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Database: PDB
Entry: 6DNB
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Original site: 6DNB 
HEADER    TRANSFERASE                             06-JUN-18   6DNB              
TITLE     CRYSTAL STRUCTURE OF T110A:S256A MUTANT HUMAN GLUTAMATE OXALOACETATE  
TITLE    2 TRANSAMINASE 1 (GOT1)                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CASPAT,CYSTEINE AMINOTRANSFERASE,CYTOPLASMIC,CYSTEINE       
COMPND   5 TRANSAMINASE,CCAT,GLUTAMATE OXALOACETATE TRANSAMINASE 1,TRANSAMINASE 
COMPND   6 A;                                                                   
COMPND   7 EC: 2.6.1.1,2.6.1.3;                                                 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GOT1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ASPARTATE AMINOTRANSFERASE, GLUTAMATE OXALOACETATE TRANSAMINASE 1,    
KEYWDS   2 GOT1, PLP, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.ASSAR,M.C.HOLT,A.J.STEIN,L.LAIRSON,C.A.LYSSIOTIS                    
REVDAT   3   05-DEC-18 6DNB    1       JRNL                                     
REVDAT   2   21-NOV-18 6DNB    1       JRNL                                     
REVDAT   1   14-NOV-18 6DNB    0                                                
JRNL        AUTH   M.C.HOLT,Z.ASSAR,R.BEHESHTI ZAVAREH,L.LIN,J.ANGLIN,          
JRNL        AUTH 2 O.MASHADOVA,D.HALDAR,E.MULLARKY,D.M.KREMER,L.C.CANTLEY,      
JRNL        AUTH 3 A.C.KIMMELMAN,A.J.STEIN,L.L.LAIRSON,C.A.LYSSIOTIS            
JRNL        TITL   BIOCHEMICAL CHARACTERIZATION AND STRUCTURE-BASED MUTATIONAL  
JRNL        TITL 2 ANALYSIS PROVIDE INSIGHT INTO THE BINDING AND MECHANISM OF   
JRNL        TITL 3 ACTION OF NOVEL ASPARTATE AMINOTRANSFERASE INHIBITORS.       
JRNL        REF    BIOCHEMISTRY                  V.  57  6604 2018              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   30365304                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.8B00914                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 46568                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2464                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3272                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 180                          
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3243                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 237                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.105         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.074         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.242         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3424 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3146 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4652 ; 2.167 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7310 ; 1.202 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   430 ; 6.505 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   163 ;35.829 ;23.804       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   557 ;14.919 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;18.733 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   506 ; 0.165 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3813 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   727 ; 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):  1663 ; 2.367 ; 2.208       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1662 ; 2.346 ; 2.205       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2082 ; 3.230 ; 3.306       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2083 ; 3.232 ; 3.309       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1761 ; 3.728 ; 2.666       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1757 ; 3.702 ; 2.666       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2555 ; 5.416 ; 3.837       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4108 ; 7.044 ;28.565       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4108 ; 7.046 ;28.562       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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 6DNB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234943.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46568                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.24                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 47.6200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3II0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 20% W/V/ PEG MME      
REMARK 280  2,000, 0.2 M TRIMETHYLAMINE N-OXIDE DEHYDRATE, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      140.08533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.04267            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      105.06400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       35.02133            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      175.10667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      140.08533            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       70.04267            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       35.02133            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      105.06400            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      175.10667            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TRP A 296    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 296    CZ3  CH2                                            
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   OG1  THR A   350     CD1  ILE A   352              1.99            
REMARK 500   O1   GOL A   504     O    HOH A   601              2.09            
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   C4   PG4 A   501     C4   PG4 A   501     7554     2.09            
REMARK 500   OE1  GLN A    12     NE2  GLN A   283    10665     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 266   CG    GLU A 266   CD      0.101                       
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    GLU A  27   CB  -  CA  -  C   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 167   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A 167   NE  -  CZ  -  NH2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    GLU A 266   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A 305   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    PRO A  73      151.87    -49.61                                   
REMARK 500    TYR A 161      -71.56   -150.49                                   
REMARK 500    SER A 224       78.77   -113.43                                   
REMARK 500    THR A 295     -143.19   -114.30                                   
REMARK 500    TRP A 296      -80.44      3.66                                   
REMARK 500    SER A 297      109.53     68.38                                   
REMARK 500    ASN A 298     -114.11   -128.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A  298     PRO A  299                  -45.69                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 A  501                                                       
REMARK 610     PG4 A  502                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 506                 
DBREF  6DNB A    3   413  UNP    P17174   AATC_HUMAN       3    413             
SEQADV 6DNB ALA A  110  UNP  P17174    THR   110 ENGINEERED MUTATION            
SEQADV 6DNB ALA A  256  UNP  P17174    SER   256 ENGINEERED MUTATION            
SEQADV 6DNB ILE A  352  UNP  P17174    ASN   352 CONFLICT                       
SEQRES   1 A  411  PRO PRO SER VAL PHE ALA GLU VAL PRO GLN ALA GLN PRO          
SEQRES   2 A  411  VAL LEU VAL PHE LYS LEU THR ALA ASP PHE ARG GLU ASP          
SEQRES   3 A  411  PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL GLY ALA TYR          
SEQRES   4 A  411  ARG THR ASP ASP CYS HIS PRO TRP VAL LEU PRO VAL VAL          
SEQRES   5 A  411  LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP ASN SER LEU          
SEQRES   6 A  411  ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU ALA GLU PHE          
SEQRES   7 A  411  ARG SER CYS ALA SER ARG LEU ALA LEU GLY ASP ASP SER          
SEQRES   8 A  411  PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY VAL GLN SER          
SEQRES   9 A  411  LEU GLY GLY ALA GLY ALA LEU ARG ILE GLY ALA ASP PHE          
SEQRES  10 A  411  LEU ALA ARG TRP TYR ASN GLY THR ASN ASN LYS ASN THR          
SEQRES  11 A  411  PRO VAL TYR VAL SER SER PRO THR TRP GLU ASN HIS ASN          
SEQRES  12 A  411  ALA VAL PHE SER ALA ALA GLY PHE LYS ASP ILE ARG SER          
SEQRES  13 A  411  TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY LEU ASP LEU          
SEQRES  14 A  411  GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA PRO GLU PHE          
SEQRES  15 A  411  SER ILE VAL VAL LEU HIS ALA CYS ALA HIS ASN PRO THR          
SEQRES  16 A  411  GLY ILE ASP PRO THR PRO GLU GLN TRP LYS GLN ILE ALA          
SEQRES  17 A  411  SER VAL MET LYS HIS ARG PHE LEU PHE PRO PHE PHE ASP          
SEQRES  18 A  411  SER ALA TYR GLN GLY PHE ALA SER GLY ASN LEU GLU ARG          
SEQRES  19 A  411  ASP ALA TRP ALA ILE ARG TYR PHE VAL SER GLU GLY PHE          
SEQRES  20 A  411  GLU PHE PHE CYS ALA GLN ALA PHE SER LYS ASN PHE GLY          
SEQRES  21 A  411  LEU TYR ASN GLU ARG VAL GLY ASN LEU THR VAL VAL GLY          
SEQRES  22 A  411  LYS GLU PRO GLU SER ILE LEU GLN VAL LEU SER GLN MET          
SEQRES  23 A  411  GLU LYS ILE VAL ARG ILE THR TRP SER ASN PRO PRO ALA          
SEQRES  24 A  411  GLN GLY ALA ARG ILE VAL ALA SER THR LEU SER ASN PRO          
SEQRES  25 A  411  GLU LEU PHE GLU GLU TRP THR GLY ASN VAL LYS THR MET          
SEQRES  26 A  411  ALA ASP ARG ILE LEU THR MET ARG SER GLU LEU ARG ALA          
SEQRES  27 A  411  ARG LEU GLU ALA LEU LYS THR PRO GLY THR TRP ILE HIS          
SEQRES  28 A  411  ILE THR ASP GLN ILE GLY MET PHE SER PHE THR GLY LEU          
SEQRES  29 A  411  ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN GLU LYS HIS          
SEQRES  30 A  411  ILE TYR LEU LEU PRO SER GLY ARG ILE ASN VAL SER GLY          
SEQRES  31 A  411  LEU THR THR LYS ASN LEU ASP TYR VAL ALA THR SER ILE          
SEQRES  32 A  411  HIS GLU ALA VAL THR LYS ILE GLN                              
HET    PG4  A 501       8                                                       
HET    PG4  A 502       7                                                       
HET    GOL  A 503       6                                                       
HET    GOL  A 504       6                                                       
HET    GOL  A 505       6                                                       
HET    PO4  A 506       5                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  PG4    2(C8 H18 O5)                                                 
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   7  PO4    O4 P 3-                                                      
FORMUL   8  HOH   *237(H2 O)                                                    
HELIX    1 AA1 VAL A   16  ASP A   28  1                                  13    
HELIX    2 AA2 LEU A   51  ASP A   64  1                                  14    
HELIX    3 AA3 LEU A   77  GLY A   90  1                                  14    
HELIX    4 AA4 SER A   93  GLU A   98  1                                   6    
HELIX    5 AA5 GLY A  108  TYR A  124  1                                  17    
HELIX    6 AA6 TRP A  141  GLY A  152  1                                  12    
HELIX    7 AA7 ASP A  170  ASN A  180  1                                  11    
HELIX    8 AA8 THR A  202  PHE A  217  1                                  16    
HELIX    9 AA9 ASN A  233  ALA A  238  1                                   6    
HELIX   10 AB1 ALA A  238  GLU A  247  1                                  10    
HELIX   11 AB2 LEU A  263  GLU A  266  5                                   4    
HELIX   12 AB3 GLU A  277  THR A  295  1                                  19    
HELIX   13 AB4 ALA A  301  SER A  312  1                                  12    
HELIX   14 AB5 ASN A  313  LEU A  345  1                                  33    
HELIX   15 AB6 ILE A  352  GLN A  357  1                                   6    
HELIX   16 AB7 ASN A  367  GLU A  377  1                                  11    
HELIX   17 AB8 SER A  391  LEU A  393  5                                   3    
HELIX   18 AB9 ASN A  397  ILE A  412  1                                  16    
SHEET    1 AA1 2 VAL A  34  ASN A  35  0                                        
SHEET    2 AA1 2 ILE A 380  TYR A 381  1  O  TYR A 381   N  VAL A  34           
SHEET    1 AA2 7 VAL A 101  LEU A 107  0                                        
SHEET    2 AA2 7 VAL A 268  VAL A 274 -1  O  LEU A 271   N  VAL A 104           
SHEET    3 AA2 7 PHE A 251  ALA A 256 -1  N  GLN A 255   O  ASN A 270           
SHEET    4 AA2 7 PHE A 219  SER A 224  1  N  SER A 224   O  ALA A 254           
SHEET    5 AA2 7 ILE A 186  HIS A 190  1  N  LEU A 189   O  ASP A 223           
SHEET    6 AA2 7 VAL A 134  SER A 138  1  N  TYR A 135   O  ILE A 186           
SHEET    7 AA2 7 ILE A 156  ARG A 160  1  O  ARG A 157   N  VAL A 134           
SHEET    1 AA3 2 TRP A 162  ASP A 163  0                                        
SHEET    2 AA3 2 GLY A 168  LEU A 169 -1  O  GLY A 168   N  ASP A 163           
SHEET    1 AA4 2 PHE A 361  PHE A 363  0                                        
SHEET    2 AA4 2 ARG A 387  ASN A 389 -1  O  ILE A 388   N  SER A 362           
CISPEP   1 SER A  138    PRO A  139          0       -10.83                     
CISPEP   2 ASN A  195    PRO A  196          0        19.91                     
SITE     1 AC1  3 LYS A 346  THR A 347  GLY A 349                               
SITE     1 AC2  7 CYS A  83  ARG A  86  LEU A  87  GLY A  90                    
SITE     2 AC2  7 ASP A  91  LEU A 311  PHE A 317                               
SITE     1 AC3 10 TYR A  71  GLY A 108  GLY A 109  ALA A 110                    
SITE     2 AC3 10 ALA A 256  SER A 258  ARG A 267  HOH A 606                    
SITE     3 AC3 10 HOH A 634  HOH A 796                                          
SITE     1 AC4  9 VAL A   6  MET A 213  PHE A 217  LEU A 218                    
SITE     2 AC4  9 PHE A 249  GLU A 250  HOH A 601  HOH A 656                    
SITE     3 AC4  9 HOH A 677                                                     
SITE     1 AC5  6 ASN A 143  ALA A 146  ILE A 294  THR A 295                    
SITE     2 AC5  6 TRP A 296  HOH A 673                                          
SITE     1 AC6  4 TYR A  41  THR A  43  TRP A  49  THR A 326                    
CRYST1   84.085   84.085  210.128  90.00  90.00 120.00 P 65 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011893  0.006866  0.000000        0.00000                         
SCALE2      0.000000  0.013733  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004759        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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