GenomeNet

Database: PDB
Entry: 1RC1
LinkDB: 1RC1
Original site: 1RC1 
HEADER    TRANSFERASE                             03-NOV-03   1RC1              
TITLE     HUMAN GAR TFASE COMPLEX STRUCTURE WITH POLYGLUTAMATED 10-             
TITLE    2 (TRIFLUOROACETYL)-5,10-DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: (RESIDUES 808-1010);                                       
COMPND   5 SYNONYM: GART; GAR TRANSFORMYLASE; 5'-PHOSPHORIBOSYLGLYCINAMIDE      
COMPND   6 TRANSFORMYLASE;                                                      
COMPND   7 EC: 2.1.2.2;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: PART OF TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN     
COMPND  10 ADENOSINE-3                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PURN;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22A                                    
KEYWDS    PROTEIN-COFACTOR ANALOGUE COMPLEX, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,J.DESHARNAIS,D.L.BOGER,I.A.WILSON                             
REVDAT   3   23-AUG-23 1RC1    1       REMARK SEQADV                            
REVDAT   2   24-FEB-09 1RC1    1       VERSN                                    
REVDAT   1   14-JUN-05 1RC1    0                                                
JRNL        AUTH   Y.ZHANG,J.DESHARNAIS,D.L.BOGER,I.A.WILSON                    
JRNL        TITL   HUMAN GAR TFASE COMPLEX STRUCTURE                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 39369                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1974                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2369                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 131                          
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3014                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
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): 0.197         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.639         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3148 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4280 ; 1.370 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   398 ; 6.292 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   524 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2294 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1314 ; 0.201 ; 0.200       
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):   179 ; 0.125 ; 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):    41 ; 0.187 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.118 ; 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):  1992 ; 0.515 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3216 ; 0.996 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1156 ; 1.800 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1064 ; 3.123 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   200                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.6602  54.4514   6.9022              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0096 T22:   0.0846                                     
REMARK   3      T33:   0.0738 T12:   0.0248                                     
REMARK   3      T13:   0.0042 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2032 L22:   3.5066                                     
REMARK   3      L33:   1.7378 L12:   0.5664                                     
REMARK   3      L13:   0.3540 L23:   0.0488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0180 S12:   0.1830 S13:  -0.2855                       
REMARK   3      S21:  -0.0198 S22:   0.0549 S23:  -0.2456                       
REMARK   3      S31:   0.1759 S32:   0.0564 S33:  -0.0369                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   200                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0504  58.4321  40.1008              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1547 T22:   0.1596                                     
REMARK   3      T33:   0.1005 T12:  -0.0113                                     
REMARK   3      T13:  -0.0262 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5934 L22:   2.3225                                     
REMARK   3      L33:   1.3120 L12:   1.7644                                     
REMARK   3      L13:  -0.4234 L23:  -0.4520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1471 S12:  -0.3030 S13:   0.1304                       
REMARK   3      S21:   0.2716 S22:  -0.0947 S23:   0.3471                       
REMARK   3      S31:  -0.0437 S32:  -0.3583 S33:  -0.0524                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1RC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020642.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.                                 
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9840                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 9                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41237                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.080                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.67000                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: 1NJS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, CALCIUM CLORIDE, IMIDAZOLE MALATE   
REMARK 280  BUFFER, PH 6., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-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       31.22667            
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       62.45333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.45333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       31.22667            
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 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     LYS A   201                                                      
REMARK 465     GLU A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     GLU B   202                                                      
REMARK 465     GLU B   203                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
REMARK 465     HIS B   209                                                      
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    ASP B  81   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 142   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 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    ASN A  25       46.54   -102.34                                   
REMARK 500    PRO A 109       46.81    -81.33                                   
REMARK 500    ASN A 119       52.54   -112.88                                   
REMARK 500    THR A 132     -154.74   -128.34                                   
REMARK 500    ASN B  13      -14.31     86.29                                   
REMARK 500    PRO B 109       48.71    -82.63                                   
REMARK 500    THR B 132     -150.10   -127.42                                   
REMARK 500    ASN B 194       -9.99    -58.37                                   
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 GLY A  187     THR A  188                 -138.41                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     KT3 A  510                                                       
REMARK 610     KT3 B  610                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KT3 A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KT3 B 610                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NJS   RELATED DB: PDB                                   
REMARK 900 HUMAN GAR TFASE COMPLEX STRUCTURE WITH 10-(TRIFLUOROACETYL)-5,10-    
REMARK 900 DIDEAZAACYCLIC-5,6,7,8-TETRAHYDROFOLIC ACID AT PHYSIOLOGICAL PH      
REMARK 900 RELATED ID: 1MEJ   RELATED DB: PDB                                   
REMARK 900 APO HUMAN GAR TFASE STRUCTURE AT PH 8.5                              
REMARK 900 RELATED ID: 1MEO   RELATED DB: PDB                                   
REMARK 900 APO HUMAN GAR TFASE STRUCTURE AT PH 4.2                              
REMARK 900 RELATED ID: 1RBM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RBQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RBY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RBZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RC0   RELATED DB: PDB                                   
DBREF  1RC1 A    1   203  UNP    P22102   PUR2_HUMAN     808   1010             
DBREF  1RC1 B    1   203  UNP    P22102   PUR2_HUMAN     808   1010             
SEQADV 1RC1 HIS A  204  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS A  205  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS A  206  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS A  207  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS A  208  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS A  209  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS B  204  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS B  205  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS B  206  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS B  207  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS B  208  UNP  P22102              EXPRESSION TAG                 
SEQADV 1RC1 HIS B  209  UNP  P22102              EXPRESSION TAG                 
SEQRES   1 A  209  ALA ARG VAL ALA VAL LEU ILE SER GLY THR GLY SER ASN          
SEQRES   2 A  209  LEU GLN ALA LEU ILE ASP SER THR ARG GLU PRO ASN SER          
SEQRES   3 A  209  SER ALA GLN ILE ASP ILE VAL ILE SER ASN LYS ALA ALA          
SEQRES   4 A  209  VAL ALA GLY LEU ASP LYS ALA GLU ARG ALA GLY ILE PRO          
SEQRES   5 A  209  THR ARG VAL ILE ASN HIS LYS LEU TYR LYS ASN ARG VAL          
SEQRES   6 A  209  GLU PHE ASP SER ALA ILE ASP LEU VAL LEU GLU GLU PHE          
SEQRES   7 A  209  SER ILE ASP ILE VAL CYS LEU ALA GLY PHE MET ARG ILE          
SEQRES   8 A  209  LEU SER GLY PRO PHE VAL GLN LYS TRP ASN GLY LYS MET          
SEQRES   9 A  209  LEU ASN ILE HIS PRO SER LEU LEU PRO SER PHE LYS GLY          
SEQRES  10 A  209  SER ASN ALA HIS GLU GLN ALA LEU GLU THR GLY VAL THR          
SEQRES  11 A  209  VAL THR GLY CYS THR VAL HIS PHE VAL ALA GLU ASP VAL          
SEQRES  12 A  209  ASP ALA GLY GLN ILE ILE LEU GLN GLU ALA VAL PRO VAL          
SEQRES  13 A  209  LYS ARG GLY ASP THR VAL ALA THR LEU SER GLU ARG VAL          
SEQRES  14 A  209  LYS LEU ALA GLU HIS LYS ILE PHE PRO ALA ALA LEU GLN          
SEQRES  15 A  209  LEU VAL ALA SER GLY THR VAL GLN LEU GLY GLU ASN GLY          
SEQRES  16 A  209  LYS ILE CYS TRP VAL LYS GLU GLU HIS HIS HIS HIS HIS          
SEQRES  17 A  209  HIS                                                          
SEQRES   1 B  209  ALA ARG VAL ALA VAL LEU ILE SER GLY THR GLY SER ASN          
SEQRES   2 B  209  LEU GLN ALA LEU ILE ASP SER THR ARG GLU PRO ASN SER          
SEQRES   3 B  209  SER ALA GLN ILE ASP ILE VAL ILE SER ASN LYS ALA ALA          
SEQRES   4 B  209  VAL ALA GLY LEU ASP LYS ALA GLU ARG ALA GLY ILE PRO          
SEQRES   5 B  209  THR ARG VAL ILE ASN HIS LYS LEU TYR LYS ASN ARG VAL          
SEQRES   6 B  209  GLU PHE ASP SER ALA ILE ASP LEU VAL LEU GLU GLU PHE          
SEQRES   7 B  209  SER ILE ASP ILE VAL CYS LEU ALA GLY PHE MET ARG ILE          
SEQRES   8 B  209  LEU SER GLY PRO PHE VAL GLN LYS TRP ASN GLY LYS MET          
SEQRES   9 B  209  LEU ASN ILE HIS PRO SER LEU LEU PRO SER PHE LYS GLY          
SEQRES  10 B  209  SER ASN ALA HIS GLU GLN ALA LEU GLU THR GLY VAL THR          
SEQRES  11 B  209  VAL THR GLY CYS THR VAL HIS PHE VAL ALA GLU ASP VAL          
SEQRES  12 B  209  ASP ALA GLY GLN ILE ILE LEU GLN GLU ALA VAL PRO VAL          
SEQRES  13 B  209  LYS ARG GLY ASP THR VAL ALA THR LEU SER GLU ARG VAL          
SEQRES  14 B  209  LYS LEU ALA GLU HIS LYS ILE PHE PRO ALA ALA LEU GLN          
SEQRES  15 B  209  LEU VAL ALA SER GLY THR VAL GLN LEU GLY GLU ASN GLY          
SEQRES  16 B  209  LYS ILE CYS TRP VAL LYS GLU GLU HIS HIS HIS HIS HIS          
SEQRES  17 B  209  HIS                                                          
HET    PO4  A 521       5                                                       
HET    KT3  A 510      38                                                       
HET    PO4  B 621       5                                                       
HET    KT3  B 610      38                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     KT3 N-{4-4-(2,4-DIAMINO-6-OXO-1,6-DIHYDRO-PYRIMIDIN-5-YL)-           
HETNAM   2 KT3  1-(2,2,2-TRIFLUORO-1,1-DIHYDROXY-ETHYL)-BUT-2-YL-               
HETNAM   3 KT3  BENZOYL}-GAMMA-GLUTAMYL-GAMMA-GLUTAMYL-GLUTAMIC ACID            
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   4  KT3    2(C32 H40 F3 N7 O14)                                         
FORMUL   7  HOH   *130(H2 O)                                                    
HELIX    1   1 GLY A   11  ARG A   22  1                                  12    
HELIX    2   2 VAL A   40  ALA A   49  1                                  10    
HELIX    3   3 ASN A   57  TYR A   61  5                                   5    
HELIX    4   4 ASN A   63  PHE A   78  1                                  16    
HELIX    5   5 SER A   93  TRP A  100  1                                   8    
HELIX    6   6 ASN A  119  GLY A  128  1                                  10    
HELIX    7   7 THR A  161  SER A  186  1                                  26    
HELIX    8   8 ASN B   13  ARG B   22  1                                  10    
HELIX    9   9 VAL B   40  ALA B   49  1                                  10    
HELIX   10  10 ASN B   57  TYR B   61  5                                   5    
HELIX   11  11 ASN B   63  PHE B   78  1                                  16    
HELIX   12  12 SER B   93  TRP B  100  1                                   8    
HELIX   13  13 ASN B  119  GLY B  128  1                                  10    
HELIX   14  14 THR B  161  SER B  186  1                                  26    
SHEET    1   A 7 THR A  53  VAL A  55  0                                        
SHEET    2   A 7 GLN A  29  SER A  35  1  N  SER A  35   O  ARG A  54           
SHEET    3   A 7 ARG A   2  ILE A   7  1  N  VAL A   3   O  GLN A  29           
SHEET    4   A 7 ILE A  82  LEU A  85  1  O  CYS A  84   N  ALA A   4           
SHEET    5   A 7 MET A 104  HIS A 108  1  O  LEU A 105   N  LEU A  85           
SHEET    6   A 7 VAL A 131  PHE A 138 -1  O  THR A 135   N  HIS A 108           
SHEET    7   A 7 ILE A 148  PRO A 155 -1  O  VAL A 154   N  THR A 132           
SHEET    1   B 2 VAL A 189  LEU A 191  0                                        
SHEET    2   B 2 ILE A 197  TRP A 199 -1  O  CYS A 198   N  GLN A 190           
SHEET    1   C 7 THR B  53  VAL B  55  0                                        
SHEET    2   C 7 GLN B  29  SER B  35  1  N  SER B  35   O  ARG B  54           
SHEET    3   C 7 ARG B   2  ILE B   7  1  N  ILE B   7   O  ILE B  34           
SHEET    4   C 7 ILE B  82  LEU B  85  1  O  CYS B  84   N  LEU B   6           
SHEET    5   C 7 MET B 104  HIS B 108  1  O  LEU B 105   N  VAL B  83           
SHEET    6   C 7 VAL B 131  PHE B 138 -1  O  THR B 135   N  HIS B 108           
SHEET    7   C 7 ILE B 148  PRO B 155 -1  O  VAL B 154   N  THR B 132           
SHEET    1   D 2 VAL B 189  LEU B 191  0                                        
SHEET    2   D 2 ILE B 197  TRP B 199 -1  O  CYS B 198   N  GLN B 190           
CISPEP   1 LEU A  112    PRO A  113          0         5.87                     
CISPEP   2 LEU B  112    PRO B  113          0         7.29                     
SITE     1 AC1  8 THR A  10  GLY A  11  SER A  12  ASN A  13                    
SITE     2 AC1  8 LYS A 170  HOH A 524  HOH A 531  HOH A 532                    
SITE     1 AC2  8 GLY B  11  SER B  12  ASN B  13  LEU B  14                    
SITE     2 AC2  8 GLN B  15  ALA B  16  LYS B  45  HIS B 174                    
SITE     1 AC3 20 ARG A  64  MET A  89  ARG A  90  ILE A  91                    
SITE     2 AC3 20 LEU A  92  VAL A  97  ASN A 106  HIS A 108                    
SITE     3 AC3 20 PRO A 109  GLY A 117  SER A 118  VAL A 139                    
SITE     4 AC3 20 ALA A 140  GLU A 141  VAL A 143  ASP A 144                    
SITE     5 AC3 20 HOH A 525  HOH A 559  HOH A 569  HOH A 594                    
SITE     1 AC4 16 ARG B  64  LEU B  85  MET B  89  ARG B  90                    
SITE     2 AC4 16 ILE B  91  LEU B  92  ASN B 106  HIS B 108                    
SITE     3 AC4 16 PRO B 109  GLY B 117  VAL B 139  ALA B 140                    
SITE     4 AC4 16 GLU B 141  VAL B 143  ASP B 144  HOH B 636                    
CRYST1  126.664  126.664   93.680  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007895  0.004558  0.000000        0.00000                         
SCALE2      0.000000  0.009116  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010675        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system