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Database: PDB
Entry: 5N53
LinkDB: 5N53
Original site: 5N53 
HEADER    OXIDOREDUCTASE                          12-FEB-17   5N53              
TITLE     CRYSTAL STRUCTURE OF HUMAN 3-PHOSPHOGLYCERATE DEHYDROGENASE IN COMPLEX
TITLE    2 WITH N-(3-CHLORO-4-METHOXYPHENYL) ACETAMIDE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-3-PHOSPHOGLYCERATE DEHYDROGENASE;                        
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 SYNONYM: 3-PGDH;                                                     
COMPND   5 EC: 1.1.1.95;                                                        
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;                                        
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA (DE3)                             
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   04-APR-18 5N53    1       JRNL                                     
REVDAT   1   05-APR-17 5N53    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.    1.48 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) : 1.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.12                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 48587                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2651                            
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) : 1.48                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2891                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 68.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 160                          
REMARK   3   BIN FREE R VALUE                    : 0.3460                       
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          : 26                                      
REMARK   3   SOLVENT ATOMS            : 238                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.68                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.04000                                             
REMARK   3    B22 (A**2) : -0.58000                                             
REMARK   3    B33 (A**2) : -0.46000                                             
REMARK   3    B12 (A**2) : -0.47000                                             
REMARK   3    B13 (A**2) : 0.68000                                              
REMARK   3    B23 (A**2) : 1.25000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.093         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.830         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3171 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3093 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4304 ; 1.978 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7147 ; 1.412 ; 2.992       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   425 ; 6.947 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   125 ;39.191 ;24.400       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   569 ;17.769 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;20.453 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   483 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3688 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   687 ; 0.006 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6264 ; 4.372 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    67 ;36.748 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  6371 ;21.853 ; 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   23386 0.070 0.050     
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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5N53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003230.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-OCT-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) : 0.9200                             
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   : 51238                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.1                               
REMARK 200  DATA REDUNDANCY                : 2.130                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
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     (%) : 85.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.14                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.08800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
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: 2G76                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
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: 4940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 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   ND2  ASN A   220     O    HOH B   518     1444     1.08            
REMARK 500   OD1  ASN A   220     O    HOH B   520     1444     1.26            
REMARK 500   CG   ASN A   220     O    HOH B   518     1444     1.62            
REMARK 500   OD1  ASN A   220     O    HOH B   518     1444     1.95            
REMARK 500   OE1  GLU B   194     OH   TYR A   174     1666     2.03            
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. =   5.4 DEGREES          
REMARK 500    ARG B 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 236   CG  -  CD  -  NE  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    ARG A 236   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A 236   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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       72.15   -117.80                                   
REMARK 500    HIS B 206       52.60   -145.35                                   
REMARK 500    ALA B 235      -75.14   -108.33                                   
REMARK 500    GLU A 134       73.61   -119.13                                   
REMARK 500    HIS A 206       53.78   -141.18                                   
REMARK 500    ALA A 235      -70.95   -105.58                                   
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 8NB B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NB A 301                 
DBREF  5N53 B  100   294  UNP    O43175   SERA_HUMAN     100    294             
DBREF  5N53 A  100   294  UNP    O43175   SERA_HUMAN     100    294             
SEQRES   1 B  195  ASN GLY ASN SER LEU SER ALA ALA GLU LEU THR CYS GLY          
SEQRES   2 B  195  MET ILE MET CYS LEU ALA ARG GLN ILE PRO GLN ALA THR          
SEQRES   3 B  195  ALA SER MET LYS ASP GLY LYS TRP GLU ARG LYS LYS PHE          
SEQRES   4 B  195  MET GLY THR GLU LEU ASN GLY LYS THR LEU GLY ILE LEU          
SEQRES   5 B  195  GLY LEU GLY ARG ILE GLY ARG GLU VAL ALA THR ARG MET          
SEQRES   6 B  195  GLN SER PHE GLY MET LYS THR ILE GLY TYR ASP PRO ILE          
SEQRES   7 B  195  ILE SER PRO GLU VAL SER ALA SER PHE GLY VAL GLN GLN          
SEQRES   8 B  195  LEU PRO LEU GLU GLU ILE TRP PRO LEU CYS ASP PHE ILE          
SEQRES   9 B  195  THR VAL HIS THR PRO LEU LEU PRO SER THR THR GLY LEU          
SEQRES  10 B  195  LEU ASN ASP ASN THR PHE ALA GLN CYS LYS LYS GLY VAL          
SEQRES  11 B  195  ARG VAL VAL ASN CYS ALA ARG GLY GLY ILE VAL ASP GLU          
SEQRES  12 B  195  GLY ALA LEU LEU ARG ALA LEU GLN SER GLY GLN CYS ALA          
SEQRES  13 B  195  GLY ALA ALA LEU ASP VAL PHE THR GLU GLU PRO PRO ARG          
SEQRES  14 B  195  ASP ARG ALA LEU VAL ASP HIS GLU ASN VAL ILE SER CYS          
SEQRES  15 B  195  PRO HIS LEU GLY ALA SER THR LYS GLU ALA GLN SER ARG          
SEQRES   1 A  195  ASN GLY ASN SER LEU SER ALA ALA GLU LEU THR CYS GLY          
SEQRES   2 A  195  MET ILE MET CYS LEU ALA ARG GLN ILE PRO GLN ALA THR          
SEQRES   3 A  195  ALA SER MET LYS ASP GLY LYS TRP GLU ARG LYS LYS PHE          
SEQRES   4 A  195  MET GLY THR GLU LEU ASN GLY LYS THR LEU GLY ILE LEU          
SEQRES   5 A  195  GLY LEU GLY ARG ILE GLY ARG GLU VAL ALA THR ARG MET          
SEQRES   6 A  195  GLN SER PHE GLY MET LYS THR ILE GLY TYR ASP PRO ILE          
SEQRES   7 A  195  ILE SER PRO GLU VAL SER ALA SER PHE GLY VAL GLN GLN          
SEQRES   8 A  195  LEU PRO LEU GLU GLU ILE TRP PRO LEU CYS ASP PHE ILE          
SEQRES   9 A  195  THR VAL HIS THR PRO LEU LEU PRO SER THR THR GLY LEU          
SEQRES  10 A  195  LEU ASN ASP ASN THR PHE ALA GLN CYS LYS LYS GLY VAL          
SEQRES  11 A  195  ARG VAL VAL ASN CYS ALA ARG GLY GLY ILE VAL ASP GLU          
SEQRES  12 A  195  GLY ALA LEU LEU ARG ALA LEU GLN SER GLY GLN CYS ALA          
SEQRES  13 A  195  GLY ALA ALA LEU ASP VAL PHE THR GLU GLU PRO PRO ARG          
SEQRES  14 A  195  ASP ARG ALA LEU VAL ASP HIS GLU ASN VAL ILE SER CYS          
SEQRES  15 A  195  PRO HIS LEU GLY ALA SER THR LYS GLU ALA GLN SER ARG          
HET    8NB  B 301      13                                                       
HET    8NB  A 301      13                                                       
HETNAM     8NB ~{N}-(3-CHLORANYL-4-METHOXY-PHENYL)ETHANAMIDE                    
FORMUL   3  8NB    2(C9 H10 CL N O2)                                            
FORMUL   5  HOH   *238(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 ARG B  135  MET B  139  5                                   5    
HELIX    4 AA4 GLY B  154  SER B  166  1                                  13    
HELIX    5 AA5 SER B  179  PHE B  186  1                                   8    
HELIX    6 AA6 PRO B  192  TRP B  197  1                                   6    
HELIX    7 AA7 PRO B  198  CYS B  200  5                                   3    
HELIX    8 AA8 ASN B  218  ALA B  223  1                                   6    
HELIX    9 AA9 ASP B  241  GLY B  252  1                                  12    
HELIX   10 AB1 ARG B  270  HIS B  275  1                                   6    
HELIX   11 AB2 THR B  288  SER B  293  1                                   6    
HELIX   12 AB3 ASN A  102  GLN A  120  1                                  19    
HELIX   13 AB4 GLN A  120  ASP A  130  1                                  11    
HELIX   14 AB5 ARG A  135  MET A  139  5                                   5    
HELIX   15 AB6 GLY A  154  SER A  166  1                                  13    
HELIX   16 AB7 SER A  179  PHE A  186  1                                   8    
HELIX   17 AB8 PRO A  192  TRP A  197  1                                   6    
HELIX   18 AB9 PRO A  198  CYS A  200  5                                   3    
HELIX   19 AC1 ASN A  218  ALA A  223  1                                   6    
HELIX   20 AC2 ASP A  241  GLY A  252  1                                  12    
HELIX   21 AC3 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 ARG B 230  ASN B 233  1  O  VAL B 232   N  ILE B 203           
SHEET    6 AA1 7 GLY B 256  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  PHE A 202   N  GLY A 149           
SHEET    5 AA2 7 ARG A 230  ASN A 233  1  O  VAL A 232   N  ILE A 203           
SHEET    6 AA2 7 GLY A 256  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        -4.89                     
CISPEP   2 GLU A  265    PRO A  266          0        -7.74                     
SITE     1 AC1  6 GLU A 194  GLY B 152  TYR B 174  PRO B 176                    
SITE     2 AC1  6 THR B 207  THR B 213                                          
SITE     1 AC2  9 GLY A 152  TYR A 174  PRO A 176  THR A 207                    
SITE     2 AC2  9 PRO A 208  LEU A 210  SER A 212  THR A 213                    
SITE     3 AC2  9 HOH A 459                                                     
CRYST1   43.353   45.323   55.255  97.90 110.06 106.35 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      0.023066  0.006765  0.010543        0.00000                         
SCALE2      0.000000  0.022993  0.006183        0.00000                         
SCALE3      0.000000  0.000000  0.019952        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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