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Database: PDB
Entry: 2QYG
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Original site: 2QYG 
HEADER    UNKNOWN FUNCTION                        14-AUG-07   2QYG              
TITLE     CRYSTAL STRUCTURE OF A RUBISCO-LIKE PROTEIN RLP2 FROM RHODOPSEUDOMONAS
TITLE    2 PALUSTRIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE-LIKE PROTEIN 2;          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: RUBISCO-LIKE PROTEIN;                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;                     
SOURCE   3 ORGANISM_TAXID: 258594;                                              
SOURCE   4 STRAIN: CGA009;                                                      
SOURCE   5 GENE: RLP2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: BL21-GOLD(DE3)                            
KEYWDS    BETA-ALPHA-BARREL, UNKNOWN FUNCTION                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,S.CHAN,F.R.TABITA,D.EISENBERG                                    
REVDAT   4   13-JUL-11 2QYG    1       VERSN                                    
REVDAT   3   24-FEB-09 2QYG    1       VERSN                                    
REVDAT   2   24-JUN-08 2QYG    1       JRNL                                     
REVDAT   1   11-SEP-07 2QYG    0                                                
JRNL        AUTH   F.R.TABITA,T.E.HANSON,H.LI,S.SATAGOPAN,J.SINGH,S.CHAN        
JRNL        TITL   FUNCTION, STRUCTURE, AND EVOLUTION OF THE RUBISCO-LIKE       
JRNL        TITL 2 PROTEINS AND THEIR RUBISCO HOMOLOGS.                         
JRNL        REF    MICROBIOL.MOL.BIOL.REV.       V.  71   576 2007              
JRNL        REFN                   ISSN 1092-2172                               
JRNL        PMID   18063718                                                     
JRNL        DOI    10.1128/MMBR.00015-07                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24549                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1307                            
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) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1754                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 103                          
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13012                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.00000                                             
REMARK   3    B22 (A**2) : 0.17000                                              
REMARK   3    B33 (A**2) : 0.83000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.568         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.413         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 56.672        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13380 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18224 ; 1.396 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1712 ; 5.944 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   588 ;32.048 ;22.517       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1960 ;21.041 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   120 ;20.890 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1964 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10568 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5939 ; 0.228 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9154 ; 0.317 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   294 ; 0.163 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   108 ; 0.386 ; 0.200       
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):  8686 ; 0.601 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13740 ; 1.102 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5102 ; 1.310 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4484 ; 2.385 ; 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 C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     429      1                      
REMARK   3           1     B      1       B     429      1                      
REMARK   3           1     C      1       C     429      1                      
REMARK   3           1     D      1       D     429      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3254 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3254 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   3254 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   3254 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3254 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   3254 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   3254 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   3254 ;  0.06 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2860 -11.1746 -11.1839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1326 T22:  -0.0798                                     
REMARK   3      T33:  -0.1493 T12:  -0.0013                                     
REMARK   3      T13:   0.0138 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6581 L22:   1.3075                                     
REMARK   3      L33:   0.6802 L12:   0.5729                                     
REMARK   3      L13:  -0.3605 L23:  -0.7327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0152 S12:  -0.0954 S13:   0.0033                       
REMARK   3      S21:   0.0498 S22:   0.0298 S23:   0.0263                       
REMARK   3      S31:  -0.0108 S32:   0.1237 S33:  -0.0145                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1436   7.7075   5.4712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0045 T22:  -0.0615                                     
REMARK   3      T33:  -0.0975 T12:   0.0075                                     
REMARK   3      T13:   0.0813 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3417 L22:   1.2535                                     
REMARK   3      L33:   1.0628 L12:   0.8247                                     
REMARK   3      L13:   0.5033 L23:   0.0524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0210 S12:  -0.0020 S13:   0.2536                       
REMARK   3      S21:   0.0809 S22:  -0.0507 S23:   0.1736                       
REMARK   3      S31:  -0.1073 S32:   0.0991 S33:   0.0297                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6433 -17.5327 -59.9262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1032 T22:  -0.1440                                     
REMARK   3      T33:  -0.1604 T12:  -0.0246                                     
REMARK   3      T13:  -0.0087 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3978 L22:   1.5874                                     
REMARK   3      L33:   0.6199 L12:  -1.0990                                     
REMARK   3      L13:   0.0032 L23:   0.1821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0524 S12:   0.0171 S13:   0.1714                       
REMARK   3      S21:  -0.0249 S22:  -0.0233 S23:   0.0845                       
REMARK   3      S31:  -0.0918 S32:  -0.1271 S33:  -0.0291                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9454   1.3123 -43.2774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1631 T22:  -0.1235                                     
REMARK   3      T33:  -0.1984 T12:  -0.0204                                     
REMARK   3      T13:   0.0041 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1604 L22:   2.7319                                     
REMARK   3      L33:   0.9476 L12:  -0.7303                                     
REMARK   3      L13:   0.3521 L23:  -0.4136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0088 S12:   0.0358 S13:   0.0715                       
REMARK   3      S21:  -0.1321 S22:   0.0194 S23:   0.0008                       
REMARK   3      S31:   0.1220 S32:  -0.0218 S33:  -0.0282                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2QYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044202.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26399                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.16400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1YKW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 280MM AMMONIUM ACETATE, 100MM SODIUM     
REMARK 280  ACETATE, 30% PEG4000, PH 4.6, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       34.33100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.52000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.76450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.52000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.33100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.76450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7460 ANGSTROM**2                          
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7480 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     GLY A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     ARG A   432                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     GLY B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     ARG B   432                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     GLY C   430                                                      
REMARK 465     GLY C   431                                                      
REMARK 465     ARG C   432                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     GLY D   430                                                      
REMARK 465     GLY D   431                                                      
REMARK 465     ARG D   432                                                      
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    PRO A   3     -135.84    -78.69                                   
REMARK 500    SER A  46     -104.34   -142.45                                   
REMARK 500    THR A  47      -73.69    -63.78                                   
REMARK 500    ALA A  48      -24.50     77.24                                   
REMARK 500    VAL A  53      -81.80    -10.44                                   
REMARK 500    GLU A  57      -61.82   -128.16                                   
REMARK 500    ASP A  58       89.23     40.60                                   
REMARK 500    PHE A  59       38.64    -99.88                                   
REMARK 500    VAL A  83     -142.29   -135.22                                   
REMARK 500    ARG A  88     -159.72   -121.90                                   
REMARK 500    SER A 114        4.25    -66.96                                   
REMARK 500    CYS A 117       53.00   -163.83                                   
REMARK 500    ASN A 174      -73.33   -121.71                                   
REMARK 500    ALA A 204     -136.92   -119.71                                   
REMARK 500    PHE A 290      -43.92     92.22                                   
REMARK 500    VAL A 385      -63.32   -109.96                                   
REMARK 500    PRO B   3     -137.30    -80.51                                   
REMARK 500    SER B  46     -102.95   -142.24                                   
REMARK 500    THR B  47      -73.03    -64.31                                   
REMARK 500    ALA B  48      -24.22     76.11                                   
REMARK 500    VAL B  53      -77.06    -13.77                                   
REMARK 500    GLU B  57      -59.94   -126.39                                   
REMARK 500    ASP B  58       89.97     40.23                                   
REMARK 500    PHE B  59       36.76    -99.83                                   
REMARK 500    VAL B  83     -142.10   -137.27                                   
REMARK 500    ARG B  88     -159.55   -120.04                                   
REMARK 500    ALA B 107       57.50    -90.09                                   
REMARK 500    SER B 114        6.54    -69.21                                   
REMARK 500    ALA B 115      -61.20   -107.76                                   
REMARK 500    CYS B 117       49.40   -163.77                                   
REMARK 500    ASN B 174      -72.81   -122.33                                   
REMARK 500    ALA B 204     -136.22   -119.22                                   
REMARK 500    PHE B 290      -44.74     92.48                                   
REMARK 500    VAL B 385      -63.11   -109.01                                   
REMARK 500    PRO C   3     -136.37    -78.83                                   
REMARK 500    SER C  46     -102.60   -139.61                                   
REMARK 500    THR C  47      -73.36    -62.08                                   
REMARK 500    ALA C  48      -24.10     74.41                                   
REMARK 500    VAL C  53      -80.11    -13.09                                   
REMARK 500    GLU C  57      -61.46   -128.72                                   
REMARK 500    ASP C  58       88.54     40.29                                   
REMARK 500    PHE C  59       37.22    -99.96                                   
REMARK 500    VAL C  83     -143.74   -136.66                                   
REMARK 500    ARG C  88     -158.72   -120.11                                   
REMARK 500    SER C 114        6.24    -67.84                                   
REMARK 500    CYS C 117       54.87   -165.13                                   
REMARK 500    ASN C 174      -74.58   -122.98                                   
REMARK 500    ALA C 204     -135.49   -121.11                                   
REMARK 500    PHE C 290      -43.39     91.87                                   
REMARK 500    VAL C 385      -63.77   -109.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YKW   RELATED DB: PDB                                   
REMARK 900 PROTEIN HOMOLOG                                                      
DBREF  2QYG A    1   432  UNP    Q6ND47   RBLL2_RHOPA      1    432             
DBREF  2QYG B    1   432  UNP    Q6ND47   RBLL2_RHOPA      1    432             
DBREF  2QYG C    1   432  UNP    Q6ND47   RBLL2_RHOPA      1    432             
DBREF  2QYG D    1   432  UNP    Q6ND47   RBLL2_RHOPA      1    432             
SEQADV 2QYG MET A  -19  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY A  -18  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER A  -17  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER A  -16  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS A  -15  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS A  -14  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS A  -13  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS A  -12  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS A  -11  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS A  -10  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER A   -9  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER A   -8  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY A   -7  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG LEU A   -6  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG VAL A   -5  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG PRO A   -4  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG ARG A   -3  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY A   -2  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER A   -1  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS A    0  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG MET B  -19  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY B  -18  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER B  -17  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER B  -16  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS B  -15  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS B  -14  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS B  -13  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS B  -12  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS B  -11  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS B  -10  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER B   -9  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER B   -8  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY B   -7  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG LEU B   -6  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG VAL B   -5  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG PRO B   -4  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG ARG B   -3  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY B   -2  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER B   -1  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS B    0  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG MET C  -19  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY C  -18  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER C  -17  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER C  -16  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS C  -15  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS C  -14  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS C  -13  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS C  -12  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS C  -11  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS C  -10  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER C   -9  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER C   -8  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY C   -7  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG LEU C   -6  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG VAL C   -5  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG PRO C   -4  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG ARG C   -3  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY C   -2  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER C   -1  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS C    0  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG MET D  -19  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY D  -18  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER D  -17  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER D  -16  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS D  -15  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS D  -14  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS D  -13  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS D  -12  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS D  -11  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS D  -10  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER D   -9  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER D   -8  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY D   -7  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG LEU D   -6  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG VAL D   -5  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG PRO D   -4  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG ARG D   -3  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG GLY D   -2  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG SER D   -1  UNP  Q6ND47              EXPRESSION TAG                 
SEQADV 2QYG HIS D    0  UNP  Q6ND47              EXPRESSION TAG                 
SEQRES   1 A  452  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  452  LEU VAL PRO ARG GLY SER HIS MET THR PRO ASP ASP ILE          
SEQRES   3 A  452  ALA GLY PHE TYR ALA LYS ARG ALA ASP LEU ASP LEU ASP          
SEQRES   4 A  452  ASN TYR ILE GLU LEU ASP PHE ASP PHE GLU CYS ALA GLY          
SEQRES   5 A  452  ASP PRO HIS GLU ALA ALA ALA HIS LEU CYS SER GLU GLN          
SEQRES   6 A  452  SER THR ALA GLN TRP ARG ARG VAL GLY PHE ASP GLU ASP          
SEQRES   7 A  452  PHE ARG PRO ARG PHE ALA ALA LYS VAL LEU GLU LEU SER          
SEQRES   8 A  452  ALA GLU PRO ARG PRO SER GLY PHE SER VAL PRO VAL GLU          
SEQRES   9 A  452  CYS ALA ALA ARG GLY PRO VAL HIS ALA CYS ARG VAL THR          
SEQRES  10 A  452  ILE ALA HIS PRO HIS GLY ASN PHE GLY ALA LYS ILE PRO          
SEQRES  11 A  452  ASN LEU LEU SER ALA VAL CYS GLY GLU GLY VAL PHE PHE          
SEQRES  12 A  452  SER PRO GLY ILE PRO LEU ILE ARG LEU GLN ASP ILE ARG          
SEQRES  13 A  452  PHE PRO GLU PRO TYR LEU ALA ALA PHE ASP GLY PRO ARG          
SEQRES  14 A  452  PHE GLY ILE ALA GLY VAL ARG GLU ARG LEU GLN ALA PHE          
SEQRES  15 A  452  ASP ARG PRO ILE PHE PHE GLY VAL ILE LYS PRO ASN ILE          
SEQRES  16 A  452  GLY LEU PRO PRO GLN PRO PHE ALA GLU LEU GLY TYR GLN          
SEQRES  17 A  452  SER TRP THR GLY GLY LEU ASP ILE ALA LYS ASP ASP GLU          
SEQRES  18 A  452  MET LEU ALA ASP VAL ASP TRP CYS PRO LEU ALA GLU ARG          
SEQRES  19 A  452  ALA ALA LEU LEU GLY ASP ALA CYS ARG ARG ALA SER ALA          
SEQRES  20 A  452  GLU THR GLY VAL PRO LYS ILE TYR LEU ALA ASN ILE THR          
SEQRES  21 A  452  ASP GLU VAL ASP ARG LEU THR GLU LEU HIS ASP VAL ALA          
SEQRES  22 A  452  VAL ALA ASN GLY ALA GLY ALA LEU LEU ILE ASN ALA MET          
SEQRES  23 A  452  PRO VAL GLY LEU SER ALA VAL ARG MET LEU ARG LYS HIS          
SEQRES  24 A  452  ALA THR VAL PRO LEU ILE ALA HIS PHE PRO PHE ILE ALA          
SEQRES  25 A  452  ALA PHE SER ARG LEU ALA ASN TYR GLY ILE HIS SER ARG          
SEQRES  26 A  452  VAL MET THR ARG LEU GLN ARG LEU ALA GLY PHE ASP VAL          
SEQRES  27 A  452  VAL ILE MET PRO GLY PHE GLY PRO ARG MET MET THR PRO          
SEQRES  28 A  452  GLU HIS GLU VAL LEU ASP CYS ILE ARG ALA CYS LEU GLU          
SEQRES  29 A  452  PRO MET GLY PRO ILE LYS PRO CYS LEU PRO VAL PRO GLY          
SEQRES  30 A  452  GLY SER ASP SER ALA ALA THR LEU GLU ASN VAL TYR ARG          
SEQRES  31 A  452  LYS VAL GLY SER ALA ASP PHE GLY PHE VAL PRO GLY ARG          
SEQRES  32 A  452  GLY VAL PHE GLY HIS PRO MET GLY PRO ALA ALA GLY ALA          
SEQRES  33 A  452  THR SER ILE ARG GLN ALA TRP ASP ALA ILE ALA ALA GLY          
SEQRES  34 A  452  ILE PRO VAL PRO ASP HIS ALA ALA SER HIS PRO GLU LEU          
SEQRES  35 A  452  ALA ALA ALA LEU ARG ALA PHE GLY GLY ARG                      
SEQRES   1 B  452  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  452  LEU VAL PRO ARG GLY SER HIS MET THR PRO ASP ASP ILE          
SEQRES   3 B  452  ALA GLY PHE TYR ALA LYS ARG ALA ASP LEU ASP LEU ASP          
SEQRES   4 B  452  ASN TYR ILE GLU LEU ASP PHE ASP PHE GLU CYS ALA GLY          
SEQRES   5 B  452  ASP PRO HIS GLU ALA ALA ALA HIS LEU CYS SER GLU GLN          
SEQRES   6 B  452  SER THR ALA GLN TRP ARG ARG VAL GLY PHE ASP GLU ASP          
SEQRES   7 B  452  PHE ARG PRO ARG PHE ALA ALA LYS VAL LEU GLU LEU SER          
SEQRES   8 B  452  ALA GLU PRO ARG PRO SER GLY PHE SER VAL PRO VAL GLU          
SEQRES   9 B  452  CYS ALA ALA ARG GLY PRO VAL HIS ALA CYS ARG VAL THR          
SEQRES  10 B  452  ILE ALA HIS PRO HIS GLY ASN PHE GLY ALA LYS ILE PRO          
SEQRES  11 B  452  ASN LEU LEU SER ALA VAL CYS GLY GLU GLY VAL PHE PHE          
SEQRES  12 B  452  SER PRO GLY ILE PRO LEU ILE ARG LEU GLN ASP ILE ARG          
SEQRES  13 B  452  PHE PRO GLU PRO TYR LEU ALA ALA PHE ASP GLY PRO ARG          
SEQRES  14 B  452  PHE GLY ILE ALA GLY VAL ARG GLU ARG LEU GLN ALA PHE          
SEQRES  15 B  452  ASP ARG PRO ILE PHE PHE GLY VAL ILE LYS PRO ASN ILE          
SEQRES  16 B  452  GLY LEU PRO PRO GLN PRO PHE ALA GLU LEU GLY TYR GLN          
SEQRES  17 B  452  SER TRP THR GLY GLY LEU ASP ILE ALA LYS ASP ASP GLU          
SEQRES  18 B  452  MET LEU ALA ASP VAL ASP TRP CYS PRO LEU ALA GLU ARG          
SEQRES  19 B  452  ALA ALA LEU LEU GLY ASP ALA CYS ARG ARG ALA SER ALA          
SEQRES  20 B  452  GLU THR GLY VAL PRO LYS ILE TYR LEU ALA ASN ILE THR          
SEQRES  21 B  452  ASP GLU VAL ASP ARG LEU THR GLU LEU HIS ASP VAL ALA          
SEQRES  22 B  452  VAL ALA ASN GLY ALA GLY ALA LEU LEU ILE ASN ALA MET          
SEQRES  23 B  452  PRO VAL GLY LEU SER ALA VAL ARG MET LEU ARG LYS HIS          
SEQRES  24 B  452  ALA THR VAL PRO LEU ILE ALA HIS PHE PRO PHE ILE ALA          
SEQRES  25 B  452  ALA PHE SER ARG LEU ALA ASN TYR GLY ILE HIS SER ARG          
SEQRES  26 B  452  VAL MET THR ARG LEU GLN ARG LEU ALA GLY PHE ASP VAL          
SEQRES  27 B  452  VAL ILE MET PRO GLY PHE GLY PRO ARG MET MET THR PRO          
SEQRES  28 B  452  GLU HIS GLU VAL LEU ASP CYS ILE ARG ALA CYS LEU GLU          
SEQRES  29 B  452  PRO MET GLY PRO ILE LYS PRO CYS LEU PRO VAL PRO GLY          
SEQRES  30 B  452  GLY SER ASP SER ALA ALA THR LEU GLU ASN VAL TYR ARG          
SEQRES  31 B  452  LYS VAL GLY SER ALA ASP PHE GLY PHE VAL PRO GLY ARG          
SEQRES  32 B  452  GLY VAL PHE GLY HIS PRO MET GLY PRO ALA ALA GLY ALA          
SEQRES  33 B  452  THR SER ILE ARG GLN ALA TRP ASP ALA ILE ALA ALA GLY          
SEQRES  34 B  452  ILE PRO VAL PRO ASP HIS ALA ALA SER HIS PRO GLU LEU          
SEQRES  35 B  452  ALA ALA ALA LEU ARG ALA PHE GLY GLY ARG                      
SEQRES   1 C  452  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  452  LEU VAL PRO ARG GLY SER HIS MET THR PRO ASP ASP ILE          
SEQRES   3 C  452  ALA GLY PHE TYR ALA LYS ARG ALA ASP LEU ASP LEU ASP          
SEQRES   4 C  452  ASN TYR ILE GLU LEU ASP PHE ASP PHE GLU CYS ALA GLY          
SEQRES   5 C  452  ASP PRO HIS GLU ALA ALA ALA HIS LEU CYS SER GLU GLN          
SEQRES   6 C  452  SER THR ALA GLN TRP ARG ARG VAL GLY PHE ASP GLU ASP          
SEQRES   7 C  452  PHE ARG PRO ARG PHE ALA ALA LYS VAL LEU GLU LEU SER          
SEQRES   8 C  452  ALA GLU PRO ARG PRO SER GLY PHE SER VAL PRO VAL GLU          
SEQRES   9 C  452  CYS ALA ALA ARG GLY PRO VAL HIS ALA CYS ARG VAL THR          
SEQRES  10 C  452  ILE ALA HIS PRO HIS GLY ASN PHE GLY ALA LYS ILE PRO          
SEQRES  11 C  452  ASN LEU LEU SER ALA VAL CYS GLY GLU GLY VAL PHE PHE          
SEQRES  12 C  452  SER PRO GLY ILE PRO LEU ILE ARG LEU GLN ASP ILE ARG          
SEQRES  13 C  452  PHE PRO GLU PRO TYR LEU ALA ALA PHE ASP GLY PRO ARG          
SEQRES  14 C  452  PHE GLY ILE ALA GLY VAL ARG GLU ARG LEU GLN ALA PHE          
SEQRES  15 C  452  ASP ARG PRO ILE PHE PHE GLY VAL ILE LYS PRO ASN ILE          
SEQRES  16 C  452  GLY LEU PRO PRO GLN PRO PHE ALA GLU LEU GLY TYR GLN          
SEQRES  17 C  452  SER TRP THR GLY GLY LEU ASP ILE ALA LYS ASP ASP GLU          
SEQRES  18 C  452  MET LEU ALA ASP VAL ASP TRP CYS PRO LEU ALA GLU ARG          
SEQRES  19 C  452  ALA ALA LEU LEU GLY ASP ALA CYS ARG ARG ALA SER ALA          
SEQRES  20 C  452  GLU THR GLY VAL PRO LYS ILE TYR LEU ALA ASN ILE THR          
SEQRES  21 C  452  ASP GLU VAL ASP ARG LEU THR GLU LEU HIS ASP VAL ALA          
SEQRES  22 C  452  VAL ALA ASN GLY ALA GLY ALA LEU LEU ILE ASN ALA MET          
SEQRES  23 C  452  PRO VAL GLY LEU SER ALA VAL ARG MET LEU ARG LYS HIS          
SEQRES  24 C  452  ALA THR VAL PRO LEU ILE ALA HIS PHE PRO PHE ILE ALA          
SEQRES  25 C  452  ALA PHE SER ARG LEU ALA ASN TYR GLY ILE HIS SER ARG          
SEQRES  26 C  452  VAL MET THR ARG LEU GLN ARG LEU ALA GLY PHE ASP VAL          
SEQRES  27 C  452  VAL ILE MET PRO GLY PHE GLY PRO ARG MET MET THR PRO          
SEQRES  28 C  452  GLU HIS GLU VAL LEU ASP CYS ILE ARG ALA CYS LEU GLU          
SEQRES  29 C  452  PRO MET GLY PRO ILE LYS PRO CYS LEU PRO VAL PRO GLY          
SEQRES  30 C  452  GLY SER ASP SER ALA ALA THR LEU GLU ASN VAL TYR ARG          
SEQRES  31 C  452  LYS VAL GLY SER ALA ASP PHE GLY PHE VAL PRO GLY ARG          
SEQRES  32 C  452  GLY VAL PHE GLY HIS PRO MET GLY PRO ALA ALA GLY ALA          
SEQRES  33 C  452  THR SER ILE ARG GLN ALA TRP ASP ALA ILE ALA ALA GLY          
SEQRES  34 C  452  ILE PRO VAL PRO ASP HIS ALA ALA SER HIS PRO GLU LEU          
SEQRES  35 C  452  ALA ALA ALA LEU ARG ALA PHE GLY GLY ARG                      
SEQRES   1 D  452  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  452  LEU VAL PRO ARG GLY SER HIS MET THR PRO ASP ASP ILE          
SEQRES   3 D  452  ALA GLY PHE TYR ALA LYS ARG ALA ASP LEU ASP LEU ASP          
SEQRES   4 D  452  ASN TYR ILE GLU LEU ASP PHE ASP PHE GLU CYS ALA GLY          
SEQRES   5 D  452  ASP PRO HIS GLU ALA ALA ALA HIS LEU CYS SER GLU GLN          
SEQRES   6 D  452  SER THR ALA GLN TRP ARG ARG VAL GLY PHE ASP GLU ASP          
SEQRES   7 D  452  PHE ARG PRO ARG PHE ALA ALA LYS VAL LEU GLU LEU SER          
SEQRES   8 D  452  ALA GLU PRO ARG PRO SER GLY PHE SER VAL PRO VAL GLU          
SEQRES   9 D  452  CYS ALA ALA ARG GLY PRO VAL HIS ALA CYS ARG VAL THR          
SEQRES  10 D  452  ILE ALA HIS PRO HIS GLY ASN PHE GLY ALA LYS ILE PRO          
SEQRES  11 D  452  ASN LEU LEU SER ALA VAL CYS GLY GLU GLY VAL PHE PHE          
SEQRES  12 D  452  SER PRO GLY ILE PRO LEU ILE ARG LEU GLN ASP ILE ARG          
SEQRES  13 D  452  PHE PRO GLU PRO TYR LEU ALA ALA PHE ASP GLY PRO ARG          
SEQRES  14 D  452  PHE GLY ILE ALA GLY VAL ARG GLU ARG LEU GLN ALA PHE          
SEQRES  15 D  452  ASP ARG PRO ILE PHE PHE GLY VAL ILE LYS PRO ASN ILE          
SEQRES  16 D  452  GLY LEU PRO PRO GLN PRO PHE ALA GLU LEU GLY TYR GLN          
SEQRES  17 D  452  SER TRP THR GLY GLY LEU ASP ILE ALA LYS ASP ASP GLU          
SEQRES  18 D  452  MET LEU ALA ASP VAL ASP TRP CYS PRO LEU ALA GLU ARG          
SEQRES  19 D  452  ALA ALA LEU LEU GLY ASP ALA CYS ARG ARG ALA SER ALA          
SEQRES  20 D  452  GLU THR GLY VAL PRO LYS ILE TYR LEU ALA ASN ILE THR          
SEQRES  21 D  452  ASP GLU VAL ASP ARG LEU THR GLU LEU HIS ASP VAL ALA          
SEQRES  22 D  452  VAL ALA ASN GLY ALA GLY ALA LEU LEU ILE ASN ALA MET          
SEQRES  23 D  452  PRO VAL GLY LEU SER ALA VAL ARG MET LEU ARG LYS HIS          
SEQRES  24 D  452  ALA THR VAL PRO LEU ILE ALA HIS PHE PRO PHE ILE ALA          
SEQRES  25 D  452  ALA PHE SER ARG LEU ALA ASN TYR GLY ILE HIS SER ARG          
SEQRES  26 D  452  VAL MET THR ARG LEU GLN ARG LEU ALA GLY PHE ASP VAL          
SEQRES  27 D  452  VAL ILE MET PRO GLY PHE GLY PRO ARG MET MET THR PRO          
SEQRES  28 D  452  GLU HIS GLU VAL LEU ASP CYS ILE ARG ALA CYS LEU GLU          
SEQRES  29 D  452  PRO MET GLY PRO ILE LYS PRO CYS LEU PRO VAL PRO GLY          
SEQRES  30 D  452  GLY SER ASP SER ALA ALA THR LEU GLU ASN VAL TYR ARG          
SEQRES  31 D  452  LYS VAL GLY SER ALA ASP PHE GLY PHE VAL PRO GLY ARG          
SEQRES  32 D  452  GLY VAL PHE GLY HIS PRO MET GLY PRO ALA ALA GLY ALA          
SEQRES  33 D  452  THR SER ILE ARG GLN ALA TRP ASP ALA ILE ALA ALA GLY          
SEQRES  34 D  452  ILE PRO VAL PRO ASP HIS ALA ALA SER HIS PRO GLU LEU          
SEQRES  35 D  452  ALA ALA ALA LEU ARG ALA PHE GLY GLY ARG                      
HELIX    1   1 PRO A    3  TYR A   10  5                                   8    
HELIX    2   2 LYS A   12  LEU A   16  5                                   5    
HELIX    3   3 ASP A   17  ASP A   19  5                                   3    
HELIX    4   4 ASP A   33  SER A   46  1                                  14    
HELIX    5   5 PHE A   59  ALA A   64  1                                   6    
HELIX    6   6 GLY A  103  PHE A  105  5                                   3    
HELIX    7   7 LYS A  108  CYS A  117  1                                  10    
HELIX    8   8 GLY A  118  PHE A  123  1                                   6    
HELIX    9   9 PRO A  138  ALA A  143  1                                   6    
HELIX   10  10 PHE A  150  GLN A  160  1                                  11    
HELIX   11  11 PRO A  179  GLY A  193  1                                  15    
HELIX   12  12 PRO A  210  GLY A  230  1                                  21    
HELIX   13  13 ASP A  244  ASN A  256  1                                  13    
HELIX   14  14 ALA A  265  GLY A  269  1                                   5    
HELIX   15  15 GLY A  269  LYS A  278  1                                  10    
HELIX   16  16 PHE A  290  ARG A  296  1                                   7    
HELIX   17  17 HIS A  303  GLY A  315  1                                  13    
HELIX   18  18 GLY A  325  MET A  329  5                                   5    
HELIX   19  19 PRO A  331  GLU A  344  1                                  14    
HELIX   20  20 THR A  364  GLY A  373  1                                  10    
HELIX   21  21 GLY A  391  ALA A  408  1                                  18    
HELIX   22  22 PRO A  411  ALA A  417  1                                   7    
HELIX   23  23 HIS A  419  PHE A  429  1                                  11    
HELIX   24  24 PRO B    3  TYR B   10  5                                   8    
HELIX   25  25 LYS B   12  LEU B   16  5                                   5    
HELIX   26  26 ASP B   17  ASP B   19  5                                   3    
HELIX   27  27 ASP B   33  SER B   46  1                                  14    
HELIX   28  28 PHE B   59  ALA B   64  1                                   6    
HELIX   29  29 GLY B  103  PHE B  105  5                                   3    
HELIX   30  30 LYS B  108  CYS B  117  1                                  10    
HELIX   31  31 GLY B  118  PHE B  123  1                                   6    
HELIX   32  32 PRO B  138  ALA B  143  1                                   6    
HELIX   33  33 PHE B  150  GLN B  160  1                                  11    
HELIX   34  34 PRO B  179  GLY B  193  1                                  15    
HELIX   35  35 PRO B  210  GLY B  230  1                                  21    
HELIX   36  36 ASP B  244  ASN B  256  1                                  13    
HELIX   37  37 ALA B  265  GLY B  269  1                                   5    
HELIX   38  38 GLY B  269  LYS B  278  1                                  10    
HELIX   39  39 PHE B  290  ARG B  296  1                                   7    
HELIX   40  40 HIS B  303  GLY B  315  1                                  13    
HELIX   41  41 GLY B  325  MET B  329  5                                   5    
HELIX   42  42 PRO B  331  GLU B  344  1                                  14    
HELIX   43  43 THR B  364  GLY B  373  1                                  10    
HELIX   44  44 GLY B  391  ALA B  408  1                                  18    
HELIX   45  45 PRO B  411  ALA B  417  1                                   7    
HELIX   46  46 HIS B  419  PHE B  429  1                                  11    
HELIX   47  47 PRO C    3  TYR C   10  5                                   8    
HELIX   48  48 LYS C   12  LEU C   16  5                                   5    
HELIX   49  49 ASP C   17  ASP C   19  5                                   3    
HELIX   50  50 ASP C   33  SER C   46  1                                  14    
HELIX   51  51 PHE C   59  ALA C   64  1                                   6    
HELIX   52  52 GLY C  103  PHE C  105  5                                   3    
HELIX   53  53 LYS C  108  CYS C  117  1                                  10    
HELIX   54  54 GLY C  118  PHE C  123  1                                   6    
HELIX   55  55 PRO C  138  ALA C  143  1                                   6    
HELIX   56  56 PHE C  150  GLN C  160  1                                  11    
HELIX   57  57 PRO C  179  GLY C  193  1                                  15    
HELIX   58  58 PRO C  210  GLY C  230  1                                  21    
HELIX   59  59 ASP C  244  ASN C  256  1                                  13    
HELIX   60  60 ALA C  265  GLY C  269  1                                   5    
HELIX   61  61 GLY C  269  LYS C  278  1                                  10    
HELIX   62  62 PHE C  290  ARG C  296  1                                   7    
HELIX   63  63 HIS C  303  GLY C  315  1                                  13    
HELIX   64  64 GLY C  325  MET C  329  5                                   5    
HELIX   65  65 PRO C  331  GLU C  344  1                                  14    
HELIX   66  66 THR C  364  GLY C  373  1                                  10    
HELIX   67  67 GLY C  391  ALA C  408  1                                  18    
HELIX   68  68 PRO C  411  ALA C  416  1                                   6    
HELIX   69  69 HIS C  419  PHE C  429  1                                  11    
HELIX   70  70 PRO D    3  TYR D   10  5                                   8    
HELIX   71  71 LYS D   12  LEU D   16  5                                   5    
HELIX   72  72 ASP D   17  ASP D   19  5                                   3    
HELIX   73  73 ASP D   33  SER D   46  1                                  14    
HELIX   74  74 PHE D   59  ALA D   64  1                                   6    
HELIX   75  75 GLY D  103  PHE D  105  5                                   3    
HELIX   76  76 LYS D  108  CYS D  117  1                                  10    
HELIX   77  77 GLY D  118  PHE D  123  1                                   6    
HELIX   78  78 PRO D  138  ALA D  143  1                                   6    
HELIX   79  79 PHE D  150  GLN D  160  1                                  11    
HELIX   80  80 PRO D  179  GLY D  193  1                                  15    
HELIX   81  81 PRO D  210  GLY D  230  1                                  21    
HELIX   82  82 ASP D  244  ASN D  256  1                                  13    
HELIX   83  83 ALA D  265  GLY D  269  1                                   5    
HELIX   84  84 GLY D  269  LYS D  278  1                                  10    
HELIX   85  85 PHE D  290  ARG D  296  1                                   7    
HELIX   86  86 HIS D  303  GLY D  315  1                                  13    
HELIX   87  87 GLY D  325  MET D  329  5                                   5    
HELIX   88  88 PRO D  331  GLU D  344  1                                  14    
HELIX   89  89 THR D  364  GLY D  373  1                                  10    
HELIX   90  90 GLY D  391  ALA D  408  1                                  18    
HELIX   91  91 PRO D  411  ALA D  417  1                                   7    
HELIX   92  92 HIS D  419  PHE D  429  1                                  11    
SHEET    1   A 5 LYS A  66  PRO A  74  0                                        
SHEET    2   A 5 VAL A  91  PRO A 101 -1  O  ALA A  99   N  LYS A  66           
SHEET    3   A 5 TYR A  21  ALA A  31 -1  N  PHE A  28   O  CYS A  94           
SHEET    4   A 5 LEU A 129  ARG A 136 -1  O  GLN A 133   N  ASP A  25           
SHEET    5   A 5 GLY A 301  ILE A 302  1  O  GLY A 301   N  ILE A 130           
SHEET    1   B 8 LEU A 353  PRO A 356  0                                        
SHEET    2   B 8 VAL A 318  MET A 321  1  N  VAL A 319   O  LEU A 353           
SHEET    3   B 8 LEU A 284  HIS A 287  1  N  ALA A 286   O  VAL A 318           
SHEET    4   B 8 ALA A 260  ASN A 264  1  N  ILE A 263   O  ILE A 285           
SHEET    5   B 8 ILE A 234  ASN A 238  1  N  ALA A 237   O  LEU A 262           
SHEET    6   B 8 ILE A 196  LYS A 198  1  N  ALA A 197   O  LEU A 236           
SHEET    7   B 8 ILE A 166  VAL A 170  1  N  GLY A 169   O  LYS A 198           
SHEET    8   B 8 GLY A 378  PHE A 379  1  O  PHE A 379   N  PHE A 168           
SHEET    1   C 5 LYS B  66  PRO B  74  0                                        
SHEET    2   C 5 VAL B  91  PRO B 101 -1  O  ALA B  99   N  LYS B  66           
SHEET    3   C 5 TYR B  21  ALA B  31 -1  N  PHE B  28   O  CYS B  94           
SHEET    4   C 5 LEU B 129  ARG B 136 -1  O  GLN B 133   N  ASP B  25           
SHEET    5   C 5 GLY B 301  ILE B 302  1  O  GLY B 301   N  ILE B 130           
SHEET    1   D 8 LEU B 353  PRO B 356  0                                        
SHEET    2   D 8 VAL B 318  MET B 321  1  N  VAL B 319   O  LEU B 353           
SHEET    3   D 8 LEU B 284  HIS B 287  1  N  ALA B 286   O  ILE B 320           
SHEET    4   D 8 ALA B 260  ASN B 264  1  N  ILE B 263   O  ILE B 285           
SHEET    5   D 8 ILE B 234  ASN B 238  1  N  ALA B 237   O  LEU B 262           
SHEET    6   D 8 ILE B 196  LYS B 198  1  N  ALA B 197   O  LEU B 236           
SHEET    7   D 8 ILE B 166  VAL B 170  1  N  GLY B 169   O  LYS B 198           
SHEET    8   D 8 GLY B 378  PHE B 379  1  O  PHE B 379   N  PHE B 168           
SHEET    1   E 5 LYS C  66  PRO C  74  0                                        
SHEET    2   E 5 VAL C  91  PRO C 101 -1  O  ALA C  99   N  LYS C  66           
SHEET    3   E 5 TYR C  21  ALA C  31 -1  N  PHE C  28   O  CYS C  94           
SHEET    4   E 5 LEU C 129  ARG C 136 -1  O  GLN C 133   N  ASP C  25           
SHEET    5   E 5 GLY C 301  ILE C 302  1  O  GLY C 301   N  ILE C 130           
SHEET    1   F 8 LEU C 353  PRO C 356  0                                        
SHEET    2   F 8 VAL C 318  MET C 321  1  N  VAL C 319   O  VAL C 355           
SHEET    3   F 8 LEU C 284  HIS C 287  1  N  ALA C 286   O  ILE C 320           
SHEET    4   F 8 ALA C 260  ASN C 264  1  N  ILE C 263   O  ILE C 285           
SHEET    5   F 8 ILE C 234  ASN C 238  1  N  ALA C 237   O  LEU C 262           
SHEET    6   F 8 ILE C 196  LYS C 198  1  N  ALA C 197   O  LEU C 236           
SHEET    7   F 8 ILE C 166  VAL C 170  1  N  GLY C 169   O  LYS C 198           
SHEET    8   F 8 GLY C 378  PHE C 379  1  O  PHE C 379   N  PHE C 168           
SHEET    1   G 5 LYS D  66  PRO D  74  0                                        
SHEET    2   G 5 VAL D  91  PRO D 101 -1  O  ALA D  99   N  LYS D  66           
SHEET    3   G 5 TYR D  21  ALA D  31 -1  N  PHE D  28   O  CYS D  94           
SHEET    4   G 5 LEU D 129  ARG D 136 -1  O  GLN D 133   N  ASP D  25           
SHEET    5   G 5 GLY D 301  ILE D 302  1  O  GLY D 301   N  ILE D 130           
SHEET    1   H 8 LEU D 353  PRO D 356  0                                        
SHEET    2   H 8 VAL D 318  MET D 321  1  N  VAL D 319   O  LEU D 353           
SHEET    3   H 8 LEU D 284  HIS D 287  1  N  ALA D 286   O  ILE D 320           
SHEET    4   H 8 ALA D 260  ASN D 264  1  N  ILE D 263   O  ILE D 285           
SHEET    5   H 8 ILE D 234  ASN D 238  1  N  ALA D 237   O  LEU D 262           
SHEET    6   H 8 ILE D 196  LYS D 198  1  N  ALA D 197   O  LEU D 236           
SHEET    7   H 8 ILE D 166  VAL D 170  1  N  GLY D 169   O  LYS D 198           
SHEET    8   H 8 GLY D 378  PHE D 379  1  O  PHE D 379   N  PHE D 168           
CISPEP   1 LYS A  172    PRO A  173          0        -5.46                     
CISPEP   2 LYS B  172    PRO B  173          0        -3.70                     
CISPEP   3 LYS C  172    PRO C  173          0        -6.80                     
CISPEP   4 LYS D  172    PRO D  173          0        -4.40                     
CRYST1   68.662  119.529  203.040  90.00  90.00  90.00 P 21 21 21   16          
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      0.014564  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008366  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004925        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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