CNRS Nantes University UFIP UFIP
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***  LYASE 17-OCT-06 2ISB  ***

elNémo ID: 22100401432988904

Job options:

ID        	=	 22100401432988904
JOBID     	=	 LYASE 17-OCT-06 2ISB
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    LYASE                                   17-OCT-06   2ISB              
TITLE     CRYSTAL STRUCTURE OF FUMARASE OF FUM-1 (NP_069927.1) FROM             
TITLE    2 ARCHAEOGLOBUS FULGIDUS AT 1.66 A RESOLUTION                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FUMARASE;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FUM-1;                                                      
COMPND   5 EC: 4.2.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 GENE: FUM-1;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    NP_069927.1, FUMARASE OF FUM-1, STRUCTURAL GENOMICS, PSI-2, PROTEIN   
KEYWDS   2 STRUCTURE INITIATIVE, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,    
KEYWDS   3 LYASE                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   4   18-OCT-17 2ISB    1       REMARK                                   
REVDAT   3   13-JUL-11 2ISB    1       VERSN                                    
REVDAT   2   24-FEB-09 2ISB    1       VERSN                                    
REVDAT   1   28-NOV-06 2ISB    0                                                
SPRSDE     28-NOV-06 2ISB      1VPJ                                             
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF FUMARASE OF FUM-1 (NP_069927.1) FROM    
JRNL        TITL 2 ARCHAEOGLOBUS FULGIDUS AT 1.66 A RESOLUTION                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25585                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1256                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.66                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1447                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1399                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 182                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 19.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.72000                                              
REMARK   3    B22 (A**2) : 0.72000                                              
REMARK   3    B33 (A**2) : -1.43000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.090         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.056         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.292         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1510 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1035 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2069 ; 1.501 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2538 ; 0.941 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   213 ; 6.332 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    56 ;35.554 ;23.036       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   262 ;12.611 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;13.826 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   235 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1709 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   312 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   258 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1092 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   726 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   814 ; 0.088 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   118 ; 0.146 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.157 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    12 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.096 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   988 ; 2.226 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   393 ; 0.505 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1553 ; 2.835 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   608 ; 4.953 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   500 ; 6.889 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -3        A   180                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8297  28.2611  12.9866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0226 T22:  -0.0657                                     
REMARK   3      T33:  -0.0390 T12:   0.0142                                     
REMARK   3      T13:  -0.0086 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8986 L22:   0.7952                                     
REMARK   3      L33:   1.4651 L12:   0.0358                                     
REMARK   3      L13:   0.3968 L23:  -0.0901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0216 S12:  -0.0074 S13:  -0.0807                       
REMARK   3      S21:   0.0546 S22:  -0.0006 S23:  -0.0205                       
REMARK   3      S31:   0.1782 S32:   0.0415 S33:  -0.0210                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                
REMARK   3   2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY                    
REMARK   3   3. DENSITY IS WEAK FOR THE FOLLOWING REGIONS: A-3 - 1,             
REMARK   3   A70 - 73.                                                          
REMARK   4                                                                      
REMARK   4 2ISB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000039954.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000, 0.97966, 0.97950          
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25660                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.660                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 21.152                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200   FOR THE DATA SET  : 5.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.66400                            
REMARK 200   FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELX, SHELXD, AUTOSHARP                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LI ACETATE, 20.0% PEG-3350, NO      
REMARK 280  BUFFER, PH 7.8, VAPOR DIFFUSION, SITTING DROP, NANODROP,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.87800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       25.83200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       25.83200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      118.31700            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       25.83200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       25.83200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.43900            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       25.83200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       25.83200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      118.31700            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       25.83200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       25.83200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       39.43900            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       78.87800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT                      
REMARK 300 SCATTERING SUPPORTS THE ASSIGNMENT OF A MONOMER                      
REMARK 300 AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.                 
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     LYS A    -7                                                      
REMARK 465     ILE A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  -3    ND1  CD2  CE1  NE2                                  
REMARK 470     HIS A  -1    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MSE A   1   SE    CE                                             
REMARK 470     LYS A  20    CE   NZ                                             
REMARK 470     LYS A  70    CE   NZ                                             
REMARK 470     ASN A  71    CG   OD1  ND2                                       
REMARK 470     ASP A  72    CG   OD1  OD2                                       
REMARK 470     GLU A  73    CD   OE1  OE2                                       
REMARK 470     LYS A  97    CE   NZ                                             
REMARK 470     LYS A 142    CD   CE   NZ                                        
REMARK 470     GLU A 159    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 180    CD   NE   CZ   NH1  NH2                             
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    ARG A  35     -137.85   -132.25                                   
REMARK 500    ARG A  35     -144.59   -125.76                                   
REMARK 500    HIS A  63       95.21    -67.67                                   
REMARK 500    ASN A  71     -118.27   -100.43                                   
REMARK 500    LYS A 120      -22.99   -146.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 356698   RELATED DB: TARGETDB                            
DBREF  2ISB A    1   180  UNP    O29167   O29167_ARCFU     1    180             
SEQADV 2ISB MSE A  -11  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB GLY A  -10  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB SER A   -9  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB ASP A   -8  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB LYS A   -7  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB ILE A   -6  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB HIS A   -5  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB HIS A   -4  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB HIS A   -3  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB HIS A   -2  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB HIS A   -1  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB HIS A    0  UNP  O29167              LEADER SEQUENCE                
SEQADV 2ISB MSE A    1  UNP  O29167    MET     1 MODIFIED RESIDUE               
SEQADV 2ISB MSE A    3  UNP  O29167    MET     3 MODIFIED RESIDUE               
SEQADV 2ISB MSE A   46  UNP  O29167    MET    46 MODIFIED RESIDUE               
SEQADV 2ISB MSE A   87  UNP  O29167    MET    87 MODIFIED RESIDUE               
SEQADV 2ISB MSE A  101  UNP  O29167    MET   101 MODIFIED RESIDUE               
SEQADV 2ISB MSE A  109  UNP  O29167    MET   109 MODIFIED RESIDUE               
SEQADV 2ISB MSE A  117  UNP  O29167    MET   117 MODIFIED RESIDUE               
SEQADV 2ISB MSE A  136  UNP  O29167    MET   136 MODIFIED RESIDUE               
SEQADV 2ISB MSE A  151  UNP  O29167    MET   151 MODIFIED RESIDUE               
SEQRES   1 A  192  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 A  192  VAL MSE GLU TYR GLU LEU ARG THR PRO LEU VAL LYS ASP          
SEQRES   3 A  192  GLN ILE LEU LYS LEU LYS VAL GLY ASP VAL VAL TYR ILE          
SEQRES   4 A  192  THR GLY GLU ILE PHE THR ALA ARG ASP GLU ALA HIS ALA          
SEQRES   5 A  192  ARG ALA LEU GLU TRP MSE GLU GLU GLY LYS GLU LEU PRO          
SEQRES   6 A  192  PHE SER PHE ASP LYS GLY VAL VAL TYR HIS CYS GLY PRO          
SEQRES   7 A  192  LEU VAL LYS LYS ASN ASP GLU TRP ARG VAL VAL SER ALA          
SEQRES   8 A  192  GLY PRO THR THR SER ALA ARG MSE ASN PRO PHE THR PRO          
SEQRES   9 A  192  LYS ILE LEU GLU LYS VAL GLU CYS MSE GLY ILE ILE GLY          
SEQRES  10 A  192  LYS GLY GLY MSE SER GLU GLU VAL VAL GLU ALA MSE ARG          
SEQRES  11 A  192  GLY LYS ALA ALA TYR PHE ALA PHE THR GLY GLY ALA GLY          
SEQRES  12 A  192  ALA LEU ALA ALA MSE SER ILE LYS LYS VAL LYS GLY VAL          
SEQRES  13 A  192  VAL TRP GLU ASP LEU GLY MSE PRO GLU ALA VAL TRP LEU          
SEQRES  14 A  192  LEU GLU VAL GLU ARG PHE GLY PRO CYS ILE VAL ALA ILE          
SEQRES  15 A  192  ASP ALA HIS GLY ASN SER LEU TYR ARG ARG                      
MODRES 2ISB MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A    3  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A   46  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A   87  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A  101  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A  109  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A  117  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A  136  MET  SELENOMETHIONINE                                   
MODRES 2ISB MSE A  151  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       6                                                       
HET    MSE  A   3       8                                                       
HET    MSE  A  46       8                                                       
HET    MSE  A  87       8                                                       
HET    MSE  A 101       8                                                       
HET    MSE  A 109       8                                                       
HET    MSE  A 117       8                                                       
HET    MSE  A 136      13                                                       
HET    MSE  A 151       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    9(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *182(H2 O)                                                    
HELIX    1   1 VAL A   12  LEU A   19  1                                   8    
HELIX    2   2 ARG A   35  GLY A   49  1                                  15    
HELIX    3   3 THR A   83  ASN A   88  5                                   6    
HELIX    4   4 PHE A   90  VAL A   98  1                                   9    
HELIX    5   5 SER A  110  ARG A  118  1                                   9    
HELIX    6   6 LEU A  133  MSE A  136  5                                   4    
HELIX    7   7 TRP A  146  GLY A  150  5                                   5    
SHEET    1   A 7 GLU A   4  ARG A   8  0                                        
SHEET    2   A 7 VAL A  24  THR A  33  1  O  TYR A  26   N  LEU A   7           
SHEET    3   A 7 VAL A  60  TYR A  62  1  O  TYR A  62   N  PHE A  32           
SHEET    4   A 7 MSE A 101  GLY A 105  1  O  ILE A 104   N  VAL A  61           
SHEET    5   A 7 ALA A 121  PHE A 126  1  O  PHE A 124   N  ILE A 103           
SHEET    6   A 7 VAL A 155  ILE A 170 -1  O  ILE A 167   N  ALA A 125           
SHEET    7   A 7 ILE A 138  VAL A 145 -1  N  LYS A 140   O  GLU A 159           
SHEET    1   B 4 GLU A   4  ARG A   8  0                                        
SHEET    2   B 4 VAL A  24  THR A  33  1  O  TYR A  26   N  LEU A   7           
SHEET    3   B 4 VAL A 155  ILE A 170 -1  O  VAL A 160   N  GLY A  29           
SHEET    4   B 4 ILE A 138  VAL A 145 -1  N  LYS A 140   O  GLU A 159           
SHEET    1   C 2 LEU A  67  LYS A  70  0                                        
SHEET    2   C 2 TRP A  74  SER A  78 -1  O  VAL A  77   N  LEU A  67           
LINK         C   HIS A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   VAL A   2     1555   1555  1.33  
LINK         C   VAL A   2                 N   MSE A   3     1555   1555  1.32  
LINK         C   MSE A   3                 N   GLU A   4     1555   1555  1.33  
LINK         C   TRP A  45                 N   MSE A  46     1555   1555  1.32  
LINK         C   MSE A  46                 N   GLU A  47     1555   1555  1.33  
LINK         C   ARG A  86                 N   MSE A  87     1555   1555  1.34  
LINK         C   MSE A  87                 N   ASN A  88     1555   1555  1.34  
LINK         C   CYS A 100                 N   MSE A 101     1555   1555  1.32  
LINK         C   MSE A 101                 N   GLY A 102     1555   1555  1.33  
LINK         C   GLY A 108                 N   MSE A 109     1555   1555  1.33  
LINK         C   MSE A 109                 N   SER A 110     1555   1555  1.32  
LINK         C   ALA A 116                 N   MSE A 117     1555   1555  1.34  
LINK         C   MSE A 117                 N   ARG A 118     1555   1555  1.34  
LINK         C   ALA A 135                 N   MSE A 136     1555   1555  1.33  
LINK         C   MSE A 136                 N   SER A 137     1555   1555  1.34  
LINK         C   GLY A 150                 N   MSE A 151     1555   1555  1.33  
LINK         C   MSE A 151                 N   PRO A 152     1555   1555  1.34  
CISPEP   1 THR A    9    PRO A   10          0        -4.50                     
CISPEP   2 GLY A  164    PRO A  165          0         1.02                     
CRYST1   51.664   51.664  157.756  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019360  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019360  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006340        0.00000                         
ATOM      1  N   HIS A  -3      30.322  18.948 -19.166  1.00 52.09           N  
ATOM      2  CA  HIS A  -3      28.936  18.668 -18.683  1.00 51.35           C  
ATOM      3  C   HIS A  -3      28.875  18.507 -17.157  1.00 51.01           C  
ATOM      4  O   HIS A  -3      27.794  18.596 -16.570  1.00 50.15           O  
ATOM      5  CB  HIS A  -3      28.361  17.433 -19.384  1.00 51.03           C  
ATOM      6  CG  HIS A  -3      28.242  17.583 -20.869  1.00 49.72           C  
ATOM      7  N   HIS A  -2      30.024  18.288 -16.515  1.00 51.42           N  
ATOM      8  CA  HIS A  -2      30.082  18.279 -15.047  1.00 51.53           C  
ATOM      9  C   HIS A  -2      30.087  19.716 -14.506  1.00 50.16           C  
ATOM     10  O   HIS A  -2      31.127  20.396 -14.511  1.00 48.71           O  
ATOM     11  CB  HIS A  -2      31.300  17.502 -14.535  1.00 52.43           C  
ATOM     12  CG  HIS A  -2      31.237  16.034 -14.822  1.00 56.85           C  
ATOM     13  ND1 HIS A  -2      32.175  15.386 -15.597  1.00 62.94           N  
ATOM     14  CD2 HIS A  -2      30.337  15.092 -14.454  1.00 60.78           C  
ATOM     15  CE1 HIS A  -2      31.861  14.105 -15.685  1.00 61.59           C  
ATOM     16  NE2 HIS A  -2      30.750  13.900 -15.001  1.00 61.75           N  
ATOM     17  N   HIS A  -1      28.914  20.167 -14.055  1.00 48.27           N  
ATOM     18  CA  HIS A  -1      28.735  21.533 -13.541  1.00 47.07           C  
ATOM     19  C   HIS A  -1      29.487  21.682 -12.222  1.00 45.13           C  
ATOM     20  O   HIS A  -1      29.576  20.723 -11.449  1.00 42.77           O  
ATOM     21  CB  HIS A  -1      27.242  21.852 -13.346  1.00 46.45           C  
ATOM     22  N   HIS A   0      30.051  22.869 -11.984  1.00 42.83           N  
ATOM     23  CA  HIS A   0      30.699  23.147 -10.705  1.00 42.02           C  
ATOM     24  C   HIS A   0      29.597  23.293  -9.644  1.00 41.22           C  
ATOM     25  O   HIS A   0      28.555  23.948  -9.860  1.00 39.19           O  
ATOM     26  CB  HIS A   0      31.596  24.393 -10.776  1.00 42.41           C  
ATOM     27  CG  HIS A   0      32.460  24.597  -9.567  1.00 44.01           C  
ATOM     28  ND1 HIS A   0      33.827  24.420  -9.590  1.00 44.77           N  
ATOM     29  CD2 HIS A   0      32.153  24.984  -8.303  1.00 46.94           C  
ATOM     30  CE1 HIS A   0      34.325  24.681  -8.392  1.00 50.30           C  
ATOM     31  NE2 HIS A   0      33.329  25.017  -7.590  1.00 45.72           N  
HETATM   32  N   MSE A   1      29.796  22.612  -8.523  1.00 39.60           N  
HETATM   33  CA  MSE A   1      28.819  22.631  -7.446  1.00 39.06           C  
HETATM   34  C   MSE A   1      29.541  23.126  -6.211  1.00 36.29           C  
HETATM   35  O   MSE A   1      30.772  22.969  -6.077  1.00 34.10           O  
HETATM   36  CB  MSE A   1      28.207  21.236  -7.203  1.00 39.55           C  
HETATM   37  CG  MSE A   1      27.288  20.710  -8.340  1.00 39.26           C  
ATOM     38  N   VAL A   2      28.769  23.740  -5.321  1.00 33.08           N  
ATOM     39  CA  VAL A   2      29.267  24.097  -4.013  1.00 28.41           C  
ATOM     40  C   VAL A   2      29.173  22.886  -3.089  1.00 25.73           C  
ATOM     41  O   VAL A   2      28.099  22.398  -2.811  1.00 27.57           O  
ATOM     42  CB  VAL A   2      28.487  25.244  -3.409  1.00 27.64           C  
ATOM     43  CG1 VAL A   2      29.111  25.601  -2.095  1.00 23.15           C  
ATOM     44  CG2 VAL A   2      28.493  26.430  -4.373  1.00 27.41           C  
HETATM   45  N   MSE A   3      30.310  22.407  -2.613  1.00 24.99           N  
HETATM   46  CA  MSE A   3      30.308  21.263  -1.717  1.00 25.74           C  
HETATM   47  C   MSE A   3      30.213  21.823  -0.317  1.00 24.73           C  
HETATM   48  O   MSE A   3      30.702  22.909  -0.073  1.00 21.97           O  
HETATM   49  CB  MSE A   3      31.610  20.481  -1.842  1.00 28.80           C  
HETATM   50  CG  MSE A   3      31.868  19.904  -3.195  1.00 33.90           C  
HETATM   51 SE   MSE A   3      30.463  18.595  -3.644  1.00 50.49          SE  
HETATM   52  CE  MSE A   3      30.428  17.468  -1.947  1.00 45.00           C  
ATOM     53  N   GLU A   4      29.572  21.074   0.577  1.00 23.48           N  
ATOM     54  CA  GLU A   4      29.494  21.416   1.984  1.00 23.10           C  
ATOM     55  C   GLU A   4      30.120  20.273   2.733  1.00 20.90           C  
ATOM     56  O   GLU A   4      29.807  19.115   2.463  1.00 20.55           O  
ATOM     57  CB  GLU A   4      28.053  21.594   2.432  1.00 24.89           C  
ATOM     58  CG  GLU A   4      27.945  21.868   3.918  1.00 30.62           C  
ATOM     59  CD  GLU A   4      26.522  22.133   4.386  1.00 33.26           C  
ATOM     60  OE1 GLU A   4      25.874  23.061   3.833  1.00 42.55           O  
ATOM     61  OE2 GLU A   4      26.070  21.419   5.322  1.00 37.86           O  
ATOM     62  N   TYR A   5      31.017  20.587   3.648  1.00 17.75           N  
ATOM     63  CA  TYR A   5      31.699  19.559   4.435  1.00 19.34           C  
ATOM     64  C   TYR A   5      31.509  19.868   5.897  1.00 21.17           C  
ATOM     65  O   TYR A   5      31.635  21.020   6.318  1.00 19.08           O  
ATOM     66  CB  TYR A   5      33.204  19.539   4.158  1.00 20.06           C  
ATOM     67  CG  TYR A   5      33.539  19.211   2.726  1.00 21.72           C  
ATOM     68  CD1 TYR A   5      33.488  17.905   2.263  1.00 26.51           C  
ATOM     69  CD2 TYR A   5      33.872  20.210   1.830  1.00 18.89           C  
ATOM     70  CE1 TYR A   5      33.781  17.597   0.938  1.00 25.17           C  
ATOM     71  CE2 TYR A   5      34.164  19.924   0.500  1.00 19.04           C  
ATOM     72  CZ  TYR A   5      34.144  18.607   0.064  1.00 19.83           C  
ATOM     73  OH  TYR A   5      34.412  18.288  -1.256  1.00 25.50           O  
ATOM     74  N   GLU A   6      31.207  18.846   6.679  1.00 18.42           N  
ATOM     75  CA  GLU A   6      31.405  18.926   8.124  1.00 19.53           C  
ATOM     76  C   GLU A   6      32.759  18.283   8.437  1.00 20.77           C  
ATOM     77  O   GLU A   6      32.884  17.067   8.465  1.00 19.22           O  
ATOM     78  CB  GLU A   6      30.279  18.254   8.895  1.00 18.35           C  
ATOM     79  CG  GLU A   6      30.356  18.481  10.412  1.00 22.11           C  
ATOM     80  CD  GLU A   6      29.155  17.900  11.175  1.00 22.79           C  
ATOM     81  OE1 GLU A   6      28.088  17.710  10.543  1.00 24.91           O  
ATOM     82  OE2 GLU A   6      29.285  17.644  12.406  1.00 22.29           O  
ATOM     83  N   LEU A   7      33.780  19.112   8.606  1.00 18.00           N  
ATOM     84  CA  LEU A   7      35.139  18.663   8.882  1.00 17.39           C  
ATOM     85  C   LEU A   7      35.315  18.322  10.355  1.00 19.24           C  
ATOM     86  O   LEU A   7      35.088  19.153  11.237  1.00 18.96           O  
ATOM     87  CB  LEU A   7      36.155  19.743   8.540  1.00 20.03           C  
ATOM     88  CG  LEU A   7      36.307  20.192   7.119  1.00 23.10           C  
ATOM     89  CD1 LEU A   7      37.412  21.317   7.086  1.00 25.00           C  
ATOM     90  CD2 LEU A   7      36.630  19.004   6.227  1.00 27.40           C  
ATOM     91  N   ARG A   8      35.807  17.129  10.625  1.00 17.64           N  
ATOM     92  CA  ARG A   8      36.060  16.696  11.976  1.00 19.21           C  
ATOM     93  C   ARG A   8      37.528  16.820  12.326  1.00 21.40           C  
ATOM     94  O   ARG A   8      38.432  16.621  11.489  1.00 21.81           O  
ATOM     95  CB  ARG A   8      35.577  15.248  12.157  1.00 21.19           C  
ATOM     96  CG  ARG A   8      34.084  15.220  12.056  1.00 28.54           C  
ATOM     97  CD  ARG A   8      33.480  13.875  12.209  1.00 46.61           C  
ATOM     98  NE  ARG A   8      32.032  14.033  12.058  1.00 52.46           N  
ATOM     99  CZ  ARG A   8      31.178  14.240  13.060  1.00 55.05           C  
ATOM    100  NH1 ARG A   8      31.583  14.249  14.335  1.00 51.40           N  
ATOM    101  NH2 ARG A   8      29.889  14.396  12.777  1.00 58.93           N  
ATOM    102  N   THR A   9      37.776  17.202  13.565  1.00 20.08           N  
ATOM    103  CA  THR A   9      39.135  17.298  14.046  1.00 19.05           C  
ATOM    104  C   THR A   9      39.403  16.049  14.893  1.00 22.61           C  
ATOM    105  O   THR A   9      38.462  15.437  15.423  1.00 23.65           O  
ATOM    106  CB  THR A   9      39.365  18.595  14.841  1.00 20.59           C  
ATOM    107  OG1 THR A   9      38.503  18.612  15.976  1.00 24.85           O  
ATOM    108  CG2 THR A   9      39.101  19.849  13.963  1.00 20.70           C  
ATOM    109  N   PRO A  10      40.669  15.630  14.989  1.00 21.61           N  
ATOM    110  CA  PRO A  10      41.878  16.141  14.321  1.00 19.46           C  
ATOM    111  C   PRO A  10      41.738  15.983  12.823  1.00 18.75           C  
ATOM    112  O   PRO A  10      41.161  15.009  12.334  1.00 19.17           O  
ATOM    113  CB  PRO A  10      43.006  15.243  14.839  1.00 21.92           C  
ATOM    114  CG  PRO A  10      42.419  14.505  16.018  1.00 26.17           C  
ATOM    115  CD  PRO A  10      40.949  14.460  15.841  1.00 23.58           C  
ATOM    116  N   LEU A  11      42.236  16.964  12.090  1.00 17.14           N  
ATOM    117  CA  LEU A  11      42.015  16.998  10.665  1.00 16.63           C  
ATOM    118  C   LEU A  11      42.659  15.820   9.954  1.00 19.85           C  
ATOM    119  O   LEU A  11      43.742  15.338  10.350  1.00 19.66           O  
ATOM    120  CB  LEU A  11      42.545  18.297  10.066  1.00 17.66           C  
ATOM    121  CG  LEU A  11      41.875  19.555  10.559  1.00 19.25           C  
ATOM    122  CD1 LEU A  11      42.681  20.789  10.056  1.00 20.27           C  
ATOM    123  CD2 LEU A  11      40.390  19.619  10.161  1.00 18.91           C  
ATOM    124  N   VAL A  12      41.954  15.377   8.912  1.00 19.89           N  
ATOM    125  CA  VAL A  12      42.426  14.383   7.956  1.00 20.60           C  
ATOM    126  C   VAL A  12      42.975  15.140   6.738  1.00 20.30           C  
ATOM    127  O   VAL A  12      42.244  15.858   6.061  1.00 20.09           O  
ATOM    128  CB  VAL A  12      41.270  13.443   7.534  1.00 22.96           C  
ATOM    129  CG1 VAL A  12      41.754  12.416   6.503  1.00 22.98           C  
ATOM    130  CG2 VAL A  12      40.664  12.732   8.795  1.00 22.11           C  
ATOM    131  N   LYS A  13      44.270  15.002   6.491  1.00 18.35           N  
ATOM    132  CA  LYS A  13      44.920  15.769   5.427  1.00 19.62           C  
ATOM    133  C   LYS A  13      44.234  15.667   4.066  1.00 17.97           C  
ATOM    134  O   LYS A  13      44.081  16.665   3.377  1.00 17.61           O  
ATOM    135  CB  LYS A  13      46.381  15.388   5.307  1.00 17.81           C  
ATOM    136  CG  LYS A  13      47.110  16.177   4.279  1.00 20.53           C  
ATOM    137  CD  LYS A  13      48.600  16.026   4.434  1.00 28.96           C  
ATOM    138  CE  LYS A  13      49.337  16.780   3.365  1.00 31.49           C  
ATOM    139  NZ  LYS A  13      50.488  15.993   2.848  1.00 41.98           N  
ATOM    140  N   ASP A  14      43.834  14.465   3.667  1.00 18.40           N  
ATOM    141  CA  ASP A  14      43.122  14.317   2.409  1.00 21.26           C  
ATOM    142  C   ASP A  14      41.806  15.107   2.326  1.00 18.30           C  
ATOM    143  O   ASP A  14      41.375  15.476   1.240  1.00 17.75           O  
ATOM    144  CB  ASP A  14      42.845  12.844   2.143  1.00 24.37           C  
ATOM    145  CG  ASP A  14      44.109  12.068   1.762  1.00 35.65           C  
ATOM    146  OD1 ASP A  14      45.071  12.676   1.209  1.00 41.01           O  
ATOM    147  OD2 ASP A  14      44.135  10.836   2.018  1.00 52.50           O  
ATOM    148  N   GLN A  15      41.144  15.327   3.451  1.00 19.15           N  
ATOM    149  CA  GLN A  15      39.913  16.129   3.431  1.00 22.07           C  
ATOM    150  C   GLN A  15      40.232  17.619   3.217  1.00 20.79           C  
ATOM    151  O   GLN A  15      39.484  18.314   2.529  1.00 22.70           O  
ATOM    152  CB  GLN A  15      39.087  15.901   4.702  1.00 20.61           C  
ATOM    153  CG  GLN A  15      38.585  14.449   4.847  1.00 20.31           C  
ATOM    154  CD  GLN A  15      37.800  14.231   6.120  1.00 29.82           C  
ATOM    155  OE1 GLN A  15      37.470  15.187   6.834  1.00 34.46           O  
ATOM    156  NE2 GLN A  15      37.489  12.960   6.416  1.00 36.96           N  
ATOM    157  N   ILE A  16      41.336  18.106   3.786  1.00 16.12           N  
ATOM    158  CA  ILE A  16      41.824  19.457   3.507  1.00 16.06           C  
ATOM    159  C   ILE A  16      42.201  19.617   2.048  1.00 15.52           C  
ATOM    160  O   ILE A  16      41.865  20.606   1.432  1.00 15.44           O  
ATOM    161  CB  ILE A  16      43.050  19.832   4.397  1.00 15.34           C  
ATOM    162  CG1 ILE A  16      42.635  19.934   5.875  1.00 19.90           C  
ATOM    163  CG2 ILE A  16      43.689  21.154   3.917  1.00 16.74           C  
ATOM    164  CD1 ILE A  16      41.667  21.132   6.206  1.00 23.73           C  
ATOM    165  N   LEU A  17      42.889  18.629   1.476  1.00 13.79           N  
ATOM    166  CA  LEU A  17      43.311  18.738   0.072  1.00 14.12           C  
ATOM    167  C   LEU A  17      42.158  18.729  -0.914  1.00 15.82           C  
ATOM    168  O   LEU A  17      42.298  19.235  -2.008  1.00 18.49           O  
ATOM    169  CB  LEU A  17      44.295  17.631  -0.289  1.00 16.60           C  
ATOM    170  CG  LEU A  17      45.611  17.575   0.477  1.00 18.52           C  
ATOM    171  CD1 LEU A  17      46.497  16.424  -0.010  1.00 21.42           C  
ATOM    172  CD2 LEU A  17      46.323  18.896   0.382  1.00 23.98           C  
ATOM    173  N   LYS A  18      41.052  18.094  -0.537  1.00 15.00           N  
ATOM    174  CA  LYS A  18      39.847  18.041  -1.375  1.00 17.58           C  
ATOM    175  C   LYS A  18      39.089  19.367  -1.460  1.00 17.49           C  
ATOM    176  O   LYS A  18      38.327  19.563  -2.398  1.00 15.82           O  
ATOM    177  CB  LYS A  18      38.929  16.962  -0.802  1.00 17.30           C  
ATOM    178  CG  LYS A  18      37.543  16.854  -1.375  1.00 29.81           C  
ATOM    179  CD  LYS A  18      36.912  15.429  -1.132  1.00 30.10           C  
ATOM    180  CE  LYS A  18      37.226  14.792   0.246  1.00 40.58           C  
ATOM    181  NZ  LYS A  18      36.340  15.204   1.381  1.00 43.34           N  
ATOM    182  N   LEU A  19      39.329  20.276  -0.522  1.00 15.72           N  
ATOM    183  CA  LEU A  19      38.628  21.560  -0.475  1.00 15.60           C  
ATOM    184  C   LEU A  19      38.982  22.447  -1.658  1.00 15.57           C  
ATOM    185  O   LEU A  19      40.120  22.430  -2.128  1.00 17.77           O  
ATOM    186  CB  LEU A  19      38.949  22.314   0.804  1.00 14.72           C  
ATOM    187  CG  LEU A  19      38.606  21.603   2.103  1.00 14.72           C  
ATOM    188  CD1 LEU A  19      39.096  22.328   3.367  1.00 14.66           C  
ATOM    189  CD2 LEU A  19      37.105  21.285   2.166  1.00 15.59           C  
ATOM    190  N   LYS A  20      37.979  23.196  -2.124  1.00 17.85           N  
ATOM    191  CA  LYS A  20      38.129  24.183  -3.200  1.00 18.14           C  
ATOM    192  C   LYS A  20      37.647  25.524  -2.664  1.00 16.96           C  
ATOM    193  O   LYS A  20      36.790  25.565  -1.812  1.00 14.55           O  
ATOM    194  CB  LYS A  20      37.250  23.819  -4.413  1.00 18.49           C  
ATOM    195  CG  LYS A  20      37.619  22.590  -5.144  1.00 25.04           C  
ATOM    196  CD  LYS A  20      36.564  22.336  -6.209  1.00 32.02           C  
ATOM    197  N   VAL A  21      38.188  26.616  -3.186  1.00 16.47           N  
ATOM    198  CA AVAL A  21      37.726  27.915  -2.754  0.50 14.92           C  
ATOM    199  CA BVAL A  21      37.721  27.949  -2.803  0.50 15.69           C  
ATOM    200  C   VAL A  21      36.217  28.019  -3.128  1.00 15.65           C  
ATOM    201  O   VAL A  21      35.783  27.598  -4.237  1.00 16.04           O  
ATOM    202  CB AVAL A  21      38.617  29.033  -3.330  0.50 15.66           C  
ATOM    203  CB BVAL A  21      38.462  29.078  -3.568  0.50 16.63           C  
ATOM    204  CG1AVAL A  21      37.907  30.334  -3.281  0.50 13.65           C  
ATOM    205  CG1BVAL A  21      39.968  29.084  -3.257  0.50 12.25           C  
ATOM    206  CG2AVAL A  21      39.940  29.117  -2.538  0.50  9.44           C  
ATOM    207  CG2BVAL A  21      38.212  28.948  -5.049  0.50 19.03           C  
ATOM    208  N   GLY A  22      35.423  28.535  -2.203  1.00 15.24           N  
ATOM    209  CA  GLY A  22      33.988  28.679  -2.350  1.00 17.83           C  
ATOM    210  C   GLY A  22      33.187  27.552  -1.724  1.00 18.12           C  
ATOM    211  O   GLY A  22      31.946  27.637  -1.618  1.00 17.98           O  
ATOM    212  N   ASP A  23      33.850  26.476  -1.305  1.00 14.75           N  
ATOM    213  CA  ASP A  23      33.140  25.430  -0.577  1.00 15.27           C  
ATOM    214  C   ASP A  23      32.726  25.932   0.811  1.00 17.30           C  
ATOM    215  O   ASP A  23      33.361  26.807   1.386  1.00 16.32           O  
ATOM    216  CB  ASP A  23      34.024  24.174  -0.405  1.00 13.20           C  
ATOM    217  CG  ASP A  23      34.237  23.381  -1.702  1.00 21.70           C  
ATOM    218  OD1 ASP A  23      33.507  23.559  -2.724  1.00 21.84           O  
ATOM    219  OD2 ASP A  23      35.168  22.535  -1.664  1.00 22.18           O  
ATOM    220  N   VAL A  24      31.648  25.345   1.325  1.00 16.70           N  
ATOM    221  CA  VAL A  24      31.107  25.635   2.654  1.00 16.12           C  
ATOM    222  C   VAL A  24      31.624  24.604   3.665  1.00 17.86           C  
ATOM    223  O   VAL A  24      31.578  23.403   3.423  1.00 17.41           O  
ATOM    224  CB  VAL A  24      29.562  25.603   2.677  1.00 18.90           C  
ATOM    225  CG1 VAL A  24      29.069  25.896   4.105  1.00 19.37           C  
ATOM    226  CG2 VAL A  24      28.993  26.618   1.691  1.00 18.83           C  
ATOM    227  N   VAL A  25      32.111  25.087   4.805  1.00 17.43           N  
ATOM    228  CA  VAL A  25      32.695  24.202   5.817  1.00 15.23           C  
ATOM    229  C   VAL A  25      32.075  24.538   7.167  1.00 16.87           C  
ATOM    230  O   VAL A  25      31.940  25.715   7.539  1.00 16.84           O  
ATOM    231  CB  VAL A  25      34.248  24.339   5.850  1.00 19.87           C  
ATOM    232  CG1 VAL A  25      34.862  23.841   7.138  1.00 26.26           C  
ATOM    233  CG2 VAL A  25      34.835  23.597   4.645  1.00 21.50           C  
ATOM    234  N   TYR A  26      31.719  23.483   7.886  1.00 16.03           N  
ATOM    235  CA  TYR A  26      31.461  23.535   9.316  1.00 16.24           C  
ATOM    236  C   TYR A  26      32.488  22.662  10.025  1.00 17.37           C  
ATOM    237  O   TYR A  26      32.946  21.658   9.458  1.00 18.63           O  
ATOM    238  CB  TYR A  26      30.085  23.017   9.625  1.00 14.66           C  
ATOM    239  CG  TYR A  26      28.975  23.830   9.086  1.00 16.80           C  
ATOM    240  CD1 TYR A  26      28.556  23.679   7.772  1.00 19.86           C  
ATOM    241  CD2 TYR A  26      28.329  24.745   9.883  1.00 17.65           C  
ATOM    242  CE1 TYR A  26      27.525  24.419   7.272  1.00 18.98           C  
ATOM    243  CE2 TYR A  26      27.263  25.498   9.379  1.00 18.63           C  
ATOM    244  CZ  TYR A  26      26.876  25.332   8.078  1.00 20.12           C  
ATOM    245  OH  TYR A  26      25.825  26.079   7.566  1.00 23.89           O  
ATOM    246  N   ILE A  27      32.866  23.029  11.248  1.00 16.82           N  
ATOM    247  CA  ILE A  27      33.878  22.277  12.008  1.00 15.89           C  
ATOM    248  C   ILE A  27      33.215  21.597  13.203  1.00 19.52           C  
ATOM    249  O   ILE A  27      32.436  22.226  13.924  1.00 16.59           O  
ATOM    250  CB  ILE A  27      35.033  23.168  12.550  1.00 18.50           C  
ATOM    251  CG1 ILE A  27      35.649  24.027  11.431  1.00 23.88           C  
ATOM    252  CG2 ILE A  27      36.091  22.329  13.234  1.00 19.46           C  
ATOM    253  CD1 ILE A  27      36.296  23.204  10.365  1.00 23.54           C  
ATOM    254  N   THR A  28      33.535  20.325  13.419  1.00 17.17           N  
ATOM    255  CA  THR A  28      33.067  19.590  14.584  1.00 17.10           C  
ATOM    256  C   THR A  28      34.261  18.888  15.238  1.00 19.34           C  
ATOM    257  O   THR A  28      35.039  18.194  14.587  1.00 22.02           O  
ATOM    258  CB  THR A  28      32.001  18.579  14.164  1.00 17.80           C  
ATOM    259  OG1 THR A  28      30.837  19.295  13.736  1.00 17.90           O  
ATOM    260  CG2 THR A  28      31.661  17.608  15.320  1.00 19.45           C  
ATOM    261  N   GLY A  29      34.409  19.087  16.533  1.00 18.45           N  
ATOM    262  CA  GLY A  29      35.526  18.565  17.283  1.00 18.16           C  
ATOM    263  C   GLY A  29      36.141  19.684  18.092  1.00 21.15           C  
ATOM    264  O   GLY A  29      35.444  20.558  18.589  1.00 26.24           O  
ATOM    265  N   GLU A  30      37.452  19.699  18.214  1.00 24.09           N  
ATOM    266  CA  GLU A  30      38.128  20.723  19.010  1.00 24.62           C  
ATOM    267  C   GLU A  30      38.650  21.807  18.095  1.00 23.75           C  
ATOM    268  O   GLU A  30      39.074  21.520  16.977  1.00 22.24           O  
ATOM    269  CB  GLU A  30      39.301  20.116  19.763  1.00 25.69           C  
ATOM    270  CG  GLU A  30      38.932  19.113  20.791  1.00 37.86           C  
ATOM    271  CD  GLU A  30      40.141  18.696  21.616  1.00 52.15           C  
ATOM    272  OE1 GLU A  30      41.290  18.908  21.130  1.00 60.18           O  
ATOM    273  OE2 GLU A  30      39.939  18.167  22.738  1.00 60.41           O  
ATOM    274  N   ILE A  31      38.582  23.055  18.550  1.00 20.30           N  
ATOM    275  CA  ILE A  31      39.292  24.156  17.913  1.00 19.02           C  
ATOM    276  C   ILE A  31      39.933  24.948  19.044  1.00 18.83           C  
ATOM    277  O   ILE A  31      39.571  24.758  20.220  1.00 19.34           O  
ATOM    278  CB  ILE A  31      38.389  25.059  17.075  1.00 19.98           C  
ATOM    279  CG1 ILE A  31      37.387  25.855  17.906  1.00 20.33           C  
ATOM    280  CG2 ILE A  31      37.632  24.235  16.007  1.00 20.54           C  
ATOM    281  CD1 ILE A  31      36.625  26.871  17.122  1.00 23.60           C  
ATOM    282  N   PHE A  32      40.897  25.774  18.709  1.00 18.19           N  
ATOM    283  CA  PHE A  32      41.403  26.687  19.710  1.00 15.09           C  
ATOM    284  C   PHE A  32      41.570  28.074  19.176  1.00 14.97           C  
ATOM    285  O   PHE A  32      41.743  28.265  17.986  1.00 17.19           O  
ATOM    286  CB  PHE A  32      42.698  26.187  20.334  1.00 16.47           C  
ATOM    287  CG  PHE A  32      43.836  26.067  19.376  1.00 16.05           C  
ATOM    288  CD1 PHE A  32      44.049  24.894  18.679  1.00 19.84           C  
ATOM    289  CD2 PHE A  32      44.693  27.123  19.177  1.00 17.77           C  
ATOM    290  CE1 PHE A  32      45.107  24.778  17.802  1.00 23.44           C  
ATOM    291  CE2 PHE A  32      45.755  27.011  18.310  1.00 21.04           C  
ATOM    292  CZ  PHE A  32      45.952  25.826  17.614  1.00 24.04           C  
ATOM    293  N   THR A  33      41.423  29.032  20.075  1.00 14.19           N  
ATOM    294  CA  THR A  33      41.504  30.437  19.700  1.00 14.21           C  
ATOM    295  C   THR A  33      42.935  30.907  19.898  1.00 16.54           C  
ATOM    296  O   THR A  33      43.606  30.500  20.835  1.00 16.14           O  
ATOM    297  CB  THR A  33      40.508  31.302  20.484  1.00 16.93           C  
ATOM    298  OG1 THR A  33      40.916  31.399  21.841  1.00 17.51           O  
ATOM    299  CG2 THR A  33      39.094  30.728  20.426  1.00 16.74           C  
ATOM    300  N   ALA A  34      43.398  31.801  19.030  1.00 16.06           N  
ATOM    301  CA  ALA A  34      44.711  32.422  19.219  1.00 17.40           C  
ATOM    302  C   ALA A  34      44.771  33.669  18.356  1.00 18.26           C  
ATOM    303  O   ALA A  34      44.345  33.647  17.197  1.00 17.86           O  
ATOM    304  CB  ALA A  34      45.829  31.459  18.842  1.00 18.64           C  
ATOM    305  N   ARG A  35      45.252  34.764  18.934  1.00 17.52           N  
ATOM    306  CA AARG A  35      45.553  35.904  18.080  0.50 16.11           C  
ATOM    307  CA BARG A  35      45.490  35.999  18.200  0.50 18.34           C  
ATOM    308  C   ARG A  35      46.939  36.456  18.405  1.00 16.06           C  
ATOM    309  O   ARG A  35      47.846  35.635  18.544  1.00 14.45           O  
ATOM    310  CB AARG A  35      44.394  36.881  18.048  0.50 14.36           C  
ATOM    311  CB BARG A  35      44.532  37.105  18.646  0.50 21.09           C  
ATOM    312  CG AARG A  35      43.865  37.242  19.394  0.50 14.59           C  
ATOM    313  CG BARG A  35      43.105  36.732  18.855  0.50 24.66           C  
ATOM    314  CD AARG A  35      42.552  37.974  19.161  0.50 24.71           C  
ATOM    315  CD BARG A  35      42.449  37.779  19.780  0.50 24.48           C  
ATOM    316  NE AARG A  35      42.391  39.004  20.151  0.50 22.81           N  
ATOM    317  NE BARG A  35      42.573  39.132  19.244  0.50 24.00           N  
ATOM    318  CZ AARG A  35      41.481  39.969  20.109  0.50 30.46           C  
ATOM    319  CZ BARG A  35      41.820  40.161  19.625  0.50 30.45           C  
ATOM    320  NH1AARG A  35      40.581  40.047  19.116  0.50 16.04           N  
ATOM    321  NH1BARG A  35      40.886  40.012  20.560  0.50 40.47           N  
ATOM    322  NH2AARG A  35      41.472  40.857  21.099  0.50 28.60           N  
ATOM    323  NH2BARG A  35      41.997  41.348  19.072  0.50 22.83           N  
ATOM    324  N   ASP A  36      47.121  37.781  18.467  1.00 15.05           N  
ATOM    325  CA  ASP A  36      48.454  38.413  18.295  1.00 14.84           C  
ATOM    326  C   ASP A  36      49.433  37.937  19.372  1.00 15.94           C  
ATOM    327  O   ASP A  36      50.527  37.412  19.084  1.00 14.09           O  
ATOM    328  CB  ASP A  36      48.321  39.945  18.339  1.00 16.82           C  
ATOM    329  CG  ASP A  36      47.263  40.487  17.364  1.00 19.59           C  
ATOM    330  OD1 ASP A  36      46.048  40.147  17.535  1.00 24.04           O  
ATOM    331  OD2 ASP A  36      47.660  41.263  16.463  1.00 25.99           O  
ATOM    332  N   GLU A  37      49.019  38.055  20.627  1.00 15.58           N  
ATOM    333  CA  GLU A  37      49.943  37.738  21.724  1.00 15.23           C  
ATOM    334  C   GLU A  37      50.313  36.249  21.762  1.00 12.88           C  
ATOM    335  O   GLU A  37      51.461  35.878  22.041  1.00 14.32           O  
ATOM    336  CB  GLU A  37      49.352  38.162  23.077  1.00 15.51           C  
ATOM    337  CG  GLU A  37      49.247  39.645  23.265  1.00 16.24           C  
ATOM    338  CD  GLU A  37      50.575  40.293  23.639  1.00 23.26           C  
ATOM    339  OE1 GLU A  37      50.874  40.353  24.843  1.00 23.45           O  
ATOM    340  OE2 GLU A  37      51.310  40.736  22.734  1.00 22.24           O  
ATOM    341  N   ALA A  38      49.317  35.405  21.564  1.00 14.18           N  
ATOM    342  CA  ALA A  38      49.534  33.971  21.588  1.00 15.50           C  
ATOM    343  C   ALA A  38      50.477  33.522  20.461  1.00 14.33           C  
ATOM    344  O   ALA A  38      51.306  32.642  20.670  1.00 15.90           O  
ATOM    345  CB  ALA A  38      48.185  33.184  21.582  1.00 15.95           C  
ATOM    346  N   HIS A  39      50.311  34.107  19.270  1.00 13.96           N  
ATOM    347  CA  HIS A  39      51.208  33.771  18.156  1.00 13.58           C  
ATOM    348  C   HIS A  39      52.639  34.218  18.456  1.00 14.00           C  
ATOM    349  O   HIS A  39      53.592  33.497  18.180  1.00 14.79           O  
ATOM    350  CB  HIS A  39      50.699  34.393  16.850  1.00 15.60           C  
ATOM    351  CG  HIS A  39      49.594  33.625  16.215  1.00 15.24           C  
ATOM    352  ND1 HIS A  39      48.297  33.661  16.668  1.00 17.28           N  
ATOM    353  CD2 HIS A  39      49.619  32.728  15.197  1.00 16.54           C  
ATOM    354  CE1 HIS A  39      47.550  32.879  15.906  1.00 19.83           C  
ATOM    355  NE2 HIS A  39      48.330  32.292  15.012  1.00 16.31           N  
ATOM    356  N   ALA A  40      52.808  35.420  19.001  1.00 14.23           N  
ATOM    357  CA  ALA A  40      54.120  35.886  19.416  1.00 13.73           C  
ATOM    358  C   ALA A  40      54.777  34.992  20.443  1.00 12.99           C  
ATOM    359  O   ALA A  40      55.948  34.612  20.298  1.00 14.27           O  
ATOM    360  CB  ALA A  40      54.027  37.325  19.908  1.00 14.41           C  
ATOM    361  N   ARG A  41      54.054  34.627  21.496  1.00 13.62           N  
ATOM    362  CA  ARG A  41      54.609  33.703  22.483  1.00 12.74           C  
ATOM    363  C   ARG A  41      54.918  32.324  21.856  1.00 12.63           C  
ATOM    364  O   ARG A  41      55.962  31.722  22.155  1.00 14.18           O  
ATOM    365  CB  ARG A  41      53.643  33.548  23.669  1.00 14.63           C  
ATOM    366  CG  ARG A  41      54.207  32.628  24.749  1.00 14.54           C  
ATOM    367  CD  ARG A  41      53.375  32.581  26.014  1.00 17.47           C  
ATOM    368  NE  ARG A  41      53.545  33.810  26.770  1.00 17.63           N  
ATOM    369  CZ  ARG A  41      52.827  34.141  27.837  1.00 21.74           C  
ATOM    370  NH1 ARG A  41      51.882  33.314  28.281  1.00 20.81           N  
ATOM    371  NH2 ARG A  41      53.092  35.295  28.467  1.00 20.94           N  
ATOM    372  N   ALA A  42      54.058  31.825  20.974  1.00 12.47           N  
ATOM    373  CA  ALA A  42      54.307  30.542  20.349  1.00 13.94           C  
ATOM    374  C   ALA A  42      55.629  30.558  19.584  1.00 12.77           C  
ATOM    375  O   ALA A  42      56.401  29.600  19.679  1.00 13.65           O  
ATOM    376  CB  ALA A  42      53.128  30.124  19.433  1.00 13.59           C  
ATOM    377  N   LEU A  43      55.892  31.613  18.806  1.00 12.69           N  
ATOM    378  CA ALEU A  43      57.152  31.703  18.054  0.50 14.66           C  
ATOM    379  CA BLEU A  43      57.149  31.677  18.049  0.50 15.10           C  
ATOM    380  C   LEU A  43      58.347  31.720  18.986  1.00 14.84           C  
ATOM    381  O   LEU A  43      59.381  31.065  18.728  1.00 15.25           O  
ATOM    382  CB ALEU A  43      57.187  32.950  17.180  0.50 16.56           C  
ATOM    383  CB BLEU A  43      57.170  32.854  17.075  0.50 16.99           C  
ATOM    384  CG ALEU A  43      56.284  32.978  15.950  0.50 18.03           C  
ATOM    385  CG BLEU A  43      56.618  32.500  15.694  0.50 21.76           C  
ATOM    386  CD1ALEU A  43      56.923  33.896  14.923  0.50 20.58           C  
ATOM    387  CD1BLEU A  43      55.091  32.350  15.749  0.50 18.66           C  
ATOM    388  CD2ALEU A  43      56.032  31.572  15.358  0.50 18.05           C  
ATOM    389  CD2BLEU A  43      57.040  33.529  14.671  0.50 23.28           C  
ATOM    390  N   GLU A  44      58.228  32.473  20.079  1.00 13.72           N  
ATOM    391  CA  GLU A  44      59.270  32.519  21.094  1.00 16.15           C  
ATOM    392  C   GLU A  44      59.562  31.127  21.666  1.00 15.86           C  
ATOM    393  O   GLU A  44      60.700  30.692  21.729  1.00 15.39           O  
ATOM    394  CB  GLU A  44      58.863  33.464  22.220  1.00 14.18           C  
ATOM    395  CG  GLU A  44      59.901  33.588  23.315  1.00 18.36           C  
ATOM    396  CD  GLU A  44      59.401  34.380  24.498  1.00 21.34           C  
ATOM    397  OE1 GLU A  44      59.010  35.550  24.278  1.00 23.61           O  
ATOM    398  OE2 GLU A  44      59.378  33.829  25.638  1.00 24.26           O  
ATOM    399  N   TRP A  45      58.526  30.417  22.078  1.00 14.68           N  
ATOM    400  CA  TRP A  45      58.699  29.068  22.625  1.00 15.25           C  
ATOM    401  C   TRP A  45      59.272  28.080  21.583  1.00 12.59           C  
ATOM    402  O   TRP A  45      60.156  27.266  21.905  1.00 14.60           O  
ATOM    403  CB  TRP A  45      57.375  28.526  23.151  1.00 14.68           C  
ATOM    404  CG  TRP A  45      56.957  29.085  24.457  1.00 14.24           C  
ATOM    405  CD1 TRP A  45      57.180  30.358  24.939  1.00 16.49           C  
ATOM    406  CD2 TRP A  45      56.233  28.397  25.475  1.00 13.22           C  
ATOM    407  NE1 TRP A  45      56.641  30.483  26.187  1.00 17.62           N  
ATOM    408  CE2 TRP A  45      56.054  29.298  26.543  1.00 17.84           C  
ATOM    409  CE3 TRP A  45      55.732  27.095  25.596  1.00 15.69           C  
ATOM    410  CZ2 TRP A  45      55.372  28.940  27.711  1.00 19.28           C  
ATOM    411  CZ3 TRP A  45      55.092  26.734  26.768  1.00 16.95           C  
ATOM    412  CH2 TRP A  45      54.904  27.659  27.799  1.00 17.61           C  
HETATM  413  N   MSE A  46      58.780  28.166  20.363  1.00 13.46           N  
HETATM  414  CA  MSE A  46      59.221  27.276  19.276  1.00 17.11           C  
HETATM  415  C   MSE A  46      60.716  27.424  19.008  1.00 20.41           C  
HETATM  416  O   MSE A  46      61.464  26.410  18.883  1.00 18.45           O  
HETATM  417  CB  MSE A  46      58.396  27.521  18.013  1.00 18.71           C  
HETATM  418  CG  MSE A  46      57.009  26.922  18.096  1.00 18.71           C  
HETATM  419 SE   MSE A  46      55.852  27.710  16.728  1.00 25.63          SE  
HETATM  420  CE  MSE A  46      56.891  27.170  15.116  1.00 23.35           C  
ATOM    421  N   GLU A  47      61.206  28.663  18.987  1.00 20.89           N  
ATOM    422  CA  GLU A  47      62.626  28.855  18.697  1.00 24.66           C  
ATOM    423  C   GLU A  47      63.527  28.470  19.858  1.00 22.61           C  
ATOM    424  O   GLU A  47      64.714  28.235  19.656  1.00 21.72           O  
ATOM    425  CB  GLU A  47      62.923  30.276  18.216  1.00 27.83           C  
ATOM    426  CG  GLU A  47      62.789  31.350  19.239  1.00 34.17           C  
ATOM    427  CD  GLU A  47      62.949  32.764  18.640  1.00 34.95           C  
ATOM    428  OE1 GLU A  47      63.273  32.885  17.430  1.00 45.26           O  
ATOM    429  OE2 GLU A  47      62.733  33.745  19.393  1.00 45.09           O  
ATOM    430  N   GLU A  48      62.964  28.386  21.057  1.00 18.92           N  
ATOM    431  CA  GLU A  48      63.682  27.924  22.229  1.00 20.70           C  
ATOM    432  C   GLU A  48      63.514  26.430  22.488  1.00 19.61           C  
ATOM    433  O   GLU A  48      64.134  25.880  23.392  1.00 21.33           O  
ATOM    434  CB  GLU A  48      63.244  28.734  23.438  1.00 21.57           C  
ATOM    435  CG  GLU A  48      63.684  30.175  23.275  1.00 30.32           C  
ATOM    436  CD  GLU A  48      63.020  31.120  24.240  1.00 32.54           C  
ATOM    437  OE1 GLU A  48      62.714  30.703  25.378  1.00 39.75           O  
ATOM    438  OE2 GLU A  48      62.820  32.283  23.837  1.00 41.44           O  
ATOM    439  N   GLY A  49      62.703  25.767  21.670  1.00 19.27           N  
ATOM    440  CA  GLY A  49      62.459  24.339  21.828  1.00 20.66           C  
ATOM    441  C   GLY A  49      61.577  23.985  23.005  1.00 22.15           C  
ATOM    442  O   GLY A  49      61.671  22.865  23.524  1.00 22.00           O  
ATOM    443  N   LYS A  50      60.746  24.932  23.462  1.00 18.40           N  
ATOM    444  CA  LYS A  50      59.796  24.664  24.546  1.00 21.54           C  
ATOM    445  C   LYS A  50      58.494  24.152  23.969  1.00 20.23           C  
ATOM    446  O   LYS A  50      57.865  24.820  23.150  1.00 20.44           O  
ATOM    447  CB  LYS A  50      59.458  25.907  25.366  1.00 20.00           C  
ATOM    448  CG  LYS A  50      60.582  26.633  26.035  1.00 26.48           C  
ATOM    449  CD  LYS A  50      60.034  27.800  26.906  1.00 28.51           C  
ATOM    450  CE  LYS A  50      59.209  27.293  28.121  1.00 38.43           C  
ATOM    451  NZ  LYS A  50      58.704  28.341  29.100  1.00 38.30           N  
ATOM    452  N   GLU A  51      58.063  22.985  24.432  1.00 22.90           N  
ATOM    453  CA  GLU A  51      56.833  22.394  23.952  1.00 25.21           C  
ATOM    454  C   GLU A  51      55.641  23.293  24.271  1.00 20.90           C  
ATOM    455  O   GLU A  51      55.501  23.790  25.391  1.00 21.91           O  
ATOM    456  CB  GLU A  51      56.633  21.000  24.565  1.00 26.25           C  
ATOM    457  CG  GLU A  51      55.397  20.293  24.008  1.00 30.78           C  
ATOM    458  CD  GLU A  51      55.382  18.797  24.308  1.00 34.59           C  
ATOM    459  OE1 GLU A  51      55.745  18.415  25.451  1.00 44.60           O  
ATOM    460  OE2 GLU A  51      54.995  18.025  23.393  1.00 50.50           O  
ATOM    461  N   LEU A  52      54.791  23.500  23.275  1.00 19.79           N  
ATOM    462  CA  LEU A  52      53.594  24.343  23.442  1.00 19.15           C  
ATOM    463  C   LEU A  52      52.511  23.547  24.178  1.00 21.12           C  
ATOM    464  O   LEU A  52      52.469  22.323  24.079  1.00 21.35           O  
ATOM    465  CB  LEU A  52      53.032  24.787  22.094  1.00 16.53           C  
ATOM    466  CG  LEU A  52      53.936  25.626  21.205  1.00 17.83           C  
ATOM    467  CD1 LEU A  52      53.197  25.962  19.919  1.00 24.87           C  
ATOM    468  CD2 LEU A  52      54.366  26.895  21.928  1.00 18.41           C  
ATOM    469  N   PRO A  53      51.641  24.234  24.916  1.00 20.72           N  
ATOM    470  CA  PRO A  53      50.568  23.526  25.608  1.00 23.61           C  
ATOM    471  C   PRO A  53      49.342  23.218  24.726  1.00 25.38           C  
ATOM    472  O   PRO A  53      48.291  22.862  25.247  1.00 29.03           O  
ATOM    473  CB  PRO A  53      50.231  24.467  26.761  1.00 23.64           C  
ATOM    474  CG  PRO A  53      50.630  25.815  26.305  1.00 24.95           C  
ATOM    475  CD  PRO A  53      51.657  25.677  25.225  1.00 22.38           C  
ATOM    476  N   PHE A  54      49.476  23.359  23.410  1.00 20.51           N  
ATOM    477  CA  PHE A  54      48.438  22.988  22.446  1.00 21.26           C  
ATOM    478  C   PHE A  54      49.226  22.638  21.181  1.00 21.83           C  
ATOM    479  O   PHE A  54      50.445  22.815  21.165  1.00 21.12           O  
ATOM    480  CB  PHE A  54      47.474  24.138  22.186  1.00 22.63           C  
ATOM    481  CG  PHE A  54      48.172  25.426  21.833  1.00 20.72           C  
ATOM    482  CD1 PHE A  54      48.602  26.288  22.835  1.00 19.19           C  
ATOM    483  CD2 PHE A  54      48.459  25.743  20.531  1.00 23.63           C  
ATOM    484  CE1 PHE A  54      49.294  27.451  22.537  1.00 21.50           C  
ATOM    485  CE2 PHE A  54      49.147  26.899  20.236  1.00 26.43           C  
ATOM    486  CZ  PHE A  54      49.564  27.756  21.256  1.00 24.74           C  
ATOM    487  N   SER A  55      48.545  22.156  20.139  1.00 20.71           N  
ATOM    488  CA ASER A  55      49.236  21.772  18.910  0.50 20.13           C  
ATOM    489  CA BSER A  55      49.208  21.720  18.917  0.50 21.41           C  
ATOM    490  C   SER A  55      48.532  22.306  17.689  1.00 19.84           C  
ATOM    491  O   SER A  55      47.324  22.162  17.532  1.00 21.63           O  
ATOM    492  CB ASER A  55      49.374  20.255  18.780  0.50 20.80           C  
ATOM    493  CB BSER A  55      49.166  20.190  18.838  0.50 21.89           C  
ATOM    494  OG ASER A  55      49.999  19.935  17.538  0.50 17.07           O  
ATOM    495  OG BSER A  55      49.875  19.605  19.915  0.50 28.28           O  
ATOM    496  N   PHE A  56      49.308  22.945  16.823  1.00 20.67           N  
ATOM    497  CA  PHE A  56      48.789  23.433  15.554  1.00 20.46           C  
ATOM    498  C   PHE A  56      48.583  22.261  14.599  1.00 18.32           C  
ATOM    499  O   PHE A  56      47.733  22.308  13.715  1.00 18.65           O  
ATOM    500  CB  PHE A  56      49.770  24.440  14.930  1.00 20.49           C  
ATOM    501  CG  PHE A  56      49.803  25.777  15.630  1.00 19.05           C  
ATOM    502  CD1 PHE A  56      48.791  26.706  15.432  1.00 24.62           C  
ATOM    503  CD2 PHE A  56      50.844  26.104  16.444  1.00 26.63           C  
ATOM    504  CE1 PHE A  56      48.830  27.950  16.050  1.00 25.89           C  
ATOM    505  CE2 PHE A  56      50.879  27.342  17.063  1.00 21.18           C  
ATOM    506  CZ  PHE A  56      49.880  28.245  16.868  1.00 25.89           C  
ATOM    507  N   ASP A  57      49.382  21.202  14.744  1.00 17.44           N  
ATOM    508  CA  ASP A  57      49.328  20.111  13.788  1.00 18.79           C  
ATOM    509  C   ASP A  57      48.003  19.355  13.840  1.00 17.08           C  
ATOM    510  O   ASP A  57      47.591  18.873  14.895  1.00 17.96           O  
ATOM    511  CB  ASP A  57      50.469  19.125  14.014  1.00 21.31           C  
ATOM    512  CG  ASP A  57      50.645  18.160  12.868  1.00 25.06           C  
ATOM    513  OD1 ASP A  57      50.293  18.481  11.719  1.00 24.95           O  
ATOM    514  OD2 ASP A  57      51.166  17.047  13.109  1.00 35.40           O  
ATOM    515  N   LYS A  58      47.364  19.258  12.678  1.00 16.15           N  
ATOM    516  CA  LYS A  58      46.046  18.663  12.504  1.00 16.07           C  
ATOM    517  C   LYS A  58      44.931  19.414  13.222  1.00 17.35           C  
ATOM    518  O   LYS A  58      43.823  18.903  13.368  1.00 19.34           O  
ATOM    519  CB  LYS A  58      46.036  17.195  12.869  1.00 18.45           C  
ATOM    520  CG  LYS A  58      47.078  16.400  12.074  1.00 22.24           C  
ATOM    521  CD  LYS A  58      46.974  14.902  12.372  1.00 31.81           C  
ATOM    522  CE  LYS A  58      48.336  14.216  12.301  1.00 40.46           C  
ATOM    523  NZ  LYS A  58      49.194  14.674  11.165  1.00 44.24           N  
ATOM    524  N   GLY A  59      45.231  20.637  13.627  1.00 16.99           N  
ATOM    525  CA  GLY A  59      44.312  21.419  14.394  1.00 17.23           C  
ATOM    526  C   GLY A  59      43.688  22.536  13.580  1.00 17.37           C  
ATOM    527  O   GLY A  59      44.101  22.838  12.456  1.00 16.09           O  
ATOM    528  N   VAL A  60      42.663  23.126  14.174  1.00 16.26           N  
ATOM    529  CA  VAL A  60      42.020  24.303  13.627  1.00 16.04           C  
ATOM    530  C   VAL A  60      42.172  25.447  14.618  1.00 16.25           C  
ATOM    531  O   VAL A  60      41.722  25.362  15.762  1.00 16.45           O  
ATOM    532  CB  VAL A  60      40.542  24.047  13.333  1.00 18.40           C  
ATOM    533  CG1 VAL A  60      39.829  25.371  12.921  1.00 17.74           C  
ATOM    534  CG2 VAL A  60      40.393  22.913  12.247  1.00 16.87           C  
ATOM    535  N   VAL A  61      42.855  26.499  14.179  1.00 14.31           N  
ATOM    536  CA AVAL A  61      43.008  27.728  14.969  0.50 13.55           C  
ATOM    537  CA BVAL A  61      43.029  27.737  14.947  0.50 15.11           C  
ATOM    538  C   VAL A  61      41.996  28.773  14.512  1.00 15.33           C  
ATOM    539  O   VAL A  61      41.812  29.006  13.311  1.00 14.79           O  
ATOM    540  CB AVAL A  61      44.452  28.310  14.887  0.50 14.18           C  
ATOM    541  CB BVAL A  61      44.440  28.349  14.727  0.50 15.41           C  
ATOM    542  CG1AVAL A  61      44.877  28.521  13.463  0.50 10.35           C  
ATOM    543  CG1BVAL A  61      44.778  29.334  15.884  0.50 19.75           C  
ATOM    544  CG2AVAL A  61      44.546  29.646  15.678  0.50 16.98           C  
ATOM    545  CG2BVAL A  61      45.491  27.259  14.604  0.50 23.68           C  
ATOM    546  N   TYR A  62      41.342  29.399  15.479  1.00 15.09           N  
ATOM    547  CA  TYR A  62      40.381  30.446  15.188  1.00 16.24           C  
ATOM    548  C   TYR A  62      40.949  31.774  15.671  1.00 15.29           C  
ATOM    549  O   TYR A  62      41.205  31.947  16.875  1.00 13.71           O  
ATOM    550  CB  TYR A  62      39.070  30.130  15.887  1.00 15.12           C  
ATOM    551  CG  TYR A  62      37.922  31.089  15.661  1.00 14.28           C  
ATOM    552  CD1 TYR A  62      37.872  31.941  14.567  1.00 16.13           C  
ATOM    553  CD2 TYR A  62      36.847  31.124  16.540  1.00 16.64           C  
ATOM    554  CE1 TYR A  62      36.782  32.782  14.363  1.00 15.26           C  
ATOM    555  CE2 TYR A  62      35.758  31.981  16.331  1.00 18.72           C  
ATOM    556  CZ  TYR A  62      35.733  32.802  15.238  1.00 14.86           C  
ATOM    557  OH  TYR A  62      34.714  33.697  14.989  1.00 18.87           O  
ATOM    558  N   HIS A  63      41.185  32.685  14.722  1.00 12.66           N  
ATOM    559  CA  HIS A  63      41.544  34.079  15.006  1.00 14.53           C  
ATOM    560  C   HIS A  63      40.344  34.771  15.636  1.00 14.10           C  
ATOM    561  O   HIS A  63      39.460  35.261  14.941  1.00 16.34           O  
ATOM    562  CB  HIS A  63      41.958  34.762  13.715  1.00 14.27           C  
ATOM    563  CG  HIS A  63      43.177  34.185  13.055  1.00 14.69           C  
ATOM    564  ND1 HIS A  63      43.419  34.362  11.710  1.00 14.49           N  
ATOM    565  CD2 HIS A  63      44.211  33.455  13.529  1.00 14.61           C  
ATOM    566  CE1 HIS A  63      44.553  33.778  11.388  1.00 20.01           C  
ATOM    567  NE2 HIS A  63      45.061  33.214  12.473  1.00 18.59           N  
ATOM    568  N   CYS A  64      40.343  34.799  16.965  1.00 15.12           N  
ATOM    569  CA  CYS A  64      39.199  35.180  17.788  1.00 16.96           C  
ATOM    570  C   CYS A  64      39.682  35.601  19.176  1.00 21.03           C  
ATOM    571  O   CYS A  64      40.550  34.926  19.765  1.00 19.61           O  
ATOM    572  CB  CYS A  64      38.284  33.992  17.971  1.00 19.76           C  
ATOM    573  SG  CYS A  64      36.907  34.255  19.080  1.00 18.82           S  
ATOM    574  N   GLY A  65      39.077  36.675  19.696  1.00 18.98           N  
ATOM    575  CA  GLY A  65      39.168  37.038  21.111  1.00 20.49           C  
ATOM    576  C   GLY A  65      37.816  36.824  21.752  1.00 17.64           C  
ATOM    577  O   GLY A  65      36.940  37.699  21.706  1.00 19.58           O  
ATOM    578  N   PRO A  66      37.623  35.655  22.359  1.00 17.98           N  
ATOM    579  CA  PRO A  66      36.259  35.358  22.828  1.00 19.61           C  
ATOM    580  C   PRO A  66      35.869  36.103  24.084  1.00 18.95           C  
ATOM    581  O   PRO A  66      36.734  36.427  24.882  1.00 19.12           O  
ATOM    582  CB  PRO A  66      36.321  33.875  23.120  1.00 20.60           C  
ATOM    583  CG  PRO A  66      37.737  33.605  23.436  1.00 21.66           C  
ATOM    584  CD  PRO A  66      38.548  34.536  22.624  1.00 17.56           C  
ATOM    585  N   LEU A  67      34.573  36.331  24.239  1.00 17.56           N  
ATOM    586  CA  LEU A  67      33.976  36.760  25.490  1.00 17.61           C  
ATOM    587  C   LEU A  67      33.446  35.492  26.217  1.00 18.60           C  
ATOM    588  O   LEU A  67      32.622  34.728  25.664  1.00 17.32           O  
ATOM    589  CB  LEU A  67      32.852  37.767  25.216  1.00 20.97           C  
ATOM    590  CG  LEU A  67      32.269  38.540  26.394  1.00 22.56           C  
ATOM    591  CD1 LEU A  67      33.364  39.168  27.243  1.00 25.51           C  
ATOM    592  CD2 LEU A  67      31.289  39.612  25.862  1.00 20.58           C  
ATOM    593  N   VAL A  68      33.936  35.278  27.435  1.00 19.58           N  
ATOM    594  CA  VAL A  68      33.690  34.049  28.193  1.00 18.61           C  
ATOM    595  C   VAL A  68      33.179  34.447  29.576  1.00 21.56           C  
ATOM    596  O   VAL A  68      33.657  35.415  30.153  1.00 22.28           O  
ATOM    597  CB  VAL A  68      34.981  33.164  28.293  1.00 19.48           C  
ATOM    598  CG1 VAL A  68      34.693  31.785  28.861  1.00 21.89           C  
ATOM    599  CG2 VAL A  68      35.632  33.012  26.903  1.00 20.14           C  
ATOM    600  N   LYS A  69      32.171  33.737  30.060  1.00 18.32           N  
ATOM    601  CA  LYS A  69      31.676  33.929  31.409  1.00 21.39           C  
ATOM    602  C   LYS A  69      31.932  32.649  32.212  1.00 21.61           C  
ATOM    603  O   LYS A  69      31.963  31.568  31.658  1.00 21.68           O  
ATOM    604  CB  LYS A  69      30.194  34.309  31.364  1.00 20.30           C  
ATOM    605  CG  LYS A  69      29.250  33.249  30.831  1.00 25.46           C  
ATOM    606  CD  LYS A  69      27.770  33.633  31.017  1.00 27.98           C  
ATOM    607  CE  LYS A  69      26.849  32.438  30.758  1.00 30.53           C  
ATOM    608  NZ  LYS A  69      25.479  32.865  30.427  1.00 42.59           N  
ATOM    609  N   LYS A  70      32.127  32.766  33.514  1.00 25.08           N  
ATOM    610  CA  LYS A  70      32.340  31.566  34.332  1.00 29.38           C  
ATOM    611  C   LYS A  70      31.190  31.366  35.312  1.00 31.78           C  
ATOM    612  O   LYS A  70      31.012  32.172  36.216  1.00 34.32           O  
ATOM    613  CB  LYS A  70      33.674  31.633  35.068  1.00 30.25           C  
ATOM    614  CG  LYS A  70      34.038  30.286  35.747  1.00 37.14           C  
ATOM    615  CD  LYS A  70      35.540  30.078  35.930  1.00 38.15           C  
ATOM    616  N   ASN A  71      30.371  30.336  35.086  1.00 35.71           N  
ATOM    617  CA  ASN A  71      29.373  29.897  36.074  1.00 37.90           C  
ATOM    618  C   ASN A  71      29.972  28.666  36.788  1.00 38.47           C  
ATOM    619  O   ASN A  71      31.038  28.784  37.401  1.00 39.34           O  
ATOM    620  CB  ASN A  71      28.028  29.596  35.398  1.00 39.05           C  
ATOM    621  N   ASP A  72      29.331  27.498  36.686  1.00 38.62           N  
ATOM    622  CA  ASP A  72      29.962  26.236  37.123  1.00 39.64           C  
ATOM    623  C   ASP A  72      31.175  25.901  36.228  1.00 39.11           C  
ATOM    624  O   ASP A  72      32.210  25.415  36.700  1.00 40.23           O  
ATOM    625  CB  ASP A  72      28.951  25.080  37.106  1.00 39.72           C  
ATOM    626  N   GLU A  73      31.027  26.177  34.938  1.00 35.69           N  
ATOM    627  CA  GLU A  73      32.091  25.999  33.963  1.00 33.27           C  
ATOM    628  C   GLU A  73      32.265  27.323  33.220  1.00 29.24           C  
ATOM    629  O   GLU A  73      31.401  28.210  33.312  1.00 26.95           O  
ATOM    630  CB  GLU A  73      31.703  24.900  32.960  1.00 35.59           C  
ATOM    631  CG  GLU A  73      31.108  23.629  33.580  1.00 35.53           C  
ATOM    632  N   TRP A  74      33.385  27.466  32.514  1.00 25.24           N  
ATOM    633  CA  TRP A  74      33.512  28.509  31.548  1.00 22.98           C  
ATOM    634  C   TRP A  74      32.441  28.303  30.466  1.00 22.67           C  
ATOM    635  O   TRP A  74      32.167  27.165  30.035  1.00 20.92           O  
ATOM    636  CB  TRP A  74      34.871  28.467  30.862  1.00 22.38           C  
ATOM    637  CG  TRP A  74      36.084  28.895  31.672  1.00 24.09           C  
ATOM    638  CD1 TRP A  74      37.133  28.108  32.035  1.00 22.94           C  
ATOM    639  CD2 TRP A  74      36.393  30.221  32.134  1.00 20.84           C  
ATOM    640  NE1 TRP A  74      38.065  28.853  32.723  1.00 23.62           N  
ATOM    641  CE2 TRP A  74      37.641  30.154  32.787  1.00 23.09           C  
ATOM    642  CE3 TRP A  74      35.737  31.460  32.053  1.00 23.34           C  
ATOM    643  CZ2 TRP A  74      38.250  31.277  33.367  1.00 26.20           C  
ATOM    644  CZ3 TRP A  74      36.355  32.583  32.623  1.00 27.42           C  
ATOM    645  CH2 TRP A  74      37.586  32.474  33.285  1.00 26.48           C  
ATOM    646  N   ARG A  75      31.859  29.411  30.008  1.00 19.83           N  
ATOM    647  CA AARG A  75      30.874  29.394  28.918  0.50 19.69           C  
ATOM    648  CA BARG A  75      30.913  29.365  28.898  0.50 19.72           C  
ATOM    649  C   ARG A  75      31.221  30.499  27.945  1.00 18.53           C  
ATOM    650  O   ARG A  75      31.345  31.661  28.358  1.00 18.62           O  
ATOM    651  CB AARG A  75      29.461  29.677  29.441  0.50 20.52           C  
ATOM    652  CB BARG A  75      29.474  29.482  29.395  0.50 20.85           C  
ATOM    653  CG AARG A  75      29.007  28.809  30.586  0.50 22.43           C  
ATOM    654  CG BARG A  75      28.437  29.204  28.322  0.50 23.03           C  
ATOM    655  CD AARG A  75      28.802  27.373  30.170  0.50 23.15           C  
ATOM    656  NE AARG A  75      28.400  26.578  31.329  0.50 24.45           N  
ATOM    657  CZ AARG A  75      28.243  25.260  31.328  0.50 31.26           C  
ATOM    658  NH1AARG A  75      28.451  24.558  30.222  0.50 33.73           N  
ATOM    659  NH2AARG A  75      27.879  24.643  32.441  0.50 31.89           N  
ATOM    660  N   VAL A  76      31.369  30.159  26.667  1.00 17.93           N  
ATOM    661  CA  VAL A  76      31.635  31.180  25.669  1.00 16.56           C  
ATOM    662  C   VAL A  76      30.327  31.871  25.294  1.00 16.61           C  
ATOM    663  O   VAL A  76      29.358  31.219  24.909  1.00 16.87           O  
ATOM    664  CB  VAL A  76      32.341  30.638  24.400  1.00 16.11           C  
ATOM    665  CG1 VAL A  76      32.581  31.804  23.402  1.00 15.80           C  
ATOM    666  CG2 VAL A  76      33.657  29.914  24.757  1.00 18.06           C  
ATOM    667  N   VAL A  77      30.344  33.206  25.416  1.00 15.64           N  
ATOM    668  CA AVAL A  77      29.223  34.124  25.135  0.50 15.09           C  
ATOM    669  CA BVAL A  77      29.167  34.006  25.098  0.50 15.57           C  
ATOM    670  C   VAL A  77      29.279  34.728  23.736  1.00 16.69           C  
ATOM    671  O   VAL A  77      28.265  34.934  23.084  1.00 18.76           O  
ATOM    672  CB AVAL A  77      29.270  35.311  26.100  0.50 17.16           C  
ATOM    673  CB BVAL A  77      28.757  34.914  26.291  0.50 16.35           C  
ATOM    674  CG1AVAL A  77      28.179  36.356  25.758  0.50 15.97           C  
ATOM    675  CG1BVAL A  77      28.403  34.051  27.499  0.50 16.79           C  
ATOM    676  CG2AVAL A  77      29.147  34.825  27.527  0.50 13.54           C  
ATOM    677  CG2BVAL A  77      29.853  35.908  26.664  0.50 17.06           C  
ATOM    678  N   SER A  78      30.491  35.066  23.286  1.00 15.39           N  
ATOM    679  CA ASER A  78      30.681  35.551  21.930  0.50 15.43           C  
ATOM    680  CA BSER A  78      30.695  35.588  21.932  0.50 15.32           C  
ATOM    681  C   SER A  78      32.011  35.043  21.379  1.00 16.62           C  
ATOM    682  O   SER A  78      33.014  34.956  22.116  1.00 16.95           O  
ATOM    683  CB ASER A  78      30.599  37.083  21.872  0.50 18.71           C  
ATOM    684  CB BSER A  78      30.677  37.136  21.895  0.50 18.57           C  
ATOM    685  OG ASER A  78      30.351  37.506  20.549  0.50 23.33           O  
ATOM    686  OG BSER A  78      31.976  37.691  22.070  0.50 22.72           O  
ATOM    687  N   ALA A  79      31.997  34.677  20.106  1.00 15.21           N  
ATOM    688  CA  ALA A  79      33.163  34.142  19.440  1.00 17.25           C  
ATOM    689  C   ALA A  79      33.165  34.623  17.990  1.00 14.91           C  
ATOM    690  O   ALA A  79      33.021  33.843  17.070  1.00 18.03           O  
ATOM    691  CB  ALA A  79      33.155  32.606  19.528  1.00 19.01           C  
ATOM    692  N   GLY A  80      33.331  35.934  17.840  1.00 17.22           N  
ATOM    693  CA  GLY A  80      33.436  36.566  16.532  1.00 17.81           C  
ATOM    694  C   GLY A  80      34.880  36.608  16.078  1.00 17.84           C  
ATOM    695  O   GLY A  80      35.811  36.493  16.897  1.00 18.41           O  
ATOM    696  N   PRO A  81      35.077  36.748  14.766  1.00 17.53           N  
ATOM    697  CA  PRO A  81      36.429  36.677  14.228  1.00 15.52           C  
ATOM    698  C   PRO A  81      37.205  37.992  14.384  1.00 15.70           C  
ATOM    699  O   PRO A  81      36.604  39.083  14.525  1.00 18.83           O  
ATOM    700  CB  PRO A  81      36.180  36.386  12.748  1.00 16.70           C  
ATOM    701  CG  PRO A  81      34.896  37.075  12.432  1.00 17.88           C  
ATOM    702  CD  PRO A  81      34.058  36.895  13.703  1.00 19.29           C  
ATOM    703  N   THR A  82      38.531  37.866  14.370  1.00 16.25           N  
ATOM    704  CA ATHR A  82      39.384  39.053  14.271  0.50 15.24           C  
ATOM    705  CA BTHR A  82      39.463  38.969  14.314  0.50 16.13           C  
ATOM    706  C   THR A  82      40.074  39.014  12.914  1.00 17.02           C  
ATOM    707  O   THR A  82      40.126  38.000  12.216  1.00 16.41           O  
ATOM    708  CB ATHR A  82      40.404  39.210  15.464  0.50 15.90           C  
ATOM    709  CB BTHR A  82      40.589  38.703  15.328  0.50 17.13           C  
ATOM    710  OG1ATHR A  82      40.860  40.575  15.560  0.50 15.05           O  
ATOM    711  OG1BTHR A  82      40.042  38.704  16.647  0.50 20.23           O  
ATOM    712  CG2ATHR A  82      41.619  38.293  15.316  0.50 14.89           C  
ATOM    713  CG2BTHR A  82      41.711  39.716  15.171  0.50 15.52           C  
ATOM    714  N   THR A  83      40.571  40.163  12.524  1.00 16.15           N  
ATOM    715  CA  THR A  83      41.251  40.318  11.243  1.00 15.18           C  
ATOM    716  C   THR A  83      42.543  39.496  11.147  1.00 17.26           C  
ATOM    717  O   THR A  83      43.537  39.761  11.833  1.00 17.36           O  
ATOM    718  CB  THR A  83      41.583  41.804  11.021  1.00 17.03           C  
ATOM    719  OG1 THR A  83      40.374  42.558  11.144  1.00 20.39           O  
ATOM    720  CG2 THR A  83      42.176  42.003   9.653  1.00 18.29           C  
ATOM    721  N   SER A  84      42.532  38.496  10.275  1.00 15.04           N  
ATOM    722  CA  SER A  84      43.604  37.539  10.200  1.00 14.28           C  
ATOM    723  C   SER A  84      44.946  38.119   9.743  1.00 14.91           C  
ATOM    724  O   SER A  84      45.990  37.529  10.049  1.00 17.11           O  
ATOM    725  CB  SER A  84      43.216  36.376   9.271  1.00 16.23           C  
ATOM    726  OG  SER A  84      42.036  35.773   9.751  1.00 14.75           O  
ATOM    727  N   ALA A  85      44.930  39.225   8.982  1.00 15.10           N  
ATOM    728  CA  ALA A  85      46.166  39.759   8.387  1.00 18.04           C  
ATOM    729  C   ALA A  85      47.190  40.091   9.484  1.00 16.37           C  
ATOM    730  O   ALA A  85      48.425  39.986   9.271  1.00 17.81           O  
ATOM    731  CB  ALA A  85      45.887  40.961   7.502  1.00 19.02           C  
ATOM    732  N   ARG A  86      46.694  40.393  10.675  1.00 18.35           N  
ATOM    733  CA  ARG A  86      47.611  40.660  11.805  1.00 18.84           C  
ATOM    734  C   ARG A  86      48.493  39.479  12.163  1.00 20.68           C  
ATOM    735  O   ARG A  86      49.562  39.658  12.762  1.00 20.66           O  
ATOM    736  CB  ARG A  86      46.829  41.094  13.023  1.00 20.36           C  
ATOM    737  CG  ARG A  86      46.109  42.407  12.812  1.00 21.23           C  
ATOM    738  CD  ARG A  86      46.060  43.173  14.101  1.00 24.53           C  
ATOM    739  NE  ARG A  86      45.457  42.344  15.132  1.00 24.13           N  
ATOM    740  CZ  ARG A  86      44.163  42.151  15.286  1.00 28.58           C  
ATOM    741  NH1 ARG A  86      43.268  42.766  14.505  1.00 29.84           N  
ATOM    742  NH2 ARG A  86      43.761  41.353  16.253  1.00 36.38           N  
HETATM  743  N   MSE A  87      48.045  38.275  11.786  1.00 18.15           N  
HETATM  744  CA  MSE A  87      48.778  37.040  12.024  1.00 18.78           C  
HETATM  745  C   MSE A  87      49.670  36.659  10.861  1.00 16.07           C  
HETATM  746  O   MSE A  87      50.375  35.643  10.936  1.00 16.02           O  
HETATM  747  CB  MSE A  87      47.812  35.911  12.365  1.00 19.44           C  
HETATM  748  CG  MSE A  87      47.626  35.705  13.862  1.00 24.14           C  
HETATM  749 SE   MSE A  87      47.002  37.279  14.851  1.00 25.62          SE  
HETATM  750  CE  MSE A  87      45.114  37.217  14.129  1.00 23.57           C  
ATOM    751  N   ASN A  88      49.659  37.450   9.782  1.00 16.53           N  
ATOM    752  CA  ASN A  88      50.496  37.109   8.616  1.00 16.86           C  
ATOM    753  C   ASN A  88      51.970  36.857   8.962  1.00 17.20           C  
ATOM    754  O   ASN A  88      52.586  35.944   8.412  1.00 17.60           O  
ATOM    755  CB  ASN A  88      50.429  38.182   7.526  1.00 17.29           C  
ATOM    756  CG  ASN A  88      49.177  38.100   6.685  1.00 19.64           C  
ATOM    757  OD1 ASN A  88      48.595  37.009   6.506  1.00 19.37           O  
ATOM    758  ND2 ASN A  88      48.773  39.264   6.115  1.00 18.21           N  
ATOM    759  N   PRO A  89      52.572  37.701   9.821  1.00 17.53           N  
ATOM    760  CA  PRO A  89      54.021  37.518  10.106  1.00 20.29           C  
ATOM    761  C   PRO A  89      54.404  36.249  10.832  1.00 18.05           C  
ATOM    762  O   PRO A  89      55.558  35.820  10.770  1.00 19.58           O  
ATOM    763  CB  PRO A  89      54.344  38.721  10.999  1.00 21.85           C  
ATOM    764  CG  PRO A  89      53.252  39.739  10.642  1.00 23.26           C  
ATOM    765  CD  PRO A  89      52.026  38.887  10.493  1.00 20.55           C  
ATOM    766  N   PHE A  90      53.449  35.650  11.529  1.00 15.22           N  
ATOM    767  CA  PHE A  90      53.703  34.467  12.355  1.00 17.01           C  
ATOM    768  C   PHE A  90      53.369  33.158  11.671  1.00 17.86           C  
ATOM    769  O   PHE A  90      53.898  32.085  12.009  1.00 16.96           O  
ATOM    770  CB  PHE A  90      52.862  34.552  13.612  1.00 18.03           C  
ATOM    771  CG  PHE A  90      52.993  35.838  14.352  1.00 14.43           C  
ATOM    772  CD1 PHE A  90      54.077  36.082  15.181  1.00 17.60           C  
ATOM    773  CD2 PHE A  90      52.000  36.779  14.303  1.00 15.33           C  
ATOM    774  CE1 PHE A  90      54.167  37.278  15.895  1.00 17.49           C  
ATOM    775  CE2 PHE A  90      52.096  37.975  15.020  1.00 19.71           C  
ATOM    776  CZ  PHE A  90      53.197  38.218  15.788  1.00 17.23           C  
ATOM    777  N   THR A  91      52.445  33.222  10.728  1.00 18.02           N  
ATOM    778  CA  THR A  91      51.764  32.004  10.269  1.00 17.12           C  
ATOM    779  C   THR A  91      52.611  31.090   9.372  1.00 16.02           C  
ATOM    780  O   THR A  91      52.549  29.870   9.533  1.00 16.04           O  
ATOM    781  CB  THR A  91      50.378  32.372   9.691  1.00 18.33           C  
ATOM    782  OG1 THR A  91      49.591  32.935  10.751  1.00 15.78           O  
ATOM    783  CG2 THR A  91      49.656  31.127   9.130  1.00 16.95           C  
ATOM    784  N   PRO A  92      53.394  31.637   8.419  1.00 17.98           N  
ATOM    785  CA  PRO A  92      54.293  30.759   7.664  1.00 18.57           C  
ATOM    786  C   PRO A  92      55.234  29.902   8.555  1.00 18.90           C  
ATOM    787  O   PRO A  92      55.422  28.725   8.285  1.00 18.30           O  
ATOM    788  CB  PRO A  92      55.074  31.730   6.774  1.00 20.98           C  
ATOM    789  CG  PRO A  92      54.178  32.895   6.620  1.00 20.07           C  
ATOM    790  CD  PRO A  92      53.424  33.018   7.908  1.00 17.76           C  
ATOM    791  N   LYS A  93      55.801  30.475   9.608  1.00 18.64           N  
ATOM    792  CA  LYS A  93      56.657  29.718  10.508  1.00 20.90           C  
ATOM    793  C   LYS A  93      55.897  28.573  11.192  1.00 18.65           C  
ATOM    794  O   LYS A  93      56.408  27.461  11.374  1.00 18.32           O  
ATOM    795  CB  LYS A  93      57.303  30.669  11.534  1.00 22.35           C  
ATOM    796  CG  LYS A  93      58.407  30.056  12.392  1.00 30.70           C  
ATOM    797  CD  LYS A  93      59.531  29.511  11.532  1.00 38.22           C  
ATOM    798  CE  LYS A  93      60.807  29.290  12.321  1.00 45.35           C  
ATOM    799  NZ  LYS A  93      61.842  28.596  11.484  1.00 47.86           N  
ATOM    800  N   ILE A  94      54.660  28.847  11.580  1.00 16.19           N  
ATOM    801  CA  ILE A  94      53.811  27.862  12.220  1.00 16.74           C  
ATOM    802  C   ILE A  94      53.459  26.729  11.240  1.00 17.92           C  
ATOM    803  O   ILE A  94      53.483  25.558  11.609  1.00 19.62           O  
ATOM    804  CB  ILE A  94      52.558  28.510  12.788  1.00 17.72           C  
ATOM    805  CG1 ILE A  94      52.924  29.290  14.063  1.00 21.40           C  
ATOM    806  CG2 ILE A  94      51.517  27.454  13.078  1.00 19.48           C  
ATOM    807  CD1 ILE A  94      51.976  30.412  14.433  1.00 23.35           C  
ATOM    808  N   LEU A  95      53.167  27.079   9.981  1.00 15.78           N  
ATOM    809  CA  LEU A  95      52.827  26.083   8.972  1.00 16.48           C  
ATOM    810  C   LEU A  95      54.012  25.177   8.585  1.00 17.79           C  
ATOM    811  O   LEU A  95      53.807  24.057   8.109  1.00 17.46           O  
ATOM    812  CB  LEU A  95      52.285  26.752   7.715  1.00 16.56           C  
ATOM    813  CG  LEU A  95      50.865  27.323   7.784  1.00 19.50           C  
ATOM    814  CD1 LEU A  95      50.615  28.395   6.724  1.00 18.97           C  
ATOM    815  CD2 LEU A  95      49.853  26.173   7.654  1.00 22.59           C  
ATOM    816  N   GLU A  96      55.234  25.688   8.748  1.00 18.42           N  
ATOM    817  CA  GLU A  96      56.441  24.981   8.341  1.00 23.38           C  
ATOM    818  C   GLU A  96      56.447  23.537   8.798  1.00 23.85           C  
ATOM    819  O   GLU A  96      56.707  22.641   7.998  1.00 24.92           O  
ATOM    820  CB  GLU A  96      57.684  25.656   8.911  1.00 24.05           C  
ATOM    821  CG  GLU A  96      58.272  26.796   8.091  1.00 35.52           C  
ATOM    822  CD  GLU A  96      59.602  27.338   8.692  1.00 36.19           C  
ATOM    823  OE1 GLU A  96      60.310  26.580   9.415  1.00 48.23           O  
ATOM    824  OE2 GLU A  96      59.916  28.537   8.448  1.00 55.20           O  
ATOM    825  N   LYS A  97      56.159  23.288  10.068  1.00 24.43           N  
ATOM    826  CA  LYS A  97      56.300  21.918  10.558  1.00 29.71           C  
ATOM    827  C   LYS A  97      55.005  21.093  10.580  1.00 28.04           C  
ATOM    828  O   LYS A  97      55.070  19.891  10.827  1.00 30.36           O  
ATOM    829  CB  LYS A  97      57.010  21.872  11.930  1.00 33.03           C  
ATOM    830  CG  LYS A  97      58.539  22.080  11.841  1.00 32.91           C  
ATOM    831  CD  LYS A  97      59.252  21.941  13.210  1.00 33.26           C  
ATOM    832  N   VAL A  98      53.849  21.678  10.275  1.00 22.77           N  
ATOM    833  CA  VAL A  98      52.622  20.891  10.370  1.00 20.32           C  
ATOM    834  C   VAL A  98      52.439  19.978   9.148  1.00 18.84           C  
ATOM    835  O   VAL A  98      52.864  20.314   8.039  1.00 20.35           O  
ATOM    836  CB  VAL A  98      51.332  21.752  10.580  1.00 20.63           C  
ATOM    837  CG1 VAL A  98      51.474  22.638  11.809  1.00 19.74           C  
ATOM    838  CG2 VAL A  98      50.948  22.539   9.320  1.00 16.16           C  
ATOM    839  N   GLU A  99      51.794  18.832   9.374  1.00 18.42           N  
ATOM    840  CA  GLU A  99      51.316  17.965   8.314  1.00 20.58           C  
ATOM    841  C   GLU A  99      50.093  18.581   7.637  1.00 17.60           C  
ATOM    842  O   GLU A  99      49.958  18.534   6.397  1.00 16.17           O  
ATOM    843  CB  GLU A  99      50.923  16.593   8.866  1.00 21.16           C  
ATOM    844  CG  GLU A  99      50.614  15.567   7.786  1.00 30.85           C  
ATOM    845  CD  GLU A  99      49.396  14.651   8.067  1.00 41.10           C  
ATOM    846  OE1 GLU A  99      48.393  15.089   8.705  1.00 38.93           O  
ATOM    847  OE2 GLU A  99      49.437  13.491   7.583  1.00 40.81           O  
ATOM    848  N   CYS A 100      49.178  19.104   8.450  1.00 16.66           N  
ATOM    849  CA  CYS A 100      48.062  19.871   7.924  1.00 16.22           C  
ATOM    850  C   CYS A 100      47.449  20.688   9.025  1.00 14.83           C  
ATOM    851  O   CYS A 100      47.742  20.484  10.206  1.00 14.26           O  
ATOM    852  CB  CYS A 100      46.996  18.992   7.285  1.00 19.08           C  
ATOM    853  SG  CYS A 100      46.097  17.924   8.409  1.00 24.61           S  
HETATM  854  N   MSE A 101      46.651  21.668   8.636  1.00 14.99           N  
HETATM  855  CA  MSE A 101      45.951  22.499   9.596  1.00 17.53           C  
HETATM  856  C   MSE A 101      44.895  23.321   8.890  1.00 15.69           C  
HETATM  857  O   MSE A 101      44.863  23.391   7.670  1.00 15.24           O  
HETATM  858  CB  MSE A 101      46.916  23.398  10.392  1.00 18.92           C  
HETATM  859  CG  MSE A 101      47.471  24.542   9.682  1.00 19.79           C  
HETATM  860 SE   MSE A 101      48.610  25.666  10.930  1.00 30.91          SE  
HETATM  861  CE  MSE A 101      47.873  25.434  12.347  1.00 23.86           C  
ATOM    862  N   GLY A 102      44.018  23.929   9.683  1.00 15.44           N  
ATOM    863  CA  GLY A 102      42.999  24.869   9.196  1.00 14.46           C  
ATOM    864  C   GLY A 102      43.033  26.125  10.035  1.00 13.96           C  
ATOM    865  O   GLY A 102      43.404  26.080  11.215  1.00 15.41           O  
ATOM    866  N   ILE A 103      42.657  27.246   9.416  1.00 13.48           N  
ATOM    867  CA  ILE A 103      42.641  28.527  10.077  1.00 15.07           C  
ATOM    868  C   ILE A 103      41.332  29.188   9.778  1.00 16.31           C  
ATOM    869  O   ILE A 103      40.941  29.223   8.623  1.00 15.91           O  
ATOM    870  CB  ILE A 103      43.807  29.435   9.582  1.00 15.06           C  
ATOM    871  CG1 ILE A 103      45.147  28.750   9.871  1.00 18.04           C  
ATOM    872  CG2 ILE A 103      43.692  30.851  10.227  1.00 16.77           C  
ATOM    873  CD1 ILE A 103      46.319  29.602   9.464  1.00 20.64           C  
ATOM    874  N   ILE A 104      40.634  29.673  10.803  1.00 13.40           N  
ATOM    875  CA  ILE A 104      39.360  30.430  10.645  1.00 14.88           C  
ATOM    876  C   ILE A 104      39.610  31.884  11.023  1.00 16.20           C  
ATOM    877  O   ILE A 104      40.231  32.165  12.067  1.00 14.96           O  
ATOM    878  CB  ILE A 104      38.218  29.871  11.551  1.00 15.68           C  
ATOM    879  CG1 ILE A 104      38.002  28.361  11.374  1.00 17.89           C  
ATOM    880  CG2 ILE A 104      36.950  30.686  11.324  1.00 17.12           C  
ATOM    881  CD1 ILE A 104      37.105  27.765  12.507  1.00 17.71           C  
ATOM    882  N   GLY A 105      39.137  32.826  10.204  1.00 13.30           N  
ATOM    883  CA  GLY A 105      39.226  34.240  10.543  1.00 14.15           C  
ATOM    884  C   GLY A 105      38.380  35.084   9.628  1.00 14.70           C  
ATOM    885  O   GLY A 105      37.463  34.587   8.984  1.00 15.12           O  
ATOM    886  N   LYS A 106      38.712  36.360   9.567  1.00 16.55           N  
ATOM    887  CA  LYS A 106      38.141  37.248   8.536  1.00 15.05           C  
ATOM    888  C   LYS A 106      39.221  38.032   7.819  1.00 15.66           C  
ATOM    889  O   LYS A 106      40.236  38.408   8.410  1.00 14.18           O  
ATOM    890  CB  LYS A 106      37.074  38.191   9.116  1.00 17.77           C  
ATOM    891  CG  LYS A 106      37.528  39.195  10.078  1.00 17.74           C  
ATOM    892  CD  LYS A 106      36.427  40.196  10.491  1.00 18.47           C  
ATOM    893  CE  LYS A 106      36.883  41.082  11.658  1.00 20.00           C  
ATOM    894  NZ  LYS A 106      35.900  42.063  12.168  1.00 22.63           N  
ATOM    895  N   GLY A 107      38.965  38.280   6.535  1.00 14.77           N  
ATOM    896  CA  GLY A 107      39.722  39.235   5.725  1.00 15.93           C  
ATOM    897  C   GLY A 107      40.867  38.642   4.962  1.00 16.01           C  
ATOM    898  O   GLY A 107      41.467  39.306   4.120  1.00 18.26           O  
ATOM    899  N   GLY A 108      41.190  37.386   5.268  1.00 15.18           N  
ATOM    900  CA  GLY A 108      42.241  36.667   4.548  1.00 17.03           C  
ATOM    901  C   GLY A 108      43.668  36.931   4.983  1.00 16.26           C  
ATOM    902  O   GLY A 108      43.929  37.639   5.959  1.00 16.61           O  
HETATM  903  N   MSE A 109      44.592  36.312   4.258  1.00 14.83           N  
HETATM  904  CA  MSE A 109      45.997  36.290   4.629  1.00 14.60           C  
HETATM  905  C   MSE A 109      46.868  36.508   3.379  1.00 14.33           C  
HETATM  906  O   MSE A 109      46.368  36.519   2.231  1.00 14.99           O  
HETATM  907  CB  MSE A 109      46.325  35.006   5.365  1.00 17.29           C  
HETATM  908  CG  MSE A 109      45.435  34.841   6.599  1.00 14.60           C  
HETATM  909 SE   MSE A 109      46.059  33.491   7.865  1.00 19.95          SE  
HETATM  910  CE  MSE A 109      47.486  34.588   8.786  1.00 18.24           C  
ATOM    911  N   SER A 110      48.147  36.757   3.601  1.00 15.57           N  
ATOM    912  CA  SER A 110      49.067  37.192   2.553  1.00 16.59           C  
ATOM    913  C   SER A 110      49.405  36.100   1.557  1.00 16.00           C  
ATOM    914  O   SER A 110      49.205  34.919   1.825  1.00 15.06           O  
ATOM    915  CB  SER A 110      50.371  37.610   3.228  1.00 17.75           C  
ATOM    916  OG  SER A 110      51.008  36.455   3.790  1.00 16.89           O  
ATOM    917  N   GLU A 111      50.034  36.490   0.453  1.00 14.80           N  
ATOM    918  CA  GLU A 111      50.474  35.493  -0.515  1.00 16.70           C  
ATOM    919  C   GLU A 111      51.543  34.564   0.085  1.00 14.25           C  
ATOM    920  O   GLU A 111      51.601  33.404  -0.298  1.00 14.68           O  
ATOM    921  CB  GLU A 111      50.947  36.137  -1.812  1.00 19.23           C  
ATOM    922  CG  GLU A 111      49.847  36.825  -2.589  1.00 20.84           C  
ATOM    923  CD  GLU A 111      48.804  35.845  -3.216  1.00 38.67           C  
ATOM    924  OE1 GLU A 111      49.011  34.599  -3.225  1.00 22.75           O  
ATOM    925  OE2 GLU A 111      47.770  36.335  -3.717  1.00 33.56           O  
ATOM    926  N   GLU A 112      52.341  35.036   1.057  1.00 16.95           N  
ATOM    927  CA AGLU A 112      53.327  34.165   1.716  0.50 17.83           C  
ATOM    928  CA BGLU A 112      53.321  34.158   1.709  0.50 16.80           C  
ATOM    929  C   GLU A 112      52.598  33.036   2.434  1.00 17.00           C  
ATOM    930  O   GLU A 112      53.019  31.891   2.420  1.00 17.15           O  
ATOM    931  CB AGLU A 112      54.206  34.953   2.716  0.50 19.67           C  
ATOM    932  CB BGLU A 112      54.210  34.939   2.694  0.50 19.09           C  
ATOM    933  CG AGLU A 112      55.407  34.163   3.250  0.50 17.86           C  
ATOM    934  CG BGLU A 112      55.134  35.919   2.018  0.50 17.10           C  
ATOM    935  CD AGLU A 112      56.157  34.874   4.384  0.50 22.26           C  
ATOM    936  OE1AGLU A 112      55.699  35.952   4.841  0.50 23.87           O  
ATOM    937  OE2AGLU A 112      57.199  34.337   4.831  0.50 24.40           O  
ATOM    938  N   VAL A 113      51.500  33.374   3.088  1.00 13.37           N  
ATOM    939  CA  VAL A 113      50.676  32.372   3.759  1.00 14.67           C  
ATOM    940  C   VAL A 113      50.057  31.436   2.736  1.00 12.75           C  
ATOM    941  O   VAL A 113      50.054  30.224   2.940  1.00 14.09           O  
ATOM    942  CB  VAL A 113      49.642  32.987   4.705  1.00 16.36           C  
ATOM    943  CG1 VAL A 113      48.601  31.933   5.191  1.00 17.09           C  
ATOM    944  CG2 VAL A 113      50.400  33.679   5.888  1.00 15.00           C  
ATOM    945  N   VAL A 114      49.501  31.983   1.652  1.00 13.67           N  
ATOM    946  CA  VAL A 114      48.946  31.121   0.605  1.00 13.69           C  
ATOM    947  C   VAL A 114      49.966  30.052   0.155  1.00 14.56           C  
ATOM    948  O   VAL A 114      49.657  28.850   0.039  1.00 14.66           O  
ATOM    949  CB  VAL A 114      48.429  31.949  -0.576  1.00 13.61           C  
ATOM    950  CG1 VAL A 114      47.979  31.057  -1.738  1.00 17.98           C  
ATOM    951  CG2 VAL A 114      47.283  32.874  -0.124  1.00 14.55           C  
ATOM    952  N   GLU A 115      51.189  30.481  -0.115  1.00 15.43           N  
ATOM    953  CA AGLU A 115      52.248  29.568  -0.530  0.50 16.16           C  
ATOM    954  CA BGLU A 115      52.230  29.553  -0.536  0.50 16.10           C  
ATOM    955  C   GLU A 115      52.568  28.542   0.563  1.00 13.36           C  
ATOM    956  O   GLU A 115      52.737  27.371   0.277  1.00 15.65           O  
ATOM    957  CB AGLU A 115      53.511  30.346  -0.909  0.50 17.60           C  
ATOM    958  CB BGLU A 115      53.472  30.313  -0.995  0.50 17.68           C  
ATOM    959  CG AGLU A 115      54.623  29.487  -1.497  0.50 20.25           C  
ATOM    960  CG BGLU A 115      53.210  31.151  -2.234  0.50 18.94           C  
ATOM    961  CD AGLU A 115      54.161  28.621  -2.660  0.50 24.57           C  
ATOM    962  CD BGLU A 115      52.748  30.317  -3.401  0.50 27.72           C  
ATOM    963  OE1AGLU A 115      53.370  29.120  -3.482  0.50 19.78           O  
ATOM    964  OE1BGLU A 115      53.544  29.462  -3.847  0.50 36.84           O  
ATOM    965  OE2AGLU A 115      54.587  27.448  -2.757  0.50 27.24           O  
ATOM    966  OE2BGLU A 115      51.587  30.489  -3.852  0.50 31.77           O  
ATOM    967  N   ALA A 116      52.642  28.995   1.813  1.00 13.42           N  
ATOM    968  CA  ALA A 116      52.965  28.124   2.931  1.00 13.90           C  
ATOM    969  C   ALA A 116      51.883  27.084   3.170  1.00 14.71           C  
ATOM    970  O   ALA A 116      52.137  26.057   3.749  1.00 16.12           O  
ATOM    971  CB  ALA A 116      53.196  28.951   4.217  1.00 15.30           C  
HETATM  972  N   MSE A 117      50.651  27.393   2.752  1.00 15.05           N  
HETATM  973  CA  MSE A 117      49.530  26.472   2.859  1.00 15.49           C  
HETATM  974  C   MSE A 117      49.521  25.401   1.780  1.00 15.79           C  
HETATM  975  O   MSE A 117      48.801  24.410   1.917  1.00 13.50           O  
HETATM  976  CB  MSE A 117      48.195  27.237   2.874  1.00 14.37           C  
HETATM  977  CG  MSE A 117      47.977  27.955   4.121  1.00 14.25           C  
HETATM  978 SE   MSE A 117      46.108  28.636   4.137  1.00 21.02          SE  
HETATM  979  CE  MSE A 117      46.129  29.073   6.123  1.00 18.96           C  
ATOM    980  N   ARG A 118      50.310  25.580   0.716  1.00 14.45           N  
ATOM    981  CA  ARG A 118      50.272  24.651  -0.407  1.00 15.91           C  
ATOM    982  C   ARG A 118      50.531  23.211   0.081  1.00 15.29           C  
ATOM    983  O   ARG A 118      51.524  22.938   0.741  1.00 14.63           O  
ATOM    984  CB  ARG A 118      51.301  25.055  -1.474  1.00 16.86           C  
ATOM    985  CG  ARG A 118      51.097  24.421  -2.803  1.00 27.50           C  
ATOM    986  CD  ARG A 118      52.144  24.942  -3.812  1.00 22.91           C  
ATOM    987  NE  ARG A 118      51.924  26.331  -4.246  1.00 27.62           N  
ATOM    988  CZ  ARG A 118      51.099  26.689  -5.232  1.00 25.81           C  
ATOM    989  NH1 ARG A 118      50.346  25.794  -5.826  1.00 26.26           N  
ATOM    990  NH2 ARG A 118      50.988  27.961  -5.593  1.00 33.60           N  
ATOM    991  N   GLY A 119      49.629  22.303  -0.280  1.00 15.78           N  
ATOM    992  CA  GLY A 119      49.746  20.907   0.066  1.00 16.46           C  
ATOM    993  C   GLY A 119      49.440  20.550   1.495  1.00 14.99           C  
ATOM    994  O   GLY A 119      49.616  19.360   1.859  1.00 16.52           O  
ATOM    995  N   LYS A 120      48.981  21.513   2.310  1.00 15.62           N  
ATOM    996  CA  LYS A 120      48.779  21.212   3.729  1.00 17.02           C  
ATOM    997  C   LYS A 120      47.646  21.889   4.482  1.00 15.92           C  
ATOM    998  O   LYS A 120      47.232  21.393   5.499  1.00 16.31           O  
ATOM    999  CB  LYS A 120      50.106  21.391   4.500  1.00 17.82           C  
ATOM   1000  CG  LYS A 120      50.621  22.776   4.552  1.00 21.16           C  
ATOM   1001  CD  LYS A 120      51.821  22.914   5.513  1.00 21.13           C  
ATOM   1002  CE  LYS A 120      53.019  22.164   5.062  1.00 20.46           C  
ATOM   1003  NZ  LYS A 120      54.188  22.264   6.037  1.00 22.10           N  
ATOM   1004  N   ALA A 121      47.162  23.031   4.030  1.00 13.61           N  
ATOM   1005  CA  ALA A 121      46.234  23.789   4.865  1.00 12.16           C  
ATOM   1006  C   ALA A 121      45.237  24.570   4.039  1.00 13.37           C  
ATOM   1007  O   ALA A 121      45.382  24.708   2.827  1.00 14.89           O  
ATOM   1008  CB  ALA A 121      46.994  24.696   5.835  1.00 15.37           C  
ATOM   1009  N   ALA A 122      44.202  25.008   4.733  1.00 15.68           N  
ATOM   1010  CA  ALA A 122      43.172  25.877   4.188  1.00 16.36           C  
ATOM   1011  C   ALA A 122      42.813  26.970   5.200  1.00 15.11           C  
ATOM   1012  O   ALA A 122      42.969  26.811   6.425  1.00 14.40           O  
ATOM   1013  CB  ALA A 122      41.925  25.096   3.765  1.00 15.20           C  
ATOM   1014  N   TYR A 123      42.303  28.056   4.641  1.00 13.47           N  
ATOM   1015  CA  TYR A 123      41.793  29.199   5.373  1.00 12.95           C  
ATOM   1016  C   TYR A 123      40.283  29.301   5.131  1.00 15.11           C  
ATOM   1017  O   TYR A 123      39.816  29.303   3.961  1.00 14.13           O  
ATOM   1018  CB  TYR A 123      42.477  30.467   4.927  1.00 15.49           C  
ATOM   1019  CG  TYR A 123      41.994  31.711   5.634  1.00 15.29           C  
ATOM   1020  CD1 TYR A 123      42.530  32.099   6.827  1.00 16.32           C  
ATOM   1021  CD2 TYR A 123      41.015  32.511   5.086  1.00 16.39           C  
ATOM   1022  CE1 TYR A 123      42.100  33.274   7.483  1.00 13.79           C  
ATOM   1023  CE2 TYR A 123      40.580  33.677   5.726  1.00 15.80           C  
ATOM   1024  CZ  TYR A 123      41.105  34.039   6.933  1.00 15.14           C  
ATOM   1025  OH  TYR A 123      40.688  35.206   7.527  1.00 16.64           O  
ATOM   1026  N   PHE A 124      39.559  29.395   6.244  1.00 13.48           N  
ATOM   1027  CA  PHE A 124      38.101  29.417   6.273  1.00 14.82           C  
ATOM   1028  C   PHE A 124      37.659  30.830   6.696  1.00 16.19           C  
ATOM   1029  O   PHE A 124      37.969  31.288   7.814  1.00 14.93           O  
ATOM   1030  CB  PHE A 124      37.569  28.396   7.257  1.00 14.89           C  
ATOM   1031  CG  PHE A 124      38.138  27.008   7.076  1.00 15.60           C  
ATOM   1032  CD1 PHE A 124      38.033  26.383   5.887  1.00 20.67           C  
ATOM   1033  CD2 PHE A 124      38.774  26.349   8.106  1.00 21.44           C  
ATOM   1034  CE1 PHE A 124      38.571  25.090   5.712  1.00 21.37           C  
ATOM   1035  CE2 PHE A 124      39.295  25.069   7.934  1.00 21.93           C  
ATOM   1036  CZ  PHE A 124      39.195  24.466   6.725  1.00 20.22           C  
ATOM   1037  N   ALA A 125      36.987  31.530   5.793  1.00 15.38           N  
ATOM   1038  CA  ALA A 125      36.410  32.848   6.070  1.00 12.75           C  
ATOM   1039  C   ALA A 125      35.126  32.642   6.869  1.00 13.24           C  
ATOM   1040  O   ALA A 125      34.185  32.037   6.396  1.00 15.93           O  
ATOM   1041  CB  ALA A 125      36.106  33.623   4.751  1.00 13.04           C  
ATOM   1042  N   PHE A 126      35.095  33.129   8.087  1.00 14.97           N  
ATOM   1043  CA  PHE A 126      33.918  32.975   8.926  1.00 16.63           C  
ATOM   1044  C   PHE A 126      32.762  33.808   8.347  1.00 17.29           C  
ATOM   1045  O   PHE A 126      32.923  35.008   8.066  1.00 18.19           O  
ATOM   1046  CB  PHE A 126      34.234  33.464  10.317  1.00 17.91           C  
ATOM   1047  CG  PHE A 126      33.101  33.334  11.286  1.00 15.68           C  
ATOM   1048  CD1 PHE A 126      32.752  32.083  11.768  1.00 24.53           C  
ATOM   1049  CD2 PHE A 126      32.371  34.450  11.692  1.00 19.53           C  
ATOM   1050  CE1 PHE A 126      31.739  31.933  12.682  1.00 31.16           C  
ATOM   1051  CE2 PHE A 126      31.339  34.292  12.627  1.00 20.44           C  
ATOM   1052  CZ  PHE A 126      31.027  33.031  13.091  1.00 21.98           C  
ATOM   1053  N   THR A 127      31.598  33.175   8.204  1.00 14.97           N  
ATOM   1054  CA  THR A 127      30.410  33.879   7.694  1.00 18.95           C  
ATOM   1055  C   THR A 127      29.216  33.537   8.579  1.00 19.34           C  
ATOM   1056  O   THR A 127      28.085  33.478   8.112  1.00 24.03           O  
ATOM   1057  CB  THR A 127      30.147  33.521   6.209  1.00 20.87           C  
ATOM   1058  OG1 THR A 127      30.015  32.093   6.055  1.00 21.76           O  
ATOM   1059  CG2 THR A 127      31.302  34.040   5.320  1.00 19.30           C  
ATOM   1060  N   GLY A 128      29.471  33.358   9.865  1.00 18.26           N  
ATOM   1061  CA  GLY A 128      28.420  32.942  10.804  1.00 20.86           C  
ATOM   1062  C   GLY A 128      27.844  34.039  11.684  1.00 22.10           C  
ATOM   1063  O   GLY A 128      27.332  33.743  12.781  1.00 22.80           O  
ATOM   1064  N   GLY A 129      27.940  35.291  11.240  1.00 24.06           N  
ATOM   1065  CA  GLY A 129      27.329  36.423  11.957  1.00 21.86           C  
ATOM   1066  C   GLY A 129      28.276  37.167  12.878  1.00 21.27           C  
ATOM   1067  O   GLY A 129      29.495  37.145  12.689  1.00 23.63           O  
ATOM   1068  N   ALA A 130      27.728  37.819  13.891  1.00 17.69           N  
ATOM   1069  CA  ALA A 130      28.517  38.716  14.740  1.00 17.57           C  
ATOM   1070  C   ALA A 130      29.364  38.005  15.794  1.00 18.45           C  
ATOM   1071  O   ALA A 130      30.260  38.618  16.406  1.00 18.36           O  
ATOM   1072  CB  ALA A 130      27.587  39.750  15.422  1.00 16.86           C  
ATOM   1073  N   GLY A 131      29.033  36.738  16.065  1.00 17.45           N  
ATOM   1074  CA  GLY A 131      29.734  35.947  17.067  1.00 16.96           C  
ATOM   1075  C   GLY A 131      28.902  35.424  18.236  1.00 17.58           C  
ATOM   1076  O   GLY A 131      29.332  34.463  18.892  1.00 18.23           O  
ATOM   1077  N   ALA A 132      27.752  36.045  18.522  1.00 16.14           N  
ATOM   1078  CA  ALA A 132      26.932  35.633  19.659  1.00 16.80           C  
ATOM   1079  C   ALA A 132      26.208  34.323  19.350  1.00 18.12           C  
ATOM   1080  O   ALA A 132      26.331  33.336  20.084  1.00 18.03           O  
ATOM   1081  CB  ALA A 132      25.936  36.714  20.061  1.00 15.10           C  
ATOM   1082  N   LEU A 133      25.468  34.311  18.256  1.00 16.95           N  
ATOM   1083  CA  LEU A 133      24.750  33.096  17.850  1.00 17.31           C  
ATOM   1084  C   LEU A 133      25.746  31.971  17.510  1.00 17.58           C  
ATOM   1085  O   LEU A 133      25.507  30.813  17.834  1.00 19.56           O  
ATOM   1086  CB  LEU A 133      23.789  33.380  16.700  1.00 18.75           C  
ATOM   1087  CG  LEU A 133      22.626  34.302  17.115  1.00 20.47           C  
ATOM   1088  CD1 LEU A 133      21.718  34.604  15.907  1.00 25.09           C  
ATOM   1089  CD2 LEU A 133      21.813  33.784  18.327  1.00 26.20           C  
ATOM   1090  N   ALA A 134      26.889  32.317  16.927  1.00 18.54           N  
ATOM   1091  CA  ALA A 134      27.921  31.314  16.575  1.00 19.69           C  
ATOM   1092  C   ALA A 134      28.429  30.583  17.819  1.00 19.92           C  
ATOM   1093  O   ALA A 134      28.706  29.367  17.765  1.00 22.41           O  
ATOM   1094  CB  ALA A 134      29.061  31.982  15.877  1.00 20.62           C  
ATOM   1095  N   ALA A 135      28.494  31.312  18.941  1.00 17.93           N  
ATOM   1096  CA  ALA A 135      28.962  30.758  20.207  1.00 19.05           C  
ATOM   1097  C   ALA A 135      28.089  29.617  20.696  1.00 17.81           C  
ATOM   1098  O   ALA A 135      28.540  28.797  21.508  1.00 17.18           O  
ATOM   1099  CB  ALA A 135      29.062  31.806  21.266  1.00 19.66           C  
HETATM 1100  N   MSE A 136      26.848  29.545  20.222  1.00 18.97           N  
HETATM 1101  CA AMSE A 136      25.979  28.474  20.670  0.50 17.18           C  
HETATM 1102  CA BMSE A 136      25.905  28.472  20.568  0.50 24.13           C  
HETATM 1103  C   MSE A 136      26.394  27.116  20.105  1.00 18.60           C  
HETATM 1104  O   MSE A 136      25.971  26.083  20.631  1.00 19.87           O  
HETATM 1105  CB AMSE A 136      24.517  28.826  20.369  0.50 16.31           C  
HETATM 1106  CB BMSE A 136      24.531  28.722  19.912  0.50 23.35           C  
HETATM 1107  CG AMSE A 136      24.097  30.136  21.000  0.50 16.36           C  
HETATM 1108  CG BMSE A 136      23.372  28.945  20.849  0.50 29.65           C  
HETATM 1109 SE  AMSE A 136      24.221  30.097  22.955  0.50 35.07          SE  
HETATM 1110 SE  BMSE A 136      21.951  29.948  19.921  0.50 45.46          SE  
HETATM 1111  CE AMSE A 136      26.114  30.588  23.267  0.50 27.75           C  
HETATM 1112  CE BMSE A 136      22.343  31.579  20.783  0.50  5.68           C  
ATOM   1113  N   SER A 137      27.271  27.115  19.096  1.00 16.98           N  
ATOM   1114  CA ASER A 137      27.844  25.874  18.562  0.50 17.00           C  
ATOM   1115  CA BSER A 137      27.844  25.878  18.558  0.50 17.95           C  
ATOM   1116  C   SER A 137      29.033  25.371  19.392  1.00 18.76           C  
ATOM   1117  O   SER A 137      29.581  24.307  19.137  1.00 17.82           O  
ATOM   1118  CB ASER A 137      28.262  26.088  17.114  0.50 17.82           C  
ATOM   1119  CB BSER A 137      28.273  26.112  17.116  0.50 18.88           C  
ATOM   1120  OG ASER A 137      27.132  26.329  16.305  0.50 17.30           O  
ATOM   1121  OG BSER A 137      29.485  26.841  17.072  0.50 25.75           O  
ATOM   1122  N   ILE A 138      29.452  26.152  20.379  1.00 16.37           N  
ATOM   1123  CA  ILE A 138      30.494  25.750  21.278  1.00 16.94           C  
ATOM   1124  C   ILE A 138      29.811  25.027  22.439  1.00 18.17           C  
ATOM   1125  O   ILE A 138      29.033  25.627  23.192  1.00 17.39           O  
ATOM   1126  CB  ILE A 138      31.277  26.951  21.791  1.00 18.13           C  
ATOM   1127  CG1 ILE A 138      31.902  27.712  20.618  1.00 20.64           C  
ATOM   1128  CG2 ILE A 138      32.322  26.490  22.832  1.00 16.13           C  
ATOM   1129  CD1 ILE A 138      32.362  29.087  20.966  1.00 20.98           C  
ATOM   1130  N   LYS A 139      30.108  23.746  22.590  1.00 17.36           N  
ATOM   1131  CA  LYS A 139      29.454  22.919  23.575  1.00 18.09           C  
ATOM   1132  C   LYS A 139      30.190  22.872  24.896  1.00 17.10           C  
ATOM   1133  O   LYS A 139      29.564  22.635  25.928  1.00 21.33           O  
ATOM   1134  CB  LYS A 139      29.273  21.510  23.025  1.00 18.86           C  
ATOM   1135  CG  LYS A 139      28.522  21.457  21.695  1.00 26.57           C  
ATOM   1136  CD  LYS A 139      27.163  22.188  21.776  1.00 31.31           C  
ATOM   1137  CE  LYS A 139      26.550  22.450  20.410  1.00 32.59           C  
ATOM   1138  NZ  LYS A 139      25.195  23.025  20.553  1.00 36.60           N  
ATOM   1139  N   LYS A 140      31.506  23.019  24.878  1.00 17.92           N  
ATOM   1140  CA  LYS A 140      32.292  22.958  26.100  1.00 18.84           C  
ATOM   1141  C   LYS A 140      33.578  23.741  25.928  1.00 19.12           C  
ATOM   1142  O   LYS A 140      34.162  23.731  24.860  1.00 18.31           O  
ATOM   1143  CB  LYS A 140      32.612  21.484  26.425  1.00 19.26           C  
ATOM   1144  CG  LYS A 140      33.326  21.262  27.747  1.00 26.16           C  
ATOM   1145  CD  LYS A 140      33.473  19.755  28.038  1.00 26.28           C  
ATOM   1146  CE  LYS A 140      34.471  19.498  29.181  1.00 37.40           C  
ATOM   1147  NZ  LYS A 140      34.417  18.078  29.688  1.00 42.33           N  
ATOM   1148  N   VAL A 141      34.002  24.422  26.989  1.00 16.87           N  
ATOM   1149  CA  VAL A 141      35.351  24.919  27.094  1.00 15.87           C  
ATOM   1150  C   VAL A 141      36.152  23.802  27.756  1.00 16.00           C  
ATOM   1151  O   VAL A 141      35.954  23.489  28.945  1.00 17.71           O  
ATOM   1152  CB  VAL A 141      35.419  26.230  27.920  1.00 13.83           C  
ATOM   1153  CG1 VAL A 141      36.879  26.678  28.102  1.00 17.36           C  
ATOM   1154  CG2 VAL A 141      34.560  27.312  27.246  1.00 18.67           C  
ATOM   1155  N   LYS A 142      36.996  23.154  26.977  1.00 16.87           N  
ATOM   1156  CA ALYS A 142      37.851  22.085  27.491  0.50 17.98           C  
ATOM   1157  CA BLYS A 142      37.859  22.084  27.492  0.50 17.89           C  
ATOM   1158  C   LYS A 142      38.902  22.626  28.464  1.00 19.40           C  
ATOM   1159  O   LYS A 142      39.227  21.996  29.473  1.00 18.53           O  
ATOM   1160  CB ALYS A 142      38.515  21.350  26.321  0.50 18.43           C  
ATOM   1161  CB BLYS A 142      38.547  21.363  26.327  0.50 18.35           C  
ATOM   1162  CG ALYS A 142      37.541  20.555  25.442  0.50 21.52           C  
ATOM   1163  CG BLYS A 142      39.375  20.139  26.741  0.50 20.87           C  
ATOM   1164  N   GLY A 143      39.443  23.790  28.165  1.00 19.22           N  
ATOM   1165  CA  GLY A 143      40.364  24.449  29.068  1.00 20.15           C  
ATOM   1166  C   GLY A 143      40.837  25.741  28.460  1.00 17.72           C  
ATOM   1167  O   GLY A 143      40.379  26.121  27.383  1.00 16.40           O  
ATOM   1168  N   VAL A 144      41.760  26.395  29.152  1.00 19.25           N  
ATOM   1169  CA  VAL A 144      42.351  27.636  28.681  1.00 17.18           C  
ATOM   1170  C   VAL A 144      43.818  27.629  29.076  1.00 18.74           C  
ATOM   1171  O   VAL A 144      44.168  27.168  30.171  1.00 16.94           O  
ATOM   1172  CB  VAL A 144      41.625  28.869  29.214  1.00 16.77           C  
ATOM   1173  CG1 VAL A 144      41.647  28.949  30.749  1.00 21.37           C  
ATOM   1174  CG2 VAL A 144      42.206  30.146  28.608  1.00 18.40           C  
ATOM   1175  N   VAL A 145      44.665  28.082  28.157  1.00 18.34           N  
ATOM   1176  CA  VAL A 145      46.057  28.205  28.461  1.00 20.70           C  
ATOM   1177  C   VAL A 145      46.536  29.628  28.194  1.00 17.99           C  
ATOM   1178  O   VAL A 145      45.896  30.405  27.456  1.00 16.48           O  
ATOM   1179  CB  VAL A 145      46.906  27.112  27.777  1.00 26.70           C  
ATOM   1180  CG1 VAL A 145      46.348  25.699  28.089  1.00 27.92           C  
ATOM   1181  CG2 VAL A 145      46.950  27.333  26.366  1.00 19.63           C  
ATOM   1182  N   TRP A 146      47.619  29.981  28.881  1.00 16.12           N  
ATOM   1183  CA  TRP A 146      48.178  31.315  28.769  1.00 15.30           C  
ATOM   1184  C   TRP A 146      47.151  32.382  29.151  1.00 15.73           C  
ATOM   1185  O   TRP A 146      47.000  33.422  28.498  1.00 15.58           O  
ATOM   1186  CB  TRP A 146      48.771  31.530  27.372  1.00 16.73           C  
ATOM   1187  CG  TRP A 146      49.940  30.691  27.053  1.00 16.39           C  
ATOM   1188  CD1 TRP A 146      50.701  29.945  27.926  1.00 18.64           C  
ATOM   1189  CD2 TRP A 146      50.537  30.517  25.762  1.00 13.08           C  
ATOM   1190  NE1 TRP A 146      51.724  29.330  27.254  1.00 16.07           N  
ATOM   1191  CE2 TRP A 146      51.650  29.654  25.927  1.00 14.33           C  
ATOM   1192  CE3 TRP A 146      50.242  31.007  24.487  1.00 15.35           C  
ATOM   1193  CZ2 TRP A 146      52.469  29.284  24.865  1.00 14.78           C  
ATOM   1194  CZ3 TRP A 146      51.051  30.627  23.439  1.00 18.59           C  
ATOM   1195  CH2 TRP A 146      52.136  29.770  23.629  1.00 19.92           C  
ATOM   1196  N   GLU A 147      46.441  32.120  30.246  1.00 15.87           N  
ATOM   1197  CA  GLU A 147      45.415  33.055  30.740  1.00 16.61           C  
ATOM   1198  C   GLU A 147      45.993  34.389  31.167  1.00 15.98           C  
ATOM   1199  O   GLU A 147      45.287  35.384  31.233  1.00 19.09           O  
ATOM   1200  CB  GLU A 147      44.685  32.484  31.948  1.00 20.56           C  
ATOM   1201  CG  GLU A 147      43.643  31.490  31.654  1.00 26.76           C  
ATOM   1202  CD  GLU A 147      42.820  31.193  32.910  1.00 31.56           C  
ATOM   1203  OE1 GLU A 147      41.932  32.017  33.233  1.00 36.01           O  
ATOM   1204  OE2 GLU A 147      43.087  30.148  33.550  1.00 32.92           O  
ATOM   1205  N   ASP A 148      47.289  34.412  31.470  1.00 14.34           N  
ATOM   1206  CA  ASP A 148      47.979  35.628  31.840  1.00 16.96           C  
ATOM   1207  C   ASP A 148      48.044  36.665  30.711  1.00 16.15           C  
ATOM   1208  O   ASP A 148      48.305  37.843  30.957  1.00 18.70           O  
ATOM   1209  CB  ASP A 148      49.397  35.273  32.261  1.00 17.73           C  
ATOM   1210  CG  ASP A 148      50.184  34.572  31.153  1.00 20.68           C  
ATOM   1211  OD1 ASP A 148      49.865  33.408  30.790  1.00 20.77           O  
ATOM   1212  OD2 ASP A 148      51.124  35.204  30.644  1.00 27.10           O  
ATOM   1213  N   LEU A 149      47.794  36.230  29.472  1.00 17.26           N  
ATOM   1214  CA  LEU A 149      47.702  37.131  28.335  1.00 16.76           C  
ATOM   1215  C   LEU A 149      46.408  37.948  28.337  1.00 17.01           C  
ATOM   1216  O   LEU A 149      46.283  38.920  27.598  1.00 20.03           O  
ATOM   1217  CB  LEU A 149      47.813  36.348  27.026  1.00 17.25           C  
ATOM   1218  CG  LEU A 149      49.130  35.617  26.758  1.00 17.22           C  
ATOM   1219  CD1 LEU A 149      49.090  34.848  25.425  1.00 18.57           C  
ATOM   1220  CD2 LEU A 149      50.356  36.543  26.843  1.00 18.18           C  
ATOM   1221  N   GLY A 150      45.454  37.564  29.186  1.00 18.41           N  
ATOM   1222  CA  GLY A 150      44.182  38.238  29.313  1.00 19.73           C  
ATOM   1223  C   GLY A 150      43.148  37.473  28.518  1.00 19.77           C  
ATOM   1224  O   GLY A 150      43.486  36.745  27.577  1.00 18.61           O  
HETATM 1225  N   MSE A 151      41.876  37.642  28.869  1.00 19.15           N  
HETATM 1226  CA  MSE A 151      40.830  36.791  28.278  1.00 19.34           C  
HETATM 1227  C   MSE A 151      40.793  36.746  26.743  1.00 17.97           C  
HETATM 1228  O   MSE A 151      40.807  35.654  26.169  1.00 19.79           O  
HETATM 1229  CB  MSE A 151      39.452  37.161  28.827  1.00 19.63           C  
HETATM 1230  CG  MSE A 151      38.330  36.534  28.074  1.00 20.29           C  
HETATM 1231 SE   MSE A 151      36.626  36.996  28.925  1.00 32.21          SE  
HETATM 1232  CE  MSE A 151      37.015  36.086  30.768  1.00 30.17           C  
ATOM   1233  N   PRO A 152      40.748  37.902  26.062  1.00 17.72           N  
ATOM   1234  CA  PRO A 152      40.689  37.789  24.576  1.00 18.47           C  
ATOM   1235  C   PRO A 152      41.955  37.246  23.898  1.00 19.67           C  
ATOM   1236  O   PRO A 152      41.875  36.692  22.782  1.00 22.87           O  
ATOM   1237  CB  PRO A 152      40.406  39.219  24.130  1.00 23.13           C  
ATOM   1238  CG  PRO A 152      40.861  40.055  25.208  1.00 18.36           C  
ATOM   1239  CD  PRO A 152      40.716  39.295  26.498  1.00 21.27           C  
ATOM   1240  N   GLU A 153      43.110  37.374  24.559  1.00 15.20           N  
ATOM   1241  CA  GLU A 153      44.394  36.916  23.999  1.00 15.60           C  
ATOM   1242  C   GLU A 153      44.810  35.503  24.430  1.00 15.88           C  
ATOM   1243  O   GLU A 153      45.718  34.902  23.859  1.00 17.85           O  
ATOM   1244  CB  GLU A 153      45.493  37.922  24.358  1.00 15.57           C  
ATOM   1245  CG  GLU A 153      45.267  39.320  23.829  1.00 20.55           C  
ATOM   1246  CD  GLU A 153      45.461  39.469  22.328  1.00 24.09           C  
ATOM   1247  OE1 GLU A 153      46.223  38.686  21.702  1.00 20.52           O  
ATOM   1248  OE2 GLU A 153      44.840  40.400  21.758  1.00 25.52           O  
ATOM   1249  N   ALA A 154      44.152  34.964  25.447  1.00 15.09           N  
ATOM   1250  CA  ALA A 154      44.431  33.601  25.868  1.00 15.46           C  
ATOM   1251  C   ALA A 154      44.041  32.568  24.818  1.00 16.18           C  
ATOM   1252  O   ALA A 154      43.278  32.840  23.881  1.00 16.74           O  
ATOM   1253  CB  ALA A 154      43.740  33.317  27.187  1.00 14.65           C  
ATOM   1254  N   VAL A 155      44.605  31.373  24.952  1.00 13.69           N  
ATOM   1255  CA  VAL A 155      44.288  30.283  24.052  1.00 13.64           C  
ATOM   1256  C   VAL A 155      43.200  29.410  24.663  1.00 15.07           C  
ATOM   1257  O   VAL A 155      43.441  28.615  25.587  1.00 15.02           O  
ATOM   1258  CB  VAL A 155      45.561  29.475  23.686  1.00 14.78           C  
ATOM   1259  CG1 VAL A 155      45.207  28.259  22.829  1.00 16.67           C  
ATOM   1260  CG2 VAL A 155      46.565  30.381  22.957  1.00 16.11           C  
ATOM   1261  N   TRP A 156      42.008  29.568  24.117  1.00 14.53           N  
ATOM   1262  CA  TRP A 156      40.838  28.822  24.591  1.00 14.62           C  
ATOM   1263  C   TRP A 156      40.656  27.553  23.776  1.00 16.19           C  
ATOM   1264  O   TRP A 156      40.601  27.586  22.546  1.00 15.56           O  
ATOM   1265  CB  TRP A 156      39.598  29.698  24.524  1.00 15.14           C  
ATOM   1266  CG  TRP A 156      39.667  30.917  25.447  1.00 13.61           C  
ATOM   1267  CD1 TRP A 156      40.207  32.140  25.171  1.00 14.69           C  
ATOM   1268  CD2 TRP A 156      39.208  30.976  26.788  1.00 14.39           C  
ATOM   1269  NE1 TRP A 156      40.116  32.963  26.261  1.00 15.17           N  
ATOM   1270  CE2 TRP A 156      39.505  32.269  27.276  1.00 14.70           C  
ATOM   1271  CE3 TRP A 156      38.543  30.072  27.619  1.00 15.79           C  
ATOM   1272  CZ2 TRP A 156      39.156  32.672  28.564  1.00 15.66           C  
ATOM   1273  CZ3 TRP A 156      38.239  30.460  28.904  1.00 16.11           C  
ATOM   1274  CH2 TRP A 156      38.552  31.750  29.360  1.00 17.07           C  
ATOM   1275  N   LEU A 157      40.566  26.433  24.486  1.00 15.20           N  
ATOM   1276  CA  LEU A 157      40.405  25.120  23.893  1.00 16.37           C  
ATOM   1277  C   LEU A 157      38.916  24.785  23.925  1.00 16.12           C  
ATOM   1278  O   LEU A 157      38.343  24.605  24.998  1.00 15.63           O  
ATOM   1279  CB  LEU A 157      41.209  24.074  24.695  1.00 18.41           C  
ATOM   1280  CG  LEU A 157      42.632  24.458  25.141  1.00 26.03           C  
ATOM   1281  CD1 LEU A 157      43.300  23.267  25.898  1.00 25.91           C  
ATOM   1282  CD2 LEU A 157      43.487  24.893  23.949  1.00 24.72           C  
ATOM   1283  N   LEU A 158      38.300  24.678  22.748  1.00 17.76           N  
ATOM   1284  CA  LEU A 158      36.842  24.621  22.625  1.00 15.47           C  
ATOM   1285  C   LEU A 158      36.389  23.345  21.937  1.00 17.70           C  
ATOM   1286  O   LEU A 158      36.992  22.925  20.950  1.00 22.16           O  
ATOM   1287  CB  LEU A 158      36.326  25.830  21.824  1.00 15.91           C  
ATOM   1288  CG  LEU A 158      36.751  27.227  22.303  1.00 17.89           C  
ATOM   1289  CD1 LEU A 158      36.227  28.290  21.327  1.00 19.43           C  
ATOM   1290  CD2 LEU A 158      36.251  27.436  23.720  1.00 15.37           C  
ATOM   1291  N   GLU A 159      35.337  22.744  22.470  1.00 16.09           N  
ATOM   1292  CA AGLU A 159      34.663  21.615  21.833  0.50 16.91           C  
ATOM   1293  CA BGLU A 159      34.663  21.615  21.833  0.50 16.91           C  
ATOM   1294  C   GLU A 159      33.451  22.177  21.098  1.00 17.59           C  
ATOM   1295  O   GLU A 159      32.607  22.843  21.707  1.00 17.41           O  
ATOM   1296  CB AGLU A 159      34.238  20.584  22.884  0.50 17.57           C  
ATOM   1297  CB BGLU A 159      34.238  20.584  22.884  0.50 17.57           C  
ATOM   1298  N   VAL A 160      33.383  21.940  19.789  1.00 14.26           N  
ATOM   1299  CA  VAL A 160      32.355  22.572  18.953  1.00 15.18           C  
ATOM   1300  C   VAL A 160      31.577  21.533  18.152  1.00 16.99           C  
ATOM   1301  O   VAL A 160      32.079  20.425  17.889  1.00 17.12           O  
ATOM   1302  CB  VAL A 160      32.933  23.646  18.006  1.00 16.48           C  
ATOM   1303  CG1 VAL A 160      33.626  24.760  18.803  1.00 16.87           C  
ATOM   1304  CG2 VAL A 160      33.892  23.023  16.976  1.00 15.34           C  
ATOM   1305  N   GLU A 161      30.330  21.872  17.828  1.00 17.24           N  
ATOM   1306  CA AGLU A 161      29.534  21.051  16.916  0.50 17.74           C  
ATOM   1307  CA BGLU A 161      29.524  21.056  16.920  0.50 17.81           C  
ATOM   1308  C   GLU A 161      29.002  21.928  15.798  1.00 17.25           C  
ATOM   1309  O  AGLU A 161      28.245  22.848  16.054  1.00 17.72           O  
ATOM   1310  CB AGLU A 161      28.395  20.339  17.658  0.50 18.00           C  
ATOM   1311  CB BGLU A 161      28.353  20.378  17.639  0.50 18.51           C  
ATOM   1312  CG AGLU A 161      28.896  19.277  18.636  0.50 16.32           C  
ATOM   1313  CG BGLU A 161      27.543  19.450  16.735  0.50 21.71           C  
ATOM   1314  CD AGLU A 161      27.775  18.538  19.369  0.50 20.52           C  
ATOM   1315  OE1AGLU A 161      26.644  18.462  18.833  0.50 24.05           O  
ATOM   1316  OE2AGLU A 161      28.035  18.005  20.476  0.50 24.89           O  
ATOM   1317  N   ARG A 162      29.449  21.656  14.573  1.00 16.48           N  
ATOM   1318  CA  ARG A 162      29.055  22.421  13.395  1.00 16.60           C  
ATOM   1319  C   ARG A 162      29.256  23.922  13.600  1.00 16.64           C  
ATOM   1320  O   ARG A 162      28.352  24.735  13.385  1.00 18.15           O  
ATOM   1321  CB  ARG A 162      27.623  22.080  12.969  1.00 19.29           C  
ATOM   1322  CG  ARG A 162      27.558  20.672  12.411  1.00 23.48           C  
ATOM   1323  CD  ARG A 162      26.190  20.314  11.908  1.00 23.59           C  
ATOM   1324  NE  ARG A 162      25.735  21.208  10.852  1.00 26.04           N  
ATOM   1325  CZ  ARG A 162      26.013  21.058   9.558  1.00 29.24           C  
ATOM   1326  NH1 ARG A 162      26.759  20.051   9.129  1.00 26.91           N  
ATOM   1327  NH2 ARG A 162      25.539  21.922   8.682  1.00 29.50           N  
ATOM   1328  N   PHE A 163      30.458  24.256  14.027  1.00 17.26           N  
ATOM   1329  CA  PHE A 163      30.865  25.640  14.092  1.00 16.03           C  
ATOM   1330  C   PHE A 163      31.003  26.213  12.677  1.00 15.71           C  
ATOM   1331  O   PHE A 163      31.699  25.644  11.838  1.00 17.06           O  
ATOM   1332  CB  PHE A 163      32.176  25.797  14.854  1.00 18.68           C  
ATOM   1333  CG  PHE A 163      32.515  27.227  15.136  1.00 18.49           C  
ATOM   1334  CD1 PHE A 163      31.932  27.876  16.209  1.00 19.79           C  
ATOM   1335  CD2 PHE A 163      33.355  27.932  14.313  1.00 23.45           C  
ATOM   1336  CE1 PHE A 163      32.223  29.195  16.484  1.00 23.24           C  
ATOM   1337  CE2 PHE A 163      33.629  29.279  14.576  1.00 26.34           C  
ATOM   1338  CZ  PHE A 163      33.051  29.889  15.660  1.00 23.72           C  
ATOM   1339  N   GLY A 164      30.419  27.382  12.442  1.00 16.29           N  
ATOM   1340  CA  GLY A 164      30.361  27.958  11.110  1.00 16.36           C  
ATOM   1341  C   GLY A 164      29.025  28.603  10.836  1.00 19.44           C  
ATOM   1342  O   GLY A 164      28.318  29.019  11.769  1.00 20.36           O  
ATOM   1343  N   PRO A 165      28.685  28.762   9.569  1.00 18.00           N  
ATOM   1344  CA  PRO A 165      29.410  28.384   8.371  1.00 17.48           C  
ATOM   1345  C   PRO A 165      30.636  29.235   8.105  1.00 18.82           C  
ATOM   1346  O   PRO A 165      30.749  30.376   8.594  1.00 17.26           O  
ATOM   1347  CB  PRO A 165      28.366  28.589   7.264  1.00 18.05           C  
ATOM   1348  CG  PRO A 165      27.462  29.625   7.779  1.00 21.65           C  
ATOM   1349  CD  PRO A 165      27.401  29.412   9.250  1.00 20.82           C  
ATOM   1350  N   CYS A 166      31.592  28.618   7.404  1.00 16.85           N  
ATOM   1351  CA  CYS A 166      32.718  29.329   6.832  1.00 17.05           C  
ATOM   1352  C   CYS A 166      32.781  29.008   5.348  1.00 16.00           C  
ATOM   1353  O   CYS A 166      32.281  27.983   4.907  1.00 17.72           O  
ATOM   1354  CB  CYS A 166      34.012  28.883   7.430  1.00 18.48           C  
ATOM   1355  SG  CYS A 166      34.069  28.893   9.224  1.00 23.18           S  
ATOM   1356  N   ILE A 167      33.440  29.876   4.599  1.00 15.12           N  
ATOM   1357  CA  ILE A 167      33.659  29.649   3.196  1.00 14.67           C  
ATOM   1358  C   ILE A 167      35.169  29.407   3.053  1.00 14.39           C  
ATOM   1359  O   ILE A 167      35.989  30.174   3.561  1.00 15.12           O  
ATOM   1360  CB  ILE A 167      33.285  30.906   2.385  1.00 16.78           C  
ATOM   1361  CG1 ILE A 167      31.782  31.204   2.508  1.00 21.14           C  
ATOM   1362  CG2 ILE A 167      33.719  30.744   0.898  1.00 17.50           C  
ATOM   1363  CD1 ILE A 167      30.922  30.111   2.059  1.00 20.44           C  
ATOM   1364  N   VAL A 168      35.544  28.361   2.342  1.00 13.18           N  
ATOM   1365  CA  VAL A 168      36.948  28.118   2.041  1.00 12.90           C  
ATOM   1366  C   VAL A 168      37.410  29.272   1.136  1.00 14.22           C  
ATOM   1367  O   VAL A 168      36.895  29.461   0.026  1.00 15.65           O  
ATOM   1368  CB  VAL A 168      37.167  26.750   1.346  1.00 15.25           C  
ATOM   1369  CG1 VAL A 168      38.664  26.530   0.957  1.00 14.91           C  
ATOM   1370  CG2 VAL A 168      36.596  25.595   2.218  1.00 14.65           C  
ATOM   1371  N   ALA A 169      38.371  30.026   1.640  1.00 14.60           N  
ATOM   1372  CA  ALA A 169      38.808  31.235   0.930  1.00 13.89           C  
ATOM   1373  C   ALA A 169      40.294  31.193   0.492  1.00 13.79           C  
ATOM   1374  O   ALA A 169      40.715  31.949  -0.392  1.00 15.47           O  
ATOM   1375  CB  ALA A 169      38.487  32.488   1.782  1.00 16.30           C  
ATOM   1376  N   ILE A 170      41.101  30.337   1.125  1.00 14.49           N  
ATOM   1377  CA  ILE A 170      42.404  29.945   0.613  1.00 14.48           C  
ATOM   1378  C   ILE A 170      42.463  28.408   0.688  1.00 12.82           C  
ATOM   1379  O   ILE A 170      42.166  27.805   1.727  1.00 13.36           O  
ATOM   1380  CB  ILE A 170      43.575  30.544   1.417  1.00 14.21           C  
ATOM   1381  CG1 ILE A 170      43.513  32.072   1.521  1.00 17.18           C  
ATOM   1382  CG2 ILE A 170      44.959  30.143   0.797  1.00 14.66           C  
ATOM   1383  CD1 ILE A 170      44.546  32.673   2.542  1.00 18.05           C  
ATOM   1384  N   ASP A 171      42.772  27.789  -0.428  1.00 14.81           N  
ATOM   1385  CA  ASP A 171      42.862  26.331  -0.455  1.00 15.03           C  
ATOM   1386  C   ASP A 171      44.328  25.878  -0.317  1.00 13.69           C  
ATOM   1387  O   ASP A 171      45.240  26.701  -0.094  1.00 15.79           O  
ATOM   1388  CB  ASP A 171      42.159  25.752  -1.706  1.00 16.54           C  
ATOM   1389  CG  ASP A 171      42.891  26.052  -3.023  1.00 19.18           C  
ATOM   1390  OD1 ASP A 171      44.035  26.521  -3.010  1.00 14.72           O  
ATOM   1391  OD2 ASP A 171      42.297  25.810  -4.096  1.00 21.92           O  
ATOM   1392  N   ALA A 172      44.528  24.559  -0.441  1.00 12.92           N  
ATOM   1393  CA  ALA A 172      45.851  23.920  -0.373  1.00 13.61           C  
ATOM   1394  C   ALA A 172      46.526  23.819  -1.728  1.00 13.60           C  
ATOM   1395  O   ALA A 172      47.521  23.058  -1.891  1.00 13.96           O  
ATOM   1396  CB  ALA A 172      45.735  22.526   0.273  1.00 15.48           C  
ATOM   1397  N   HIS A 173      46.005  24.564  -2.718  1.00 13.94           N  
ATOM   1398  CA  HIS A 173      46.496  24.521  -4.093  1.00 14.24           C  
ATOM   1399  C   HIS A 173      46.897  25.884  -4.681  1.00 13.48           C  
ATOM   1400  O   HIS A 173      46.958  26.058  -5.907  1.00 15.10           O  
ATOM   1401  CB  HIS A 173      45.453  23.840  -4.961  1.00 15.50           C  
ATOM   1402  CG  HIS A 173      45.044  22.507  -4.425  1.00 16.55           C  
ATOM   1403  ND1 HIS A 173      45.764  21.359  -4.654  1.00 20.65           N  
ATOM   1404  CD2 HIS A 173      44.028  22.165  -3.607  1.00 19.27           C  
ATOM   1405  CE1 HIS A 173      45.185  20.354  -4.018  1.00 22.36           C  
ATOM   1406  NE2 HIS A 173      44.121  20.816  -3.387  1.00 15.56           N  
ATOM   1407  N   GLY A 174      47.165  26.833  -3.801  1.00 13.70           N  
ATOM   1408  CA  GLY A 174      47.687  28.133  -4.177  1.00 15.53           C  
ATOM   1409  C   GLY A 174      46.631  29.133  -4.628  1.00 16.09           C  
ATOM   1410  O   GLY A 174      46.968  30.147  -5.225  1.00 17.83           O  
ATOM   1411  N   ASN A 175      45.361  28.824  -4.393  1.00 15.46           N  
ATOM   1412  CA  ASN A 175      44.261  29.726  -4.730  1.00 15.06           C  
ATOM   1413  C   ASN A 175      43.803  30.542  -3.529  1.00 14.22           C  
ATOM   1414  O   ASN A 175      43.729  30.019  -2.407  1.00 14.81           O  
ATOM   1415  CB  ASN A 175      43.076  28.941  -5.233  1.00 16.27           C  
ATOM   1416  CG  ASN A 175      43.375  28.231  -6.518  1.00 23.31           C  
ATOM   1417  OD1 ASN A 175      43.670  28.885  -7.523  1.00 22.42           O  
ATOM   1418  ND2 ASN A 175      43.365  26.909  -6.495  1.00 22.32           N  
ATOM   1419  N   SER A 176      43.448  31.797  -3.791  1.00 14.69           N  
ATOM   1420  CA  SER A 176      42.908  32.691  -2.765  1.00 12.01           C  
ATOM   1421  C   SER A 176      41.786  33.574  -3.342  1.00 14.57           C  
ATOM   1422  O   SER A 176      42.006  34.249  -4.344  1.00 15.02           O  
ATOM   1423  CB  SER A 176      44.023  33.600  -2.261  1.00 14.65           C  
ATOM   1424  OG  SER A 176      43.553  34.585  -1.403  1.00 13.97           O  
ATOM   1425  N   LEU A 177      40.634  33.639  -2.664  1.00 14.67           N  
ATOM   1426  CA  LEU A 177      39.568  34.593  -2.990  1.00 13.92           C  
ATOM   1427  C   LEU A 177      40.025  36.044  -2.882  1.00 13.41           C  
ATOM   1428  O   LEU A 177      39.436  36.921  -3.492  1.00 14.85           O  
ATOM   1429  CB  LEU A 177      38.343  34.425  -2.055  1.00 18.24           C  
ATOM   1430  CG  LEU A 177      37.524  33.181  -2.310  1.00 30.18           C  
ATOM   1431  CD1 LEU A 177      36.241  33.225  -1.506  1.00 26.87           C  
ATOM   1432  CD2 LEU A 177      37.220  33.012  -3.799  1.00 31.01           C  
ATOM   1433  N   TYR A 178      41.110  36.260  -2.134  1.00 12.11           N  
ATOM   1434  CA  TYR A 178      41.553  37.614  -1.805  1.00 12.79           C  
ATOM   1435  C   TYR A 178      42.572  38.164  -2.803  1.00 17.36           C  
ATOM   1436  O   TYR A 178      42.954  39.328  -2.712  1.00 20.73           O  
ATOM   1437  CB  TYR A 178      42.143  37.628  -0.416  1.00 14.55           C  
ATOM   1438  CG  TYR A 178      41.199  37.054   0.620  1.00 13.07           C  
ATOM   1439  CD1 TYR A 178      40.180  37.842   1.177  1.00 13.85           C  
ATOM   1440  CD2 TYR A 178      41.365  35.750   1.086  1.00 13.09           C  
ATOM   1441  CE1 TYR A 178      39.320  37.312   2.129  1.00 16.77           C  
ATOM   1442  CE2 TYR A 178      40.513  35.225   2.016  1.00 15.67           C  
ATOM   1443  CZ  TYR A 178      39.496  36.002   2.530  1.00 16.23           C  
ATOM   1444  OH  TYR A 178      38.654  35.469   3.451  1.00 16.18           O  
ATOM   1445  N   ARG A 179      42.993  37.345  -3.746  1.00 16.18           N  
ATOM   1446  CA  ARG A 179      44.099  37.724  -4.624  1.00 19.48           C  
ATOM   1447  C   ARG A 179      43.749  38.980  -5.415  1.00 25.47           C  
ATOM   1448  O   ARG A 179      42.713  39.024  -6.028  1.00 25.93           O  
ATOM   1449  CB  ARG A 179      44.424  36.569  -5.557  1.00 18.43           C  
ATOM   1450  CG  ARG A 179      45.607  36.845  -6.497  1.00 18.14           C  
ATOM   1451  CD  ARG A 179      46.093  35.528  -7.058  1.00 17.77           C  
ATOM   1452  NE  ARG A 179      46.780  34.814  -5.982  1.00 19.64           N  
ATOM   1453  CZ  ARG A 179      46.820  33.488  -5.862  1.00 25.29           C  
ATOM   1454  NH1 ARG A 179      46.273  32.698  -6.777  1.00 26.46           N  
ATOM   1455  NH2 ARG A 179      47.469  32.957  -4.842  1.00 22.73           N  
ATOM   1456  N   ARG A 180      44.624  39.976  -5.392  1.00 33.88           N  
ATOM   1457  CA  ARG A 180      44.338  41.269  -6.039  1.00 37.25           C  
ATOM   1458  C   ARG A 180      43.017  41.953  -5.507  1.00 38.56           C  
ATOM   1459  O   ARG A 180      42.350  42.765  -6.173  1.00 31.15           O  
ATOM   1460  CB  ARG A 180      44.338  41.098  -7.575  1.00 41.05           C  
ATOM   1461  CG  ARG A 180      45.600  40.393  -8.193  1.00 32.99           C  
ATOM   1462  OXT ARG A 180      42.577  41.733  -4.346  1.00 38.96           O  
TER    1463      ARG A 180                                                      
HETATM 1464  O   HOH A 181      37.112  36.971  -4.878  1.00 11.02           O  
HETATM 1465  O   HOH A 182      42.641  39.738   7.247  1.00 12.64           O  
HETATM 1466  O   HOH A 183      46.454  35.949  21.426  1.00 14.24           O  
HETATM 1467  O   HOH A 184      34.938  36.637   6.633  1.00 16.07           O  
HETATM 1468  O   HOH A 185      47.808  26.949  -0.962  1.00 15.78           O  
HETATM 1469  O   HOH A 186      27.071  34.802  15.289  1.00 16.27           O  
HETATM 1470  O   HOH A 187      47.453  31.747  12.319  1.00 15.93           O  
HETATM 1471  O   HOH A 188      37.608  38.289  17.895  1.00 18.14           O  
HETATM 1472  O   HOH A 189      42.456  22.492  -0.586  1.00 18.11           O  
HETATM 1473  O   HOH A 190      42.420  33.770  21.587  1.00 19.44           O  
HETATM 1474  O   HOH A 191      43.171  32.040  -6.761  1.00 20.03           O  
HETATM 1475  O   HOH A 192      40.047  26.079  -5.283  1.00 21.72           O  
HETATM 1476  O   HOH A 193      54.536  25.247   4.914  1.00 21.46           O  
HETATM 1477  O   HOH A 194      32.930  37.543   9.391  1.00 23.22           O  
HETATM 1478  O   HOH A 195      46.754  39.808   4.032  1.00 22.46           O  
HETATM 1479  O   HOH A 196      40.327  31.571  -6.089  1.00 23.89           O  
HETATM 1480  O   HOH A 197      28.668  28.655  24.257  1.00 24.35           O  
HETATM 1481  O   HOH A 198      57.983  36.133  19.467  1.00 25.30           O  
HETATM 1482  O   HOH A 199      35.573  20.230  -2.699  1.00 25.11           O  
HETATM 1483  O   HOH A 200      30.661  41.241  15.819  1.00 24.63           O  
HETATM 1484  O   HOH A 201      38.579  43.107   9.156  1.00 25.31           O  
HETATM 1485  O   HOH A 202      56.398  33.380   9.859  1.00 24.56           O  
HETATM 1486  O   HOH A 203      55.637  35.689  26.045  1.00 25.06           O  
HETATM 1487  O   HOH A 204      34.199  37.613  20.211  1.00 25.76           O  
HETATM 1488  O   HOH A 205      43.475  44.626  12.257  1.00 24.97           O  
HETATM 1489  O   HOH A 206      39.946  42.764  13.974  1.00 25.82           O  
HETATM 1490  O   HOH A 207      50.043  40.835  15.320  1.00 27.69           O  
HETATM 1491  O   HOH A 208      40.830  20.573  -4.444  1.00 25.87           O  
HETATM 1492  O   HOH A 209      44.845  12.005   4.885  1.00 28.27           O  
HETATM 1493  O   HOH A 210      35.923  43.933   9.928  1.00 25.06           O  
HETATM 1494  O   HOH A 211      39.112  16.377   8.835  1.00 25.01           O  
HETATM 1495  O   HOH A 212      51.420  31.402  31.038  1.00 29.97           O  
HETATM 1496  O   HOH A 213      27.970  31.314   4.482  1.00 25.13           O  
HETATM 1497  O   HOH A 214      55.613  31.150   2.029  1.00 27.37           O  
HETATM 1498  O   HOH A 215      52.271  22.986  17.424  1.00 26.82           O  
HETATM 1499  O   HOH A 216      55.833  27.521   5.883  1.00 27.25           O  
HETATM 1500  O   HOH A 217      28.928  36.679   8.844  1.00 28.13           O  
HETATM 1501  O   HOH A 218      33.362  25.834  -4.623  1.00 30.11           O  
HETATM 1502  O   HOH A 219      53.593  24.500   1.402  1.00 26.94           O  
HETATM 1503  O   HOH A 220      57.439  36.949   9.096  1.00 30.41           O  
HETATM 1504  O   HOH A 221      43.618  42.399  22.909  1.00 26.82           O  
HETATM 1505  O   HOH A 222      50.114  39.311  -0.006  1.00 28.88           O  
HETATM 1506  O   HOH A 223      51.037  42.039  11.825  1.00 31.38           O  
HETATM 1507  O   HOH A 224      45.594  28.469  -9.263  1.00 30.06           O  
HETATM 1508  O   HOH A 225      53.113  20.813   1.441  1.00 28.10           O  
HETATM 1509  O   HOH A 226      50.774  17.520   0.368  1.00 30.65           O  
HETATM 1510  O   HOH A 227      27.024  31.021  13.321  1.00 31.22           O  
HETATM 1511  O   HOH A 228      48.766  27.435  -8.145  1.00 35.11           O  
HETATM 1512  O   HOH A 229      63.195  34.501  25.042  1.00 32.12           O  
HETATM 1513  O   HOH A 230      37.201  38.867  25.821  1.00 33.32           O  
HETATM 1514  O   HOH A 231      36.849  17.504   2.438  1.00 33.44           O  
HETATM 1515  O   HOH A 232      36.405  27.016  -6.801  1.00 32.29           O  
HETATM 1516  O   HOH A 233      57.809  24.232  20.456  1.00 33.76           O  
HETATM 1517  O   HOH A 234      41.351  39.655  30.790  1.00 35.26           O  
HETATM 1518  O   HOH A 235      29.434  14.982 -17.610  1.00 56.76           O  
HETATM 1519  O   HOH A 236      27.523  17.412  14.248  1.00 48.09           O  
HETATM 1520  O   HOH A 237      31.461  14.806   9.420  1.00 38.41           O  
HETATM 1521  O   HOH A 238      40.088  29.104  -7.259  1.00 38.45           O  
HETATM 1522  O   HOH A 239      56.391  24.790  12.355  1.00 37.50           O  
HETATM 1523  O   HOH A 240      54.157  24.229  13.809  1.00 32.64           O  
HETATM 1524  O   HOH A 241      48.634  40.942   2.148  1.00 46.48           O  
HETATM 1525  O   HOH A 242      37.019  40.555  27.757  1.00 46.52           O  
HETATM 1526  O   HOH A 243      47.887  43.844   9.632  1.00 41.58           O  
HETATM 1527  O   HOH A 244      41.796  21.521  16.588  1.00 18.55           O  
HETATM 1528  O   HOH A 245      40.952  35.646  -6.535  1.00 23.62           O  
HETATM 1529  O   HOH A 246      47.197  30.178  32.312  1.00 23.08           O  
HETATM 1530  O   HOH A 247      30.776  27.432  25.809  1.00 20.97           O  
HETATM 1531  O   HOH A 248      28.639  28.365  14.717  1.00 24.77           O  
HETATM 1532  O   HOH A 249      39.001  33.779  -7.143  1.00 22.20           O  
HETATM 1533  O   HOH A 250      54.424  24.764  16.495  1.00 30.12           O  
HETATM 1534  O   HOH A 251      51.952  27.236  29.511  1.00 25.59           O  
HETATM 1535  O   HOH A 252      42.062  25.213  31.829  1.00 33.77           O  
HETATM 1536  O   HOH A 253      45.263  18.490  16.406  1.00 28.04           O  
HETATM 1537  O   HOH A 254      60.524  31.598  26.239  1.00 34.23           O  
HETATM 1538  O   HOH A 255      33.544  40.542  12.744  1.00 27.12           O  
HETATM 1539  O   HOH A 256      52.697  21.708  19.891  1.00 30.99           O  
HETATM 1540  O   HOH A 257      59.851  30.269  15.959  1.00 26.16           O  
HETATM 1541  O   HOH A 258      45.151  43.887   9.988  1.00 32.51           O  
HETATM 1542  O   HOH A 259      45.705  21.579  20.875  1.00 35.07           O  
HETATM 1543  O   HOH A 260      27.241  18.996   6.037  1.00 46.61           O  
HETATM 1544  O   HOH A 261      31.775  38.531  18.965  1.00 35.13           O  
HETATM 1545  O   HOH A 262      60.235  37.638  23.278  1.00 27.62           O  
HETATM 1546  O   HOH A 263      45.566  36.031  -0.448  1.00 23.14           O  
HETATM 1547  O   HOH A 264      49.255  40.388  26.948  1.00 31.75           O  
HETATM 1548  O   HOH A 265      53.229  37.891   1.152  1.00 28.95           O  
HETATM 1549  O   HOH A 266      50.761  42.054   9.147  1.00 48.58           O  
HETATM 1550  O   HOH A 267      32.381  24.567  29.399  1.00 27.80           O  
HETATM 1551  O   HOH A 268      55.330  22.300  20.731  1.00 28.00           O  
HETATM 1552  O   HOH A 269      49.112  27.752  30.299  1.00 26.00           O  
HETATM 1553  O   HOH A 270      61.244  27.981  15.680  1.00 33.96           O  
HETATM 1554  O   HOH A 271      50.223  15.499  15.120  1.00 52.03           O  
HETATM 1555  O   HOH A 272      25.840  25.518  13.104  1.00 29.29           O  
HETATM 1556  O   HOH A 273      31.253  16.377   5.401  1.00 31.44           O  
HETATM 1557  O   HOH A 274      31.461  37.781  30.401  1.00 41.77           O  
HETATM 1558  O   HOH A 275      42.625  18.804  16.360  1.00 25.05           O  
HETATM 1559  O   HOH A 276      53.257  24.694  29.626  1.00 33.14           O  
HETATM 1560  O   HOH A 277      47.638  38.848  -4.056  1.00 33.53           O  
HETATM 1561  O   HOH A 278      44.083  42.560  25.447  1.00 36.02           O  
HETATM 1562  O   HOH A 279      44.226  44.110  -7.544  1.00 31.95           O  
HETATM 1563  O   HOH A 280      42.759  34.214  -8.295  1.00 28.03           O  
HETATM 1564  O   HOH A 281      56.543  32.483  28.340  1.00 25.83           O  
HETATM 1565  O   HOH A 282      45.506  20.478  18.083  1.00 33.82           O  
HETATM 1566  O   HOH A 283      25.763  34.678  23.755  1.00 30.60           O  
HETATM 1567  O   HOH A 284      56.259  28.550   1.639  1.00 38.26           O  
HETATM 1568  O   HOH A 285      30.768  37.645  10.271  1.00 44.82           O  
HETATM 1569  O   HOH A 286      56.800  23.814  27.831  1.00 34.52           O  
HETATM 1570  O   HOH A 287      48.623  20.860  -3.178  1.00 34.41           O  
HETATM 1571  O   HOH A 288      35.825  15.093   8.593  1.00 32.52           O  
HETATM 1572  O   HOH A 289      29.304  14.871   7.346  1.00 42.42           O  
HETATM 1573  O   HOH A 290      45.149  28.271  32.481  1.00 35.79           O  
HETATM 1574  O   HOH A 291      56.383  32.694  -0.256  1.00 34.13           O  
HETATM 1575  O   HOH A 292      40.806  28.135  33.794  1.00 49.02           O  
HETATM 1576  O   HOH A 293      53.159  36.686   5.691  1.00 33.94           O  
HETATM 1577  O   HOH A 294      37.277  24.503  31.270  1.00 37.52           O  
HETATM 1578  O   HOH A 295      43.829  40.386  26.891  1.00 35.24           O  
HETATM 1579  O   HOH A 296      44.927  41.377  19.509  1.00 28.66           O  
HETATM 1580  O   HOH A 297      27.485  16.050   8.393  1.00 45.11           O  
HETATM 1581  O   HOH A 298      52.324  37.407  31.515  1.00 40.93           O  
HETATM 1582  O   HOH A 299      31.924  20.660  -8.421  1.00 55.37           O  
HETATM 1583  O   HOH A 300      39.302  13.086  12.304  1.00 42.89           O  
HETATM 1584  O   HOH A 301      53.554  39.489   6.355  1.00 45.66           O  
HETATM 1585  O   HOH A 302      35.420  15.353  15.655  1.00 38.80           O  
HETATM 1586  O   HOH A 303      27.868  18.810  -0.388  1.00 40.98           O  
HETATM 1587  O   HOH A 304      55.034  37.040  -1.115  1.00 52.78           O  
HETATM 1588  O   HOH A 305      25.273  28.508  16.404  1.00 32.92           O  
HETATM 1589  O   HOH A 306      60.550  23.831  18.945  1.00 34.05           O  
HETATM 1590  O   HOH A 307      33.172  20.115 -12.803  1.00 43.05           O  
HETATM 1591  O   HOH A 308      29.924  25.508  27.518  1.00 42.34           O  
HETATM 1592  O   HOH A 309      53.437  21.619  14.346  1.00 46.94           O  
HETATM 1593  O   HOH A 310      47.780  29.790  -8.032  1.00 35.59           O  
HETATM 1594  O   HOH A 311      60.162  25.706  14.893  1.00 37.98           O  
HETATM 1595  O   HOH A 312      57.617  34.810  27.521  1.00 34.95           O  
HETATM 1596  O   HOH A 313      59.095  23.847  16.285  1.00 44.08           O  
HETATM 1597  O   HOH A 314      32.373  18.101  19.416  1.00 35.35           O  
HETATM 1598  O   HOH A 315      30.554  18.352  21.414  1.00 46.25           O  
HETATM 1599  O   HOH A 316      38.990  16.846  18.121  1.00 31.39           O  
HETATM 1600  O   HOH A 317      40.447  34.613  31.578  1.00 39.63           O  
HETATM 1601  O   HOH A 318      42.423  32.118  35.885  1.00 49.72           O  
HETATM 1602  O   HOH A 319      45.765  13.981   8.689  1.00 39.58           O  
HETATM 1603  O   HOH A 320      43.729  12.934  11.737  1.00 35.89           O  
HETATM 1604  O   HOH A 321      30.345  24.696 -14.099  1.00 42.69           O  
HETATM 1605  O   HOH A 322      26.281  25.691  23.758  1.00 48.61           O  
HETATM 1606  O   HOH A 323      24.200  23.988  10.967  1.00 55.54           O  
HETATM 1607  O   HOH A 324      34.899  19.092  -5.274  1.00 48.15           O  
HETATM 1608  O   HOH A 325      38.768  19.768  -5.731  1.00 43.25           O  
HETATM 1609  O   HOH A 326      32.688  18.219 -17.821  1.00 30.98           O  
HETATM 1610  O   HOH A 327      33.705  22.400  -5.035  1.00 40.40           O  
HETATM 1611  O   HOH A 328      25.590  23.002  16.964  1.00 39.80           O  
HETATM 1612  O   HOH A 329      25.335  32.931  22.349  1.00 42.38           O  
HETATM 1613  O   HOH A 330      49.808  23.012  -5.248  1.00 54.48           O  
HETATM 1614  O   HOH A 331      53.701  23.076  27.460  1.00 40.95           O  
HETATM 1615  O   HOH A 332      25.533  27.706  12.307  1.00 42.05           O  
HETATM 1616  O   HOH A 333      41.532  11.740  12.307  1.00 43.62           O  
HETATM 1617  O   HOH A 334      57.517  31.887   4.017  1.00 40.72           O  
HETATM 1618  O   HOH A 335      50.994  33.017  -3.395  1.00 38.38           O  
HETATM 1619  O   HOH A 336      45.892  33.152  -9.615  1.00 36.32           O  
HETATM 1620  O   HOH A 337      49.027  17.285  16.739  1.00 39.33           O  
HETATM 1621  O   HOH A 338      59.857  21.415  26.209  1.00 39.17           O  
HETATM 1622  O   HOH A 339      46.047  21.745  25.131  1.00 41.52           O  
HETATM 1623  O   HOH A 340      54.892  25.897  -0.443  1.00 49.43           O  
HETATM 1624  O   HOH A 341      25.099  20.226  18.049  1.00 46.06           O  
HETATM 1625  O   HOH A 342      31.961  15.247 -18.591  1.00 44.75           O  
HETATM 1626  O   HOH A 343      61.255  32.225  14.923  1.00 38.93           O  
HETATM 1627  O   HOH A 344      35.307  25.213  32.755  1.00 38.42           O  
HETATM 1628  O   HOH A 345      53.028  18.846   2.976  1.00 42.00           O  
HETATM 1629  O   HOH A 346      31.783  40.377  22.465  1.00 39.45           O  
HETATM 1630  O   HOH A 347      40.869  42.764  22.821  1.00 46.04           O  
HETATM 1631  O   HOH A 348      25.528  24.325  -5.414  1.00 46.18           O  
HETATM 1632  O   HOH A 349      60.579  35.359  18.996  1.00 41.32           O  
HETATM 1633  O   HOH A 350      53.698  33.971  -3.730  1.00 49.81           O  
HETATM 1634  O   HOH A 351      41.286  45.616  11.048  1.00 42.04           O  
HETATM 1635  O   HOH A 352      31.665  34.620  37.832  1.00 58.77           O  
HETATM 1636  O   HOH A 353      38.892  41.820  16.844  1.00 44.07           O  
HETATM 1637  O   HOH A 354      36.592  39.976  22.964  1.00 48.93           O  
HETATM 1638  O   HOH A 355      58.022  33.594   7.965  1.00 50.33           O  
HETATM 1639  O   HOH A 356      54.900  34.393  -1.554  1.00 40.65           O  
HETATM 1640  O   HOH A 357      41.762  17.354  18.542  1.00 36.68           O  
HETATM 1641  O   HOH A 358      43.072  21.465  19.119  1.00 29.58           O  
HETATM 1642  O   HOH A 359      34.176  41.348  23.516  1.00 41.97           O  
HETATM 1643  O   HOH A 360      30.518  41.045  10.170  1.00 40.24           O  
HETATM 1644  O   HOH A 361      34.502  42.601  25.900  1.00 40.78           O  
HETATM 1645  O   HOH A 362      51.826  17.633   4.828  1.00 36.26           O  
CONECT   24   32                                                                
CONECT   32   24   33                                                           
CONECT   33   32   34   36                                                      
CONECT   34   33   35   38                                                      
CONECT   35   34                                                                
CONECT   36   33   37                                                           
CONECT   37   36                                                                
CONECT   38   34                                                                
CONECT   40   45                                                                
CONECT   45   40   46                                                           
CONECT   46   45   47   49                                                      
CONECT   47   46   48   53                                                      
CONECT   48   47                                                                
CONECT   49   46   50                                                           
CONECT   50   49   51                                                           
CONECT   51   50   52                                                           
CONECT   52   51                                                                
CONECT   53   47                                                                
CONECT  401  413                                                                
CONECT  413  401  414                                                           
CONECT  414  413  415  417                                                      
CONECT  415  414  416  421                                                      
CONECT  416  415                                                                
CONECT  417  414  418                                                           
CONECT  418  417  419                                                           
CONECT  419  418  420                                                           
CONECT  420  419                                                                
CONECT  421  415                                                                
CONECT  734  743                                                                
CONECT  743  734  744                                                           
CONECT  744  743  745  747                                                      
CONECT  745  744  746  751                                                      
CONECT  746  745                                                                
CONECT  747  744  748                                                           
CONECT  748  747  749                                                           
CONECT  749  748  750                                                           
CONECT  750  749                                                                
CONECT  751  745                                                                
CONECT  850  854                                                                
CONECT  854  850  855                                                           
CONECT  855  854  856  858                                                      
CONECT  856  855  857  862                                                      
CONECT  857  856                                                                
CONECT  858  855  859                                                           
CONECT  859  858  860                                                           
CONECT  860  859  861                                                           
CONECT  861  860                                                                
CONECT  862  856                                                                
CONECT  901  903                                                                
CONECT  903  901  904                                                           
CONECT  904  903  905  907                                                      
CONECT  905  904  906  911                                                      
CONECT  906  905                                                                
CONECT  907  904  908                                                           
CONECT  908  907  909                                                           
CONECT  909  908  910                                                           
CONECT  910  909                                                                
CONECT  911  905                                                                
CONECT  969  972                                                                
CONECT  972  969  973                                                           
CONECT  973  972  974  976                                                      
CONECT  974  973  975  980                                                      
CONECT  975  974                                                                
CONECT  976  973  977                                                           
CONECT  977  976  978                                                           
CONECT  978  977  979                                                           
CONECT  979  978                                                                
CONECT  980  974                                                                
CONECT 1097 1100                                                                
CONECT 1100 1097 1101 1102                                                      
CONECT 1101 1100 1103 1105                                                      
CONECT 1102 1100 1103 1106                                                      
CONECT 1103 1101 1102 1104 1113                                                 
CONECT 1104 1103                                                                
CONECT 1105 1101 1107                                                           
CONECT 1106 1102 1108                                                           
CONECT 1107 1105 1109                                                           
CONECT 1108 1106 1110                                                           
CONECT 1109 1107 1111                                                           
CONECT 1110 1108 1112                                                           
CONECT 1111 1109                                                                
CONECT 1112 1110                                                                
CONECT 1113 1103                                                                
CONECT 1223 1225                                                                
CONECT 1225 1223 1226                                                           
CONECT 1226 1225 1227 1229                                                      
CONECT 1227 1226 1228 1233                                                      
CONECT 1228 1227                                                                
CONECT 1229 1226 1230                                                           
CONECT 1230 1229 1231                                                           
CONECT 1231 1230 1232                                                           
CONECT 1232 1231                                                                
CONECT 1233 1227                                                                
MASTER      332    0    9    7   13    0    0    6 1581    1   93   15          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.