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Database: PDB
Entry: 2JGD
LinkDB: 2JGD
Original site: 2JGD 
HEADER    OXIDOREDUCTASE                          12-FEB-07   2JGD              
TITLE     E. COLI 2-OXOGLUTARATE DEHYDROGENASE (E1O)                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA- KETOGLUTARATE DEHYDROGENASE;                         
COMPND   5 EC: 1.2.4.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT;                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: ALPHA- KETOGLUTARATE DEHYDROGENASE;                         
COMPND  11 EC: 1.2.4.2;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 83333;                                               
SOURCE  12 STRAIN: K12;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    2-OXOGLUTARATE DEHYDROGENASE, FLAVOPROTEIN, OXIDOREDUCTASE,           
KEYWDS   2 THIAMINE DIPHOSPHATE, THIAMINE PYROPHOSPHATE, ADENOSINE              
KEYWDS   3 MONOPHOSPHATE, E1O, KGDH, OGDH, GLYCOLYSIS, OXALOACETATE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.W.FRANK,A.J.PRICE,F.D.NORTHROP,R.N.PERHAM,B.F.LUISI               
REVDAT   4   24-FEB-09 2JGD    1       VERSN                                    
REVDAT   3   17-APR-07 2JGD    1       JRNL                                     
REVDAT   2   03-APR-07 2JGD    1       JRNL                                     
REVDAT   1   27-FEB-07 2JGD    0                                                
JRNL        AUTH   R.A.W.FRANK,A.J.PRICE,F.D.NORTHROP,R.N.PERHAM,               
JRNL        AUTH 2 B.F.LUISI                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE E1 COMPONENT OF THE                 
JRNL        TITL 2 ESCHERICHIA COLI 2-OXOGLUTARATE DEHYDROGENASE                
JRNL        TITL 3 MULTIENZYME COMPLEX.                                         
JRNL        REF    J.MOL.BIOL.                   V. 368   639 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17367808                                                     
JRNL        DOI    10.1016/J.JMB.2007.01.080                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.6  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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 76341                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4041                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5422                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 290                          
REMARK   3   BIN FREE R VALUE                    : 0.3990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12593                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 735                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
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): 0.376         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.276         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12931 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17527 ; 1.079 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1611 ; 9.894 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   618 ;36.348 ;23.738       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2086 ;19.587 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    93 ;21.838 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1906 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9959 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6181 ; 0.259 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8807 ; 0.333 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   723 ; 0.234 ; 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):    31 ; 0.300 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.224 ; 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):  8041 ; 8.388 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12864 ;10.148 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4890 ;15.484 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4659 ;16.373 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     84       A     933      1                      
REMARK   3           1     B     84       B     933      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   6112 ;  0.48 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   6112 ;  2.13 ;  0.50           
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   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2JGD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-FEB-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-31427.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.939272                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80455                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: SELENIUM SITES WERE FOUND WITH MAD DATA IN SHELXD.           
REMARK 200  PHASES WERE DETERMINED WITH SAD DATA IN PHASER                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 63.67                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP: 1UL 12% PEG 4000,          
REMARK 280  50MM SOCIUM CITRATE PH5.6. 1UL 10MG/ML TE1O. RESERVOIR:             
REMARK 280  1UL 12% PEG 4000, 50MM SOCIUM CITRATE PH5.6.                        
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      125.90550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       71.24650            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       71.24650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.95275            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       71.24650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       71.24650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      188.85825            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       71.24650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.24650            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       62.95275            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       71.24650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.24650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      188.85825            
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      125.90550            
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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     TRP A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     TYR A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     GLN A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     TRP A    22                                                      
REMARK 465     ILE A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     TYR A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     ASP A    29                                                      
REMARK 465     PHE A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     ASP A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     VAL A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     ALA A    39                                                      
REMARK 465     ASN A    40                                                      
REMARK 465     TRP A    41                                                      
REMARK 465     ARG A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     PHE A    45                                                      
REMARK 465     GLN A    46                                                      
REMARK 465     GLN A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     PRO A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     THR A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     VAL A    53                                                      
REMARK 465     LYS A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     ASP A    56                                                      
REMARK 465     GLN A    57                                                      
REMARK 465     PHE A    58                                                      
REMARK 465     HIS A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     GLN A    61                                                      
REMARK 465     THR A    62                                                      
REMARK 465     ARG A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     TYR A    65                                                      
REMARK 465     PHE A    66                                                      
REMARK 465     ARG A    67                                                      
REMARK 465     ARG A    68                                                      
REMARK 465     LEU A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     LYS A    71                                                      
REMARK 465     ASP A    72                                                      
REMARK 465     ALA A    73                                                      
REMARK 465     SER A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     TYR A    76                                                      
REMARK 465     SER A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     ILE A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     ASP A    82                                                      
REMARK 465     PRO A    83                                                      
REMARK 465     LYS A   119                                                      
REMARK 465     VAL A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     ALA A   133                                                      
REMARK 465     SER A   146                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     ALA A   224                                                      
REMARK 465     LYS A   225                                                      
REMARK 465     LYS A   287                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     VAL A   392                                                      
REMARK 465     GLY A   393                                                      
REMARK 465     PHE A   394                                                      
REMARK 465     THR A   395                                                      
REMARK 465     THR A   396                                                      
REMARK 465     SER A   397                                                      
REMARK 465     ASN A   398                                                      
REMARK 465     PRO A   399                                                      
REMARK 465     LEU A   400                                                      
REMARK 465     ASP A   401                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     ARG A   403                                                      
REMARK 465     SER A   404                                                      
REMARK 465     THR A   405                                                      
REMARK 465     PRO A   406                                                      
REMARK 465     GLY A   459                                                      
REMARK 465     HIS A   460                                                      
REMARK 465     ASN A   461                                                      
REMARK 465     GLU A   462                                                      
REMARK 465     ALA A   463                                                      
REMARK 465     ASP A   464                                                      
REMARK 465     GLU A   465                                                      
REMARK 465     PRO A   466                                                      
REMARK 465     SER A   467                                                      
REMARK 465     ALA A   468                                                      
REMARK 465     THR A   469                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     TRP B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     ASP B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     TYR B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     GLN B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     TRP B    22                                                      
REMARK 465     ILE B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     TYR B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     ASP B    29                                                      
REMARK 465     PHE B    30                                                      
REMARK 465     LEU B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     ASP B    33                                                      
REMARK 465     PRO B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     SER B    36                                                      
REMARK 465     VAL B    37                                                      
REMARK 465     ASP B    38                                                      
REMARK 465     ALA B    39                                                      
REMARK 465     ASN B    40                                                      
REMARK 465     TRP B    41                                                      
REMARK 465     ARG B    42                                                      
REMARK 465     SER B    43                                                      
REMARK 465     THR B    44                                                      
REMARK 465     PHE B    45                                                      
REMARK 465     GLN B    46                                                      
REMARK 465     GLN B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     PRO B    49                                                      
REMARK 465     GLY B    50                                                      
REMARK 465     THR B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     VAL B    53                                                      
REMARK 465     LYS B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     ASP B    56                                                      
REMARK 465     GLN B    57                                                      
REMARK 465     PHE B    58                                                      
REMARK 465     HIS B    59                                                      
REMARK 465     SER B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     THR B    62                                                      
REMARK 465     ARG B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     TYR B    65                                                      
REMARK 465     PHE B    66                                                      
REMARK 465     ARG B    67                                                      
REMARK 465     ARG B    68                                                      
REMARK 465     LEU B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     LYS B    71                                                      
REMARK 465     ASP B    72                                                      
REMARK 465     ALA B    73                                                      
REMARK 465     SER B    74                                                      
REMARK 465     ARG B    75                                                      
REMARK 465     TYR B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     ILE B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     ASP B    82                                                      
REMARK 465     PRO B    83                                                      
REMARK 465     ASP B    84                                                      
REMARK 465     GLN B   116                                                      
REMARK 465     GLN B   117                                                      
REMARK 465     ASP B   118                                                      
REMARK 465     GLY B   223                                                      
REMARK 465     ALA B   224                                                      
REMARK 465     LYS B   225                                                      
REMARK 465     LYS B   287                                                      
REMARK 465     GLU B   288                                                      
REMARK 465     HIS B   289                                                      
REMARK 465     LEU B   290                                                      
REMARK 465     VAL B   392                                                      
REMARK 465     GLY B   393                                                      
REMARK 465     PHE B   394                                                      
REMARK 465     THR B   395                                                      
REMARK 465     THR B   396                                                      
REMARK 465     SER B   397                                                      
REMARK 465     ASN B   398                                                      
REMARK 465     PRO B   399                                                      
REMARK 465     LEU B   400                                                      
REMARK 465     ASP B   401                                                      
REMARK 465     ALA B   402                                                      
REMARK 465     ARG B   403                                                      
REMARK 465     SER B   404                                                      
REMARK 465     THR B   405                                                      
REMARK 465     PRO B   406                                                      
REMARK 465     GLY B   459                                                      
REMARK 465     HIS B   460                                                      
REMARK 465     ASN B   461                                                      
REMARK 465     GLU B   462                                                      
REMARK 465     ALA B   463                                                      
REMARK 465     ASP B   464                                                      
REMARK 465     GLU B   465                                                      
REMARK 465     PRO B   466                                                      
REMARK 465     SER B   467                                                      
REMARK 465     ALA B   468                                                      
REMARK 465     THR B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     PRO B   471                                                      
REMARK 465     LEU B   472                                                      
REMARK 465     MET B   473                                                      
REMARK 465     VAL B   658                                                      
REMARK 465     LEU B   659                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A  84    CG   OD1  OD2                                       
REMARK 470     TRP A 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3  CH2         
REMARK 470     GLN A 116    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 118    CG   OD1  OD2                                       
REMARK 470     ASP A 122    CG   OD1  OD2                                       
REMARK 470     LEU A 123    CG   CD1  CD2                                       
REMARK 470     GLU A 132    CD   OE1  OE2                                       
REMARK 470     GLU A 137    CD   OE1  OE2                                       
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 152    CD   CE   NZ                                        
REMARK 470     GLU A 155    CD   OE1  OE2                                       
REMARK 470     GLU A 158    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 252    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 274    CE   NZ                                             
REMARK 470     HIS A 289    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 290    CG   CD1  CD2                                       
REMARK 470     GLU A 343    CD   OE1  OE2                                       
REMARK 470     LYS A 374    CD   CE   NZ                                        
REMARK 470     ARG A 376    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A 391    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 413    CD   CE   NZ                                        
REMARK 470     ARG A 446    NH1  NH2                                            
REMARK 470     GLN A 470    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 472    CG   CD1  CD2                                       
REMARK 470     LYS A 476    CD   CE   NZ                                        
REMARK 470     LYS A 479    CG   CD   CE   NZ                                   
REMARK 470     GLN A 493    CD   OE1  NE2                                       
REMARK 470     LYS A 495    CD   CE   NZ                                        
REMARK 470     GLU A 566    CD   OE1  OE2                                       
REMARK 470     ARG A 573    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASN A 635    CG   OD1  ND2                                       
REMARK 470     VAL A 658    CG1  CG2                                            
REMARK 470     GLN A 685    O                                                   
REMARK 470     THR A 753    CG2                                                 
REMARK 470     GLU A 808    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 812    CG   CD   CE   NZ                                   
REMARK 470     LYS A 854    CE   NZ                                             
REMARK 470     GLN A 861    CD   OE1  NE2                                       
REMARK 470     LYS A 867    CD   CE   NZ                                        
REMARK 470     GLU A 933    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 114    CG   CD1  CD2                                       
REMARK 470     TRP B 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3  CH2         
REMARK 470     LYS B 119    CG   CD   CE   NZ                                   
REMARK 470     GLN B 136    CD   OE1  NE2                                       
REMARK 470     LYS B 148    CE   NZ                                             
REMARK 470     GLN B 162    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 189    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 192    CD   NE   CZ   NH1  NH2                             
REMARK 470     THR B 194    OG1  CG2                                            
REMARK 470     ARG B 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 285    CD   CE   NZ                                        
REMARK 470     ASP B 342    CG   OD1  OD2                                       
REMARK 470     ALA B 358    CB                                                  
REMARK 470     LYS B 374    CG   CD   CE   NZ                                   
REMARK 470     ARG B 376    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 407    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR B 474    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 475    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 476    CG   CD   CE   NZ                                   
REMARK 470     LYS B 478    CD   CE   NZ                                        
REMARK 470     GLN B 493    CD   OE1  NE2                                       
REMARK 470     LYS B 495    CG   CD   CE   NZ                                   
REMARK 470     GLU B 500    CD   OE1  OE2                                       
REMARK 470     GLU B 540    CD   OE1  OE2                                       
REMARK 470     LYS B 552    NZ                                                  
REMARK 470     LYS B 559    CE   NZ                                             
REMARK 470     GLU B 569    CD   OE1  OE2                                       
REMARK 470     GLN B 571    CD   OE1  NE2                                       
REMARK 470     ARG B 573    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 576    CD   CE   NZ                                        
REMARK 470     ALA B 579    CB                                                  
REMARK 470     GLU B 588    CD   OE1  OE2                                       
REMARK 470     SER B 634    OG                                                  
REMARK 470     ASN B 635    CG   OD1  ND2                                       
REMARK 470     THR B 753    CG2                                                 
REMARK 470     GLU B 808    CD   OE1  OE2                                       
REMARK 470     LYS B 812    CD   CE   NZ                                        
REMARK 470     LYS B 815    CE   NZ                                             
REMARK 470     LYS B 834    CD   CE   NZ                                        
REMARK 470     LYS B 854    CD   CE   NZ                                        
REMARK 470     GLN B 857    CD   OE1  NE2                                       
REMARK 470     GLN B 861    CD   OE1  NE2                                       
REMARK 470     LYS B 867    CE   NZ                                             
REMARK 470     LYS B 920    CE   NZ                                             
REMARK 470     GLU B 933    CG   CD   OE1  OE2                                  
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 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 123       -2.32    -57.66                                   
REMARK 500    LEU A 130       76.27     63.06                                   
REMARK 500    TYR A 172        2.71   -165.12                                   
REMARK 500    PHE A 227       37.97    -91.31                                   
REMARK 500    ALA A 259     -134.30   -120.81                                   
REMARK 500    PHE A 301      143.86   -173.26                                   
REMARK 500    GLU A 324       -0.06     98.68                                   
REMARK 500    PRO A 344       62.81   -110.25                                   
REMARK 500    SER A 373        0.41    -60.45                                   
REMARK 500    ASN A 390      -72.80   -104.40                                   
REMARK 500    CYS A 454     -156.35   -151.77                                   
REMARK 500    PRO A 546       77.72    -66.54                                   
REMARK 500    GLN A 571      155.48    -46.12                                   
REMARK 500    ILE A 645      -62.08    -91.55                                   
REMARK 500    SER A 657      170.77    -29.59                                   
REMARK 500    LEU A 659     -155.19     36.97                                   
REMARK 500    PHE A 700      -70.66   -124.59                                   
REMARK 500    HIS A 729       34.55   -140.85                                   
REMARK 500    SER A 730      -38.94   -137.35                                   
REMARK 500    ALA A 742      151.02    179.70                                   
REMARK 500    ARG A 783       22.24   -142.88                                   
REMARK 500    ALA B 145       68.01   -103.11                                   
REMARK 500    LYS B 148      110.97    -28.95                                   
REMARK 500    TYR B 172      -19.94   -142.93                                   
REMARK 500    ARG B 192      -56.33   -141.69                                   
REMARK 500    ALA B 193      101.44   -160.17                                   
REMARK 500    PHE B 227       66.72   -115.25                                   
REMARK 500    ALA B 259     -135.36   -118.43                                   
REMARK 500    VAL B 270      -51.61   -121.22                                   
REMARK 500    GLU B 324       -7.98     91.40                                   
REMARK 500    GLU B 343       74.13   -109.60                                   
REMARK 500    PRO B 344       33.69    -69.55                                   
REMARK 500    GLN B 416       48.78     77.40                                   
REMARK 500    CYS B 518      135.72    -39.68                                   
REMARK 500    PHE B 700      -69.88   -121.00                                   
REMARK 500    SER B 730      -42.05   -134.94                                   
REMARK 500    MET B 776       96.47    -67.28                                   
REMARK 500    LYS B 779      -76.09   -110.96                                   
REMARK 500    GLN B 886      -64.43    -22.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE A  144     ALA A  145                 -149.24                    
REMARK 500 GLU A  171     TYR A  172                 -137.18                    
REMARK 500 ARG A  226     PHE A  227                  124.54                    
REMARK 500 GLU A  230     GLY A  231                  -43.09                    
REMARK 500 GLY A  231     GLY A  232                  139.76                    
REMARK 500 LEU A  290     GLY A  291                  145.47                    
REMARK 500 ASP A  342     GLU A  343                  149.51                    
REMARK 500 MET A  414     VAL A  415                  145.41                    
REMARK 500 SER A  657     VAL A  658                  124.21                    
REMARK 500 GLY A  896     ALA A  897                 -148.80                    
REMARK 500 PHE B  144     ALA B  145                 -140.80                    
REMARK 500 ALA B  145     SER B  146                 -146.51                    
REMARK 500 SER B  146     GLY B  147                  -63.48                    
REMARK 500 GLY B  147     LYS B  148                  115.67                    
REMARK 500 GLU B  189     SER B  190                 -147.78                    
REMARK 500 SER B  190     GLY B  191                 -114.38                    
REMARK 500 GLY B  191     ARG B  192                  103.33                    
REMARK 500 ARG B  192     ALA B  193                 -146.98                    
REMARK 500 PHE B  227     SER B  228                 -149.47                    
REMARK 500 ARG B  376     GLY B  377                  -71.98                    
REMARK 500 GLY B  377     TYR B  378                  146.00                    
REMARK 500 TYR B  536     LEU B  537                 -149.25                    
REMARK 500 GLY B  896     ALA B  897                 -142.72                    
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 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    VAL A 334        23.9      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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP A1934                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B1934                 
DBREF  2JGD A    1   933  UNP    P0AFG3   ODO1_ECOLI       1    933             
DBREF  2JGD B    1   933  UNP    P0AFG3   ODO1_ECOLI       1    933             
SEQADV 2JGD HIS A  914  UNP  P0AFG3    TYR   914 CONFLICT                       
SEQADV 2JGD ALA B  579  UNP  P0AFG3    GLY   579 CONFLICT                       
SEQRES   1 A  933  MET GLN ASN SER ALA LEU LYS ALA TRP LEU ASP SER SER          
SEQRES   2 A  933  TYR LEU SER GLY ALA ASN GLN SER TRP ILE GLU GLN LEU          
SEQRES   3 A  933  TYR GLU ASP PHE LEU THR ASP PRO ASP SER VAL ASP ALA          
SEQRES   4 A  933  ASN TRP ARG SER THR PHE GLN GLN LEU PRO GLY THR GLY          
SEQRES   5 A  933  VAL LYS PRO ASP GLN PHE HIS SER GLN THR ARG GLU TYR          
SEQRES   6 A  933  PHE ARG ARG LEU ALA LYS ASP ALA SER ARG TYR SER SER          
SEQRES   7 A  933  THR ILE SER ASP PRO ASP THR ASN VAL LYS GLN VAL LYS          
SEQRES   8 A  933  VAL LEU GLN LEU ILE ASN ALA TYR ARG PHE ARG GLY HIS          
SEQRES   9 A  933  GLN HIS ALA ASN LEU ASP PRO LEU GLY LEU TRP GLN GLN          
SEQRES  10 A  933  ASP LYS VAL ALA ASP LEU ASP PRO SER PHE HIS ASP LEU          
SEQRES  11 A  933  THR GLU ALA ASP PHE GLN GLU THR PHE ASN VAL GLY SER          
SEQRES  12 A  933  PHE ALA SER GLY LYS GLU THR MET LYS LEU GLY GLU LEU          
SEQRES  13 A  933  LEU GLU ALA LEU LYS GLN THR TYR CYS GLY PRO ILE GLY          
SEQRES  14 A  933  ALA GLU TYR MET HIS ILE THR SER THR GLU GLU LYS ARG          
SEQRES  15 A  933  TRP ILE GLN GLN ARG ILE GLU SER GLY ARG ALA THR PHE          
SEQRES  16 A  933  ASN SER GLU GLU LYS LYS ARG PHE LEU SER GLU LEU THR          
SEQRES  17 A  933  ALA ALA GLU GLY LEU GLU ARG TYR LEU GLY ALA LYS PHE          
SEQRES  18 A  933  PRO GLY ALA LYS ARG PHE SER LEU GLU GLY GLY ASP ALA          
SEQRES  19 A  933  LEU ILE PRO MET LEU LYS GLU MET ILE ARG HIS ALA GLY          
SEQRES  20 A  933  ASN SER GLY THR ARG GLU VAL VAL LEU GLY MET ALA HIS          
SEQRES  21 A  933  ARG GLY ARG LEU ASN VAL LEU VAL ASN VAL LEU GLY LYS          
SEQRES  22 A  933  LYS PRO GLN ASP LEU PHE ASP GLU PHE ALA GLY LYS HIS          
SEQRES  23 A  933  LYS GLU HIS LEU GLY THR GLY ASP VAL LYS TYR HIS MET          
SEQRES  24 A  933  GLY PHE SER SER ASP PHE GLN THR ASP GLY GLY LEU VAL          
SEQRES  25 A  933  HIS LEU ALA LEU ALA PHE ASN PRO SER HIS LEU GLU ILE          
SEQRES  26 A  933  VAL SER PRO VAL VAL ILE GLY SER VAL ARG ALA ARG LEU          
SEQRES  27 A  933  ASP ARG LEU ASP GLU PRO SER SER ASN LYS VAL LEU PRO          
SEQRES  28 A  933  ILE THR ILE HIS GLY ASP ALA ALA VAL THR GLY GLN GLY          
SEQRES  29 A  933  VAL VAL GLN GLU THR LEU ASN MET SER LYS ALA ARG GLY          
SEQRES  30 A  933  TYR GLU VAL GLY GLY THR VAL ARG ILE VAL ILE ASN ASN          
SEQRES  31 A  933  GLN VAL GLY PHE THR THR SER ASN PRO LEU ASP ALA ARG          
SEQRES  32 A  933  SER THR PRO TYR CYS THR ASP ILE GLY LYS MET VAL GLN          
SEQRES  33 A  933  ALA PRO ILE PHE HIS VAL ASN ALA ASP ASP PRO GLU ALA          
SEQRES  34 A  933  VAL ALA PHE VAL THR ARG LEU ALA LEU ASP PHE ARG ASN          
SEQRES  35 A  933  THR PHE LYS ARG ASP VAL PHE ILE ASP LEU VAL CYS TYR          
SEQRES  36 A  933  ARG ARG HIS GLY HIS ASN GLU ALA ASP GLU PRO SER ALA          
SEQRES  37 A  933  THR GLN PRO LEU MET TYR GLN LYS ILE LYS LYS HIS PRO          
SEQRES  38 A  933  THR PRO ARG LYS ILE TYR ALA ASP LYS LEU GLU GLN GLU          
SEQRES  39 A  933  LYS VAL ALA THR LEU GLU ASP ALA THR GLU MET VAL ASN          
SEQRES  40 A  933  LEU TYR ARG ASP ALA LEU ASP ALA GLY ASP CYS VAL VAL          
SEQRES  41 A  933  ALA GLU TRP ARG PRO MET ASN MET HIS SER PHE THR TRP          
SEQRES  42 A  933  SER PRO TYR LEU ASN HIS GLU TRP ASP GLU GLU TYR PRO          
SEQRES  43 A  933  ASN LYS VAL GLU MET LYS ARG LEU GLN GLU LEU ALA LYS          
SEQRES  44 A  933  ARG ILE SER THR VAL PRO GLU ALA VAL GLU MET GLN SER          
SEQRES  45 A  933  ARG VAL ALA LYS ILE TYR GLY ASP ARG GLN ALA MET ALA          
SEQRES  46 A  933  ALA GLY GLU LYS LEU PHE ASP TRP GLY GLY ALA GLU ASN          
SEQRES  47 A  933  LEU ALA TYR ALA THR LEU VAL ASP GLU GLY ILE PRO VAL          
SEQRES  48 A  933  ARG LEU SER GLY GLU ASP SER GLY ARG GLY THR PHE PHE          
SEQRES  49 A  933  HIS ARG HIS ALA VAL ILE HIS ASN GLN SER ASN GLY SER          
SEQRES  50 A  933  THR TYR THR PRO LEU GLN HIS ILE HIS ASN GLY GLN GLY          
SEQRES  51 A  933  ALA PHE ARG VAL TRP ASP SER VAL LEU SER GLU GLU ALA          
SEQRES  52 A  933  VAL LEU ALA PHE GLU TYR GLY TYR ALA THR ALA GLU PRO          
SEQRES  53 A  933  ARG THR LEU THR ILE TRP GLU ALA GLN PHE GLY ASP PHE          
SEQRES  54 A  933  ALA ASN GLY ALA GLN VAL VAL ILE ASP GLN PHE ILE SER          
SEQRES  55 A  933  SER GLY GLU GLN LYS TRP GLY ARG MET CYS GLY LEU VAL          
SEQRES  56 A  933  MET LEU LEU PRO HIS GLY TYR GLU GLY GLN GLY PRO GLU          
SEQRES  57 A  933  HIS SER SER ALA ARG LEU GLU ARG TYR LEU GLN LEU CYS          
SEQRES  58 A  933  ALA GLU GLN ASN MET GLN VAL CYS VAL PRO SER THR PRO          
SEQRES  59 A  933  ALA GLN VAL TYR HIS MET LEU ARG ARG GLN ALA LEU ARG          
SEQRES  60 A  933  GLY MET ARG ARG PRO LEU VAL VAL MET SER PRO LYS SER          
SEQRES  61 A  933  LEU LEU ARG HIS PRO LEU ALA VAL SER SER LEU GLU GLU          
SEQRES  62 A  933  LEU ALA ASN GLY THR PHE LEU PRO ALA ILE GLY GLU ILE          
SEQRES  63 A  933  ASP GLU LEU ASP PRO LYS GLY VAL LYS ARG VAL VAL MET          
SEQRES  64 A  933  CYS SER GLY LYS VAL TYR TYR ASP LEU LEU GLU GLN ARG          
SEQRES  65 A  933  ARG LYS ASN ASN GLN HIS ASP VAL ALA ILE VAL ARG ILE          
SEQRES  66 A  933  GLU GLN LEU TYR PRO PHE PRO HIS LYS ALA MET GLN GLU          
SEQRES  67 A  933  VAL LEU GLN GLN PHE ALA HIS VAL LYS ASP PHE VAL TRP          
SEQRES  68 A  933  CYS GLN GLU GLU PRO LEU ASN GLN GLY ALA TRP TYR CYS          
SEQRES  69 A  933  SER GLN HIS HIS PHE ARG GLU VAL ILE PRO PHE GLY ALA          
SEQRES  70 A  933  SER LEU ARG TYR ALA GLY ARG PRO ALA SER ALA SER PRO          
SEQRES  71 A  933  ALA VAL GLY HIS MET SER VAL HIS GLN LYS GLN GLN GLN          
SEQRES  72 A  933  ASP LEU VAL ASN ASP ALA LEU ASN VAL GLU                      
SEQRES   1 B  933  MET GLN ASN SER ALA LEU LYS ALA TRP LEU ASP SER SER          
SEQRES   2 B  933  TYR LEU SER GLY ALA ASN GLN SER TRP ILE GLU GLN LEU          
SEQRES   3 B  933  TYR GLU ASP PHE LEU THR ASP PRO ASP SER VAL ASP ALA          
SEQRES   4 B  933  ASN TRP ARG SER THR PHE GLN GLN LEU PRO GLY THR GLY          
SEQRES   5 B  933  VAL LYS PRO ASP GLN PHE HIS SER GLN THR ARG GLU TYR          
SEQRES   6 B  933  PHE ARG ARG LEU ALA LYS ASP ALA SER ARG TYR SER SER          
SEQRES   7 B  933  THR ILE SER ASP PRO ASP THR ASN VAL LYS GLN VAL LYS          
SEQRES   8 B  933  VAL LEU GLN LEU ILE ASN ALA TYR ARG PHE ARG GLY HIS          
SEQRES   9 B  933  GLN HIS ALA ASN LEU ASP PRO LEU GLY LEU TRP GLN GLN          
SEQRES  10 B  933  ASP LYS VAL ALA ASP LEU ASP PRO SER PHE HIS ASP LEU          
SEQRES  11 B  933  THR GLU ALA ASP PHE GLN GLU THR PHE ASN VAL GLY SER          
SEQRES  12 B  933  PHE ALA SER GLY LYS GLU THR MET LYS LEU GLY GLU LEU          
SEQRES  13 B  933  LEU GLU ALA LEU LYS GLN THR TYR CYS GLY PRO ILE GLY          
SEQRES  14 B  933  ALA GLU TYR MET HIS ILE THR SER THR GLU GLU LYS ARG          
SEQRES  15 B  933  TRP ILE GLN GLN ARG ILE GLU SER GLY ARG ALA THR PHE          
SEQRES  16 B  933  ASN SER GLU GLU LYS LYS ARG PHE LEU SER GLU LEU THR          
SEQRES  17 B  933  ALA ALA GLU GLY LEU GLU ARG TYR LEU GLY ALA LYS PHE          
SEQRES  18 B  933  PRO GLY ALA LYS ARG PHE SER LEU GLU GLY GLY ASP ALA          
SEQRES  19 B  933  LEU ILE PRO MET LEU LYS GLU MET ILE ARG HIS ALA GLY          
SEQRES  20 B  933  ASN SER GLY THR ARG GLU VAL VAL LEU GLY MET ALA HIS          
SEQRES  21 B  933  ARG GLY ARG LEU ASN VAL LEU VAL ASN VAL LEU GLY LYS          
SEQRES  22 B  933  LYS PRO GLN ASP LEU PHE ASP GLU PHE ALA GLY LYS HIS          
SEQRES  23 B  933  LYS GLU HIS LEU GLY THR GLY ASP VAL LYS TYR HIS MET          
SEQRES  24 B  933  GLY PHE SER SER ASP PHE GLN THR ASP GLY GLY LEU VAL          
SEQRES  25 B  933  HIS LEU ALA LEU ALA PHE ASN PRO SER HIS LEU GLU ILE          
SEQRES  26 B  933  VAL SER PRO VAL VAL ILE GLY SER VAL ARG ALA ARG LEU          
SEQRES  27 B  933  ASP ARG LEU ASP GLU PRO SER SER ASN LYS VAL LEU PRO          
SEQRES  28 B  933  ILE THR ILE HIS GLY ASP ALA ALA VAL THR GLY GLN GLY          
SEQRES  29 B  933  VAL VAL GLN GLU THR LEU ASN MET SER LYS ALA ARG GLY          
SEQRES  30 B  933  TYR GLU VAL GLY GLY THR VAL ARG ILE VAL ILE ASN ASN          
SEQRES  31 B  933  GLN VAL GLY PHE THR THR SER ASN PRO LEU ASP ALA ARG          
SEQRES  32 B  933  SER THR PRO TYR CYS THR ASP ILE GLY LYS MET VAL GLN          
SEQRES  33 B  933  ALA PRO ILE PHE HIS VAL ASN ALA ASP ASP PRO GLU ALA          
SEQRES  34 B  933  VAL ALA PHE VAL THR ARG LEU ALA LEU ASP PHE ARG ASN          
SEQRES  35 B  933  THR PHE LYS ARG ASP VAL PHE ILE ASP LEU VAL CYS TYR          
SEQRES  36 B  933  ARG ARG HIS GLY HIS ASN GLU ALA ASP GLU PRO SER ALA          
SEQRES  37 B  933  THR GLN PRO LEU MET TYR GLN LYS ILE LYS LYS HIS PRO          
SEQRES  38 B  933  THR PRO ARG LYS ILE TYR ALA ASP LYS LEU GLU GLN GLU          
SEQRES  39 B  933  LYS VAL ALA THR LEU GLU ASP ALA THR GLU MET VAL ASN          
SEQRES  40 B  933  LEU TYR ARG ASP ALA LEU ASP ALA GLY ASP CYS VAL VAL          
SEQRES  41 B  933  ALA GLU TRP ARG PRO MET ASN MET HIS SER PHE THR TRP          
SEQRES  42 B  933  SER PRO TYR LEU ASN HIS GLU TRP ASP GLU GLU TYR PRO          
SEQRES  43 B  933  ASN LYS VAL GLU MET LYS ARG LEU GLN GLU LEU ALA LYS          
SEQRES  44 B  933  ARG ILE SER THR VAL PRO GLU ALA VAL GLU MET GLN SER          
SEQRES  45 B  933  ARG VAL ALA LYS ILE TYR ALA ASP ARG GLN ALA MET ALA          
SEQRES  46 B  933  ALA GLY GLU LYS LEU PHE ASP TRP GLY GLY ALA GLU ASN          
SEQRES  47 B  933  LEU ALA TYR ALA THR LEU VAL ASP GLU GLY ILE PRO VAL          
SEQRES  48 B  933  ARG LEU SER GLY GLU ASP SER GLY ARG GLY THR PHE PHE          
SEQRES  49 B  933  HIS ARG HIS ALA VAL ILE HIS ASN GLN SER ASN GLY SER          
SEQRES  50 B  933  THR TYR THR PRO LEU GLN HIS ILE HIS ASN GLY GLN GLY          
SEQRES  51 B  933  ALA PHE ARG VAL TRP ASP SER VAL LEU SER GLU GLU ALA          
SEQRES  52 B  933  VAL LEU ALA PHE GLU TYR GLY TYR ALA THR ALA GLU PRO          
SEQRES  53 B  933  ARG THR LEU THR ILE TRP GLU ALA GLN PHE GLY ASP PHE          
SEQRES  54 B  933  ALA ASN GLY ALA GLN VAL VAL ILE ASP GLN PHE ILE SER          
SEQRES  55 B  933  SER GLY GLU GLN LYS TRP GLY ARG MET CYS GLY LEU VAL          
SEQRES  56 B  933  MET LEU LEU PRO HIS GLY TYR GLU GLY GLN GLY PRO GLU          
SEQRES  57 B  933  HIS SER SER ALA ARG LEU GLU ARG TYR LEU GLN LEU CYS          
SEQRES  58 B  933  ALA GLU GLN ASN MET GLN VAL CYS VAL PRO SER THR PRO          
SEQRES  59 B  933  ALA GLN VAL TYR HIS MET LEU ARG ARG GLN ALA LEU ARG          
SEQRES  60 B  933  GLY MET ARG ARG PRO LEU VAL VAL MET SER PRO LYS SER          
SEQRES  61 B  933  LEU LEU ARG HIS PRO LEU ALA VAL SER SER LEU GLU GLU          
SEQRES  62 B  933  LEU ALA ASN GLY THR PHE LEU PRO ALA ILE GLY GLU ILE          
SEQRES  63 B  933  ASP GLU LEU ASP PRO LYS GLY VAL LYS ARG VAL VAL MET          
SEQRES  64 B  933  CYS SER GLY LYS VAL TYR TYR ASP LEU LEU GLU GLN ARG          
SEQRES  65 B  933  ARG LYS ASN ASN GLN HIS ASP VAL ALA ILE VAL ARG ILE          
SEQRES  66 B  933  GLU GLN LEU TYR PRO PHE PRO HIS LYS ALA MET GLN GLU          
SEQRES  67 B  933  VAL LEU GLN GLN PHE ALA HIS VAL LYS ASP PHE VAL TRP          
SEQRES  68 B  933  CYS GLN GLU GLU PRO LEU ASN GLN GLY ALA TRP TYR CYS          
SEQRES  69 B  933  SER GLN HIS HIS PHE ARG GLU VAL ILE PRO PHE GLY ALA          
SEQRES  70 B  933  SER LEU ARG TYR ALA GLY ARG PRO ALA SER ALA SER PRO          
SEQRES  71 B  933  ALA VAL GLY TYR MET SER VAL HIS GLN LYS GLN GLN GLN          
SEQRES  72 B  933  ASP LEU VAL ASN ASP ALA LEU ASN VAL GLU                      
HET    AMP  A1934      23                                                       
HET    AMP  B1934      23                                                       
HETNAM     AMP ADENOSINE MONOPHOSPHATE                                          
FORMUL   3  AMP    2(C10 H14 N5 O7 P)                                           
FORMUL   5  HOH   *735(H2 O1)                                                   
HELIX    1   1 ASP A   84  GLY A  103  1                                  20    
HELIX    2   2 HIS A  104  ALA A  107  5                                   4    
HELIX    3   3 PRO A  125  LEU A  130  5                                   6    
HELIX    4   4 LEU A  153  GLY A  166  1                                  14    
HELIX    5   5 SER A  177  GLU A  189  1                                  13    
HELIX    6   6 ASN A  196  PHE A  221  1                                  26    
HELIX    7   7 ALA A  234  ASN A  248  1                                  15    
HELIX    8   8 GLY A  262  VAL A  270  1                                   9    
HELIX    9   9 LYS A  274  ALA A  283  1                                  10    
HELIX   10  10 VAL A  295  MET A  299  5                                   5    
HELIX   11  11 ILE A  325  ASP A  339  1                                  15    
HELIX   12  12 SER A  345  ASN A  347  5                                   3    
HELIX   13  13 ASP A  357  GLN A  363  1                                   7    
HELIX   14  14 GLY A  364  SER A  373  1                                  10    
HELIX   15  15 TYR A  407  MET A  414  5                                   8    
HELIX   16  16 ASP A  426  LYS A  445  1                                  20    
HELIX   17  17 MET A  473  LYS A  479  1                                   7    
HELIX   18  18 THR A  482  GLN A  493  1                                  12    
HELIX   19  19 THR A  498  GLY A  516  1                                  19    
HELIX   20  20 ASN A  527  PHE A  531  5                                   5    
HELIX   21  21 TRP A  533  LEU A  537  5                                   5    
HELIX   22  22 GLU A  550  ILE A  561  1                                  12    
HELIX   23  23 GLN A  571  ALA A  586  1                                  16    
HELIX   24  24 ASP A  592  ASP A  606  1                                  15    
HELIX   25  25 THR A  640  HIS A  644  5                                   5    
HELIX   26  26 SER A  660  GLU A  675  1                                  16    
HELIX   27  27 PHE A  686  GLY A  692  5                                   7    
HELIX   28  28 ALA A  693  PHE A  700  1                                   8    
HELIX   29  29 SER A  703  GLY A  709  1                                   7    
HELIX   30  30 ARG A  733  LEU A  740  1                                   8    
HELIX   31  31 THR A  753  ARG A  767  1                                  15    
HELIX   32  32 LYS A  779  HIS A  784  5                                   6    
HELIX   33  33 SER A  790  GLY A  797  1                                   8    
HELIX   34  34 ASP A  810  VAL A  814  5                                   5    
HELIX   35  35 LYS A  823  ASN A  835  1                                  13    
HELIX   36  36 PRO A  852  GLN A  861  1                                  10    
HELIX   37  37 GLN A  862  ALA A  864  5                                   3    
HELIX   38  38 ALA A  881  GLU A  891  1                                  11    
HELIX   39  39 HIS A  914  ASN A  931  1                                  18    
HELIX   40  40 THR B   85  GLY B  103  1                                  19    
HELIX   41  41 HIS B  104  ALA B  107  5                                   4    
HELIX   42  42 VAL B  120  ASP B  124  5                                   5    
HELIX   43  43 ASP B  124  ASP B  129  5                                   6    
HELIX   44  44 THR B  131  GLN B  136  5                                   6    
HELIX   45  45 LEU B  153  CYS B  165  1                                  13    
HELIX   46  46 SER B  177  GLU B  189  1                                  13    
HELIX   47  47 ASN B  196  PHE B  221  1                                  26    
HELIX   48  48 ALA B  234  ASN B  248  1                                  15    
HELIX   49  49 GLY B  262  VAL B  270  1                                   9    
HELIX   50  50 LYS B  274  ALA B  283  1                                  10    
HELIX   51  51 VAL B  295  MET B  299  5                                   5    
HELIX   52  52 ILE B  325  ARG B  340  1                                  16    
HELIX   53  53 SER B  345  ASN B  347  5                                   3    
HELIX   54  54 ASP B  357  GLN B  363  1                                   7    
HELIX   55  55 GLY B  364  SER B  373  1                                  10    
HELIX   56  56 THR B  409  MET B  414  5                                   6    
HELIX   57  57 ASP B  426  LYS B  445  1                                  20    
HELIX   58  58 TYR B  474  LYS B  479  1                                   6    
HELIX   59  59 THR B  482  GLU B  494  1                                  13    
HELIX   60  60 THR B  498  GLY B  516  1                                  19    
HELIX   61  61 ASN B  527  PHE B  531  5                                   5    
HELIX   62  62 TRP B  533  LEU B  537  5                                   5    
HELIX   63  63 GLU B  550  ILE B  561  1                                  12    
HELIX   64  64 GLN B  571  ALA B  586  1                                  16    
HELIX   65  65 ASP B  592  GLU B  607  1                                  16    
HELIX   66  66 THR B  640  HIS B  644  5                                   5    
HELIX   67  67 SER B  660  GLU B  675  1                                  16    
HELIX   68  68 PHE B  686  GLY B  692  5                                   7    
HELIX   69  69 ALA B  693  PHE B  700  1                                   8    
HELIX   70  70 SER B  703  GLY B  709  1                                   7    
HELIX   71  71 ARG B  733  CYS B  741  1                                   9    
HELIX   72  72 THR B  753  ARG B  767  1                                  15    
HELIX   73  73 LYS B  779  HIS B  784  5                                   6    
HELIX   74  74 SER B  790  GLY B  797  1                                   8    
HELIX   75  75 ASP B  810  VAL B  814  5                                   5    
HELIX   76  76 LYS B  823  ASN B  835  1                                  13    
HELIX   77  77 PRO B  852  GLN B  861  1                                  10    
HELIX   78  78 GLN B  862  ALA B  864  5                                   3    
HELIX   79  79 ALA B  881  ILE B  893  1                                  13    
HELIX   80  80 TYR B  914  ASN B  931  1                                  18    
SHEET    1  AA 2 THR A 138  ASN A 140  0                                        
SHEET    2  AA 2 THR A 150  LYS A 152 -1  O  MET A 151   N  PHE A 139           
SHEET    1  AB 9 ILE A 168  GLU A 171  0                                        
SHEET    2  AB 9 ILE A 419  ASN A 423 -1  O  ILE A 419   N  GLU A 171           
SHEET    3  AB 9 VAL A 448  VAL A 453  1  O  PHE A 449   N  PHE A 420           
SHEET    4  AB 9 VAL A 384  ASN A 389  1  O  ARG A 385   N  ILE A 450           
SHEET    5  AB 9 VAL A 349  GLY A 356  1  O  PRO A 351   N  VAL A 384           
SHEET    6  AB 9 GLU A 253  GLY A 257  1  O  GLU A 253   N  LEU A 350           
SHEET    7  AB 9 GLY A 310  LEU A 316  1  O  HIS A 313   N  VAL A 254           
SHEET    8  AB 9 PHE A 301  THR A 307 -1  O  PHE A 301   N  LEU A 316           
SHEET    9  AB 9 TRP A 523  ARG A 524 -1  O  ARG A 524   N  ASP A 304           
SHEET    1  AC 7 PHE A 652  TRP A 655  0                                        
SHEET    2  AC 7 VAL A 611  GLY A 615  1  O  VAL A 611   N  ARG A 653           
SHEET    3  AC 7 LEU A 679  GLU A 683  1  O  LEU A 679   N  ARG A 612           
SHEET    4  AC 7 VAL A 715  PRO A 719  1  O  VAL A 715   N  TRP A 682           
SHEET    5  AC 7 LEU A 773  SER A 777  1  O  LEU A 773   N  MET A 716           
SHEET    6  AC 7 GLN A 747  CYS A 749  1  O  GLN A 747   N  VAL A 774           
SHEET    7  AC 7 GLN A 847  TYR A 849 -1  N  LEU A 848   O  VAL A 748           
SHEET    1  AD 2 ILE A 630  HIS A 631  0                                        
SHEET    2  AD 2 THR A 638  TYR A 639 -1  O  TYR A 639   N  ILE A 630           
SHEET    1  AE 5 ALA A 802  ILE A 803  0                                        
SHEET    2  AE 5 VAL A 840  ILE A 845 -1  O  ARG A 844   N  ILE A 803           
SHEET    3  AE 5 ARG A 816  CYS A 820  1  O  ARG A 816   N  ALA A 841           
SHEET    4  AE 5 ASP A 868  PRO A 876  1  O  ASP A 868   N  VAL A 817           
SHEET    5  AE 5 SER A 898  ARG A 904  1  O  SER A 898   N  PHE A 869           
SHEET    1  BA 2 THR B 138  ASN B 140  0                                        
SHEET    2  BA 2 THR B 150  LYS B 152 -1  O  MET B 151   N  PHE B 139           
SHEET    1  BB 9 ILE B 168  GLU B 171  0                                        
SHEET    2  BB 9 ILE B 419  ASN B 423 -1  O  ILE B 419   N  GLU B 171           
SHEET    3  BB 9 VAL B 448  VAL B 453  1  O  PHE B 449   N  PHE B 420           
SHEET    4  BB 9 VAL B 384  ASN B 389  1  O  ARG B 385   N  ILE B 450           
SHEET    5  BB 9 VAL B 349  GLY B 356  1  O  PRO B 351   N  VAL B 384           
SHEET    6  BB 9 GLU B 253  GLY B 257  1  O  GLU B 253   N  LEU B 350           
SHEET    7  BB 9 GLY B 310  LEU B 316  1  O  HIS B 313   N  VAL B 254           
SHEET    8  BB 9 PHE B 301  THR B 307 -1  O  PHE B 301   N  LEU B 316           
SHEET    9  BB 9 TRP B 523  ARG B 524 -1  O  ARG B 524   N  ASP B 304           
SHEET    1  BC 7 PHE B 652  ASP B 656  0                                        
SHEET    2  BC 7 VAL B 611  GLY B 615  1  O  VAL B 611   N  ARG B 653           
SHEET    3  BC 7 LEU B 679  GLU B 683  1  O  LEU B 679   N  ARG B 612           
SHEET    4  BC 7 VAL B 715  PRO B 719  1  O  VAL B 715   N  TRP B 682           
SHEET    5  BC 7 LEU B 773  SER B 777  1  O  LEU B 773   N  MET B 716           
SHEET    6  BC 7 GLN B 747  CYS B 749  1  O  GLN B 747   N  VAL B 774           
SHEET    7  BC 7 GLN B 847  TYR B 849 -1  N  LEU B 848   O  VAL B 748           
SHEET    1  BD 2 ILE B 630  HIS B 631  0                                        
SHEET    2  BD 2 THR B 638  TYR B 639 -1  O  TYR B 639   N  ILE B 630           
SHEET    1  BE 5 ALA B 802  ILE B 803  0                                        
SHEET    2  BE 5 VAL B 840  ILE B 845 -1  O  ARG B 844   N  ILE B 803           
SHEET    3  BE 5 ARG B 816  CYS B 820  1  O  ARG B 816   N  ALA B 841           
SHEET    4  BE 5 ASP B 868  PRO B 876  1  O  ASP B 868   N  VAL B 817           
SHEET    5  BE 5 SER B 898  ARG B 904  1  O  SER B 898   N  PHE B 869           
CISPEP   1 TYR A  849    PRO A  850          0       -19.03                     
CISPEP   2 TYR B  849    PRO B  850          0       -26.78                     
SITE     1 AC1 17 SER A 302  HIS A 313  ALA A 315  ARG A 337                    
SITE     2 AC1 17 MET A 526  SER A 530  PHE A 531  TRP A 533                    
SITE     3 AC1 17 THR A 673  GLY A 709  ARG A 710  MET A 711                    
SITE     4 AC1 17 HOH A2145  HOH A2146  HOH A2335  HOH A2336                    
SITE     5 AC1 17 HOH A2337                                                     
SITE     1 AC2 16 SER B 302  HIS B 313  ALA B 315  ARG B 337                    
SITE     2 AC2 16 SER B 530  PHE B 531  TRP B 533  THR B 673                    
SITE     3 AC2 16 GLY B 709  ARG B 710  MET B 711  HOH B2394                    
SITE     4 AC2 16 HOH B2395  HOH B2396  HOH B2397  HOH B2398                    
CRYST1  142.493  142.493  251.811  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      0.007018  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007018  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003971        0.00000                         
MTRIX1   1  0.790320  0.612290 -0.022060       15.62862    1                    
MTRIX2   1  0.612310 -0.790590 -0.006650      -44.72879    1                    
MTRIX3   1 -0.021510 -0.008250 -0.999730       50.09098    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system