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Database: PDB
Entry: 6GT6
LinkDB: 6GT6
Original site: 6GT6 
HEADER    BLOOD CLOTTING                          15-JUN-18   6GT6              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT COAGULATION FACTOR BETA-XIIA         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR XII;                                    
COMPND   3 CHAIN: B;                                                            
COMPND   4 SYNONYM: HAGEMAN FACTOR,HAF;                                         
COMPND   5 EC: 3.4.21.38;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F12;                                                           
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227                                        
KEYWDS    HUMAN COAGULATION FACTOR XIIA, HYDROLASE, SERINE PROTEASE, BLOOD      
KEYWDS   2 CLOTTING                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PATHAK,J.EMSLEY                                                     
REVDAT   2   29-JUL-20 6GT6    1       COMPND REMARK HETNAM SSBOND              
REVDAT   2 2                   1       LINK   SITE   ATOM                       
REVDAT   1   17-JUL-19 6GT6    0                                                
JRNL        AUTH   M.PATHAK,R.MANNA,C.LI,B.G.KAIRA,B.K.HAMAD,B.D.BELVISO,       
JRNL        AUTH 2 C.R.BONTURI,I.DREVENY,P.M.FISCHER,L.V.DEKKER,M.L.V.OLIVA,    
JRNL        AUTH 3 J.EMSLEY                                                     
JRNL        TITL   CRYSTAL STRUCTURES OF THE RECOMBINANT BETA-FACTOR XIIA       
JRNL        TITL 2 PROTEASE WITH BOUND THR-ARG AND PRO-ARG SUBSTRATE MIMETICS.  
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  75   578 2019              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   31205020                                                     
JRNL        DOI    10.1107/S2059798319006910                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.54 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0222                                      
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) : 2.54                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12479                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 620                             
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) : 2.54                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 896                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 39                           
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1795                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 59                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.74000                                             
REMARK   3    B22 (A**2) : -1.74000                                             
REMARK   3    B33 (A**2) : 3.49000                                              
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): 0.343         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.266         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.252         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.596        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1905 ; 0.009 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  1623 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2604 ; 1.434 ; 1.683       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3812 ; 0.853 ; 1.661       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   235 ; 7.961 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    92 ;30.949 ;21.630       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   265 ;18.230 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;20.897 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   247 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2140 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   351 ; 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):  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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 6GT6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010427.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-18                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13130                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.540                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.61                     
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: 4XDE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS.CL PH 8.0, 1.5M AMSO4, VAPOR   
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 292.15K                        
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       32.98100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       53.46600            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       53.46600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       16.49050            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       53.46600            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       53.46600            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       49.47150            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       53.46600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.46600            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       16.49050            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       53.46600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.46600            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       49.47150            
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       32.98100            
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: 1140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA B   128                                                      
REMARK 465     ARG B   129                                                      
REMARK 465     GLN B   203A                                                     
REMARK 465     ALA B   203B                                                     
REMARK 465     ALA B   203C                                                     
REMARK 465     GLU B   203D                                                     
REMARK 465     ARG B   203E                                                     
REMARK 465     THR B   247                                                      
REMARK 465     GLY B   248                                                      
REMARK 465     HIS B   249                                                      
REMARK 465     HIS B   250                                                      
REMARK 465     HIS B   251                                                      
REMARK 465     HIS B   252                                                      
REMARK 465     HIS B   253                                                      
REMARK 465     HIS B   254                                                      
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    ASP B   109B    O    ASP B   109D             2.07            
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    ASP B 109B    -178.08    -68.52                                   
REMARK 500    CYS B 111     -154.72   -103.02                                   
REMARK 500    ALA B 112      124.96    -32.20                                   
REMARK 500    SER B 131       57.45   -161.03                                   
REMARK 500    THR B 133       50.27     70.20                                   
REMARK 500    SER B 153      -66.18    -92.66                                   
REMARK 500    VAL B 171      -77.33    -96.03                                   
REMARK 500    LEU B 181      136.38   -170.21                                   
REMARK 500    SER B 214      -78.73   -125.69                                   
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     CYS B  306                                                       
DBREF  6GT6 B   16   244  UNP    P00748   FA12_HUMAN     373    615             
SEQADV 6GT6 THR B  245  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 ARG B  246  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 THR B  247  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 GLY B  248  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 HIS B  249  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 HIS B  250  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 HIS B  251  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 HIS B  252  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 HIS B  253  UNP  P00748              EXPRESSION TAG                 
SEQADV 6GT6 HIS B  254  UNP  P00748              EXPRESSION TAG                 
SEQRES   1 B  253  VAL VAL GLY GLY LEU VAL ALA LEU ARG GLY ALA HIS PRO          
SEQRES   2 B  253  TYR ILE ALA ALA LEU TYR TRP GLY HIS SER PHE CYS ALA          
SEQRES   3 B  253  GLY SER LEU ILE ALA PRO CYS TRP VAL LEU THR ALA ALA          
SEQRES   4 B  253  HIS CYS LEU GLN ASP ARG PRO ALA PRO GLU ASP LEU THR          
SEQRES   5 B  253  VAL VAL LEU GLY GLN GLU ARG ARG ASN HIS SER CYS GLU          
SEQRES   6 B  253  PRO CYS GLN THR LEU ALA VAL ARG SER TYR ARG LEU HIS          
SEQRES   7 B  253  GLU ALA PHE SER PRO VAL SER TYR GLN HIS ASP LEU ALA          
SEQRES   8 B  253  LEU LEU ARG LEU GLN GLU ASP ALA ASP GLY SER CYS ALA          
SEQRES   9 B  253  LEU LEU SER PRO TYR VAL GLN PRO VAL CYS LEU PRO SER          
SEQRES  10 B  253  GLY ALA ALA ARG PRO SER GLU THR THR LEU CYS GLN VAL          
SEQRES  11 B  253  ALA GLY TRP GLY HIS GLN PHE GLU GLY ALA GLU GLU TYR          
SEQRES  12 B  253  ALA SER PHE LEU GLN GLU ALA GLN VAL PRO PHE LEU SER          
SEQRES  13 B  253  LEU GLU ARG CYS SER ALA PRO ASP VAL HIS GLY SER SER          
SEQRES  14 B  253  ILE LEU PRO GLY MET LEU CYS ALA GLY PHE LEU GLU GLY          
SEQRES  15 B  253  GLY THR ASP ALA CYS GLN GLY ASP SER GLY GLY PRO LEU          
SEQRES  16 B  253  VAL CYS GLU ASP GLN ALA ALA GLU ARG ARG LEU THR LEU          
SEQRES  17 B  253  GLN GLY ILE ILE SER TRP GLY SER GLY CYS GLY ASP ARG          
SEQRES  18 B  253  ASN LYS PRO GLY VAL TYR THR ASP VAL ALA TYR TYR LEU          
SEQRES  19 B  253  ALA TRP ILE ARG GLU HIS THR VAL SER THR ARG THR GLY          
SEQRES  20 B  253  HIS HIS HIS HIS HIS HIS                                      
HET    NAG  A   1      14                                                       
HET    NAG  A   2      14                                                       
HET    MAN  A   3      11                                                       
HET    GOL  B 304       6                                                       
HET    SO4  B 305       5                                                       
HET    CYS  B 306       6                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     CYS CYSTEINE                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   2  MAN    C6 H12 O6                                                    
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  CYS    C3 H7 N O2 S                                                 
FORMUL   6  HOH   *59(H2 O)                                                     
HELIX    1 AA1 ALA B   56  GLN B   60  5                                   5    
HELIX    2 AA2 ALA B   60D LEU B   64  5                                   5    
HELIX    3 AA3 SER B  164  SER B  169  1                                   6    
HELIX    4 AA4 HIS B  172  ILE B  176  5                                   5    
HELIX    5 AA5 TYR B  234  HIS B  241  1                                   8    
SHEET    1 AA1 8 LEU B  20  VAL B  21  0                                        
SHEET    2 AA1 8 GLN B 156  GLN B 159 -1  O  GLU B 157   N  LEU B  20           
SHEET    3 AA1 8 CYS B 136  GLY B 140 -1  N  VAL B 138   O  ALA B 158           
SHEET    4 AA1 8 PRO B 198  CYS B 201 -1  O  VAL B 200   N  GLN B 137           
SHEET    5 AA1 8 THR B 208  TRP B 215 -1  O  THR B 208   N  CYS B 201           
SHEET    6 AA1 8 GLY B 226  ASP B 230 -1  O  THR B 229   N  ILE B 212           
SHEET    7 AA1 8 MET B 180  ALA B 183 -1  N  LEU B 181   O  TYR B 228           
SHEET    8 AA1 8 PHE B 162  LEU B 163 -1  N  LEU B 163   O  CYS B 182           
SHEET    1 AA2 7 GLN B  81  LEU B  83  0                                        
SHEET    2 AA2 7 THR B  65  LEU B  68 -1  N  LEU B  68   O  GLN B  81           
SHEET    3 AA2 7 ILE B  30  TRP B  37 -1  N  TYR B  34   O  THR B  65           
SHEET    4 AA2 7 SER B  40  ALA B  48 -1  O  CYS B  42   N  LEU B  33           
SHEET    5 AA2 7 TRP B  51  THR B  54 -1  O  LEU B  53   N  SER B  45           
SHEET    6 AA2 7 ALA B 104  LEU B 108 -1  O  LEU B 106   N  VAL B  52           
SHEET    7 AA2 7 VAL B  85  LEU B  90 -1  N  ARG B  89   O  LEU B 105           
SSBOND   1 CYS B   42    CYS B   58                          1555   1555  2.04  
SSBOND   2 CYS B   50    CYS B  111                          1555   1555  1.93  
SSBOND   3 CYS B   77    CYS B   80                          1555   1555  2.12  
SSBOND   4 CYS B  122    CYS B  306                          1555   1555  1.99  
SSBOND   5 CYS B  136    CYS B  201                          1555   1555  2.08  
SSBOND   6 CYS B  168    CYS B  182                          1555   1555  2.01  
SSBOND   7 CYS B  191    CYS B  220                          1555   1555  2.04  
LINK         ND2 ASN B  74                 C1  NAG A   1     1555   1555  1.46  
LINK         O4  NAG A   1                 C1  NAG A   2     1555   1555  1.47  
LINK         O4  NAG A   2                 C1  MAN A   3     1555   1555  1.47  
CRYST1  106.932  106.932   65.962  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      0.009352  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009352  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015160        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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