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Database: PDB
Entry: 5OFM
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Original site: 5OFM 
HEADER    OXIDOREDUCTASE                          11-JUL-17   5OFM              
TITLE     CRYSTAL STRUCTURE OF HUMAN 3-PHOSPHOGLYCERATE DEHYDROGENASE IN COMPLEX
TITLE    2 WITH 5-AMINO-1-METHYL-1H-INDOLE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 SYNONYM: 3-PGDH,2-OXOGLUTARATE REDUCTASE,MALATE DEHYDROGENASE;       
COMPND   5 EC: 1.1.1.95,1.1.1.399,1.1.1.37;                                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PHGDH, PGDH3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DEHYDROGENASE, SERINE METABOLISM, FBDD, OXIDOREDUCTASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.UNTERLASS,A.BASLE,T.J.BLACKBURN,J.TUCKER,C.CANO,M.E.M.NOBLE,      
AUTHOR   2 N.J.CURTIN                                                           
REVDAT   2   18-APR-18 5OFM    1       JRNL                                     
REVDAT   1   16-AUG-17 5OFM    0                                                
JRNL        AUTH   J.E.UNTERLASS,N.J.CURTIN                                     
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN 3-PHOSPHOGLYCERATE DEHYDROGENASE  
JRNL        TITL 2 IN COMPLEX WITH 5-AMINO-1-METHYL-1H-INDOLE                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.E.UNTERLASS,A.BASLE,T.J.BLACKBURN,J.TUCKER,C.CANO,         
REMARK   1  AUTH 2 M.E.M.NOBLE,N.J.CURTIN                                       
REMARK   1  TITL   VALIDATING AND ENABLING PHOSPHOGLYCERATE DEHYDROGENASE       
REMARK   1  TITL 2 (PHGDH) AS A TARGET FOR FRAGMENT-BASED DRUG DISCOVERY IN     
REMARK   1  TITL 3 PHGDH-AMPLIFIED BREAST CANCER.                               
REMARK   1  REF    ONCOTARGET                    V.   9 13139 2018              
REMARK   1  REFN                   ESSN 1949-2553                               
REMARK   1  PMID   29568346                                                     
REMARK   1  DOI    10.18632/ONCOTARGET.11487                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 48623                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2653                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2780                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 157                          
REMARK   3   BIN FREE R VALUE                    : 0.4190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2920                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 305                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.27000                                              
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : 0.87000                                              
REMARK   3    B12 (A**2) : 0.19000                                              
REMARK   3    B13 (A**2) : -0.70000                                             
REMARK   3    B23 (A**2) : -0.18000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.134         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.106         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.139         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3177 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3101 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4312 ; 2.155 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7161 ; 1.157 ; 2.993       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   425 ; 7.035 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;36.676 ;24.173       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   573 ;17.043 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;20.688 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   481 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3704 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   701 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1652 ; 2.874 ; 1.381       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1651 ; 2.462 ; 1.378       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2093 ; 3.259 ; 2.065       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2094 ; 3.259 ; 2.068       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1525 ; 3.274 ; 1.660       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1526 ; 3.274 ; 1.660       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2220 ; 3.718 ; 2.391       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3839 ; 4.591 ;12.318       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3840 ; 4.591 ;12.320       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6278 ; 3.158 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    97 ;32.417 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6420 ;12.662 ; 5.000       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5OFM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004963.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.917                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2 0.3.8.0                       
REMARK 200  DATA SCALING SOFTWARE          : XIA2 0.3.8.0                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51430                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.660                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37600                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PCTP, PH 7, 23-25 % PEG 1500,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: 4890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     MET B    93                                                      
REMARK 465     LEU B    94                                                      
REMARK 465     VAL B    95                                                      
REMARK 465     MET B    96                                                      
REMARK 465     ASN B    97                                                      
REMARK 465     THR B    98                                                      
REMARK 465     PRO B    99                                                      
REMARK 465     CYS B   295                                                      
REMARK 465     GLY B   296                                                      
REMARK 465     GLU B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     ILE B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     VAL B   301                                                      
REMARK 465     GLN B   302                                                      
REMARK 465     PHE B   303                                                      
REMARK 465     VAL B   304                                                      
REMARK 465     ASP B   305                                                      
REMARK 465     MET B   306                                                      
REMARK 465     VAL B   307                                                      
REMARK 465     LYS B   308                                                      
REMARK 465     GLY B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     SER B   311                                                      
REMARK 465     LEU B   312                                                      
REMARK 465     THR B   313                                                      
REMARK 465     GLY B   314                                                      
REMARK 465     VAL B   315                                                      
REMARK 465     MET A    93                                                      
REMARK 465     LEU A    94                                                      
REMARK 465     VAL A    95                                                      
REMARK 465     MET A    96                                                      
REMARK 465     ASN A    97                                                      
REMARK 465     THR A    98                                                      
REMARK 465     PRO A    99                                                      
REMARK 465     CYS A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     GLU A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     ILE A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     VAL A   301                                                      
REMARK 465     GLN A   302                                                      
REMARK 465     PHE A   303                                                      
REMARK 465     VAL A   304                                                      
REMARK 465     ASP A   305                                                      
REMARK 465     MET A   306                                                      
REMARK 465     VAL A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     GLY A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     THR A   313                                                      
REMARK 465     GLY A   314                                                      
REMARK 465     VAL A   315                                                      
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    LEU B   284     NH2  ARG A   119              2.00            
REMARK 500   NH2  ARG B   119     O    LEU A   284              2.09            
REMARK 500   O    HIS B   283     NH1  ARG A   135              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   195     NH2  ARG A   268     1455     2.17            
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    ARG B 119   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG B 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG B 135   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 158   CG  -  CD  -  NE  ANGL. DEV. = -14.8 DEGREES          
REMARK 500    ARG B 158   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG B 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A 158   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ASP A 201   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A 247   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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    GLU B 134       78.92   -111.28                                   
REMARK 500    ALA B 235      -81.07   -115.39                                   
REMARK 500    GLU A 134       79.58   -108.94                                   
REMARK 500    ALA A 235      -78.30   -104.34                                   
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 9TT B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9TT A 401                 
DBREF  5OFM B   94   315  UNP    O43175   SERA_HUMAN      94    315             
DBREF  5OFM A   94   315  UNP    O43175   SERA_HUMAN      94    315             
SEQADV 5OFM MET B   93  UNP  O43175              INITIATING METHIONINE          
SEQADV 5OFM MET A   93  UNP  O43175              INITIATING METHIONINE          
SEQRES   1 B  223  MET LEU VAL MET ASN THR PRO ASN GLY ASN SER LEU SER          
SEQRES   2 B  223  ALA ALA GLU LEU THR CYS GLY MET ILE MET CYS LEU ALA          
SEQRES   3 B  223  ARG GLN ILE PRO GLN ALA THR ALA SER MET LYS ASP GLY          
SEQRES   4 B  223  LYS TRP GLU ARG LYS LYS PHE MET GLY THR GLU LEU ASN          
SEQRES   5 B  223  GLY LYS THR LEU GLY ILE LEU GLY LEU GLY ARG ILE GLY          
SEQRES   6 B  223  ARG GLU VAL ALA THR ARG MET GLN SER PHE GLY MET LYS          
SEQRES   7 B  223  THR ILE GLY TYR ASP PRO ILE ILE SER PRO GLU VAL SER          
SEQRES   8 B  223  ALA SER PHE GLY VAL GLN GLN LEU PRO LEU GLU GLU ILE          
SEQRES   9 B  223  TRP PRO LEU CYS ASP PHE ILE THR VAL HIS THR PRO LEU          
SEQRES  10 B  223  LEU PRO SER THR THR GLY LEU LEU ASN ASP ASN THR PHE          
SEQRES  11 B  223  ALA GLN CYS LYS LYS GLY VAL ARG VAL VAL ASN CYS ALA          
SEQRES  12 B  223  ARG GLY GLY ILE VAL ASP GLU GLY ALA LEU LEU ARG ALA          
SEQRES  13 B  223  LEU GLN SER GLY GLN CYS ALA GLY ALA ALA LEU ASP VAL          
SEQRES  14 B  223  PHE THR GLU GLU PRO PRO ARG ASP ARG ALA LEU VAL ASP          
SEQRES  15 B  223  HIS GLU ASN VAL ILE SER CYS PRO HIS LEU GLY ALA SER          
SEQRES  16 B  223  THR LYS GLU ALA GLN SER ARG CYS GLY GLU GLU ILE ALA          
SEQRES  17 B  223  VAL GLN PHE VAL ASP MET VAL LYS GLY LYS SER LEU THR          
SEQRES  18 B  223  GLY VAL                                                      
SEQRES   1 A  223  MET LEU VAL MET ASN THR PRO ASN GLY ASN SER LEU SER          
SEQRES   2 A  223  ALA ALA GLU LEU THR CYS GLY MET ILE MET CYS LEU ALA          
SEQRES   3 A  223  ARG GLN ILE PRO GLN ALA THR ALA SER MET LYS ASP GLY          
SEQRES   4 A  223  LYS TRP GLU ARG LYS LYS PHE MET GLY THR GLU LEU ASN          
SEQRES   5 A  223  GLY LYS THR LEU GLY ILE LEU GLY LEU GLY ARG ILE GLY          
SEQRES   6 A  223  ARG GLU VAL ALA THR ARG MET GLN SER PHE GLY MET LYS          
SEQRES   7 A  223  THR ILE GLY TYR ASP PRO ILE ILE SER PRO GLU VAL SER          
SEQRES   8 A  223  ALA SER PHE GLY VAL GLN GLN LEU PRO LEU GLU GLU ILE          
SEQRES   9 A  223  TRP PRO LEU CYS ASP PHE ILE THR VAL HIS THR PRO LEU          
SEQRES  10 A  223  LEU PRO SER THR THR GLY LEU LEU ASN ASP ASN THR PHE          
SEQRES  11 A  223  ALA GLN CYS LYS LYS GLY VAL ARG VAL VAL ASN CYS ALA          
SEQRES  12 A  223  ARG GLY GLY ILE VAL ASP GLU GLY ALA LEU LEU ARG ALA          
SEQRES  13 A  223  LEU GLN SER GLY GLN CYS ALA GLY ALA ALA LEU ASP VAL          
SEQRES  14 A  223  PHE THR GLU GLU PRO PRO ARG ASP ARG ALA LEU VAL ASP          
SEQRES  15 A  223  HIS GLU ASN VAL ILE SER CYS PRO HIS LEU GLY ALA SER          
SEQRES  16 A  223  THR LYS GLU ALA GLN SER ARG CYS GLY GLU GLU ILE ALA          
SEQRES  17 A  223  VAL GLN PHE VAL ASP MET VAL LYS GLY LYS SER LEU THR          
SEQRES  18 A  223  GLY VAL                                                      
HET    9TT  B 401      11                                                       
HET    9TT  A 401      11                                                       
HETNAM     9TT 1-METHYLINDOL-5-AMINE                                            
FORMUL   3  9TT    2(C9 H10 N2)                                                 
FORMUL   5  HOH   *305(H2 O)                                                    
HELIX    1 AA1 ASN B  102  GLN B  120  1                                  19    
HELIX    2 AA2 GLN B  120  ASP B  130  1                                  11    
HELIX    3 AA3 GLY B  154  PHE B  167  1                                  14    
HELIX    4 AA4 SER B  179  PHE B  186  1                                   8    
HELIX    5 AA5 PRO B  192  TRP B  197  1                                   6    
HELIX    6 AA6 PRO B  198  CYS B  200  5                                   3    
HELIX    7 AA7 ASN B  218  ALA B  223  1                                   6    
HELIX    8 AA8 ASP B  241  GLY B  252  1                                  12    
HELIX    9 AA9 ARG B  270  HIS B  275  1                                   6    
HELIX   10 AB1 THR B  288  SER B  293  1                                   6    
HELIX   11 AB2 ASN A  102  GLN A  120  1                                  19    
HELIX   12 AB3 GLN A  120  ASP A  130  1                                  11    
HELIX   13 AB4 ARG A  135  MET A  139  5                                   5    
HELIX   14 AB5 GLY A  154  SER A  166  1                                  13    
HELIX   15 AB6 SER A  179  PHE A  186  1                                   8    
HELIX   16 AB7 PRO A  192  TRP A  197  1                                   6    
HELIX   17 AB8 PRO A  198  CYS A  200  5                                   3    
HELIX   18 AB9 ASN A  218  CYS A  225  1                                   8    
HELIX   19 AC1 ASP A  241  GLY A  252  1                                  12    
HELIX   20 AC2 THR A  288  SER A  293  1                                   6    
SHEET    1 AA1 7 GLN B 189  GLN B 190  0                                        
SHEET    2 AA1 7 LYS B 170  TYR B 174  1  N  GLY B 173   O  GLN B 189           
SHEET    3 AA1 7 THR B 147  LEU B 151  1  N  LEU B 148   O  LYS B 170           
SHEET    4 AA1 7 PHE B 202  VAL B 205  1  O  PHE B 202   N  GLY B 149           
SHEET    5 AA1 7 VAL B 229  ASN B 233  1  O  ARG B 230   N  ILE B 203           
SHEET    6 AA1 7 CYS B 254  LEU B 259  1  O  ALA B 258   N  ASN B 233           
SHEET    7 AA1 7 VAL B 278  SER B 280  1  O  ILE B 279   N  ALA B 257           
SHEET    1 AA2 7 GLN A 189  GLN A 190  0                                        
SHEET    2 AA2 7 LYS A 170  TYR A 174  1  N  THR A 171   O  GLN A 189           
SHEET    3 AA2 7 THR A 147  LEU A 151  1  N  LEU A 148   O  LYS A 170           
SHEET    4 AA2 7 PHE A 202  VAL A 205  1  O  PHE A 202   N  GLY A 149           
SHEET    5 AA2 7 VAL A 229  ASN A 233  1  O  VAL A 232   N  ILE A 203           
SHEET    6 AA2 7 CYS A 254  LEU A 259  1  O  ALA A 258   N  ASN A 233           
SHEET    7 AA2 7 VAL A 278  SER A 280  1  O  ILE A 279   N  ALA A 257           
CISPEP   1 GLU B  265    PRO B  266          0       -14.49                     
CISPEP   2 GLU A  265    PRO A  266          0        -6.50                     
SITE     1 AC1  5 TYR B 174  PRO B 176  THR B 207  SER B 212                    
SITE     2 AC1  5 THR B 213                                                     
SITE     1 AC2  7 TYR A 174  PRO A 176  THR A 207  PRO A 208                    
SITE     2 AC2  7 SER A 212  THR A 213  HOH A 573                               
CRYST1   43.342   45.860   56.175  97.91 110.74 106.39 P 1           2          
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      0.023072  0.006788  0.010923        0.00000                         
SCALE2      0.000000  0.022730  0.006241        0.00000                         
SCALE3      0.000000  0.000000  0.019739        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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