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Database: PDB
Entry: 2GUG
LinkDB: 2GUG
Original site: 2GUG 
HEADER    OXIDOREDUCTASE                          30-APR-06   2GUG              
TITLE     NAD-DEPENDENT FORMATE DEHYDROGENASE FROM PSEUDOMONAS SP.101 IN COMPLEX
TITLE    2 WITH FORMATE                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FORMATE DEHYDROGENASE;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: NAD-DEPENDENT FORMATE DEHYDROGENASE, FDH;                   
COMPND   5 EC: 1.2.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;                                
SOURCE   3 ORGANISM_TAXID: 33067;                                               
SOURCE   4 STRAIN: 101;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPSFDH8A                                  
KEYWDS    OXIDOREDUCTASE (ALDEHUDE (D), NAD+(A)), OXIDOREDUCTASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.V.FILIPPOVA,K.M.POLYAKOV,T.V.TIKHONOVA,K.M.BOIKO,V.I.TISHKOV,       
AUTHOR   2 V.O.POPOV                                                            
REVDAT   3   13-JUL-11 2GUG    1       VERSN                                    
REVDAT   2   24-FEB-09 2GUG    1       VERSN                                    
REVDAT   1   16-MAY-06 2GUG    0                                                
JRNL        AUTH   E.V.FILIPPOVA,K.M.POLYAKOV,T.V.TIKHONOVA,T.N.STEKHANOVA,     
JRNL        AUTH 2 K.M.BOIKO,I.G.SADIHOV,V.I.TISHKOV,N.LABROU,V.O.POPOV         
JRNL        TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF NAD-DEPENDENT FORMATE    
JRNL        TITL 2 DEHYDROGENASE FROM METYLOTROPHIC BACTERIUM PSEUDOMONAS       
JRNL        TITL 3 SP.101 WITH FORMATE.                                         
JRNL        REF    KRISTALLOGRAFIYA              V.  51   663 2006              
JRNL        REFN                   ISSN 0023-4761                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 69594                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3696                            
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) : 2.28                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4880                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 244                          
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11504                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 77                                      
REMARK   3   SOLVENT ATOMS            : 389                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.56000                                             
REMARK   3    B22 (A**2) : 4.58000                                              
REMARK   3    B33 (A**2) : -1.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.341         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.261         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.194         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.933         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11883 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16170 ; 1.862 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1462 ; 7.363 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   534 ;38.671 ;23.127       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1892 ;17.353 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    95 ;18.227 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1795 ; 0.126 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9065 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6206 ; 0.234 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8069 ; 0.316 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   695 ; 0.163 ; 0.200       
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):    82 ; 0.305 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.242 ; 0.200       
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):  7519 ; 1.052 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11854 ; 1.769 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4992 ; 2.729 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4316 ; 3.982 ; 4.500       
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 : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 2GUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037563.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
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) : 0.8019                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARHKL, DENZO                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73290                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.280                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: MOLREP                       
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2NAC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8% PEG400, 2M NA FORMATE, 0.1M         
REMARK 280  HEPES, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       27.49000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 9680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     MET A     0                                                      
REMARK 465     LEU A   257                                                      
REMARK 465     HIS A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLU A   260                                                      
REMARK 465     THR A   261                                                      
REMARK 465     GLU A   262                                                      
REMARK 465     GLY A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     ALA A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     SER A   380                                                      
REMARK 465     TYR A   381                                                      
REMARK 465     SER A   382                                                      
REMARK 465     LYS A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     ASN A   385                                                      
REMARK 465     ALA A   386                                                      
REMARK 465     THR A   387                                                      
REMARK 465     GLY A   388                                                      
REMARK 465     GLY A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     GLU A   392                                                      
REMARK 465     ALA A   393                                                      
REMARK 465     ALA A   394                                                      
REMARK 465     LYS A   395                                                      
REMARK 465     PHE A   396                                                      
REMARK 465     LYS A   397                                                      
REMARK 465     LYS A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     VAL A   400                                                      
REMARK 465     MET B     0                                                      
REMARK 465     GLY B   370                                                      
REMARK 465     GLY B   371                                                      
REMARK 465     ALA B   372                                                      
REMARK 465     LEU B   373                                                      
REMARK 465     ALA B   374                                                      
REMARK 465     GLY B   375                                                      
REMARK 465     THR B   376                                                      
REMARK 465     GLY B   377                                                      
REMARK 465     ALA B   378                                                      
REMARK 465     HIS B   379                                                      
REMARK 465     SER B   380                                                      
REMARK 465     TYR B   381                                                      
REMARK 465     SER B   382                                                      
REMARK 465     LYS B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     ASN B   385                                                      
REMARK 465     ALA B   386                                                      
REMARK 465     THR B   387                                                      
REMARK 465     GLY B   388                                                      
REMARK 465     GLY B   389                                                      
REMARK 465     SER B   390                                                      
REMARK 465     GLU B   391                                                      
REMARK 465     GLU B   392                                                      
REMARK 465     ALA B   393                                                      
REMARK 465     ALA B   394                                                      
REMARK 465     LYS B   395                                                      
REMARK 465     PHE B   396                                                      
REMARK 465     LYS B   397                                                      
REMARK 465     LYS B   398                                                      
REMARK 465     ALA B   399                                                      
REMARK 465     VAL B   400                                                      
REMARK 465     MET C     0                                                      
REMARK 465     GLY C   370                                                      
REMARK 465     GLY C   371                                                      
REMARK 465     ALA C   372                                                      
REMARK 465     LEU C   373                                                      
REMARK 465     ALA C   374                                                      
REMARK 465     GLY C   375                                                      
REMARK 465     THR C   376                                                      
REMARK 465     GLY C   377                                                      
REMARK 465     ALA C   378                                                      
REMARK 465     HIS C   379                                                      
REMARK 465     SER C   380                                                      
REMARK 465     TYR C   381                                                      
REMARK 465     SER C   382                                                      
REMARK 465     LYS C   383                                                      
REMARK 465     GLY C   384                                                      
REMARK 465     ASN C   385                                                      
REMARK 465     ALA C   386                                                      
REMARK 465     THR C   387                                                      
REMARK 465     GLY C   388                                                      
REMARK 465     GLY C   389                                                      
REMARK 465     SER C   390                                                      
REMARK 465     GLU C   391                                                      
REMARK 465     GLU C   392                                                      
REMARK 465     ALA C   393                                                      
REMARK 465     ALA C   394                                                      
REMARK 465     LYS C   395                                                      
REMARK 465     PHE C   396                                                      
REMARK 465     LYS C   397                                                      
REMARK 465     LYS C   398                                                      
REMARK 465     ALA C   399                                                      
REMARK 465     VAL C   400                                                      
REMARK 465     MET D     0                                                      
REMARK 465     LEU D   257                                                      
REMARK 465     HIS D   258                                                      
REMARK 465     PRO D   259                                                      
REMARK 465     GLU D   260                                                      
REMARK 465     THR D   261                                                      
REMARK 465     GLU D   262                                                      
REMARK 465     HIS D   263                                                      
REMARK 465     GLY D   370                                                      
REMARK 465     GLY D   371                                                      
REMARK 465     ALA D   372                                                      
REMARK 465     LEU D   373                                                      
REMARK 465     ALA D   374                                                      
REMARK 465     GLY D   375                                                      
REMARK 465     THR D   376                                                      
REMARK 465     GLY D   377                                                      
REMARK 465     ALA D   378                                                      
REMARK 465     HIS D   379                                                      
REMARK 465     SER D   380                                                      
REMARK 465     TYR D   381                                                      
REMARK 465     SER D   382                                                      
REMARK 465     LYS D   383                                                      
REMARK 465     GLY D   384                                                      
REMARK 465     ASN D   385                                                      
REMARK 465     ALA D   386                                                      
REMARK 465     THR D   387                                                      
REMARK 465     GLY D   388                                                      
REMARK 465     GLY D   389                                                      
REMARK 465     SER D   390                                                      
REMARK 465     GLU D   391                                                      
REMARK 465     GLU D   392                                                      
REMARK 465     ALA D   393                                                      
REMARK 465     ALA D   394                                                      
REMARK 465     LYS D   395                                                      
REMARK 465     PHE D   396                                                      
REMARK 465     LYS D   397                                                      
REMARK 465     LYS D   398                                                      
REMARK 465     ALA D   399                                                      
REMARK 465     VAL D   400                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG D 343   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  23     -178.77   -171.91                                   
REMARK 500    PRO A  31      117.18    -39.68                                   
REMARK 500    LEU A  57       21.01     45.75                                   
REMARK 500    VAL A  88      -39.54    -36.80                                   
REMARK 500    TRP A  99       72.64   -156.99                                   
REMARK 500    SER A 124       21.46   -150.85                                   
REMARK 500    TYR A 144      -10.33     70.09                                   
REMARK 500    TRP A 177      -68.39   -145.68                                   
REMARK 500    ALA A 191       -0.77     69.44                                   
REMARK 500    ALA A 198      139.63     77.61                                   
REMARK 500    GLU A 242      -33.32    -34.97                                   
REMARK 500    CYS A 255      -58.04      5.14                                   
REMARK 500    ALA A 283      -74.64    -91.43                                   
REMARK 500    LYS A 317      -32.75    -29.47                                   
REMARK 500    ILE A 333       -7.90   -149.18                                   
REMARK 500    LEU B  57       19.34     49.79                                   
REMARK 500    TRP B  99       68.02   -156.29                                   
REMARK 500    LEU B 103       67.13   -103.68                                   
REMARK 500    SER B 124       37.82   -150.77                                   
REMARK 500    ASN B 146       17.80   -140.89                                   
REMARK 500    TRP B 177      -68.12   -139.76                                   
REMARK 500    ALA B 191       -1.19     62.81                                   
REMARK 500    ALA B 198      126.82     76.99                                   
REMARK 500    ARG B 224      160.17    -49.20                                   
REMARK 500    ALA B 283      -82.93    -87.81                                   
REMARK 500    PRO B 331      177.10    -58.54                                   
REMARK 500    GLU C  56       18.91     57.80                                   
REMARK 500    LEU C  57       19.14     55.78                                   
REMARK 500    TRP C  99       69.41   -161.04                                   
REMARK 500    LEU C 103       78.51   -105.42                                   
REMARK 500    ALA C 111       71.46    -67.79                                   
REMARK 500    SER C 124       28.99   -153.35                                   
REMARK 500    TYR C 144       -2.81     65.02                                   
REMARK 500    TRP C 177      -73.08   -142.68                                   
REMARK 500    GLU C 190      126.25    -37.12                                   
REMARK 500    ALA C 198      133.56     78.77                                   
REMARK 500    PRO C 259       94.47    -58.90                                   
REMARK 500    GLU C 260      -50.29    155.06                                   
REMARK 500    ALA C 283      -81.74    -88.85                                   
REMARK 500    ARG C 295      -71.31    -35.20                                   
REMARK 500    LYS C 317      -39.65    -34.71                                   
REMARK 500    ILE C 333       -4.21   -141.09                                   
REMARK 500    ARG C 362      138.24    -36.95                                   
REMARK 500    LEU D  57       19.01     50.32                                   
REMARK 500    ASP D  75       91.69    -66.99                                   
REMARK 500    TRP D  99       76.19   -162.29                                   
REMARK 500    SER D 124       33.58   -163.24                                   
REMARK 500    THR D 143      134.47    -33.96                                   
REMARK 500    TYR D 144       -2.52     75.17                                   
REMARK 500    TRP D 177      -68.52   -147.90                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    CYS A 255        20.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 344        23.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR C 344        22.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 565        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH A 570        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH B 520        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH B 539        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH B 545        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B 558        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH B 567        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B 583        DISTANCE =  7.42 ANGSTROMS                       
REMARK 525    HOH B 587        DISTANCE =  9.74 ANGSTROMS                       
REMARK 525    HOH C 484        DISTANCE =  8.12 ANGSTROMS                       
REMARK 525    HOH C 516        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH C 525        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH C 529        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH C 570        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH D 535        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH D 546        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH D 551        DISTANCE =  7.55 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 483                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NAC   RELATED DB: PDB                                   
REMARK 900 APO-FORM                                                             
REMARK 900 RELATED ID: 2NAD   RELATED DB: PDB                                   
REMARK 900 COMPLEX WITH NAD AND AZIDE                                           
DBREF  2GUG A    0   400  UNP    P33160   FDH_PSESR        0    400             
DBREF  2GUG B    0   400  UNP    P33160   FDH_PSESR        0    400             
DBREF  2GUG C    0   400  UNP    P33160   FDH_PSESR        0    400             
DBREF  2GUG D    0   400  UNP    P33160   FDH_PSESR        0    400             
SEQADV 2GUG OCS A  354  UNP  P33160    CYS   354 MODIFIED RESIDUE               
SEQADV 2GUG OCS B  354  UNP  P33160    CYS   354 MODIFIED RESIDUE               
SEQADV 2GUG OCS C  354  UNP  P33160    CYS   354 MODIFIED RESIDUE               
SEQADV 2GUG OCS D  354  UNP  P33160    CYS   354 MODIFIED RESIDUE               
SEQRES   1 A  401  MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL          
SEQRES   2 A  401  ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO          
SEQRES   3 A  401  LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR          
SEQRES   4 A  401  PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY          
SEQRES   5 A  401  SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU          
SEQRES   6 A  401  SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP          
SEQRES   7 A  401  GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA          
SEQRES   8 A  401  ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU          
SEQRES   9 A  401  THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU          
SEQRES  10 A  401  ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU          
SEQRES  11 A  401  GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL          
SEQRES  12 A  401  THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL          
SEQRES  13 A  401  MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER          
SEQRES  14 A  401  HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP          
SEQRES  15 A  401  CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL          
SEQRES  16 A  401  GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU          
SEQRES  17 A  401  ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR          
SEQRES  18 A  401  ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU          
SEQRES  19 A  401  ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO          
SEQRES  20 A  401  VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO          
SEQRES  21 A  401  GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU          
SEQRES  22 A  401  PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY          
SEQRES  23 A  401  LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU          
SEQRES  24 A  401  SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE          
SEQRES  25 A  401  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET          
SEQRES  26 A  401  PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR          
SEQRES  27 A  401  LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU          
SEQRES  28 A  401  ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP          
SEQRES  29 A  401  GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR          
SEQRES  30 A  401  GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY          
SEQRES  31 A  401  SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL                  
SEQRES   1 B  401  MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL          
SEQRES   2 B  401  ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO          
SEQRES   3 B  401  LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR          
SEQRES   4 B  401  PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY          
SEQRES   5 B  401  SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU          
SEQRES   6 B  401  SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP          
SEQRES   7 B  401  GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA          
SEQRES   8 B  401  ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU          
SEQRES   9 B  401  THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU          
SEQRES  10 B  401  ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU          
SEQRES  11 B  401  GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL          
SEQRES  12 B  401  THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL          
SEQRES  13 B  401  MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER          
SEQRES  14 B  401  HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP          
SEQRES  15 B  401  CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL          
SEQRES  16 B  401  GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU          
SEQRES  17 B  401  ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR          
SEQRES  18 B  401  ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU          
SEQRES  19 B  401  ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO          
SEQRES  20 B  401  VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO          
SEQRES  21 B  401  GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU          
SEQRES  22 B  401  PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY          
SEQRES  23 B  401  LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU          
SEQRES  24 B  401  SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE          
SEQRES  25 B  401  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET          
SEQRES  26 B  401  PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR          
SEQRES  27 B  401  LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU          
SEQRES  28 B  401  ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP          
SEQRES  29 B  401  GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR          
SEQRES  30 B  401  GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY          
SEQRES  31 B  401  SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL                  
SEQRES   1 C  401  MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL          
SEQRES   2 C  401  ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO          
SEQRES   3 C  401  LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR          
SEQRES   4 C  401  PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY          
SEQRES   5 C  401  SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU          
SEQRES   6 C  401  SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP          
SEQRES   7 C  401  GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA          
SEQRES   8 C  401  ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU          
SEQRES   9 C  401  THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU          
SEQRES  10 C  401  ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU          
SEQRES  11 C  401  GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL          
SEQRES  12 C  401  THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL          
SEQRES  13 C  401  MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER          
SEQRES  14 C  401  HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP          
SEQRES  15 C  401  CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL          
SEQRES  16 C  401  GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU          
SEQRES  17 C  401  ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR          
SEQRES  18 C  401  ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU          
SEQRES  19 C  401  ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO          
SEQRES  20 C  401  VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO          
SEQRES  21 C  401  GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU          
SEQRES  22 C  401  PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY          
SEQRES  23 C  401  LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU          
SEQRES  24 C  401  SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE          
SEQRES  25 C  401  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET          
SEQRES  26 C  401  PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR          
SEQRES  27 C  401  LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU          
SEQRES  28 C  401  ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP          
SEQRES  29 C  401  GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR          
SEQRES  30 C  401  GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY          
SEQRES  31 C  401  SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL                  
SEQRES   1 D  401  MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL          
SEQRES   2 D  401  ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO          
SEQRES   3 D  401  LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR          
SEQRES   4 D  401  PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY          
SEQRES   5 D  401  SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU          
SEQRES   6 D  401  SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP          
SEQRES   7 D  401  GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA          
SEQRES   8 D  401  ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU          
SEQRES   9 D  401  THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU          
SEQRES  10 D  401  ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU          
SEQRES  11 D  401  GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL          
SEQRES  12 D  401  THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL          
SEQRES  13 D  401  MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER          
SEQRES  14 D  401  HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP          
SEQRES  15 D  401  CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL          
SEQRES  16 D  401  GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU          
SEQRES  17 D  401  ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR          
SEQRES  18 D  401  ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU          
SEQRES  19 D  401  ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO          
SEQRES  20 D  401  VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO          
SEQRES  21 D  401  GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU          
SEQRES  22 D  401  PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY          
SEQRES  23 D  401  LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU          
SEQRES  24 D  401  SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE          
SEQRES  25 D  401  PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET          
SEQRES  26 D  401  PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR          
SEQRES  27 D  401  LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU          
SEQRES  28 D  401  ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP          
SEQRES  29 D  401  GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR          
SEQRES  30 D  401  GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY          
SEQRES  31 D  401  SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL                  
MODRES 2GUG OCS A  354  CYS  CYSTEINESULFONIC ACID                              
MODRES 2GUG OCS B  354  CYS  CYSTEINESULFONIC ACID                              
MODRES 2GUG OCS C  354  CYS  CYSTEINESULFONIC ACID                              
MODRES 2GUG OCS D  354  CYS  CYSTEINESULFONIC ACID                              
HET    OCS  A 354       9                                                       
HET    OCS  B 354       9                                                       
HET    OCS  C 354       9                                                       
HET    OCS  D 354       9                                                       
HET    PG4  A 478      13                                                       
HET    PG4  D 480      13                                                       
HET    FMT  A 479       3                                                       
HET    FMT  B 401       3                                                       
HET    FMT  C 401       3                                                       
HET    PEG  A 476       7                                                       
HET    PEG  A 477       7                                                       
HET    PEG  A 480       7                                                       
HET    PEG  B 481       7                                                       
HET    PEG  C 482       7                                                       
HET    PEG  C 483       7                                                       
HETNAM     OCS CYSTEINESULFONIC ACID                                            
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     FMT FORMIC ACID                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   1  OCS    4(C3 H7 N O5 S)                                              
FORMUL   5  PG4    2(C8 H18 O5)                                                 
FORMUL   7  FMT    3(C H2 O2)                                                   
FORMUL  10  PEG    6(C4 H10 O3)                                                 
FORMUL  16  HOH   *389(H2 O)                                                    
HELIX    1   1 GLY A   55  GLY A   58  5                                   4    
HELIX    2   2 LEU A   59  ASN A   66  1                                   8    
HELIX    3   3 SER A   81  VAL A   88  1                                   8    
HELIX    4   4 THR A  104  ALA A  111  1                                   8    
HELIX    5   5 ASP A  128  ARG A  135  1                                   8    
HELIX    6   6 ASN A  146  ASN A  164  1                                  19    
HELIX    7   7 ASN A  164  LYS A  174  1                                  11    
HELIX    8   8 ASN A  178  SER A  184  1                                   7    
HELIX    9   9 GLY A  200  ALA A  211  1                                  12    
HELIX   10  10 PRO A  212  ASP A  214  5                                   3    
HELIX   11  11 PRO A  226  LEU A  233  1                                   8    
HELIX   12  12 THR A  240  TYR A  245  1                                   6    
HELIX   13  13 PRO A  246  CYS A  248  5                                   3    
HELIX   14  14 GLU A  268  PHE A  273  5                                   6    
HELIX   15  15 ARG A  284  CYS A  288  5                                   5    
HELIX   16  16 ASP A  289  SER A  299  1                                  11    
HELIX   17  17 HIS A  319  THR A  323  5                                   5    
HELIX   18  18 THR A  337  GLU A  357  1                                  21    
HELIX   19  19 ARG A  362  GLU A  364  5                                   3    
HELIX   20  20 SER B   52  GLY B   58  5                                   7    
HELIX   21  21 LEU B   59  SER B   65  1                                   7    
HELIX   22  22 SER B   81  VAL B   88  1                                   8    
HELIX   23  23 THR B  104  ALA B  111  1                                   8    
HELIX   24  24 ASP B  128  ARG B  135  1                                   8    
HELIX   25  25 ASN B  146  ARG B  163  1                                  18    
HELIX   26  26 ASN B  164  LYS B  174  1                                  11    
HELIX   27  27 ASN B  178  SER B  184  1                                   7    
HELIX   28  28 GLY B  200  ALA B  211  1                                  12    
HELIX   29  29 PRO B  212  ASP B  214  5                                   3    
HELIX   30  30 PRO B  226  ASN B  234  1                                   9    
HELIX   31  31 THR B  240  TYR B  245  1                                   6    
HELIX   32  32 PRO B  246  CYS B  248  5                                   3    
HELIX   33  33 ASN B  266  LYS B  271  1                                   6    
HELIX   34  34 ARG B  284  CYS B  288  5                                   5    
HELIX   35  35 ASP B  289  GLY B  300  1                                  12    
HELIX   36  36 HIS B  319  THR B  323  5                                   5    
HELIX   37  37 THR B  337  GLY B  358  1                                  22    
HELIX   38  38 GLY C   55  GLY C   58  5                                   4    
HELIX   39  39 LEU C   59  ASN C   66  1                                   8    
HELIX   40  40 SER C   81  VAL C   88  1                                   8    
HELIX   41  41 THR C  104  ALA C  111  1                                   8    
HELIX   42  42 ASP C  128  ARG C  135  1                                   8    
HELIX   43  43 ASN C  146  ARG C  163  1                                  18    
HELIX   44  44 ASN C  164  LYS C  174  1                                  11    
HELIX   45  45 ASN C  178  SER C  184  1                                   7    
HELIX   46  46 GLY C  200  ALA C  211  1                                  12    
HELIX   47  47 PRO C  212  ASP C  214  5                                   3    
HELIX   48  48 PRO C  226  ASN C  234  1                                   9    
HELIX   49  49 THR C  240  TYR C  245  1                                   6    
HELIX   50  50 PRO C  246  CYS C  248  5                                   3    
HELIX   51  51 GLU C  268  PHE C  273  5                                   6    
HELIX   52  52 ARG C  284  CYS C  288  5                                   5    
HELIX   53  53 ASP C  289  SER C  299  1                                  11    
HELIX   54  54 THR C  337  GLU C  357  1                                  21    
HELIX   55  55 GLY D   55  GLY D   58  5                                   4    
HELIX   56  56 LEU D   59  SER D   65  1                                   7    
HELIX   57  57 SER D   81  VAL D   88  1                                   8    
HELIX   58  58 THR D  104  ALA D  111  1                                   8    
HELIX   59  59 ASP D  128  ARG D  135  1                                   8    
HELIX   60  60 ASN D  146  ASN D  164  1                                  19    
HELIX   61  61 ASN D  164  LYS D  174  1                                  11    
HELIX   62  62 ASN D  178  SER D  184  1                                   7    
HELIX   63  63 GLY D  200  ALA D  211  1                                  12    
HELIX   64  64 PRO D  212  ASP D  214  5                                   3    
HELIX   65  65 PRO D  226  LEU D  233  1                                   8    
HELIX   66  66 THR D  240  TYR D  245  1                                   6    
HELIX   67  67 PRO D  246  CYS D  248  5                                   3    
HELIX   68  68 ASN D  266  LYS D  271  1                                   6    
HELIX   69  69 ARG D  284  CYS D  288  5                                   5    
HELIX   70  70 ASP D  289  GLY D  300  1                                  12    
HELIX   71  71 HIS D  319  THR D  323  5                                   5    
HELIX   72  72 THR D  337  GLU D  357  1                                  21    
HELIX   73  73 ARG D  362  GLU D  364  5                                   3    
SHEET    1   A 7 THR A  69  THR A  73  0                                        
SHEET    2   A 7 LYS A   2  VAL A   6  1  N  CYS A   5   O  VAL A  71           
SHEET    3   A 7 VAL A  92  SER A  95  1  O  VAL A  92   N  LEU A   4           
SHEET    4   A 7 LEU A 116  THR A 119  1  O  LEU A 118   N  VAL A  93           
SHEET    5   A 7 THR A 138  GLU A 141  1  O  ALA A 140   N  THR A 119           
SHEET    6   A 7 LEU A 366  GLN A 369 -1  O  ILE A 367   N  VAL A 139           
SHEET    7   A 7 ALA A 372  LEU A 373 -1  O  ALA A 372   N  GLN A 369           
SHEET    1   B 6 THR A 236  HIS A 238  0                                        
SHEET    2   B 6 HIS A 216  THR A 220  1  N  LEU A 217   O  THR A 236           
SHEET    3   B 6 HIS A 193  VAL A 197  1  N  VAL A 194   O  HIS A 218           
SHEET    4   B 6 VAL A 250  LEU A 253  1  O  VAL A 250   N  GLY A 195           
SHEET    5   B 6 ALA A 277  ASN A 281  1  O  TYR A 278   N  VAL A 251           
SHEET    6   B 6 LEU A 302  GLY A 307  1  O  ALA A 306   N  ASN A 281           
SHEET    1   C 6 THR B  69  THR B  73  0                                        
SHEET    2   C 6 LYS B   2  VAL B   6  1  N  CYS B   5   O  VAL B  71           
SHEET    3   C 6 VAL B  92  SER B  95  1  O  ILE B  94   N  VAL B   6           
SHEET    4   C 6 LEU B 116  THR B 119  1  O  LEU B 118   N  VAL B  93           
SHEET    5   C 6 THR B 138  GLU B 141  1  O  THR B 138   N  ALA B 117           
SHEET    6   C 6 LEU B 366  VAL B 368 -1  O  VAL B 368   N  VAL B 139           
SHEET    1   D 6 THR B 236  TRP B 237  0                                        
SHEET    2   D 6 HIS B 216  THR B 220  1  N  LEU B 217   O  THR B 236           
SHEET    3   D 6 HIS B 193  VAL B 197  1  N  VAL B 194   O  HIS B 218           
SHEET    4   D 6 VAL B 250  LEU B 253  1  O  VAL B 250   N  GLY B 195           
SHEET    5   D 6 TYR B 278  ASN B 281  1  O  VAL B 280   N  LEU B 253           
SHEET    6   D 6 GLY B 304  ALA B 306  1  O  ALA B 306   N  ASN B 281           
SHEET    1   E 6 THR C  69  THR C  73  0                                        
SHEET    2   E 6 LYS C   2  VAL C   6  1  N  VAL C   3   O  VAL C  71           
SHEET    3   E 6 VAL C  92  SER C  95  1  O  ILE C  94   N  VAL C   6           
SHEET    4   E 6 LEU C 116  THR C 119  1  O  LEU C 118   N  VAL C  93           
SHEET    5   E 6 THR C 138  GLU C 141  1  O  THR C 138   N  ALA C 117           
SHEET    6   E 6 LEU C 366  VAL C 368 -1  O  ILE C 367   N  VAL C 139           
SHEET    1   F 6 THR C 236  TRP C 237  0                                        
SHEET    2   F 6 HIS C 216  THR C 220  1  N  TYR C 219   O  THR C 236           
SHEET    3   F 6 HIS C 193  VAL C 197  1  N  VAL C 194   O  HIS C 218           
SHEET    4   F 6 VAL C 250  LEU C 253  1  O  VAL C 250   N  GLY C 195           
SHEET    5   F 6 ALA C 277  ASN C 281  1  O  VAL C 280   N  VAL C 251           
SHEET    6   F 6 LEU C 302  GLY C 307  1  O  ALA C 306   N  ASN C 281           
SHEET    1   G 6 THR D  69  THR D  73  0                                        
SHEET    2   G 6 LYS D   2  VAL D   6  1  N  CYS D   5   O  VAL D  71           
SHEET    3   G 6 VAL D  92  SER D  95  1  O  ILE D  94   N  LEU D   4           
SHEET    4   G 6 LEU D 116  THR D 119  1  O  LEU D 118   N  VAL D  93           
SHEET    5   G 6 THR D 138  GLU D 141  1  O  ALA D 140   N  THR D 119           
SHEET    6   G 6 LEU D 366  VAL D 368 -1  O  VAL D 368   N  VAL D 139           
SHEET    1   H 6 THR D 236  TRP D 237  0                                        
SHEET    2   H 6 HIS D 216  THR D 220  1  N  TYR D 219   O  THR D 236           
SHEET    3   H 6 HIS D 193  VAL D 197  1  N  VAL D 194   O  HIS D 216           
SHEET    4   H 6 VAL D 250  LEU D 253  1  O  VAL D 250   N  GLY D 195           
SHEET    5   H 6 ALA D 277  ASN D 281  1  O  TYR D 278   N  VAL D 251           
SHEET    6   H 6 LEU D 302  GLY D 307  1  O  ALA D 306   N  ASN D 281           
LINK         C   GLU A 353                 N   OCS A 354     1555   1555  1.32  
LINK         C   OCS A 354                 N   PHE A 355     1555   1555  1.32  
LINK         C   GLU B 353                 N   OCS B 354     1555   1555  1.31  
LINK         C   OCS B 354                 N   PHE B 355     1555   1555  1.33  
LINK         C   GLU C 353                 N   OCS C 354     1555   1555  1.33  
LINK         C   OCS C 354                 N   PHE C 355     1555   1555  1.34  
LINK         C   GLU D 353                 N   OCS D 354     1555   1555  1.34  
LINK         C   OCS D 354                 N   PHE D 355     1555   1555  1.33  
CISPEP   1 HIS A  263    MET A  264          0        15.83                     
CISPEP   2 PHE A  311    PRO A  312          0        -3.82                     
CISPEP   3 GLN A  313    PRO A  314          0        -2.58                     
CISPEP   4 PHE B  311    PRO B  312          0         2.35                     
CISPEP   5 GLN B  313    PRO B  314          0        -3.86                     
CISPEP   6 PHE C  311    PRO C  312          0        -9.72                     
CISPEP   7 GLN C  313    PRO C  314          0        -5.50                     
CISPEP   8 PHE D  311    PRO D  312          0       -16.33                     
CISPEP   9 GLN D  313    PRO D  314          0         4.02                     
SITE     1 AC1  6 SER A 184  PEG A 480  HOH A 526  ASP C  13                    
SITE     2 AC1  6 THR C  18  TYR C  19                                          
SITE     1 AC2  6 THR B  18  SER D 184  HIS D 185  GLU D 298                    
SITE     2 AC2  6 TYR D 326  HOH D 550                                          
SITE     1 AC3  7 PRO A  97  PHE A  98  GLY A 121  ILE A 122                    
SITE     2 AC3  7 ASN A 146  PEG A 476  HOH A 587                               
SITE     1 AC4  5 PRO B  97  PHE B  98  ILE B 122  ASN B 146                    
SITE     2 AC4  5 HOH B 499                                                     
SITE     1 AC5  6 PRO C  97  PHE C  98  GLY C 121  ILE C 122                    
SITE     2 AC5  6 ASN C 146  HOH C 531                                          
SITE     1 AC6  8 ILE A 122  ASN A 146  SER A 147  VAL A 150                    
SITE     2 AC6  8 ILE A 202  THR A 282  FMT A 479  HOH A 554                    
SITE     1 AC7  8 PRO A  31  TYR A 144  ARG A 201  ALA A 205                    
SITE     2 AC7  8 ARG A 208  ARG A 209  GLU C 190  ASP C 214                    
SITE     1 AC8  3 GLU A 298  TYR A 326  PG4 A 478                               
SITE     1 AC9  1 LEU B 204                                                     
SITE     1 BC1  2 ALA C 199  GLY C 200                                          
SITE     1 BC2  2 GLU C 298  TYR C 326                                          
CRYST1  117.000   54.980  128.910  90.00  95.74  90.00 P 1 21 1      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      0.008547  0.000000  0.000859        0.00000                         
SCALE2      0.000000  0.018188  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007796        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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