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Database: PDB
Entry: 4XDE
LinkDB: 4XDE
Original site: 4XDE 
HEADER    BLOOD CLOTTING                          19-DEC-14   4XDE              
TITLE     COAGULATION FACTOR XII PROTEASE DOMAIN CRYSTAL STRUCTURE              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR XII;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEASE DOMAIN, UNP RESIDUES 373-615;                     
COMPND   5 SYNONYM: HAGEMAN FACTOR,HAF;                                         
COMPND   6 EC: 3.4.21.38;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: F12;                                                           
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER 2 (S2);                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMT-PURO                                  
KEYWDS    FACTOR XII, CATALYTIC DOMAIN, ZYMOGENS, HYDROLASE, BLOOD CLOTTING     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PATHAK,P.WILMANN,J.AWFORD,C.LI,P.M.FISHER,I.DREVENY,L.V.DEKKER,     
AUTHOR   2 J.EMSLEY                                                             
REVDAT   3   28-OCT-15 4XDE    1       JRNL                                     
REVDAT   2   15-APR-15 4XDE    1       JRNL                                     
REVDAT   1   04-FEB-15 4XDE    0                                                
JRNL        AUTH   M.PATHAK,P.WILMANN,J.AWFORD,C.LI,B.K.HAMAD,P.M.FISCHER,      
JRNL        AUTH 2 I.DREVENY,L.V.DEKKER,J.EMSLEY                                
JRNL        TITL   COAGULATION FACTOR XII PROTEASE DOMAIN CRYSTAL STRUCTURE.    
JRNL        REF    J.THROMB.HAEMOST.             V.  13   580 2015              
JRNL        REFN                   ESSN 1538-7836                               
JRNL        PMID   25604127                                                     
JRNL        DOI    10.1111/JTH.12849                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.14 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 15301                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 814                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.14                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.20                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 953                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 53                           
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1829                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.89000                                              
REMARK   3    B22 (A**2) : 0.89000                                              
REMARK   3    B33 (A**2) : -1.78000                                             
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): 0.251         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.208         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1903 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1729 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2600 ; 1.855 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3962 ; 3.851 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   240 ; 6.497 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    85 ;35.225 ;23.294       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   269 ;18.534 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;19.758 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   280 ; 0.146 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2194 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   445 ; 0.009 ; 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):  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 4XDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205476.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16670                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.140                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 12.90                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1YBW WITH 44% IDENTITY                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULPHATE, 0.05 M TRI      
REMARK 280  -SODIUM CITRATE, 3%(W/V) ISOPROPANOL., VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
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       19.07250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       62.06300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       62.06300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        9.53625            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       62.06300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       62.06300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       28.60875            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       62.06300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.06300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        9.53625            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       62.06300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.06300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       28.60875            
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       19.07250            
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 TOTAL BURIED SURFACE AREA: 800 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 12090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 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     ARG A   352                                                      
REMARK 465     SER A   353                                                      
REMARK 465     VAL A   354                                                      
REMARK 465     VAL A   355                                                      
REMARK 465     GLY A   356                                                      
REMARK 465     GLY A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     GLY A   600                                                      
REMARK 465     THR A   601                                                      
REMARK 465     ARG A   602                                                      
REMARK 465     HIS A   603                                                      
REMARK 465     HIS A   604                                                      
REMARK 465     HIS A   605                                                      
REMARK 465     HIS A   606                                                      
REMARK 465     HIS A   607                                                      
REMARK 465     HIS A   608                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG A   413     N    ASN A   414              1.65            
REMARK 500   O    ASN A   414     N    HIS A   415              1.79            
REMARK 500   CA   ARG A   413     N    ASN A   414              1.80            
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    ARG A 413   C     ASN A 414   N      -0.763                       
REMARK 500    ASN A 414   C     HIS A 415   N      -0.306                       
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 361   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    ASN A 414   CA  -  C   -  N   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ASN A 414   O   -  C   -  N   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    THR A 537   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ASP A 538   N   -  CA  -  CB  ANGL. DEV. =  10.9 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    ASN A 414       32.50     32.27                                   
REMARK 500    CYS A 456      -89.09   -110.59                                   
REMARK 500    ALA A 493       73.31     47.76                                   
REMARK 500    VAL A 518      -87.05   -109.49                                   
REMARK 500    THR A 537       45.51     31.38                                   
REMARK 500    GLN A 553      -50.78     70.43                                   
REMARK 500    ALA A 554       13.47    -69.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASN A 414        -11.12                                           
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 IPA A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 703                 
DBREF  4XDE A  354   596  UNP    P00748   FA12_HUMAN     373    615             
SEQADV 4XDE ARG A  352  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE SER A  353  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE SER A  467  UNP  P00748    CYS   486 ENGINEERED MUTATION            
SEQADV 4XDE HIS A  597  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE HIS A  598  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE THR A  599  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE GLY A  600  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE THR A  601  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE ARG A  602  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE HIS A  603  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE HIS A  604  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE HIS A  605  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE HIS A  606  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE HIS A  607  UNP  P00748              EXPRESSION TAG                 
SEQADV 4XDE HIS A  608  UNP  P00748              EXPRESSION TAG                 
SEQRES   1 A  257  ARG SER VAL VAL GLY GLY LEU VAL ALA LEU ARG GLY ALA          
SEQRES   2 A  257  HIS PRO TYR ILE ALA ALA LEU TYR TRP GLY HIS SER PHE          
SEQRES   3 A  257  CYS ALA GLY SER LEU ILE ALA PRO CYS TRP VAL LEU THR          
SEQRES   4 A  257  ALA ALA HIS CYS LEU GLN ASP ARG PRO ALA PRO GLU ASP          
SEQRES   5 A  257  LEU THR VAL VAL LEU GLY GLN GLU ARG ARG ASN HIS SER          
SEQRES   6 A  257  CYS GLU PRO CYS GLN THR LEU ALA VAL ARG SER TYR ARG          
SEQRES   7 A  257  LEU HIS GLU ALA PHE SER PRO VAL SER TYR GLN HIS ASP          
SEQRES   8 A  257  LEU ALA LEU LEU ARG LEU GLN GLU ASP ALA ASP GLY SER          
SEQRES   9 A  257  CYS ALA LEU LEU SER PRO TYR VAL GLN PRO VAL SER LEU          
SEQRES  10 A  257  PRO SER GLY ALA ALA ARG PRO SER GLU THR THR LEU CYS          
SEQRES  11 A  257  GLN VAL ALA GLY TRP GLY HIS GLN PHE GLU GLY ALA GLU          
SEQRES  12 A  257  GLU TYR ALA SER PHE LEU GLN GLU ALA GLN VAL PRO PHE          
SEQRES  13 A  257  LEU SER LEU GLU ARG CYS SER ALA PRO ASP VAL HIS GLY          
SEQRES  14 A  257  SER SER ILE LEU PRO GLY MET LEU CYS ALA GLY PHE LEU          
SEQRES  15 A  257  GLU GLY GLY THR ASP ALA CYS GLN GLY ASP SER GLY GLY          
SEQRES  16 A  257  PRO LEU VAL CYS GLU ASP GLN ALA ALA GLU ARG ARG LEU          
SEQRES  17 A  257  THR LEU GLN GLY ILE ILE SER TRP GLY SER GLY CYS GLY          
SEQRES  18 A  257  ASP ARG ASN LYS PRO GLY VAL TYR THR ASP VAL ALA TYR          
SEQRES  19 A  257  TYR LEU ALA TRP ILE ARG GLU HIS THR VAL SER HIS HIS          
SEQRES  20 A  257  THR GLY THR ARG HIS HIS HIS HIS HIS HIS                      
HET    IPA  A 701       4                                                       
HET    IPA  A 702       4                                                       
HET    FLC  A 703      13                                                       
HETNAM     IPA ISOPROPYL ALCOHOL                                                
HETNAM     FLC CITRATE ANION                                                    
HETSYN     IPA 2-PROPANOL                                                       
FORMUL   2  IPA    2(C3 H8 O)                                                   
FORMUL   4  FLC    C6 H5 O7 3-                                                  
FORMUL   5  HOH   *97(H2 O)                                                     
HELIX    1 AA1 ALA A  391  GLN A  396  5                                   6    
HELIX    2 AA2 ALA A  400  ASP A  403  5                                   4    
HELIX    3 AA3 ALA A  493  ALA A  497  5                                   5    
HELIX    4 AA4 SER A  509  SER A  514  1                                   6    
HELIX    5 AA5 HIS A  519  ILE A  523  5                                   5    
HELIX    6 AA6 TYR A  586  HIS A  593  1                                   8    
SHEET    1 AA1 7 ILE A 368  TRP A 373  0                                        
SHEET    2 AA1 7 SER A 376  ALA A 384 -1  O  CYS A 378   N  LEU A 371           
SHEET    3 AA1 7 TRP A 387  THR A 390 -1  O  LEU A 389   N  SER A 381           
SHEET    4 AA1 7 ALA A 444  LEU A 448 -1  O  LEU A 446   N  VAL A 388           
SHEET    5 AA1 7 GLN A 421  LEU A 430 -1  N  SER A 427   O  ARG A 447           
SHEET    6 AA1 7 THR A 405  LEU A 408 -1  N  VAL A 406   O  LEU A 423           
SHEET    7 AA1 7 ILE A 368  TRP A 373 -1  N  ALA A 370   O  VAL A 407           
SHEET    1 AA2 7 LEU A 480  GLY A 485  0                                        
SHEET    2 AA2 7 GLN A 501  LEU A 508 -1  O  GLN A 501   N  GLY A 485           
SHEET    3 AA2 7 MET A 527  ALA A 530 -1  O  CYS A 529   N  LEU A 508           
SHEET    4 AA2 7 GLY A 578  ASP A 582 -1  O  TYR A 580   N  LEU A 528           
SHEET    5 AA2 7 LEU A 559  TRP A 567 -1  N  TRP A 567   O  VAL A 579           
SHEET    6 AA2 7 PRO A 547  GLU A 551 -1  N  CYS A 550   O  THR A 560           
SHEET    7 AA2 7 LEU A 480  GLY A 485 -1  N  GLN A 482   O  VAL A 549           
SSBOND   1 CYS A  378    CYS A  394                          1555   1555  2.10  
SSBOND   2 CYS A  386    CYS A  456                          1555   1555  2.10  
SSBOND   3 CYS A  417    CYS A  420                          1555   1555  2.10  
SSBOND   4 CYS A  481    CYS A  550                          1555   1555  2.04  
SSBOND   5 CYS A  513    CYS A  529                          1555   1555  2.03  
SSBOND   6 CYS A  540    CYS A  571                          1555   1555  2.06  
SITE     1 AC1  2 LEU A 371  CYS A 394                                          
SITE     1 AC2  7 TRP A 373  SER A 376  ASP A 397  LEU A 524                    
SITE     2 AC2  7 PRO A 525  HOH A 810  HOH A 853                               
SITE     1 AC3  6 VAL A 437  SER A 438  TYR A 439  SER A 522                    
SITE     2 AC3  6 TRP A 567  HOH A 861                                          
CRYST1  124.126  124.126   38.145  90.00  90.00  90.00 P 41 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      0.008056  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008056  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.026216        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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