METHYLTRANSFERASE, PROTEIN REPAIR, ISOASPARTYL FORMATION, P.          
KEYWDS   2 FALCIPARUM, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.WERNIMONT,A.HASSANALI,L.LIN,J.LEW,Y.ZHAO,M.RAVICHANDRAN,G.WASNEY, 
AUTHOR   2 M.VEDADI,I.KOZIERADZKI,A.BOCHKAREV,A.M.EDWARDS,C.H.ARROWSMITH,       
AUTHOR   3 J.WEIGELT,M.SUNDSTROM,R.HUI,W.QIU,STRUCTURAL GENOMICS CONSORTIUM     
AUTHOR   4 (SGC)                                                                
REVDAT   5   30-AUG-23 2PBF    1       REMARK SEQADV                            
REVDAT   4   18-OCT-17 2PBF    1       REMARK                                   
REVDAT   3   13-JUL-11 2PBF    1       VERSN                                    
REVDAT   2   24-FEB-09 2PBF    1       VERSN                                    
REVDAT   1   10-APR-07 2PBF    0                                                
JRNL        AUTH   A.K.WERNIMONT,A.HASSANALI,L.LIN,J.LEW,Y.ZHAO,M.RAVICHANDRAN, 
JRNL        AUTH 2 G.WASNEY,M.VEDADI,I.KOZIERADZKI,A.BOCHKAREV,A.M.EDWARDS,     
JRNL        AUTH 3 C.H.ARROWSMITH,J.WEIGELT,M.SUNDSTROM,R.HUI,W.QIU             
JRNL        TITL   CRYSTAL STRUCTURE OF A PUTATIVE PROTEIN-L-ISOASPARTATE       
JRNL        TITL 2 O-METHYLTRANSFERASE BETA-ASPARTATE METHYLTRANSFERASE (PCMT)  
JRNL        TITL 3 FROM PLASMODIUM FALCIPARUM IN COMPLEX WITH                   
JRNL        TITL 4 S-ADENOSYL-L-HOMOCYSTEINE                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 31337                          
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1673                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2278                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 124                          
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3476                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 181                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.46000                                              
REMARK   3    B22 (A**2) : 1.46000                                              
REMARK   3    B33 (A**2) : -2.19000                                             
REMARK   3    B12 (A**2) : 0.73000                                              
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): 0.216         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.188         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.175         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.398         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3582 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4832 ; 1.503 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   432 ; 6.484 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   154 ;38.433 ;25.325       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   696 ;16.646 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;23.120 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   566 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2580 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1845 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2434 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   229 ; 0.175 ; 0.200       
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):    18 ; 0.243 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.126 ; 0.200       
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):  2246 ; 0.761 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3540 ; 1.309 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1502 ; 1.906 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1292 ; 2.870 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      9       A     227      5                      
REMARK   3           1     B      9       B     227      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    872 ;  0.05 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    863 ;  0.24 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    872 ;  0.29 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    863 ;  0.78 ; 10.00           
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   : 1.40                                          
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 2PBF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042191.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33234                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.07400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.89900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.71300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1L1N                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M (NH4)2SO4, 0.1 M     
REMARK 280  HEPES PH 7.2, 2 MM SAH, VAPOR DIFFUSION, SITTING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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       51.59267            
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       25.79633            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). AUTHORS STATE THAT THE                 
REMARK 300 BIOLOGICAL UNIT OF THIS PROTEIN IS A MONOMER.                        
REMARK 300 SEE REMARK 350 FOR INFORMATION ON GENERATING THE                     
REMARK 300 BIOLOGICAL MOLECULE(S).                                              
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     TYR A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     TYR B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     LYS B   210                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 155    CD   OE1  OE2                                       
REMARK 470     ASP A 196    CG   OD1  OD2                                       
REMARK 470     GLU B 159    CD   OE1  OE2                                       
REMARK 470     ASP B 196    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   384     O    HOH A   388              2.10            
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    LEU A 189   CA  -  CB  -  CG  ANGL. DEV. =  15.3 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    ILE A  46       60.84     23.56                                   
REMARK 500    ILE A  55      -66.65   -104.27                                   
REMARK 500    SER A  56      166.67    175.81                                   
REMARK 500    ASN A 186       -1.53     73.06                                   
REMARK 500    ASP A 196     -101.31     54.67                                   
REMARK 500    ASN A 208      -69.68   -134.59                                   
REMARK 500    LEU A 216      -79.86    -90.05                                   
REMARK 500    ILE B  46       60.86     26.53                                   
REMARK 500    ILE B  55      -68.44   -104.37                                   
REMARK 500    SER B  56      165.79    176.00                                   
REMARK 500    GLU B 194      109.77    -53.06                                   
REMARK 500    ASP B 196     -102.95     57.68                                   
REMARK 500    ASN B 208      -78.47   -129.08                                   
REMARK 500    LEU B 216      -77.26    -93.76                                   
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 LYS A  207     ASN A  208                  148.48                    
REMARK 500 LYS B  207     ASN B  208                  143.38                    
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 SAH A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAH B 301                 
DBREF  2PBF A    2   227  UNP    Q8ILD5   Q8ILD5_PLAF7    15    240             
DBREF  2PBF B    2   227  UNP    Q8ILD5   Q8ILD5_PLAF7    15    240             
SEQADV 2PBF GLY A    1  UNP  Q8ILD5              CLONING ARTIFACT               
SEQADV 2PBF GLY B    1  UNP  Q8ILD5              CLONING ARTIFACT               
SEQRES   1 A  227  GLY ASN ASN MET TYR LYS LEU SER GLU ASN ASN HIS LYS          
SEQRES   2 A  227  SER LEU LEU GLU ASN LEU LYS ARG ARG GLY ILE ILE ASP          
SEQRES   3 A  227  ASP ASP ASP VAL TYR ASN THR MET LEU GLN VAL ASP ARG          
SEQRES   4 A  227  GLY LYS TYR ILE LYS GLU ILE PRO TYR ILE ASP THR PRO          
SEQRES   5 A  227  VAL TYR ILE SER HIS GLY VAL THR ILE SER ALA PRO HIS          
SEQRES   6 A  227  MET HIS ALA LEU SER LEU LYS ARG LEU ILE ASN VAL LEU          
SEQRES   7 A  227  LYS PRO GLY SER ARG ALA ILE ASP VAL GLY SER GLY SER          
SEQRES   8 A  227  GLY TYR LEU THR VAL CYS MET ALA ILE LYS MET ASN VAL          
SEQRES   9 A  227  LEU GLU ASN LYS ASN SER TYR VAL ILE GLY LEU GLU ARG          
SEQRES  10 A  227  VAL LYS ASP LEU VAL ASN PHE SER LEU GLU ASN ILE LYS          
SEQRES  11 A  227  ARG ASP LYS PRO GLU LEU LEU LYS ILE ASP ASN PHE LYS          
SEQRES  12 A  227  ILE ILE HIS LYS ASN ILE TYR GLN VAL ASN GLU GLU GLU          
SEQRES  13 A  227  LYS LYS GLU LEU GLY LEU PHE ASP ALA ILE HIS VAL GLY          
SEQRES  14 A  227  ALA SER ALA SER GLU LEU PRO GLU ILE LEU VAL ASP LEU          
SEQRES  15 A  227  LEU ALA GLU ASN GLY LYS LEU ILE ILE PRO ILE GLU GLU          
SEQRES  16 A  227  ASP TYR THR GLN VAL LEU TYR GLU ILE THR LYS LYS ASN          
SEQRES  17 A  227  GLY LYS ILE ILE LYS ASP ARG LEU PHE ASP VAL CYS PHE          
SEQRES  18 A  227  VAL SER LEU LYS LYS ASN                                      
SEQRES   1 B  227  GLY ASN ASN MET TYR LYS LEU SER GLU ASN ASN HIS LYS          
SEQRES   2 B  227  SER LEU LEU GLU ASN LEU LYS ARG ARG GLY ILE ILE ASP          
SEQRES   3 B  227  ASP ASP ASP VAL TYR ASN THR MET LEU GLN VAL ASP ARG          
SEQRES   4 B  227  GLY LYS TYR ILE LYS GLU ILE PRO TYR ILE ASP THR PRO          
SEQRES   5 B  227  VAL TYR ILE SER HIS GLY VAL THR ILE SER ALA PRO HIS          
SEQRES   6 B  227  MET HIS ALA LEU SER LEU LYS ARG LEU ILE ASN VAL LEU          
SEQRES   7 B  227  LYS PRO GLY SER ARG ALA ILE ASP VAL GLY SER GLY SER          
SEQRES   8 B  227  GLY TYR LEU THR VAL CYS MET ALA ILE LYS MET ASN VAL          
SEQRES   9 B  227  LEU GLU ASN LYS ASN SER TYR VAL ILE GLY LEU GLU ARG          
SEQRES  10 B  227  VAL LYS ASP LEU VAL ASN PHE SER LEU GLU ASN ILE LYS          
SEQRES  11 B  227  ARG ASP LYS PRO GLU LEU LEU LYS ILE ASP ASN PHE LYS          
SEQRES  12 B  227  ILE ILE HIS LYS ASN ILE TYR GLN VAL ASN GLU GLU GLU          
SEQRES  13 B  227  LYS LYS GLU LEU GLY LEU PHE ASP ALA ILE HIS VAL GLY          
SEQRES  14 B  227  ALA SER ALA SER GLU LEU PRO GLU ILE LEU VAL ASP LEU          
SEQRES  15 B  227  LEU ALA GLU ASN GLY LYS LEU ILE ILE PRO ILE GLU GLU          
SEQRES  16 B  227  ASP TYR THR GLN VAL LEU TYR GLU ILE THR LYS LYS ASN          
SEQRES  17 B  227  GLY LYS ILE ILE LYS ASP ARG LEU PHE ASP VAL CYS PHE          
SEQRES  18 B  227  VAL SER LEU LYS LYS ASN                                      
HET    SAH  A 301      26                                                       
HET    SAH  B 301      26                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   5  HOH   *181(H2 O)                                                    
HELIX    1   1 ASN A   11  ARG A   22  1                                  12    
HELIX    2   2 ASP A   27  GLN A   36  1                                  10    
HELIX    3   3 VAL A   37  TYR A   42  5                                   6    
HELIX    4   4 ALA A   63  ILE A   75  1                                  13    
HELIX    5   5 GLY A   92  MET A  102  1                                  11    
HELIX    6   6 VAL A  118  LYS A  133  1                                  16    
HELIX    7   7 PRO A  134  LYS A  138  5                                   5    
HELIX    8   8 ASN A  148  VAL A  152  5                                   5    
HELIX    9   9 ASN A  153  GLY A  161  1                                   9    
HELIX   10  10 PRO A  176  LEU A  182  1                                   7    
HELIX   11  11 ASN B   11  ARG B   22  1                                  12    
HELIX   12  12 ASP B   27  GLN B   36  1                                  10    
HELIX   13  13 VAL B   37  TYR B   42  5                                   6    
HELIX   14  14 ALA B   63  ILE B   75  1                                  13    
HELIX   15  15 GLY B   92  MET B  102  1                                  11    
HELIX   16  16 VAL B  118  LYS B  133  1                                  16    
HELIX   17  17 PRO B  134  ILE B  139  5                                   6    
HELIX   18  18 ASN B  148  VAL B  152  5                                   5    
HELIX   19  19 ASN B  153  GLY B  161  1                                   9    
HELIX   20  20 PRO B  176  LEU B  182  1                                   7    
SHEET    1   A 2 VAL A  53  SER A  56  0                                        
SHEET    2   A 2 VAL A  59  ILE A  61 -1  O  VAL A  59   N  ILE A  55           
SHEET    1   B 7 PHE A 142  HIS A 146  0                                        
SHEET    2   B 7 TYR A 111  GLU A 116  1  N  GLY A 114   O  ILE A 145           
SHEET    3   B 7 ARG A  83  VAL A  87  1  N  ASP A  86   O  LEU A 115           
SHEET    4   B 7 PHE A 163  VAL A 168  1  O  HIS A 167   N  VAL A  87           
SHEET    5   B 7 LEU A 183  GLU A 195  1  O  ILE A 190   N  ILE A 166           
SHEET    6   B 7 THR A 198  THR A 205 -1  O  ILE A 204   N  LEU A 189           
SHEET    7   B 7 ILE A 212  VAL A 219 -1  O  VAL A 219   N  GLN A 199           
SHEET    1   C 2 VAL B  53  SER B  56  0                                        
SHEET    2   C 2 VAL B  59  ILE B  61 -1  O  VAL B  59   N  ILE B  55           
SHEET    1   D 7 PHE B 142  HIS B 146  0                                        
SHEET    2   D 7 TYR B 111  GLU B 116  1  N  GLY B 114   O  ILE B 145           
SHEET    3   D 7 ARG B  83  VAL B  87  1  N  ALA B  84   O  TYR B 111           
SHEET    4   D 7 PHE B 163  VAL B 168  1  O  HIS B 167   N  VAL B  87           
SHEET    5   D 7 LEU B 183  GLU B 195  1  O  ILE B 190   N  ILE B 166           
SHEET    6   D 7 THR B 198  THR B 205 -1  O  ILE B 204   N  LEU B 189           
SHEET    7   D 7 ILE B 212  VAL B 219 -1  O  VAL B 219   N  GLN B 199           
SITE     1 AC1 24 VAL A  59  THR A  60  ILE A  61  SER A  62                    
SITE     2 AC1 24 HIS A  67  GLY A  88  SER A  89  GLY A  90                    
SITE     3 AC1 24 SER A  91  GLU A 116  ARG A 117  VAL A 118                    
SITE     4 AC1 24 LYS A 147  ASN A 148  ILE A 149  GLY A 169                    
SITE     5 AC1 24 VAL A 222  SER A 223  LEU A 224  LYS A 225                    
SITE     6 AC1 24 HOH A 305  HOH A 315  HOH A 319  HOH A 379                    
SITE     1 AC2 24 VAL B  59  THR B  60  ILE B  61  SER B  62                    
SITE     2 AC2 24 HIS B  67  GLY B  88  SER B  89  GLY B  90                    
SITE     3 AC2 24 SER B  91  GLU B 116  ARG B 117  VAL B 118                    
SITE     4 AC2 24 LYS B 147  ASN B 148  ILE B 149  GLY B 169                    
SITE     5 AC2 24 VAL B 222  SER B 223  LEU B 224  LYS B 225                    
SITE     6 AC2 24 HOH B 307  HOH B 317  HOH B 321  HOH B 379                    
CRYST1   75.156   75.156   77.389  90.00  90.00 120.00 P 32          6          
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      0.013306  0.007682  0.000000        0.00000                         
SCALE2      0.000000  0.015364  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012922        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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