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Database: PDB
Entry: 4H0M
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Original site: 4H0M 
HEADER    PHOTOSYNTHESIS                          09-SEP-12   4H0M              
TITLE     X-RAY CRYSTAL STRUCTURE OF PHYCOCYANIN FROM SYNECHOCOCCUS ELONGATUS   
TITLE    2 SP. PCC 7942                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-PHYCOCYANIN ALPHA CHAIN;                                 
COMPND   3 CHAIN: A, C, E, G, I, K, M, O, Q, S, U, W;                           
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: C-PHYCOCYANIN BETA CHAIN;                                  
COMPND   6 CHAIN: B, D, F, H, J, L, N, P, R, T, V, X                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;                        
SOURCE   3 ORGANISM_TAXID: 1140;                                                
SOURCE   4 STRAIN: PCC 7942;                                                    
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;                        
SOURCE   7 ORGANISM_TAXID: 1140;                                                
SOURCE   8 STRAIN: PCC 7942                                                     
KEYWDS    COMPONENT OF THE PHYCOBILISOME, PHOTOSYNTHETIC ANTENNA COMPLEX,       
KEYWDS   2 PHOTOSYNTHESIS                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MARX,N.ADIR                                                         
REVDAT   1   06-MAR-13 4H0M    0                                                
JRNL        AUTH   A.MARX,N.ADIR                                                
JRNL        TITL   ALLOPHYCOCYANIN AND PHYCOCYANIN CRYSTAL STRUCTURES REVEAL    
JRNL        TITL 2 FACETS OF PHYCOBILISOME ASSEMBLY.                            
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1827   311 2013              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   23201474                                                     
JRNL        DOI    10.1016/J.BBABIO.2012.11.006                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 185314                         
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 SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9751                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.52                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 14100                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 760                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 29832                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1548                                    
REMARK   3   SOLVENT ATOMS            : 772                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.29000                                             
REMARK   3    B22 (A**2) : 1.84000                                              
REMARK   3    B33 (A**2) : -0.55000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.51000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4H0M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074868.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 195069                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 50MM TRIS PH 8, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       56.76000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 37640 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -225.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, K, L, C, D, I, J, E,            
REMARK 350                    AND CHAINS: F, G, H                               
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 37700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -232.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, W, X, Q, R, S, T, O,            
REMARK 350                    AND CHAINS: P, U, V                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET B     0                                                      
REMARK 465     MET C     0                                                      
REMARK 465     MET D     0                                                      
REMARK 465     MET E     0                                                      
REMARK 465     MET F     0                                                      
REMARK 465     MET G     0                                                      
REMARK 465     MET H     0                                                      
REMARK 465     MET I     0                                                      
REMARK 465     MET J     0                                                      
REMARK 465     MET K     0                                                      
REMARK 465     MET L     0                                                      
REMARK 465     MET M     0                                                      
REMARK 465     MET N     0                                                      
REMARK 465     MET O     0                                                      
REMARK 465     MET P     0                                                      
REMARK 465     MET Q     0                                                      
REMARK 465     MET R     0                                                      
REMARK 465     MET S     0                                                      
REMARK 465     MET T     0                                                      
REMARK 465     MET U     0                                                      
REMARK 465     MET V     0                                                      
REMARK 465     MET W     0                                                      
REMARK 465     MET X     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS F 153   CB    CYS F 153   SG     -0.227                       
REMARK 500    CYS H 153   CB    CYS H 153   SG     -0.183                       
REMARK 500    CYS J 153   CB    CYS J 153   SG     -0.292                       
REMARK 500    CYS L 153   CB    CYS L 153   SG     -0.128                       
REMARK 500    CYS N 153   CB    CYS N 153   SG     -0.275                       
REMARK 500    GLY P  70   C     GLY P  70   O      -0.099                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    HIS C 140   CB  -  CA  -  C   ANGL. DEV. = -23.2 DEGREES          
REMARK 500    CYS F 153   CA  -  CB  -  SG  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    LEU K 111   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    CYS L 153   CA  -  CB  -  SG  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    TYR P  74   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES          
REMARK 500    THR P  75   C   -  N   -  CA  ANGL. DEV. = -18.5 DEGREES          
REMARK 500    CYS P 153   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500    CYS T 153   CA  -  CB  -  SG  ANGL. DEV. =  12.3 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    LEU A 111      -65.98   -126.63                                   
REMARK 500    THR B  75      150.21     65.27                                   
REMARK 500    CYS B 109      -58.10   -125.20                                   
REMARK 500    ALA C  75       51.83   -105.81                                   
REMARK 500    LEU C 111      -58.04   -126.26                                   
REMARK 500    ASP C 123       62.12     37.41                                   
REMARK 500    CYS D 109      -72.88   -138.16                                   
REMARK 500    CYS D 153       44.08   -107.38                                   
REMARK 500    VAL D 171      -78.90   -124.70                                   
REMARK 500    LYS E   2      109.05   -161.25                                   
REMARK 500    LEU E 111      -61.12   -122.06                                   
REMARK 500    TYR F  74      -79.97    -42.96                                   
REMARK 500    PRO F 123       90.60    -54.95                                   
REMARK 500    PHE G  63       69.77   -118.65                                   
REMARK 500    ALA G  75       51.76   -105.93                                   
REMARK 500    LEU G 111      -64.35   -120.90                                   
REMARK 500    ASN H 111      104.92    -56.43                                   
REMARK 500    PRO H 123       88.42    -68.23                                   
REMARK 500    ALA I  75       52.32    -96.78                                   
REMARK 500    CYS J 109      -60.52   -143.14                                   
REMARK 500    PRO J 123       88.31    -53.65                                   
REMARK 500    ALA K  75       55.94   -113.02                                   
REMARK 500    GLU K 109      -63.91    -92.31                                   
REMARK 500    LEU K 111      -64.08   -125.21                                   
REMARK 500    CYS L 109      -70.61   -128.95                                   
REMARK 500    PRO L 123       88.35    -63.79                                   
REMARK 500    ALA M  75       56.94   -104.01                                   
REMARK 500    LEU M 111      -46.42   -130.85                                   
REMARK 500    CYS N 109      -69.98   -133.41                                   
REMARK 500    PRO N 123       99.12    -60.81                                   
REMARK 500    ALA O  75       60.02   -117.63                                   
REMARK 500    LEU O 111      -55.45   -128.84                                   
REMARK 500    ASP P  21      -19.85    -48.10                                   
REMARK 500    CYS P 109      -74.04   -125.18                                   
REMARK 500    PRO P 123       88.06    -66.38                                   
REMARK 500    CYS P 153       68.07   -102.19                                   
REMARK 500    ALA Q  75       42.44   -105.70                                   
REMARK 500    THR R  75      133.62     79.44                                   
REMARK 500    LEU S 111      -63.83   -123.33                                   
REMARK 500    ASN T 146      130.11    177.05                                   
REMARK 500    LEU U 111      -58.62   -123.85                                   
REMARK 500    THR V  75      132.11     95.96                                   
REMARK 500    SER V 103      -78.52    -28.59                                   
REMARK 500    ILE V 104      -57.60    -24.15                                   
REMARK 500    CYS V 109      -76.73   -133.96                                   
REMARK 500    LEU W 111      -65.69   -126.79                                   
REMARK 500    THR X  75      154.62     81.41                                   
REMARK 500    CYS X 109      -60.74   -129.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR X  75        24.2      L          L   OUTSIDE RANGE           
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 CYC A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC H 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC I 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC J 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC J 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC K 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC L 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC L 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC M 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC N 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC N 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC O 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC P 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC P 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC Q 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC R 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC R 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC S 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC T 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC T 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC U 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC V 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC W 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC X 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYC X 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GXE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GY3   RELATED DB: PDB                                   
DBREF  4H0M A    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M B    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M C    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M D    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M E    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M F    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M G    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M H    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M I    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M J    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M K    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M L    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M M    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M N    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M O    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M P    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M Q    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M R    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M S    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M T    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M U    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M V    0   172  UNP    P06539   PHCB_SYNE7       1    173             
DBREF  4H0M W    0   162  UNP    P13530   PHCA_SYNE7       1    163             
DBREF  4H0M X    0   172  UNP    P06539   PHCB_SYNE7       1    173             
SEQRES   1 A  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 A  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 A  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 A  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 A  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 A  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 A  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 A  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 A  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 A  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 A  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 A  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 A  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 B  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 B  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 B  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 B  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 B  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 B  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 B  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 B  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 B  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 B  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 B  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 B  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 B  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 B  173  ALA ALA VAL ALA                                              
SEQRES   1 C  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 C  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 C  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 C  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 C  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 C  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 C  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 C  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 C  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 C  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 C  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 C  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 C  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 D  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 D  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 D  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 D  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 D  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 D  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 D  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 D  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 D  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 D  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 D  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 D  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 D  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 D  173  ALA ALA VAL ALA                                              
SEQRES   1 E  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 E  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 E  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 E  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 E  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 E  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 E  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 E  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 E  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 E  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 E  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 E  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 E  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 F  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 F  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 F  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 F  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 F  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 F  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 F  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 F  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 F  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 F  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 F  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 F  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 F  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 F  173  ALA ALA VAL ALA                                              
SEQRES   1 G  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 G  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 G  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 G  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 G  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 G  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 G  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 G  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 G  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 G  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 G  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 G  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 G  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 H  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 H  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 H  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 H  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 H  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 H  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 H  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 H  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 H  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 H  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 H  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 H  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 H  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 H  173  ALA ALA VAL ALA                                              
SEQRES   1 I  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 I  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 I  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 I  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 I  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 I  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 I  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 I  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 I  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 I  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 I  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 I  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 I  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 J  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 J  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 J  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 J  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 J  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 J  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 J  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 J  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 J  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 J  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 J  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 J  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 J  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 J  173  ALA ALA VAL ALA                                              
SEQRES   1 K  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 K  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 K  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 K  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 K  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 K  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 K  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 K  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 K  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 K  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 K  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 K  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 K  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 L  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 L  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 L  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 L  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 L  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 L  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 L  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 L  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 L  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 L  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 L  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 L  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 L  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 L  173  ALA ALA VAL ALA                                              
SEQRES   1 M  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 M  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 M  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 M  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 M  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 M  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 M  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 M  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 M  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 M  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 M  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 M  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 M  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 N  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 N  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 N  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 N  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 N  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 N  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 N  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 N  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 N  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 N  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 N  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 N  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 N  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 N  173  ALA ALA VAL ALA                                              
SEQRES   1 O  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 O  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 O  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 O  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 O  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 O  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 O  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 O  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 O  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 O  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 O  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 O  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 O  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 P  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 P  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 P  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 P  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 P  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 P  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 P  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 P  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 P  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 P  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 P  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 P  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 P  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 P  173  ALA ALA VAL ALA                                              
SEQRES   1 Q  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 Q  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 Q  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 Q  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 Q  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 Q  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 Q  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 Q  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 Q  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 Q  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 Q  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 Q  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 Q  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 R  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 R  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 R  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 R  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 R  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 R  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 R  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 R  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 R  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 R  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 R  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 R  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 R  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 R  173  ALA ALA VAL ALA                                              
SEQRES   1 S  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 S  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 S  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 S  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 S  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 S  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 S  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 S  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 S  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 S  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 S  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 S  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 S  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 T  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 T  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 T  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 T  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 T  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 T  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 T  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 T  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 T  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 T  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 T  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 T  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 T  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 T  173  ALA ALA VAL ALA                                              
SEQRES   1 U  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 U  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 U  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 U  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 U  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 U  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 U  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 U  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 U  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 U  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 U  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 U  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 U  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 V  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 V  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 V  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 V  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 V  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 V  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 V  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 V  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 V  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 V  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 V  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 V  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 V  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 V  173  ALA ALA VAL ALA                                              
SEQRES   1 W  163  MET SER LYS THR PRO LEU THR GLU ALA VAL ALA ALA ALA          
SEQRES   2 W  163  ASP SER GLN GLY ARG PHE LEU SER SER THR GLU LEU GLN          
SEQRES   3 W  163  VAL ALA PHE GLY ARG PHE ARG GLN ALA ALA SER GLY LEU          
SEQRES   4 W  163  ALA ALA ALA LYS ALA LEU ALA ASN ASN ALA ASP SER LEU          
SEQRES   5 W  163  VAL ASN GLY ALA ALA ASN ALA VAL TYR SER LYS PHE PRO          
SEQRES   6 W  163  TYR THR THR SER THR PRO GLY ASN ASN PHE ALA SER THR          
SEQRES   7 W  163  PRO GLU GLY LYS ALA LYS CYS ALA ARG ASP ILE GLY TYR          
SEQRES   8 W  163  TYR LEU ARG ILE VAL THR TYR ALA LEU VAL ALA GLY GLY          
SEQRES   9 W  163  THR GLY PRO ILE ASP GLU TYR LEU LEU ALA GLY LEU ASP          
SEQRES  10 W  163  GLU ILE ASN LYS THR PHE ASP LEU ALA PRO SER TRP TYR          
SEQRES  11 W  163  VAL GLU ALA LEU LYS TYR ILE LYS ALA ASN HIS GLY LEU          
SEQRES  12 W  163  SER GLY ASP SER ARG ASP GLU ALA ASN SER TYR ILE ASP          
SEQRES  13 W  163  TYR LEU ILE ASN ALA LEU SER                                  
SEQRES   1 X  173  MET THR PHE ASP ALA PHE THR LYS VAL VAL ALA GLN ALA          
SEQRES   2 X  173  ASP ALA ARG GLY GLU PHE LEU SER ASP ALA GLN LEU ASP          
SEQRES   3 X  173  ALA LEU SER ARG LEU VAL ALA GLU GLY ASN LYS ARG ILE          
SEQRES   4 X  173  ASP THR VAL ASN ARG ILE THR GLY ASN ALA SER SER ILE          
SEQRES   5 X  173  VAL ALA ASN ALA ALA ARG ALA LEU PHE ALA GLU GLN PRO          
SEQRES   6 X  173  SER LEU ILE ALA PRO GLY GLY MEN ALA TYR THR ASN ARG          
SEQRES   7 X  173  ARG MET ALA ALA CYS LEU ARG ASP MET GLU ILE ILE LEU          
SEQRES   8 X  173  ARG TYR VAL THR TYR ALA VAL PHE THR GLY ASP ALA SER          
SEQRES   9 X  173  ILE LEU ASP ASP ARG CYS LEU ASN GLY LEU ARG GLU THR          
SEQRES  10 X  173  TYR LEU ALA LEU GLY VAL PRO GLY ALA SER VAL ALA GLU          
SEQRES  11 X  173  GLY VAL ARG LYS MET LYS ASP ALA ALA VAL ALA ILE VAL          
SEQRES  12 X  173  SER ASP ARG ASN GLY ILE THR GLN GLY ASP CYS SER ALA          
SEQRES  13 X  173  ILE ILE SER GLU LEU GLY SER TYR PHE ASP LYS ALA ALA          
SEQRES  14 X  173  ALA ALA VAL ALA                                              
MODRES 4H0M MEN B   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN D   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN F   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN H   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN J   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN L   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN N   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN P   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN R   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN T   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN V   72  ASN  N-METHYL ASPARAGINE                                
MODRES 4H0M MEN X   72  ASN  N-METHYL ASPARAGINE                                
HET    MEN  B  72       9                                                       
HET    MEN  D  72       9                                                       
HET    MEN  F  72       9                                                       
HET    MEN  H  72       9                                                       
HET    MEN  J  72       9                                                       
HET    MEN  L  72       9                                                       
HET    MEN  N  72       9                                                       
HET    MEN  P  72       9                                                       
HET    MEN  R  72       9                                                       
HET    MEN  T  72       9                                                       
HET    MEN  V  72       9                                                       
HET    MEN  X  72       9                                                       
HET    CYC  A 201      43                                                       
HET    CYC  B 201      43                                                       
HET    CYC  B 202      43                                                       
HET    CYC  C 201      43                                                       
HET    CYC  D 201      43                                                       
HET    CYC  D 202      43                                                       
HET    CYC  E 201      43                                                       
HET    CYC  F 201      43                                                       
HET    CYC  F 202      43                                                       
HET    CYC  G 201      43                                                       
HET    CYC  H 201      43                                                       
HET    CYC  H 202      43                                                       
HET    CYC  I 201      43                                                       
HET    CYC  J 201      43                                                       
HET    CYC  J 202      43                                                       
HET    CYC  K 201      43                                                       
HET    CYC  L 201      43                                                       
HET    CYC  L 202      43                                                       
HET    CYC  M 201      43                                                       
HET    CYC  N 201      43                                                       
HET    CYC  N 202      43                                                       
HET    CYC  O 201      43                                                       
HET    CYC  P 201      43                                                       
HET    CYC  P 202      43                                                       
HET    CYC  Q 201      43                                                       
HET    CYC  R 201      43                                                       
HET    CYC  R 202      43                                                       
HET    CYC  S 201      43                                                       
HET    CYC  T 201      43                                                       
HET    CYC  T 202      43                                                       
HET    CYC  U 201      43                                                       
HET    CYC  V 201      43                                                       
HET    CYC  V 202      43                                                       
HET    CYC  W 201      43                                                       
HET    CYC  X 201      43                                                       
HET    CYC  X 202      43                                                       
HETNAM     MEN N-METHYL ASPARAGINE                                              
HETNAM     CYC PHYCOCYANOBILIN                                                  
FORMUL   2  MEN    12(C5 H10 N2 O3)                                             
FORMUL  25  CYC    36(C33 H40 N4 O6)                                            
FORMUL  61  HOH   *772(H2 O)                                                    
HELIX    1   1 THR A    3  GLY A   16  1                                  14    
HELIX    2   2 SER A   20  ASN A   47  1                                  28    
HELIX    3   3 ASN A   47  PHE A   63  1                                  17    
HELIX    4   4 PRO A   64  THR A   69  1                                   6    
HELIX    5   5 THR A   77  GLY A  102  1                                  26    
HELIX    6   6 THR A  104  LEU A  111  1                                   8    
HELIX    7   7 GLY A  114  PHE A  122  1                                   9    
HELIX    8   8 ALA A  125  HIS A  140  1                                  16    
HELIX    9   9 SER A  143  LEU A  161  1                                  19    
HELIX   10  10 ASP B    3  ARG B   15  1                                  13    
HELIX   11  11 SER B   20  GLU B   33  1                                  14    
HELIX   12  12 GLU B   33  ASN B   47  1                                  15    
HELIX   13  13 ASN B   47  GLN B   63  1                                  17    
HELIX   14  14 PRO B   64  ILE B   67  5                                   4    
HELIX   15  15 THR B   75  GLY B  100  1                                  26    
HELIX   16  16 ALA B  102  CYS B  109  1                                   8    
HELIX   17  17 GLY B  112  GLY B  121  1                                  10    
HELIX   18  18 PRO B  123  SER B  143  1                                  21    
HELIX   19  19 CYS B  153  ALA B  172  1                                  20    
HELIX   20  20 THR C    3  GLN C   15  1                                  13    
HELIX   21  21 SER C   20  ASN C   47  1                                  28    
HELIX   22  22 ASN C   47  PHE C   63  1                                  17    
HELIX   23  23 PRO C   64  THR C   69  1                                   6    
HELIX   24  24 THR C   77  GLY C  102  1                                  26    
HELIX   25  25 THR C  104  LEU C  111  1                                   8    
HELIX   26  26 GLY C  114  PHE C  122  1                                   9    
HELIX   27  27 ALA C  125  ASN C  139  1                                  15    
HELIX   28  28 SER C  143  LEU C  161  1                                  19    
HELIX   29  29 ASP D    3  GLY D   16  1                                  14    
HELIX   30  30 SER D   20  GLU D   33  1                                  14    
HELIX   31  31 GLU D   33  ASN D   47  1                                  15    
HELIX   32  32 ASN D   47  GLN D   63  1                                  17    
HELIX   33  33 PRO D   64  ILE D   67  5                                   4    
HELIX   34  34 THR D   75  GLY D  100  1                                  26    
HELIX   35  35 ALA D  102  CYS D  109  1                                   8    
HELIX   36  36 GLY D  112  GLY D  121  1                                  10    
HELIX   37  37 PRO D  123  ASP D  144  1                                  22    
HELIX   38  38 CYS D  153  ALA D  170  1                                  18    
HELIX   39  39 THR E    3  GLN E   15  1                                  13    
HELIX   40  40 SER E   20  ASN E   47  1                                  28    
HELIX   41  41 ASN E   47  PHE E   63  1                                  17    
HELIX   42  42 PRO E   64  THR E   69  1                                   6    
HELIX   43  43 THR E   77  GLY E  102  1                                  26    
HELIX   44  44 THR E  104  LEU E  111  1                                   8    
HELIX   45  45 GLY E  114  PHE E  122  1                                   9    
HELIX   46  46 ALA E  125  HIS E  140  1                                  16    
HELIX   47  47 SER E  143  LEU E  161  1                                  19    
HELIX   48  48 ASP F    3  ARG F   15  1                                  13    
HELIX   49  49 SER F   20  GLU F   33  1                                  14    
HELIX   50  50 GLU F   33  ASN F   47  1                                  15    
HELIX   51  51 ASN F   47  GLN F   63  1                                  17    
HELIX   52  52 PRO F   64  ALA F   68  5                                   5    
HELIX   53  53 THR F   75  GLY F  100  1                                  26    
HELIX   54  54 ALA F  102  CYS F  109  1                                   8    
HELIX   55  55 GLY F  112  GLY F  121  1                                  10    
HELIX   56  56 PRO F  123  ASP F  144  1                                  22    
HELIX   57  57 CYS F  153  ALA F  170  1                                  18    
HELIX   58  58 THR G    3  GLN G   15  1                                  13    
HELIX   59  59 SER G   20  ASN G   47  1                                  28    
HELIX   60  60 ASN G   47  PHE G   63  1                                  17    
HELIX   61  61 PRO G   64  THR G   69  1                                   6    
HELIX   62  62 THR G   77  GLY G  102  1                                  26    
HELIX   63  63 THR G  104  LEU G  111  1                                   8    
HELIX   64  64 GLY G  114  PHE G  122  1                                   9    
HELIX   65  65 ALA G  125  ASN G  139  1                                  15    
HELIX   66  66 SER G  143  LEU G  161  1                                  19    
HELIX   67  67 ASP H    3  ALA H   14  1                                  12    
HELIX   68  68 SER H   20  GLU H   33  1                                  14    
HELIX   69  69 GLU H   33  ASN H   47  1                                  15    
HELIX   70  70 ASN H   47  GLN H   63  1                                  17    
HELIX   71  71 PRO H   64  ILE H   67  5                                   4    
HELIX   72  72 THR H   75  GLY H  100  1                                  26    
HELIX   73  73 ALA H  102  CYS H  109  1                                   8    
HELIX   74  74 GLY H  112  ALA H  119  1                                   8    
HELIX   75  75 PRO H  123  ASP H  144  1                                  22    
HELIX   76  76 CYS H  153  ALA H  170  1                                  18    
HELIX   77  77 THR I    3  GLN I   15  1                                  13    
HELIX   78  78 SER I   20  ASN I   47  1                                  28    
HELIX   79  79 ASN I   47  PHE I   63  1                                  17    
HELIX   80  80 PRO I   64  THR I   69  1                                   6    
HELIX   81  81 THR I   77  GLY I  102  1                                  26    
HELIX   82  82 THR I  104  LEU I  111  1                                   8    
HELIX   83  83 GLY I  114  PHE I  122  1                                   9    
HELIX   84  84 ALA I  125  HIS I  140  1                                  16    
HELIX   85  85 SER I  143  LEU I  161  1                                  19    
HELIX   86  86 ASP J    3  ALA J   14  1                                  12    
HELIX   87  87 SER J   20  GLU J   33  1                                  14    
HELIX   88  88 GLU J   33  GLY J   46  1                                  14    
HELIX   89  89 ASN J   47  GLN J   63  1                                  17    
HELIX   90  90 PRO J   64  ILE J   67  5                                   4    
HELIX   91  91 THR J   75  GLY J  100  1                                  26    
HELIX   92  92 ALA J  102  CYS J  109  1                                   8    
HELIX   93  93 GLY J  112  GLY J  121  1                                  10    
HELIX   94  94 PRO J  123  ASP J  144  1                                  22    
HELIX   95  95 CYS J  153  ALA J  172  1                                  20    
HELIX   96  96 THR K    3  GLN K   15  1                                  13    
HELIX   97  97 SER K   20  ASN K   47  1                                  28    
HELIX   98  98 ASN K   47  PHE K   63  1                                  17    
HELIX   99  99 PRO K   64  THR K   67  5                                   4    
HELIX  100 100 THR K   77  GLY K  102  1                                  26    
HELIX  101 101 THR K  104  LEU K  111  1                                   8    
HELIX  102 102 GLY K  114  PHE K  122  1                                   9    
HELIX  103 103 ALA K  125  ASN K  139  1                                  15    
HELIX  104 104 GLY K  144  LEU K  161  1                                  18    
HELIX  105 105 ASP L    3  ARG L   15  1                                  13    
HELIX  106 106 SER L   20  GLU L   33  1                                  14    
HELIX  107 107 GLU L   33  GLY L   46  1                                  14    
HELIX  108 108 ASN L   47  GLN L   63  1                                  17    
HELIX  109 109 PRO L   64  ILE L   67  5                                   4    
HELIX  110 110 THR L   75  GLY L  100  1                                  26    
HELIX  111 111 ALA L  102  CYS L  109  1                                   8    
HELIX  112 112 GLY L  112  GLY L  121  1                                  10    
HELIX  113 113 PRO L  123  ASP L  144  1                                  22    
HELIX  114 114 CYS L  153  ALA L  172  1                                  20    
HELIX  115 115 THR M    3  GLN M   15  1                                  13    
HELIX  116 116 SER M   20  ASN M   47  1                                  28    
HELIX  117 117 ASN M   47  PHE M   63  1                                  17    
HELIX  118 118 PRO M   64  THR M   69  1                                   6    
HELIX  119 119 THR M   77  GLY M  102  1                                  26    
HELIX  120 120 THR M  104  LEU M  111  1                                   8    
HELIX  121 121 GLY M  114  PHE M  122  1                                   9    
HELIX  122 122 ALA M  125  ALA M  138  1                                  14    
HELIX  123 123 SER M  143  LEU M  161  1                                  19    
HELIX  124 124 ASP N    3  ALA N   14  1                                  12    
HELIX  125 125 SER N   20  GLU N   33  1                                  14    
HELIX  126 126 GLU N   33  ASN N   47  1                                  15    
HELIX  127 127 ASN N   47  GLN N   63  1                                  17    
HELIX  128 128 PRO N   64  ILE N   67  5                                   4    
HELIX  129 129 THR N   75  GLY N  100  1                                  26    
HELIX  130 130 ALA N  102  CYS N  109  1                                   8    
HELIX  131 131 GLY N  112  GLY N  121  1                                  10    
HELIX  132 132 PRO N  123  ASP N  144  1                                  22    
HELIX  133 133 CYS N  153  ALA N  172  1                                  20    
HELIX  134 134 THR O    3  GLN O   15  1                                  13    
HELIX  135 135 SER O   20  ASN O   47  1                                  28    
HELIX  136 136 ASN O   47  PHE O   63  1                                  17    
HELIX  137 137 PRO O   64  THR O   69  1                                   6    
HELIX  138 138 THR O   77  GLY O  102  1                                  26    
HELIX  139 139 THR O  104  LEU O  111  1                                   8    
HELIX  140 140 GLY O  114  PHE O  122  1                                   9    
HELIX  141 141 ALA O  125  ALA O  138  1                                  14    
HELIX  142 142 SER O  143  LEU O  161  1                                  19    
HELIX  143 143 ASP P    3  ALA P   14  1                                  12    
HELIX  144 144 SER P   20  GLU P   33  1                                  14    
HELIX  145 145 GLU P   33  GLY P   46  1                                  14    
HELIX  146 146 ASN P   47  GLN P   63  1                                  17    
HELIX  147 147 GLN P   63  ALA P   68  1                                   6    
HELIX  148 148 THR P   75  GLY P  100  1                                  26    
HELIX  149 149 ALA P  102  CYS P  109  1                                   8    
HELIX  150 150 GLY P  112  GLY P  121  1                                  10    
HELIX  151 151 PRO P  123  SER P  143  1                                  21    
HELIX  152 152 SER P  154  ALA P  172  1                                  19    
HELIX  153 153 THR Q    3  GLN Q   15  1                                  13    
HELIX  154 154 SER Q   20  ASN Q   47  1                                  28    
HELIX  155 155 ASN Q   47  PHE Q   63  1                                  17    
HELIX  156 156 PRO Q   64  THR Q   69  1                                   6    
HELIX  157 157 THR Q   77  GLY Q  102  1                                  26    
HELIX  158 158 THR Q  104  LEU Q  111  1                                   8    
HELIX  159 159 GLY Q  114  PHE Q  122  1                                   9    
HELIX  160 160 ALA Q  125  HIS Q  140  1                                  16    
HELIX  161 161 SER Q  143  LEU Q  161  1                                  19    
HELIX  162 162 ASP R    3  ALA R   14  1                                  12    
HELIX  163 163 SER R   20  GLU R   33  1                                  14    
HELIX  164 164 GLU R   33  ASN R   47  1                                  15    
HELIX  165 165 ASN R   47  GLN R   63  1                                  17    
HELIX  166 166 PRO R   64  ILE R   67  5                                   4    
HELIX  167 167 THR R   75  GLY R  100  1                                  26    
HELIX  168 168 ALA R  102  CYS R  109  1                                   8    
HELIX  169 169 GLY R  112  GLY R  121  1                                  10    
HELIX  170 170 PRO R  123  ASP R  144  1                                  22    
HELIX  171 171 CYS R  153  ALA R  172  1                                  20    
HELIX  172 172 THR S    3  GLY S   16  1                                  14    
HELIX  173 173 SER S   20  ASN S   47  1                                  28    
HELIX  174 174 ASN S   47  PHE S   63  1                                  17    
HELIX  175 175 PRO S   64  THR S   67  5                                   4    
HELIX  176 176 THR S   77  GLY S  102  1                                  26    
HELIX  177 177 THR S  104  LEU S  111  1                                   8    
HELIX  178 178 GLY S  114  PHE S  122  1                                   9    
HELIX  179 179 ALA S  125  HIS S  140  1                                  16    
HELIX  180 180 SER S  143  LEU S  161  1                                  19    
HELIX  181 181 ASP T    3  ALA T   14  1                                  12    
HELIX  182 182 SER T   20  GLU T   33  1                                  14    
HELIX  183 183 GLU T   33  GLN T   63  1                                  31    
HELIX  184 184 PRO T   64  ILE T   67  5                                   4    
HELIX  185 185 THR T   75  GLY T  100  1                                  26    
HELIX  186 186 ALA T  102  CYS T  109  1                                   8    
HELIX  187 187 GLY T  112  GLY T  121  1                                  10    
HELIX  188 188 PRO T  123  ASP T  144  1                                  22    
HELIX  189 189 CYS T  153  ALA T  172  1                                  20    
HELIX  190 190 THR U    3  GLY U   16  1                                  14    
HELIX  191 191 SER U   20  ASN U   47  1                                  28    
HELIX  192 192 ASN U   47  PHE U   63  1                                  17    
HELIX  193 193 PRO U   64  THR U   69  1                                   6    
HELIX  194 194 THR U   77  GLY U  102  1                                  26    
HELIX  195 195 THR U  104  LEU U  111  1                                   8    
HELIX  196 196 GLY U  114  PHE U  122  1                                   9    
HELIX  197 197 ALA U  125  ALA U  138  1                                  14    
HELIX  198 198 SER U  143  LEU U  161  1                                  19    
HELIX  199 199 ASP V    3  ALA V   14  1                                  12    
HELIX  200 200 SER V   20  GLU V   33  1                                  14    
HELIX  201 201 GLU V   33  GLY V   46  1                                  14    
HELIX  202 202 ASN V   47  GLN V   63  1                                  17    
HELIX  203 203 PRO V   64  ILE V   67  5                                   4    
HELIX  204 204 ARG V   77  GLY V  100  1                                  24    
HELIX  205 205 ALA V  102  CYS V  109  1                                   8    
HELIX  206 206 GLY V  112  GLY V  121  1                                  10    
HELIX  207 207 PRO V  123  ASP V  144  1                                  22    
HELIX  208 208 CYS V  153  ALA V  172  1                                  20    
HELIX  209 209 THR W    3  GLN W   15  1                                  13    
HELIX  210 210 SER W   20  ASN W   47  1                                  28    
HELIX  211 211 ASN W   47  PHE W   63  1                                  17    
HELIX  212 212 PRO W   64  THR W   69  1                                   6    
HELIX  213 213 THR W   77  GLY W  102  1                                  26    
HELIX  214 214 THR W  104  LEU W  111  1                                   8    
HELIX  215 215 GLY W  114  PHE W  122  1                                   9    
HELIX  216 216 ALA W  125  ASN W  139  1                                  15    
HELIX  217 217 SER W  143  LEU W  161  1                                  19    
HELIX  218 218 ASP X    3  GLY X   16  1                                  14    
HELIX  219 219 SER X   20  GLU X   33  1                                  14    
HELIX  220 220 GLU X   33  ASN X   47  1                                  15    
HELIX  221 221 ASN X   47  GLN X   63  1                                  17    
HELIX  222 222 PRO X   64  ILE X   67  5                                   4    
HELIX  223 223 THR X   75  GLY X  100  1                                  26    
HELIX  224 224 ALA X  102  CYS X  109  1                                   8    
HELIX  225 225 GLY X  112  GLY X  121  1                                  10    
HELIX  226 226 PRO X  123  ASP X  144  1                                  22    
HELIX  227 227 CYS X  153  ALA X  172  1                                  20    
LINK         C   GLY B  71                 N   MEN B  72     1555   1555  1.32  
LINK         C   MEN B  72                 N   ALA B  73     1555   1555  1.30  
LINK         C   GLY D  71                 N   MEN D  72     1555   1555  1.33  
LINK         C   MEN D  72                 N   ALA D  73     1555   1555  1.34  
LINK         C   GLY F  71                 N   MEN F  72     1555   1555  1.33  
LINK         C   MEN F  72                 N   ALA F  73     1555   1555  1.33  
LINK         C   GLY H  71                 N   MEN H  72     1555   1555  1.33  
LINK         C   MEN H  72                 N   ALA H  73     1555   1555  1.32  
LINK         C   GLY J  71                 N   MEN J  72     1555   1555  1.32  
LINK         C   MEN J  72                 N   ALA J  73     1555   1555  1.31  
LINK         C   GLY L  71                 N   MEN L  72     1555   1555  1.33  
LINK         C   MEN L  72                 N   ALA L  73     1555   1555  1.33  
LINK         C   GLY N  71                 N   MEN N  72     1555   1555  1.33  
LINK         C   MEN N  72                 N   ALA N  73     1555   1555  1.33  
LINK         C   GLY P  71                 N   MEN P  72     1555   1555  1.30  
LINK         C   MEN P  72                 N   ALA P  73     1555   1555  1.32  
LINK         C   GLY R  71                 N   MEN R  72     1555   1555  1.31  
LINK         C   MEN R  72                 N   ALA R  73     1555   1555  1.30  
LINK         C   GLY T  71                 N   MEN T  72     1555   1555  1.31  
LINK         C   MEN T  72                 N   ALA T  73     1555   1555  1.33  
LINK         C   GLY V  71                 N   MEN V  72     1555   1555  1.26  
LINK         C   MEN V  72                 N   ALA V  73     1555   1555  1.29  
LINK         C   GLY X  71                 N   MEN X  72     1555   1555  1.32  
LINK         C   MEN X  72                 N   ALA X  73     1555   1555  1.34  
LINK         SG  CYS X  82                 CAC CYC X 201     1555   1555  1.79  
LINK         SG  CYS D  82                 CAC CYC D 201     1555   1555  1.82  
LINK         SG  CYS F  82                 CAC CYC F 201     1555   1555  1.82  
LINK         SG  CYS N  82                 CAC CYC N 201     1555   1555  1.82  
LINK         SG  CYS P  82                 CAC CYC P 201     1555   1555  1.82  
LINK         SG  CYS J  82                 CAC CYC J 201     1555   1555  1.82  
LINK         SG  CYS B  82                 CAC CYC B 201     1555   1555  1.82  
LINK         SG  CYS T  82                 CAC CYC T 201     1555   1555  1.82  
LINK         SG  CYS H  82                 CAC CYC H 201     1555   1555  1.83  
LINK         SG  CYS R  82                 CAC CYC R 201     1555   1555  1.87  
LINK         SG  CYS A  84                 CAC CYC A 201     1555   1555  1.82  
LINK         SG  CYS U  84                 CAC CYC U 201     1555   1555  1.87  
LINK         SG  CYS M  84                 CAC CYC M 201     1555   1555  1.80  
LINK         SG  CYS I  84                 CAC CYC I 201     1555   1555  1.80  
LINK         SG  CYS G  84                 CAC CYC G 201     1555   1555  1.80  
LINK         SG  CYS O  84                 CAC CYC O 201     1555   1555  1.80  
LINK         SG  CYS Q  84                 CAC CYC Q 201     1555   1555  1.80  
LINK         SG  CYS C  84                 CAC CYC C 201     1555   1555  1.81  
LINK         SG  CYS K  84                 CAC CYC K 201     1555   1555  1.81  
LINK         SG  CYS W  84                 CAC CYC W 201     1555   1555  1.81  
LINK         SG  CYS E  84                 CAC CYC E 201     1555   1555  1.81  
LINK         SG  CYS S  84                 CAC CYC S 201     1555   1555  1.93  
LINK         SG  CYS B 153                 CAC CYC B 202     1555   1555  2.06  
LINK         SG  CYS D 153                 CAC CYC D 202     1555   1555  2.07  
LINK         SG  CYS J 153                 CAC CYC J 202     1555   1555  2.08  
LINK         SG  CYS V 153                 CAC CYC V 202     1555   1555  2.13  
LINK         SG  CYS P 153                 CAC CYC P 202     1555   1555  2.15  
LINK         SG  CYS F 153                 CAC CYC F 202     1555   1555  2.16  
LINK         SG  CYS H 153                 CAC CYC H 202     1555   1555  1.66  
LINK         SG  CYS L 153                 CAC CYC L 202     1555   1555  1.71  
LINK         SG  CYS N 153                 CAC CYC N 202     1555   1555  1.87  
LINK         SG  CYS T 153                 CAC CYC T 202     1555   1555  1.88  
LINK         SG  CYS R 153                 CAC CYC R 202     1555   1555  1.90  
LINK         SG  CYS X 153                 CAC CYC X 202     1555   1555  1.92  
CISPEP   1 GLY H   71    MEN H   72          0         7.56                     
CISPEP   2 GLY P   71    MEN P   72          0       -16.85                     
SITE     1 AC1 22 VAL A  59  THR A  66  ASN A  72  ASN A  73                    
SITE     2 AC1 22 PHE A  74  ALA A  75  LYS A  83  CYS A  84                    
SITE     3 AC1 22 ARG A  86  ASP A  87  ILE A  88  TYR A  90                    
SITE     4 AC1 22 TYR A 110  ILE A 118  PHE A 122  TRP A 128                    
SITE     5 AC1 22 TYR A 129  ARG D  57  TYR D  74  THR D  75                    
SITE     6 AC1 22 ASN D  76  MET D  79                                          
SITE     1 AC2 17 LEU B  66  MEN B  72  ALA B  73  ARG B  77                    
SITE     2 AC2 17 ARG B  78  CYS B  82  ARG B  84  ASP B  85                    
SITE     3 AC2 17 MET B  86  ILE B  88  ARG B 108  LEU B 113                    
SITE     4 AC2 17 LEU B 120  SER B 126  VAL B 127  HOH B 312                    
SITE     5 AC2 17 HOH B 340                                                     
SITE     1 AC3 17 PHE A  28  ASN B  35  LYS B  36  ASP B  39                    
SITE     2 AC3 17 ASN B  42  ARG B  43  VAL B 142  ASP B 144                    
SITE     3 AC3 17 ILE B 148  THR B 149  GLN B 150  GLY B 151                    
SITE     4 AC3 17 CYS B 153  HOH B 305  GLN K  33  ASP K 145                    
SITE     5 AC3 17 ASP K 148                                                     
SITE     1 AC4 24 VAL C  59  THR C  66  ASN C  72  ASN C  73                    
SITE     2 AC4 24 PHE C  74  ALA C  75  LYS C  83  CYS C  84                    
SITE     3 AC4 24 ARG C  86  ASP C  87  TYR C 110  ILE C 118                    
SITE     4 AC4 24 PHE C 122  LEU C 124  TRP C 128  TYR C 129                    
SITE     5 AC4 24 HOH C 301  HOH C 322  ARG F  57  ILE F  67                    
SITE     6 AC4 24 TYR F  74  THR F  75  ASN F  76  HOH F 309                    
SITE     1 AC5 13 LEU D  66  MEN D  72  ARG D  78  CYS D  82                    
SITE     2 AC5 13 ARG D  84  ASP D  85  MET D  86  ILE D  88                    
SITE     3 AC5 13 ARG D 108  LEU D 113  LEU D 120  VAL D 122                    
SITE     4 AC5 13 SER D 126                                                     
SITE     1 AC6 20 PHE C  28  ASN D  35  LYS D  36  ASP D  39                    
SITE     2 AC6 20 ASN D  42  VAL D 142  SER D 143  ASP D 144                    
SITE     3 AC6 20 ILE D 148  THR D 149  GLY D 151  CYS D 153                    
SITE     4 AC6 20 HOH D 301  HOH D 304  HOH D 318  ARG I  32                    
SITE     5 AC6 20 GLN I  33  ASP I 145  ASP I 148  GLU I 149                    
SITE     1 AC7 20 ARG B  57  THR B  75  ASN B  76  VAL E  59                    
SITE     2 AC7 20 THR E  66  ASN E  72  ASN E  73  PHE E  74                    
SITE     3 AC7 20 ALA E  75  LYS E  83  CYS E  84  ARG E  86                    
SITE     4 AC7 20 ASP E  87  TYR E  90  TYR E 110  PHE E 122                    
SITE     5 AC7 20 LEU E 124  TRP E 128  HOH E 301  HOH E 339                    
SITE     1 AC8 11 MEN F  72  ARG F  78  CYS F  82  ARG F  84                    
SITE     2 AC8 11 ASP F  85  ILE F  88  ARG F 108  LEU F 113                    
SITE     3 AC8 11 LEU F 120  PRO F 123  SER F 126                               
SITE     1 AC9 16 PHE E  28  ASN F  35  LYS F  36  ASP F  39                    
SITE     2 AC9 16 THR F  40  ARG F  43  VAL F 142  SER F 143                    
SITE     3 AC9 16 ASP F 144  THR F 149  GLY F 151  CYS F 153                    
SITE     4 AC9 16 ARG G  32  GLN G  33  ASP G 145  ASP G 148                    
SITE     1 BC1 23 VAL G  59  THR G  66  ASN G  72  ASN G  73                    
SITE     2 BC1 23 PHE G  74  ALA G  75  LYS G  83  CYS G  84                    
SITE     3 BC1 23 ASP G  87  TYR G  90  TYR G 110  LEU G 111                    
SITE     4 BC1 23 PHE G 122  LEU G 124  TRP G 128  TYR G 129                    
SITE     5 BC1 23 HOH G 301  HOH G 303  ARG J  57  ILE J  67                    
SITE     6 BC1 23 TYR J  74  THR J  75  ASN J  76                               
SITE     1 BC2 14 LEU H  66  MEN H  72  ALA H  73  ARG H  77                    
SITE     2 BC2 14 ARG H  78  CYS H  82  ASP H  85  MET H  86                    
SITE     3 BC2 14 ILE H  88  ARG H 108  LEU H 113  LEU H 120                    
SITE     4 BC2 14 VAL H 122  SER H 126                                          
SITE     1 BC3 19 ARG E  32  GLN E  33  ASP E 145  ASP E 148                    
SITE     2 BC3 19 LEU G  24  PHE G  28  ASN H  35  LYS H  36                    
SITE     3 BC3 19 ASP H  39  THR H  40  ARG H  43  VAL H 142                    
SITE     4 BC3 19 SER H 143  ASP H 144  THR H 149  GLY H 151                    
SITE     5 BC3 19 CYS H 153  HOH H 310  HOH H 316                               
SITE     1 BC4 23 VAL I  59  THR I  66  ASN I  72  ASN I  73                    
SITE     2 BC4 23 PHE I  74  ALA I  75  LYS I  83  CYS I  84                    
SITE     3 BC4 23 ARG I  86  ASP I  87  ILE I  88  TYR I  90                    
SITE     4 BC4 23 TYR I 110  PHE I 122  TRP I 128  TYR I 129                    
SITE     5 BC4 23 HOH I 303  HOH I 307  ARG L  57  ILE L  67                    
SITE     6 BC4 23 TYR L  74  THR L  75  ASN L  76                               
SITE     1 BC5 14 LEU J  66  MEN J  72  ALA J  73  ARG J  77                    
SITE     2 BC5 14 ARG J  78  CYS J  82  ASP J  85  MET J  86                    
SITE     3 BC5 14 ARG J 108  LEU J 113  LEU J 120  PRO J 123                    
SITE     4 BC5 14 SER J 126  VAL J 127                                          
SITE     1 BC6 18 ARG C  32  GLN C  33  ASP C 145  ASP C 148                    
SITE     2 BC6 18 PHE I  28  ASN J  35  LYS J  36  ASP J  39                    
SITE     3 BC6 18 ASN J  42  VAL J 142  SER J 143  ASP J 144                    
SITE     4 BC6 18 THR J 149  GLN J 150  GLY J 151  CYS J 153                    
SITE     5 BC6 18 HOH J 314  HOH J 315                                          
SITE     1 BC7 22 ARG H  57  ILE H  67  TYR H  74  THR H  75                    
SITE     2 BC7 22 ASN H  76  THR K  66  ASN K  72  ASN K  73                    
SITE     3 BC7 22 PHE K  74  ALA K  75  LYS K  83  CYS K  84                    
SITE     4 BC7 22 ARG K  86  ASP K  87  TYR K 110  PHE K 122                    
SITE     5 BC7 22 LEU K 124  TRP K 128  TYR K 129  HOH K 301                    
SITE     6 BC7 22 HOH K 304  HOH K 311                                          
SITE     1 BC8 12 MEN L  72  ALA L  73  ARG L  78  CYS L  82                    
SITE     2 BC8 12 ASP L  85  MET L  86  ILE L  88  ARG L 108                    
SITE     3 BC8 12 CYS L 109  LEU L 120  PRO L 123  SER L 126                    
SITE     1 BC9 17 ARG A  32  GLN A  33  ASP A 145  ASP A 148                    
SITE     2 BC9 17 PHE K  28  ASN L  35  LYS L  36  ASP L  39                    
SITE     3 BC9 17 ARG L  43  VAL L 142  SER L 143  ASP L 144                    
SITE     4 BC9 17 ARG L 145  THR L 149  GLY L 151  CYS L 153                    
SITE     5 BC9 17 HOH L 309                                                     
SITE     1 CC1 21 VAL M  59  THR M  66  ASN M  72  ASN M  73                    
SITE     2 CC1 21 PHE M  74  ALA M  75  CYS M  84  ARG M  86                    
SITE     3 CC1 21 ASP M  87  TYR M  90  TYR M 110  PHE M 122                    
SITE     4 CC1 21 LEU M 124  TRP M 128  TYR M 129  HOH M 301                    
SITE     5 CC1 21 HOH M 310  HOH M 316  ARG P  57  TYR P  74                    
SITE     6 CC1 21 ASN P  76                                                     
SITE     1 CC2 12 MEN N  72  ALA N  73  ARG N  77  ARG N  78                    
SITE     2 CC2 12 CYS N  82  ASP N  85  MET N  86  ILE N  88                    
SITE     3 CC2 12 ARG N 108  LEU N 113  SER N 126  HOH N 303                    
SITE     1 CC3 19 LEU M  24  PHE M  28  ASN N  35  LYS N  36                    
SITE     2 CC3 19 ASP N  39  THR N  40  ASN N  42  ARG N  43                    
SITE     3 CC3 19 VAL N 142  SER N 143  ASP N 144  ILE N 148                    
SITE     4 CC3 19 THR N 149  GLN N 150  GLY N 151  CYS N 153                    
SITE     5 CC3 19 GLN W  33  ASP W 145  ASP W 148                               
SITE     1 CC4 21 THR O  66  ASN O  72  ASN O  73  PHE O  74                    
SITE     2 CC4 21 ALA O  75  LYS O  83  CYS O  84  ARG O  86                    
SITE     3 CC4 21 ASP O  87  TYR O  90  TYR O 110  TRP O 128                    
SITE     4 CC4 21 TYR O 129  HOH O 301  HOH O 305  HOH O 333                    
SITE     5 CC4 21 ARG R  57  ILE R  67  THR R  75  ASN R  76                    
SITE     6 CC4 21 HOH R 309                                                     
SITE     1 CC5 13 LEU P  66  MEN P  72  ALA P  73  ARG P  77                    
SITE     2 CC5 13 CYS P  82  ARG P  84  ASP P  85  MET P  86                    
SITE     3 CC5 13 ILE P  88  ARG P 108  LEU P 120  VAL P 122                    
SITE     4 CC5 13 SER P 126                                                     
SITE     1 CC6 17 PHE O  28  ASN P  35  LYS P  36  ASP P  39                    
SITE     2 CC6 17 VAL P 142  SER P 143  ASP P 144  ARG P 145                    
SITE     3 CC6 17 THR P 149  GLY P 151  CYS P 153  HOH P 309                    
SITE     4 CC6 17 HOH P 316  GLN U  33  ASP U 145  ASP U 148                    
SITE     5 CC6 17 HOH U 333                                                     
SITE     1 CC7 24 ARG N  57  TYR N  74  THR N  75  ASN N  76                    
SITE     2 CC7 24 VAL Q  59  THR Q  66  ASN Q  72  ASN Q  73                    
SITE     3 CC7 24 PHE Q  74  ALA Q  75  LYS Q  83  CYS Q  84                    
SITE     4 CC7 24 ARG Q  86  ASP Q  87  TYR Q  90  TYR Q 110                    
SITE     5 CC7 24 LEU Q 111  PHE Q 122  LEU Q 124  TRP Q 128                    
SITE     6 CC7 24 TYR Q 129  HOH Q 301  HOH Q 323  HOH Q 325                    
SITE     1 CC8 15 MEN R  72  ALA R  73  ARG R  78  ALA R  81                    
SITE     2 CC8 15 CYS R  82  ARG R  84  ASP R  85  MET R  86                    
SITE     3 CC8 15 ILE R  88  ARG R 108  CYS R 109  LEU R 120                    
SITE     4 CC8 15 VAL R 122  SER R 126  HOH R 302                               
SITE     1 CC9 17 PHE Q  28  ASN R  35  LYS R  36  ASP R  39                    
SITE     2 CC9 17 THR R  40  VAL R 142  SER R 143  ILE R 148                    
SITE     3 CC9 17 THR R 149  GLY R 151  CYS R 153  HOH R 313                    
SITE     4 CC9 17 GLN S  33  ASP S 145  ASP S 148  GLU S 149                    
SITE     5 CC9 17 HOH S 318                                                     
SITE     1 DC1 22 THR S  66  ASN S  72  ASN S  73  PHE S  74                    
SITE     2 DC1 22 ALA S  75  LYS S  83  CYS S  84  ARG S  86                    
SITE     3 DC1 22 ASP S  87  TYR S  90  ILE S  94  TYR S 110                    
SITE     4 DC1 22 PHE S 122  LEU S 124  TYR S 129  HOH S 306                    
SITE     5 DC1 22 HOH S 338  ARG V  57  ILE V  67  THR V  75                    
SITE     6 DC1 22 ASN V  76  HOH V 314                                          
SITE     1 DC2 12 MEN T  72  ARG T  77  ARG T  78  ALA T  81                    
SITE     2 DC2 12 CYS T  82  ASP T  85  MET T  86  ILE T  88                    
SITE     3 DC2 12 ARG T 108  LEU T 120  VAL T 122  SER T 126                    
SITE     1 DC3 19 ARG Q  32  GLN Q  33  ASP Q 145  ASP Q 148                    
SITE     2 DC3 19 GLU Q 149  HOH Q 320  PHE S  28  ASN T  35                    
SITE     3 DC3 19 LYS T  36  ASP T  39  VAL T 142  SER T 143                    
SITE     4 DC3 19 ASP T 144  THR T 149  GLN T 150  GLY T 151                    
SITE     5 DC3 19 CYS T 153  HOH T 313  HOH T 314                               
SITE     1 DC4 21 VAL U  59  THR U  66  ASN U  72  ASN U  73                    
SITE     2 DC4 21 PHE U  74  ALA U  75  LYS U  83  CYS U  84                    
SITE     3 DC4 21 ARG U  86  ASP U  87  ILE U  88  TYR U 110                    
SITE     4 DC4 21 PHE U 122  TRP U 128  TYR U 129  HOH U 321                    
SITE     5 DC4 21 HOH U 325  ARG X  57  THR X  75  ASN X  76                    
SITE     6 DC4 21 HOH X 324                                                     
SITE     1 DC5 12 MEN V  72  ALA V  73  ARG V  78  CYS V  82                    
SITE     2 DC5 12 ASP V  85  ILE V  88  ARG V 108  LEU V 113                    
SITE     3 DC5 12 LEU V 120  VAL V 122  SER V 126  HOH V 329                    
SITE     1 DC6 16 GLN O  33  ASP O 145  ASP O 148  PHE U  28                    
SITE     2 DC6 16 ALA V  32  ASN V  35  ASP V  39  THR V  40                    
SITE     3 DC6 16 ARG V  43  VAL V 142  ASP V 144  THR V 149                    
SITE     4 DC6 16 GLN V 150  GLY V 151  CYS V 153  HOH V 306                    
SITE     1 DC7 21 ARG T  57  ILE T  67  TYR T  74  ASN T  76                    
SITE     2 DC7 21 HOH T 318  THR W  66  ASN W  72  ASN W  73                    
SITE     3 DC7 21 PHE W  74  ALA W  75  LYS W  83  CYS W  84                    
SITE     4 DC7 21 ARG W  86  ASP W  87  TYR W 110  PHE W 122                    
SITE     5 DC7 21 LEU W 124  TRP W 128  TYR W 129  HOH W 301                    
SITE     6 DC7 21 HOH W 327                                                     
SITE     1 DC8 14 MEN X  72  ALA X  73  ARG X  77  ARG X  78                    
SITE     2 DC8 14 CYS X  82  ARG X  84  ASP X  85  MET X  86                    
SITE     3 DC8 14 ILE X  88  ARG X 108  LEU X 113  LEU X 120                    
SITE     4 DC8 14 PRO X 123  SER X 126                                          
SITE     1 DC9 16 GLN M  33  ASP M 145  ASP M 148  PHE W  28                    
SITE     2 DC9 16 ASN X  35  LYS X  36  ASP X  39  THR X  40                    
SITE     3 DC9 16 VAL X 142  SER X 143  ASP X 144  THR X 149                    
SITE     4 DC9 16 GLY X 151  CYS X 153  HOH X 301  HOH X 315                    
CRYST1  106.840  113.520  184.440  90.00  89.97  90.00 P 1 21 1     24          
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      0.009360  0.000000 -0.000005        0.00000                         
SCALE2      0.000000  0.008809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005422        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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