HEADER    CELL ADHESION                           13-NOV-97   1AY2              
TITLE     STRUCTURE OF THE FIBER-FORMING PROTEIN PILIN AT 2.6 ANGSTROMS         
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE 4 PILIN;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FIMBRIAE                                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEISSERIA GONORRHOEAE;                          
SOURCE   3 ORGANISM_TAXID: 485;                                                 
SOURCE   4 STRAIN: MS11;                                                        
SOURCE   5 ORGANELLE: PILUS;                                                    
SOURCE   6 CELLULAR_LOCATION: EXTRACELLULAR                                     
KEYWDS    TYPE IV PILIN, FIBER-FORMING PROTEIN, MEMBRANE PROTEIN, DNA INDING    
KEYWDS   2 PROTEIN, CONTRACTILE PROTEIN, CELL ADHESION                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.T.FOREST,H.E.PARGE,J.A.TAINER                                       
REVDAT   5   15-FEB-23 1AY2    1       COMPND REMARK SEQRES HET                 
REVDAT   5 2                   1       HETNAM HETSYN FORMUL LINK                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   29-JUL-20 1AY2    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   13-JUL-11 1AY2    1       VERSN                                    
REVDAT   2   24-FEB-09 1AY2    1       VERSN                                    
REVDAT   1   29-APR-98 1AY2    0                                                
JRNL        AUTH   H.E.PARGE,K.T.FOREST,M.J.HICKEY,D.A.CHRISTENSEN,E.D.GETZOFF, 
JRNL        AUTH 2 J.A.TAINER                                                   
JRNL        TITL   STRUCTURE OF THE FIBRE-FORMING PROTEIN PILIN AT 2.6 A        
JRNL        TITL 2 RESOLUTION.                                                  
JRNL        REF    NATURE                        V. 378    32 1995              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7477282                                                      
JRNL        DOI    10.1038/378032A0                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 6565                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 723                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 1208                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 129                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.25000                                             
REMARK   3    B22 (A**2) : 8.25000                                              
REMARK   3    B33 (A**2) : -4.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 10.0                            
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) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.359                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
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  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM_AUX.PRO                                  
REMARK   3  PARAMETER FILE  3  : PARAM3_MOD.CHO                                 
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  3   : HEPT123.TOP                                    
REMARK   3  TOPOLOGY FILE  4   : TOPH19.PEP                                     
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  SOLVENT FLATTENING (WITH 50%) SOLVENT) USING PHASES WAS USED TO     
REMARK   3  IMPROVE PHASES (F.O.M. INCREASED FROM 0.75 - 0.86) FOR FITTING.     
REMARK   3  DATA FROM A PT-SOAKED DERIVATIVE CRYSTAL WAS USED FOR REFINEMENT    
REMARK   3  BECAUSE IT WAS STRONGER THAN "NATIVE" DATA.                         
REMARK   3                                                                      
REMARK   3  THE EXPECTED N-TERMINAL METHYL-PHE WAS VERIFIED BY                  
REMARK   3  N-TERMINAL SEQUENCING BUT WAS NOT INCLUDED IN THE MODEL             
REMARK   3  BECAUSE IT WAS NOT APPARENT IN ELECTRON DENSITY.                    
REMARK   3                                                                      
REMARK   3  WATERS WERE NOT RESTRAINED DURING REFINEMENT AND TWO WATERS         
REMARK   3  (333 AND 348) MOVED CLOSE TO THE PT SITE.                           
REMARK   4                                                                      
REMARK   4 1AY2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171396.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAY-93                             
REMARK 200  TEMPERATURE           (KELVIN) : 290                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : BENT MIRROR                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, ROTAVATA, AGROVATA         
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6494                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 60%        
REMARK 280  PEG400, 50 MM CHESS, PH 8.0, 1% BETA-OCTYL GLUCOSIDE, 0.6% 1,2,3-   
REMARK 280  HEPTANETRIOL.                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z                                         
REMARK 290       7555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       63.79000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       60.54000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       63.79000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       60.54000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       63.79000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       60.54000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       63.79000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       60.54000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 PT    PT A 200  LIES ON A SPECIAL POSITION.                          
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    HIS A 146   NE2   HIS A 146   CD2    -0.079                       
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    PHE A   1   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES          
REMARK 500    THR A   2   N   -  CA  -  C   ANGL. DEV. =  24.1 DEGREES          
REMARK 500    VAL A  19   CA  -  CB  -  CG2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    TYR A  27   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    TRP A  57   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A  57   CB  -  CG  -  CD1 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    TRP A  57   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TRP A  57   CG  -  CD2 -  CE3 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    SER A  68   CA  -  CB  -  OG  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    TYR A  77   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    LEU A 106   CA  -  CB  -  CG  ANGL. DEV. =  21.5 DEGREES          
REMARK 500    TRP A 109   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP A 109   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP A 119   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP A 119   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TRP A 119   CG  -  CD2 -  CE3 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    VAL A 125   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 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    HIS A  54      -29.57   -147.14                                   
REMARK 500    GLU A 113       77.08   -109.63                                   
REMARK 500    ASN A 114      106.11     -4.61                                   
REMARK 500    ALA A 136       62.29   -118.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  50         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              PT A 200  PT                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  54   NE2                                                    
REMARK 620 2 HIS A  54   NE2  97.4                                              
REMARK 620 3 HOH A 333   O    73.6  60.2                                        
REMARK 620 4 HOH A 333   O    60.2  73.6 107.6                                  
REMARK 620 5 HOH A 348   O   173.0  79.2 109.3 112.9                            
REMARK 620 6 HOH A 348   O    79.2 173.1 113.0 109.4 104.9                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  1AY2 A    1   158  UNP    P02974   FMM1_NEIGO       8    165             
SEQRES   1 A  158  PHE THR LEU ILE GLU LEU MET ILE VAL ILE ALA ILE VAL          
SEQRES   2 A  158  GLY ILE LEU ALA ALA VAL ALA LEU PRO ALA TYR GLN ASP          
SEQRES   3 A  158  TYR THR ALA ARG ALA GLN VAL SER GLU ALA ILE LEU LEU          
SEQRES   4 A  158  ALA GLU GLY GLN LYS SER ALA VAL THR GLU TYR TYR LEU          
SEQRES   5 A  158  ASN HIS GLY LYS TRP PRO GLU ASN ASN THR SER ALA GLY          
SEQRES   6 A  158  VAL ALA SER PRO PRO SER ASP ILE LYS GLY LYS TYR VAL          
SEQRES   7 A  158  LYS GLU VAL GLU VAL LYS ASN GLY VAL VAL THR ALA THR          
SEQRES   8 A  158  MET LEU SER SER GLY VAL ASN ASN GLU ILE LYS GLY LYS          
SEQRES   9 A  158  LYS LEU SER LEU TRP ALA ARG ARG GLU ASN GLY SER VAL          
SEQRES  10 A  158  LYS TRP PHE CYS GLY GLN PRO VAL THR ARG THR ASP ASP          
SEQRES  11 A  158  ASP THR VAL ALA ASP ALA LYS ASP GLY LYS GLU ILE ASP          
SEQRES  12 A  158  THR LYS HIS LEU PRO SER THR CYS ARG ASP ASN PHE ASP          
SEQRES  13 A  158  ALA LYS                                                      
MODRES 1AY2 SER A   63  SER  GLYCOSYLATION SITE                                 
MODRES 1AY2 PHE A    1  PHE  METHYL L-PHENYLALANINATE                           
HET    NAG  B   1      14                                                       
HET    GLA  B   2      11                                                       
HET     PT  A 200       1                                                       
HET    HTO  A 162      10                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GLA ALPHA-D-GALACTOPYRANOSE                                          
HETNAM      PT PLATINUM (II) ION                                                
HETNAM     HTO HEPTANE-1,2,3-TRIOL                                              
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     GLA ALPHA-D-GALACTOSE; D-GALACTOSE; GALACTOSE; ALPHA D-              
HETSYN   2 GLA  GALACTOSE                                                       
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   2  GLA    C6 H12 O6                                                    
FORMUL   3   PT    PT 2+                                                        
FORMUL   4  HTO    C7 H16 O3                                                    
FORMUL   5  HOH   *129(H2 O)                                                    
HELIX    1   1 THR A    2  HIS A   54  1                                  53    
HELIX    2   2 ASN A   60  ALA A   64  1                                   5    
HELIX    3   3 PRO A   69  ASP A   72  5                                   4    
HELIX    4   4 ASN A   99  LYS A  102  5                                   4    
HELIX    5   5 THR A  144  HIS A  146  5                                   3    
SHEET    1   A 4 SER A 116  GLN A 123  0                                        
SHEET    2   A 4 LYS A 105  GLU A 113 -1  N  GLU A 113   O  SER A 116           
SHEET    3   A 4 VAL A  87  MET A  92 -1  N  ALA A  90   O  LEU A 106           
SHEET    4   A 4 VAL A  78  LYS A  84 -1  N  LYS A  84   O  VAL A  87           
SHEET    1   B 2 VAL A 125  ASP A 129  0                                        
SHEET    2   B 2 THR A 132  ASP A 135 -1  N  ALA A 134   O  THR A 126           
SSBOND   1 CYS A  121    CYS A  151                          1555   1555  2.01  
LINK         C   PHE A   1                 N   THR A   2     1555   1555  1.40  
LINK         OG  SER A  63                 C1  NAG B   1     1555   1555  1.40  
LINK         O3  NAG B   1                 C1  GLA B   2     1555   1555  1.40  
LINK         NE2 HIS A  54                PT    PT A 200     1555   1555  3.38  
LINK         NE2 HIS A  54                PT    PT A 200     4566   1555  3.38  
LINK        PT    PT A 200                 O   HOH A 333     1555   1555  1.65  
LINK        PT    PT A 200                 O   HOH A 333     1555   4566  1.65  
LINK        PT    PT A 200                 O   HOH A 348     1555   1555  1.63  
LINK        PT    PT A 200                 O   HOH A 348     1555   4566  1.63  
CRYST1  127.580  121.080   26.860  90.00  90.00  90.00 C 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007838  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.037230        0.00000                         
ATOM      1  N   PHE A   1      61.140 -19.698  -3.349  1.00 30.05           N  
ATOM      2  CA  PHE A   1      61.356 -18.393  -3.935  1.00 34.00           C  
ATOM      3  C   PHE A   1      60.239 -17.249  -3.830  1.00 32.91           C  
ATOM      4  O   PHE A   1      59.569 -16.977  -4.824  1.00 25.46           O  
ATOM      5  CB  PHE A   1      61.777 -18.828  -5.333  1.00 38.69           C  
ATOM      6  CG  PHE A   1      63.251 -19.272  -5.562  1.00 47.89           C  
ATOM      7  CD1 PHE A   1      64.229 -18.331  -5.992  1.00 51.41           C  
ATOM      8  CD2 PHE A   1      63.650 -20.625  -5.541  1.00 52.67           C  
ATOM      9  CE1 PHE A   1      65.533 -18.742  -6.402  1.00 54.51           C  
ATOM     10  CE2 PHE A   1      64.954 -21.013  -5.955  1.00 50.29           C  
ATOM     11  CZ  PHE A   1      65.904 -20.092  -6.393  1.00 50.11           C  
ATOM     12  N   THR A   2      60.137 -16.518  -2.645  1.00 38.44           N  
ATOM     13  CA  THR A   2      59.163 -15.498  -2.068  1.00 40.35           C  
ATOM     14  C   THR A   2      58.808 -14.014  -2.377  1.00 39.33           C  
ATOM     15  O   THR A   2      59.050 -13.040  -1.638  1.00 39.29           O  
ATOM     16  CB  THR A   2      59.286 -15.336  -0.485  1.00 41.48           C  
ATOM     17  OG1 THR A   2      60.692 -15.197  -0.142  1.00 37.72           O  
ATOM     18  CG2 THR A   2      58.374 -16.354   0.178  1.00 37.06           C  
ATOM     19  N   LEU A   3      58.022 -13.863  -3.414  1.00 38.99           N  
ATOM     20  CA  LEU A   3      57.442 -12.611  -3.767  1.00 35.17           C  
ATOM     21  C   LEU A   3      56.308 -12.410  -2.773  1.00 35.96           C  
ATOM     22  O   LEU A   3      56.251 -11.386  -2.113  1.00 38.75           O  
ATOM     23  CB  LEU A   3      57.011 -12.794  -5.180  1.00 33.43           C  
ATOM     24  CG  LEU A   3      56.914 -11.588  -6.031  1.00 39.79           C  
ATOM     25  CD1 LEU A   3      58.180 -10.728  -5.936  1.00 37.18           C  
ATOM     26  CD2 LEU A   3      56.576 -12.109  -7.428  1.00 44.02           C  
ATOM     27  N   ILE A   4      55.476 -13.410  -2.513  1.00 34.25           N  
ATOM     28  CA  ILE A   4      54.293 -13.250  -1.681  1.00 35.64           C  
ATOM     29  C   ILE A   4      54.426 -12.516  -0.365  1.00 36.85           C  
ATOM     30  O   ILE A   4      53.673 -11.612  -0.045  1.00 38.89           O  
ATOM     31  CB  ILE A   4      53.658 -14.677  -1.436  1.00 36.25           C  
ATOM     32  CG1 ILE A   4      52.255 -14.471  -0.829  1.00 38.33           C  
ATOM     33  CG2 ILE A   4      54.491 -15.578  -0.505  1.00 37.05           C  
ATOM     34  CD1 ILE A   4      51.185 -14.065  -1.862  1.00 32.51           C  
ATOM     35  N   GLU A   5      55.441 -12.874   0.385  1.00 39.81           N  
ATOM     36  CA  GLU A   5      55.663 -12.349   1.719  1.00 41.63           C  
ATOM     37  C   GLU A   5      56.004 -10.846   1.608  1.00 38.80           C  
ATOM     38  O   GLU A   5      55.504  -9.999   2.363  1.00 37.25           O  
ATOM     39  CB  GLU A   5      56.810 -13.143   2.290  1.00 47.45           C  
ATOM     40  CG  GLU A   5      56.943 -13.231   3.783  1.00 56.30           C  
ATOM     41  CD  GLU A   5      56.095 -14.372   4.317  1.00 64.22           C  
ATOM     42  OE1 GLU A   5      56.649 -15.477   4.369  1.00 65.31           O  
ATOM     43  OE2 GLU A   5      54.918 -14.163   4.663  1.00 65.48           O  
ATOM     44  N   LEU A   6      56.842 -10.529   0.602  1.00 33.67           N  
ATOM     45  CA  LEU A   6      57.244  -9.181   0.354  1.00 30.89           C  
ATOM     46  C   LEU A   6      55.953  -8.519  -0.064  1.00 31.94           C  
ATOM     47  O   LEU A   6      55.578  -7.537   0.571  1.00 36.33           O  
ATOM     48  CB  LEU A   6      58.253  -9.114  -0.756  1.00 28.53           C  
ATOM     49  CG  LEU A   6      58.825  -7.745  -1.115  1.00 27.87           C  
ATOM     50  CD1 LEU A   6      59.579  -7.110   0.058  1.00 24.44           C  
ATOM     51  CD2 LEU A   6      59.710  -7.951  -2.319  1.00 26.41           C  
ATOM     52  N   MET A   7      55.151  -9.065  -0.980  1.00 32.86           N  
ATOM     53  CA  MET A   7      53.915  -8.433  -1.413  1.00 29.22           C  
ATOM     54  C   MET A   7      52.939  -8.188  -0.313  1.00 26.98           C  
ATOM     55  O   MET A   7      52.100  -7.309  -0.436  1.00 30.94           O  
ATOM     56  CB  MET A   7      53.249  -9.268  -2.448  1.00 30.79           C  
ATOM     57  CG  MET A   7      54.021  -9.194  -3.754  1.00 34.56           C  
ATOM     58  SD  MET A   7      53.243 -10.327  -4.912  1.00 41.80           S  
ATOM     59  CE  MET A   7      51.630  -9.607  -4.857  1.00 30.39           C  
ATOM     60  N   ILE A   8      53.058  -8.899   0.785  1.00 26.82           N  
ATOM     61  CA  ILE A   8      52.225  -8.680   1.934  1.00 30.17           C  
ATOM     62  C   ILE A   8      52.751  -7.537   2.782  1.00 32.95           C  
ATOM     63  O   ILE A   8      51.997  -6.734   3.344  1.00 33.49           O  
ATOM     64  CB  ILE A   8      52.201 -10.011   2.632  1.00 33.18           C  
ATOM     65  CG1 ILE A   8      51.189 -10.841   1.838  1.00 38.28           C  
ATOM     66  CG2 ILE A   8      51.867  -9.913   4.118  1.00 33.65           C  
ATOM     67  CD1 ILE A   8      51.368 -12.365   1.939  1.00 39.34           C  
ATOM     68  N   VAL A   9      54.054  -7.409   2.915  1.00 32.04           N  
ATOM     69  CA  VAL A   9      54.586  -6.306   3.685  1.00 35.26           C  
ATOM     70  C   VAL A   9      54.356  -4.993   2.933  1.00 35.50           C  
ATOM     71  O   VAL A   9      53.974  -3.986   3.543  1.00 40.51           O  
ATOM     72  CB  VAL A   9      56.076  -6.646   3.953  1.00 37.34           C  
ATOM     73  CG1 VAL A   9      56.931  -5.439   4.372  1.00 33.17           C  
ATOM     74  CG2 VAL A   9      56.034  -7.759   5.036  1.00 38.32           C  
ATOM     75  N   ILE A  10      54.516  -4.981   1.609  1.00 29.30           N  
ATOM     76  CA  ILE A  10      54.292  -3.790   0.819  1.00 28.91           C  
ATOM     77  C   ILE A  10      52.841  -3.424   0.972  1.00 34.30           C  
ATOM     78  O   ILE A  10      52.534  -2.263   1.217  1.00 39.07           O  
ATOM     79  CB  ILE A  10      54.568  -4.019  -0.667  1.00 29.57           C  
ATOM     80  CG1 ILE A  10      56.018  -4.343  -0.824  1.00 31.06           C  
ATOM     81  CG2 ILE A  10      54.225  -2.826  -1.506  1.00 26.71           C  
ATOM     82  CD1 ILE A  10      56.998  -3.523   0.027  1.00 37.04           C  
ATOM     83  N   ALA A  11      51.963  -4.425   0.882  1.00 35.45           N  
ATOM     84  CA  ALA A  11      50.527  -4.222   0.966  1.00 29.49           C  
ATOM     85  C   ALA A  11      50.175  -3.628   2.321  1.00 29.33           C  
ATOM     86  O   ALA A  11      49.513  -2.582   2.347  1.00 34.08           O  
ATOM     87  CB  ALA A  11      49.820  -5.553   0.776  1.00 27.12           C  
ATOM     88  N   ILE A  12      50.672  -4.146   3.448  1.00 27.60           N  
ATOM     89  CA  ILE A  12      50.253  -3.566   4.696  1.00 31.21           C  
ATOM     90  C   ILE A  12      50.911  -2.187   4.900  1.00 31.93           C  
ATOM     91  O   ILE A  12      50.270  -1.254   5.384  1.00 33.36           O  
ATOM     92  CB  ILE A  12      50.555  -4.532   5.923  1.00 34.07           C  
ATOM     93  CG1 ILE A  12      52.012  -4.631   6.253  1.00 42.83           C  
ATOM     94  CG2 ILE A  12      50.166  -5.967   5.600  1.00 36.23           C  
ATOM     95  CD1 ILE A  12      52.088  -4.568   7.802  1.00 47.01           C  
ATOM     96  N   VAL A  13      52.151  -1.919   4.517  1.00 32.33           N  
ATOM     97  CA  VAL A  13      52.706  -0.590   4.739  1.00 30.62           C  
ATOM     98  C   VAL A  13      51.997   0.390   3.811  1.00 29.73           C  
ATOM     99  O   VAL A  13      51.584   1.429   4.303  1.00 32.25           O  
ATOM    100  CB  VAL A  13      54.228  -0.730   4.528  1.00 28.85           C  
ATOM    101  CG1 VAL A  13      54.970   0.524   4.242  1.00 27.15           C  
ATOM    102  CG2 VAL A  13      54.749  -1.191   5.872  1.00 25.87           C  
ATOM    103  N   GLY A  14      51.742   0.104   2.544  1.00 28.35           N  
ATOM    104  CA  GLY A  14      51.009   0.978   1.651  1.00 32.22           C  
ATOM    105  C   GLY A  14      49.549   1.274   2.069  1.00 37.04           C  
ATOM    106  O   GLY A  14      49.068   2.380   1.774  1.00 37.69           O  
ATOM    107  N   ILE A  15      48.730   0.411   2.709  1.00 37.80           N  
ATOM    108  CA  ILE A  15      47.394   0.875   3.097  1.00 38.76           C  
ATOM    109  C   ILE A  15      47.500   1.769   4.338  1.00 36.87           C  
ATOM    110  O   ILE A  15      46.802   2.781   4.434  1.00 36.29           O  
ATOM    111  CB  ILE A  15      46.416  -0.285   3.399  1.00 41.65           C  
ATOM    112  CG1 ILE A  15      46.999  -1.198   4.452  1.00 45.25           C  
ATOM    113  CG2 ILE A  15      46.103  -1.032   2.102  1.00 40.69           C  
ATOM    114  CD1 ILE A  15      45.951  -1.914   5.341  1.00 52.28           C  
ATOM    115  N   LEU A  16      48.402   1.452   5.274  1.00 33.97           N  
ATOM    116  CA  LEU A  16      48.709   2.270   6.440  1.00 35.49           C  
ATOM    117  C   LEU A  16      49.064   3.702   5.994  1.00 37.01           C  
ATOM    118  O   LEU A  16      48.556   4.675   6.537  1.00 35.95           O  
ATOM    119  CB  LEU A  16      49.900   1.662   7.194  1.00 34.15           C  
ATOM    120  CG  LEU A  16      49.761   0.867   8.459  1.00 34.73           C  
ATOM    121  CD1 LEU A  16      48.675  -0.170   8.337  1.00 36.45           C  
ATOM    122  CD2 LEU A  16      51.110   0.232   8.743  1.00 34.44           C  
ATOM    123  N   ALA A  17      49.938   3.875   5.000  1.00 37.56           N  
ATOM    124  CA  ALA A  17      50.290   5.173   4.453  1.00 37.08           C  
ATOM    125  C   ALA A  17      49.067   5.843   3.848  1.00 36.30           C  
ATOM    126  O   ALA A  17      48.884   7.024   4.140  1.00 35.32           O  
ATOM    127  CB  ALA A  17      51.335   5.065   3.341  1.00 35.21           C  
ATOM    128  N   ALA A  18      48.209   5.151   3.083  1.00 34.29           N  
ATOM    129  CA  ALA A  18      47.017   5.777   2.525  1.00 36.34           C  
ATOM    130  C   ALA A  18      46.114   6.214   3.654  1.00 38.42           C  
ATOM    131  O   ALA A  18      45.535   7.292   3.582  1.00 42.12           O  
ATOM    132  CB  ALA A  18      46.187   4.849   1.662  1.00 34.91           C  
ATOM    133  N   VAL A  19      46.039   5.452   4.732  1.00 40.19           N  
ATOM    134  CA  VAL A  19      45.279   5.825   5.914  1.00 39.73           C  
ATOM    135  C   VAL A  19      45.875   7.067   6.605  1.00 36.59           C  
ATOM    136  O   VAL A  19      45.160   8.015   6.943  1.00 39.02           O  
ATOM    137  CB  VAL A  19      45.239   4.480   6.750  1.00 40.75           C  
ATOM    138  CG1 VAL A  19      45.440   4.534   8.283  1.00 39.93           C  
ATOM    139  CG2 VAL A  19      43.847   3.971   6.399  1.00 40.77           C  
ATOM    140  N   ALA A  20      47.192   7.130   6.756  1.00 31.60           N  
ATOM    141  CA  ALA A  20      47.870   8.243   7.365  1.00 29.85           C  
ATOM    142  C   ALA A  20      47.778   9.527   6.556  1.00 29.52           C  
ATOM    143  O   ALA A  20      47.483  10.601   7.085  1.00 27.40           O  
ATOM    144  CB  ALA A  20      49.312   7.886   7.528  1.00 31.20           C  
ATOM    145  N   LEU A  21      48.017   9.379   5.266  1.00 30.02           N  
ATOM    146  CA  LEU A  21      48.074  10.444   4.298  1.00 33.00           C  
ATOM    147  C   LEU A  21      47.033  11.543   4.516  1.00 37.53           C  
ATOM    148  O   LEU A  21      47.479  12.674   4.734  1.00 38.39           O  
ATOM    149  CB  LEU A  21      47.947   9.821   2.907  1.00 32.87           C  
ATOM    150  CG  LEU A  21      48.214  10.633   1.669  1.00 32.15           C  
ATOM    151  CD1 LEU A  21      49.683  10.919   1.582  1.00 30.82           C  
ATOM    152  CD2 LEU A  21      47.764   9.877   0.441  1.00 31.83           C  
ATOM    153  N   PRO A  22      45.701  11.413   4.558  1.00 41.58           N  
ATOM    154  CA  PRO A  22      44.816  12.497   4.998  1.00 43.13           C  
ATOM    155  C   PRO A  22      45.199  13.230   6.286  1.00 42.57           C  
ATOM    156  O   PRO A  22      45.233  14.456   6.305  1.00 45.94           O  
ATOM    157  CB  PRO A  22      43.433  11.825   5.066  1.00 42.26           C  
ATOM    158  CG  PRO A  22      43.690  10.331   4.979  1.00 42.00           C  
ATOM    159  CD  PRO A  22      44.905  10.281   4.078  1.00 42.17           C  
ATOM    160  N   ALA A  23      45.581  12.545   7.347  1.00 40.86           N  
ATOM    161  CA  ALA A  23      45.877  13.181   8.599  1.00 36.53           C  
ATOM    162  C   ALA A  23      47.060  14.096   8.449  1.00 35.42           C  
ATOM    163  O   ALA A  23      46.985  15.253   8.852  1.00 37.29           O  
ATOM    164  CB  ALA A  23      46.189  12.134   9.628  1.00 39.85           C  
ATOM    165  N   TYR A  24      48.123  13.616   7.812  1.00 34.00           N  
ATOM    166  CA  TYR A  24      49.323  14.413   7.620  1.00 33.20           C  
ATOM    167  C   TYR A  24      49.007  15.493   6.611  1.00 31.70           C  
ATOM    168  O   TYR A  24      49.490  16.589   6.834  1.00 30.56           O  
ATOM    169  CB  TYR A  24      50.481  13.507   7.158  1.00 32.87           C  
ATOM    170  CG  TYR A  24      51.805  14.153   6.746  1.00 30.65           C  
ATOM    171  CD1 TYR A  24      52.779  14.508   7.677  1.00 31.48           C  
ATOM    172  CD2 TYR A  24      52.049  14.346   5.386  1.00 31.13           C  
ATOM    173  CE1 TYR A  24      53.992  15.049   7.226  1.00 33.94           C  
ATOM    174  CE2 TYR A  24      53.246  14.874   4.934  1.00 28.67           C  
ATOM    175  CZ  TYR A  24      54.202  15.221   5.854  1.00 33.63           C  
ATOM    176  OH  TYR A  24      55.389  15.721   5.359  1.00 40.63           O  
ATOM    177  N   GLN A  25      48.176  15.278   5.587  1.00 32.80           N  
ATOM    178  CA  GLN A  25      47.670  16.320   4.672  1.00 33.10           C  
ATOM    179  C   GLN A  25      47.038  17.465   5.457  1.00 31.92           C  
ATOM    180  O   GLN A  25      47.200  18.640   5.107  1.00 30.71           O  
ATOM    181  CB  GLN A  25      46.570  15.806   3.742  1.00 35.96           C  
ATOM    182  CG  GLN A  25      46.628  16.370   2.343  1.00 46.76           C  
ATOM    183  CD  GLN A  25      47.935  15.969   1.638  1.00 52.65           C  
ATOM    184  OE1 GLN A  25      49.016  16.527   1.867  1.00 54.56           O  
ATOM    185  NE2 GLN A  25      47.923  15.003   0.726  1.00 56.30           N  
ATOM    186  N   ASP A  26      46.275  17.155   6.507  1.00 30.09           N  
ATOM    187  CA  ASP A  26      45.656  18.158   7.329  1.00 25.18           C  
ATOM    188  C   ASP A  26      46.585  18.650   8.376  1.00 25.24           C  
ATOM    189  O   ASP A  26      46.332  19.719   8.930  1.00 31.85           O  
ATOM    190  CB  ASP A  26      44.443  17.680   8.069  1.00 23.35           C  
ATOM    191  CG  ASP A  26      43.245  17.422   7.177  1.00 22.63           C  
ATOM    192  OD1 ASP A  26      43.158  17.935   6.070  1.00 23.94           O  
ATOM    193  OD2 ASP A  26      42.372  16.677   7.597  1.00 28.03           O  
ATOM    194  N   TYR A  27      47.657  17.978   8.680  1.00 23.17           N  
ATOM    195  CA  TYR A  27      48.537  18.473   9.692  1.00 22.73           C  
ATOM    196  C   TYR A  27      49.300  19.636   9.109  1.00 24.58           C  
ATOM    197  O   TYR A  27      49.396  20.722   9.682  1.00 26.72           O  
ATOM    198  CB  TYR A  27      49.453  17.395  10.048  1.00 25.46           C  
ATOM    199  CG  TYR A  27      50.329  17.799  11.185  1.00 35.51           C  
ATOM    200  CD1 TYR A  27      49.738  17.835  12.453  1.00 41.03           C  
ATOM    201  CD2 TYR A  27      51.681  18.124  10.971  1.00 37.38           C  
ATOM    202  CE1 TYR A  27      50.516  18.202  13.547  1.00 47.28           C  
ATOM    203  CE2 TYR A  27      52.460  18.495  12.070  1.00 47.08           C  
ATOM    204  CZ  TYR A  27      51.869  18.529  13.353  1.00 49.49           C  
ATOM    205  OH  TYR A  27      52.607  18.883  14.476  1.00 54.71           O  
ATOM    206  N   THR A  28      49.858  19.383   7.939  1.00 29.13           N  
ATOM    207  CA  THR A  28      50.703  20.333   7.247  1.00 31.05           C  
ATOM    208  C   THR A  28      49.956  21.633   7.020  1.00 30.05           C  
ATOM    209  O   THR A  28      50.460  22.685   7.393  1.00 34.11           O  
ATOM    210  CB  THR A  28      51.188  19.773   5.868  1.00 30.95           C  
ATOM    211  OG1 THR A  28      50.033  19.420   5.099  1.00 37.94           O  
ATOM    212  CG2 THR A  28      52.145  18.634   6.050  1.00 26.85           C  
ATOM    213  N   ALA A  29      48.771  21.550   6.435  1.00 26.91           N  
ATOM    214  CA  ALA A  29      47.935  22.694   6.206  1.00 28.44           C  
ATOM    215  C   ALA A  29      47.709  23.532   7.455  1.00 31.00           C  
ATOM    216  O   ALA A  29      47.633  24.749   7.351  1.00 33.50           O  
ATOM    217  CB  ALA A  29      46.589  22.247   5.680  1.00 24.58           C  
ATOM    218  N   ARG A  30      47.595  22.943   8.644  1.00 34.12           N  
ATOM    219  CA  ARG A  30      47.440  23.701   9.863  1.00 32.88           C  
ATOM    220  C   ARG A  30      48.770  24.336  10.153  1.00 35.02           C  
ATOM    221  O   ARG A  30      48.766  25.516  10.503  1.00 41.45           O  
ATOM    222  CB  ARG A  30      47.073  22.835  11.014  1.00 37.01           C  
ATOM    223  CG  ARG A  30      45.571  22.592  11.054  1.00 49.70           C  
ATOM    224  CD  ARG A  30      45.176  21.880  12.347  1.00 60.23           C  
ATOM    225  NE  ARG A  30      45.707  22.579  13.510  1.00 69.86           N  
ATOM    226  CZ  ARG A  30      44.981  22.852  14.598  1.00 73.00           C  
ATOM    227  NH1 ARG A  30      43.690  22.479  14.711  1.00 74.92           N  
ATOM    228  NH2 ARG A  30      45.599  23.504  15.593  1.00 73.29           N  
ATOM    229  N   ALA A  31      49.919  23.669   9.980  1.00 32.70           N  
ATOM    230  CA  ALA A  31      51.215  24.304  10.183  1.00 23.73           C  
ATOM    231  C   ALA A  31      51.398  25.407   9.148  1.00 20.84           C  
ATOM    232  O   ALA A  31      51.865  26.471   9.507  1.00 25.82           O  
ATOM    233  CB  ALA A  31      52.306  23.280  10.028  1.00 26.27           C  
ATOM    234  N   GLN A  32      51.032  25.314   7.883  1.00 18.70           N  
ATOM    235  CA  GLN A  32      51.074  26.427   6.925  1.00 23.50           C  
ATOM    236  C   GLN A  32      50.111  27.594   7.258  1.00 25.07           C  
ATOM    237  O   GLN A  32      50.517  28.723   7.084  1.00 24.79           O  
ATOM    238  CB  GLN A  32      50.748  25.922   5.525  1.00 24.94           C  
ATOM    239  CG  GLN A  32      51.614  24.723   5.099  1.00 31.57           C  
ATOM    240  CD  GLN A  32      51.181  24.022   3.803  1.00 36.34           C  
ATOM    241  OE1 GLN A  32      50.009  23.806   3.499  1.00 37.60           O  
ATOM    242  NE2 GLN A  32      52.074  23.646   2.902  1.00 42.45           N  
ATOM    243  N   VAL A  33      48.865  27.549   7.734  1.00 23.41           N  
ATOM    244  CA  VAL A  33      48.160  28.765   8.068  1.00 23.42           C  
ATOM    245  C   VAL A  33      48.670  29.203   9.439  1.00 25.45           C  
ATOM    246  O   VAL A  33      48.453  30.345   9.836  1.00 29.31           O  
ATOM    247  CB  VAL A  33      46.584  28.599   8.088  1.00 21.36           C  
ATOM    248  CG1 VAL A  33      46.172  27.582   7.033  1.00 16.83           C  
ATOM    249  CG2 VAL A  33      46.060  28.182   9.434  1.00 26.44           C  
ATOM    250  N   SER A  34      49.369  28.401  10.226  1.00 27.01           N  
ATOM    251  CA  SER A  34      50.003  28.881  11.457  1.00 31.77           C  
ATOM    252  C   SER A  34      50.954  30.068  11.211  1.00 30.08           C  
ATOM    253  O   SER A  34      51.070  31.010  12.007  1.00 27.58           O  
ATOM    254  CB  SER A  34      50.870  27.813  12.117  1.00 38.46           C  
ATOM    255  OG  SER A  34      50.221  26.597  12.483  1.00 55.68           O  
ATOM    256  N   GLU A  35      51.707  30.015  10.116  1.00 27.43           N  
ATOM    257  CA  GLU A  35      52.598  31.098   9.755  1.00 27.19           C  
ATOM    258  C   GLU A  35      51.773  32.329   9.356  1.00 24.47           C  
ATOM    259  O   GLU A  35      52.062  33.410   9.847  1.00 23.99           O  
ATOM    260  CB  GLU A  35      53.463  30.634   8.608  1.00 28.22           C  
ATOM    261  CG  GLU A  35      54.553  31.573   8.156  1.00 29.07           C  
ATOM    262  CD  GLU A  35      54.967  31.281   6.712  1.00 34.77           C  
ATOM    263  OE1 GLU A  35      54.118  31.313   5.818  1.00 36.59           O  
ATOM    264  OE2 GLU A  35      56.147  31.027   6.471  1.00 38.47           O  
ATOM    265  N   ALA A  36      50.710  32.206   8.574  1.00 19.44           N  
ATOM    266  CA  ALA A  36      49.895  33.311   8.161  1.00 22.10           C  
ATOM    267  C   ALA A  36      49.424  34.016   9.412  1.00 25.49           C  
ATOM    268  O   ALA A  36      49.580  35.232   9.537  1.00 26.74           O  
ATOM    269  CB  ALA A  36      48.679  32.827   7.370  1.00 21.19           C  
ATOM    270  N   ILE A  37      48.944  33.252  10.388  1.00 23.58           N  
ATOM    271  CA  ILE A  37      48.490  33.829  11.634  1.00 20.82           C  
ATOM    272  C   ILE A  37      49.667  34.528  12.272  1.00 26.83           C  
ATOM    273  O   ILE A  37      49.426  35.586  12.859  1.00 33.92           O  
ATOM    274  CB  ILE A  37      47.949  32.745  12.575  1.00 13.13           C  
ATOM    275  CG1 ILE A  37      46.710  32.176  11.941  1.00  8.61           C  
ATOM    276  CG2 ILE A  37      47.642  33.290  13.969  1.00 13.11           C  
ATOM    277  CD1 ILE A  37      46.167  30.980  12.748  1.00  8.73           C  
ATOM    278  N   LEU A  38      50.921  34.088  12.139  1.00 27.80           N  
ATOM    279  CA  LEU A  38      51.998  34.760  12.840  1.00 29.68           C  
ATOM    280  C   LEU A  38      52.513  36.032  12.171  1.00 28.02           C  
ATOM    281  O   LEU A  38      52.900  37.037  12.781  1.00 28.13           O  
ATOM    282  CB  LEU A  38      53.141  33.774  13.052  1.00 31.11           C  
ATOM    283  CG  LEU A  38      53.739  33.906  14.474  1.00 34.29           C  
ATOM    284  CD1 LEU A  38      52.727  33.447  15.567  1.00 33.66           C  
ATOM    285  CD2 LEU A  38      55.015  33.096  14.519  1.00 37.21           C  
ATOM    286  N   LEU A  39      52.489  35.989  10.863  1.00 26.98           N  
ATOM    287  CA  LEU A  39      52.762  37.139  10.065  1.00 26.55           C  
ATOM    288  C   LEU A  39      51.737  38.255  10.315  1.00 28.39           C  
ATOM    289  O   LEU A  39      52.061  39.439  10.250  1.00 29.95           O  
ATOM    290  CB  LEU A  39      52.744  36.667   8.642  1.00 25.30           C  
ATOM    291  CG  LEU A  39      54.042  36.128   8.189  1.00 23.92           C  
ATOM    292  CD1 LEU A  39      54.038  35.716   6.749  1.00 24.21           C  
ATOM    293  CD2 LEU A  39      55.016  37.251   8.309  1.00 31.35           C  
ATOM    294  N   ALA A  40      50.482  37.927  10.580  1.00 23.20           N  
ATOM    295  CA  ALA A  40      49.479  38.913  10.829  1.00 20.54           C  
ATOM    296  C   ALA A  40      49.526  39.455  12.253  1.00 25.40           C  
ATOM    297  O   ALA A  40      49.245  40.629  12.504  1.00 25.07           O  
ATOM    298  CB  ALA A  40      48.145  38.298  10.569  1.00 19.60           C  
ATOM    299  N   GLU A  41      49.874  38.636  13.235  1.00 30.56           N  
ATOM    300  CA  GLU A  41      49.979  39.081  14.615  1.00 32.90           C  
ATOM    301  C   GLU A  41      51.169  39.990  14.823  1.00 36.58           C  
ATOM    302  O   GLU A  41      51.167  40.832  15.731  1.00 40.46           O  
ATOM    303  CB  GLU A  41      50.101  37.898  15.539  1.00 37.94           C  
ATOM    304  CG  GLU A  41      48.823  37.028  15.638  1.00 50.64           C  
ATOM    305  CD  GLU A  41      48.973  35.804  16.542  1.00 56.76           C  
ATOM    306  OE1 GLU A  41      49.608  34.836  16.106  1.00 61.70           O  
ATOM    307  OE2 GLU A  41      48.471  35.821  17.673  1.00 61.68           O  
ATOM    308  N   GLY A  42      52.199  39.877  13.973  1.00 38.71           N  
ATOM    309  CA  GLY A  42      53.367  40.776  13.975  1.00 39.32           C  
ATOM    310  C   GLY A  42      52.975  42.260  13.827  1.00 39.98           C  
ATOM    311  O   GLY A  42      53.439  43.084  14.618  1.00 43.49           O  
ATOM    312  N   GLN A  43      52.101  42.551  12.839  1.00 36.98           N  
ATOM    313  CA  GLN A  43      51.413  43.804  12.541  1.00 32.29           C  
ATOM    314  C   GLN A  43      50.465  44.360  13.612  1.00 32.14           C  
ATOM    315  O   GLN A  43      50.020  45.493  13.450  1.00 35.79           O  
ATOM    316  CB  GLN A  43      50.575  43.651  11.288  1.00 33.68           C  
ATOM    317  CG  GLN A  43      51.197  43.898   9.946  1.00 34.12           C  
ATOM    318  CD  GLN A  43      52.533  43.245   9.791  1.00 30.96           C  
ATOM    319  OE1 GLN A  43      53.564  43.844  10.024  1.00 37.23           O  
ATOM    320  NE2 GLN A  43      52.611  41.997   9.434  1.00 33.18           N  
ATOM    321  N   LYS A  44      50.080  43.720  14.720  1.00 28.85           N  
ATOM    322  CA  LYS A  44      49.125  44.305  15.647  1.00 25.19           C  
ATOM    323  C   LYS A  44      49.679  45.425  16.502  1.00 26.57           C  
ATOM    324  O   LYS A  44      48.924  46.294  16.921  1.00 31.43           O  
ATOM    325  CB  LYS A  44      48.600  43.313  16.607  1.00 24.68           C  
ATOM    326  CG  LYS A  44      48.002  42.141  15.898  1.00 32.73           C  
ATOM    327  CD  LYS A  44      47.270  41.258  16.878  1.00 33.82           C  
ATOM    328  CE  LYS A  44      48.106  40.630  17.958  1.00 36.97           C  
ATOM    329  NZ  LYS A  44      47.183  40.041  18.903  1.00 36.80           N  
ATOM    330  N   SER A  45      50.969  45.501  16.811  1.00 26.63           N  
ATOM    331  CA  SER A  45      51.561  46.532  17.655  1.00 19.84           C  
ATOM    332  C   SER A  45      51.394  47.866  16.978  1.00 19.72           C  
ATOM    333  O   SER A  45      50.848  48.805  17.563  1.00 20.35           O  
ATOM    334  CB  SER A  45      53.023  46.243  17.842  1.00 21.15           C  
ATOM    335  OG  SER A  45      53.576  47.101  18.836  1.00 36.04           O  
ATOM    336  N   ALA A  46      51.837  47.908  15.728  1.00 13.73           N  
ATOM    337  CA  ALA A  46      51.690  49.057  14.908  1.00 14.45           C  
ATOM    338  C   ALA A  46      50.241  49.541  14.821  1.00 19.36           C  
ATOM    339  O   ALA A  46      50.005  50.736  15.077  1.00 23.89           O  
ATOM    340  CB  ALA A  46      52.235  48.725  13.517  1.00  9.80           C  
ATOM    341  N   VAL A  47      49.247  48.664  14.558  1.00 17.02           N  
ATOM    342  CA  VAL A  47      47.847  49.040  14.410  1.00 13.59           C  
ATOM    343  C   VAL A  47      47.272  49.563  15.716  1.00 17.21           C  
ATOM    344  O   VAL A  47      46.540  50.553  15.721  1.00 20.22           O  
ATOM    345  CB  VAL A  47      47.027  47.804  13.913  1.00 10.86           C  
ATOM    346  CG1 VAL A  47      45.530  48.014  13.987  1.00 10.01           C  
ATOM    347  CG2 VAL A  47      47.337  47.569  12.455  1.00  6.52           C  
ATOM    348  N   THR A  48      47.622  48.902  16.818  1.00 19.76           N  
ATOM    349  CA  THR A  48      47.153  49.227  18.157  1.00 20.71           C  
ATOM    350  C   THR A  48      47.678  50.599  18.530  1.00 22.70           C  
ATOM    351  O   THR A  48      46.941  51.441  19.047  1.00 23.93           O  
ATOM    352  CB  THR A  48      47.667  48.172  19.158  1.00 21.42           C  
ATOM    353  OG1 THR A  48      47.086  46.913  18.810  1.00 22.30           O  
ATOM    354  CG2 THR A  48      47.310  48.507  20.580  1.00 18.14           C  
ATOM    355  N   GLU A  49      48.959  50.821  18.223  1.00 25.14           N  
ATOM    356  CA  GLU A  49      49.647  52.079  18.476  1.00 28.20           C  
ATOM    357  C   GLU A  49      48.996  53.226  17.731  1.00 27.66           C  
ATOM    358  O   GLU A  49      48.571  54.225  18.339  1.00 29.82           O  
ATOM    359  CB  GLU A  49      51.088  51.967  18.042  1.00 32.34           C  
ATOM    360  CG  GLU A  49      52.014  52.384  19.175  1.00 46.94           C  
ATOM    361  CD  GLU A  49      51.817  51.660  20.510  1.00 52.80           C  
ATOM    362  OE1 GLU A  49      52.225  50.500  20.621  1.00 59.52           O  
ATOM    363  OE2 GLU A  49      51.263  52.260  21.441  1.00 56.57           O  
ATOM    364  N   TYR A  50      48.844  52.991  16.413  1.00 24.64           N  
ATOM    365  CA  TYR A  50      48.256  53.940  15.523  1.00 18.99           C  
ATOM    366  C   TYR A  50      46.882  54.225  16.077  1.00 19.50           C  
ATOM    367  O   TYR A  50      46.622  55.401  16.327  1.00 23.63           O  
ATOM    368  CB  TYR A  50      48.123  53.404  14.079  1.00 19.32           C  
ATOM    369  CG  TYR A  50      47.674  54.513  13.095  1.00 21.64           C  
ATOM    370  CD1 TYR A  50      46.371  55.051  13.132  1.00 17.92           C  
ATOM    371  CD2 TYR A  50      48.618  55.084  12.231  1.00 18.00           C  
ATOM    372  CE1 TYR A  50      46.041  56.147  12.355  1.00 19.16           C  
ATOM    373  CE2 TYR A  50      48.277  56.183  11.450  1.00 16.81           C  
ATOM    374  CZ  TYR A  50      47.002  56.713  11.531  1.00 18.21           C  
ATOM    375  OH  TYR A  50      46.764  57.938  10.935  1.00 29.03           O  
ATOM    376  N   TYR A  51      46.004  53.303  16.347  1.00 13.47           N  
ATOM    377  CA  TYR A  51      44.717  53.714  16.817  1.00 12.61           C  
ATOM    378  C   TYR A  51      44.778  54.427  18.173  1.00 15.48           C  
ATOM    379  O   TYR A  51      43.998  55.350  18.468  1.00 18.08           O  
ATOM    380  CB  TYR A  51      43.857  52.483  16.890  1.00  9.92           C  
ATOM    381  CG  TYR A  51      42.442  52.760  17.309  1.00  5.11           C  
ATOM    382  CD1 TYR A  51      41.578  53.313  16.385  1.00 11.18           C  
ATOM    383  CD2 TYR A  51      42.029  52.464  18.595  1.00  7.45           C  
ATOM    384  CE1 TYR A  51      40.265  53.571  16.751  1.00  4.11           C  
ATOM    385  CE2 TYR A  51      40.727  52.719  18.978  1.00  7.59           C  
ATOM    386  CZ  TYR A  51      39.876  53.262  18.035  1.00 11.72           C  
ATOM    387  OH  TYR A  51      38.558  53.435  18.340  1.00 23.49           O  
ATOM    388  N   LEU A  52      45.737  54.107  19.018  1.00 17.16           N  
ATOM    389  CA  LEU A  52      45.725  54.684  20.349  1.00 18.39           C  
ATOM    390  C   LEU A  52      46.165  56.147  20.336  1.00 21.28           C  
ATOM    391  O   LEU A  52      45.592  57.050  20.932  1.00 21.94           O  
ATOM    392  CB  LEU A  52      46.589  53.734  21.202  1.00 16.11           C  
ATOM    393  CG  LEU A  52      45.829  52.928  22.321  1.00 18.63           C  
ATOM    394  CD1 LEU A  52      44.359  52.674  21.991  1.00  9.76           C  
ATOM    395  CD2 LEU A  52      46.537  51.611  22.527  1.00 13.55           C  
ATOM    396  N   ASN A  53      47.149  56.440  19.529  1.00 23.34           N  
ATOM    397  CA  ASN A  53      47.618  57.798  19.376  1.00 24.19           C  
ATOM    398  C   ASN A  53      46.664  58.728  18.636  1.00 24.09           C  
ATOM    399  O   ASN A  53      47.029  59.881  18.359  1.00 30.63           O  
ATOM    400  CB  ASN A  53      48.922  57.824  18.605  1.00 23.05           C  
ATOM    401  CG  ASN A  53      50.149  57.358  19.333  1.00 27.45           C  
ATOM    402  OD1 ASN A  53      51.142  57.013  18.687  1.00 35.04           O  
ATOM    403  ND2 ASN A  53      50.164  57.356  20.659  1.00 32.49           N  
ATOM    404  N   HIS A  54      45.544  58.249  18.103  1.00 21.51           N  
ATOM    405  CA  HIS A  54      44.822  59.151  17.251  1.00 18.59           C  
ATOM    406  C   HIS A  54      43.340  59.017  17.253  1.00 21.23           C  
ATOM    407  O   HIS A  54      42.707  60.028  16.990  1.00 23.07           O  
ATOM    408  CB  HIS A  54      45.119  59.043  15.801  1.00 21.11           C  
ATOM    409  CG  HIS A  54      46.461  58.541  15.378  1.00 24.02           C  
ATOM    410  ND1 HIS A  54      47.347  57.821  16.037  1.00 31.19           N  
ATOM    411  CD2 HIS A  54      46.966  58.727  14.133  1.00 26.22           C  
ATOM    412  CE1 HIS A  54      48.359  57.553  15.273  1.00 25.50           C  
ATOM    413  NE2 HIS A  54      48.128  58.088  14.092  1.00 19.80           N  
ATOM    414  N   GLY A  55      42.776  57.832  17.493  1.00 20.34           N  
ATOM    415  CA  GLY A  55      41.351  57.653  17.385  1.00 23.70           C  
ATOM    416  C   GLY A  55      40.952  57.137  16.007  1.00 24.89           C  
ATOM    417  O   GLY A  55      39.774  56.845  15.805  1.00 29.15           O  
ATOM    418  N   LYS A  56      41.870  56.889  15.067  1.00 23.61           N  
ATOM    419  CA  LYS A  56      41.532  56.449  13.723  1.00 22.77           C  
ATOM    420  C   LYS A  56      42.295  55.134  13.486  1.00 19.10           C  
ATOM    421  O   LYS A  56      43.394  54.959  14.033  1.00 17.52           O  
ATOM    422  CB  LYS A  56      41.953  57.597  12.733  1.00 23.30           C  
ATOM    423  CG  LYS A  56      40.881  58.304  11.859  1.00 27.24           C  
ATOM    424  CD  LYS A  56      40.633  57.561  10.511  1.00 38.83           C  
ATOM    425  CE  LYS A  56      39.711  58.181   9.409  1.00 42.70           C  
ATOM    426  NZ  LYS A  56      39.705  57.406   8.165  1.00 39.40           N  
ATOM    427  N   TRP A  57      41.735  54.188  12.726  1.00 14.63           N  
ATOM    428  CA  TRP A  57      42.468  52.995  12.324  1.00 12.42           C  
ATOM    429  C   TRP A  57      43.344  53.363  11.148  1.00 11.44           C  
ATOM    430  O   TRP A  57      42.943  54.162  10.293  1.00  9.68           O  
ATOM    431  CB  TRP A  57      41.527  51.870  11.901  1.00 10.40           C  
ATOM    432  CG  TRP A  57      40.671  51.325  13.050  1.00  7.85           C  
ATOM    433  CD1 TRP A  57      39.363  51.682  13.116  1.00  6.38           C  
ATOM    434  CD2 TRP A  57      41.062  50.529  14.118  1.00  6.38           C  
ATOM    435  NE1 TRP A  57      38.910  51.133  14.216  1.00 10.05           N  
ATOM    436  CE2 TRP A  57      39.881  50.449  14.844  1.00  8.63           C  
ATOM    437  CE3 TRP A  57      42.203  49.875  14.619  1.00 14.22           C  
ATOM    438  CZ2 TRP A  57      39.817  49.743  16.057  1.00 11.11           C  
ATOM    439  CZ3 TRP A  57      42.150  49.160  15.837  1.00 14.96           C  
ATOM    440  CH2 TRP A  57      40.959  49.104  16.552  1.00 12.14           C  
ATOM    441  N   PRO A  58      44.592  52.862  11.080  1.00 13.65           N  
ATOM    442  CA  PRO A  58      45.535  53.097   9.971  1.00 13.93           C  
ATOM    443  C   PRO A  58      44.940  52.663   8.646  1.00 18.99           C  
ATOM    444  O   PRO A  58      44.326  51.580   8.556  1.00 24.61           O  
ATOM    445  CB  PRO A  58      46.761  52.313  10.326  1.00 13.14           C  
ATOM    446  CG  PRO A  58      46.232  51.270  11.251  1.00 10.05           C  
ATOM    447  CD  PRO A  58      45.195  51.997  12.087  1.00 11.70           C  
ATOM    448  N   GLU A  59      45.092  53.445   7.598  1.00 17.03           N  
ATOM    449  CA  GLU A  59      44.379  53.052   6.419  1.00 19.47           C  
ATOM    450  C   GLU A  59      45.099  51.962   5.676  1.00 17.44           C  
ATOM    451  O   GLU A  59      44.472  51.093   5.073  1.00 17.94           O  
ATOM    452  CB  GLU A  59      44.189  54.247   5.529  1.00 27.00           C  
ATOM    453  CG  GLU A  59      43.299  53.948   4.319  1.00 35.18           C  
ATOM    454  CD  GLU A  59      43.420  54.945   3.168  1.00 40.68           C  
ATOM    455  OE1 GLU A  59      44.470  55.024   2.482  1.00 42.48           O  
ATOM    456  OE2 GLU A  59      42.405  55.624   2.979  1.00 42.27           O  
ATOM    457  N   ASN A  60      46.410  51.953   5.739  1.00 18.96           N  
ATOM    458  CA  ASN A  60      47.192  50.996   4.994  1.00 19.53           C  
ATOM    459  C   ASN A  60      48.487  50.628   5.681  1.00 20.43           C  
ATOM    460  O   ASN A  60      48.728  50.928   6.854  1.00 20.37           O  
ATOM    461  CB  ASN A  60      47.484  51.539   3.587  1.00 21.54           C  
ATOM    462  CG  ASN A  60      47.983  52.971   3.513  1.00 22.96           C  
ATOM    463  OD1 ASN A  60      48.959  53.300   4.210  1.00 20.97           O  
ATOM    464  ND2 ASN A  60      47.293  53.799   2.699  1.00 16.37           N  
ATOM    465  N   ASN A  61      49.336  49.892   4.972  1.00 23.48           N  
ATOM    466  CA  ASN A  61      50.578  49.441   5.511  1.00 21.67           C  
ATOM    467  C   ASN A  61      51.373  50.619   5.909  1.00 20.44           C  
ATOM    468  O   ASN A  61      51.788  50.658   7.052  1.00 18.43           O  
ATOM    469  CB  ASN A  61      51.331  48.660   4.487  1.00 25.87           C  
ATOM    470  CG  ASN A  61      50.934  47.189   4.503  1.00 27.92           C  
ATOM    471  OD1 ASN A  61      49.763  46.885   4.301  1.00 27.89           O  
ATOM    472  ND2 ASN A  61      51.791  46.204   4.710  1.00 23.99           N  
ATOM    473  N   THR A  62      51.448  51.593   4.987  1.00 25.12           N  
ATOM    474  CA  THR A  62      52.232  52.829   5.129  1.00 26.92           C  
ATOM    475  C   THR A  62      51.721  53.720   6.301  1.00 24.99           C  
ATOM    476  O   THR A  62      52.563  54.123   7.117  1.00 24.63           O  
ATOM    477  CB  THR A  62      52.210  53.553   3.741  1.00 29.00           C  
ATOM    478  OG1 THR A  62      52.764  52.685   2.741  1.00 28.51           O  
ATOM    479  CG2 THR A  62      53.059  54.799   3.739  1.00 30.86           C  
ATOM    480  N   SER A  63      50.427  54.039   6.492  1.00 17.44           N  
ATOM    481  CA  SER A  63      49.954  54.633   7.731  1.00 15.12           C  
ATOM    482  C   SER A  63      50.332  53.947   9.019  1.00 15.73           C  
ATOM    483  O   SER A  63      50.751  54.607   9.966  1.00 19.21           O  
ATOM    484  CB  SER A  63      48.442  54.727   7.721  1.00 16.57           C  
ATOM    485  OG  SER A  63      48.083  55.477   6.509  1.00 20.28           O  
ATOM    486  N   ALA A  64      50.108  52.639   9.150  1.00 20.69           N  
ATOM    487  CA  ALA A  64      50.460  51.896  10.352  1.00 20.92           C  
ATOM    488  C   ALA A  64      51.988  51.858  10.537  1.00 19.35           C  
ATOM    489  O   ALA A  64      52.499  51.679  11.637  1.00 24.28           O  
ATOM    490  CB  ALA A  64      49.895  50.466  10.243  1.00 22.25           C  
ATOM    491  N   GLY A  65      52.754  52.066   9.482  1.00 18.65           N  
ATOM    492  CA  GLY A  65      54.175  52.139   9.631  1.00 23.26           C  
ATOM    493  C   GLY A  65      54.842  50.803   9.551  1.00 28.49           C  
ATOM    494  O   GLY A  65      55.787  50.539  10.306  1.00 34.83           O  
ATOM    495  N   VAL A  66      54.338  49.954   8.639  1.00 28.08           N  
ATOM    496  CA  VAL A  66      54.938  48.650   8.350  1.00 25.92           C  
ATOM    497  C   VAL A  66      55.268  48.694   6.852  1.00 29.33           C  
ATOM    498  O   VAL A  66      54.912  49.681   6.196  1.00 29.53           O  
ATOM    499  CB  VAL A  66      53.960  47.471   8.681  1.00 22.03           C  
ATOM    500  CG1 VAL A  66      53.600  47.588  10.148  1.00 18.91           C  
ATOM    501  CG2 VAL A  66      52.702  47.476   7.827  1.00 21.43           C  
ATOM    502  N   ALA A  67      55.898  47.691   6.227  1.00 28.03           N  
ATOM    503  CA  ALA A  67      56.304  47.814   4.832  1.00 30.35           C  
ATOM    504  C   ALA A  67      55.152  48.161   3.937  1.00 32.33           C  
ATOM    505  O   ALA A  67      54.126  47.475   3.965  1.00 33.90           O  
ATOM    506  CB  ALA A  67      56.903  46.532   4.260  1.00 28.04           C  
ATOM    507  N   SER A  68      55.366  49.288   3.245  1.00 35.68           N  
ATOM    508  CA  SER A  68      54.390  49.836   2.341  1.00 37.26           C  
ATOM    509  C   SER A  68      53.740  48.791   1.412  1.00 40.31           C  
ATOM    510  O   SER A  68      52.501  48.840   1.397  1.00 41.28           O  
ATOM    511  CB  SER A  68      55.064  51.054   1.566  1.00 38.13           C  
ATOM    512  OG  SER A  68      56.336  51.080   0.874  1.00 35.74           O  
ATOM    513  N   PRO A  69      54.310  47.812   0.653  1.00 44.42           N  
ATOM    514  CA  PRO A  69      53.554  46.714   0.055  1.00 43.53           C  
ATOM    515  C   PRO A  69      53.546  45.492   0.959  1.00 42.75           C  
ATOM    516  O   PRO A  69      54.555  45.039   1.523  1.00 38.96           O  
ATOM    517  CB  PRO A  69      54.176  46.390  -1.314  1.00 43.51           C  
ATOM    518  CG  PRO A  69      55.444  47.205  -1.369  1.00 47.92           C  
ATOM    519  CD  PRO A  69      55.653  47.771   0.078  1.00 48.72           C  
ATOM    520  N   PRO A  70      52.335  44.937   1.075  1.00 43.10           N  
ATOM    521  CA  PRO A  70      52.065  43.650   1.689  1.00 40.47           C  
ATOM    522  C   PRO A  70      52.933  42.521   1.203  1.00 39.19           C  
ATOM    523  O   PRO A  70      53.287  41.685   2.010  1.00 37.61           O  
ATOM    524  CB  PRO A  70      50.617  43.447   1.408  1.00 44.54           C  
ATOM    525  CG  PRO A  70      50.241  44.425   0.307  1.00 44.70           C  
ATOM    526  CD  PRO A  70      51.078  45.600   0.725  1.00 42.39           C  
ATOM    527  N   SER A  71      53.294  42.461  -0.084  1.00 38.68           N  
ATOM    528  CA  SER A  71      54.171  41.444  -0.635  1.00 37.72           C  
ATOM    529  C   SER A  71      55.496  41.462   0.043  1.00 36.62           C  
ATOM    530  O   SER A  71      56.259  40.549  -0.165  1.00 39.54           O  
ATOM    531  CB  SER A  71      54.415  41.674  -2.083  1.00 38.82           C  
ATOM    532  OG  SER A  71      53.161  41.923  -2.697  1.00 51.10           O  
ATOM    533  N   ASP A  72      55.854  42.474   0.805  1.00 36.23           N  
ATOM    534  CA  ASP A  72      57.089  42.398   1.527  1.00 38.31           C  
ATOM    535  C   ASP A  72      56.921  41.828   2.905  1.00 38.27           C  
ATOM    536  O   ASP A  72      57.922  41.612   3.614  1.00 39.15           O  
ATOM    537  CB  ASP A  72      57.687  43.753   1.614  1.00 46.17           C  
ATOM    538  CG  ASP A  72      57.924  44.316   0.227  1.00 50.65           C  
ATOM    539  OD1 ASP A  72      58.246  43.556  -0.698  1.00 51.18           O  
ATOM    540  OD2 ASP A  72      57.773  45.527   0.093  1.00 54.90           O  
ATOM    541  N   ILE A  73      55.655  41.665   3.316  1.00 34.49           N  
ATOM    542  CA  ILE A  73      55.370  40.878   4.500  1.00 35.10           C  
ATOM    543  C   ILE A  73      54.903  39.521   3.951  1.00 34.35           C  
ATOM    544  O   ILE A  73      53.721  39.239   3.787  1.00 35.76           O  
ATOM    545  CB  ILE A  73      54.256  41.481   5.385  1.00 34.44           C  
ATOM    546  CG1 ILE A  73      54.400  42.946   5.683  1.00 31.59           C  
ATOM    547  CG2 ILE A  73      54.347  40.720   6.714  1.00 35.00           C  
ATOM    548  CD1 ILE A  73      53.120  43.464   6.349  1.00 37.46           C  
ATOM    549  N   LYS A  74      55.863  38.669   3.647  1.00 36.55           N  
ATOM    550  CA  LYS A  74      55.616  37.376   3.042  1.00 38.52           C  
ATOM    551  C   LYS A  74      56.425  36.317   3.780  1.00 39.19           C  
ATOM    552  O   LYS A  74      57.412  36.655   4.445  1.00 40.09           O  
ATOM    553  CB  LYS A  74      56.017  37.407   1.582  1.00 38.50           C  
ATOM    554  CG  LYS A  74      57.463  37.700   1.212  1.00 42.69           C  
ATOM    555  CD  LYS A  74      57.585  37.378  -0.285  1.00 52.04           C  
ATOM    556  CE  LYS A  74      58.126  38.504  -1.203  1.00 60.43           C  
ATOM    557  NZ  LYS A  74      59.387  39.083  -0.729  1.00 62.67           N  
ATOM    558  N   GLY A  75      56.029  35.044   3.727  1.00 38.42           N  
ATOM    559  CA  GLY A  75      56.812  33.981   4.345  1.00 39.12           C  
ATOM    560  C   GLY A  75      57.023  32.792   3.388  1.00 39.86           C  
ATOM    561  O   GLY A  75      56.984  32.914   2.155  1.00 38.65           O  
ATOM    562  N   LYS A  76      57.255  31.611   3.990  1.00 37.72           N  
ATOM    563  CA  LYS A  76      57.344  30.348   3.262  1.00 34.89           C  
ATOM    564  C   LYS A  76      55.997  30.023   2.605  1.00 33.94           C  
ATOM    565  O   LYS A  76      55.913  29.477   1.501  1.00 35.82           O  
ATOM    566  CB  LYS A  76      57.670  29.177   4.191  1.00 37.28           C  
ATOM    567  CG  LYS A  76      58.811  29.451   5.121  1.00 45.90           C  
ATOM    568  CD  LYS A  76      58.660  28.656   6.408  1.00 55.42           C  
ATOM    569  CE  LYS A  76      59.737  29.038   7.447  1.00 62.42           C  
ATOM    570  NZ  LYS A  76      59.633  30.409   7.927  1.00 65.16           N  
ATOM    571  N   TYR A  77      54.896  30.282   3.308  1.00 28.56           N  
ATOM    572  CA  TYR A  77      53.607  29.917   2.749  1.00 27.27           C  
ATOM    573  C   TYR A  77      52.678  31.108   2.569  1.00 27.39           C  
ATOM    574  O   TYR A  77      51.653  31.022   1.895  1.00 26.20           O  
ATOM    575  CB  TYR A  77      52.948  28.860   3.652  1.00 31.96           C  
ATOM    576  CG  TYR A  77      53.844  27.733   4.199  1.00 32.75           C  
ATOM    577  CD1 TYR A  77      54.408  26.723   3.395  1.00 25.00           C  
ATOM    578  CD2 TYR A  77      54.100  27.768   5.582  1.00 31.94           C  
ATOM    579  CE1 TYR A  77      55.230  25.764   3.997  1.00 24.93           C  
ATOM    580  CE2 TYR A  77      54.911  26.814   6.177  1.00 29.52           C  
ATOM    581  CZ  TYR A  77      55.475  25.824   5.382  1.00 29.60           C  
ATOM    582  OH  TYR A  77      56.325  24.937   6.028  1.00 30.97           O  
ATOM    583  N   VAL A  78      52.999  32.272   3.134  1.00 26.65           N  
ATOM    584  CA  VAL A  78      52.139  33.432   2.986  1.00 25.52           C  
ATOM    585  C   VAL A  78      52.707  34.280   1.863  1.00 22.82           C  
ATOM    586  O   VAL A  78      53.915  34.484   1.861  1.00 22.41           O  
ATOM    587  CB  VAL A  78      52.140  34.243   4.289  1.00 27.97           C  
ATOM    588  CG1 VAL A  78      51.202  35.454   4.253  1.00 27.50           C  
ATOM    589  CG2 VAL A  78      51.711  33.327   5.379  1.00 28.35           C  
ATOM    590  N   LYS A  79      51.884  34.789   0.950  1.00 25.08           N  
ATOM    591  CA  LYS A  79      52.285  35.771  -0.068  1.00 27.65           C  
ATOM    592  C   LYS A  79      52.365  37.215   0.436  1.00 27.74           C  
ATOM    593  O   LYS A  79      53.260  37.938   0.006  1.00 30.02           O  
ATOM    594  CB  LYS A  79      51.299  35.753  -1.197  1.00 30.80           C  
ATOM    595  CG  LYS A  79      51.320  36.795  -2.323  1.00 40.05           C  
ATOM    596  CD  LYS A  79      49.986  36.568  -3.093  1.00 48.65           C  
ATOM    597  CE  LYS A  79      49.728  37.406  -4.373  1.00 55.21           C  
ATOM    598  NZ  LYS A  79      48.556  36.927  -5.117  1.00 55.71           N  
ATOM    599  N   GLU A  80      51.449  37.672   1.295  1.00 25.83           N  
ATOM    600  CA  GLU A  80      51.356  39.075   1.647  1.00 25.44           C  
ATOM    601  C   GLU A  80      50.422  39.295   2.795  1.00 24.61           C  
ATOM    602  O   GLU A  80      49.371  38.649   2.811  1.00 27.16           O  
ATOM    603  CB  GLU A  80      50.815  39.869   0.521  1.00 25.01           C  
ATOM    604  CG  GLU A  80      49.410  39.567   0.077  1.00 30.68           C  
ATOM    605  CD  GLU A  80      49.049  40.304  -1.179  1.00 38.57           C  
ATOM    606  OE1 GLU A  80      49.678  41.313  -1.473  1.00 46.40           O  
ATOM    607  OE2 GLU A  80      48.140  39.875  -1.882  1.00 44.48           O  
ATOM    608  N   VAL A  81      50.743  40.204   3.700  1.00 22.87           N  
ATOM    609  CA  VAL A  81      49.953  40.522   4.873  1.00 20.58           C  
ATOM    610  C   VAL A  81      49.627  41.982   4.654  1.00 24.69           C  
ATOM    611  O   VAL A  81      50.556  42.755   4.412  1.00 30.08           O  
ATOM    612  CB  VAL A  81      50.827  40.293   6.114  1.00 20.84           C  
ATOM    613  CG1 VAL A  81      50.174  40.796   7.381  1.00 17.89           C  
ATOM    614  CG2 VAL A  81      51.090  38.802   6.235  1.00 20.53           C  
ATOM    615  N   GLU A  82      48.364  42.413   4.787  1.00 27.07           N  
ATOM    616  CA  GLU A  82      47.903  43.742   4.434  1.00 21.75           C  
ATOM    617  C   GLU A  82      47.030  44.493   5.405  1.00 20.53           C  
ATOM    618  O   GLU A  82      45.944  43.993   5.641  1.00 19.99           O  
ATOM    619  CB  GLU A  82      47.156  43.623   3.120  1.00 26.32           C  
ATOM    620  CG  GLU A  82      46.644  44.930   2.558  1.00 34.40           C  
ATOM    621  CD  GLU A  82      45.889  44.871   1.247  1.00 38.53           C  
ATOM    622  OE1 GLU A  82      45.279  43.843   0.935  1.00 43.45           O  
ATOM    623  OE2 GLU A  82      45.905  45.884   0.548  1.00 39.30           O  
ATOM    624  N   VAL A  83      47.375  45.709   5.889  1.00 21.83           N  
ATOM    625  CA  VAL A  83      46.519  46.550   6.765  1.00 13.45           C  
ATOM    626  C   VAL A  83      45.558  47.432   5.945  1.00  8.93           C  
ATOM    627  O   VAL A  83      45.895  48.255   5.118  1.00  9.61           O  
ATOM    628  CB  VAL A  83      47.408  47.424   7.673  1.00  8.50           C  
ATOM    629  CG1 VAL A  83      46.479  48.279   8.440  1.00  8.88           C  
ATOM    630  CG2 VAL A  83      48.283  46.635   8.661  1.00  3.67           C  
ATOM    631  N   LYS A  84      44.294  47.265   6.115  1.00  7.22           N  
ATOM    632  CA  LYS A  84      43.382  48.004   5.324  1.00 12.12           C  
ATOM    633  C   LYS A  84      42.288  48.299   6.297  1.00 12.81           C  
ATOM    634  O   LYS A  84      41.448  47.470   6.605  1.00 15.81           O  
ATOM    635  CB  LYS A  84      42.994  47.112   4.169  1.00 12.00           C  
ATOM    636  CG  LYS A  84      41.620  47.383   3.595  1.00 20.92           C  
ATOM    637  CD  LYS A  84      41.607  46.835   2.197  1.00 32.52           C  
ATOM    638  CE  LYS A  84      41.996  45.395   2.170  1.00 36.33           C  
ATOM    639  NZ  LYS A  84      42.565  45.067   0.873  1.00 43.42           N  
ATOM    640  N   ASN A  85      42.456  49.490   6.854  1.00 15.23           N  
ATOM    641  CA  ASN A  85      41.596  50.127   7.846  1.00 12.19           C  
ATOM    642  C   ASN A  85      41.615  49.465   9.186  1.00  9.41           C  
ATOM    643  O   ASN A  85      40.607  49.242   9.847  1.00  6.99           O  
ATOM    644  CB  ASN A  85      40.159  50.185   7.414  1.00 16.34           C  
ATOM    645  CG  ASN A  85      39.726  51.612   7.172  1.00 27.89           C  
ATOM    646  OD1 ASN A  85      38.890  52.098   7.939  1.00 31.92           O  
ATOM    647  ND2 ASN A  85      40.231  52.327   6.156  1.00 29.58           N  
ATOM    648  N   GLY A  86      42.830  49.244   9.618  1.00  8.23           N  
ATOM    649  CA  GLY A  86      42.996  48.575  10.879  1.00 12.97           C  
ATOM    650  C   GLY A  86      42.831  47.055  10.804  1.00 16.48           C  
ATOM    651  O   GLY A  86      43.125  46.432  11.823  1.00 15.37           O  
ATOM    652  N   VAL A  87      42.392  46.406   9.697  1.00 17.01           N  
ATOM    653  CA  VAL A  87      42.187  44.959   9.648  1.00 16.15           C  
ATOM    654  C   VAL A  87      43.400  44.428   8.937  1.00 16.51           C  
ATOM    655  O   VAL A  87      43.682  44.960   7.848  1.00 18.55           O  
ATOM    656  CB  VAL A  87      40.932  44.567   8.836  1.00 16.71           C  
ATOM    657  CG1 VAL A  87      40.752  43.087   8.848  1.00 15.52           C  
ATOM    658  CG2 VAL A  87      39.670  45.059   9.487  1.00 15.48           C  
ATOM    659  N   VAL A  88      44.134  43.481   9.539  1.00 12.65           N  
ATOM    660  CA  VAL A  88      45.256  42.937   8.835  1.00  9.93           C  
ATOM    661  C   VAL A  88      44.829  41.584   8.274  1.00 12.52           C  
ATOM    662  O   VAL A  88      44.216  40.780   8.967  1.00 16.04           O  
ATOM    663  CB  VAL A  88      46.513  42.956   9.818  1.00 12.72           C  
ATOM    664  CG1 VAL A  88      46.149  43.105  11.277  1.00 12.29           C  
ATOM    665  CG2 VAL A  88      47.363  41.758   9.510  1.00  9.55           C  
ATOM    666  N   THR A  89      45.031  41.343   6.973  1.00 12.38           N  
ATOM    667  CA  THR A  89      44.620  40.145   6.280  1.00 13.51           C  
ATOM    668  C   THR A  89      45.793  39.444   5.615  1.00 16.84           C  
ATOM    669  O   THR A  89      46.516  40.098   4.847  1.00 16.45           O  
ATOM    670  CB  THR A  89      43.569  40.508   5.236  1.00 12.56           C  
ATOM    671  OG1 THR A  89      42.411  41.060   5.907  1.00 14.40           O  
ATOM    672  CG2 THR A  89      43.109  39.292   4.476  1.00 11.85           C  
ATOM    673  N   ALA A  90      46.020  38.143   5.895  1.00 17.23           N  
ATOM    674  CA  ALA A  90      47.161  37.392   5.342  1.00 16.22           C  
ATOM    675  C   ALA A  90      46.632  36.464   4.253  1.00 19.73           C  
ATOM    676  O   ALA A  90      45.584  35.856   4.472  1.00 20.80           O  
ATOM    677  CB  ALA A  90      47.844  36.529   6.389  1.00  6.90           C  
ATOM    678  N   THR A  91      47.292  36.436   3.084  1.00 24.29           N  
ATOM    679  CA  THR A  91      46.942  35.630   1.930  1.00 25.16           C  
ATOM    680  C   THR A  91      47.995  34.563   1.782  1.00 24.42           C  
ATOM    681  O   THR A  91      49.187  34.863   1.833  1.00 22.94           O  
ATOM    682  CB  THR A  91      46.907  36.476   0.624  1.00 27.31           C  
ATOM    683  OG1 THR A  91      45.780  37.363   0.771  1.00 32.68           O  
ATOM    684  CG2 THR A  91      46.801  35.643  -0.675  1.00 20.99           C  
ATOM    685  N   MET A  92      47.572  33.320   1.554  1.00 28.10           N  
ATOM    686  CA  MET A  92      48.469  32.182   1.397  1.00 25.93           C  
ATOM    687  C   MET A  92      48.956  32.160  -0.028  1.00 24.92           C  
ATOM    688  O   MET A  92      48.272  32.619  -0.943  1.00 25.06           O  
ATOM    689  CB  MET A  92      47.723  30.903   1.720  1.00 25.53           C  
ATOM    690  CG  MET A  92      47.087  30.787   3.106  1.00 21.57           C  
ATOM    691  SD  MET A  92      48.232  30.861   4.484  1.00 19.85           S  
ATOM    692  CE  MET A  92      48.976  29.289   4.188  1.00 20.49           C  
ATOM    693  N   LEU A  93      50.122  31.614  -0.262  1.00 25.41           N  
ATOM    694  CA  LEU A  93      50.699  31.628  -1.590  1.00 31.98           C  
ATOM    695  C   LEU A  93      50.002  30.594  -2.461  1.00 35.37           C  
ATOM    696  O   LEU A  93      48.949  30.090  -2.055  1.00 33.67           O  
ATOM    697  CB  LEU A  93      52.181  31.348  -1.421  1.00 35.82           C  
ATOM    698  CG  LEU A  93      53.310  31.833  -2.366  1.00 43.51           C  
ATOM    699  CD1 LEU A  93      52.782  32.555  -3.614  1.00 43.42           C  
ATOM    700  CD2 LEU A  93      54.242  32.720  -1.520  1.00 42.07           C  
ATOM    701  N   SER A  94      50.456  30.278  -3.679  1.00 40.54           N  
ATOM    702  CA  SER A  94      49.882  29.155  -4.410  1.00 45.47           C  
ATOM    703  C   SER A  94      51.057  28.304  -4.898  1.00 49.78           C  
ATOM    704  O   SER A  94      51.184  27.894  -6.058  1.00 53.98           O  
ATOM    705  CB  SER A  94      49.015  29.630  -5.613  1.00 42.26           C  
ATOM    706  OG  SER A  94      48.864  31.033  -5.837  1.00 48.95           O  
ATOM    707  N   SER A  95      51.985  28.044  -3.982  1.00 52.72           N  
ATOM    708  CA  SER A  95      53.180  27.247  -4.244  1.00 55.83           C  
ATOM    709  C   SER A  95      53.812  26.857  -2.897  1.00 53.88           C  
ATOM    710  O   SER A  95      53.991  27.712  -2.027  1.00 56.02           O  
ATOM    711  CB  SER A  95      54.164  28.086  -5.121  1.00 56.65           C  
ATOM    712  OG  SER A  95      54.024  29.505  -4.954  1.00 61.67           O  
ATOM    713  N   GLY A  96      54.103  25.588  -2.631  1.00 48.98           N  
ATOM    714  CA  GLY A  96      54.653  25.226  -1.332  1.00 45.18           C  
ATOM    715  C   GLY A  96      53.551  25.124  -0.292  1.00 44.21           C  
ATOM    716  O   GLY A  96      53.822  24.837   0.875  1.00 44.14           O  
ATOM    717  N   VAL A  97      52.296  25.256  -0.733  1.00 44.41           N  
ATOM    718  CA  VAL A  97      51.122  25.306   0.136  1.00 45.00           C  
ATOM    719  C   VAL A  97      50.164  24.230  -0.401  1.00 47.89           C  
ATOM    720  O   VAL A  97      50.157  23.998  -1.624  1.00 49.96           O  
ATOM    721  CB  VAL A  97      50.465  26.736   0.060  1.00 42.39           C  
ATOM    722  CG1 VAL A  97      49.108  26.787   0.735  1.00 40.68           C  
ATOM    723  CG2 VAL A  97      51.320  27.732   0.784  1.00 36.99           C  
ATOM    724  N   ASN A  98      49.405  23.580   0.512  1.00 47.35           N  
ATOM    725  CA  ASN A  98      48.382  22.556   0.245  1.00 46.00           C  
ATOM    726  C   ASN A  98      47.261  23.057  -0.707  1.00 46.81           C  
ATOM    727  O   ASN A  98      46.867  24.223  -0.559  1.00 50.80           O  
ATOM    728  CB  ASN A  98      47.895  22.135   1.665  1.00 41.74           C  
ATOM    729  CG  ASN A  98      46.507  21.505   1.847  1.00 45.51           C  
ATOM    730  OD1 ASN A  98      45.512  21.745   1.152  1.00 45.67           O  
ATOM    731  ND2 ASN A  98      46.336  20.645   2.832  1.00 46.84           N  
ATOM    732  N   ASN A  99      46.645  22.322  -1.668  1.00 48.19           N  
ATOM    733  CA  ASN A  99      45.629  22.955  -2.543  1.00 52.74           C  
ATOM    734  C   ASN A  99      44.405  23.527  -1.852  1.00 49.43           C  
ATOM    735  O   ASN A  99      43.981  24.624  -2.232  1.00 49.06           O  
ATOM    736  CB  ASN A  99      44.975  22.061  -3.653  1.00 59.84           C  
ATOM    737  CG  ASN A  99      44.134  22.868  -4.696  1.00 65.34           C  
ATOM    738  OD1 ASN A  99      44.618  23.205  -5.777  1.00 67.37           O  
ATOM    739  ND2 ASN A  99      42.875  23.259  -4.497  1.00 66.26           N  
ATOM    740  N   GLU A 100      43.810  22.862  -0.856  1.00 47.97           N  
ATOM    741  CA  GLU A 100      42.616  23.442  -0.284  1.00 47.05           C  
ATOM    742  C   GLU A 100      42.908  24.743   0.458  1.00 41.54           C  
ATOM    743  O   GLU A 100      41.962  25.471   0.745  1.00 41.44           O  
ATOM    744  CB  GLU A 100      41.924  22.396   0.616  1.00 53.09           C  
ATOM    745  CG  GLU A 100      42.579  21.735   1.813  1.00 61.86           C  
ATOM    746  CD  GLU A 100      41.861  20.460   2.267  1.00 67.56           C  
ATOM    747  OE1 GLU A 100      40.738  20.521   2.780  1.00 70.77           O  
ATOM    748  OE2 GLU A 100      42.446  19.391   2.106  1.00 71.87           O  
ATOM    749  N   ILE A 101      44.153  25.093   0.782  1.00 33.76           N  
ATOM    750  CA  ILE A 101      44.359  26.409   1.330  1.00 32.44           C  
ATOM    751  C   ILE A 101      45.208  27.249   0.391  1.00 33.86           C  
ATOM    752  O   ILE A 101      45.618  28.326   0.828  1.00 36.48           O  
ATOM    753  CB  ILE A 101      45.041  26.385   2.744  1.00 27.66           C  
ATOM    754  CG1 ILE A 101      46.428  25.809   2.731  1.00 25.24           C  
ATOM    755  CG2 ILE A 101      44.194  25.547   3.654  1.00 31.37           C  
ATOM    756  CD1 ILE A 101      47.158  25.766   4.079  1.00 21.46           C  
ATOM    757  N   LYS A 102      45.509  26.944  -0.872  1.00 32.09           N  
ATOM    758  CA  LYS A 102      46.412  27.840  -1.555  1.00 31.67           C  
ATOM    759  C   LYS A 102      45.647  29.082  -2.019  1.00 33.29           C  
ATOM    760  O   LYS A 102      44.495  28.997  -2.464  1.00 32.67           O  
ATOM    761  CB  LYS A 102      47.094  27.099  -2.719  1.00 34.27           C  
ATOM    762  CG  LYS A 102      46.274  26.510  -3.872  1.00 42.87           C  
ATOM    763  CD  LYS A 102      47.163  25.948  -5.010  1.00 49.63           C  
ATOM    764  CE  LYS A 102      48.113  24.804  -4.586  1.00 54.92           C  
ATOM    765  NZ  LYS A 102      49.063  24.391  -5.621  1.00 57.64           N  
ATOM    766  N   GLY A 103      46.246  30.266  -1.819  1.00 30.64           N  
ATOM    767  CA  GLY A 103      45.657  31.526  -2.201  1.00 25.69           C  
ATOM    768  C   GLY A 103      44.545  31.990  -1.269  1.00 25.91           C  
ATOM    769  O   GLY A 103      43.907  33.015  -1.519  1.00 27.40           O  
ATOM    770  N   LYS A 104      44.250  31.318  -0.168  1.00 25.16           N  
ATOM    771  CA  LYS A 104      43.117  31.717   0.635  1.00 22.43           C  
ATOM    772  C   LYS A 104      43.617  32.635   1.762  1.00 24.92           C  
ATOM    773  O   LYS A 104      44.850  32.778   1.917  1.00 17.72           O  
ATOM    774  CB  LYS A 104      42.428  30.463   1.225  1.00 24.64           C  
ATOM    775  CG  LYS A 104      41.947  29.238   0.444  1.00 19.09           C  
ATOM    776  CD  LYS A 104      40.827  29.580  -0.470  1.00 24.83           C  
ATOM    777  CE  LYS A 104      40.303  28.353  -1.202  1.00 24.57           C  
ATOM    778  NZ  LYS A 104      39.829  27.392  -0.219  1.00 32.28           N  
ATOM    779  N   LYS A 105      42.684  33.209   2.575  1.00 23.91           N  
ATOM    780  CA  LYS A 105      43.024  34.152   3.639  1.00 24.27           C  
ATOM    781  C   LYS A 105      42.239  34.187   4.936  1.00 22.46           C  
ATOM    782  O   LYS A 105      41.103  33.691   4.987  1.00 22.92           O  
ATOM    783  CB  LYS A 105      43.010  35.587   3.102  1.00 24.93           C  
ATOM    784  CG  LYS A 105      41.980  35.958   2.084  1.00 27.66           C  
ATOM    785  CD  LYS A 105      42.587  36.895   1.035  1.00 24.50           C  
ATOM    786  CE  LYS A 105      41.560  37.092  -0.092  1.00 24.92           C  
ATOM    787  NZ  LYS A 105      40.271  37.637   0.393  1.00 33.21           N  
ATOM    788  N   LEU A 106      42.900  34.725   5.982  1.00 19.23           N  
ATOM    789  CA  LEU A 106      42.282  35.009   7.271  1.00 17.21           C  
ATOM    790  C   LEU A 106      42.564  36.488   7.615  1.00 17.45           C  
ATOM    791  O   LEU A 106      43.324  37.136   6.856  1.00 14.27           O  
ATOM    792  CB  LEU A 106      42.826  34.052   8.390  1.00 20.05           C  
ATOM    793  CG  LEU A 106      44.228  33.689   9.009  1.00 17.93           C  
ATOM    794  CD1 LEU A 106      45.080  33.001   7.988  1.00 19.86           C  
ATOM    795  CD2 LEU A 106      44.938  34.945   9.504  1.00 24.13           C  
ATOM    796  N   SER A 107      41.990  37.015   8.723  1.00 14.05           N  
ATOM    797  CA  SER A 107      42.102  38.410   9.165  1.00 14.04           C  
ATOM    798  C   SER A 107      42.046  38.563  10.673  1.00 14.98           C  
ATOM    799  O   SER A 107      41.290  37.844  11.324  1.00 16.36           O  
ATOM    800  CB  SER A 107      40.966  39.288   8.679  1.00 12.19           C  
ATOM    801  OG  SER A 107      40.727  39.219   7.286  1.00 16.23           O  
ATOM    802  N   LEU A 108      42.789  39.526  11.223  1.00 17.05           N  
ATOM    803  CA  LEU A 108      42.793  39.928  12.628  1.00 16.81           C  
ATOM    804  C   LEU A 108      42.215  41.309  12.637  1.00 18.02           C  
ATOM    805  O   LEU A 108      42.605  42.082  11.754  1.00 23.63           O  
ATOM    806  CB  LEU A 108      44.164  40.080  13.192  1.00 14.99           C  
ATOM    807  CG  LEU A 108      45.009  38.881  13.638  1.00 16.16           C  
ATOM    808  CD1 LEU A 108      45.096  37.797  12.589  1.00 13.46           C  
ATOM    809  CD2 LEU A 108      46.407  39.410  13.881  1.00 14.30           C  
ATOM    810  N   TRP A 109      41.332  41.725  13.533  1.00 17.30           N  
ATOM    811  CA  TRP A 109      40.821  43.107  13.575  1.00 13.30           C  
ATOM    812  C   TRP A 109      40.646  43.445  15.029  1.00 14.40           C  
ATOM    813  O   TRP A 109      40.687  42.496  15.804  1.00 17.69           O  
ATOM    814  CB  TRP A 109      39.451  43.270  12.911  1.00 14.30           C  
ATOM    815  CG  TRP A 109      38.345  42.352  13.431  1.00 17.73           C  
ATOM    816  CD1 TRP A 109      37.299  42.850  14.170  1.00 18.32           C  
ATOM    817  CD2 TRP A 109      38.257  40.988  13.229  1.00 14.27           C  
ATOM    818  NE1 TRP A 109      36.548  41.797  14.438  1.00 14.34           N  
ATOM    819  CE2 TRP A 109      37.069  40.682  13.899  1.00 13.27           C  
ATOM    820  CE3 TRP A 109      38.979  39.986  12.570  1.00 13.60           C  
ATOM    821  CZ2 TRP A 109      36.578  39.371  13.927  1.00  9.55           C  
ATOM    822  CZ3 TRP A 109      38.488  38.690  12.594  1.00 10.55           C  
ATOM    823  CH2 TRP A 109      37.292  38.379  13.272  1.00  6.48           C  
ATOM    824  N   ALA A 110      40.410  44.659  15.504  1.00 17.88           N  
ATOM    825  CA  ALA A 110      40.218  44.900  16.927  1.00 19.28           C  
ATOM    826  C   ALA A 110      39.010  45.774  17.146  1.00 20.78           C  
ATOM    827  O   ALA A 110      38.419  46.273  16.188  1.00 21.15           O  
ATOM    828  CB  ALA A 110      41.428  45.595  17.527  1.00 21.79           C  
ATOM    829  N   ARG A 111      38.553  45.948  18.364  1.00 23.36           N  
ATOM    830  CA  ARG A 111      37.401  46.783  18.648  1.00 25.82           C  
ATOM    831  C   ARG A 111      37.953  47.665  19.744  1.00 27.27           C  
ATOM    832  O   ARG A 111      38.904  47.227  20.412  1.00 23.08           O  
ATOM    833  CB  ARG A 111      36.291  45.932  19.190  1.00 32.14           C  
ATOM    834  CG  ARG A 111      34.922  46.577  19.330  1.00 42.21           C  
ATOM    835  CD  ARG A 111      33.993  46.172  18.180  1.00 53.76           C  
ATOM    836  NE  ARG A 111      33.281  44.914  18.401  1.00 65.42           N  
ATOM    837  CZ  ARG A 111      31.933  44.822  18.305  1.00 72.38           C  
ATOM    838  NH1 ARG A 111      31.160  45.887  18.017  1.00 72.64           N  
ATOM    839  NH2 ARG A 111      31.329  43.640  18.516  1.00 73.79           N  
ATOM    840  N   ARG A 112      37.479  48.889  19.981  1.00 31.94           N  
ATOM    841  CA  ARG A 112      38.041  49.630  21.101  1.00 39.36           C  
ATOM    842  C   ARG A 112      37.349  49.265  22.376  1.00 37.78           C  
ATOM    843  O   ARG A 112      36.134  49.404  22.468  1.00 35.97           O  
ATOM    844  CB  ARG A 112      37.929  51.142  20.980  1.00 45.94           C  
ATOM    845  CG  ARG A 112      36.619  51.754  20.530  1.00 57.41           C  
ATOM    846  CD  ARG A 112      36.515  53.166  21.107  1.00 69.50           C  
ATOM    847  NE  ARG A 112      37.620  54.078  20.793  1.00 80.76           N  
ATOM    848  CZ  ARG A 112      38.574  54.434  21.681  1.00 86.12           C  
ATOM    849  NH1 ARG A 112      38.579  53.979  22.943  1.00 88.42           N  
ATOM    850  NH2 ARG A 112      39.545  55.265  21.292  1.00 86.81           N  
ATOM    851  N   GLU A 113      38.063  48.749  23.355  1.00 38.13           N  
ATOM    852  CA  GLU A 113      37.440  48.517  24.644  1.00 44.18           C  
ATOM    853  C   GLU A 113      38.169  49.602  25.387  1.00 49.55           C  
ATOM    854  O   GLU A 113      39.247  49.457  25.973  1.00 52.25           O  
ATOM    855  CB  GLU A 113      37.743  47.128  25.199  1.00 40.96           C  
ATOM    856  CG  GLU A 113      39.185  46.694  25.116  1.00 44.63           C  
ATOM    857  CD  GLU A 113      39.513  45.311  25.641  1.00 49.46           C  
ATOM    858  OE1 GLU A 113      38.648  44.653  26.240  1.00 53.46           O  
ATOM    859  OE2 GLU A 113      40.658  44.897  25.428  1.00 51.51           O  
ATOM    860  N   ASN A 114      37.575  50.745  25.031  1.00 53.41           N  
ATOM    861  CA  ASN A 114      37.929  52.109  25.422  1.00 56.10           C  
ATOM    862  C   ASN A 114      39.063  52.224  26.443  1.00 55.60           C  
ATOM    863  O   ASN A 114      38.872  51.933  27.633  1.00 57.06           O  
ATOM    864  CB  ASN A 114      36.679  52.777  25.962  1.00 61.33           C  
ATOM    865  CG  ASN A 114      35.431  52.482  25.139  1.00 66.81           C  
ATOM    866  OD1 ASN A 114      34.678  51.556  25.451  1.00 70.13           O  
ATOM    867  ND2 ASN A 114      35.165  53.202  24.054  1.00 67.80           N  
ATOM    868  N   GLY A 115      40.245  52.649  25.966  1.00 50.55           N  
ATOM    869  CA  GLY A 115      41.464  52.625  26.766  1.00 45.84           C  
ATOM    870  C   GLY A 115      42.532  51.790  26.032  1.00 45.49           C  
ATOM    871  O   GLY A 115      43.748  52.094  26.032  1.00 41.40           O  
ATOM    872  N   SER A 116      42.032  50.715  25.382  1.00 44.76           N  
ATOM    873  CA  SER A 116      42.824  49.861  24.516  1.00 42.74           C  
ATOM    874  C   SER A 116      41.867  49.228  23.520  1.00 37.51           C  
ATOM    875  O   SER A 116      40.692  49.604  23.373  1.00 35.84           O  
ATOM    876  CB  SER A 116      43.559  48.780  25.357  1.00 46.38           C  
ATOM    877  OG  SER A 116      42.671  48.053  26.208  1.00 50.06           O  
ATOM    878  N   VAL A 117      42.467  48.325  22.778  1.00 33.49           N  
ATOM    879  CA  VAL A 117      41.745  47.518  21.848  1.00 30.34           C  
ATOM    880  C   VAL A 117      41.783  46.074  22.356  1.00 30.08           C  
ATOM    881  O   VAL A 117      42.640  45.650  23.141  1.00 28.89           O  
ATOM    882  CB  VAL A 117      42.380  47.612  20.452  1.00 27.14           C  
ATOM    883  CG1 VAL A 117      42.090  48.966  19.879  1.00 23.51           C  
ATOM    884  CG2 VAL A 117      43.876  47.428  20.514  1.00 26.42           C  
ATOM    885  N   LYS A 118      40.796  45.346  21.840  1.00 29.24           N  
ATOM    886  CA  LYS A 118      40.527  43.930  22.044  1.00 24.47           C  
ATOM    887  C   LYS A 118      40.791  43.242  20.686  1.00 20.88           C  
ATOM    888  O   LYS A 118      40.137  43.676  19.739  1.00 18.17           O  
ATOM    889  CB  LYS A 118      39.081  43.906  22.484  1.00 25.45           C  
ATOM    890  CG  LYS A 118      38.430  42.601  22.572  1.00 28.35           C  
ATOM    891  CD  LYS A 118      39.146  41.802  23.614  1.00 31.87           C  
ATOM    892  CE  LYS A 118      38.415  40.468  23.764  1.00 39.34           C  
ATOM    893  NZ  LYS A 118      37.027  40.635  24.186  1.00 35.54           N  
ATOM    894  N   TRP A 119      41.682  42.262  20.463  1.00 19.40           N  
ATOM    895  CA  TRP A 119      41.843  41.673  19.131  1.00 21.15           C  
ATOM    896  C   TRP A 119      41.076  40.377  18.798  1.00 18.62           C  
ATOM    897  O   TRP A 119      40.631  39.639  19.678  1.00 20.34           O  
ATOM    898  CB  TRP A 119      43.310  41.419  18.841  1.00 19.95           C  
ATOM    899  CG  TRP A 119      44.032  42.663  18.351  1.00 26.05           C  
ATOM    900  CD1 TRP A 119      44.620  43.506  19.255  1.00 26.56           C  
ATOM    901  CD2 TRP A 119      44.224  43.062  17.045  1.00 29.57           C  
ATOM    902  NE1 TRP A 119      45.194  44.427  18.530  1.00 27.07           N  
ATOM    903  CE2 TRP A 119      44.995  44.207  17.220  1.00 29.84           C  
ATOM    904  CE3 TRP A 119      43.896  42.670  15.752  1.00 36.10           C  
ATOM    905  CZ2 TRP A 119      45.443  44.953  16.133  1.00 30.16           C  
ATOM    906  CZ3 TRP A 119      44.343  43.420  14.642  1.00 35.51           C  
ATOM    907  CH2 TRP A 119      45.113  44.554  14.836  1.00 33.45           C  
ATOM    908  N   PHE A 120      40.804  40.064  17.545  1.00 15.76           N  
ATOM    909  CA  PHE A 120      40.082  38.873  17.169  1.00 14.45           C  
ATOM    910  C   PHE A 120      40.818  38.290  15.982  1.00 15.37           C  
ATOM    911  O   PHE A 120      41.615  38.991  15.333  1.00 17.72           O  
ATOM    912  CB  PHE A 120      38.688  39.204  16.753  1.00 14.33           C  
ATOM    913  CG  PHE A 120      37.937  40.001  17.789  1.00 13.76           C  
ATOM    914  CD1 PHE A 120      37.246  39.338  18.796  1.00 17.50           C  
ATOM    915  CD2 PHE A 120      37.935  41.392  17.711  1.00 16.47           C  
ATOM    916  CE1 PHE A 120      36.542  40.086  19.733  1.00 18.06           C  
ATOM    917  CE2 PHE A 120      37.233  42.139  18.650  1.00 17.79           C  
ATOM    918  CZ  PHE A 120      36.536  41.481  19.660  1.00 19.47           C  
ATOM    919  N   CYS A 121      40.568  37.006  15.707  1.00 14.88           N  
ATOM    920  CA  CYS A 121      41.286  36.246  14.682  1.00 11.58           C  
ATOM    921  C   CYS A 121      40.221  35.424  13.997  1.00 10.13           C  
ATOM    922  O   CYS A 121      39.335  34.920  14.701  1.00 13.02           O  
ATOM    923  CB  CYS A 121      42.302  35.351  15.352  1.00 11.43           C  
ATOM    924  SG  CYS A 121      43.382  34.606  14.102  1.00 16.31           S  
ATOM    925  N   GLY A 122      40.158  35.283  12.689  1.00  5.97           N  
ATOM    926  CA  GLY A 122      39.089  34.502  12.104  1.00  3.81           C  
ATOM    927  C   GLY A 122      39.204  34.630  10.614  1.00  3.63           C  
ATOM    928  O   GLY A 122      40.248  34.938  10.054  1.00  6.23           O  
ATOM    929  N   GLN A 123      38.124  34.401   9.939  1.00  7.38           N  
ATOM    930  CA  GLN A 123      38.096  34.436   8.482  1.00 15.50           C  
ATOM    931  C   GLN A 123      37.886  35.853   8.011  1.00 13.56           C  
ATOM    932  O   GLN A 123      37.376  36.617   8.807  1.00 14.14           O  
ATOM    933  CB  GLN A 123      36.960  33.507   7.991  1.00 17.53           C  
ATOM    934  CG  GLN A 123      37.145  32.054   8.382  1.00 22.90           C  
ATOM    935  CD  GLN A 123      35.995  31.172   7.907  1.00 27.60           C  
ATOM    936  OE1 GLN A 123      34.911  31.129   8.479  1.00 31.29           O  
ATOM    937  NE2 GLN A 123      36.128  30.388   6.862  1.00 27.95           N  
ATOM    938  N   PRO A 124      38.182  36.262   6.790  1.00 13.77           N  
ATOM    939  CA  PRO A 124      38.297  37.668   6.419  1.00 13.25           C  
ATOM    940  C   PRO A 124      37.078  38.491   6.761  1.00 17.90           C  
ATOM    941  O   PRO A 124      35.898  38.077   6.686  1.00 19.12           O  
ATOM    942  CB  PRO A 124      38.581  37.659   4.947  1.00 16.46           C  
ATOM    943  CG  PRO A 124      39.258  36.332   4.768  1.00 19.78           C  
ATOM    944  CD  PRO A 124      38.471  35.400   5.668  1.00 10.56           C  
ATOM    945  N   VAL A 125      37.409  39.741   7.110  1.00 22.73           N  
ATOM    946  CA  VAL A 125      36.404  40.724   7.530  1.00 17.23           C  
ATOM    947  C   VAL A 125      36.701  42.102   6.881  1.00 20.67           C  
ATOM    948  O   VAL A 125      37.857  42.338   6.477  1.00 20.24           O  
ATOM    949  CB  VAL A 125      36.543  40.541   9.049  1.00 11.60           C  
ATOM    950  CG1 VAL A 125      37.350  41.619   9.712  1.00 15.10           C  
ATOM    951  CG2 VAL A 125      35.172  40.380   9.560  1.00 15.37           C  
ATOM    952  N   THR A 126      35.755  43.047   6.658  1.00 20.52           N  
ATOM    953  CA  THR A 126      36.081  44.360   6.119  1.00 19.26           C  
ATOM    954  C   THR A 126      35.550  45.318   7.150  1.00 17.08           C  
ATOM    955  O   THR A 126      34.487  45.042   7.699  1.00 12.75           O  
ATOM    956  CB  THR A 126      35.383  44.691   4.773  1.00 21.35           C  
ATOM    957  OG1 THR A 126      34.485  43.643   4.441  1.00 27.10           O  
ATOM    958  CG2 THR A 126      36.391  44.834   3.650  1.00 25.65           C  
ATOM    959  N   ARG A 127      36.245  46.413   7.466  1.00 14.55           N  
ATOM    960  CA  ARG A 127      35.731  47.382   8.390  1.00 12.90           C  
ATOM    961  C   ARG A 127      34.639  48.235   7.760  1.00 15.18           C  
ATOM    962  O   ARG A 127      34.811  48.807   6.683  1.00 18.18           O  
ATOM    963  CB  ARG A 127      36.907  48.233   8.871  1.00 14.51           C  
ATOM    964  CG  ARG A 127      36.384  49.275   9.876  1.00 12.42           C  
ATOM    965  CD  ARG A 127      37.426  49.854  10.758  1.00 10.50           C  
ATOM    966  NE  ARG A 127      38.169  48.860  11.534  1.00 14.34           N  
ATOM    967  CZ  ARG A 127      37.688  48.272  12.639  1.00 14.31           C  
ATOM    968  NH1 ARG A 127      36.453  48.480  13.048  1.00 12.68           N  
ATOM    969  NH2 ARG A 127      38.450  47.418  13.283  1.00 11.76           N  
ATOM    970  N   THR A 128      33.467  48.293   8.363  1.00 20.35           N  
ATOM    971  CA  THR A 128      32.368  49.117   7.897  1.00 25.10           C  
ATOM    972  C   THR A 128      32.485  50.481   8.555  1.00 26.17           C  
ATOM    973  O   THR A 128      32.411  51.484   7.842  1.00 29.55           O  
ATOM    974  CB  THR A 128      31.085  48.366   8.250  1.00 30.43           C  
ATOM    975  OG1 THR A 128      30.864  47.571   7.078  1.00 40.47           O  
ATOM    976  CG2 THR A 128      29.857  49.215   8.597  1.00 37.90           C  
ATOM    977  N   ASP A 129      32.660  50.590   9.874  1.00 25.57           N  
ATOM    978  CA  ASP A 129      32.927  51.873  10.483  1.00 24.98           C  
ATOM    979  C   ASP A 129      33.922  51.727  11.630  1.00 24.38           C  
ATOM    980  O   ASP A 129      34.399  50.618  11.843  1.00 28.41           O  
ATOM    981  CB  ASP A 129      31.605  52.479  10.939  1.00 25.72           C  
ATOM    982  CG  ASP A 129      30.749  51.692  11.901  1.00 28.48           C  
ATOM    983  OD1 ASP A 129      31.292  51.216  12.898  1.00 31.53           O  
ATOM    984  OD2 ASP A 129      29.543  51.578  11.656  1.00 32.83           O  
ATOM    985  N   ASP A 130      34.217  52.704  12.482  1.00 24.18           N  
ATOM    986  CA  ASP A 130      35.297  52.568  13.441  1.00 25.41           C  
ATOM    987  C   ASP A 130      35.189  51.517  14.508  1.00 26.69           C  
ATOM    988  O   ASP A 130      36.168  51.163  15.191  1.00 25.06           O  
ATOM    989  CB  ASP A 130      35.523  53.918  14.072  1.00 29.90           C  
ATOM    990  CG  ASP A 130      36.495  54.789  13.266  1.00 34.57           C  
ATOM    991  OD1 ASP A 130      36.388  54.883  12.028  1.00 39.25           O  
ATOM    992  OD2 ASP A 130      37.367  55.387  13.909  1.00 33.04           O  
ATOM    993  N   ASP A 131      33.977  51.016  14.628  1.00 27.36           N  
ATOM    994  CA  ASP A 131      33.779  49.887  15.507  1.00 35.36           C  
ATOM    995  C   ASP A 131      33.043  48.683  14.898  1.00 32.78           C  
ATOM    996  O   ASP A 131      32.589  47.858  15.687  1.00 33.83           O  
ATOM    997  CB  ASP A 131      33.038  50.361  16.764  1.00 45.28           C  
ATOM    998  CG  ASP A 131      33.738  51.468  17.549  1.00 52.60           C  
ATOM    999  OD1 ASP A 131      34.968  51.469  17.686  1.00 57.66           O  
ATOM   1000  OD2 ASP A 131      33.017  52.341  18.028  1.00 57.16           O  
ATOM   1001  N   THR A 132      32.809  48.469  13.592  1.00 29.25           N  
ATOM   1002  CA  THR A 132      32.149  47.256  13.163  1.00 25.65           C  
ATOM   1003  C   THR A 132      32.853  46.747  11.945  1.00 23.80           C  
ATOM   1004  O   THR A 132      33.240  47.547  11.094  1.00 22.17           O  
ATOM   1005  CB  THR A 132      30.659  47.442  12.775  1.00 29.40           C  
ATOM   1006  OG1 THR A 132      30.616  48.360  11.702  1.00 36.82           O  
ATOM   1007  CG2 THR A 132      29.798  47.996  13.896  1.00 32.22           C  
ATOM   1008  N   VAL A 133      33.085  45.442  11.858  1.00 25.23           N  
ATOM   1009  CA  VAL A 133      33.590  44.837  10.650  1.00 19.79           C  
ATOM   1010  C   VAL A 133      32.453  43.946  10.150  1.00 20.36           C  
ATOM   1011  O   VAL A 133      31.479  43.623  10.854  1.00 22.19           O  
ATOM   1012  CB  VAL A 133      34.804  44.004  10.924  1.00 16.07           C  
ATOM   1013  CG1 VAL A 133      35.903  44.874  11.389  1.00 15.25           C  
ATOM   1014  CG2 VAL A 133      34.491  42.936  11.952  1.00 18.55           C  
ATOM   1015  N   ALA A 134      32.545  43.523   8.915  1.00 19.29           N  
ATOM   1016  CA  ALA A 134      31.528  42.705   8.310  1.00 20.22           C  
ATOM   1017  C   ALA A 134      32.280  41.582   7.658  1.00 21.39           C  
ATOM   1018  O   ALA A 134      33.459  41.773   7.332  1.00 21.08           O  
ATOM   1019  CB  ALA A 134      30.767  43.416   7.211  1.00 19.67           C  
ATOM   1020  N   ASP A 135      31.627  40.415   7.515  1.00 22.02           N  
ATOM   1021  CA  ASP A 135      32.247  39.267   6.890  1.00 26.14           C  
ATOM   1022  C   ASP A 135      32.510  39.610   5.463  1.00 26.45           C  
ATOM   1023  O   ASP A 135      31.634  40.115   4.763  1.00 27.99           O  
ATOM   1024  CB  ASP A 135      31.400  38.023   6.817  1.00 29.35           C  
ATOM   1025  CG  ASP A 135      31.690  36.972   7.866  1.00 38.21           C  
ATOM   1026  OD1 ASP A 135      32.824  36.852   8.383  1.00 44.03           O  
ATOM   1027  OD2 ASP A 135      30.734  36.256   8.148  1.00 37.49           O  
ATOM   1028  N   ALA A 136      33.730  39.291   5.082  1.00 29.42           N  
ATOM   1029  CA  ALA A 136      34.186  39.532   3.738  1.00 31.76           C  
ATOM   1030  C   ALA A 136      34.512  38.159   3.170  1.00 33.44           C  
ATOM   1031  O   ALA A 136      35.661  37.844   2.815  1.00 31.49           O  
ATOM   1032  CB  ALA A 136      35.446  40.405   3.757  1.00 34.52           C  
ATOM   1033  N   LYS A 137      33.501  37.312   3.080  1.00 33.52           N  
ATOM   1034  CA  LYS A 137      33.800  35.985   2.625  1.00 38.28           C  
ATOM   1035  C   LYS A 137      33.276  36.018   1.203  1.00 38.42           C  
ATOM   1036  O   LYS A 137      32.158  36.391   0.881  1.00 39.04           O  
ATOM   1037  CB  LYS A 137      33.112  34.922   3.547  1.00 44.42           C  
ATOM   1038  CG  LYS A 137      33.710  34.718   4.994  1.00 46.78           C  
ATOM   1039  CD  LYS A 137      32.813  33.757   5.854  1.00 49.66           C  
ATOM   1040  CE  LYS A 137      33.148  33.690   7.369  1.00 50.46           C  
ATOM   1041  NZ  LYS A 137      32.188  32.951   8.187  1.00 44.53           N  
ATOM   1042  N   ASP A 138      34.271  35.806   0.358  1.00 39.85           N  
ATOM   1043  CA  ASP A 138      34.147  35.867  -1.092  1.00 37.23           C  
ATOM   1044  C   ASP A 138      34.458  34.534  -1.730  1.00 36.24           C  
ATOM   1045  O   ASP A 138      34.628  34.439  -2.942  1.00 36.70           O  
ATOM   1046  CB  ASP A 138      35.131  36.920  -1.663  1.00 34.92           C  
ATOM   1047  CG  ASP A 138      36.602  36.765  -1.279  1.00 31.99           C  
ATOM   1048  OD1 ASP A 138      36.950  35.821  -0.569  1.00 32.48           O  
ATOM   1049  OD2 ASP A 138      37.407  37.610  -1.664  1.00 34.86           O  
ATOM   1050  N   GLY A 139      34.661  33.532  -0.878  1.00 34.83           N  
ATOM   1051  CA  GLY A 139      35.077  32.202  -1.303  1.00 30.30           C  
ATOM   1052  C   GLY A 139      36.584  32.014  -1.258  1.00 26.66           C  
ATOM   1053  O   GLY A 139      37.061  30.955  -1.649  1.00 29.91           O  
ATOM   1054  N   LYS A 140      37.389  32.969  -0.798  1.00 22.16           N  
ATOM   1055  CA  LYS A 140      38.813  32.753  -0.724  1.00 16.70           C  
ATOM   1056  C   LYS A 140      39.270  32.742   0.731  1.00 16.95           C  
ATOM   1057  O   LYS A 140      40.440  32.922   1.059  1.00 12.75           O  
ATOM   1058  CB  LYS A 140      39.510  33.841  -1.547  1.00 21.04           C  
ATOM   1059  CG  LYS A 140      39.080  33.803  -3.034  1.00 24.43           C  
ATOM   1060  CD  LYS A 140      39.914  34.687  -3.959  1.00 27.25           C  
ATOM   1061  CE  LYS A 140      39.445  34.475  -5.420  1.00 34.70           C  
ATOM   1062  NZ  LYS A 140      38.059  34.828  -5.690  1.00 33.06           N  
ATOM   1063  N   GLU A 141      38.380  32.451   1.673  1.00 17.27           N  
ATOM   1064  CA  GLU A 141      38.785  32.378   3.070  1.00 22.60           C  
ATOM   1065  C   GLU A 141      39.220  30.969   3.524  1.00 19.99           C  
ATOM   1066  O   GLU A 141      38.716  29.968   3.014  1.00 16.91           O  
ATOM   1067  CB  GLU A 141      37.662  32.841   3.945  1.00 26.53           C  
ATOM   1068  CG  GLU A 141      36.283  32.283   3.740  1.00 38.77           C  
ATOM   1069  CD  GLU A 141      35.554  32.751   2.488  1.00 43.60           C  
ATOM   1070  OE1 GLU A 141      35.990  33.702   1.828  1.00 45.20           O  
ATOM   1071  OE2 GLU A 141      34.524  32.151   2.177  1.00 49.40           O  
ATOM   1072  N   ILE A 142      40.164  30.835   4.472  1.00 20.84           N  
ATOM   1073  CA  ILE A 142      40.646  29.552   4.977  1.00 19.12           C  
ATOM   1074  C   ILE A 142      39.425  28.991   5.640  1.00 22.60           C  
ATOM   1075  O   ILE A 142      38.702  29.680   6.366  1.00 23.17           O  
ATOM   1076  CB  ILE A 142      41.622  29.554   6.130  1.00 20.28           C  
ATOM   1077  CG1 ILE A 142      42.761  30.498   5.912  1.00 20.88           C  
ATOM   1078  CG2 ILE A 142      42.133  28.147   6.303  1.00 18.61           C  
ATOM   1079  CD1 ILE A 142      43.628  30.208   4.729  1.00 25.54           C  
ATOM   1080  N   ASP A 143      39.239  27.731   5.319  1.00 23.26           N  
ATOM   1081  CA  ASP A 143      38.175  26.901   5.845  1.00 24.15           C  
ATOM   1082  C   ASP A 143      38.307  26.812   7.348  1.00 19.28           C  
ATOM   1083  O   ASP A 143      39.430  26.911   7.850  1.00 17.21           O  
ATOM   1084  CB  ASP A 143      38.267  25.482   5.233  1.00 33.78           C  
ATOM   1085  CG  ASP A 143      38.269  25.507   3.711  1.00 36.39           C  
ATOM   1086  OD1 ASP A 143      39.273  25.897   3.101  1.00 42.95           O  
ATOM   1087  OD2 ASP A 143      37.242  25.170   3.143  1.00 36.80           O  
ATOM   1088  N   THR A 144      37.208  26.553   8.049  1.00 18.66           N  
ATOM   1089  CA  THR A 144      37.246  26.483   9.484  1.00 20.17           C  
ATOM   1090  C   THR A 144      38.089  25.287   9.929  1.00 23.18           C  
ATOM   1091  O   THR A 144      38.854  25.432  10.893  1.00 23.91           O  
ATOM   1092  CB  THR A 144      35.821  26.369  10.024  1.00 18.95           C  
ATOM   1093  OG1 THR A 144      35.056  27.440   9.494  1.00 22.51           O  
ATOM   1094  CG2 THR A 144      35.771  26.511  11.517  1.00 22.62           C  
ATOM   1095  N   LYS A 145      38.063  24.122   9.244  1.00 22.10           N  
ATOM   1096  CA  LYS A 145      38.809  22.950   9.695  1.00 18.69           C  
ATOM   1097  C   LYS A 145      40.290  23.228   9.832  1.00 19.29           C  
ATOM   1098  O   LYS A 145      40.934  22.544  10.625  1.00 25.93           O  
ATOM   1099  CB  LYS A 145      38.568  21.783   8.720  1.00 16.97           C  
ATOM   1100  CG  LYS A 145      39.096  21.947   7.305  1.00 22.79           C  
ATOM   1101  CD  LYS A 145      38.540  20.971   6.280  1.00 26.61           C  
ATOM   1102  CE  LYS A 145      39.494  19.815   6.057  1.00 31.20           C  
ATOM   1103  NZ  LYS A 145      39.788  19.129   7.300  1.00 35.65           N  
ATOM   1104  N   HIS A 146      40.884  24.209   9.141  1.00 15.81           N  
ATOM   1105  CA  HIS A 146      42.325  24.486   9.278  1.00 16.23           C  
ATOM   1106  C   HIS A 146      42.703  25.654  10.200  1.00 18.14           C  
ATOM   1107  O   HIS A 146      43.892  25.966  10.370  1.00 18.18           O  
ATOM   1108  CB  HIS A 146      42.953  24.794   7.945  1.00 17.93           C  
ATOM   1109  CG  HIS A 146      42.774  23.669   6.962  1.00 22.88           C  
ATOM   1110  ND1 HIS A 146      43.162  22.406   7.079  1.00 23.85           N  
ATOM   1111  CD2 HIS A 146      42.078  23.813   5.788  1.00 23.36           C  
ATOM   1112  CE1 HIS A 146      42.717  21.784   6.018  1.00 25.89           C  
ATOM   1113  NE2 HIS A 146      42.066  22.636   5.250  1.00 25.24           N  
ATOM   1114  N   LEU A 147      41.712  26.339  10.792  1.00 20.56           N  
ATOM   1115  CA  LEU A 147      41.928  27.458  11.692  1.00 20.30           C  
ATOM   1116  C   LEU A 147      42.001  26.878  13.109  1.00 21.17           C  
ATOM   1117  O   LEU A 147      41.141  26.079  13.512  1.00 26.55           O  
ATOM   1118  CB  LEU A 147      40.755  28.465  11.587  1.00 17.02           C  
ATOM   1119  CG  LEU A 147      40.824  29.731  10.760  1.00 14.68           C  
ATOM   1120  CD1 LEU A 147      42.103  29.860  10.004  1.00 11.23           C  
ATOM   1121  CD2 LEU A 147      39.750  29.680   9.734  1.00 16.10           C  
ATOM   1122  N   PRO A 148      42.999  27.211  13.919  1.00 17.78           N  
ATOM   1123  CA  PRO A 148      43.015  26.894  15.329  1.00 18.62           C  
ATOM   1124  C   PRO A 148      41.772  27.397  16.017  1.00 21.27           C  
ATOM   1125  O   PRO A 148      41.129  28.349  15.575  1.00 23.52           O  
ATOM   1126  CB  PRO A 148      44.256  27.550  15.858  1.00 18.75           C  
ATOM   1127  CG  PRO A 148      45.147  27.636  14.657  1.00 21.10           C  
ATOM   1128  CD  PRO A 148      44.160  27.986  13.537  1.00 20.67           C  
ATOM   1129  N   SER A 149      41.469  26.830  17.170  1.00 24.05           N  
ATOM   1130  CA  SER A 149      40.317  27.229  17.970  1.00 27.14           C  
ATOM   1131  C   SER A 149      40.420  28.646  18.528  1.00 29.63           C  
ATOM   1132  O   SER A 149      39.453  29.302  18.938  1.00 30.47           O  
ATOM   1133  CB  SER A 149      40.211  26.226  19.069  1.00 28.46           C  
ATOM   1134  OG  SER A 149      41.537  25.954  19.534  1.00 34.87           O  
ATOM   1135  N   THR A 150      41.643  29.146  18.569  1.00 30.31           N  
ATOM   1136  CA  THR A 150      41.925  30.518  18.932  1.00 30.74           C  
ATOM   1137  C   THR A 150      41.544  31.484  17.807  1.00 28.37           C  
ATOM   1138  O   THR A 150      41.400  32.697  18.013  1.00 30.78           O  
ATOM   1139  CB  THR A 150      43.404  30.672  19.202  1.00 30.05           C  
ATOM   1140  OG1 THR A 150      44.022  29.913  18.171  1.00 36.21           O  
ATOM   1141  CG2 THR A 150      43.858  30.208  20.567  1.00 33.26           C  
ATOM   1142  N   CYS A 151      41.375  30.978  16.595  1.00 22.33           N  
ATOM   1143  CA  CYS A 151      41.164  31.857  15.499  1.00 18.87           C  
ATOM   1144  C   CYS A 151      39.954  31.401  14.784  1.00 18.27           C  
ATOM   1145  O   CYS A 151      39.952  31.019  13.632  1.00 23.75           O  
ATOM   1146  CB  CYS A 151      42.394  31.818  14.630  1.00 18.02           C  
ATOM   1147  SG  CYS A 151      42.234  33.118  13.390  1.00 23.20           S  
ATOM   1148  N   ARG A 152      38.884  31.489  15.492  1.00 18.53           N  
ATOM   1149  CA  ARG A 152      37.601  31.050  14.998  1.00 20.20           C  
ATOM   1150  C   ARG A 152      36.644  32.199  15.218  1.00 22.90           C  
ATOM   1151  O   ARG A 152      35.463  31.933  15.428  1.00 27.62           O  
ATOM   1152  CB  ARG A 152      37.146  29.851  15.821  1.00 19.53           C  
ATOM   1153  CG  ARG A 152      37.939  28.585  15.572  1.00 24.81           C  
ATOM   1154  CD  ARG A 152      37.533  28.003  14.230  1.00 24.53           C  
ATOM   1155  NE  ARG A 152      38.260  26.781  13.932  1.00 28.46           N  
ATOM   1156  CZ  ARG A 152      37.835  25.589  14.312  1.00 23.25           C  
ATOM   1157  NH1 ARG A 152      36.706  25.395  14.975  1.00 21.96           N  
ATOM   1158  NH2 ARG A 152      38.583  24.577  13.983  1.00 25.05           N  
ATOM   1159  N   ASP A 153      37.033  33.479  15.230  1.00 24.35           N  
ATOM   1160  CA  ASP A 153      36.092  34.562  15.573  1.00 19.60           C  
ATOM   1161  C   ASP A 153      35.221  35.071  14.435  1.00 16.10           C  
ATOM   1162  O   ASP A 153      35.588  35.225  13.257  1.00 12.24           O  
ATOM   1163  CB  ASP A 153      36.821  35.787  16.185  1.00 17.03           C  
ATOM   1164  CG  ASP A 153      37.426  35.544  17.563  1.00 15.90           C  
ATOM   1165  OD1 ASP A 153      36.687  35.183  18.475  1.00 17.70           O  
ATOM   1166  OD2 ASP A 153      38.623  35.745  17.742  1.00  9.39           O  
ATOM   1167  N   ASN A 154      33.968  35.189  14.817  1.00 18.48           N  
ATOM   1168  CA  ASN A 154      32.993  35.612  13.848  1.00 24.91           C  
ATOM   1169  C   ASN A 154      32.955  37.125  13.825  1.00 27.11           C  
ATOM   1170  O   ASN A 154      33.355  37.772  14.796  1.00 26.36           O  
ATOM   1171  CB  ASN A 154      31.601  35.023  14.184  1.00 26.56           C  
ATOM   1172  CG  ASN A 154      31.383  33.544  13.800  1.00 26.01           C  
ATOM   1173  OD1 ASN A 154      30.619  32.843  14.476  1.00 23.32           O  
ATOM   1174  ND2 ASN A 154      31.986  33.028  12.721  1.00 21.75           N  
ATOM   1175  N   PHE A 155      32.414  37.666  12.726  1.00 22.39           N  
ATOM   1176  CA  PHE A 155      32.464  39.072  12.460  1.00 18.36           C  
ATOM   1177  C   PHE A 155      31.950  39.951  13.585  1.00 20.28           C  
ATOM   1178  O   PHE A 155      32.398  41.066  13.846  1.00 24.11           O  
ATOM   1179  CB  PHE A 155      31.699  39.337  11.157  1.00 15.83           C  
ATOM   1180  CG  PHE A 155      30.192  39.322  11.318  1.00 15.68           C  
ATOM   1181  CD1 PHE A 155      29.496  38.117  11.222  1.00 12.70           C  
ATOM   1182  CD2 PHE A 155      29.525  40.507  11.636  1.00 12.88           C  
ATOM   1183  CE1 PHE A 155      28.126  38.107  11.450  1.00 13.43           C  
ATOM   1184  CE2 PHE A 155      28.158  40.479  11.865  1.00 14.21           C  
ATOM   1185  CZ  PHE A 155      27.451  39.290  11.773  1.00 16.64           C  
ATOM   1186  N   ASP A 156      30.985  39.424  14.290  1.00 21.10           N  
ATOM   1187  CA  ASP A 156      30.353  40.185  15.332  1.00 22.89           C  
ATOM   1188  C   ASP A 156      30.917  39.864  16.695  1.00 23.52           C  
ATOM   1189  O   ASP A 156      30.261  40.225  17.660  1.00 22.77           O  
ATOM   1190  CB  ASP A 156      28.869  39.901  15.284  1.00 25.23           C  
ATOM   1191  CG  ASP A 156      28.430  38.433  15.400  1.00 38.48           C  
ATOM   1192  OD1 ASP A 156      29.255  37.498  15.518  1.00 45.18           O  
ATOM   1193  OD2 ASP A 156      27.213  38.232  15.375  1.00 42.11           O  
ATOM   1194  N   ALA A 157      32.060  39.191  16.816  1.00 25.28           N  
ATOM   1195  CA  ALA A 157      32.595  38.787  18.110  1.00 27.02           C  
ATOM   1196  C   ALA A 157      32.853  40.022  18.918  1.00 30.58           C  
ATOM   1197  O   ALA A 157      33.123  41.097  18.375  1.00 29.56           O  
ATOM   1198  CB  ALA A 157      33.938  38.081  18.004  1.00 22.02           C  
ATOM   1199  N   LYS A 158      32.722  39.823  20.204  1.00 38.05           N  
ATOM   1200  CA  LYS A 158      33.060  40.831  21.180  1.00 44.08           C  
ATOM   1201  C   LYS A 158      33.670  40.061  22.362  1.00 47.39           C  
ATOM   1202  O   LYS A 158      33.479  38.826  22.496  1.00 47.51           O  
ATOM   1203  CB  LYS A 158      31.801  41.601  21.579  1.00 45.59           C  
ATOM   1204  CG  LYS A 158      31.708  43.106  21.325  1.00 52.03           C  
ATOM   1205  CD  LYS A 158      32.429  44.018  22.302  1.00 58.76           C  
ATOM   1206  CE  LYS A 158      31.684  44.433  23.558  1.00 60.56           C  
ATOM   1207  NZ  LYS A 158      32.050  43.534  24.623  1.00 61.95           N  
ATOM   1208  OXT LYS A 158      34.412  40.714  23.101  1.00 48.90           O  
TER    1209      LYS A 158                                                      
HETATM 1210  C1  NAG B   1      47.466  56.703   6.770  1.00 25.34           C  
HETATM 1211  C2  NAG B   1      47.113  57.291   5.426  1.00 26.66           C  
HETATM 1212  C3  NAG B   1      46.407  58.592   5.701  1.00 29.26           C  
HETATM 1213  C4  NAG B   1      45.110  58.259   6.424  1.00 32.68           C  
HETATM 1214  C5  NAG B   1      45.449  57.536   7.740  1.00 28.42           C  
HETATM 1215  C6  NAG B   1      44.221  57.060   8.483  1.00 34.28           C  
HETATM 1216  C7  NAG B   1      48.445  56.944   3.472  1.00 27.81           C  
HETATM 1217  C8  NAG B   1      49.808  56.996   2.816  1.00 28.26           C  
HETATM 1218  N2  NAG B   1      48.325  57.493   4.662  1.00 24.24           N  
HETATM 1219  O3  NAG B   1      46.136  59.277   4.470  1.00 36.15           O  
HETATM 1220  O4  NAG B   1      44.372  59.449   6.670  1.00 35.03           O  
HETATM 1221  O5  NAG B   1      46.262  56.372   7.471  1.00 26.02           O  
HETATM 1222  O6  NAG B   1      43.410  58.147   8.890  1.00 43.95           O  
HETATM 1223  O7  NAG B   1      47.453  56.548   2.858  1.00 35.20           O  
HETATM 1224  C1  GLA B   2      46.372  60.653   4.503  1.00 35.48           C  
HETATM 1225  C2  GLA B   2      45.628  61.326   3.359  1.00 38.03           C  
HETATM 1226  C3  GLA B   2      46.267  60.958   2.026  1.00 42.34           C  
HETATM 1227  C4  GLA B   2      47.743  61.320   2.060  1.00 38.43           C  
HETATM 1228  C5  GLA B   2      48.432  60.643   3.240  1.00 35.49           C  
HETATM 1229  C6  GLA B   2      49.873  61.098   3.395  1.00 36.89           C  
HETATM 1230  O2  GLA B   2      44.266  60.907   3.361  1.00 41.52           O  
HETATM 1231  O3  GLA B   2      45.618  61.678   0.988  1.00 47.60           O  
HETATM 1232  O4  GLA B   2      47.877  62.727   2.172  1.00 50.40           O  
HETATM 1233  O5  GLA B   2      47.760  60.966   4.472  1.00 31.49           O  
HETATM 1234  O6  GLA B   2      50.563  61.071   2.153  1.00 43.04           O  
HETATM 1235 PT    PT A 200      50.361  60.539  13.430  0.50 73.12          PT  
HETATM 1236  C1  HTO A 162      64.725 -23.987  -8.652  1.00 98.79           C  
HETATM 1237  O1  HTO A 162      65.992 -24.357  -9.210  1.00 97.76           O  
HETATM 1238  C2  HTO A 162      64.275 -25.145  -7.721  1.00 98.89           C  
HETATM 1239  O2  HTO A 162      65.487 -25.763  -7.262  1.00101.20           O  
HETATM 1240  C3  HTO A 162      63.502 -24.756  -6.397  1.00 96.88           C  
HETATM 1241  O3  HTO A 162      62.483 -23.832  -6.749  1.00 94.96           O  
HETATM 1242  C4  HTO A 162      64.406 -24.180  -5.322  1.00 93.04           C  
HETATM 1243  C5  HTO A 162      63.718 -23.852  -4.008  1.00 91.71           C  
HETATM 1244  C6  HTO A 162      64.748 -23.216  -3.091  1.00 90.13           C  
HETATM 1245  C7  HTO A 162      64.117 -22.687  -1.805  1.00 88.42           C  
HETATM 1246  O   HOH A 301      37.426  50.323  17.741  1.00 25.61           O  
HETATM 1247  O   HOH A 303      20.870  40.253  11.015  1.00 36.24           O  
HETATM 1248  O   HOH A 307      38.855  46.801   6.247  1.00  6.84           O  
HETATM 1249  O   HOH A 308      45.874  44.749  -4.034  1.00 31.74           O  
HETATM 1250  O   HOH A 310      46.907   7.846  -3.703  1.00 45.16           O  
HETATM 1251  O   HOH A 311      59.738  -0.578  -1.189  1.00 41.55           O  
HETATM 1252  O   HOH A 314      46.609   9.314  12.764  1.00 71.21           O  
HETATM 1253  O   HOH A 315      36.605  18.023   8.888  1.00 34.90           O  
HETATM 1254  O   HOH A 317      31.726  48.755   2.515  1.00 36.23           O  
HETATM 1255  O   HOH A 322      35.055  36.025  10.354  1.00 13.96           O  
HETATM 1256  O   HOH A 323      36.173  46.912  15.133  1.00 14.45           O  
HETATM 1257  O   HOH A 324      34.210  42.083  16.007  1.00 23.52           O  
HETATM 1258  O   HOH A 325      41.141  35.378  18.779  1.00 37.32           O  
HETATM 1259  O   HOH A 326      27.332  37.084   6.804  1.00 24.43           O  
HETATM 1260  O   HOH A 328      39.108  54.806  11.336  1.00 28.88           O  
HETATM 1261  O   HOH A 333      49.386  60.426  12.103  1.00 34.17           O  
HETATM 1262  O   HOH A 334      48.597  48.626   2.526  1.00 35.36           O  
HETATM 1263  O   HOH A 335      59.298  24.847   6.201  1.00 60.47           O  
HETATM 1264  O   HOH A 336      45.678  48.623   2.550  1.00 18.23           O  
HETATM 1265  O   HOH A 338      35.562  52.115   7.530  1.00 45.72           O  
HETATM 1266  O   HOH A 340      52.175  30.821  -6.617  1.00 39.61           O  
HETATM 1267  O   HOH A 341      40.894  41.757  -0.646  1.00 62.06           O  
HETATM 1268  O   HOH A 343      35.052  25.996   6.068  1.00 41.89           O  
HETATM 1269  O   HOH A 344      45.383  35.495  22.579  1.00 81.31           O  
HETATM 1270  O   HOH A 345      49.063  27.318  -7.710  1.00 59.06           O  
HETATM 1271  O   HOH A 346      50.504  32.869  20.063  1.00 59.69           O  
HETATM 1272  O   HOH A 347      55.796  38.294  14.084  1.00 25.92           O  
HETATM 1273  O   HOH A 348      51.354  61.820  13.261  1.00137.49           O  
HETATM 1274  O   HOH A 352      45.558  41.670  -5.278  1.00 63.49           O  
HETATM 1275  O   HOH A 353      39.288  37.694  -5.601  1.00 33.26           O  
HETATM 1276  O   HOH A 354      46.423  39.899   1.996  1.00 20.51           O  
HETATM 1277  O   HOH A 355      55.833  43.117  16.145  1.00 35.24           O  
HETATM 1278  O   HOH A 356      40.522  54.885   8.842  1.00 36.09           O  
HETATM 1279  O   HOH A 357      40.171  57.311  -0.006  1.00 58.55           O  
HETATM 1280  O   HOH A 358      40.201  42.793   2.889  1.00 54.86           O  
HETATM 1281  O   HOH A 359      53.291  58.463   0.897  1.00 57.24           O  
HETATM 1282  O   HOH A 361      37.159  27.793  19.116  1.00 60.19           O  
HETATM 1283  O   HOH A 362      40.436  43.632   5.449  1.00 36.33           O  
HETATM 1284  O   HOH A 364      62.313  28.793   4.651  1.00 32.91           O  
HETATM 1285  O   HOH A 365      59.275  26.308  -3.825  1.00 31.94           O  
HETATM 1286  O   HOH A 366      42.957  37.031  19.762  1.00 43.42           O  
HETATM 1287  O   HOH A 367      43.059  44.033   5.493  1.00 14.17           O  
HETATM 1288  O   HOH A 371      25.355  48.312  18.010  1.00 54.80           O  
HETATM 1289  O   HOH A 372      37.786  41.966  27.104  1.00 35.64           O  
HETATM 1290  O   HOH A 375      37.903  36.433   1.956  1.00 36.08           O  
HETATM 1291  O   HOH A 376      34.243  46.644   0.545  1.00 48.23           O  
HETATM 1292  O   HOH A 377      41.361  46.807  13.584  1.00 10.38           O  
HETATM 1293  O   HOH A 378      26.963  43.010   6.181  1.00 54.26           O  
HETATM 1294  O   HOH A 381      23.448  39.596  13.263  1.00 39.57           O  
HETATM 1295  O   HOH A 382      20.735  45.219  14.295  1.00 81.17           O  
HETATM 1296  O   HOH A 383      36.368  32.665  12.047  1.00 29.89           O  
HETATM 1297  O   HOH A 384      45.738  15.398  11.562  1.00 36.93           O  
HETATM 1298  O   HOH A 386      39.214  30.155  22.023  1.00 70.78           O  
HETATM 1299  O   HOH A 387      50.991  57.661  -0.387  1.00 68.89           O  
HETATM 1300  O   HOH A 388      55.078  52.208  19.503  1.00 71.64           O  
HETATM 1301  O   HOH A 389      41.413   7.578   3.200  1.00 46.32           O  
HETATM 1302  O   HOH A 390      54.128  46.210  14.665  1.00 33.20           O  
HETATM 1303  O   HOH A 391      50.156  49.343  -0.117  1.00 47.75           O  
HETATM 1304  O   HOH A 394      53.794  -8.921  -8.192  1.00 58.48           O  
HETATM 1305  O   HOH A 395      54.717 -12.024 -10.345  1.00 47.54           O  
HETATM 1306  O   HOH A 396      55.016  -6.615  -6.995  1.00 46.27           O  
HETATM 1307  O   HOH A 397      56.551  15.972   8.566  1.00 67.58           O  
HETATM 1308  O   HOH A 398      56.008 -17.214   8.788  1.00 39.60           O  
HETATM 1309  O   HOH A 399      61.092  -3.529  -4.202  1.00 62.11           O  
HETATM 1310  O   HOH A 401      54.047   1.568  13.901  1.00 72.66           O  
HETATM 1311  O   HOH A 403      59.528   1.482  -2.881  1.00 59.61           O  
HETATM 1312  O   HOH A 404      54.386  20.816   2.606  1.00 61.46           O  
HETATM 1313  O   HOH A 405      50.750  17.708  17.100  1.00 62.27           O  
HETATM 1314  O   HOH A 406      53.913  14.154  13.123  1.00 73.47           O  
HETATM 1315  O   HOH A 407      45.538  18.648  11.857  1.00 47.65           O  
HETATM 1316  O   HOH A 408      50.693  19.538   0.162  1.00 46.11           O  
HETATM 1317  O   HOH A 409      51.765  23.654  15.146  1.00 78.55           O  
HETATM 1318  O   HOH A 415      61.722  35.699   8.323  1.00 56.31           O  
HETATM 1319  O   HOH A 416      55.039  38.109  -5.057  1.00 54.87           O  
HETATM 1320  O   HOH A 420      32.471  51.375   3.674  1.00 42.82           O  
HETATM 1321  O   HOH A 425      43.567  50.282  29.405  1.00 24.58           O  
HETATM 1322  O   HOH A 426      32.315  35.347  17.339  1.00 19.21           O  
HETATM 1323  O   HOH A 427      40.309  53.869  30.211  1.00 42.49           O  
HETATM 1324  O   HOH A 430      25.098  42.371  15.777  1.00 68.93           O  
HETATM 1325  O   HOH A 431      28.639  41.261   4.894  1.00 27.15           O  
HETATM 1326  O   HOH A 432      36.253  54.066  17.647  1.00 38.97           O  
HETATM 1327  O   HOH A 433      27.987  48.743   4.275  1.00 70.30           O  
HETATM 1328  O   HOH A 436      30.501  43.587  30.346  1.00 40.27           O  
HETATM 1329  O   HOH A 437      28.084  44.637  31.220  1.00 46.62           O  
HETATM 1330  O   HOH A 438      68.411 -27.830  -8.903  1.00 44.67           O  
HETATM 1331  O   HOH A 440      33.338  30.325  11.028  1.00 45.79           O  
HETATM 1332  O   HOH A 503      49.383  13.151  13.138  1.00 40.70           O  
HETATM 1333  O   HOH A 508      42.949  57.395  22.584  1.00 93.22           O  
HETATM 1334  O   HOH A 509      50.591  51.424   1.600  1.00 22.94           O  
HETATM 1335  O   HOH A 510      60.866  41.535   5.755  1.00 77.59           O  
HETATM 1336  O   HOH A 513      42.997  42.774   3.041  1.00 47.33           O  
HETATM 1337  O   HOH A 514      48.289  33.058  -4.079  1.00 52.44           O  
HETATM 1338  O   HOH A 515      56.810  30.048  -3.589  1.00 36.96           O  
HETATM 1339  O   HOH A 517      34.264  48.866   3.680  1.00 50.29           O  
HETATM 1340  O   HOH A 518      27.474  50.011   6.859  1.00 60.66           O  
HETATM 1341  O   HOH A 522      35.268  35.904  -5.382  1.00 40.59           O  
HETATM 1342  O   HOH A 602      61.937 -13.049  -5.522  1.00 36.37           O  
HETATM 1343  O   HOH A 603      62.800 -10.643  -0.955  1.00 47.53           O  
HETATM 1344  O   HOH A 604      43.329   8.838   1.075  1.00 51.34           O  
HETATM 1345  O   HOH A 605      43.347  12.976   0.880  1.00 74.52           O  
HETATM 1346  O   HOH A 606      46.199  31.835  17.397  1.00 47.42           O  
HETATM 1347  O   HOH A 608      53.602  51.564  23.811  1.00 44.71           O  
HETATM 1348  O   HOH A 609      37.587  20.663   1.390  1.00 46.11           O  
HETATM 1349  O   HOH A 610      27.693  39.203  19.496  1.00 52.77           O  
HETATM 1350  O   HOH A 701      52.471 -15.901   4.805  1.00 59.28           O  
HETATM 1351  O   HOH A 702      45.386  37.458  18.179  1.00 48.81           O  
HETATM 1352  O   HOH A 801      57.913 -19.879   7.471  1.00 29.72           O  
HETATM 1353  O   HOH A 802      50.326  10.572  17.085  1.00 55.12           O  
HETATM 1354  O   HOH A 803      48.321  20.783  14.455  1.00 59.76           O  
HETATM 1355  O   HOH A 804      48.229  16.558  17.893  1.00 74.17           O  
HETATM 1356  O   HOH A 805      45.575  13.038  -1.694  1.00 48.14           O  
HETATM 1357  O   HOH A 806      32.447  50.476  26.850  1.00 56.74           O  
HETATM 1358  O   HOH A 807      31.437  43.765  13.676  1.00 41.19           O  
HETATM 1359  O   HOH A 808      25.119  39.290  17.322  1.00 54.63           O  
HETATM 1360  O   HOH A 809      36.993  54.460   7.899  1.00 53.79           O  
HETATM 1361  O   HOH A 810      52.180  56.906  12.229  1.00 80.95           O  
HETATM 1362  O   HOH A 811      32.969  55.300  12.333  1.00 70.21           O  
HETATM 1363  O   HOH A 812      34.241  34.786  19.293  1.00 30.03           O  
HETATM 1364  O   HOH A 813      57.073  32.573  -4.804  1.00 63.64           O  
HETATM 1365  O   HOH A 814      42.825  27.373  23.065  1.00 53.81           O  
HETATM 1366  O   HOH A 815      50.300  31.142  14.705  1.00 63.53           O  
HETATM 1367  O   HOH A 816      64.532  30.648   4.913  1.00 54.12           O  
HETATM 1368  O   HOH A 817      61.352  36.931   5.849  1.00 75.13           O  
HETATM 1369  O   HOH A 818      46.040  49.953   0.095  1.00 71.19           O  
HETATM 1370  O   HOH A 819      51.396  54.140   0.783  1.00 69.12           O  
HETATM 1371  O   HOH A 820      38.464  31.971  18.219  1.00 51.94           O  
HETATM 1372  O   HOH A 821      34.184  29.939  18.638  1.00 68.50           O  
HETATM 1373  O   HOH A 822      44.161  19.660   4.350  1.00 46.53           O  
HETATM 1374  O   HOH A 823      39.348  16.012   6.541  1.00 88.54           O  
CONECT    3   12                                                                
CONECT   12    3                                                                
CONECT  413 1235                                                                
CONECT  485 1210                                                                
CONECT  924 1147                                                                
CONECT 1147  924                                                                
CONECT 1210  485 1211 1221                                                      
CONECT 1211 1210 1212 1218                                                      
CONECT 1212 1211 1213 1219                                                      
CONECT 1213 1212 1214 1220                                                      
CONECT 1214 1213 1215 1221                                                      
CONECT 1215 1214 1222                                                           
CONECT 1216 1217 1218 1223                                                      
CONECT 1217 1216                                                                
CONECT 1218 1211 1216                                                           
CONECT 1219 1212 1224                                                           
CONECT 1220 1213                                                                
CONECT 1221 1210 1214                                                           
CONECT 1222 1215                                                                
CONECT 1223 1216                                                                
CONECT 1224 1219 1225 1233                                                      
CONECT 1225 1224 1226 1230                                                      
CONECT 1226 1225 1227 1231                                                      
CONECT 1227 1226 1228 1232                                                      
CONECT 1228 1227 1229 1233                                                      
CONECT 1229 1228 1234                                                           
CONECT 1230 1225                                                                
CONECT 1231 1226                                                                
CONECT 1232 1227                                                                
CONECT 1233 1224 1228                                                           
CONECT 1234 1229                                                                
CONECT 1235  413 1261 1273                                                      
CONECT 1236 1237 1238                                                           
CONECT 1237 1236                                                                
CONECT 1238 1236 1239 1240                                                      
CONECT 1239 1238                                                                
CONECT 1240 1238 1241 1242                                                      
CONECT 1241 1240                                                                
CONECT 1242 1240 1243                                                           
CONECT 1243 1242 1244                                                           
CONECT 1244 1243 1245                                                           
CONECT 1245 1244                                                                
CONECT 1261 1235                                                                
CONECT 1273 1235                                                                
MASTER      355    0    4    5    6    0    0    6 1373    1   44   13          
END                                                                             
