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Database: PDB
Entry: 6JV9
LinkDB: 6JV9
Original site: 6JV9 
HEADER    STRUCTURAL PROTEIN                      16-APR-19   6JV9              
TITLE     CRYSTAL STRUCTURE OF HUMAN CRMP2 1-532, UNMODIFIED                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPYRIMIDINASE-RELATED PROTEIN 2;                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DRP-2,COLLAPSIN RESPONSE MEDIATOR PROTEIN 2,CRMP-2,N2A3,UNC-
COMPND   5 33-LIKE PHOSPHOPROTEIN 2,ULIP-2;                                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DPYSL2, CRMP2, ULIP2;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K19                                        
KEYWDS    MICROTUBULE ASSOCIATED PROTEIN, GAP ACTIVITY, NEURONAL PROTEIN,       
KEYWDS   2 STRUCTURAL PROTEIN                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.JIANG,T.OGAWA,N.HIROKAWA                                            
REVDAT   2   23-OCT-19 6JV9    1       JRNL                                     
REVDAT   1   09-OCT-19 6JV9    0                                                
JRNL        AUTH   M.TOYOSHIMA,X.JIANG,T.OGAWA,T.OHNISHI,S.YOSHIHARA,S.BALAN,   
JRNL        AUTH 2 T.YOSHIKAWA,N.HIROKAWA                                       
JRNL        TITL   ENHANCED CARBONYL STRESS INDUCES IRREVERSIBLE                
JRNL        TITL 2 MULTIMERIZATION OF CRMP2 IN SCHIZOPHRENIA PATHOGENESIS.      
JRNL        REF    LIFE SCI ALLIANCE             V.   2       2019              
JRNL        REFN                   ESSN 2575-1077                               
JRNL        PMID   31591136                                                     
JRNL        DOI    10.26508/LSA.201900478                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 97166                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5112                            
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) : 2.26                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7053                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 349                          
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14883                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 571                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.58000                                             
REMARK   3    B22 (A**2) : -0.83000                                             
REMARK   3    B33 (A**2) : 1.43000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.19000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.260         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.177         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.137         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.552         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15219 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 14376 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20646 ; 1.520 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 33136 ; 1.849 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1943 ; 5.798 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   657 ;36.334 ;24.612       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2522 ;12.734 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    80 ;16.893 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2336 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17308 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3348 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7784 ; 2.072 ; 2.917       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  7783 ; 2.072 ; 2.916       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9723 ; 3.127 ; 4.365       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  9724 ; 3.127 ; 4.365       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7435 ; 3.030 ; 3.256       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  7431 ; 3.021 ; 3.253       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 10918 ; 4.722 ; 4.728       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 16529 ; 6.014 ;23.038       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 16387 ; 6.009 ;22.987       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    15    499       B    15    499   60692  0.05  0.05     
REMARK   3    2     A    15    496       C    15    496   60738  0.04  0.05     
REMARK   3    3     A    15    495       D    15    495   60360  0.05  0.05     
REMARK   3    4     B    15    496       C    15    496   60786  0.03  0.05     
REMARK   3    5     B    14    495       D    14    495   60510  0.05  0.05     
REMARK   3    6     C    15    495       D    15    495   60666  0.04  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6JV9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300011872.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102278                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.16300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5MKV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES (PH 6.0), 15% (V/V) PEG 400,   
REMARK 280  0.1 M CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 287K                                                    
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       79.21250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 62550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     TYR A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     GLY A   501                                                      
REMARK 465     PRO A   502                                                      
REMARK 465     VAL A   503                                                      
REMARK 465     CYS A   504                                                      
REMARK 465     GLU A   505                                                      
REMARK 465     VAL A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     VAL A   508                                                      
REMARK 465     THR A   509                                                      
REMARK 465     PRO A   510                                                      
REMARK 465     LYS A   511                                                      
REMARK 465     THR A   512                                                      
REMARK 465     VAL A   513                                                      
REMARK 465     THR A   514                                                      
REMARK 465     PRO A   515                                                      
REMARK 465     ALA A   516                                                      
REMARK 465     SER A   517                                                      
REMARK 465     SER A   518                                                      
REMARK 465     ALA A   519                                                      
REMARK 465     LYS A   520                                                      
REMARK 465     THR A   521                                                      
REMARK 465     SER A   522                                                      
REMARK 465     PRO A   523                                                      
REMARK 465     ALA A   524                                                      
REMARK 465     LYS A   525                                                      
REMARK 465     GLN A   526                                                      
REMARK 465     GLN A   527                                                      
REMARK 465     ALA A   528                                                      
REMARK 465     PRO A   529                                                      
REMARK 465     PRO A   530                                                      
REMARK 465     VAL A   531                                                      
REMARK 465     ARG A   532                                                      
REMARK 465     MET B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     TYR B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     ILE B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     VAL B   508                                                      
REMARK 465     THR B   509                                                      
REMARK 465     PRO B   510                                                      
REMARK 465     LYS B   511                                                      
REMARK 465     THR B   512                                                      
REMARK 465     VAL B   513                                                      
REMARK 465     THR B   514                                                      
REMARK 465     PRO B   515                                                      
REMARK 465     ALA B   516                                                      
REMARK 465     SER B   517                                                      
REMARK 465     SER B   518                                                      
REMARK 465     ALA B   519                                                      
REMARK 465     LYS B   520                                                      
REMARK 465     THR B   521                                                      
REMARK 465     SER B   522                                                      
REMARK 465     PRO B   523                                                      
REMARK 465     ALA B   524                                                      
REMARK 465     LYS B   525                                                      
REMARK 465     GLN B   526                                                      
REMARK 465     GLN B   527                                                      
REMARK 465     ALA B   528                                                      
REMARK 465     PRO B   529                                                      
REMARK 465     PRO B   530                                                      
REMARK 465     VAL B   531                                                      
REMARK 465     ARG B   532                                                      
REMARK 465     MET C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     TYR C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     LYS C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     ASN C     8                                                      
REMARK 465     ILE C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ARG C    11                                                      
REMARK 465     ILE C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     LEU C   498                                                      
REMARK 465     TYR C   499                                                      
REMARK 465     ASP C   500                                                      
REMARK 465     GLY C   501                                                      
REMARK 465     PRO C   502                                                      
REMARK 465     VAL C   503                                                      
REMARK 465     CYS C   504                                                      
REMARK 465     GLU C   505                                                      
REMARK 465     VAL C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     VAL C   508                                                      
REMARK 465     THR C   509                                                      
REMARK 465     PRO C   510                                                      
REMARK 465     LYS C   511                                                      
REMARK 465     THR C   512                                                      
REMARK 465     VAL C   513                                                      
REMARK 465     THR C   514                                                      
REMARK 465     PRO C   515                                                      
REMARK 465     ALA C   516                                                      
REMARK 465     SER C   517                                                      
REMARK 465     SER C   518                                                      
REMARK 465     ALA C   519                                                      
REMARK 465     LYS C   520                                                      
REMARK 465     THR C   521                                                      
REMARK 465     SER C   522                                                      
REMARK 465     PRO C   523                                                      
REMARK 465     ALA C   524                                                      
REMARK 465     LYS C   525                                                      
REMARK 465     GLN C   526                                                      
REMARK 465     GLN C   527                                                      
REMARK 465     ALA C   528                                                      
REMARK 465     PRO C   529                                                      
REMARK 465     PRO C   530                                                      
REMARK 465     VAL C   531                                                      
REMARK 465     ARG C   532                                                      
REMARK 465     MET D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     TYR D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     ASN D     8                                                      
REMARK 465     ILE D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     ARG D    11                                                      
REMARK 465     ILE D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     GLY D   497                                                      
REMARK 465     LEU D   498                                                      
REMARK 465     TYR D   499                                                      
REMARK 465     ASP D   500                                                      
REMARK 465     GLY D   501                                                      
REMARK 465     PRO D   502                                                      
REMARK 465     VAL D   503                                                      
REMARK 465     CYS D   504                                                      
REMARK 465     GLU D   505                                                      
REMARK 465     VAL D   506                                                      
REMARK 465     SER D   507                                                      
REMARK 465     VAL D   508                                                      
REMARK 465     THR D   509                                                      
REMARK 465     PRO D   510                                                      
REMARK 465     LYS D   511                                                      
REMARK 465     THR D   512                                                      
REMARK 465     VAL D   513                                                      
REMARK 465     THR D   514                                                      
REMARK 465     PRO D   515                                                      
REMARK 465     ALA D   516                                                      
REMARK 465     SER D   517                                                      
REMARK 465     SER D   518                                                      
REMARK 465     ALA D   519                                                      
REMARK 465     LYS D   520                                                      
REMARK 465     THR D   521                                                      
REMARK 465     SER D   522                                                      
REMARK 465     PRO D   523                                                      
REMARK 465     ALA D   524                                                      
REMARK 465     LYS D   525                                                      
REMARK 465     GLN D   526                                                      
REMARK 465     GLN D   527                                                      
REMARK 465     ALA D   528                                                      
REMARK 465     PRO D   529                                                      
REMARK 465     PRO D   530                                                      
REMARK 465     VAL D   531                                                      
REMARK 465     ARG D   532                                                      
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     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     GLU A 490    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 492    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 498    CG   CD1  CD2                                       
REMARK 470     THR B  13    OG1  CG2                                            
REMARK 470     SER B  14    OG                                                  
REMARK 470     ASP B  15    CG   OD1  OD2                                       
REMARK 470     GLU B  47    CG   CD   OE1  OE2                                  
REMARK 470     ASN B  48    CG   OD1  ND2                                       
REMARK 470     ILE B  50    CG1  CG2  CD1                                       
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     GLU B 490    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 492    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 505    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  15    CG   OD1  OD2                                       
REMARK 470     ILE C  50    CG1  CG2  CD1                                       
REMARK 470     GLN C  81    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 146    CG   CD   CE   NZ                                   
REMARK 470     GLU C 490    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 491    CG   CD1  CD2                                       
REMARK 470     ARG C 492    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D  14    OG                                                  
REMARK 470     ASP D  15    CG   OD1  OD2                                       
REMARK 470     ILE D  50    CG1  CG2  CD1                                       
REMARK 470     GLN D  81    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 146    CG   CD   CE   NZ                                   
REMARK 470     GLU D 490    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 491    CG   CD1  CD2                                       
REMARK 470     ARG D 492    CG   CD   NE   CZ   NH1  NH2                        
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    PRO A 305   C   -  N   -  CD  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    PRO B 305   C   -  N   -  CD  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PRO C 305   C   -  N   -  CD  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    PRO D 305   C   -  N   -  CD  ANGL. DEV. =  14.5 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    GLN A  77       39.42     39.44                                   
REMARK 500    PHE A 170       63.36     65.43                                   
REMARK 500    ARG A 173      -73.19   -136.42                                   
REMARK 500    CYS A 334       76.67   -152.33                                   
REMARK 500    ASN A 347      101.94   -167.63                                   
REMARK 500    SER A 385      -51.24   -146.06                                   
REMARK 500    ASN A 393       36.26     70.46                                   
REMARK 500    ASN A 426       59.36    -92.05                                   
REMARK 500    GLU A 490      106.58    -56.11                                   
REMARK 500    ASP B  15      171.36     69.37                                   
REMARK 500    GLN B  77       40.79     35.76                                   
REMARK 500    PHE B 170       65.49     61.89                                   
REMARK 500    ARG B 173      -72.81   -136.75                                   
REMARK 500    CYS B 334       76.87   -152.48                                   
REMARK 500    ASN B 347      102.24   -168.38                                   
REMARK 500    SER B 385      -51.28   -144.36                                   
REMARK 500    ASN B 426       58.17    -91.68                                   
REMARK 500    ARG B 492      -65.02    -93.17                                   
REMARK 500    PHE C 170       64.55     63.25                                   
REMARK 500    ARG C 173      -74.62   -138.23                                   
REMARK 500    CYS C 334       75.25   -150.62                                   
REMARK 500    ASN C 347      102.42   -167.01                                   
REMARK 500    SER C 385      -52.18   -145.27                                   
REMARK 500    ASN C 393       38.30     70.44                                   
REMARK 500    ASN C 426       58.70    -91.54                                   
REMARK 500    GLU C 490       67.80   -119.14                                   
REMARK 500    GLN D  77       39.19     37.70                                   
REMARK 500    PHE D 170       65.41     63.99                                   
REMARK 500    ARG D 173      -73.18   -138.42                                   
REMARK 500    CYS D 334       75.07   -152.22                                   
REMARK 500    ASN D 347      102.89   -166.22                                   
REMARK 500    SER D 385      -51.97   -146.42                                   
REMARK 500    ASN D 393       39.68     70.16                                   
REMARK 500    ASN D 426       58.45    -90.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 601                 
DBREF  6JV9 A    1   532  UNP    Q16555   DPYL2_HUMAN      1    532             
DBREF  6JV9 B    1   532  UNP    Q16555   DPYL2_HUMAN      1    532             
DBREF  6JV9 C    1   532  UNP    Q16555   DPYL2_HUMAN      1    532             
DBREF  6JV9 D    1   532  UNP    Q16555   DPYL2_HUMAN      1    532             
SEQADV 6JV9 MET A   -7  UNP  Q16555              INITIATING METHIONINE          
SEQADV 6JV9 HIS A   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS A   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS A   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS A   -3  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS A   -2  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS A   -1  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS A    0  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 MET B   -7  UNP  Q16555              INITIATING METHIONINE          
SEQADV 6JV9 HIS B   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS B   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS B   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS B   -3  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS B   -2  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS B   -1  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS B    0  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 MET C   -7  UNP  Q16555              INITIATING METHIONINE          
SEQADV 6JV9 HIS C   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS C   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS C   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS C   -3  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS C   -2  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS C   -1  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS C    0  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 MET D   -7  UNP  Q16555              INITIATING METHIONINE          
SEQADV 6JV9 HIS D   -6  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS D   -5  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS D   -4  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS D   -3  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS D   -2  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS D   -1  UNP  Q16555              EXPRESSION TAG                 
SEQADV 6JV9 HIS D    0  UNP  Q16555              EXPRESSION TAG                 
SEQRES   1 A  540  MET HIS HIS HIS HIS HIS HIS HIS MET SER TYR GLN GLY          
SEQRES   2 A  540  LYS LYS ASN ILE PRO ARG ILE THR SER ASP ARG LEU LEU          
SEQRES   3 A  540  ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP GLN SER PHE          
SEQRES   4 A  540  TYR ALA ASP ILE TYR MET GLU ASP GLY LEU ILE LYS GLN          
SEQRES   5 A  540  ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY VAL LYS THR          
SEQRES   6 A  540  ILE GLU ALA HIS SER ARG MET VAL ILE PRO GLY GLY ILE          
SEQRES   7 A  540  ASP VAL HIS THR ARG PHE GLN MET PRO ASP GLN GLY MET          
SEQRES   8 A  540  THR SER ALA ASP ASP PHE PHE GLN GLY THR LYS ALA ALA          
SEQRES   9 A  540  LEU ALA GLY GLY THR THR MET ILE ILE ASP HIS VAL VAL          
SEQRES  10 A  540  PRO GLU PRO GLY THR SER LEU LEU ALA ALA PHE ASP GLN          
SEQRES  11 A  540  TRP ARG GLU TRP ALA ASP SER LYS SER CYS CYS ASP TYR          
SEQRES  12 A  540  SER LEU HIS VAL ASP ILE SER GLU TRP HIS LYS GLY ILE          
SEQRES  13 A  540  GLN GLU GLU MET GLU ALA LEU VAL LYS ASP HIS GLY VAL          
SEQRES  14 A  540  ASN SER PHE LEU VAL TYR MET ALA PHE LYS ASP ARG PHE          
SEQRES  15 A  540  GLN LEU THR ASP CYS GLN ILE TYR GLU VAL LEU SER VAL          
SEQRES  16 A  540  ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL HIS ALA GLU          
SEQRES  17 A  540  ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN ARG ILE LEU          
SEQRES  18 A  540  ASP LEU GLY ILE THR GLY PRO GLU GLY HIS VAL LEU SER          
SEQRES  19 A  540  ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL ASN ARG ALA          
SEQRES  20 A  540  ILE THR ILE ALA ASN GLN THR ASN CYS PRO LEU TYR ILE          
SEQRES  21 A  540  THR LYS VAL MET SER LYS SER SER ALA GLU VAL ILE ALA          
SEQRES  22 A  540  GLN ALA ARG LYS LYS GLY THR VAL VAL TYR GLY GLU PRO          
SEQRES  23 A  540  ILE THR ALA SER LEU GLY THR ASP GLY SER HIS TYR TRP          
SEQRES  24 A  540  SER LYS ASN TRP ALA LYS ALA ALA ALA PHE VAL THR SER          
SEQRES  25 A  540  PRO PRO LEU SER PRO ASP PRO THR THR PRO ASP PHE LEU          
SEQRES  26 A  540  ASN SER LEU LEU SER CYS GLY ASP LEU GLN VAL THR GLY          
SEQRES  27 A  540  SER ALA HIS CYS THR PHE ASN THR ALA GLN LYS ALA VAL          
SEQRES  28 A  540  GLY LYS ASP ASN PHE THR LEU ILE PRO GLU GLY THR ASN          
SEQRES  29 A  540  GLY THR GLU GLU ARG MET SER VAL ILE TRP ASP LYS ALA          
SEQRES  30 A  540  VAL VAL THR GLY LYS MET ASP GLU ASN GLN PHE VAL ALA          
SEQRES  31 A  540  VAL THR SER THR ASN ALA ALA LYS VAL PHE ASN LEU TYR          
SEQRES  32 A  540  PRO ARG LYS GLY ARG ILE ALA VAL GLY SER ASP ALA ASP          
SEQRES  33 A  540  LEU VAL ILE TRP ASP PRO ASP SER VAL LYS THR ILE SER          
SEQRES  34 A  540  ALA LYS THR HIS ASN SER SER LEU GLU TYR ASN ILE PHE          
SEQRES  35 A  540  GLU GLY MET GLU CYS ARG GLY SER PRO LEU VAL VAL ILE          
SEQRES  36 A  540  SER GLN GLY LYS ILE VAL LEU GLU ASP GLY THR LEU HIS          
SEQRES  37 A  540  VAL THR GLU GLY SER GLY ARG TYR ILE PRO ARG LYS PRO          
SEQRES  38 A  540  PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS ALA ARG SER          
SEQRES  39 A  540  ARG LEU ALA GLU LEU ARG GLY VAL PRO ARG GLY LEU TYR          
SEQRES  40 A  540  ASP GLY PRO VAL CYS GLU VAL SER VAL THR PRO LYS THR          
SEQRES  41 A  540  VAL THR PRO ALA SER SER ALA LYS THR SER PRO ALA LYS          
SEQRES  42 A  540  GLN GLN ALA PRO PRO VAL ARG                                  
SEQRES   1 B  540  MET HIS HIS HIS HIS HIS HIS HIS MET SER TYR GLN GLY          
SEQRES   2 B  540  LYS LYS ASN ILE PRO ARG ILE THR SER ASP ARG LEU LEU          
SEQRES   3 B  540  ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP GLN SER PHE          
SEQRES   4 B  540  TYR ALA ASP ILE TYR MET GLU ASP GLY LEU ILE LYS GLN          
SEQRES   5 B  540  ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY VAL LYS THR          
SEQRES   6 B  540  ILE GLU ALA HIS SER ARG MET VAL ILE PRO GLY GLY ILE          
SEQRES   7 B  540  ASP VAL HIS THR ARG PHE GLN MET PRO ASP GLN GLY MET          
SEQRES   8 B  540  THR SER ALA ASP ASP PHE PHE GLN GLY THR LYS ALA ALA          
SEQRES   9 B  540  LEU ALA GLY GLY THR THR MET ILE ILE ASP HIS VAL VAL          
SEQRES  10 B  540  PRO GLU PRO GLY THR SER LEU LEU ALA ALA PHE ASP GLN          
SEQRES  11 B  540  TRP ARG GLU TRP ALA ASP SER LYS SER CYS CYS ASP TYR          
SEQRES  12 B  540  SER LEU HIS VAL ASP ILE SER GLU TRP HIS LYS GLY ILE          
SEQRES  13 B  540  GLN GLU GLU MET GLU ALA LEU VAL LYS ASP HIS GLY VAL          
SEQRES  14 B  540  ASN SER PHE LEU VAL TYR MET ALA PHE LYS ASP ARG PHE          
SEQRES  15 B  540  GLN LEU THR ASP CYS GLN ILE TYR GLU VAL LEU SER VAL          
SEQRES  16 B  540  ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL HIS ALA GLU          
SEQRES  17 B  540  ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN ARG ILE LEU          
SEQRES  18 B  540  ASP LEU GLY ILE THR GLY PRO GLU GLY HIS VAL LEU SER          
SEQRES  19 B  540  ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL ASN ARG ALA          
SEQRES  20 B  540  ILE THR ILE ALA ASN GLN THR ASN CYS PRO LEU TYR ILE          
SEQRES  21 B  540  THR LYS VAL MET SER LYS SER SER ALA GLU VAL ILE ALA          
SEQRES  22 B  540  GLN ALA ARG LYS LYS GLY THR VAL VAL TYR GLY GLU PRO          
SEQRES  23 B  540  ILE THR ALA SER LEU GLY THR ASP GLY SER HIS TYR TRP          
SEQRES  24 B  540  SER LYS ASN TRP ALA LYS ALA ALA ALA PHE VAL THR SER          
SEQRES  25 B  540  PRO PRO LEU SER PRO ASP PRO THR THR PRO ASP PHE LEU          
SEQRES  26 B  540  ASN SER LEU LEU SER CYS GLY ASP LEU GLN VAL THR GLY          
SEQRES  27 B  540  SER ALA HIS CYS THR PHE ASN THR ALA GLN LYS ALA VAL          
SEQRES  28 B  540  GLY LYS ASP ASN PHE THR LEU ILE PRO GLU GLY THR ASN          
SEQRES  29 B  540  GLY THR GLU GLU ARG MET SER VAL ILE TRP ASP LYS ALA          
SEQRES  30 B  540  VAL VAL THR GLY LYS MET ASP GLU ASN GLN PHE VAL ALA          
SEQRES  31 B  540  VAL THR SER THR ASN ALA ALA LYS VAL PHE ASN LEU TYR          
SEQRES  32 B  540  PRO ARG LYS GLY ARG ILE ALA VAL GLY SER ASP ALA ASP          
SEQRES  33 B  540  LEU VAL ILE TRP ASP PRO ASP SER VAL LYS THR ILE SER          
SEQRES  34 B  540  ALA LYS THR HIS ASN SER SER LEU GLU TYR ASN ILE PHE          
SEQRES  35 B  540  GLU GLY MET GLU CYS ARG GLY SER PRO LEU VAL VAL ILE          
SEQRES  36 B  540  SER GLN GLY LYS ILE VAL LEU GLU ASP GLY THR LEU HIS          
SEQRES  37 B  540  VAL THR GLU GLY SER GLY ARG TYR ILE PRO ARG LYS PRO          
SEQRES  38 B  540  PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS ALA ARG SER          
SEQRES  39 B  540  ARG LEU ALA GLU LEU ARG GLY VAL PRO ARG GLY LEU TYR          
SEQRES  40 B  540  ASP GLY PRO VAL CYS GLU VAL SER VAL THR PRO LYS THR          
SEQRES  41 B  540  VAL THR PRO ALA SER SER ALA LYS THR SER PRO ALA LYS          
SEQRES  42 B  540  GLN GLN ALA PRO PRO VAL ARG                                  
SEQRES   1 C  540  MET HIS HIS HIS HIS HIS HIS HIS MET SER TYR GLN GLY          
SEQRES   2 C  540  LYS LYS ASN ILE PRO ARG ILE THR SER ASP ARG LEU LEU          
SEQRES   3 C  540  ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP GLN SER PHE          
SEQRES   4 C  540  TYR ALA ASP ILE TYR MET GLU ASP GLY LEU ILE LYS GLN          
SEQRES   5 C  540  ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY VAL LYS THR          
SEQRES   6 C  540  ILE GLU ALA HIS SER ARG MET VAL ILE PRO GLY GLY ILE          
SEQRES   7 C  540  ASP VAL HIS THR ARG PHE GLN MET PRO ASP GLN GLY MET          
SEQRES   8 C  540  THR SER ALA ASP ASP PHE PHE GLN GLY THR LYS ALA ALA          
SEQRES   9 C  540  LEU ALA GLY GLY THR THR MET ILE ILE ASP HIS VAL VAL          
SEQRES  10 C  540  PRO GLU PRO GLY THR SER LEU LEU ALA ALA PHE ASP GLN          
SEQRES  11 C  540  TRP ARG GLU TRP ALA ASP SER LYS SER CYS CYS ASP TYR          
SEQRES  12 C  540  SER LEU HIS VAL ASP ILE SER GLU TRP HIS LYS GLY ILE          
SEQRES  13 C  540  GLN GLU GLU MET GLU ALA LEU VAL LYS ASP HIS GLY VAL          
SEQRES  14 C  540  ASN SER PHE LEU VAL TYR MET ALA PHE LYS ASP ARG PHE          
SEQRES  15 C  540  GLN LEU THR ASP CYS GLN ILE TYR GLU VAL LEU SER VAL          
SEQRES  16 C  540  ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL HIS ALA GLU          
SEQRES  17 C  540  ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN ARG ILE LEU          
SEQRES  18 C  540  ASP LEU GLY ILE THR GLY PRO GLU GLY HIS VAL LEU SER          
SEQRES  19 C  540  ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL ASN ARG ALA          
SEQRES  20 C  540  ILE THR ILE ALA ASN GLN THR ASN CYS PRO LEU TYR ILE          
SEQRES  21 C  540  THR LYS VAL MET SER LYS SER SER ALA GLU VAL ILE ALA          
SEQRES  22 C  540  GLN ALA ARG LYS LYS GLY THR VAL VAL TYR GLY GLU PRO          
SEQRES  23 C  540  ILE THR ALA SER LEU GLY THR ASP GLY SER HIS TYR TRP          
SEQRES  24 C  540  SER LYS ASN TRP ALA LYS ALA ALA ALA PHE VAL THR SER          
SEQRES  25 C  540  PRO PRO LEU SER PRO ASP PRO THR THR PRO ASP PHE LEU          
SEQRES  26 C  540  ASN SER LEU LEU SER CYS GLY ASP LEU GLN VAL THR GLY          
SEQRES  27 C  540  SER ALA HIS CYS THR PHE ASN THR ALA GLN LYS ALA VAL          
SEQRES  28 C  540  GLY LYS ASP ASN PHE THR LEU ILE PRO GLU GLY THR ASN          
SEQRES  29 C  540  GLY THR GLU GLU ARG MET SER VAL ILE TRP ASP LYS ALA          
SEQRES  30 C  540  VAL VAL THR GLY LYS MET ASP GLU ASN GLN PHE VAL ALA          
SEQRES  31 C  540  VAL THR SER THR ASN ALA ALA LYS VAL PHE ASN LEU TYR          
SEQRES  32 C  540  PRO ARG LYS GLY ARG ILE ALA VAL GLY SER ASP ALA ASP          
SEQRES  33 C  540  LEU VAL ILE TRP ASP PRO ASP SER VAL LYS THR ILE SER          
SEQRES  34 C  540  ALA LYS THR HIS ASN SER SER LEU GLU TYR ASN ILE PHE          
SEQRES  35 C  540  GLU GLY MET GLU CYS ARG GLY SER PRO LEU VAL VAL ILE          
SEQRES  36 C  540  SER GLN GLY LYS ILE VAL LEU GLU ASP GLY THR LEU HIS          
SEQRES  37 C  540  VAL THR GLU GLY SER GLY ARG TYR ILE PRO ARG LYS PRO          
SEQRES  38 C  540  PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS ALA ARG SER          
SEQRES  39 C  540  ARG LEU ALA GLU LEU ARG GLY VAL PRO ARG GLY LEU TYR          
SEQRES  40 C  540  ASP GLY PRO VAL CYS GLU VAL SER VAL THR PRO LYS THR          
SEQRES  41 C  540  VAL THR PRO ALA SER SER ALA LYS THR SER PRO ALA LYS          
SEQRES  42 C  540  GLN GLN ALA PRO PRO VAL ARG                                  
SEQRES   1 D  540  MET HIS HIS HIS HIS HIS HIS HIS MET SER TYR GLN GLY          
SEQRES   2 D  540  LYS LYS ASN ILE PRO ARG ILE THR SER ASP ARG LEU LEU          
SEQRES   3 D  540  ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP GLN SER PHE          
SEQRES   4 D  540  TYR ALA ASP ILE TYR MET GLU ASP GLY LEU ILE LYS GLN          
SEQRES   5 D  540  ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY VAL LYS THR          
SEQRES   6 D  540  ILE GLU ALA HIS SER ARG MET VAL ILE PRO GLY GLY ILE          
SEQRES   7 D  540  ASP VAL HIS THR ARG PHE GLN MET PRO ASP GLN GLY MET          
SEQRES   8 D  540  THR SER ALA ASP ASP PHE PHE GLN GLY THR LYS ALA ALA          
SEQRES   9 D  540  LEU ALA GLY GLY THR THR MET ILE ILE ASP HIS VAL VAL          
SEQRES  10 D  540  PRO GLU PRO GLY THR SER LEU LEU ALA ALA PHE ASP GLN          
SEQRES  11 D  540  TRP ARG GLU TRP ALA ASP SER LYS SER CYS CYS ASP TYR          
SEQRES  12 D  540  SER LEU HIS VAL ASP ILE SER GLU TRP HIS LYS GLY ILE          
SEQRES  13 D  540  GLN GLU GLU MET GLU ALA LEU VAL LYS ASP HIS GLY VAL          
SEQRES  14 D  540  ASN SER PHE LEU VAL TYR MET ALA PHE LYS ASP ARG PHE          
SEQRES  15 D  540  GLN LEU THR ASP CYS GLN ILE TYR GLU VAL LEU SER VAL          
SEQRES  16 D  540  ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL HIS ALA GLU          
SEQRES  17 D  540  ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN ARG ILE LEU          
SEQRES  18 D  540  ASP LEU GLY ILE THR GLY PRO GLU GLY HIS VAL LEU SER          
SEQRES  19 D  540  ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL ASN ARG ALA          
SEQRES  20 D  540  ILE THR ILE ALA ASN GLN THR ASN CYS PRO LEU TYR ILE          
SEQRES  21 D  540  THR LYS VAL MET SER LYS SER SER ALA GLU VAL ILE ALA          
SEQRES  22 D  540  GLN ALA ARG LYS LYS GLY THR VAL VAL TYR GLY GLU PRO          
SEQRES  23 D  540  ILE THR ALA SER LEU GLY THR ASP GLY SER HIS TYR TRP          
SEQRES  24 D  540  SER LYS ASN TRP ALA LYS ALA ALA ALA PHE VAL THR SER          
SEQRES  25 D  540  PRO PRO LEU SER PRO ASP PRO THR THR PRO ASP PHE LEU          
SEQRES  26 D  540  ASN SER LEU LEU SER CYS GLY ASP LEU GLN VAL THR GLY          
SEQRES  27 D  540  SER ALA HIS CYS THR PHE ASN THR ALA GLN LYS ALA VAL          
SEQRES  28 D  540  GLY LYS ASP ASN PHE THR LEU ILE PRO GLU GLY THR ASN          
SEQRES  29 D  540  GLY THR GLU GLU ARG MET SER VAL ILE TRP ASP LYS ALA          
SEQRES  30 D  540  VAL VAL THR GLY LYS MET ASP GLU ASN GLN PHE VAL ALA          
SEQRES  31 D  540  VAL THR SER THR ASN ALA ALA LYS VAL PHE ASN LEU TYR          
SEQRES  32 D  540  PRO ARG LYS GLY ARG ILE ALA VAL GLY SER ASP ALA ASP          
SEQRES  33 D  540  LEU VAL ILE TRP ASP PRO ASP SER VAL LYS THR ILE SER          
SEQRES  34 D  540  ALA LYS THR HIS ASN SER SER LEU GLU TYR ASN ILE PHE          
SEQRES  35 D  540  GLU GLY MET GLU CYS ARG GLY SER PRO LEU VAL VAL ILE          
SEQRES  36 D  540  SER GLN GLY LYS ILE VAL LEU GLU ASP GLY THR LEU HIS          
SEQRES  37 D  540  VAL THR GLU GLY SER GLY ARG TYR ILE PRO ARG LYS PRO          
SEQRES  38 D  540  PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS ALA ARG SER          
SEQRES  39 D  540  ARG LEU ALA GLU LEU ARG GLY VAL PRO ARG GLY LEU TYR          
SEQRES  40 D  540  ASP GLY PRO VAL CYS GLU VAL SER VAL THR PRO LYS THR          
SEQRES  41 D  540  VAL THR PRO ALA SER SER ALA LYS THR SER PRO ALA LYS          
SEQRES  42 D  540  GLN GLN ALA PRO PRO VAL ARG                                  
HET    SO4  A 601       5                                                       
HET    DTT  B 601       8                                                       
HET    SO4  B 602       5                                                       
HET    EDO  C 601       4                                                       
HET    PGE  D 601      10                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   6  DTT    C4 H10 O2 S2                                                 
FORMUL   8  EDO    C2 H6 O2                                                     
FORMUL   9  PGE    C6 H14 O4                                                    
FORMUL  10  HOH   *571(H2 O)                                                    
HELIX    1 AA1 ASP A   88  GLY A   99  1                                  12    
HELIX    2 AA2 SER A  115  SER A  131  1                                  17    
HELIX    3 AA3 GLY A  147  HIS A  159  1                                  13    
HELIX    4 AA4 THR A  177  GLY A  192  1                                  16    
HELIX    5 AA5 ASN A  201  LEU A  215  1                                  15    
HELIX    6 AA6 PRO A  220  SER A  226  1                                   7    
HELIX    7 AA7 PRO A  228  ASN A  247  1                                  20    
HELIX    8 AA8 SER A  257  LYS A  270  1                                  14    
HELIX    9 AA9 ILE A  279  THR A  285  1                                   7    
HELIX   10 AB1 ASP A  286  SER A  292  5                                   7    
HELIX   11 AB2 ASN A  294  PHE A  301  1                                   8    
HELIX   12 AB3 THR A  312  CYS A  323  1                                  12    
HELIX   13 AB4 ASN A  337  ALA A  342  1                                   6    
HELIX   14 AB5 VAL A  343  LYS A  345  5                                   3    
HELIX   15 AB6 ASN A  347  ILE A  351  5                                   5    
HELIX   16 AB7 GLU A  360  VAL A  370  1                                  11    
HELIX   17 AB8 ASP A  376  SER A  385  1                                  10    
HELIX   18 AB9 SER A  385  PHE A  392  1                                   8    
HELIX   19 AC1 PRO A  475  ALA A  489  1                                  15    
HELIX   20 AC2 ASP B   88  GLY B   99  1                                  12    
HELIX   21 AC3 SER B  115  SER B  131  1                                  17    
HELIX   22 AC4 GLY B  147  HIS B  159  1                                  13    
HELIX   23 AC5 THR B  177  GLY B  192  1                                  16    
HELIX   24 AC6 ASN B  201  LEU B  215  1                                  15    
HELIX   25 AC7 GLY B  219  SER B  226  1                                   8    
HELIX   26 AC8 PRO B  228  ASN B  247  1                                  20    
HELIX   27 AC9 SER B  257  LYS B  270  1                                  14    
HELIX   28 AD1 ILE B  279  THR B  285  1                                   7    
HELIX   29 AD2 ASP B  286  SER B  292  5                                   7    
HELIX   30 AD3 ASN B  294  PHE B  301  1                                   8    
HELIX   31 AD4 THR B  312  CYS B  323  1                                  12    
HELIX   32 AD5 ASN B  337  ALA B  342  1                                   6    
HELIX   33 AD6 VAL B  343  LYS B  345  5                                   3    
HELIX   34 AD7 ASN B  347  ILE B  351  5                                   5    
HELIX   35 AD8 GLU B  360  VAL B  370  1                                  11    
HELIX   36 AD9 ASP B  376  SER B  385  1                                  10    
HELIX   37 AE1 SER B  385  PHE B  392  1                                   8    
HELIX   38 AE2 PRO B  475  LEU B  488  1                                  14    
HELIX   39 AE3 ASP C   88  GLY C   99  1                                  12    
HELIX   40 AE4 SER C  115  SER C  131  1                                  17    
HELIX   41 AE5 GLY C  147  HIS C  159  1                                  13    
HELIX   42 AE6 THR C  177  GLY C  192  1                                  16    
HELIX   43 AE7 ASN C  201  LEU C  215  1                                  15    
HELIX   44 AE8 GLY C  219  SER C  226  1                                   8    
HELIX   45 AE9 PRO C  228  ASN C  247  1                                  20    
HELIX   46 AF1 SER C  257  LYS C  270  1                                  14    
HELIX   47 AF2 ILE C  279  THR C  285  1                                   7    
HELIX   48 AF3 ASP C  286  SER C  292  5                                   7    
HELIX   49 AF4 ASN C  294  PHE C  301  1                                   8    
HELIX   50 AF5 THR C  312  CYS C  323  1                                  12    
HELIX   51 AF6 ASN C  337  ALA C  342  1                                   6    
HELIX   52 AF7 VAL C  343  LYS C  345  5                                   3    
HELIX   53 AF8 ASN C  347  ILE C  351  5                                   5    
HELIX   54 AF9 GLU C  360  VAL C  370  1                                  11    
HELIX   55 AG1 ASP C  376  SER C  385  1                                  10    
HELIX   56 AG2 SER C  385  PHE C  392  1                                   8    
HELIX   57 AG3 PRO C  475  ALA C  489  1                                  15    
HELIX   58 AG4 ASP D   88  GLY D   99  1                                  12    
HELIX   59 AG5 SER D  115  SER D  131  1                                  17    
HELIX   60 AG6 GLY D  147  HIS D  159  1                                  13    
HELIX   61 AG7 THR D  177  GLY D  192  1                                  16    
HELIX   62 AG8 ASN D  201  LEU D  215  1                                  15    
HELIX   63 AG9 GLY D  219  SER D  226  1                                   8    
HELIX   64 AH1 PRO D  228  ASN D  247  1                                  20    
HELIX   65 AH2 SER D  257  LYS D  270  1                                  14    
HELIX   66 AH3 ILE D  279  THR D  285  1                                   7    
HELIX   67 AH4 ASP D  286  SER D  292  5                                   7    
HELIX   68 AH5 ASN D  294  PHE D  301  1                                   8    
HELIX   69 AH6 THR D  312  CYS D  323  1                                  12    
HELIX   70 AH7 ASN D  337  ALA D  342  1                                   6    
HELIX   71 AH8 VAL D  343  LYS D  345  5                                   3    
HELIX   72 AH9 ASN D  347  ILE D  351  5                                   5    
HELIX   73 AI1 GLU D  360  VAL D  370  1                                  11    
HELIX   74 AI2 ASP D  376  SER D  385  1                                  10    
HELIX   75 AI3 SER D  385  PHE D  392  1                                   8    
HELIX   76 AI4 PRO D  475  LEU D  488  1                                  14    
SHEET    1 AA1 4 LEU A  41  GLY A  46  0                                        
SHEET    2 AA1 4 SER A  30  GLU A  38 -1  N  ASP A  34   O  GLY A  46           
SHEET    3 AA1 4 ARG A  16  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4 AA1 4 LYS A  56  GLU A  59  1  O  ILE A  58   N  LYS A  20           
SHEET    1 AA2 8 LEU A  41  GLY A  46  0                                        
SHEET    2 AA2 8 SER A  30  GLU A  38 -1  N  ASP A  34   O  GLY A  46           
SHEET    3 AA2 8 ARG A  16  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4 AA2 8 MET A  64  PRO A  67  1  O  VAL A  65   N  LYS A  23           
SHEET    5 AA2 8 LEU A 409  THR A 419 -1  O  VAL A 410   N  ILE A  66           
SHEET    6 AA2 8 GLU A 438  SER A 448 -1  O  CYS A 439   N  LYS A 418           
SHEET    7 AA2 8 LYS A 451  GLU A 455 -1  O  VAL A 453   N  VAL A 446           
SHEET    8 AA2 8 THR A 458  LEU A 459 -1  O  THR A 458   N  GLU A 455           
SHEET    1 AA3 7 GLY A  69  THR A  74  0                                        
SHEET    2 AA3 7 THR A 101  VAL A 108  1  O  MET A 103   N  ASP A  71           
SHEET    3 AA3 7 ASP A 134  ASP A 140  1  O  HIS A 138   N  VAL A 108           
SHEET    4 AA3 7 SER A 163  TYR A 167  1  O  SER A 163   N  VAL A 139           
SHEET    5 AA3 7 ILE A 194  HIS A 198  1  O  GLN A 196   N  PHE A 164           
SHEET    6 AA3 7 LEU A 250  VAL A 255  1  O  TYR A 251   N  ALA A 195           
SHEET    7 AA3 7 VAL A 274  PRO A 278  1  O  TYR A 275   N  ILE A 252           
SHEET    1 AA4 2 PRO A  79  ASP A  80  0                                        
SHEET    2 AA4 2 MET A  83  THR A  84 -1  O  MET A  83   N  ASP A  80           
SHEET    1 AA5 4 LEU B  41  GLY B  46  0                                        
SHEET    2 AA5 4 SER B  30  GLU B  38 -1  N  ASP B  34   O  GLY B  46           
SHEET    3 AA5 4 ARG B  16  VAL B  25 -1  N  LEU B  17   O  MET B  37           
SHEET    4 AA5 4 THR B  57  GLU B  59  1  O  ILE B  58   N  LYS B  20           
SHEET    1 AA6 8 LEU B  41  GLY B  46  0                                        
SHEET    2 AA6 8 SER B  30  GLU B  38 -1  N  ASP B  34   O  GLY B  46           
SHEET    3 AA6 8 ARG B  16  VAL B  25 -1  N  LEU B  17   O  MET B  37           
SHEET    4 AA6 8 MET B  64  PRO B  67  1  O  VAL B  65   N  LYS B  23           
SHEET    5 AA6 8 LEU B 409  THR B 419 -1  O  VAL B 410   N  ILE B  66           
SHEET    6 AA6 8 GLU B 438  SER B 448 -1  O  ILE B 447   N  LEU B 409           
SHEET    7 AA6 8 LYS B 451  GLU B 455 -1  O  VAL B 453   N  VAL B 446           
SHEET    8 AA6 8 THR B 458  LEU B 459 -1  O  THR B 458   N  GLU B 455           
SHEET    1 AA7 7 GLY B  69  THR B  74  0                                        
SHEET    2 AA7 7 THR B 101  VAL B 108  1  O  MET B 103   N  ASP B  71           
SHEET    3 AA7 7 ASP B 134  ASP B 140  1  O  HIS B 138   N  ASP B 106           
SHEET    4 AA7 7 SER B 163  TYR B 167  1  O  SER B 163   N  VAL B 139           
SHEET    5 AA7 7 ILE B 194  HIS B 198  1  O  GLN B 196   N  PHE B 164           
SHEET    6 AA7 7 LEU B 250  VAL B 255  1  O  TYR B 251   N  ALA B 195           
SHEET    7 AA7 7 VAL B 274  PRO B 278  1  O  TYR B 275   N  ILE B 252           
SHEET    1 AA8 2 PRO B  79  ASP B  80  0                                        
SHEET    2 AA8 2 MET B  83  THR B  84 -1  O  MET B  83   N  ASP B  80           
SHEET    1 AA9 4 LEU C  41  GLY C  46  0                                        
SHEET    2 AA9 4 SER C  30  GLU C  38 -1  N  ASP C  34   O  GLY C  46           
SHEET    3 AA9 4 ARG C  16  VAL C  25 -1  N  LEU C  17   O  MET C  37           
SHEET    4 AA9 4 THR C  57  GLU C  59  1  O  ILE C  58   N  LYS C  20           
SHEET    1 AB1 8 LEU C  41  GLY C  46  0                                        
SHEET    2 AB1 8 SER C  30  GLU C  38 -1  N  ASP C  34   O  GLY C  46           
SHEET    3 AB1 8 ARG C  16  VAL C  25 -1  N  LEU C  17   O  MET C  37           
SHEET    4 AB1 8 MET C  64  PRO C  67  1  O  VAL C  65   N  VAL C  25           
SHEET    5 AB1 8 LEU C 409  THR C 419 -1  O  VAL C 410   N  ILE C  66           
SHEET    6 AB1 8 GLU C 438  SER C 448 -1  O  CYS C 439   N  LYS C 418           
SHEET    7 AB1 8 LYS C 451  GLU C 455 -1  O  VAL C 453   N  VAL C 446           
SHEET    8 AB1 8 THR C 458  LEU C 459 -1  O  THR C 458   N  GLU C 455           
SHEET    1 AB2 7 GLY C  69  THR C  74  0                                        
SHEET    2 AB2 7 THR C 101  VAL C 108  1  O  MET C 103   N  ASP C  71           
SHEET    3 AB2 7 ASP C 134  ASP C 140  1  O  HIS C 138   N  VAL C 108           
SHEET    4 AB2 7 SER C 163  TYR C 167  1  O  SER C 163   N  VAL C 139           
SHEET    5 AB2 7 ILE C 194  HIS C 198  1  O  GLN C 196   N  PHE C 164           
SHEET    6 AB2 7 LEU C 250  VAL C 255  1  O  TYR C 251   N  ALA C 195           
SHEET    7 AB2 7 VAL C 274  PRO C 278  1  O  TYR C 275   N  ILE C 252           
SHEET    1 AB3 2 PRO C  79  ASP C  80  0                                        
SHEET    2 AB3 2 MET C  83  THR C  84 -1  O  MET C  83   N  ASP C  80           
SHEET    1 AB4 4 LEU D  41  GLY D  46  0                                        
SHEET    2 AB4 4 SER D  30  GLU D  38 -1  N  ASP D  34   O  GLY D  46           
SHEET    3 AB4 4 LEU D  17  VAL D  25 -1  N  LEU D  17   O  MET D  37           
SHEET    4 AB4 4 LYS D  56  GLU D  59  1  O  ILE D  58   N  LYS D  20           
SHEET    1 AB5 8 LEU D  41  GLY D  46  0                                        
SHEET    2 AB5 8 SER D  30  GLU D  38 -1  N  ASP D  34   O  GLY D  46           
SHEET    3 AB5 8 LEU D  17  VAL D  25 -1  N  LEU D  17   O  MET D  37           
SHEET    4 AB5 8 MET D  64  PRO D  67  1  O  VAL D  65   N  LYS D  23           
SHEET    5 AB5 8 LEU D 409  THR D 419 -1  O  VAL D 410   N  ILE D  66           
SHEET    6 AB5 8 GLU D 438  SER D 448 -1  O  CYS D 439   N  LYS D 418           
SHEET    7 AB5 8 LYS D 451  GLU D 455 -1  O  VAL D 453   N  VAL D 446           
SHEET    8 AB5 8 THR D 458  LEU D 459 -1  O  THR D 458   N  GLU D 455           
SHEET    1 AB6 7 GLY D  69  THR D  74  0                                        
SHEET    2 AB6 7 THR D 101  VAL D 108  1  O  MET D 103   N  ASP D  71           
SHEET    3 AB6 7 ASP D 134  ASP D 140  1  O  HIS D 138   N  ASP D 106           
SHEET    4 AB6 7 SER D 163  TYR D 167  1  O  SER D 163   N  VAL D 139           
SHEET    5 AB6 7 ILE D 194  HIS D 198  1  O  GLN D 196   N  PHE D 164           
SHEET    6 AB6 7 LEU D 250  VAL D 255  1  O  TYR D 251   N  ALA D 195           
SHEET    7 AB6 7 VAL D 274  PRO D 278  1  O  TYR D 275   N  ILE D 252           
SHEET    1 AB7 2 PRO D  79  ASP D  80  0                                        
SHEET    2 AB7 2 MET D  83  THR D  84 -1  O  MET D  83   N  ASP D  80           
CISPEP   1 SER A  304    PRO A  305          0        -3.34                     
CISPEP   2 TYR A  395    PRO A  396          0         4.69                     
CISPEP   3 SER B  304    PRO B  305          0        -3.05                     
CISPEP   4 TYR B  395    PRO B  396          0         4.07                     
CISPEP   5 SER C  304    PRO C  305          0        -2.15                     
CISPEP   6 TYR C  395    PRO C  396          0         1.90                     
CISPEP   7 SER D  304    PRO D  305          0        -0.14                     
CISPEP   8 TYR D  395    PRO D  396          0         2.09                     
SITE     1 AC1  4 ARG A 400  HOH A 788  HOH A 800  ARG D 400                    
SITE     1 AC2  6 SER B 288  HIS B 289  SER B 292  LYS B 293                    
SITE     2 AC2  6 LYS B 297  PRO B 502                                          
SITE     1 AC3  2 ASP A 500  TRP B 295                                          
SITE     1 AC4  2 ARG B 400  ARG C 400                                          
SITE     1 AC5  1 ALA D 339                                                     
CRYST1   80.088  158.425   88.000  90.00  94.19  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      0.012486  0.000000  0.000914        0.00000                         
SCALE2      0.000000  0.006312  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011394        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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