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Database: PDB
Entry: 4MRA
LinkDB: 4MRA
Original site: 4MRA 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       17-SEP-13   4MRA              
TITLE     CRYSTAL STRUCTURE OF GPB IN COMPLEX WITH QUERCETIN                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOGEN PHOSPHORYLASE, MUSCLE FORM;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MYOPHOSPHORYLASE;                                           
COMPND   5 EC: 2.4.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE   3 ORGANISM_COMMON: EUROPEAN RABBIT,JAPANESE WHITE RABBIT,DOMESTIC      
SOURCE   4 RABBIT,RABBITS;                                                      
SOURCE   5 ORGANISM_TAXID: 9986;                                                
SOURCE   6 OTHER_DETAILS: MUSCLE                                                
KEYWDS    ALPHA AND BETA PROTEIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.A.KANTSADI,S.M.D.CHATZILEONTIADOU,D.D.LEONIDAS                      
REVDAT   3   06-DEC-23 4MRA    1       REMARK                                   
REVDAT   2   20-SEP-23 4MRA    1       REMARK LINK                              
REVDAT   1   07-MAY-14 4MRA    0                                                
JRNL        AUTH   A.L.KANTSADI,A.APOSTOLOU,S.THEOFANOUS,G.A.STRAVODIMOS,       
JRNL        AUTH 2 E.KYRIAKIS,V.A.GORGOGIETAS,D.S.CHATZILEONTIADOU,K.PEGIOU,    
JRNL        AUTH 3 V.T.SKAMNAKI,D.STAGOS,D.KOURETAS,A.M.PSARRA,                 
JRNL        AUTH 4 S.A.HAROUTOUNIAN,D.D.LEONIDAS                                
JRNL        TITL   BIOCHEMICAL AND BIOLOGICAL ASSESSMENT OF THE INHIBITORY      
JRNL        TITL 2 POTENCY OF EXTRACTS FROM VINIFICATION BYPRODUCTS OF VITIS    
JRNL        TITL 3 VINIFERA EXTRACTS AGAINST GLYCOGEN PHOSPHORYLASE.            
JRNL        REF    FOOD CHEM.TOXICOL.            V.  67    35 2014              
JRNL        REFN                   ISSN 0278-6915                               
JRNL        PMID   24556570                                                     
JRNL        DOI    10.1016/J.FCT.2014.01.055                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 38265                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2023                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.34                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2736                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6578                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 352                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.12000                                              
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): 0.348         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.248         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.170         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.084         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6761 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6458 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9156 ; 1.616 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14783 ; 0.895 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   806 ; 6.782 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   346 ;36.391 ;23.497       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1172 ;17.341 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;20.955 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   985 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7663 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1645 ; 0.001 ; 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):  3227 ; 2.188 ; 2.813       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3226 ; 2.184 ; 2.811       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4029 ; 3.393 ; 4.201       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3534 ; 2.850 ; 3.196       
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):  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 : MASK                                                 
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 4MRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082267.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X13                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8                                
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40399                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.00                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3SYM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MM BES BUFFER, PH 6.7, SMALL TUBES,    
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.91050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       63.30000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       86.86575            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       63.30000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.95525            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.30000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       86.86575            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.30000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       28.95525            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       57.91050            
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: 5930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      115.82100            
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     PHE A   252                                                      
REMARK 465     ASN A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     LYS A   255                                                      
REMARK 465     ASP A   256                                                      
REMARK 465     PHE A   257                                                      
REMARK 465     ASN A   258                                                      
REMARK 465     VAL A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     PHE A   316                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     CYS A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     ASP A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     VAL A   322                                                      
REMARK 465     ARG A   323                                                      
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   O29  QUE A   901     O    HOH A  1165              2.09            
REMARK 500   NH1  ARG A   770     O    HOH A  1053              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   178     OD1  ASP A   251     7556     2.19            
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    LEU A  85   CB  -  CG  -  CD2 ANGL. DEV. = -10.9 DEGREES          
REMARK 500    LEU A  87   CA  -  CB  -  CG  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    ARG A 138   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG A 398   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 424   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 639   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 649   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 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    LEU A 131       41.97    -87.70                                   
REMARK 500    TYR A 203     -141.88     64.22                                   
REMARK 500    THR A 209     -156.12   -106.53                                   
REMARK 500    ASN A 236       13.01     58.03                                   
REMARK 500    ASP A 339     -174.50     67.58                                   
REMARK 500    THR A 466     -101.62   -129.01                                   
REMARK 500    ARG A 489      -78.95    -67.42                                   
REMARK 500    LEU A 492      -67.99   -146.80                                   
REMARK 500    ASP A 514       71.59   -159.45                                   
REMARK 500    LYS A 568      169.64    171.07                                   
REMARK 500    SER A 674      -56.81   -139.80                                   
REMARK 500    SER A 751       69.80   -162.20                                   
REMARK 500    ILE A 824      -52.41   -122.18                                   
REMARK 500    ARG A 833      150.23    -48.62                                   
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 QUE A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 902                 
DBREF  4MRA A   12   836  UNP    P00489   PYGM_RABIT      13    837             
SEQRES   1 A  825  GLN ILE SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL          
SEQRES   2 A  825  THR GLU LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE          
SEQRES   3 A  825  THR LEU VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP          
SEQRES   4 A  825  TYR TYR PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU          
SEQRES   5 A  825  VAL GLY ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU          
SEQRES   6 A  825  LYS ASP PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE          
SEQRES   7 A  825  TYR MET GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU          
SEQRES   8 A  825  ALA LEU GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU          
SEQRES   9 A  825  GLY LEU ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP          
SEQRES  10 A  825  ALA GLY LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA          
SEQRES  11 A  825  CYS PHE LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA          
SEQRES  12 A  825  TYR GLY TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN          
SEQRES  13 A  825  GLN LYS ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP          
SEQRES  14 A  825  ASP TRP LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG          
SEQRES  15 A  825  PRO GLU PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL          
SEQRES  16 A  825  GLU HIS THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN          
SEQRES  17 A  825  VAL VAL LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY          
SEQRES  18 A  825  TYR ARG ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER          
SEQRES  19 A  825  ALA LYS ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN          
SEQRES  20 A  825  VAL GLY GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU          
SEQRES  21 A  825  ALA GLU ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN          
SEQRES  22 A  825  PHE PHE GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR          
SEQRES  23 A  825  PHE VAL VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG          
SEQRES  24 A  825  PHE LYS SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG          
SEQRES  25 A  825  THR ASN PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN          
SEQRES  26 A  825  LEU ASN ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU          
SEQRES  27 A  825  MET ARG VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP          
SEQRES  28 A  825  LYS ALA TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR          
SEQRES  29 A  825  ASN HIS THR VAL LEU PRO GLU ALA LEU GLU ARG TRP PRO          
SEQRES  30 A  825  VAL HIS LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN          
SEQRES  31 A  825  ILE ILE TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL          
SEQRES  32 A  825  ALA ALA ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG          
SEQRES  33 A  825  MET SER LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN          
SEQRES  34 A  825  MET ALA HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN          
SEQRES  35 A  825  GLY VAL ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR          
SEQRES  36 A  825  ILE PHE LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE          
SEQRES  37 A  825  GLN ASN LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU          
SEQRES  38 A  825  VAL LEU CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU          
SEQRES  39 A  825  ARG ILE GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU          
SEQRES  40 A  825  ARG LYS LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE          
SEQRES  41 A  825  ARG ASP VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS          
SEQRES  42 A  825  PHE ALA ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE          
SEQRES  43 A  825  ASN PRO ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE          
SEQRES  44 A  825  HIS GLU TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL          
SEQRES  45 A  825  ILE THR LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS          
SEQRES  46 A  825  PHE VAL VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA          
SEQRES  47 A  825  ALA PRO GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU          
SEQRES  48 A  825  ILE THR ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL          
SEQRES  49 A  825  VAL GLY ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR          
SEQRES  50 A  825  ARG VAL SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP          
SEQRES  51 A  825  LEU SER GLU GLN ILE SER THR ALA GLY THR GLU ALA SER          
SEQRES  52 A  825  GLY THR GLY ASN MET LLP PHE MET LEU ASN GLY ALA LEU          
SEQRES  53 A  825  THR ILE GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA          
SEQRES  54 A  825  GLU GLU ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET          
SEQRES  55 A  825  ARG VAL GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR          
SEQRES  56 A  825  ASN ALA GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG          
SEQRES  57 A  825  GLN ILE ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO          
SEQRES  58 A  825  LYS GLN PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU          
SEQRES  59 A  825  MET HIS HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU          
SEQRES  60 A  825  GLU TYR VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR          
SEQRES  61 A  825  LYS ASN PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN          
SEQRES  62 A  825  ILE ALA THR SER GLY LYS PHE SER SER ASP ARG THR ILE          
SEQRES  63 A  825  ALA GLN TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER          
SEQRES  64 A  825  ARG GLN ARG LEU PRO ALA                                      
MODRES 4MRA LLP A  680  LYS                                                     
HET    LLP  A 680      24                                                       
HET    QUE  A 901      22                                                       
HET    DMS  A 902       4                                                       
HETNAM     LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-                           
HETNAM   2 LLP  (PHOSPHONOOXYMETHYL)PYRIDIN-4-                                  
HETNAM   3 LLP  YL]METHYLIDENEAMINO]HEXANOIC ACID                               
HETNAM     QUE 3,5,7,3',4'-PENTAHYDROXYFLAVONE                                  
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
HETSYN     QUE QUERCETIN                                                        
FORMUL   1  LLP    C14 H22 N3 O7 P                                              
FORMUL   2  QUE    C15 H10 O7                                                   
FORMUL   3  DMS    C2 H6 O S                                                    
FORMUL   4  HOH   *352(H2 O)                                                    
HELIX    1   1 ILE A   13  GLY A   17  5                                   5    
HELIX    2   2 GLY A   20  THR A   38  1                                  19    
HELIX    3   3 THR A   47  ASP A   78  1                                  32    
HELIX    4   4 THR A   94  ALA A  103  1                                  10    
HELIX    5   5 LEU A  104  LEU A  115  1                                  12    
HELIX    6   6 ASP A  118  GLU A  124  1                                   7    
HELIX    7   7 GLY A  134  LEU A  150  1                                  17    
HELIX    8   8 PRO A  194  THR A  197  5                                   4    
HELIX    9   9 TYR A  262  ASP A  268  1                                   7    
HELIX   10  10 ASP A  268  ASN A  274  1                                   7    
HELIX   11  11 ILE A  275  ARG A  277  5                                   3    
HELIX   12  12 LYS A  289  SER A  313  1                                  25    
HELIX   13  13 ASN A  325  ASP A  327  5                                   3    
HELIX   14  14 ALA A  328  LYS A  332  1                                   5    
HELIX   15  15 LEU A  344  LEU A  356  1                                  13    
HELIX   16  16 ASP A  360  THR A  371  1                                  12    
HELIX   17  17 LEU A  380  LEU A  384  5                                   5    
HELIX   18  18 VAL A  389  LEU A  396  1                                   8    
HELIX   19  19 LEU A  396  PHE A  418  1                                  23    
HELIX   20  20 ASP A  421  SER A  429  1                                   9    
HELIX   21  21 MET A  441  SER A  449  1                                   9    
HELIX   22  22 ALA A  456  THR A  466  1                                  11    
HELIX   23  23 PHE A  468  GLU A  475  1                                   8    
HELIX   24  24 ASN A  496  GLY A  508  1                                  13    
HELIX   25  25 GLU A  509  VAL A  525  5                                  17    
HELIX   26  26 ASP A  527  LYS A  554  1                                  28    
HELIX   27  27 ARG A  575  GLU A  593  1                                  19    
HELIX   28  28 TYR A  613  ASN A  631  1                                  19    
HELIX   29  29 VAL A  636  ASP A  638  5                                   3    
HELIX   30  30 ARG A  649  ILE A  657  1                                   9    
HELIX   31  31 THR A  676  ASN A  684  1                                   9    
HELIX   32  32 ALA A  695  GLY A  704  1                                  10    
HELIX   33  33 GLU A  705  PHE A  708  5                                   4    
HELIX   34  34 ARG A  714  GLY A  725  1                                  12    
HELIX   35  35 ASN A  727  ILE A  735  1                                   9    
HELIX   36  36 ILE A  735  GLY A  748  1                                  14    
HELIX   37  37 PHE A  758  HIS A  768  1                                  11    
HELIX   38  38 VAL A  773  ALA A  775  5                                   3    
HELIX   39  39 ASP A  776  LYS A  792  1                                  17    
HELIX   40  40 ASN A  793  ALA A  806  1                                  14    
HELIX   41  41 THR A  807  PHE A  811  5                                   5    
HELIX   42  42 SER A  812  ILE A  824  1                                  13    
SHEET    1   A 3 LYS A 191  ALA A 192  0                                        
SHEET    2   A 3 GLN A 219  PRO A 231 -1  O  ASP A 227   N  LYS A 191           
SHEET    3   A 3 LEU A 198  PHE A 202 -1  N  LEU A 198   O  ALA A 223           
SHEET    1   B 9 LYS A 191  ALA A 192  0                                        
SHEET    2   B 9 GLN A 219  PRO A 231 -1  O  ASP A 227   N  LYS A 191           
SHEET    3   B 9 VAL A 238  LYS A 247 -1  O  SER A 245   N  MET A 224           
SHEET    4   B 9 ALA A 154  ILE A 159  1  N  GLY A 156   O  ARG A 242           
SHEET    5   B 9 ARG A  81  LEU A  85  1  N  ILE A  82   O  TYR A 155           
SHEET    6   B 9 VAL A 333  ASN A 338  1  O  ALA A 334   N  TYR A  83           
SHEET    7   B 9 CYS A 372  THR A 375  1  O  ALA A 373   N  LEU A 337           
SHEET    8   B 9 ALA A 451  GLY A 454  1  O  ALA A 451   N  TYR A 374           
SHEET    9   B 9 PHE A 479  ASN A 481  1  O  GLN A 480   N  VAL A 452           
SHEET    1   C 2 PHE A  89  GLY A  92  0                                        
SHEET    2   C 2 ALA A 129  LEU A 131 -1  O  LEU A 131   N  PHE A  89           
SHEET    1   D 2 ASN A 167  CYS A 171  0                                        
SHEET    2   D 2 TRP A 174  GLU A 178 -1  O  MET A 176   N  LYS A 169           
SHEET    1   E 2 ARG A 205  HIS A 208  0                                        
SHEET    2   E 2 ALA A 213  VAL A 216 -1  O  LYS A 214   N  GLU A 207           
SHEET    1   F 3 ARG A 386  PRO A 388  0                                        
SHEET    2   F 3 ARG A 438  ASN A 440 -1  O  ILE A 439   N  TRP A 387           
SHEET    3   F 3 VAL A 431  GLU A 432 -1  N  GLU A 432   O  ARG A 438           
SHEET    1   G 6 LEU A 640  LEU A 645  0                                        
SHEET    2   G 6 ARG A 601  GLY A 606  1  N  VAL A 603   O  ARG A 641           
SHEET    3   G 6 LEU A 562  VAL A 567  1  N  ASP A 564   O  MET A 604           
SHEET    4   G 6 LEU A 662  GLN A 665  1  O  GLU A 664   N  VAL A 565           
SHEET    5   G 6 LEU A 687  GLY A 690  1  O  LEU A 687   N  SER A 663           
SHEET    6   G 6 PHE A 709  ILE A 710  1  O  PHE A 709   N  GLY A 690           
LINK         C   MET A 679                 N   LLP A 680     1555   1555  1.34  
LINK         C   LLP A 680                 N   PHE A 681     1555   1555  1.32  
CISPEP   1 SER A  210    GLN A  211          0        21.32                     
SITE     1 AC1  8 GLU A 121  GLU A 124  LYS A 544  TYR A 548                    
SITE     2 AC1  8 ARG A 551  GLU A 552  HOH A1042  HOH A1165                    
SITE     1 AC2  4 ARG A 519  GLU A 702  ALA A 703  HOH A1207                    
CRYST1  126.600  126.600  115.821  90.00  90.00  90.00 P 43 21 2     8          
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      0.007899  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007899  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008634        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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