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Database: PDB
Entry: 5NZQ
LinkDB: 5NZQ
Original site: 5NZQ 
HEADER    OXIDOREDUCTASE                          14-MAY-17   5NZQ              
TITLE     CRYSTAL STRUCTURE OF HUMAN 3-PHOSPHOGLYCERATE DEHYDROGENASE IN COMPLEX
TITLE    2 WITH 3-(1,3-OXAZOL-5-YL)ANILINE.                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 94-315;                                       
COMPND   5 SYNONYM: 3-PGDH,2-OXOGLUTARATE REDUCTASE,MALATE DEHYDROGENASE;       
COMPND   6 EC: 1.1.1.95,1.1.1.399,1.1.1.37;                                     
COMPND   7 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   3   04-APR-18 5NZQ    1       JRNL                                     
REVDAT   2   30-AUG-17 5NZQ    1       REMARK                                   
REVDAT   1   14-JUN-17 5NZQ    0                                                
JRNL        AUTH   J.E.UNTERLASS,A.BASLE,T.J.BLACKBURN,J.TUCKER,C.CANO,         
JRNL        AUTH 2 M.E.M.NOBLE,N.J.CURTIN                                       
JRNL        TITL   VALIDATING AND ENABLING PHOSPHOGLYCERATE DEHYDROGENASE       
JRNL        TITL 2 (PHGDH) AS A TARGET FOR FRAGMENT-BASED DRUG DISCOVERY IN     
JRNL        TITL 3 PHGDH-AMPLIFIED BREAST CANCER.                               
JRNL        REF    ONCOTARGET                    V.   9 13139 2018              
JRNL        REFN                   ESSN 1949-2553                               
JRNL        PMID   29568346                                                     
JRNL        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) : 50.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 48604                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.293                           
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) : 2811                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 65.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 149                          
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
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          : 24                                      
REMARK   3   SOLVENT ATOMS            : 264                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.79000                                             
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : -0.47000                                             
REMARK   3    B12 (A**2) : 1.10000                                              
REMARK   3    B13 (A**2) : 0.37000                                              
REMARK   3    B23 (A**2) : 1.34000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.157         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.618         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3155 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3071 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4278 ; 2.051 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7095 ; 1.393 ; 2.995       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   421 ; 6.955 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   125 ;38.528 ;24.400       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   567 ;16.689 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;20.254 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   479 ; 0.131 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3668 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   691 ; 0.005 ; 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):  1642 ; 4.547 ; 2.057       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1641 ; 4.472 ; 2.054       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2077 ; 5.331 ; 3.099       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2078 ; 5.347 ; 3.101       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1513 ; 4.945 ; 2.319       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1514 ; 4.945 ; 2.320       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2202 ; 5.694 ; 3.387       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3715 ; 7.085 ;17.986       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3716 ; 7.084 ;17.990       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6226 ; 3.572 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    76 ;45.870 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6350 ;20.110 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     B   100    294       A   100    294   23496  0.06  0.05     
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 5NZQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004505.                                   
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                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51377                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY                : 2.150                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
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     (%) : 86.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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   (%): 39.16                                     
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 293K                     
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: 4960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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                                             
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   OD1  ASN A   220     O    HOH B   623     1444     1.45            
REMARK 500   O    THR B   214     OD1  ASN A   220     1666     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 236   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG B 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 236   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B 235      -80.41   -105.55                                   
REMARK 500    ALA A 235      -77.70   -105.97                                   
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 5AO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5AO A 401                 
DBREF  5NZQ B   94   315  UNP    O43175   SERA_HUMAN      94    315             
DBREF  5NZQ A   94   315  UNP    O43175   SERA_HUMAN      94    315             
SEQADV 5NZQ MET B   93  UNP  O43175              INITIATING METHIONINE          
SEQADV 5NZQ 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    5AO  B 401      12                                                       
HET    5AO  A 401      12                                                       
HETNAM     5AO 3-(1,3-OXAZOL-5-YL)ANILINE                                       
FORMUL   3  5AO    2(C9 H8 N2 O)                                                
FORMUL   5  HOH   *264(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  SER B  166  1                                  13    
HELIX    4 AA4 SER B  179  SER B  185  1                                   7    
HELIX    5 AA5 PRO B  192  CYS B  200  1                                   9    
HELIX    6 AA6 ASN B  218  CYS B  225  1                                   8    
HELIX    7 AA7 ASP B  241  GLY B  252  1                                  12    
HELIX    8 AA8 ARG B  270  HIS B  275  1                                   6    
HELIX    9 AA9 THR B  288  SER B  293  1                                   6    
HELIX   10 AB1 ASN A  102  GLN A  120  1                                  19    
HELIX   11 AB2 GLN A  120  ASP A  130  1                                  11    
HELIX   12 AB3 GLY A  154  SER A  166  1                                  13    
HELIX   13 AB4 SER A  179  SER A  185  1                                   7    
HELIX   14 AB5 PRO A  192  TRP A  197  1                                   6    
HELIX   15 AB6 PRO A  198  CYS A  200  5                                   3    
HELIX   16 AB7 ASN A  218  ALA A  223  1                                   6    
HELIX   17 AB8 ASP A  241  GLY A  252  1                                  12    
HELIX   18 AB9 ARG A  270  HIS A  275  1                                   6    
HELIX   19 AC1 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  THR B 204   N  GLY B 149           
SHEET    5 AA1 7 VAL B 229  ASN B 233  1  O  VAL B 232   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  LEU B 259           
SHEET    1 AA2 7 GLN A 189  GLN A 190  0                                        
SHEET    2 AA2 7 LYS A 170  TYR A 174  1  N  GLY A 173   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  THR A 204   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  LEU A 259           
CISPEP   1 GLU B  265    PRO B  266          0        -6.98                     
CISPEP   2 GLU A  265    PRO A  266          0        -5.75                     
SITE     1 AC1  6 TYR B 174  ASP B 175  PRO B 176  THR B 207                    
SITE     2 AC1  6 PRO B 208  LEU B 216                                          
SITE     1 AC2  5 TYR A 174  PRO A 176  THR A 207  PRO A 208                    
SITE     2 AC2  5 THR A 213                                                     
CRYST1   43.335   45.914   56.203  97.85 111.05 106.04 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      0.023076  0.006633  0.011013        0.00000                         
SCALE2      0.000000  0.022662  0.006175        0.00000                         
SCALE3      0.000000  0.000000  0.019760        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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