HEADER    ENDONUCLEASE                            28-MAY-97   1AK0              
TITLE     P1 NUCLEASE IN COMPLEX WITH A SUBSTRATE ANALOG                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: P1 NUCLEASE;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.30.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PENICILLIUM CITRINUM;                           
SOURCE   3 ORGANISM_TAXID: 5077                                                 
KEYWDS    ENDONUCLEASE, P1 NUCLEASE, REACTION MECHANISM, THIOPHOSPHORYLATED     
KEYWDS   2 OLIGONUCLEOTIDES, GLYCOSYLATED PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ROMIER,D.SUCK                                                       
REVDAT   4   29-JUL-20 1AK0    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   13-JUL-11 1AK0    1       VERSN                                    
REVDAT   2   24-FEB-09 1AK0    1       VERSN                                    
REVDAT   1   03-DEC-97 1AK0    0                                                
JRNL        AUTH   C.ROMIER,R.DOMINGUEZ,A.LAHM,O.DAHL,D.SUCK                    
JRNL        TITL   RECOGNITION OF SINGLE-STRANDED DNA BY NUCLEASE P1: HIGH      
JRNL        TITL 2 RESOLUTION CRYSTAL STRUCTURES OF COMPLEXES WITH SUBSTRATE    
JRNL        TITL 3 ANALOGS.                                                     
JRNL        REF    PROTEINS                      V.  32   414 1998              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   9726413                                                      
JRNL        DOI    10.1002/(SICI)1097-0134(19980901)32:4<414::AID-PROT2>3.3.CO; 
JRNL        DOI  2 2-5                                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.VOLBEDA,A.LAHM,F.SAKIYAMA,D.SUCK                           
REMARK   1  TITL   CRYSTAL STRUCTURE OF PENICILLIUM CITRINUM P1 NUCLEASE AT 2.8 
REMARK   1  TITL 2 A RESOLUTION                                                 
REMARK   1  REF    EMBO J.                       V.  10  1607 1991              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 27019                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2021                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 8.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.700                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.500 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM3.CHO                                     
REMARK   3  PARAMETER FILE  3  : PARNAH1E.DNA                                   
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  3   : TOPNAH1E.DNA                                   
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000170911.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 5.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27854                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.24700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000 12 - 20% 25 MM NA ACETATE PH    
REMARK 280  5.3                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.99000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.06500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.02000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.06500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.99000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.02000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     GLU A   267                                                      
REMARK 465     ILE A   268                                                      
REMARK 465     ALA A   269                                                      
REMARK 465     LYS A   270                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O7   NAG A   287     O    HOH A   552              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A 105   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  66     -158.88   -110.16                                   
REMARK 500    TYR A 130      125.45    -37.70                                   
REMARK 500    ASP A 146     -169.64   -112.59                                   
REMARK 500    THR A 154      -58.80   -122.14                                   
REMARK 500    SER A 182       58.71   -149.34                                   
REMARK 500    GLU A 200       55.30   -145.62                                   
REMARK 500    GLN A 229       36.12    -99.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     ADS A  292                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 273  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP A   1   O                                                      
REMARK 620 2 TRP A   1   N    72.5                                              
REMARK 620 3 HIS A   6   NE2  99.8 113.2                                        
REMARK 620 4 ASP A 120   OD1 166.3  94.0  87.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 274  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  15   NE2                                                    
REMARK 620 2 GLU A 181   CD  104.9                                              
REMARK 620 3 GLU A 181   OE2  87.5  30.9                                        
REMARK 620 4 GLU A 181   OE1 104.8  29.5  58.3                                  
REMARK 620 5 HIS A 223   ND1 106.9 104.4  85.7 130.2                            
REMARK 620 6 HOH A 539   O    96.5 131.5 161.5 103.2 110.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 271  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  45   OD1                                                    
REMARK 620 2 HIS A  60   ND1  80.7                                              
REMARK 620 3 HIS A 116   NE2  75.0 101.4                                        
REMARK 620 4 ASP A 120   OD2 172.6 103.5  98.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 272  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 126   NE2                                                    
REMARK 620 2 HIS A 149   NE2  95.3                                              
REMARK 620 3 ASP A 153   OD2 143.9  96.0                                        
REMARK 620 4 ASP A 153   OD1  93.9  92.2  51.5                                  
REMARK 620 5 THS A 295   O3' 111.2 100.2 100.3 150.6                            
REMARK 620 N                    1     2     3     4                             
DBREF  1AK0 A    1   270  UNP    P24289   NUP1_PENCI       1    270             
SEQRES   1 A  270  TRP GLY ALA LEU GLY HIS ALA THR VAL ALA TYR VAL ALA          
SEQRES   2 A  270  GLN HIS TYR VAL SER PRO GLU ALA ALA SER TRP ALA GLN          
SEQRES   3 A  270  GLY ILE LEU GLY SER SER SER SER SER TYR LEU ALA SER          
SEQRES   4 A  270  ILE ALA SER TRP ALA ASP GLU TYR ARG LEU THR SER ALA          
SEQRES   5 A  270  GLY LYS TRP SER ALA SER LEU HIS PHE ILE ASP ALA GLU          
SEQRES   6 A  270  ASP ASN PRO PRO THR ASN CYS ASN VAL ASP TYR GLU ARG          
SEQRES   7 A  270  ASP CYS GLY SER SER GLY CYS SER ILE SER ALA ILE ALA          
SEQRES   8 A  270  ASN TYR THR GLN ARG VAL SER ASP SER SER LEU SER SER          
SEQRES   9 A  270  GLU ASN HIS ALA GLU ALA LEU ARG PHE LEU VAL HIS PHE          
SEQRES  10 A  270  ILE GLY ASP MET THR GLN PRO LEU HIS ASP GLU ALA TYR          
SEQRES  11 A  270  ALA VAL GLY GLY ASN LYS ILE ASN VAL THR PHE ASP GLY          
SEQRES  12 A  270  TYR HIS ASP ASN LEU HIS SER ASP TRP ASP THR TYR MET          
SEQRES  13 A  270  PRO GLN LYS LEU ILE GLY GLY HIS ALA LEU SER ASP ALA          
SEQRES  14 A  270  GLU SER TRP ALA LYS THR LEU VAL GLN ASN ILE GLU SER          
SEQRES  15 A  270  GLY ASN TYR THR ALA GLN ALA ILE GLY TRP ILE LYS GLY          
SEQRES  16 A  270  ASP ASN ILE SER GLU PRO ILE THR THR ALA THR ARG TRP          
SEQRES  17 A  270  ALA SER ASP ALA ASN ALA LEU VAL CYS THR VAL VAL MET          
SEQRES  18 A  270  PRO HIS GLY ALA ALA ALA LEU GLN THR GLY ASP LEU TYR          
SEQRES  19 A  270  PRO THR TYR TYR ASP SER VAL ILE ASP THR ILE GLU LEU          
SEQRES  20 A  270  GLN ILE ALA LYS GLY GLY TYR ARG LEU ALA ASN TRP ILE          
SEQRES  21 A  270  ASN GLU ILE HIS GLY SER GLU ILE ALA LYS                      
MODRES 1AK0 ASN A   92  ASN  GLYCOSYLATION SITE                                 
MODRES 1AK0 ASN A  197  ASN  GLYCOSYLATION SITE                                 
MODRES 1AK0 ASN A  138  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    NAG  A 285      14                                                       
HET    NAG  A 287      14                                                       
HET     ZN  A 271       1                                                       
HET     ZN  A 272       1                                                       
HET     ZN  A 273       1                                                       
HET     ZN  A 274       1                                                       
HET    ADS  A 292      18                                                       
HET    THS  A 293      20                                                       
HET    THS  A 294      20                                                       
HET    THS  A 295      20                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      ZN ZINC ION                                                         
HETNAM     ADS ADENOSINE-5'-(DITHIO)PHOSPHATE                                   
HETNAM     THS THYMIDINE-5'-(DITHIO)PHOSPHATE                                   
FORMUL   2  NAG    4(C8 H15 N O6)                                               
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   9  ADS    C10 H14 N5 O5 P S2                                           
FORMUL  10  THS    3(C10 H15 N2 O6 P S2)                                        
FORMUL  13  HOH   *154(H2 O)                                                    
HELIX    1   1 ALA A    3  TYR A   16  1                                  14    
HELIX    2   2 PRO A   19  LEU A   29  1                                  11    
HELIX    3   3 ALA A   38  ILE A   40  5                                   3    
HELIX    4   4 TRP A   43  LEU A   49  1                                   7    
HELIX    5   5 LYS A   54  HIS A   60  5                                   7    
HELIX    6   6 TYR A   76  ASP A   79  1                                   4    
HELIX    7   7 SER A   86  VAL A   97  1                                  12    
HELIX    8   8 SER A  104  THR A  122  1                                  19    
HELIX    9   9 PRO A  124  ASP A  127  5                                   4    
HELIX   10  10 TYR A  130  GLY A  133  1                                   4    
HELIX   11  11 LEU A  148  ASP A  153  1                                   6    
HELIX   12  12 TYR A  155  ILE A  161  1                                   7    
HELIX   13  13 LEU A  166  SER A  182  1                                  17    
HELIX   14  14 THR A  186  TRP A  192  1                                   7    
HELIX   15  15 ILE A  198  THR A  218  5                                  21    
HELIX   16  16 ALA A  226  LEU A  228  5                                   3    
HELIX   17  17 THR A  236  GLU A  262  1                                  27    
SHEET    1   A 2 ASN A 138  PHE A 141  0                                        
SHEET    2   A 2 TYR A 144  ASN A 147 -1  N  ASP A 146   O  VAL A 139           
SSBOND   1 CYS A   72    CYS A  217                          1555   1555  2.03  
SSBOND   2 CYS A   80    CYS A   85                          1555   1555  2.05  
LINK         ND2 ASN A  92                 C1  NAG B   1     1555   1555  1.46  
LINK         ND2 ASN A 138                 C1  NAG A 287     1555   1555  1.45  
LINK         ND2 ASN A 197                 C1  NAG A 285     1555   1555  1.47  
LINK         O3' ADS A 292                 P   THS A 293     1555   1555  1.64  
LINK         O3' THS A 293                 P   THS A 294     1555   1555  1.67  
LINK         O3' THS A 294                 P   THS A 295     1555   1555  1.64  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.39  
LINK         O   TRP A   1                ZN    ZN A 273     1555   1555  2.00  
LINK         N   TRP A   1                ZN    ZN A 273     1555   1555  2.53  
LINK         NE2 HIS A   6                ZN    ZN A 273     1555   1555  2.27  
LINK         NE2 HIS A  15                ZN    ZN A 274     1555   1555  2.22  
LINK         OD1 ASP A  45                ZN    ZN A 271     1555   1555  2.77  
LINK         ND1 HIS A  60                ZN    ZN A 271     1555   1555  2.31  
LINK         NE2 HIS A 116                ZN    ZN A 271     1555   1555  2.29  
LINK         OD2 ASP A 120                ZN    ZN A 271     1555   1555  2.01  
LINK         OD1 ASP A 120                ZN    ZN A 273     1555   1555  1.98  
LINK         NE2 HIS A 126                ZN    ZN A 272     1555   1555  2.32  
LINK         NE2 HIS A 149                ZN    ZN A 272     1555   1555  2.31  
LINK         OD2 ASP A 153                ZN    ZN A 272     1555   1555  1.97  
LINK         OD1 ASP A 153                ZN    ZN A 272     1555   1555  2.78  
LINK         CD  GLU A 181                ZN    ZN A 274     1555   1555  2.36  
LINK         OE2 GLU A 181                ZN    ZN A 274     1555   1555  1.81  
LINK         OE1 GLU A 181                ZN    ZN A 274     1555   1555  2.49  
LINK         ND1 HIS A 223                ZN    ZN A 274     3655   1555  2.22  
LINK        ZN    ZN A 272                 O3' THS A 295     1555   1555  2.02  
LINK        ZN    ZN A 274                 O   HOH A 539     1555   1555  2.02  
CISPEP   1 PRO A   68    PRO A   69          0         0.35                     
CISPEP   2 TYR A  234    PRO A  235          0        -4.87                     
CRYST1   41.980   74.040  102.130  90.00  90.00  90.00 P 21 21 21    4          
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      0.023821  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013506  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009791        0.00000                         
ATOM      1  N   TRP A   1      15.626  25.306  11.376  1.00  8.99           N  
ATOM      2  CA  TRP A   1      14.292  25.263  12.055  1.00  8.93           C  
ATOM      3  C   TRP A   1      13.188  25.524  11.051  1.00 11.85           C  
ATOM      4  O   TRP A   1      13.463  26.075   9.930  1.00 10.10           O  
ATOM      5  CB  TRP A   1      14.223  26.340  13.138  1.00  9.25           C  
ATOM      6  CG  TRP A   1      15.419  26.340  14.027  1.00  8.31           C  
ATOM      7  CD1 TRP A   1      16.413  27.262  14.060  1.00  9.07           C  
ATOM      8  CD2 TRP A   1      15.747  25.354  15.014  1.00  8.95           C  
ATOM      9  NE1 TRP A   1      17.347  26.915  14.996  1.00  9.22           N  
ATOM     10  CE2 TRP A   1      16.964  25.749  15.598  1.00  8.55           C  
ATOM     11  CE3 TRP A   1      15.131  24.172  15.445  1.00  7.35           C  
ATOM     12  CZ2 TRP A   1      17.583  25.002  16.614  1.00  9.97           C  
ATOM     13  CZ3 TRP A   1      15.750  23.423  16.449  1.00  7.12           C  
ATOM     14  CH2 TRP A   1      16.964  23.841  17.019  1.00  8.41           C  
ATOM     15  N   GLY A   2      12.015  25.029  11.429  1.00 11.84           N  
ATOM     16  CA  GLY A   2      10.788  25.203  10.682  1.00 12.64           C  
ATOM     17  C   GLY A   2      10.161  26.513  11.153  1.00 12.13           C  
ATOM     18  O   GLY A   2      10.841  27.331  11.789  1.00 10.37           O  
ATOM     19  N   ALA A   3       8.876  26.707  10.853  1.00 12.60           N  
ATOM     20  CA  ALA A   3       8.141  27.930  11.176  1.00 13.75           C  
ATOM     21  C   ALA A   3       8.093  28.356  12.646  1.00 15.18           C  
ATOM     22  O   ALA A   3       8.363  29.528  12.962  1.00 14.70           O  
ATOM     23  CB  ALA A   3       6.736  27.845  10.611  1.00 13.43           C  
ATOM     24  N   LEU A   4       7.708  27.439  13.535  1.00 13.80           N  
ATOM     25  CA  LEU A   4       7.655  27.743  14.962  1.00 13.52           C  
ATOM     26  C   LEU A   4       9.028  28.217  15.476  1.00 13.79           C  
ATOM     27  O   LEU A   4       9.131  29.227  16.180  1.00 13.41           O  
ATOM     28  CB  LEU A   4       7.192  26.505  15.749  1.00 15.19           C  
ATOM     29  CG  LEU A   4       7.191  26.544  17.284  1.00 15.92           C  
ATOM     30  CD1 LEU A   4       6.187  27.567  17.797  1.00 13.48           C  
ATOM     31  CD2 LEU A   4       6.841  25.168  17.822  1.00 16.42           C  
ATOM     32  N   GLY A   5      10.079  27.493  15.112  1.00 12.93           N  
ATOM     33  CA  GLY A   5      11.408  27.846  15.558  1.00 12.70           C  
ATOM     34  C   GLY A   5      11.832  29.237  15.126  1.00 14.18           C  
ATOM     35  O   GLY A   5      12.349  30.026  15.939  1.00 12.70           O  
ATOM     36  N   HIS A   6      11.608  29.563  13.854  1.00 13.72           N  
ATOM     37  CA  HIS A   6      11.991  30.879  13.350  1.00 12.89           C  
ATOM     38  C   HIS A   6      11.276  32.062  13.982  1.00 11.86           C  
ATOM     39  O   HIS A   6      11.924  33.077  14.292  1.00 12.53           O  
ATOM     40  CB  HIS A   6      11.926  30.931  11.820  1.00  9.92           C  
ATOM     41  CG  HIS A   6      13.154  30.346  11.180  1.00 10.46           C  
ATOM     42  ND1 HIS A   6      14.380  30.934  11.317  1.00  9.48           N  
ATOM     43  CD2 HIS A   6      13.354  29.171  10.548  1.00 10.84           C  
ATOM     44  CE1 HIS A   6      15.311  30.143  10.807  1.00 10.58           C  
ATOM     45  NE2 HIS A   6      14.719  29.066  10.335  1.00  6.81           N  
ATOM     46  N   ALA A   7       9.966  31.913  14.186  1.00 12.28           N  
ATOM     47  CA  ALA A   7       9.144  32.950  14.788  1.00 13.84           C  
ATOM     48  C   ALA A   7       9.594  33.160  16.244  1.00 14.46           C  
ATOM     49  O   ALA A   7       9.732  34.294  16.709  1.00 16.05           O  
ATOM     50  CB  ALA A   7       7.656  32.555  14.731  1.00 12.70           C  
ATOM     51  N   THR A   8       9.862  32.059  16.939  1.00 13.92           N  
ATOM     52  CA  THR A   8      10.301  32.109  18.329  1.00 12.34           C  
ATOM     53  C   THR A   8      11.611  32.871  18.461  1.00 11.43           C  
ATOM     54  O   THR A   8      11.730  33.763  19.296  1.00 13.36           O  
ATOM     55  CB  THR A   8      10.440  30.678  18.921  1.00 13.15           C  
ATOM     56  OG1 THR A   8       9.193  29.989  18.783  1.00 14.92           O  
ATOM     57  CG2 THR A   8      10.806  30.726  20.401  1.00 11.90           C  
ATOM     58  N   VAL A   9      12.611  32.506  17.667  1.00  9.84           N  
ATOM     59  CA  VAL A   9      13.899  33.198  17.697  1.00 11.07           C  
ATOM     60  C   VAL A   9      13.662  34.713  17.530  1.00 12.14           C  
ATOM     61  O   VAL A   9      14.247  35.537  18.251  1.00 10.40           O  
ATOM     62  CB  VAL A   9      14.830  32.675  16.551  1.00 11.49           C  
ATOM     63  CG1 VAL A   9      15.992  33.642  16.276  1.00 11.81           C  
ATOM     64  CG2 VAL A   9      15.389  31.300  16.919  1.00 10.17           C  
ATOM     65  N   ALA A  10      12.754  35.068  16.612  1.00 13.06           N  
ATOM     66  CA  ALA A  10      12.427  36.469  16.326  1.00 14.14           C  
ATOM     67  C   ALA A  10      11.771  37.193  17.513  1.00 13.98           C  
ATOM     68  O   ALA A  10      12.175  38.307  17.857  1.00 14.57           O  
ATOM     69  CB  ALA A  10      11.549  36.558  15.099  1.00 13.40           C  
ATOM     70  N   TYR A  11      10.784  36.557  18.144  1.00 14.29           N  
ATOM     71  CA  TYR A  11      10.117  37.146  19.310  1.00 15.13           C  
ATOM     72  C   TYR A  11      11.109  37.362  20.460  1.00 16.18           C  
ATOM     73  O   TYR A  11      11.074  38.398  21.139  1.00 17.72           O  
ATOM     74  CB  TYR A  11       8.945  36.279  19.768  1.00 15.34           C  
ATOM     75  CG  TYR A  11       7.647  36.561  19.044  1.00 18.48           C  
ATOM     76  CD1 TYR A  11       7.129  37.861  18.971  1.00 18.51           C  
ATOM     77  CD2 TYR A  11       6.927  35.533  18.442  1.00 17.46           C  
ATOM     78  CE1 TYR A  11       5.921  38.126  18.321  1.00 18.97           C  
ATOM     79  CE2 TYR A  11       5.716  35.789  17.794  1.00 19.67           C  
ATOM     80  CZ  TYR A  11       5.224  37.086  17.736  1.00 19.84           C  
ATOM     81  OH  TYR A  11       4.027  37.328  17.099  1.00 22.44           O  
ATOM     82  N   VAL A  12      12.026  36.410  20.653  1.00 16.13           N  
ATOM     83  CA  VAL A  12      13.051  36.538  21.696  1.00 14.77           C  
ATOM     84  C   VAL A  12      13.918  37.764  21.360  1.00 16.41           C  
ATOM     85  O   VAL A  12      14.226  38.568  22.250  1.00 15.19           O  
ATOM     86  CB  VAL A  12      13.976  35.251  21.805  1.00 14.29           C  
ATOM     87  CG1 VAL A  12      15.201  35.529  22.674  1.00 10.60           C  
ATOM     88  CG2 VAL A  12      13.200  34.080  22.388  1.00 12.22           C  
ATOM     89  N   ALA A  13      14.299  37.913  20.084  1.00 14.80           N  
ATOM     90  CA  ALA A  13      15.121  39.044  19.672  1.00 14.21           C  
ATOM     91  C   ALA A  13      14.414  40.367  19.901  1.00 13.17           C  
ATOM     92  O   ALA A  13      15.031  41.318  20.358  1.00 14.44           O  
ATOM     93  CB  ALA A  13      15.520  38.917  18.211  1.00 13.46           C  
ATOM     94  N   GLN A  14      13.132  40.424  19.562  1.00 13.09           N  
ATOM     95  CA  GLN A  14      12.328  41.632  19.722  1.00 16.36           C  
ATOM     96  C   GLN A  14      12.383  42.149  21.169  1.00 18.52           C  
ATOM     97  O   GLN A  14      12.400  43.366  21.414  1.00 19.90           O  
ATOM     98  CB  GLN A  14      10.867  41.375  19.315  1.00 15.80           C  
ATOM     99  CG  GLN A  14      10.649  41.270  17.813  1.00 16.00           C  
ATOM    100  CD  GLN A  14       9.189  41.042  17.423  1.00 19.46           C  
ATOM    101  OE1 GLN A  14       8.894  40.626  16.290  1.00 19.93           O  
ATOM    102  NE2 GLN A  14       8.268  41.298  18.351  1.00 18.93           N  
ATOM    103  N   HIS A  15      12.449  41.226  22.118  1.00 16.23           N  
ATOM    104  CA  HIS A  15      12.505  41.603  23.517  1.00 15.79           C  
ATOM    105  C   HIS A  15      13.802  42.305  23.936  1.00 16.16           C  
ATOM    106  O   HIS A  15      13.798  43.161  24.839  1.00 14.34           O  
ATOM    107  CB  HIS A  15      12.319  40.363  24.394  1.00 13.82           C  
ATOM    108  CG  HIS A  15      12.137  40.691  25.841  1.00 16.86           C  
ATOM    109  ND1 HIS A  15      10.891  40.965  26.379  1.00 15.65           N  
ATOM    110  CD2 HIS A  15      13.018  40.875  26.836  1.00 14.51           C  
ATOM    111  CE1 HIS A  15      11.022  41.306  27.635  1.00 15.81           C  
ATOM    112  NE2 HIS A  15      12.295  41.268  27.955  1.00 15.35           N  
ATOM    113  N   TYR A  16      14.905  41.918  23.305  1.00 15.53           N  
ATOM    114  CA  TYR A  16      16.219  42.426  23.663  1.00 16.00           C  
ATOM    115  C   TYR A  16      16.837  43.536  22.830  1.00 16.11           C  
ATOM    116  O   TYR A  16      17.954  43.961  23.103  1.00 15.78           O  
ATOM    117  CB  TYR A  16      17.186  41.239  23.815  1.00 17.35           C  
ATOM    118  CG  TYR A  16      16.819  40.364  24.978  1.00 16.65           C  
ATOM    119  CD1 TYR A  16      17.092  40.776  26.274  1.00 17.65           C  
ATOM    120  CD2 TYR A  16      16.146  39.158  24.796  1.00 16.74           C  
ATOM    121  CE1 TYR A  16      16.670  40.028  27.374  1.00 17.90           C  
ATOM    122  CE2 TYR A  16      15.721  38.398  25.882  1.00 18.09           C  
ATOM    123  CZ  TYR A  16      15.990  38.838  27.177  1.00 20.07           C  
ATOM    124  OH  TYR A  16      15.501  38.173  28.286  1.00 20.59           O  
ATOM    125  N   VAL A  17      16.142  43.984  21.796  1.00 18.59           N  
ATOM    126  CA  VAL A  17      16.661  45.075  20.967  1.00 21.11           C  
ATOM    127  C   VAL A  17      16.405  46.410  21.680  1.00 22.50           C  
ATOM    128  O   VAL A  17      15.385  46.574  22.341  1.00 22.13           O  
ATOM    129  CB  VAL A  17      15.991  45.100  19.566  1.00 22.05           C  
ATOM    130  CG1 VAL A  17      16.459  43.908  18.737  1.00 20.98           C  
ATOM    131  CG2 VAL A  17      14.476  45.081  19.696  1.00 22.37           C  
ATOM    132  N   SER A  18      17.328  47.352  21.573  1.00 23.91           N  
ATOM    133  CA  SER A  18      17.149  48.636  22.235  1.00 27.89           C  
ATOM    134  C   SER A  18      15.971  49.354  21.590  1.00 30.21           C  
ATOM    135  O   SER A  18      15.652  49.103  20.427  1.00 30.65           O  
ATOM    136  CB  SER A  18      18.418  49.485  22.087  1.00 28.68           C  
ATOM    137  OG  SER A  18      18.514  50.077  20.796  1.00 32.24           O  
ATOM    138  N   PRO A  19      15.333  50.286  22.317  1.00 32.22           N  
ATOM    139  CA  PRO A  19      14.198  50.975  21.699  1.00 33.81           C  
ATOM    140  C   PRO A  19      14.540  51.696  20.390  1.00 34.54           C  
ATOM    141  O   PRO A  19      13.724  51.776  19.506  1.00 34.66           O  
ATOM    142  CB  PRO A  19      13.730  51.941  22.805  1.00 34.74           C  
ATOM    143  CG  PRO A  19      14.255  51.365  24.042  1.00 34.22           C  
ATOM    144  CD  PRO A  19      15.620  50.879  23.629  1.00 32.56           C  
ATOM    145  N   GLU A  20      15.729  52.270  20.301  1.00 35.34           N  
ATOM    146  CA  GLU A  20      16.237  52.992  19.126  1.00 37.83           C  
ATOM    147  C   GLU A  20      16.433  52.030  17.948  1.00 37.08           C  
ATOM    148  O   GLU A  20      16.069  52.363  16.802  1.00 36.59           O  
ATOM    149  CB  GLU A  20      17.586  53.729  19.416  1.00 41.69           C  
ATOM    150  CG  GLU A  20      17.616  54.577  20.686  1.00 52.58           C  
ATOM    151  CD  GLU A  20      17.614  53.717  21.971  1.00 57.33           C  
ATOM    152  OE1 GLU A  20      17.822  52.486  21.906  1.00 60.68           O  
ATOM    153  OE2 GLU A  20      17.445  54.273  23.074  1.00 62.07           O  
ATOM    154  N   ALA A  21      17.102  50.894  18.196  1.00 35.61           N  
ATOM    155  CA  ALA A  21      17.339  49.829  17.209  1.00 35.04           C  
ATOM    156  C   ALA A  21      15.998  49.273  16.696  1.00 34.54           C  
ATOM    157  O   ALA A  21      15.867  48.856  15.523  1.00 34.68           O  
ATOM    158  CB  ALA A  21      18.093  48.686  17.864  1.00 35.11           C  
ATOM    159  N   ALA A  22      15.003  49.228  17.589  1.00 34.22           N  
ATOM    160  CA  ALA A  22      13.728  48.693  17.212  1.00 34.75           C  
ATOM    161  C   ALA A  22      12.973  49.703  16.336  1.00 35.73           C  
ATOM    162  O   ALA A  22      12.118  49.300  15.505  1.00 35.06           O  
ATOM    163  CB  ALA A  22      12.981  48.200  18.389  1.00 34.18           C  
ATOM    164  N   SER A  23      13.293  50.993  16.455  1.00 36.67           N  
ATOM    165  CA  SER A  23      12.628  51.828  15.527  1.00 37.63           C  
ATOM    166  C   SER A  23      13.306  51.839  14.130  1.00 36.43           C  
ATOM    167  O   SER A  23      12.583  52.006  13.155  1.00 36.45           O  
ATOM    168  CB  SER A  23      12.133  53.112  16.179  1.00 39.52           C  
ATOM    169  OG  SER A  23      13.209  53.964  16.136  1.00 42.27           O  
ATOM    170  N   TRP A  24      14.637  51.782  14.048  1.00 36.40           N  
ATOM    171  CA  TRP A  24      15.386  51.616  12.760  1.00 38.02           C  
ATOM    172  C   TRP A  24      14.967  50.301  12.040  1.00 37.87           C  
ATOM    173  O   TRP A  24      14.741  50.297  10.838  1.00 39.14           O  
ATOM    174  CB  TRP A  24      16.952  51.669  12.927  1.00 39.62           C  
ATOM    175  CG  TRP A  24      17.880  51.007  11.821  1.00 41.72           C  
ATOM    176  CD1 TRP A  24      18.415  51.617  10.716  1.00 42.69           C  
ATOM    177  CD2 TRP A  24      18.455  49.688  11.847  1.00 42.31           C  
ATOM    178  NE1 TRP A  24      19.291  50.773  10.074  1.00 43.76           N  
ATOM    179  CE2 TRP A  24      19.335  49.575  10.751  1.00 42.78           C  
ATOM    180  CE3 TRP A  24      18.317  48.588  12.709  1.00 42.33           C  
ATOM    181  CZ2 TRP A  24      20.071  48.421  10.479  1.00 42.18           C  
ATOM    182  CZ3 TRP A  24      19.051  47.433  12.443  1.00 42.80           C  
ATOM    183  CH2 TRP A  24      19.917  47.361  11.338  1.00 42.30           C  
ATOM    184  N   ALA A  25      14.806  49.195  12.748  1.00 35.89           N  
ATOM    185  CA  ALA A  25      14.398  47.959  12.037  1.00 34.61           C  
ATOM    186  C   ALA A  25      12.971  47.999  11.499  1.00 33.86           C  
ATOM    187  O   ALA A  25      12.737  47.629  10.357  1.00 33.85           O  
ATOM    188  CB  ALA A  25      14.736  46.594  12.828  1.00 33.33           C  
ATOM    189  N   GLN A  26      12.082  48.605  12.272  1.00 33.50           N  
ATOM    190  CA  GLN A  26      10.672  48.835  11.922  1.00 34.77           C  
ATOM    191  C   GLN A  26      10.601  49.808  10.737  1.00 33.90           C  
ATOM    192  O   GLN A  26       9.693  49.704   9.884  1.00 33.35           O  
ATOM    193  CB  GLN A  26       9.929  49.508  13.085  1.00 36.79           C  
ATOM    194  CG  GLN A  26       9.451  48.560  14.148  1.00 40.71           C  
ATOM    195  CD  GLN A  26       9.015  49.231  15.419  1.00 42.44           C  
ATOM    196  OE1 GLN A  26       8.850  48.572  16.443  1.00 45.49           O  
ATOM    197  NE2 GLN A  26       8.842  50.542  15.377  1.00 42.65           N  
ATOM    198  N   GLY A  27      11.515  50.784  10.670  1.00 33.77           N  
ATOM    199  CA  GLY A  27      11.471  51.698   9.551  1.00 34.90           C  
ATOM    200  C   GLY A  27      11.927  50.930   8.323  1.00 34.84           C  
ATOM    201  O   GLY A  27      11.308  50.994   7.254  1.00 35.68           O  
ATOM    202  N   ILE A  28      13.045  50.232   8.469  1.00 34.16           N  
ATOM    203  CA  ILE A  28      13.590  49.466   7.368  1.00 34.78           C  
ATOM    204  C   ILE A  28      12.599  48.411   6.844  1.00 36.60           C  
ATOM    205  O   ILE A  28      12.475  48.239   5.639  1.00 37.57           O  
ATOM    206  CB  ILE A  28      14.961  48.855   7.746  1.00 33.07           C  
ATOM    207  CG1 ILE A  28      16.016  49.963   7.832  1.00 33.14           C  
ATOM    208  CG2 ILE A  28      15.362  47.789   6.750  1.00 34.36           C  
ATOM    209  CD1 ILE A  28      17.434  49.460   7.951  1.00 31.61           C  
ATOM    210  N   LEU A  29      11.834  47.780   7.732  1.00 37.70           N  
ATOM    211  CA  LEU A  29      10.864  46.737   7.356  1.00 38.88           C  
ATOM    212  C   LEU A  29       9.500  47.294   6.980  1.00 39.45           C  
ATOM    213  O   LEU A  29       8.592  46.569   6.589  1.00 39.05           O  
ATOM    214  CB  LEU A  29      10.665  45.748   8.507  1.00 39.02           C  
ATOM    215  CG  LEU A  29      11.260  44.344   8.366  1.00 41.31           C  
ATOM    216  CD1 LEU A  29      12.554  44.354   7.551  1.00 40.21           C  
ATOM    217  CD2 LEU A  29      11.493  43.771   9.766  1.00 39.60           C  
ATOM    218  N   GLY A  30       9.325  48.583   7.204  1.00 40.89           N  
ATOM    219  CA  GLY A  30       8.059  49.199   6.875  1.00 42.41           C  
ATOM    220  C   GLY A  30       6.900  48.683   7.702  1.00 44.65           C  
ATOM    221  O   GLY A  30       5.746  48.806   7.272  1.00 45.44           O  
ATOM    222  N   SER A  31       7.186  48.108   8.873  1.00 45.95           N  
ATOM    223  CA  SER A  31       6.122  47.617   9.753  1.00 47.27           C  
ATOM    224  C   SER A  31       6.421  47.929  11.204  1.00 47.60           C  
ATOM    225  O   SER A  31       7.505  47.612  11.698  1.00 47.80           O  
ATOM    226  CB  SER A  31       5.893  46.118   9.609  1.00 47.68           C  
ATOM    227  OG  SER A  31       4.876  45.701  10.515  1.00 49.63           O  
ATOM    228  N   SER A  32       5.440  48.507  11.894  1.00 48.18           N  
ATOM    229  CA  SER A  32       5.595  48.873  13.301  1.00 48.77           C  
ATOM    230  C   SER A  32       4.814  47.927  14.184  1.00 47.95           C  
ATOM    231  O   SER A  32       4.580  48.208  15.379  1.00 49.02           O  
ATOM    232  CB  SER A  32       5.067  50.291  13.526  1.00 50.60           C  
ATOM    233  OG  SER A  32       5.791  51.217  12.741  1.00 53.92           O  
ATOM    234  N   SER A  33       4.457  46.774  13.617  1.00 45.74           N  
ATOM    235  CA  SER A  33       3.683  45.821  14.347  1.00 43.71           C  
ATOM    236  C   SER A  33       4.382  45.145  15.518  1.00 41.75           C  
ATOM    237  O   SER A  33       5.619  45.108  15.606  1.00 41.39           O  
ATOM    238  CB  SER A  33       3.214  44.773  13.386  1.00 44.94           C  
ATOM    239  OG  SER A  33       4.156  43.726  13.349  1.00 47.83           O  
ATOM    240  N   SER A  34       3.581  44.420  16.290  1.00 39.45           N  
ATOM    241  CA  SER A  34       4.110  43.698  17.423  1.00 38.64           C  
ATOM    242  C   SER A  34       4.871  42.452  16.971  1.00 35.85           C  
ATOM    243  O   SER A  34       5.532  41.792  17.764  1.00 35.34           O  
ATOM    244  CB  SER A  34       2.973  43.299  18.333  1.00 39.04           C  
ATOM    245  OG  SER A  34       1.926  42.782  17.541  1.00 44.07           O  
ATOM    246  N   SER A  35       4.719  42.103  15.703  1.00 33.91           N  
ATOM    247  CA  SER A  35       5.378  40.940  15.151  1.00 31.43           C  
ATOM    248  C   SER A  35       6.275  41.414  14.033  1.00 29.16           C  
ATOM    249  O   SER A  35       6.508  40.684  13.074  1.00 29.63           O  
ATOM    250  CB  SER A  35       4.316  40.004  14.585  1.00 32.68           C  
ATOM    251  OG  SER A  35       3.692  40.593  13.451  1.00 38.44           O  
ATOM    252  N   TYR A  36       6.797  42.625  14.153  1.00 26.27           N  
ATOM    253  CA  TYR A  36       7.616  43.157  13.082  1.00 25.76           C  
ATOM    254  C   TYR A  36       8.755  42.250  12.599  1.00 25.28           C  
ATOM    255  O   TYR A  36       9.019  42.196  11.398  1.00 25.63           O  
ATOM    256  CB  TYR A  36       8.075  44.586  13.384  1.00 24.68           C  
ATOM    257  CG  TYR A  36       9.173  44.719  14.404  1.00 23.21           C  
ATOM    258  CD1 TYR A  36       8.902  44.667  15.769  1.00 23.19           C  
ATOM    259  CD2 TYR A  36      10.481  44.964  14.002  1.00 23.39           C  
ATOM    260  CE1 TYR A  36       9.921  44.865  16.707  1.00 22.23           C  
ATOM    261  CE2 TYR A  36      11.504  45.153  14.929  1.00 21.49           C  
ATOM    262  CZ  TYR A  36      11.213  45.108  16.270  1.00 21.60           C  
ATOM    263  OH  TYR A  36      12.228  45.309  17.163  1.00 23.21           O  
ATOM    264  N   LEU A  37       9.409  41.520  13.506  1.00 23.18           N  
ATOM    265  CA  LEU A  37      10.481  40.607  13.083  1.00 20.56           C  
ATOM    266  C   LEU A  37       9.932  39.194  12.882  1.00 20.09           C  
ATOM    267  O   LEU A  37      10.250  38.529  11.900  1.00 19.30           O  
ATOM    268  CB  LEU A  37      11.642  40.549  14.095  1.00 18.34           C  
ATOM    269  CG  LEU A  37      12.599  41.729  14.333  1.00 17.98           C  
ATOM    270  CD1 LEU A  37      13.665  41.312  15.320  1.00 14.61           C  
ATOM    271  CD2 LEU A  37      13.255  42.181  13.036  1.00 17.54           C  
ATOM    272  N   ALA A  38       9.070  38.757  13.796  1.00 18.76           N  
ATOM    273  CA  ALA A  38       8.508  37.411  13.746  1.00 19.38           C  
ATOM    274  C   ALA A  38       7.743  37.058  12.472  1.00 20.79           C  
ATOM    275  O   ALA A  38       7.849  35.933  11.975  1.00 18.82           O  
ATOM    276  CB  ALA A  38       7.624  37.170  14.953  1.00 20.25           C  
ATOM    277  N   SER A  39       6.989  38.020  11.944  1.00 20.20           N  
ATOM    278  CA  SER A  39       6.185  37.799  10.751  1.00 21.05           C  
ATOM    279  C   SER A  39       6.991  37.553   9.477  1.00 20.99           C  
ATOM    280  O   SER A  39       6.470  36.997   8.513  1.00 22.98           O  
ATOM    281  CB  SER A  39       5.245  38.979  10.540  1.00 22.22           C  
ATOM    282  OG  SER A  39       5.993  40.171  10.353  1.00 26.70           O  
ATOM    283  N   ILE A  40       8.253  37.954   9.465  1.00 19.31           N  
ATOM    284  CA  ILE A  40       9.074  37.757   8.282  1.00 19.71           C  
ATOM    285  C   ILE A  40      10.241  36.803   8.528  1.00 18.68           C  
ATOM    286  O   ILE A  40      11.125  36.658   7.678  1.00 18.09           O  
ATOM    287  CB  ILE A  40       9.575  39.119   7.737  1.00 20.77           C  
ATOM    288  CG1 ILE A  40      10.182  39.978   8.859  1.00 19.16           C  
ATOM    289  CG2 ILE A  40       8.417  39.874   7.113  1.00 20.63           C  
ATOM    290  CD1 ILE A  40      11.648  39.743   9.123  1.00 18.85           C  
ATOM    291  N   ALA A  41      10.216  36.115   9.669  1.00 18.52           N  
ATOM    292  CA  ALA A  41      11.289  35.190  10.036  1.00 16.94           C  
ATOM    293  C   ALA A  41      11.449  33.984   9.099  1.00 15.75           C  
ATOM    294  O   ALA A  41      12.532  33.403   9.029  1.00 14.74           O  
ATOM    295  CB  ALA A  41      11.120  34.731  11.497  1.00 15.99           C  
ATOM    296  N   SER A  42      10.385  33.604   8.391  1.00 16.82           N  
ATOM    297  CA  SER A  42      10.442  32.481   7.458  1.00 18.46           C  
ATOM    298  C   SER A  42      10.443  32.896   5.989  1.00 19.57           C  
ATOM    299  O   SER A  42      10.405  32.030   5.118  1.00 18.99           O  
ATOM    300  CB  SER A  42       9.277  31.508   7.690  1.00 19.53           C  
ATOM    301  OG  SER A  42       9.524  30.668   8.814  1.00 21.51           O  
ATOM    302  N   TRP A  43      10.509  34.196   5.706  1.00 19.05           N  
ATOM    303  CA  TRP A  43      10.500  34.659   4.319  1.00 18.62           C  
ATOM    304  C   TRP A  43      11.567  34.005   3.445  1.00 18.23           C  
ATOM    305  O   TRP A  43      11.268  33.595   2.323  1.00 19.34           O  
ATOM    306  CB  TRP A  43      10.636  36.184   4.238  1.00 19.25           C  
ATOM    307  CG  TRP A  43      10.905  36.698   2.822  1.00 20.11           C  
ATOM    308  CD1 TRP A  43       9.978  36.977   1.859  1.00 20.43           C  
ATOM    309  CD2 TRP A  43      12.191  36.951   2.227  1.00 18.79           C  
ATOM    310  NE1 TRP A  43      10.610  37.380   0.700  1.00 18.41           N  
ATOM    311  CE2 TRP A  43      11.957  37.360   0.896  1.00 18.97           C  
ATOM    312  CE3 TRP A  43      13.505  36.848   2.685  1.00 19.86           C  
ATOM    313  CZ2 TRP A  43      12.998  37.683   0.031  1.00 18.10           C  
ATOM    314  CZ3 TRP A  43      14.542  37.170   1.820  1.00 21.00           C  
ATOM    315  CH2 TRP A  43      14.280  37.573   0.504  1.00 19.88           C  
ATOM    316  N   ALA A  44      12.792  33.876   3.953  1.00 15.40           N  
ATOM    317  CA  ALA A  44      13.866  33.281   3.166  1.00 15.70           C  
ATOM    318  C   ALA A  44      13.564  31.849   2.721  1.00 16.96           C  
ATOM    319  O   ALA A  44      14.092  31.381   1.717  1.00 17.53           O  
ATOM    320  CB  ALA A  44      15.185  33.347   3.908  1.00 13.52           C  
ATOM    321  N   ASP A  45      12.766  31.120   3.489  1.00 15.32           N  
ATOM    322  CA  ASP A  45      12.441  29.763   3.087  1.00 16.85           C  
ATOM    323  C   ASP A  45      11.446  29.795   1.935  1.00 19.42           C  
ATOM    324  O   ASP A  45      11.532  28.990   1.017  1.00 20.65           O  
ATOM    325  CB  ASP A  45      11.856  28.966   4.249  1.00 15.86           C  
ATOM    326  CG  ASP A  45      12.922  28.420   5.195  1.00 13.91           C  
ATOM    327  OD1 ASP A  45      14.129  28.471   4.887  1.00 11.29           O  
ATOM    328  OD2 ASP A  45      12.531  27.908   6.266  1.00 15.74           O  
ATOM    329  N   GLU A  46      10.512  30.737   1.983  1.00 20.77           N  
ATOM    330  CA  GLU A  46       9.501  30.876   0.929  1.00 24.47           C  
ATOM    331  C   GLU A  46      10.180  31.315  -0.353  1.00 23.19           C  
ATOM    332  O   GLU A  46       9.873  30.827  -1.441  1.00 24.70           O  
ATOM    333  CB  GLU A  46       8.462  31.920   1.321  1.00 26.92           C  
ATOM    334  CG  GLU A  46       8.088  31.812   2.769  1.00 36.33           C  
ATOM    335  CD  GLU A  46       6.757  32.427   3.102  1.00 41.82           C  
ATOM    336  OE1 GLU A  46       6.024  32.825   2.167  1.00 46.73           O  
ATOM    337  OE2 GLU A  46       6.432  32.481   4.312  1.00 44.97           O  
ATOM    338  N   TYR A  47      11.155  32.195  -0.206  1.00 21.23           N  
ATOM    339  CA  TYR A  47      11.881  32.719  -1.341  1.00 20.80           C  
ATOM    340  C   TYR A  47      12.644  31.650  -2.099  1.00 22.12           C  
ATOM    341  O   TYR A  47      12.655  31.655  -3.331  1.00 23.26           O  
ATOM    342  CB  TYR A  47      12.837  33.805  -0.872  1.00 18.79           C  
ATOM    343  CG  TYR A  47      13.718  34.421  -1.934  1.00 16.45           C  
ATOM    344  CD1 TYR A  47      13.183  35.225  -2.940  1.00 18.37           C  
ATOM    345  CD2 TYR A  47      15.093  34.265  -1.880  1.00 16.29           C  
ATOM    346  CE1 TYR A  47      14.006  35.859  -3.869  1.00 17.49           C  
ATOM    347  CE2 TYR A  47      15.925  34.893  -2.792  1.00 17.29           C  
ATOM    348  CZ  TYR A  47      15.372  35.691  -3.784  1.00 18.43           C  
ATOM    349  OH  TYR A  47      16.213  36.300  -4.695  1.00 22.86           O  
ATOM    350  N   ARG A  48      13.270  30.720  -1.392  1.00 21.48           N  
ATOM    351  CA  ARG A  48      14.038  29.701  -2.091  1.00 21.57           C  
ATOM    352  C   ARG A  48      13.129  28.745  -2.868  1.00 21.64           C  
ATOM    353  O   ARG A  48      13.581  28.003  -3.725  1.00 20.93           O  
ATOM    354  CB  ARG A  48      14.958  28.947  -1.136  1.00 22.12           C  
ATOM    355  CG  ARG A  48      14.230  27.987  -0.266  1.00 20.90           C  
ATOM    356  CD  ARG A  48      15.149  27.049   0.495  1.00 22.11           C  
ATOM    357  NE  ARG A  48      14.314  26.311   1.436  1.00 19.82           N  
ATOM    358  CZ  ARG A  48      14.695  25.916   2.641  1.00 18.96           C  
ATOM    359  NH1 ARG A  48      15.924  26.151   3.081  1.00 16.59           N  
ATOM    360  NH2 ARG A  48      13.794  25.389   3.444  1.00 21.15           N  
ATOM    361  N   LEU A  49      11.833  28.800  -2.605  1.00 22.42           N  
ATOM    362  CA  LEU A  49      10.897  27.951  -3.330  1.00 23.46           C  
ATOM    363  C   LEU A  49      10.503  28.562  -4.684  1.00 25.84           C  
ATOM    364  O   LEU A  49       9.661  28.005  -5.395  1.00 28.35           O  
ATOM    365  CB  LEU A  49       9.649  27.716  -2.490  1.00 24.30           C  
ATOM    366  CG  LEU A  49       9.491  26.349  -1.823  1.00 24.87           C  
ATOM    367  CD1 LEU A  49      10.832  25.738  -1.495  1.00 23.11           C  
ATOM    368  CD2 LEU A  49       8.634  26.514  -0.589  1.00 24.44           C  
ATOM    369  N   THR A  50      11.081  29.711  -5.028  1.00 25.41           N  
ATOM    370  CA  THR A  50      10.769  30.369  -6.291  1.00 24.54           C  
ATOM    371  C   THR A  50      11.964  30.284  -7.226  1.00 24.84           C  
ATOM    372  O   THR A  50      13.109  30.142  -6.774  1.00 24.07           O  
ATOM    373  CB  THR A  50      10.407  31.871  -6.110  1.00 23.07           C  
ATOM    374  OG1 THR A  50      11.583  32.614  -5.759  1.00 22.20           O  
ATOM    375  CG2 THR A  50       9.344  32.055  -5.049  1.00 20.16           C  
ATOM    376  N   SER A  51      11.699  30.400  -8.526  1.00 24.55           N  
ATOM    377  CA  SER A  51      12.766  30.356  -9.512  1.00 25.67           C  
ATOM    378  C   SER A  51      13.740  31.492  -9.246  1.00 24.02           C  
ATOM    379  O   SER A  51      14.950  31.321  -9.356  1.00 24.16           O  
ATOM    380  CB  SER A  51      12.201  30.478 -10.927  1.00 28.39           C  
ATOM    381  OG  SER A  51      11.590  31.738 -11.140  1.00 34.19           O  
ATOM    382  N   ALA A  52      13.203  32.647  -8.870  1.00 24.04           N  
ATOM    383  CA  ALA A  52      14.039  33.801  -8.569  1.00 25.69           C  
ATOM    384  C   ALA A  52      14.951  33.516  -7.368  1.00 25.75           C  
ATOM    385  O   ALA A  52      16.117  33.936  -7.347  1.00 26.15           O  
ATOM    386  CB  ALA A  52      13.166  35.015  -8.284  1.00 26.69           C  
ATOM    387  N   GLY A  53      14.429  32.762  -6.403  1.00 24.65           N  
ATOM    388  CA  GLY A  53      15.199  32.472  -5.213  1.00 24.51           C  
ATOM    389  C   GLY A  53      16.025  31.209  -5.106  1.00 24.51           C  
ATOM    390  O   GLY A  53      16.862  31.121  -4.188  1.00 24.19           O  
ATOM    391  N   LYS A  54      15.846  30.257  -6.026  1.00 22.93           N  
ATOM    392  CA  LYS A  54      16.587  28.988  -5.979  1.00 20.59           C  
ATOM    393  C   LYS A  54      18.074  29.096  -5.693  1.00 18.67           C  
ATOM    394  O   LYS A  54      18.649  28.227  -5.050  1.00 17.95           O  
ATOM    395  CB  LYS A  54      16.396  28.186  -7.276  1.00 22.86           C  
ATOM    396  CG  LYS A  54      14.985  27.698  -7.515  1.00 23.53           C  
ATOM    397  CD  LYS A  54      14.659  26.440  -6.735  1.00 26.33           C  
ATOM    398  CE  LYS A  54      13.149  26.367  -6.525  1.00 30.00           C  
ATOM    399  NZ  LYS A  54      12.576  25.025  -6.774  1.00 34.98           N  
ATOM    400  N   TRP A  55      18.707  30.148  -6.192  1.00 17.29           N  
ATOM    401  CA  TRP A  55      20.140  30.331  -5.991  1.00 17.65           C  
ATOM    402  C   TRP A  55      20.547  30.408  -4.513  1.00 17.78           C  
ATOM    403  O   TRP A  55      21.683  30.079  -4.167  1.00 17.13           O  
ATOM    404  CB  TRP A  55      20.601  31.622  -6.687  1.00 16.56           C  
ATOM    405  CG  TRP A  55      20.080  32.875  -6.036  1.00 16.10           C  
ATOM    406  CD1 TRP A  55      18.879  33.476  -6.261  1.00 16.94           C  
ATOM    407  CD2 TRP A  55      20.717  33.631  -4.991  1.00 17.45           C  
ATOM    408  NE1 TRP A  55      18.721  34.550  -5.413  1.00 18.64           N  
ATOM    409  CE2 TRP A  55      19.831  34.660  -4.624  1.00 18.09           C  
ATOM    410  CE3 TRP A  55      21.949  33.523  -4.328  1.00 20.06           C  
ATOM    411  CZ2 TRP A  55      20.139  35.583  -3.610  1.00 20.04           C  
ATOM    412  CZ3 TRP A  55      22.254  34.443  -3.322  1.00 19.64           C  
ATOM    413  CH2 TRP A  55      21.348  35.455  -2.974  1.00 18.45           C  
ATOM    414  N   SER A  56      19.626  30.874  -3.660  1.00 18.39           N  
ATOM    415  CA  SER A  56      19.891  31.074  -2.222  1.00 17.23           C  
ATOM    416  C   SER A  56      19.775  29.864  -1.299  1.00 18.23           C  
ATOM    417  O   SER A  56      20.077  29.971  -0.101  1.00 15.16           O  
ATOM    418  CB  SER A  56      19.012  32.197  -1.666  1.00 15.43           C  
ATOM    419  OG  SER A  56      17.640  31.858  -1.687  1.00 17.49           O  
ATOM    420  N   ALA A  57      19.400  28.708  -1.849  1.00 16.33           N  
ATOM    421  CA  ALA A  57      19.249  27.512  -1.029  1.00 16.25           C  
ATOM    422  C   ALA A  57      20.493  27.171  -0.223  1.00 16.11           C  
ATOM    423  O   ALA A  57      20.385  26.866   0.956  1.00 15.18           O  
ATOM    424  CB  ALA A  57      18.810  26.315  -1.873  1.00 15.04           C  
ATOM    425  N   SER A  58      21.671  27.284  -0.818  1.00 15.22           N  
ATOM    426  CA  SER A  58      22.897  26.929  -0.120  1.00 16.35           C  
ATOM    427  C   SER A  58      23.286  27.843   1.039  1.00 15.58           C  
ATOM    428  O   SER A  58      24.155  27.510   1.820  1.00 17.37           O  
ATOM    429  CB  SER A  58      24.053  26.855  -1.123  1.00 19.86           C  
ATOM    430  OG  SER A  58      24.312  28.138  -1.671  1.00 25.67           O  
ATOM    431  N   LEU A  59      22.644  28.990   1.162  1.00 15.08           N  
ATOM    432  CA  LEU A  59      22.989  29.942   2.222  1.00 15.29           C  
ATOM    433  C   LEU A  59      22.440  29.553   3.581  1.00 13.97           C  
ATOM    434  O   LEU A  59      22.843  30.110   4.596  1.00 14.04           O  
ATOM    435  CB  LEU A  59      22.452  31.341   1.879  1.00 13.14           C  
ATOM    436  CG  LEU A  59      23.000  32.016   0.616  1.00 14.91           C  
ATOM    437  CD1 LEU A  59      22.256  33.309   0.388  1.00 15.12           C  
ATOM    438  CD2 LEU A  59      24.505  32.242   0.733  1.00 13.89           C  
ATOM    439  N   HIS A  60      21.493  28.631   3.599  1.00 12.60           N  
ATOM    440  CA  HIS A  60      20.877  28.229   4.849  1.00 11.77           C  
ATOM    441  C   HIS A  60      21.711  27.304   5.728  1.00 11.74           C  
ATOM    442  O   HIS A  60      21.317  27.034   6.870  1.00 14.21           O  
ATOM    443  CB  HIS A  60      19.524  27.597   4.560  1.00 10.26           C  
ATOM    444  CG  HIS A  60      18.592  28.502   3.819  1.00 11.65           C  
ATOM    445  ND1 HIS A  60      17.360  28.876   4.309  1.00 10.01           N  
ATOM    446  CD2 HIS A  60      18.708  29.103   2.610  1.00 11.16           C  
ATOM    447  CE1 HIS A  60      16.752  29.659   3.437  1.00 11.30           C  
ATOM    448  NE2 HIS A  60      17.552  29.814   2.396  1.00  9.47           N  
ATOM    449  N   PHE A  61      22.869  26.863   5.257  1.00 10.29           N  
ATOM    450  CA  PHE A  61      23.653  25.924   6.051  1.00 10.45           C  
ATOM    451  C   PHE A  61      25.111  25.919   5.694  1.00 10.43           C  
ATOM    452  O   PHE A  61      25.542  26.684   4.828  1.00 11.96           O  
ATOM    453  CB  PHE A  61      23.098  24.502   5.833  1.00 11.94           C  
ATOM    454  CG  PHE A  61      22.946  24.120   4.376  1.00 12.16           C  
ATOM    455  CD1 PHE A  61      24.062  23.775   3.608  1.00 12.12           C  
ATOM    456  CD2 PHE A  61      21.700  24.193   3.755  1.00 13.59           C  
ATOM    457  CE1 PHE A  61      23.934  23.505   2.241  1.00 12.94           C  
ATOM    458  CE2 PHE A  61      21.561  23.921   2.379  1.00 14.02           C  
ATOM    459  CZ  PHE A  61      22.682  23.588   1.627  1.00 11.44           C  
ATOM    460  N   ILE A  62      25.890  25.153   6.449  1.00 10.60           N  
ATOM    461  CA  ILE A  62      27.301  24.970   6.144  1.00 13.67           C  
ATOM    462  C   ILE A  62      27.578  23.471   6.309  1.00 16.62           C  
ATOM    463  O   ILE A  62      27.361  22.894   7.381  1.00 14.47           O  
ATOM    464  CB  ILE A  62      28.284  25.885   6.965  1.00 15.14           C  
ATOM    465  CG1 ILE A  62      29.729  25.530   6.614  1.00 15.93           C  
ATOM    466  CG2 ILE A  62      28.046  25.799   8.459  1.00 16.69           C  
ATOM    467  CD1 ILE A  62      30.688  26.675   6.782  1.00 16.89           C  
ATOM    468  N   ASP A  63      27.942  22.811   5.210  1.00 16.77           N  
ATOM    469  CA  ASP A  63      28.214  21.372   5.257  1.00 18.17           C  
ATOM    470  C   ASP A  63      29.588  21.046   5.815  1.00 16.64           C  
ATOM    471  O   ASP A  63      30.522  20.766   5.058  1.00 16.12           O  
ATOM    472  CB  ASP A  63      28.037  20.733   3.870  1.00 19.22           C  
ATOM    473  CG  ASP A  63      26.592  20.743   3.411  1.00 25.13           C  
ATOM    474  OD1 ASP A  63      25.685  20.364   4.202  1.00 25.88           O  
ATOM    475  OD2 ASP A  63      26.347  21.156   2.256  1.00 27.91           O  
ATOM    476  N   ALA A  64      29.719  21.077   7.141  1.00 15.98           N  
ATOM    477  CA  ALA A  64      31.015  20.781   7.758  1.00 16.43           C  
ATOM    478  C   ALA A  64      31.440  19.349   7.378  1.00 17.21           C  
ATOM    479  O   ALA A  64      30.704  18.388   7.613  1.00 16.81           O  
ATOM    480  CB  ALA A  64      30.936  20.936   9.256  1.00 14.02           C  
ATOM    481  N   GLU A  65      32.617  19.214   6.779  1.00 17.56           N  
ATOM    482  CA  GLU A  65      33.114  17.909   6.359  1.00 18.20           C  
ATOM    483  C   GLU A  65      33.958  17.259   7.438  1.00 17.93           C  
ATOM    484  O   GLU A  65      35.167  17.118   7.282  1.00 18.83           O  
ATOM    485  CB  GLU A  65      33.931  18.050   5.078  1.00 19.29           C  
ATOM    486  CG  GLU A  65      33.171  18.659   3.911  1.00 25.12           C  
ATOM    487  CD  GLU A  65      32.032  17.787   3.357  1.00 30.19           C  
ATOM    488  OE1 GLU A  65      31.993  16.546   3.587  1.00 31.68           O  
ATOM    489  OE2 GLU A  65      31.168  18.366   2.661  1.00 30.93           O  
ATOM    490  N   ASP A  66      33.312  16.859   8.531  1.00 17.07           N  
ATOM    491  CA  ASP A  66      34.004  16.229   9.643  1.00 16.14           C  
ATOM    492  C   ASP A  66      33.653  14.746   9.764  1.00 15.91           C  
ATOM    493  O   ASP A  66      33.133  14.154   8.818  1.00 17.15           O  
ATOM    494  CB  ASP A  66      33.740  17.003  10.946  1.00 13.54           C  
ATOM    495  CG  ASP A  66      32.266  17.273  11.189  1.00 14.82           C  
ATOM    496  OD1 ASP A  66      31.418  16.707  10.471  1.00 14.10           O  
ATOM    497  OD2 ASP A  66      31.944  18.080  12.086  1.00 13.87           O  
ATOM    498  N   ASN A  67      33.851  14.158  10.937  1.00 16.15           N  
ATOM    499  CA  ASN A  67      33.599  12.729  11.105  1.00 16.09           C  
ATOM    500  C   ASN A  67      32.829  12.383  12.372  1.00 16.07           C  
ATOM    501  O   ASN A  67      33.379  11.805  13.313  1.00 17.54           O  
ATOM    502  CB  ASN A  67      34.959  12.008  11.062  1.00 17.43           C  
ATOM    503  CG  ASN A  67      34.846  10.498  11.137  1.00 17.79           C  
ATOM    504  OD1 ASN A  67      35.766   9.837  11.609  1.00 22.42           O  
ATOM    505  ND2 ASN A  67      33.749   9.942  10.647  1.00 17.00           N  
ATOM    506  N   PRO A  68      31.528  12.710  12.414  1.00 17.04           N  
ATOM    507  CA  PRO A  68      30.737  12.402  13.615  1.00 18.57           C  
ATOM    508  C   PRO A  68      30.544  10.889  13.795  1.00 20.63           C  
ATOM    509  O   PRO A  68      30.530  10.145  12.820  1.00 21.08           O  
ATOM    510  CB  PRO A  68      29.412  13.137  13.350  1.00 16.93           C  
ATOM    511  CG  PRO A  68      29.296  13.078  11.819  1.00 18.25           C  
ATOM    512  CD  PRO A  68      30.712  13.400  11.389  1.00 15.75           C  
ATOM    513  N   PRO A  69      30.414  10.413  15.047  1.00 21.90           N  
ATOM    514  CA  PRO A  69      30.429  11.192  16.285  1.00 21.52           C  
ATOM    515  C   PRO A  69      31.830  11.305  16.867  1.00 20.94           C  
ATOM    516  O   PRO A  69      32.005  11.848  17.950  1.00 21.88           O  
ATOM    517  CB  PRO A  69      29.550  10.353  17.201  1.00 22.48           C  
ATOM    518  CG  PRO A  69      29.992   8.947  16.847  1.00 21.08           C  
ATOM    519  CD  PRO A  69      30.022   9.013  15.323  1.00 22.34           C  
ATOM    520  N   THR A  70      32.817  10.759  16.165  1.00 21.00           N  
ATOM    521  CA  THR A  70      34.202  10.781  16.642  1.00 22.10           C  
ATOM    522  C   THR A  70      34.840  12.157  16.677  1.00 21.95           C  
ATOM    523  O   THR A  70      35.553  12.494  17.603  1.00 22.31           O  
ATOM    524  CB  THR A  70      35.118   9.984  15.720  1.00 22.36           C  
ATOM    525  OG1 THR A  70      34.414   8.859  15.213  1.00 27.87           O  
ATOM    526  CG2 THR A  70      36.331   9.501  16.449  1.00 25.35           C  
ATOM    527  N   ASN A  71      34.668  12.890  15.586  1.00 21.03           N  
ATOM    528  CA  ASN A  71      35.262  14.206  15.442  1.00 20.11           C  
ATOM    529  C   ASN A  71      34.345  15.208  14.749  1.00 19.20           C  
ATOM    530  O   ASN A  71      33.954  15.025  13.590  1.00 19.33           O  
ATOM    531  CB  ASN A  71      36.564  14.078  14.656  1.00 22.51           C  
ATOM    532  CG  ASN A  71      37.432  15.309  14.766  1.00 27.76           C  
ATOM    533  OD1 ASN A  71      36.945  16.425  14.935  1.00 32.04           O  
ATOM    534  ND2 ASN A  71      38.736  15.108  14.709  1.00 32.20           N  
ATOM    535  N   CYS A  72      33.994  16.260  15.476  1.00 17.89           N  
ATOM    536  CA  CYS A  72      33.152  17.318  14.952  1.00 16.58           C  
ATOM    537  C   CYS A  72      33.955  18.608  14.889  1.00 16.40           C  
ATOM    538  O   CYS A  72      34.536  19.027  15.881  1.00 17.15           O  
ATOM    539  CB  CYS A  72      31.944  17.535  15.861  1.00 15.42           C  
ATOM    540  SG  CYS A  72      30.588  16.351  15.687  1.00 14.41           S  
ATOM    541  N   ASN A  73      34.041  19.212  13.717  1.00 16.23           N  
ATOM    542  CA  ASN A  73      34.749  20.477  13.580  1.00 16.65           C  
ATOM    543  C   ASN A  73      34.308  21.218  12.323  1.00 18.08           C  
ATOM    544  O   ASN A  73      33.832  20.603  11.340  1.00 16.39           O  
ATOM    545  CB  ASN A  73      36.271  20.302  13.615  1.00 18.63           C  
ATOM    546  CG  ASN A  73      36.788  19.438  12.493  1.00 19.83           C  
ATOM    547  OD1 ASN A  73      36.898  18.225  12.640  1.00 20.92           O  
ATOM    548  ND2 ASN A  73      37.118  20.054  11.372  1.00 20.02           N  
ATOM    549  N   VAL A  74      34.413  22.542  12.388  1.00 16.56           N  
ATOM    550  CA  VAL A  74      34.020  23.412  11.294  1.00 16.01           C  
ATOM    551  C   VAL A  74      35.246  24.172  10.812  1.00 17.65           C  
ATOM    552  O   VAL A  74      36.079  24.586  11.612  1.00 18.21           O  
ATOM    553  CB  VAL A  74      32.978  24.433  11.776  1.00 15.67           C  
ATOM    554  CG1 VAL A  74      32.610  25.382  10.656  1.00 17.17           C  
ATOM    555  CG2 VAL A  74      31.742  23.737  12.280  1.00 13.36           C  
ATOM    556  N   ASP A  75      35.381  24.322   9.503  1.00 17.59           N  
ATOM    557  CA  ASP A  75      36.507  25.057   8.939  1.00 19.13           C  
ATOM    558  C   ASP A  75      35.949  25.856   7.789  1.00 18.59           C  
ATOM    559  O   ASP A  75      35.596  25.284   6.765  1.00 18.53           O  
ATOM    560  CB  ASP A  75      37.597  24.120   8.439  1.00 18.95           C  
ATOM    561  CG  ASP A  75      38.814  24.872   7.942  1.00 23.95           C  
ATOM    562  OD1 ASP A  75      38.706  25.610   6.946  1.00 24.89           O  
ATOM    563  OD2 ASP A  75      39.882  24.751   8.560  1.00 27.51           O  
ATOM    564  N   TYR A  76      35.948  27.176   7.932  1.00 18.02           N  
ATOM    565  CA  TYR A  76      35.391  28.059   6.922  1.00 19.28           C  
ATOM    566  C   TYR A  76      35.815  27.807   5.479  1.00 21.47           C  
ATOM    567  O   TYR A  76      34.961  27.591   4.607  1.00 20.95           O  
ATOM    568  CB  TYR A  76      35.633  29.529   7.277  1.00 17.21           C  
ATOM    569  CG  TYR A  76      34.982  30.461   6.289  1.00 16.92           C  
ATOM    570  CD1 TYR A  76      33.618  30.426   6.079  1.00 16.92           C  
ATOM    571  CD2 TYR A  76      35.731  31.372   5.555  1.00 18.91           C  
ATOM    572  CE1 TYR A  76      33.012  31.262   5.152  1.00 20.37           C  
ATOM    573  CE2 TYR A  76      35.130  32.217   4.617  1.00 19.91           C  
ATOM    574  CZ  TYR A  76      33.774  32.161   4.435  1.00 20.77           C  
ATOM    575  OH  TYR A  76      33.176  33.006   3.538  1.00 24.49           O  
ATOM    576  N   GLU A  77      37.119  27.802   5.221  1.00 24.67           N  
ATOM    577  CA  GLU A  77      37.574  27.604   3.846  1.00 28.02           C  
ATOM    578  C   GLU A  77      37.366  26.188   3.311  1.00 25.35           C  
ATOM    579  O   GLU A  77      37.086  25.996   2.135  1.00 26.64           O  
ATOM    580  CB  GLU A  77      39.020  28.082   3.657  1.00 33.84           C  
ATOM    581  CG  GLU A  77      40.091  27.029   3.842  1.00 43.11           C  
ATOM    582  CD  GLU A  77      41.336  27.343   3.024  1.00 49.62           C  
ATOM    583  OE1 GLU A  77      41.802  28.510   3.044  1.00 53.64           O  
ATOM    584  OE2 GLU A  77      41.841  26.422   2.347  1.00 51.25           O  
ATOM    585  N   ARG A  78      37.456  25.201   4.189  1.00 24.03           N  
ATOM    586  CA  ARG A  78      37.253  23.807   3.809  1.00 20.15           C  
ATOM    587  C   ARG A  78      35.778  23.497   3.514  1.00 19.75           C  
ATOM    588  O   ARG A  78      35.441  22.842   2.506  1.00 19.02           O  
ATOM    589  CB  ARG A  78      37.729  22.896   4.949  1.00 20.50           C  
ATOM    590  CG  ARG A  78      37.589  21.405   4.655  1.00 21.04           C  
ATOM    591  CD  ARG A  78      37.807  20.532   5.870  1.00 21.51           C  
ATOM    592  NE  ARG A  78      36.696  20.671   6.811  1.00 23.97           N  
ATOM    593  CZ  ARG A  78      36.737  20.327   8.096  1.00 22.59           C  
ATOM    594  NH1 ARG A  78      37.842  19.802   8.619  1.00 21.50           N  
ATOM    595  NH2 ARG A  78      35.678  20.557   8.866  1.00 21.29           N  
ATOM    596  N   ASP A  79      34.896  24.042   4.351  1.00 16.79           N  
ATOM    597  CA  ASP A  79      33.472  23.754   4.263  1.00 15.64           C  
ATOM    598  C   ASP A  79      32.474  24.662   3.586  1.00 14.28           C  
ATOM    599  O   ASP A  79      31.410  24.196   3.189  1.00 16.38           O  
ATOM    600  CB  ASP A  79      32.933  23.515   5.676  1.00 14.89           C  
ATOM    601  CG  ASP A  79      33.694  22.441   6.417  1.00 16.93           C  
ATOM    602  OD1 ASP A  79      34.110  21.456   5.761  1.00 17.40           O  
ATOM    603  OD2 ASP A  79      33.881  22.584   7.649  1.00 16.24           O  
ATOM    604  N   CYS A  80      32.776  25.940   3.433  1.00 15.28           N  
ATOM    605  CA  CYS A  80      31.761  26.858   2.899  1.00 16.66           C  
ATOM    606  C   CYS A  80      31.306  26.515   1.466  1.00 17.78           C  
ATOM    607  O   CYS A  80      30.066  26.499   1.151  1.00 16.86           O  
ATOM    608  CB  CYS A  80      32.288  28.288   2.914  1.00 15.08           C  
ATOM    609  SG  CYS A  80      30.941  29.421   2.559  1.00 16.36           S  
ATOM    610  N   GLY A  81      32.303  26.351   0.563  1.00 19.96           N  
ATOM    611  CA  GLY A  81      32.036  26.007  -0.819  1.00 23.29           C  
ATOM    612  C   GLY A  81      31.868  27.136  -1.810  1.00 25.12           C  
ATOM    613  O   GLY A  81      31.690  28.288  -1.417  1.00 26.34           O  
ATOM    614  N   SER A  82      31.812  26.753  -3.081  1.00 24.69           N  
ATOM    615  CA  SER A  82      31.717  27.666  -4.223  1.00 23.99           C  
ATOM    616  C   SER A  82      30.458  28.506  -4.335  1.00 22.98           C  
ATOM    617  O   SER A  82      30.473  29.604  -4.900  1.00 23.92           O  
ATOM    618  CB  SER A  82      31.871  26.892  -5.545  1.00 26.82           C  
ATOM    619  OG  SER A  82      32.839  25.862  -5.433  1.00 31.10           O  
ATOM    620  N   SER A  83      29.344  27.975  -3.869  1.00 19.86           N  
ATOM    621  CA  SER A  83      28.109  28.723  -3.982  1.00 21.88           C  
ATOM    622  C   SER A  83      27.701  29.438  -2.698  1.00 20.09           C  
ATOM    623  O   SER A  83      26.557  29.862  -2.563  1.00 22.65           O  
ATOM    624  CB  SER A  83      26.970  27.833  -4.483  1.00 23.13           C  
ATOM    625  OG  SER A  83      26.839  26.671  -3.684  1.00 30.81           O  
ATOM    626  N   GLY A  84      28.634  29.602  -1.773  1.00 19.21           N  
ATOM    627  CA  GLY A  84      28.289  30.264  -0.527  1.00 18.55           C  
ATOM    628  C   GLY A  84      27.668  29.343   0.516  1.00 17.36           C  
ATOM    629  O   GLY A  84      27.201  28.238   0.208  1.00 14.96           O  
ATOM    630  N   CYS A  85      27.629  29.847   1.751  1.00 16.06           N  
ATOM    631  CA  CYS A  85      27.106  29.119   2.902  1.00 15.26           C  
ATOM    632  C   CYS A  85      26.587  30.138   3.927  1.00 16.57           C  
ATOM    633  O   CYS A  85      26.738  31.357   3.725  1.00 17.39           O  
ATOM    634  CB  CYS A  85      28.223  28.271   3.515  1.00 13.18           C  
ATOM    635  SG  CYS A  85      29.656  29.217   4.144  1.00 15.89           S  
ATOM    636  N   SER A  86      26.036  29.660   5.046  1.00 14.60           N  
ATOM    637  CA  SER A  86      25.486  30.552   6.064  1.00 12.62           C  
ATOM    638  C   SER A  86      26.494  31.602   6.554  1.00 11.86           C  
ATOM    639  O   SER A  86      26.145  32.759   6.722  1.00 13.39           O  
ATOM    640  CB  SER A  86      24.955  29.718   7.226  1.00 10.83           C  
ATOM    641  OG  SER A  86      25.988  28.867   7.692  1.00 11.79           O  
ATOM    642  N   ILE A  87      27.755  31.221   6.722  1.00 12.38           N  
ATOM    643  CA  ILE A  87      28.769  32.147   7.205  1.00 13.62           C  
ATOM    644  C   ILE A  87      29.018  33.299   6.236  1.00 16.42           C  
ATOM    645  O   ILE A  87      29.023  34.467   6.633  1.00 16.49           O  
ATOM    646  CB  ILE A  87      30.086  31.405   7.505  1.00 13.88           C  
ATOM    647  CG1 ILE A  87      29.848  30.433   8.668  1.00 13.22           C  
ATOM    648  CG2 ILE A  87      31.233  32.387   7.779  1.00 13.15           C  
ATOM    649  CD1 ILE A  87      31.060  29.658   9.121  1.00  9.99           C  
ATOM    650  N   SER A  88      29.212  32.981   4.962  1.00 17.34           N  
ATOM    651  CA  SER A  88      29.460  34.022   3.980  1.00 15.56           C  
ATOM    652  C   SER A  88      28.206  34.872   3.817  1.00 14.41           C  
ATOM    653  O   SER A  88      28.284  36.068   3.570  1.00 16.04           O  
ATOM    654  CB  SER A  88      29.915  33.406   2.647  1.00 17.39           C  
ATOM    655  OG  SER A  88      28.859  32.703   2.010  1.00 18.10           O  
ATOM    656  N   ALA A  89      27.039  34.277   3.993  1.00 13.62           N  
ATOM    657  CA  ALA A  89      25.823  35.062   3.871  1.00 14.59           C  
ATOM    658  C   ALA A  89      25.692  36.067   5.022  1.00 15.64           C  
ATOM    659  O   ALA A  89      25.115  37.135   4.836  1.00 16.58           O  
ATOM    660  CB  ALA A  89      24.575  34.165   3.801  1.00 12.71           C  
ATOM    661  N   ILE A  90      26.169  35.712   6.217  1.00 17.16           N  
ATOM    662  CA  ILE A  90      26.081  36.634   7.367  1.00 17.00           C  
ATOM    663  C   ILE A  90      26.965  37.856   7.073  1.00 17.21           C  
ATOM    664  O   ILE A  90      26.593  38.999   7.354  1.00 17.25           O  
ATOM    665  CB  ILE A  90      26.535  35.969   8.730  1.00 16.81           C  
ATOM    666  CG1 ILE A  90      25.561  34.861   9.142  1.00 16.19           C  
ATOM    667  CG2 ILE A  90      26.560  37.012   9.864  1.00 16.12           C  
ATOM    668  CD1 ILE A  90      24.149  35.322   9.340  1.00 15.35           C  
ATOM    669  N   ALA A  91      28.137  37.607   6.511  1.00 16.82           N  
ATOM    670  CA  ALA A  91      29.057  38.678   6.161  1.00 18.57           C  
ATOM    671  C   ALA A  91      28.469  39.566   5.049  1.00 18.98           C  
ATOM    672  O   ALA A  91      28.467  40.793   5.159  1.00 20.16           O  
ATOM    673  CB  ALA A  91      30.394  38.097   5.732  1.00 16.62           C  
ATOM    674  N   ASN A  92      27.912  38.951   4.013  1.00 19.04           N  
ATOM    675  CA  ASN A  92      27.322  39.699   2.905  1.00 20.05           C  
ATOM    676  C   ASN A  92      26.230  40.653   3.366  1.00 20.53           C  
ATOM    677  O   ASN A  92      26.301  41.851   3.123  1.00 20.88           O  
ATOM    678  CB  ASN A  92      26.746  38.734   1.823  1.00 22.69           C  
ATOM    679  CG  ASN A  92      26.191  39.477   0.549  1.00 24.47           C  
ATOM    680  OD1 ASN A  92      26.542  40.638   0.312  1.00 24.47           O  
ATOM    681  ND2 ASN A  92      25.336  38.785  -0.233  1.00 25.87           N  
ATOM    682  N   TYR A  93      25.224  40.131   4.049  1.00 19.33           N  
ATOM    683  CA  TYR A  93      24.127  40.962   4.464  1.00 19.65           C  
ATOM    684  C   TYR A  93      24.329  41.883   5.667  1.00 20.22           C  
ATOM    685  O   TYR A  93      23.557  42.819   5.852  1.00 20.80           O  
ATOM    686  CB  TYR A  93      22.884  40.114   4.640  1.00 22.71           C  
ATOM    687  CG  TYR A  93      22.524  39.360   3.391  1.00 25.92           C  
ATOM    688  CD1 TYR A  93      22.018  40.022   2.276  1.00 26.56           C  
ATOM    689  CD2 TYR A  93      22.674  37.977   3.328  1.00 27.08           C  
ATOM    690  CE1 TYR A  93      21.664  39.315   1.125  1.00 27.97           C  
ATOM    691  CE2 TYR A  93      22.329  37.263   2.186  1.00 28.22           C  
ATOM    692  CZ  TYR A  93      21.823  37.935   1.089  1.00 28.05           C  
ATOM    693  OH  TYR A  93      21.473  37.213  -0.030  1.00 27.49           O  
ATOM    694  N   THR A  94      25.336  41.639   6.490  1.00 18.63           N  
ATOM    695  CA  THR A  94      25.580  42.531   7.638  1.00 21.70           C  
ATOM    696  C   THR A  94      26.085  43.840   7.015  1.00 24.66           C  
ATOM    697  O   THR A  94      25.664  44.959   7.345  1.00 24.67           O  
ATOM    698  CB  THR A  94      26.675  41.981   8.547  1.00 20.40           C  
ATOM    699  OG1 THR A  94      26.152  40.862   9.254  1.00 17.87           O  
ATOM    700  CG2 THR A  94      27.164  43.052   9.561  1.00 17.70           C  
ATOM    701  N   GLN A  95      26.904  43.648   5.993  1.00 27.22           N  
ATOM    702  CA  GLN A  95      27.444  44.758   5.283  1.00 30.34           C  
ATOM    703  C   GLN A  95      26.408  45.490   4.448  1.00 29.30           C  
ATOM    704  O   GLN A  95      26.478  46.718   4.353  1.00 30.65           O  
ATOM    705  CB  GLN A  95      28.617  44.248   4.471  1.00 33.19           C  
ATOM    706  CG  GLN A  95      28.353  44.225   3.009  1.00 41.81           C  
ATOM    707  CD  GLN A  95      28.896  45.462   2.317  1.00 45.90           C  
ATOM    708  OE1 GLN A  95      29.712  46.180   2.889  1.00 48.61           O  
ATOM    709  NE2 GLN A  95      28.466  45.708   1.075  1.00 47.53           N  
ATOM    710  N   ARG A  96      25.465  44.763   3.836  1.00 28.52           N  
ATOM    711  CA  ARG A  96      24.449  45.379   3.000  1.00 27.30           C  
ATOM    712  C   ARG A  96      23.320  46.165   3.686  1.00 28.98           C  
ATOM    713  O   ARG A  96      22.748  47.091   3.097  1.00 27.84           O  
ATOM    714  CB  ARG A  96      23.858  44.348   2.040  1.00 25.75           C  
ATOM    715  CG  ARG A  96      24.843  43.862   0.969  1.00 23.76           C  
ATOM    716  CD  ARG A  96      24.219  42.793   0.068  1.00 24.90           C  
ATOM    717  NE  ARG A  96      22.958  43.212  -0.562  1.00 23.33           N  
ATOM    718  CZ  ARG A  96      22.866  43.733  -1.785  1.00 21.09           C  
ATOM    719  NH1 ARG A  96      23.952  43.912  -2.511  1.00 20.25           N  
ATOM    720  NH2 ARG A  96      21.690  44.083  -2.278  1.00 19.81           N  
ATOM    721  N   VAL A  97      22.941  45.778   4.902  1.00 30.82           N  
ATOM    722  CA  VAL A  97      21.877  46.507   5.614  1.00 33.46           C  
ATOM    723  C   VAL A  97      22.300  47.934   5.908  1.00 35.22           C  
ATOM    724  O   VAL A  97      21.479  48.846   5.909  1.00 36.16           O  
ATOM    725  CB  VAL A  97      21.481  45.918   7.022  1.00 32.40           C  
ATOM    726  CG1 VAL A  97      20.110  45.286   6.966  1.00 32.21           C  
ATOM    727  CG2 VAL A  97      22.531  44.978   7.575  1.00 31.92           C  
ATOM    728  N   SER A  98      23.586  48.115   6.160  1.00 37.83           N  
ATOM    729  CA  SER A  98      24.102  49.424   6.512  1.00 42.62           C  
ATOM    730  C   SER A  98      24.881  50.071   5.380  1.00 45.04           C  
ATOM    731  O   SER A  98      25.697  50.959   5.570  1.00 46.11           O  
ATOM    732  CB  SER A  98      24.990  49.337   7.733  1.00 43.15           C  
ATOM    733  OG  SER A  98      26.026  48.401   7.515  1.00 45.38           O  
ATOM    734  N   ASP A  99      24.676  49.586   4.183  1.00 45.93           N  
ATOM    735  CA  ASP A  99      25.357  50.259   3.099  1.00 46.96           C  
ATOM    736  C   ASP A  99      24.493  51.436   2.588  1.00 46.99           C  
ATOM    737  O   ASP A  99      23.384  51.194   2.133  1.00 44.91           O  
ATOM    738  CB  ASP A  99      25.650  49.276   1.983  1.00 49.39           C  
ATOM    739  CG  ASP A  99      26.484  49.891   0.881  1.00 51.15           C  
ATOM    740  OD1 ASP A  99      26.341  51.118   0.656  1.00 53.16           O  
ATOM    741  OD2 ASP A  99      27.314  49.197   0.270  1.00 52.18           O  
ATOM    742  N   SER A 100      24.966  52.685   2.660  1.00 49.05           N  
ATOM    743  CA  SER A 100      24.217  53.885   2.165  1.00 50.81           C  
ATOM    744  C   SER A 100      23.918  54.009   0.638  1.00 51.10           C  
ATOM    745  O   SER A 100      22.926  54.705   0.242  1.00 52.61           O  
ATOM    746  CB  SER A 100      24.786  55.233   2.765  1.00 51.63           C  
ATOM    747  OG  SER A 100      26.206  55.291   2.684  1.00 54.95           O  
ATOM    748  N   SER A 101      24.741  53.378  -0.229  1.00 50.68           N  
ATOM    749  CA  SER A 101      24.558  53.347  -1.665  1.00 50.93           C  
ATOM    750  C   SER A 101      23.413  52.413  -2.143  1.00 49.92           C  
ATOM    751  O   SER A 101      23.027  52.407  -3.336  1.00 50.16           O  
ATOM    752  CB  SER A 101      25.792  52.747  -2.242  1.00 52.44           C  
ATOM    753  OG  SER A 101      26.428  53.493  -3.238  1.00 58.68           O  
ATOM    754  N   LEU A 102      23.014  51.474  -1.292  1.00 49.04           N  
ATOM    755  CA  LEU A 102      21.965  50.530  -1.656  1.00 47.38           C  
ATOM    756  C   LEU A 102      20.580  51.086  -1.437  1.00 46.37           C  
ATOM    757  O   LEU A 102      20.417  52.052  -0.705  1.00 46.70           O  
ATOM    758  CB  LEU A 102      22.137  49.216  -0.904  1.00 47.91           C  
ATOM    759  CG  LEU A 102      23.359  48.405  -1.323  1.00 48.03           C  
ATOM    760  CD1 LEU A 102      23.497  47.203  -0.420  1.00 47.99           C  
ATOM    761  CD2 LEU A 102      23.209  47.962  -2.772  1.00 48.84           C  
ATOM    762  N   SER A 103      19.575  50.447  -2.021  1.00 45.94           N  
ATOM    763  CA  SER A 103      18.208  50.912  -1.878  1.00 46.22           C  
ATOM    764  C   SER A 103      17.543  50.446  -0.594  1.00 47.40           C  
ATOM    765  O   SER A 103      18.001  49.513   0.078  1.00 46.74           O  
ATOM    766  CB  SER A 103      17.365  50.439  -3.052  1.00 45.63           C  
ATOM    767  OG  SER A 103      17.188  49.035  -3.007  1.00 46.50           O  
ATOM    768  N   SER A 104      16.393  51.049  -0.319  1.00 48.37           N  
ATOM    769  CA  SER A 104      15.600  50.729   0.861  1.00 49.88           C  
ATOM    770  C   SER A 104      15.210  49.269   0.805  1.00 49.96           C  
ATOM    771  O   SER A 104      15.448  48.520   1.760  1.00 49.53           O  
ATOM    772  CB  SER A 104      14.343  51.579   0.903  1.00 50.60           C  
ATOM    773  OG  SER A 104      13.560  51.383  -0.271  1.00 54.00           O  
ATOM    774  N   GLU A 105      14.632  48.831  -0.310  1.00 50.09           N  
ATOM    775  CA  GLU A 105      14.315  47.449  -0.301  1.00 50.46           C  
ATOM    776  C   GLU A 105      15.487  46.459  -0.398  1.00 47.96           C  
ATOM    777  O   GLU A 105      15.276  45.231  -0.257  1.00 47.81           O  
ATOM    778  CB  GLU A 105      12.905  47.154  -0.839  1.00 54.55           C  
ATOM    779  CG  GLU A 105      12.808  47.194  -2.283  1.00 60.83           C  
ATOM    780  CD  GLU A 105      11.699  48.071  -2.814  1.00 65.84           C  
ATOM    781  OE1 GLU A 105      11.518  49.202  -2.307  1.00 68.28           O  
ATOM    782  OE2 GLU A 105      11.013  47.632  -3.767  1.00 69.03           O  
ATOM    783  N   ASN A 106      16.708  46.971  -0.599  1.00 44.77           N  
ATOM    784  CA  ASN A 106      17.887  46.117  -0.606  1.00 42.12           C  
ATOM    785  C   ASN A 106      18.163  45.901   0.903  1.00 40.18           C  
ATOM    786  O   ASN A 106      18.588  44.824   1.362  1.00 38.22           O  
ATOM    787  CB  ASN A 106      19.150  46.799  -1.163  1.00 43.98           C  
ATOM    788  CG  ASN A 106      19.254  46.763  -2.648  1.00 46.12           C  
ATOM    789  OD1 ASN A 106      19.813  47.678  -3.260  1.00 47.30           O  
ATOM    790  ND2 ASN A 106      18.685  45.736  -3.253  1.00 46.11           N  
ATOM    791  N   HIS A 107      17.954  46.964   1.676  1.00 37.50           N  
ATOM    792  CA  HIS A 107      18.129  46.930   3.133  1.00 35.21           C  
ATOM    793  C   HIS A 107      17.107  45.978   3.762  1.00 33.34           C  
ATOM    794  O   HIS A 107      17.471  45.148   4.591  1.00 33.17           O  
ATOM    795  CB  HIS A 107      17.964  48.332   3.736  1.00 35.88           C  
ATOM    796  CG  HIS A 107      19.058  49.288   3.336  1.00 35.78           C  
ATOM    797  ND1 HIS A 107      20.314  48.879   2.985  1.00 36.50           N  
ATOM    798  CD2 HIS A 107      19.046  50.644   3.238  1.00 35.39           C  
ATOM    799  CE1 HIS A 107      21.053  49.940   2.678  1.00 35.68           C  
ATOM    800  NE2 HIS A 107      20.314  51.009   2.822  1.00 36.15           N  
ATOM    801  N   ALA A 108      15.843  46.085   3.356  1.00 30.44           N  
ATOM    802  CA  ALA A 108      14.797  45.207   3.883  1.00 29.90           C  
ATOM    803  C   ALA A 108      15.122  43.741   3.580  1.00 29.99           C  
ATOM    804  O   ALA A 108      14.955  42.865   4.431  1.00 29.15           O  
ATOM    805  CB  ALA A 108      13.434  45.584   3.319  1.00 27.80           C  
ATOM    806  N   GLU A 109      15.618  43.472   2.380  1.00 28.72           N  
ATOM    807  CA  GLU A 109      15.970  42.110   2.044  1.00 27.83           C  
ATOM    808  C   GLU A 109      17.096  41.612   2.960  1.00 25.87           C  
ATOM    809  O   GLU A 109      17.013  40.516   3.513  1.00 27.33           O  
ATOM    810  CB  GLU A 109      16.397  42.005   0.582  1.00 29.42           C  
ATOM    811  CG  GLU A 109      16.924  40.631   0.223  1.00 31.30           C  
ATOM    812  CD  GLU A 109      17.575  40.586  -1.138  1.00 32.35           C  
ATOM    813  OE1 GLU A 109      18.702  41.106  -1.283  1.00 30.48           O  
ATOM    814  OE2 GLU A 109      16.958  40.004  -2.054  1.00 33.01           O  
ATOM    815  N   ALA A 110      18.141  42.414   3.132  1.00 24.69           N  
ATOM    816  CA  ALA A 110      19.269  42.030   3.986  1.00 23.74           C  
ATOM    817  C   ALA A 110      18.870  41.720   5.439  1.00 23.73           C  
ATOM    818  O   ALA A 110      19.342  40.751   6.029  1.00 23.38           O  
ATOM    819  CB  ALA A 110      20.328  43.112   3.960  1.00 23.44           C  
ATOM    820  N   LEU A 111      17.996  42.547   6.002  1.00 23.15           N  
ATOM    821  CA  LEU A 111      17.531  42.372   7.367  1.00 23.20           C  
ATOM    822  C   LEU A 111      16.723  41.087   7.459  1.00 23.01           C  
ATOM    823  O   LEU A 111      16.919  40.295   8.378  1.00 22.98           O  
ATOM    824  CB  LEU A 111      16.654  43.553   7.800  1.00 23.66           C  
ATOM    825  CG  LEU A 111      16.773  44.023   9.259  1.00 24.72           C  
ATOM    826  CD1 LEU A 111      15.412  44.390   9.747  1.00 21.68           C  
ATOM    827  CD2 LEU A 111      17.361  42.951  10.158  1.00 23.92           C  
ATOM    828  N   ARG A 112      15.810  40.881   6.511  1.00 22.45           N  
ATOM    829  CA  ARG A 112      14.998  39.666   6.498  1.00 22.03           C  
ATOM    830  C   ARG A 112      15.899  38.420   6.432  1.00 20.73           C  
ATOM    831  O   ARG A 112      15.632  37.438   7.119  1.00 20.57           O  
ATOM    832  CB  ARG A 112      13.999  39.668   5.333  1.00 22.68           C  
ATOM    833  CG  ARG A 112      12.808  40.592   5.520  1.00 24.48           C  
ATOM    834  CD  ARG A 112      11.678  40.262   4.528  1.00 27.71           C  
ATOM    835  NE  ARG A 112      12.176  40.226   3.156  1.00 30.75           N  
ATOM    836  CZ  ARG A 112      12.179  41.269   2.327  1.00 33.09           C  
ATOM    837  NH1 ARG A 112      11.669  42.436   2.705  1.00 31.80           N  
ATOM    838  NH2 ARG A 112      12.662  41.130   1.098  1.00 33.83           N  
ATOM    839  N   PHE A 113      16.986  38.490   5.665  1.00 19.25           N  
ATOM    840  CA  PHE A 113      17.919  37.378   5.552  1.00 18.61           C  
ATOM    841  C   PHE A 113      18.657  37.148   6.861  1.00 18.37           C  
ATOM    842  O   PHE A 113      18.816  35.999   7.298  1.00 16.90           O  
ATOM    843  CB  PHE A 113      18.926  37.609   4.423  1.00 22.34           C  
ATOM    844  CG  PHE A 113      18.479  37.071   3.081  1.00 25.46           C  
ATOM    845  CD1 PHE A 113      17.944  35.789   2.977  1.00 25.63           C  
ATOM    846  CD2 PHE A 113      18.569  37.848   1.927  1.00 27.60           C  
ATOM    847  CE1 PHE A 113      17.547  35.270   1.748  1.00 27.14           C  
ATOM    848  CE2 PHE A 113      18.168  37.330   0.681  1.00 26.79           C  
ATOM    849  CZ  PHE A 113      17.642  36.048   0.603  1.00 25.93           C  
ATOM    850  N   LEU A 114      19.089  38.234   7.500  1.00 15.91           N  
ATOM    851  CA  LEU A 114      19.799  38.118   8.772  1.00 14.87           C  
ATOM    852  C   LEU A 114      18.919  37.504   9.864  1.00 14.21           C  
ATOM    853  O   LEU A 114      19.378  36.631  10.606  1.00 14.19           O  
ATOM    854  CB  LEU A 114      20.336  39.472   9.227  1.00 14.53           C  
ATOM    855  CG  LEU A 114      21.525  40.024   8.446  1.00 14.08           C  
ATOM    856  CD1 LEU A 114      21.788  41.460   8.894  1.00 14.08           C  
ATOM    857  CD2 LEU A 114      22.744  39.137   8.628  1.00 13.68           C  
ATOM    858  N   VAL A 115      17.657  37.925   9.943  1.00 12.06           N  
ATOM    859  CA  VAL A 115      16.747  37.397  10.944  1.00 12.34           C  
ATOM    860  C   VAL A 115      16.659  35.884  10.827  1.00 13.64           C  
ATOM    861  O   VAL A 115      16.673  35.151  11.817  1.00 14.07           O  
ATOM    862  CB  VAL A 115      15.345  38.017  10.789  1.00 13.28           C  
ATOM    863  CG1 VAL A 115      14.294  37.238  11.583  1.00 10.63           C  
ATOM    864  CG2 VAL A 115      15.367  39.449  11.276  1.00 13.98           C  
ATOM    865  N   HIS A 116      16.630  35.414   9.593  1.00 13.19           N  
ATOM    866  CA  HIS A 116      16.517  33.990   9.314  1.00 11.79           C  
ATOM    867  C   HIS A 116      17.751  33.134   9.555  1.00 11.26           C  
ATOM    868  O   HIS A 116      17.670  32.067  10.181  1.00 11.50           O  
ATOM    869  CB  HIS A 116      16.095  33.791   7.866  1.00 12.92           C  
ATOM    870  CG  HIS A 116      15.694  32.390   7.562  1.00  8.85           C  
ATOM    871  ND1 HIS A 116      14.418  31.925   7.825  1.00  8.56           N  
ATOM    872  CD2 HIS A 116      16.372  31.349   7.043  1.00  8.74           C  
ATOM    873  CE1 HIS A 116      14.338  30.663   7.483  1.00  7.32           C  
ATOM    874  NE2 HIS A 116      15.505  30.278   7.006  1.00  7.02           N  
ATOM    875  N   PHE A 117      18.857  33.546   8.954  1.00 10.73           N  
ATOM    876  CA  PHE A 117      20.112  32.824   9.027  1.00 11.39           C  
ATOM    877  C   PHE A 117      20.743  32.769  10.411  1.00 12.51           C  
ATOM    878  O   PHE A 117      21.428  31.787  10.734  1.00 11.27           O  
ATOM    879  CB  PHE A 117      21.122  33.379   8.010  1.00 12.89           C  
ATOM    880  CG  PHE A 117      20.695  33.226   6.569  1.00 14.74           C  
ATOM    881  CD1 PHE A 117      19.911  32.145   6.172  1.00 13.54           C  
ATOM    882  CD2 PHE A 117      21.037  34.197   5.618  1.00 15.14           C  
ATOM    883  CE1 PHE A 117      19.473  32.028   4.840  1.00 13.98           C  
ATOM    884  CE2 PHE A 117      20.608  34.087   4.287  1.00 13.11           C  
ATOM    885  CZ  PHE A 117      19.817  33.007   3.903  1.00 11.52           C  
ATOM    886  N   ILE A 118      20.546  33.804  11.228  1.00 11.45           N  
ATOM    887  CA  ILE A 118      21.125  33.767  12.572  1.00 10.89           C  
ATOM    888  C   ILE A 118      20.431  32.656  13.377  1.00  9.23           C  
ATOM    889  O   ILE A 118      21.067  32.010  14.231  1.00 11.84           O  
ATOM    890  CB  ILE A 118      21.104  35.154  13.274  1.00 10.52           C  
ATOM    891  CG1 ILE A 118      22.143  36.062  12.600  1.00  9.22           C  
ATOM    892  CG2 ILE A 118      21.497  35.007  14.756  1.00 12.90           C  
ATOM    893  CD1 ILE A 118      22.195  37.481  13.120  1.00 10.51           C  
ATOM    894  N   GLY A 119      19.168  32.389  13.041  1.00  7.75           N  
ATOM    895  CA  GLY A 119      18.405  31.321  13.667  1.00  8.23           C  
ATOM    896  C   GLY A 119      18.818  29.960  13.097  1.00 10.60           C  
ATOM    897  O   GLY A 119      19.131  29.044  13.859  1.00 11.15           O  
ATOM    898  N   ASP A 120      18.833  29.812  11.766  1.00  9.38           N  
ATOM    899  CA  ASP A 120      19.230  28.537  11.126  1.00 10.03           C  
ATOM    900  C   ASP A 120      20.575  28.028  11.621  1.00 11.11           C  
ATOM    901  O   ASP A 120      20.739  26.824  11.803  1.00 13.37           O  
ATOM    902  CB  ASP A 120      19.323  28.654   9.591  1.00  9.46           C  
ATOM    903  CG  ASP A 120      18.059  28.152   8.844  1.00  9.97           C  
ATOM    904  OD1 ASP A 120      17.094  27.569   9.439  1.00  7.79           O  
ATOM    905  OD2 ASP A 120      18.054  28.350   7.591  1.00 10.27           O  
ATOM    906  N   MET A 121      21.536  28.921  11.846  1.00  9.92           N  
ATOM    907  CA  MET A 121      22.848  28.489  12.297  1.00 10.10           C  
ATOM    908  C   MET A 121      22.878  27.726  13.622  1.00  9.07           C  
ATOM    909  O   MET A 121      23.804  26.970  13.855  1.00  8.06           O  
ATOM    910  CB  MET A 121      23.827  29.667  12.347  1.00 12.02           C  
ATOM    911  CG  MET A 121      24.259  30.127  10.946  1.00 17.15           C  
ATOM    912  SD  MET A 121      25.667  31.247  10.893  1.00 18.67           S  
ATOM    913  CE  MET A 121      26.939  30.117  11.267  1.00 16.31           C  
ATOM    914  N   THR A 122      21.870  27.900  14.477  1.00  7.34           N  
ATOM    915  CA  THR A 122      21.880  27.199  15.772  1.00  6.49           C  
ATOM    916  C   THR A 122      21.338  25.776  15.710  1.00  8.21           C  
ATOM    917  O   THR A 122      21.466  25.043  16.673  1.00  7.86           O  
ATOM    918  CB  THR A 122      21.177  28.008  16.912  1.00  5.25           C  
ATOM    919  OG1 THR A 122      19.761  28.015  16.717  1.00  6.82           O  
ATOM    920  CG2 THR A 122      21.688  29.427  16.949  1.00  7.18           C  
ATOM    921  N   GLN A 123      20.718  25.395  14.594  1.00  9.33           N  
ATOM    922  CA  GLN A 123      20.197  24.035  14.414  1.00  9.11           C  
ATOM    923  C   GLN A 123      21.446  23.257  14.005  1.00  8.90           C  
ATOM    924  O   GLN A 123      22.017  23.482  12.936  1.00  9.19           O  
ATOM    925  CB  GLN A 123      19.094  24.021  13.328  1.00  9.13           C  
ATOM    926  CG  GLN A 123      18.034  22.918  13.442  1.00  7.61           C  
ATOM    927  CD  GLN A 123      18.524  21.561  12.982  1.00  9.07           C  
ATOM    928  OE1 GLN A 123      19.575  21.092  13.398  1.00  9.64           O  
ATOM    929  NE2 GLN A 123      17.758  20.924  12.104  1.00  7.87           N  
ATOM    930  N   PRO A 124      21.893  22.323  14.861  1.00  8.08           N  
ATOM    931  CA  PRO A 124      23.091  21.519  14.619  1.00  7.58           C  
ATOM    932  C   PRO A 124      23.224  20.839  13.256  1.00  7.68           C  
ATOM    933  O   PRO A 124      24.324  20.801  12.696  1.00  8.25           O  
ATOM    934  CB  PRO A 124      23.066  20.513  15.777  1.00  8.39           C  
ATOM    935  CG  PRO A 124      22.349  21.249  16.842  1.00  7.17           C  
ATOM    936  CD  PRO A 124      21.217  21.872  16.088  1.00  6.51           C  
ATOM    937  N   LEU A 125      22.121  20.312  12.724  1.00  8.37           N  
ATOM    938  CA  LEU A 125      22.170  19.632  11.438  1.00  7.99           C  
ATOM    939  C   LEU A 125      22.361  20.618  10.271  1.00 11.27           C  
ATOM    940  O   LEU A 125      22.578  20.205   9.134  1.00 11.64           O  
ATOM    941  CB  LEU A 125      20.962  18.723  11.247  1.00  6.17           C  
ATOM    942  CG  LEU A 125      21.060  17.485  12.148  1.00  7.43           C  
ATOM    943  CD1 LEU A 125      19.768  16.712  12.009  1.00  9.55           C  
ATOM    944  CD2 LEU A 125      22.264  16.606  11.794  1.00  6.96           C  
ATOM    945  N   HIS A 126      22.284  21.915  10.563  1.00  9.39           N  
ATOM    946  CA  HIS A 126      22.549  22.961   9.562  1.00  9.34           C  
ATOM    947  C   HIS A 126      24.033  23.298   9.507  1.00  8.95           C  
ATOM    948  O   HIS A 126      24.444  24.180   8.754  1.00  9.18           O  
ATOM    949  CB  HIS A 126      21.769  24.240   9.871  1.00  8.73           C  
ATOM    950  CG  HIS A 126      20.397  24.246   9.289  1.00  8.28           C  
ATOM    951  ND1 HIS A 126      20.035  25.093   8.269  1.00  8.18           N  
ATOM    952  CD2 HIS A 126      19.312  23.473   9.546  1.00  7.49           C  
ATOM    953  CE1 HIS A 126      18.784  24.843   7.911  1.00  8.37           C  
ATOM    954  NE2 HIS A 126      18.328  23.866   8.673  1.00  9.30           N  
ATOM    955  N   ASP A 127      24.833  22.592  10.306  1.00  8.02           N  
ATOM    956  CA  ASP A 127      26.270  22.811  10.367  1.00  8.72           C  
ATOM    957  C   ASP A 127      26.970  21.476  10.251  1.00  7.85           C  
ATOM    958  O   ASP A 127      28.013  21.255  10.883  1.00  7.60           O  
ATOM    959  CB  ASP A 127      26.647  23.446  11.710  1.00 10.16           C  
ATOM    960  CG  ASP A 127      25.895  24.718  11.978  1.00 12.78           C  
ATOM    961  OD1 ASP A 127      26.286  25.765  11.427  1.00 16.23           O  
ATOM    962  OD2 ASP A 127      24.915  24.686  12.735  1.00 13.41           O  
ATOM    963  N   GLU A 128      26.426  20.601   9.412  1.00  7.55           N  
ATOM    964  CA  GLU A 128      26.987  19.272   9.270  1.00  8.16           C  
ATOM    965  C   GLU A 128      26.660  18.659   7.897  1.00  7.64           C  
ATOM    966  O   GLU A 128      25.522  18.697   7.441  1.00  7.57           O  
ATOM    967  CB  GLU A 128      26.427  18.398  10.410  1.00  8.56           C  
ATOM    968  CG  GLU A 128      26.742  16.928  10.317  1.00  9.70           C  
ATOM    969  CD  GLU A 128      28.233  16.663  10.226  1.00 14.02           C  
ATOM    970  OE1 GLU A 128      29.012  17.270  10.996  1.00 13.90           O  
ATOM    971  OE2 GLU A 128      28.634  15.843   9.375  1.00 12.19           O  
ATOM    972  N   ALA A 129      27.670  18.086   7.251  1.00  8.51           N  
ATOM    973  CA  ALA A 129      27.491  17.446   5.933  1.00 10.07           C  
ATOM    974  C   ALA A 129      26.809  16.066   5.953  1.00 10.49           C  
ATOM    975  O   ALA A 129      25.961  15.775   5.117  1.00 12.79           O  
ATOM    976  CB  ALA A 129      28.849  17.325   5.237  1.00  5.63           C  
ATOM    977  N   TYR A 130      27.131  15.255   6.954  1.00 11.58           N  
ATOM    978  CA  TYR A 130      26.632  13.888   7.075  1.00 11.61           C  
ATOM    979  C   TYR A 130      25.185  13.609   6.659  1.00 12.15           C  
ATOM    980  O   TYR A 130      24.243  14.229   7.157  1.00  9.57           O  
ATOM    981  CB  TYR A 130      26.934  13.345   8.486  1.00 15.75           C  
ATOM    982  CG  TYR A 130      26.693  11.865   8.653  1.00 16.16           C  
ATOM    983  CD1 TYR A 130      27.669  10.942   8.320  1.00 19.85           C  
ATOM    984  CD2 TYR A 130      25.471  11.390   9.103  1.00 18.00           C  
ATOM    985  CE1 TYR A 130      27.425   9.561   8.423  1.00 20.64           C  
ATOM    986  CE2 TYR A 130      25.215  10.022   9.211  1.00 19.89           C  
ATOM    987  CZ  TYR A 130      26.191   9.119   8.873  1.00 20.20           C  
ATOM    988  OH  TYR A 130      25.922   7.781   8.992  1.00 23.30           O  
ATOM    989  N   ALA A 131      25.025  12.637   5.752  1.00 11.12           N  
ATOM    990  CA  ALA A 131      23.721  12.231   5.232  1.00 11.14           C  
ATOM    991  C   ALA A 131      22.886  13.409   4.755  1.00 11.25           C  
ATOM    992  O   ALA A 131      21.665  13.423   4.932  1.00 10.37           O  
ATOM    993  CB  ALA A 131      22.954  11.435   6.286  1.00 12.24           C  
ATOM    994  N   VAL A 132      23.544  14.376   4.116  1.00 11.82           N  
ATOM    995  CA  VAL A 132      22.881  15.591   3.630  1.00 12.10           C  
ATOM    996  C   VAL A 132      22.207  16.305   4.829  1.00 11.59           C  
ATOM    997  O   VAL A 132      20.980  16.476   4.879  1.00 11.00           O  
ATOM    998  CB  VAL A 132      21.840  15.279   2.530  1.00 12.25           C  
ATOM    999  CG1 VAL A 132      21.345  16.557   1.901  1.00 14.50           C  
ATOM   1000  CG2 VAL A 132      22.451  14.385   1.471  1.00 13.10           C  
ATOM   1001  N   GLY A 133      23.021  16.689   5.811  1.00 11.53           N  
ATOM   1002  CA  GLY A 133      22.492  17.369   6.988  1.00 12.35           C  
ATOM   1003  C   GLY A 133      21.448  16.550   7.736  1.00 12.69           C  
ATOM   1004  O   GLY A 133      20.518  17.110   8.319  1.00 12.27           O  
ATOM   1005  N   GLY A 134      21.577  15.222   7.681  1.00 12.60           N  
ATOM   1006  CA  GLY A 134      20.630  14.342   8.347  1.00 11.01           C  
ATOM   1007  C   GLY A 134      19.359  14.063   7.567  1.00 11.05           C  
ATOM   1008  O   GLY A 134      18.533  13.293   8.040  1.00 11.64           O  
ATOM   1009  N   ASN A 135      19.159  14.687   6.404  1.00 12.01           N  
ATOM   1010  CA  ASN A 135      17.936  14.429   5.626  1.00 12.34           C  
ATOM   1011  C   ASN A 135      17.812  12.973   5.172  1.00 12.44           C  
ATOM   1012  O   ASN A 135      16.705  12.461   5.028  1.00 12.12           O  
ATOM   1013  CB  ASN A 135      17.832  15.348   4.410  1.00 13.09           C  
ATOM   1014  CG  ASN A 135      17.285  16.701   4.767  1.00 13.62           C  
ATOM   1015  OD1 ASN A 135      16.109  16.834   5.109  1.00 14.12           O  
ATOM   1016  ND2 ASN A 135      18.138  17.718   4.726  1.00 16.27           N  
ATOM   1017  N   LYS A 136      18.945  12.311   4.957  1.00 14.09           N  
ATOM   1018  CA  LYS A 136      18.925  10.920   4.520  1.00 16.72           C  
ATOM   1019  C   LYS A 136      18.787   9.896   5.647  1.00 17.41           C  
ATOM   1020  O   LYS A 136      18.770   8.689   5.388  1.00 17.77           O  
ATOM   1021  CB  LYS A 136      20.160  10.588   3.706  1.00 17.30           C  
ATOM   1022  CG  LYS A 136      20.156  11.069   2.294  1.00 23.11           C  
ATOM   1023  CD  LYS A 136      21.302  10.370   1.587  1.00 28.71           C  
ATOM   1024  CE  LYS A 136      21.732  11.132   0.370  1.00 35.13           C  
ATOM   1025  NZ  LYS A 136      22.833  10.468  -0.390  1.00 37.68           N  
ATOM   1026  N   ILE A 137      18.711  10.359   6.890  1.00 14.83           N  
ATOM   1027  CA  ILE A 137      18.569   9.440   8.013  1.00 14.42           C  
ATOM   1028  C   ILE A 137      17.096   9.234   8.306  1.00 14.13           C  
ATOM   1029  O   ILE A 137      16.465  10.031   9.002  1.00 15.29           O  
ATOM   1030  CB  ILE A 137      19.311   9.956   9.276  1.00 15.95           C  
ATOM   1031  CG1 ILE A 137      20.805  10.111   8.976  1.00 17.09           C  
ATOM   1032  CG2 ILE A 137      19.103   8.980  10.457  1.00 17.69           C  
ATOM   1033  CD1 ILE A 137      21.619  10.662  10.147  1.00 18.57           C  
ATOM   1034  N   ASN A 138      16.531   8.181   7.738  1.00 13.50           N  
ATOM   1035  CA  ASN A 138      15.126   7.881   7.934  1.00 15.73           C  
ATOM   1036  C   ASN A 138      14.915   7.260   9.315  1.00 14.77           C  
ATOM   1037  O   ASN A 138      15.638   6.340   9.707  1.00 14.12           O  
ATOM   1038  CB  ASN A 138      14.607   6.977   6.801  1.00 20.67           C  
ATOM   1039  CG  ASN A 138      15.418   5.712   6.620  1.00 28.83           C  
ATOM   1040  OD1 ASN A 138      16.653   5.737   6.523  1.00 29.06           O  
ATOM   1041  ND2 ASN A 138      14.682   4.610   6.545  1.00 37.98           N  
ATOM   1042  N   VAL A 139      13.945   7.794  10.056  1.00 13.65           N  
ATOM   1043  CA  VAL A 139      13.661   7.333  11.418  1.00 13.34           C  
ATOM   1044  C   VAL A 139      12.156   7.296  11.729  1.00 13.95           C  
ATOM   1045  O   VAL A 139      11.329   7.724  10.922  1.00 16.23           O  
ATOM   1046  CB  VAL A 139      14.331   8.289  12.467  1.00 12.59           C  
ATOM   1047  CG1 VAL A 139      15.857   8.305  12.316  1.00  9.88           C  
ATOM   1048  CG2 VAL A 139      13.781   9.703  12.325  1.00 11.91           C  
ATOM   1049  N   THR A 140      11.793   6.748  12.886  1.00 14.56           N  
ATOM   1050  CA  THR A 140      10.390   6.718  13.306  1.00 14.58           C  
ATOM   1051  C   THR A 140      10.241   7.607  14.553  1.00 14.83           C  
ATOM   1052  O   THR A 140      10.950   7.425  15.541  1.00 14.86           O  
ATOM   1053  CB  THR A 140       9.913   5.294  13.655  1.00 15.60           C  
ATOM   1054  OG1 THR A 140      10.096   4.435  12.521  1.00 15.85           O  
ATOM   1055  CG2 THR A 140       8.437   5.306  14.048  1.00 13.61           C  
ATOM   1056  N   PHE A 141       9.369   8.602  14.474  1.00 14.89           N  
ATOM   1057  CA  PHE A 141       9.129   9.485  15.591  1.00 13.63           C  
ATOM   1058  C   PHE A 141       7.648   9.588  15.873  1.00 14.05           C  
ATOM   1059  O   PHE A 141       6.878  10.014  15.028  1.00 11.86           O  
ATOM   1060  CB  PHE A 141       9.701  10.887  15.330  1.00 15.33           C  
ATOM   1061  CG  PHE A 141       9.363  11.898  16.424  1.00 16.87           C  
ATOM   1062  CD1 PHE A 141      10.009  11.846  17.669  1.00 17.64           C  
ATOM   1063  CD2 PHE A 141       8.397  12.891  16.218  1.00 16.26           C  
ATOM   1064  CE1 PHE A 141       9.675  12.743  18.692  1.00 14.56           C  
ATOM   1065  CE2 PHE A 141       8.069  13.783  17.238  1.00 15.92           C  
ATOM   1066  CZ  PHE A 141       8.721  13.711  18.471  1.00 15.09           C  
ATOM   1067  N   ASP A 142       7.244   9.147  17.059  1.00 16.22           N  
ATOM   1068  CA  ASP A 142       5.852   9.262  17.479  1.00 18.20           C  
ATOM   1069  C   ASP A 142       4.932   8.514  16.520  1.00 18.45           C  
ATOM   1070  O   ASP A 142       3.786   8.905  16.304  1.00 18.89           O  
ATOM   1071  CB  ASP A 142       5.505  10.767  17.528  1.00 21.36           C  
ATOM   1072  CG  ASP A 142       4.383  11.108  18.496  1.00 25.62           C  
ATOM   1073  OD1 ASP A 142       4.043  10.292  19.382  1.00 26.71           O  
ATOM   1074  OD2 ASP A 142       3.850  12.229  18.372  1.00 24.55           O  
ATOM   1075  N   GLY A 143       5.452   7.449  15.923  1.00 19.53           N  
ATOM   1076  CA  GLY A 143       4.655   6.663  14.991  1.00 20.94           C  
ATOM   1077  C   GLY A 143       4.763   7.058  13.520  1.00 22.33           C  
ATOM   1078  O   GLY A 143       4.330   6.313  12.624  1.00 23.79           O  
ATOM   1079  N   TYR A 144       5.371   8.205  13.245  1.00 21.00           N  
ATOM   1080  CA  TYR A 144       5.499   8.659  11.871  1.00 19.35           C  
ATOM   1081  C   TYR A 144       6.867   8.381  11.274  1.00 17.70           C  
ATOM   1082  O   TYR A 144       7.852   8.216  11.983  1.00 16.93           O  
ATOM   1083  CB  TYR A 144       5.205  10.151  11.777  1.00 20.71           C  
ATOM   1084  CG  TYR A 144       3.817  10.536  12.215  1.00 22.52           C  
ATOM   1085  CD1 TYR A 144       3.528  10.750  13.558  1.00 23.50           C  
ATOM   1086  CD2 TYR A 144       2.792  10.690  11.283  1.00 23.91           C  
ATOM   1087  CE1 TYR A 144       2.245  11.117  13.968  1.00 26.38           C  
ATOM   1088  CE2 TYR A 144       1.518  11.055  11.674  1.00 25.52           C  
ATOM   1089  CZ  TYR A 144       1.246  11.265  13.018  1.00 27.53           C  
ATOM   1090  OH  TYR A 144      -0.018  11.653  13.406  1.00 30.90           O  
ATOM   1091  N   HIS A 145       6.908   8.317   9.953  1.00 16.21           N  
ATOM   1092  CA  HIS A 145       8.141   8.081   9.228  1.00 16.25           C  
ATOM   1093  C   HIS A 145       8.700   9.404   8.773  1.00 15.40           C  
ATOM   1094  O   HIS A 145       8.259   9.968   7.773  1.00 15.37           O  
ATOM   1095  CB  HIS A 145       7.885   7.152   8.043  1.00 18.68           C  
ATOM   1096  CG  HIS A 145       7.481   5.780   8.454  1.00 21.70           C  
ATOM   1097  ND1 HIS A 145       8.373   4.880   9.019  1.00 24.99           N  
ATOM   1098  CD2 HIS A 145       6.283   5.160   8.458  1.00 25.80           C  
ATOM   1099  CE1 HIS A 145       7.737   3.780   9.348  1.00 25.28           C  
ATOM   1100  NE2 HIS A 145       6.457   3.918   9.019  1.00 26.02           N  
ATOM   1101  N   ASP A 146       9.620   9.927   9.574  1.00 12.69           N  
ATOM   1102  CA  ASP A 146      10.261  11.202   9.308  1.00 11.31           C  
ATOM   1103  C   ASP A 146      11.723  10.936   8.996  1.00 11.07           C  
ATOM   1104  O   ASP A 146      12.119   9.796   8.748  1.00 10.72           O  
ATOM   1105  CB  ASP A 146      10.223  12.070  10.580  1.00 10.02           C  
ATOM   1106  CG  ASP A 146       8.825  12.307  11.109  1.00 12.45           C  
ATOM   1107  OD1 ASP A 146       7.832  12.348  10.356  1.00 13.41           O  
ATOM   1108  OD2 ASP A 146       8.702  12.502  12.320  1.00 11.74           O  
ATOM   1109  N   ASN A 147      12.506  12.009   8.938  1.00 11.07           N  
ATOM   1110  CA  ASN A 147      13.945  11.904   8.770  1.00 11.32           C  
ATOM   1111  C   ASN A 147      14.517  12.738   9.924  1.00 12.99           C  
ATOM   1112  O   ASN A 147      13.815  13.606  10.465  1.00 14.45           O  
ATOM   1113  CB  ASN A 147      14.428  12.373   7.392  1.00 12.78           C  
ATOM   1114  CG  ASN A 147      14.251  13.864   7.161  1.00 13.85           C  
ATOM   1115  OD1 ASN A 147      14.872  14.689   7.815  1.00 14.22           O  
ATOM   1116  ND2 ASN A 147      13.408  14.211   6.210  1.00 16.79           N  
ATOM   1117  N   LEU A 148      15.759  12.476  10.324  1.00 12.07           N  
ATOM   1118  CA  LEU A 148      16.362  13.191  11.448  1.00 12.48           C  
ATOM   1119  C   LEU A 148      16.252  14.701  11.344  1.00 12.43           C  
ATOM   1120  O   LEU A 148      15.903  15.380  12.328  1.00 13.13           O  
ATOM   1121  CB  LEU A 148      17.835  12.826  11.623  1.00 14.01           C  
ATOM   1122  CG  LEU A 148      18.309  12.401  13.023  1.00 18.15           C  
ATOM   1123  CD1 LEU A 148      19.642  13.026  13.340  1.00 15.76           C  
ATOM   1124  CD2 LEU A 148      17.281  12.695  14.110  1.00 16.68           C  
ATOM   1125  N   HIS A 149      16.534  15.227  10.158  1.00  8.87           N  
ATOM   1126  CA  HIS A 149      16.490  16.659   9.944  1.00  8.10           C  
ATOM   1127  C   HIS A 149      15.154  17.310  10.226  1.00  7.93           C  
ATOM   1128  O   HIS A 149      15.089  18.349  10.900  1.00  7.98           O  
ATOM   1129  CB  HIS A 149      16.923  16.991   8.522  1.00  8.86           C  
ATOM   1130  CG  HIS A 149      17.259  18.440   8.336  1.00  5.20           C  
ATOM   1131  ND1 HIS A 149      18.553  18.891   8.326  1.00  7.89           N  
ATOM   1132  CD2 HIS A 149      16.481  19.540   8.276  1.00  7.65           C  
ATOM   1133  CE1 HIS A 149      18.575  20.200   8.285  1.00  4.47           C  
ATOM   1134  NE2 HIS A 149      17.314  20.626   8.255  1.00  6.32           N  
ATOM   1135  N   SER A 150      14.085  16.751   9.676  1.00  7.80           N  
ATOM   1136  CA  SER A 150      12.766  17.328   9.891  1.00  9.39           C  
ATOM   1137  C   SER A 150      12.302  17.198  11.342  1.00  9.89           C  
ATOM   1138  O   SER A 150      11.465  17.969  11.802  1.00  9.42           O  
ATOM   1139  CB  SER A 150      11.721  16.742   8.916  1.00 10.15           C  
ATOM   1140  OG  SER A 150      11.572  15.338   9.049  1.00 15.77           O  
ATOM   1141  N   ASP A 151      12.815  16.203  12.054  1.00  9.67           N  
ATOM   1142  CA  ASP A 151      12.452  16.038  13.451  1.00  9.62           C  
ATOM   1143  C   ASP A 151      13.064  17.182  14.247  1.00  6.81           C  
ATOM   1144  O   ASP A 151      12.388  17.773  15.072  1.00  8.13           O  
ATOM   1145  CB  ASP A 151      12.893  14.662  13.983  1.00  9.80           C  
ATOM   1146  CG  ASP A 151      11.925  13.550  13.588  1.00 12.89           C  
ATOM   1147  OD1 ASP A 151      10.712  13.844  13.405  1.00 12.99           O  
ATOM   1148  OD2 ASP A 151      12.373  12.391  13.439  1.00 13.16           O  
ATOM   1149  N   TRP A 152      14.310  17.535  13.954  1.00  8.33           N  
ATOM   1150  CA  TRP A 152      14.972  18.643  14.649  1.00  9.29           C  
ATOM   1151  C   TRP A 152      14.400  20.006  14.223  1.00 10.09           C  
ATOM   1152  O   TRP A 152      14.185  20.883  15.049  1.00 10.23           O  
ATOM   1153  CB  TRP A 152      16.500  18.604  14.452  1.00  7.76           C  
ATOM   1154  CG  TRP A 152      17.225  17.724  15.463  1.00  9.57           C  
ATOM   1155  CD1 TRP A 152      17.311  16.358  15.455  1.00  9.39           C  
ATOM   1156  CD2 TRP A 152      17.932  18.161  16.635  1.00 10.04           C  
ATOM   1157  NE1 TRP A 152      18.022  15.920  16.549  1.00  8.76           N  
ATOM   1158  CE2 TRP A 152      18.415  16.996  17.289  1.00  8.78           C  
ATOM   1159  CE3 TRP A 152      18.203  19.421  17.191  1.00  8.84           C  
ATOM   1160  CZ2 TRP A 152      19.156  17.052  18.484  1.00  8.55           C  
ATOM   1161  CZ3 TRP A 152      18.949  19.473  18.390  1.00 12.77           C  
ATOM   1162  CH2 TRP A 152      19.414  18.287  19.017  1.00 10.69           C  
ATOM   1163  N   ASP A 153      14.130  20.185  12.935  1.00 11.08           N  
ATOM   1164  CA  ASP A 153      13.585  21.459  12.442  1.00  9.36           C  
ATOM   1165  C   ASP A 153      12.170  21.727  12.917  1.00  9.95           C  
ATOM   1166  O   ASP A 153      11.839  22.830  13.392  1.00  9.43           O  
ATOM   1167  CB  ASP A 153      13.476  21.450  10.902  1.00  9.16           C  
ATOM   1168  CG  ASP A 153      14.641  22.130  10.194  1.00 10.07           C  
ATOM   1169  OD1 ASP A 153      15.591  22.572  10.858  1.00  9.59           O  
ATOM   1170  OD2 ASP A 153      14.618  22.194   8.938  1.00  8.09           O  
ATOM   1171  N   THR A 154      11.341  20.699  12.765  1.00  9.77           N  
ATOM   1172  CA  THR A 154       9.914  20.812  12.998  1.00 10.01           C  
ATOM   1173  C   THR A 154       9.144  19.956  14.005  1.00 10.00           C  
ATOM   1174  O   THR A 154       8.455  20.492  14.872  1.00 11.99           O  
ATOM   1175  CB  THR A 154       9.213  20.672  11.600  1.00  8.84           C  
ATOM   1176  OG1 THR A 154       9.735  21.665  10.714  1.00  9.91           O  
ATOM   1177  CG2 THR A 154       7.696  20.795  11.680  1.00  9.51           C  
ATOM   1178  N   TYR A 155       9.183  18.643  13.842  1.00 10.03           N  
ATOM   1179  CA  TYR A 155       8.404  17.755  14.685  1.00 12.26           C  
ATOM   1180  C   TYR A 155       8.671  17.683  16.176  1.00 12.49           C  
ATOM   1181  O   TYR A 155       7.728  17.559  16.952  1.00 13.48           O  
ATOM   1182  CB  TYR A 155       8.346  16.378  14.049  1.00 15.34           C  
ATOM   1183  CG  TYR A 155       7.740  16.473  12.672  1.00 17.51           C  
ATOM   1184  CD1 TYR A 155       6.420  16.905  12.508  1.00 19.62           C  
ATOM   1185  CD2 TYR A 155       8.498  16.196  11.528  1.00 19.03           C  
ATOM   1186  CE1 TYR A 155       5.876  17.064  11.249  1.00 21.41           C  
ATOM   1187  CE2 TYR A 155       7.962  16.351  10.259  1.00 19.10           C  
ATOM   1188  CZ  TYR A 155       6.655  16.779  10.136  1.00 22.42           C  
ATOM   1189  OH  TYR A 155       6.096  16.908   8.902  1.00 26.85           O  
ATOM   1190  N   MET A 156       9.928  17.751  16.592  1.00 12.07           N  
ATOM   1191  CA  MET A 156      10.207  17.728  18.016  1.00 12.50           C  
ATOM   1192  C   MET A 156       9.784  19.078  18.632  1.00 13.85           C  
ATOM   1193  O   MET A 156       9.089  19.094  19.655  1.00 14.75           O  
ATOM   1194  CB  MET A 156      11.653  17.321  18.276  1.00 12.40           C  
ATOM   1195  CG  MET A 156      11.916  15.873  17.821  1.00 12.83           C  
ATOM   1196  SD  MET A 156      13.425  15.090  18.459  1.00 15.93           S  
ATOM   1197  CE  MET A 156      14.688  15.982  17.558  1.00 16.18           C  
ATOM   1198  N   PRO A 157      10.124  20.218  17.987  1.00 14.22           N  
ATOM   1199  CA  PRO A 157       9.714  21.520  18.534  1.00 15.13           C  
ATOM   1200  C   PRO A 157       8.176  21.606  18.644  1.00 16.77           C  
ATOM   1201  O   PRO A 157       7.643  22.109  19.644  1.00 17.02           O  
ATOM   1202  CB  PRO A 157      10.253  22.499  17.495  1.00 14.89           C  
ATOM   1203  CG  PRO A 157      11.508  21.870  17.099  1.00 14.72           C  
ATOM   1204  CD  PRO A 157      11.144  20.412  16.938  1.00 13.40           C  
ATOM   1205  N   GLN A 158       7.459  21.121  17.628  1.00 15.80           N  
ATOM   1206  CA  GLN A 158       6.004  21.153  17.679  1.00 16.85           C  
ATOM   1207  C   GLN A 158       5.452  20.145  18.688  1.00 17.57           C  
ATOM   1208  O   GLN A 158       4.371  20.335  19.224  1.00 19.65           O  
ATOM   1209  CB  GLN A 158       5.389  20.952  16.295  1.00 17.38           C  
ATOM   1210  CG  GLN A 158       5.678  22.120  15.370  1.00 18.38           C  
ATOM   1211  CD  GLN A 158       5.107  21.982  13.955  1.00 20.62           C  
ATOM   1212  OE1 GLN A 158       5.283  22.879  13.134  1.00 20.07           O  
ATOM   1213  NE2 GLN A 158       4.412  20.873  13.670  1.00 20.12           N  
ATOM   1214  N   LYS A 159       6.198  19.091  18.983  1.00 18.80           N  
ATOM   1215  CA  LYS A 159       5.728  18.113  19.961  1.00 19.90           C  
ATOM   1216  C   LYS A 159       5.726  18.801  21.319  1.00 20.86           C  
ATOM   1217  O   LYS A 159       4.801  18.645  22.109  1.00 23.04           O  
ATOM   1218  CB  LYS A 159       6.659  16.903  20.002  1.00 21.00           C  
ATOM   1219  CG  LYS A 159       6.299  15.856  21.032  1.00 23.07           C  
ATOM   1220  CD  LYS A 159       5.017  15.158  20.660  1.00 24.13           C  
ATOM   1221  CE  LYS A 159       4.789  13.949  21.528  1.00 25.66           C  
ATOM   1222  NZ  LYS A 159       3.476  13.323  21.204  1.00 29.68           N  
ATOM   1223  N   LEU A 160       6.780  19.558  21.577  1.00 20.12           N  
ATOM   1224  CA  LEU A 160       6.930  20.297  22.813  1.00 21.26           C  
ATOM   1225  C   LEU A 160       5.867  21.383  23.021  1.00 21.48           C  
ATOM   1226  O   LEU A 160       5.219  21.430  24.067  1.00 23.76           O  
ATOM   1227  CB  LEU A 160       8.321  20.942  22.850  1.00 22.39           C  
ATOM   1228  CG  LEU A 160       8.645  21.793  24.081  1.00 24.22           C  
ATOM   1229  CD1 LEU A 160       8.938  20.873  25.275  1.00 24.99           C  
ATOM   1230  CD2 LEU A 160       9.828  22.693  23.794  1.00 23.65           C  
ATOM   1231  N   ILE A 161       5.699  22.251  22.026  1.00 21.17           N  
ATOM   1232  CA  ILE A 161       4.771  23.383  22.090  1.00 22.20           C  
ATOM   1233  C   ILE A 161       3.310  23.151  21.682  1.00 24.16           C  
ATOM   1234  O   ILE A 161       2.405  23.822  22.196  1.00 24.59           O  
ATOM   1235  CB  ILE A 161       5.351  24.578  21.293  1.00 21.27           C  
ATOM   1236  CG1 ILE A 161       6.730  24.942  21.847  1.00 21.07           C  
ATOM   1237  CG2 ILE A 161       4.431  25.780  21.342  1.00 21.62           C  
ATOM   1238  CD1 ILE A 161       6.745  25.327  23.293  1.00 19.33           C  
ATOM   1239  N   GLY A 162       3.084  22.294  20.691  1.00 26.04           N  
ATOM   1240  CA  GLY A 162       1.723  22.006  20.270  1.00 26.00           C  
ATOM   1241  C   GLY A 162       1.121  22.721  19.076  1.00 27.52           C  
ATOM   1242  O   GLY A 162      -0.073  22.559  18.820  1.00 30.46           O  
ATOM   1243  N   GLY A 163       1.913  23.468  18.318  1.00 27.07           N  
ATOM   1244  CA  GLY A 163       1.370  24.164  17.165  1.00 27.55           C  
ATOM   1245  C   GLY A 163       2.442  25.051  16.573  1.00 28.38           C  
ATOM   1246  O   GLY A 163       3.503  25.194  17.177  1.00 28.33           O  
ATOM   1247  N   HIS A 164       2.188  25.646  15.409  1.00 29.04           N  
ATOM   1248  CA  HIS A 164       3.182  26.513  14.791  1.00 29.53           C  
ATOM   1249  C   HIS A 164       2.655  27.899  14.418  1.00 28.22           C  
ATOM   1250  O   HIS A 164       3.218  28.582  13.567  1.00 28.98           O  
ATOM   1251  CB  HIS A 164       3.846  25.815  13.594  1.00 33.14           C  
ATOM   1252  CG  HIS A 164       2.971  25.695  12.388  1.00 38.18           C  
ATOM   1253  ND1 HIS A 164       3.181  26.447  11.240  1.00 40.29           N  
ATOM   1254  CD2 HIS A 164       1.879  24.939  12.132  1.00 39.42           C  
ATOM   1255  CE1 HIS A 164       2.258  26.158  10.353  1.00 41.76           C  
ATOM   1256  NE2 HIS A 164       1.448  25.243  10.865  1.00 40.61           N  
ATOM   1257  N   ALA A 165       1.557  28.302  15.041  1.00 27.08           N  
ATOM   1258  CA  ALA A 165       0.992  29.620  14.784  1.00 27.55           C  
ATOM   1259  C   ALA A 165       1.851  30.657  15.492  1.00 27.62           C  
ATOM   1260  O   ALA A 165       2.579  30.324  16.435  1.00 27.66           O  
ATOM   1261  CB  ALA A 165      -0.438  29.693  15.300  1.00 27.68           C  
ATOM   1262  N   LEU A 166       1.731  31.917  15.078  1.00 27.10           N  
ATOM   1263  CA  LEU A 166       2.504  32.987  15.695  1.00 26.11           C  
ATOM   1264  C   LEU A 166       2.225  33.066  17.182  1.00 25.27           C  
ATOM   1265  O   LEU A 166       3.118  33.360  17.960  1.00 24.31           O  
ATOM   1266  CB  LEU A 166       2.238  34.327  15.012  1.00 27.48           C  
ATOM   1267  CG  LEU A 166       3.158  34.592  13.822  1.00 27.82           C  
ATOM   1268  CD1 LEU A 166       2.667  35.792  13.077  1.00 28.22           C  
ATOM   1269  CD2 LEU A 166       4.598  34.803  14.282  1.00 29.96           C  
ATOM   1270  N   SER A 167       1.002  32.740  17.581  1.00 25.05           N  
ATOM   1271  CA  SER A 167       0.660  32.759  19.001  1.00 26.92           C  
ATOM   1272  C   SER A 167       1.439  31.691  19.778  1.00 25.82           C  
ATOM   1273  O   SER A 167       1.805  31.910  20.932  1.00 27.09           O  
ATOM   1274  CB  SER A 167      -0.855  32.619  19.224  1.00 26.07           C  
ATOM   1275  OG  SER A 167      -1.396  31.542  18.489  1.00 26.76           O  
ATOM   1276  N   ASP A 168       1.729  30.561  19.137  1.00 24.57           N  
ATOM   1277  CA  ASP A 168       2.497  29.495  19.785  1.00 23.55           C  
ATOM   1278  C   ASP A 168       3.937  29.938  19.961  1.00 22.09           C  
ATOM   1279  O   ASP A 168       4.548  29.710  21.006  1.00 21.88           O  
ATOM   1280  CB  ASP A 168       2.460  28.216  18.951  1.00 24.52           C  
ATOM   1281  CG  ASP A 168       1.071  27.658  18.838  1.00 26.09           C  
ATOM   1282  OD1 ASP A 168       0.443  27.422  19.893  1.00 28.34           O  
ATOM   1283  OD2 ASP A 168       0.588  27.489  17.701  1.00 28.16           O  
ATOM   1284  N   ALA A 169       4.473  30.595  18.942  1.00 20.22           N  
ATOM   1285  CA  ALA A 169       5.841  31.066  19.018  1.00 19.09           C  
ATOM   1286  C   ALA A 169       5.932  32.161  20.072  1.00 19.81           C  
ATOM   1287  O   ALA A 169       6.892  32.209  20.842  1.00 18.40           O  
ATOM   1288  CB  ALA A 169       6.296  31.576  17.678  1.00 15.56           C  
ATOM   1289  N   GLU A 170       4.903  33.004  20.156  1.00 21.55           N  
ATOM   1290  CA  GLU A 170       4.910  34.081  21.140  1.00 24.42           C  
ATOM   1291  C   GLU A 170       4.972  33.533  22.564  1.00 23.91           C  
ATOM   1292  O   GLU A 170       5.769  34.018  23.379  1.00 25.17           O  
ATOM   1293  CB  GLU A 170       3.705  35.006  20.981  1.00 26.81           C  
ATOM   1294  CG  GLU A 170       3.960  36.401  21.577  1.00 33.33           C  
ATOM   1295  CD  GLU A 170       2.751  37.348  21.512  1.00 37.16           C  
ATOM   1296  OE1 GLU A 170       1.595  36.866  21.410  1.00 38.55           O  
ATOM   1297  OE2 GLU A 170       2.962  38.586  21.584  1.00 40.20           O  
ATOM   1298  N   SER A 171       4.202  32.486  22.857  1.00 23.37           N  
ATOM   1299  CA  SER A 171       4.218  31.922  24.207  1.00 23.40           C  
ATOM   1300  C   SER A 171       5.506  31.186  24.529  1.00 21.73           C  
ATOM   1301  O   SER A 171       5.952  31.195  25.677  1.00 20.93           O  
ATOM   1302  CB  SER A 171       3.006  31.025  24.470  1.00 26.51           C  
ATOM   1303  OG  SER A 171       3.113  29.791  23.789  1.00 34.86           O  
ATOM   1304  N   TRP A 172       6.112  30.549  23.529  1.00 18.81           N  
ATOM   1305  CA  TRP A 172       7.367  29.844  23.767  1.00 18.26           C  
ATOM   1306  C   TRP A 172       8.444  30.888  24.081  1.00 17.21           C  
ATOM   1307  O   TRP A 172       9.198  30.748  25.041  1.00 18.07           O  
ATOM   1308  CB  TRP A 172       7.763  29.023  22.543  1.00 16.81           C  
ATOM   1309  CG  TRP A 172       8.891  28.042  22.770  1.00 18.98           C  
ATOM   1310  CD1 TRP A 172       9.468  27.697  23.964  1.00 19.86           C  
ATOM   1311  CD2 TRP A 172       9.559  27.262  21.764  1.00 18.04           C  
ATOM   1312  NE1 TRP A 172      10.457  26.749  23.761  1.00 19.05           N  
ATOM   1313  CE2 TRP A 172      10.529  26.463  22.420  1.00 18.14           C  
ATOM   1314  CE3 TRP A 172       9.431  27.158  20.371  1.00 17.81           C  
ATOM   1315  CZ2 TRP A 172      11.361  25.569  21.732  1.00 17.73           C  
ATOM   1316  CZ3 TRP A 172      10.258  26.270  19.682  1.00 16.79           C  
ATOM   1317  CH2 TRP A 172      11.213  25.486  20.369  1.00 17.96           C  
ATOM   1318  N   ALA A 173       8.463  31.972  23.312  1.00 17.42           N  
ATOM   1319  CA  ALA A 173       9.440  33.033  23.510  1.00 16.61           C  
ATOM   1320  C   ALA A 173       9.323  33.629  24.916  1.00 18.45           C  
ATOM   1321  O   ALA A 173      10.334  33.968  25.544  1.00 17.44           O  
ATOM   1322  CB  ALA A 173       9.248  34.106  22.473  1.00 14.79           C  
ATOM   1323  N   LYS A 174       8.096  33.716  25.425  1.00 19.44           N  
ATOM   1324  CA  LYS A 174       7.858  34.267  26.760  1.00 21.70           C  
ATOM   1325  C   LYS A 174       8.586  33.471  27.856  1.00 21.54           C  
ATOM   1326  O   LYS A 174       9.217  34.048  28.751  1.00 22.48           O  
ATOM   1327  CB  LYS A 174       6.359  34.305  27.057  1.00 25.08           C  
ATOM   1328  CG  LYS A 174       5.926  35.543  27.807  1.00 32.40           C  
ATOM   1329  CD  LYS A 174       6.859  35.825  29.004  1.00 37.70           C  
ATOM   1330  CE  LYS A 174       7.533  37.209  28.918  1.00 38.37           C  
ATOM   1331  NZ  LYS A 174       8.737  37.287  29.800  1.00 39.12           N  
ATOM   1332  N   THR A 175       8.524  32.148  27.775  1.00 20.09           N  
ATOM   1333  CA  THR A 175       9.168  31.310  28.769  1.00 19.78           C  
ATOM   1334  C   THR A 175      10.679  31.401  28.610  1.00 18.46           C  
ATOM   1335  O   THR A 175      11.427  31.448  29.587  1.00 18.84           O  
ATOM   1336  CB  THR A 175       8.694  29.837  28.657  1.00 21.85           C  
ATOM   1337  OG1 THR A 175       9.445  29.170  27.646  1.00 28.08           O  
ATOM   1338  CG2 THR A 175       7.236  29.776  28.261  1.00 21.77           C  
ATOM   1339  N   LEU A 176      11.131  31.466  27.368  1.00 16.62           N  
ATOM   1340  CA  LEU A 176      12.557  31.558  27.100  1.00 16.64           C  
ATOM   1341  C   LEU A 176      13.112  32.870  27.667  1.00 16.10           C  
ATOM   1342  O   LEU A 176      14.186  32.886  28.284  1.00 15.95           O  
ATOM   1343  CB  LEU A 176      12.803  31.466  25.595  1.00 17.79           C  
ATOM   1344  CG  LEU A 176      13.288  30.147  24.999  1.00 19.67           C  
ATOM   1345  CD1 LEU A 176      13.012  28.941  25.867  1.00 18.14           C  
ATOM   1346  CD2 LEU A 176      12.666  29.991  23.643  1.00 19.24           C  
ATOM   1347  N   VAL A 177      12.391  33.972  27.440  1.00 16.86           N  
ATOM   1348  CA  VAL A 177      12.803  35.284  27.947  1.00 17.45           C  
ATOM   1349  C   VAL A 177      12.886  35.237  29.473  1.00 18.69           C  
ATOM   1350  O   VAL A 177      13.906  35.636  30.054  1.00 18.92           O  
ATOM   1351  CB  VAL A 177      11.848  36.401  27.491  1.00 17.76           C  
ATOM   1352  CG1 VAL A 177      12.120  37.698  28.271  1.00 17.99           C  
ATOM   1353  CG2 VAL A 177      12.056  36.666  26.009  1.00 16.22           C  
ATOM   1354  N   GLN A 178      11.863  34.670  30.113  1.00 19.85           N  
ATOM   1355  CA  GLN A 178      11.850  34.543  31.576  1.00 22.47           C  
ATOM   1356  C   GLN A 178      13.130  33.863  32.052  1.00 21.46           C  
ATOM   1357  O   GLN A 178      13.814  34.341  32.959  1.00 21.73           O  
ATOM   1358  CB  GLN A 178      10.639  33.735  32.046  1.00 27.12           C  
ATOM   1359  CG  GLN A 178      10.785  33.249  33.490  1.00 38.66           C  
ATOM   1360  CD  GLN A 178       9.576  32.474  34.005  1.00 45.27           C  
ATOM   1361  OE1 GLN A 178       8.720  33.028  34.705  1.00 48.74           O  
ATOM   1362  NE2 GLN A 178       9.519  31.176  33.696  1.00 49.66           N  
ATOM   1363  N   ASN A 179      13.490  32.774  31.393  1.00 19.68           N  
ATOM   1364  CA  ASN A 179      14.685  32.041  31.741  1.00 18.56           C  
ATOM   1365  C   ASN A 179      15.998  32.766  31.538  1.00 17.03           C  
ATOM   1366  O   ASN A 179      16.969  32.494  32.248  1.00 16.98           O  
ATOM   1367  CB  ASN A 179      14.695  30.713  31.011  1.00 22.54           C  
ATOM   1368  CG  ASN A 179      13.683  29.753  31.582  1.00 28.84           C  
ATOM   1369  OD1 ASN A 179      12.525  29.713  31.160  1.00 32.61           O  
ATOM   1370  ND2 ASN A 179      14.091  29.023  32.609  1.00 30.61           N  
ATOM   1371  N   ILE A 180      16.063  33.641  30.541  1.00 16.18           N  
ATOM   1372  CA  ILE A 180      17.297  34.385  30.275  1.00 17.80           C  
ATOM   1373  C   ILE A 180      17.474  35.545  31.275  1.00 19.34           C  
ATOM   1374  O   ILE A 180      18.574  35.800  31.768  1.00 19.56           O  
ATOM   1375  CB  ILE A 180      17.315  34.954  28.835  1.00 17.64           C  
ATOM   1376  CG1 ILE A 180      17.400  33.818  27.804  1.00 18.06           C  
ATOM   1377  CG2 ILE A 180      18.503  35.894  28.648  1.00 18.33           C  
ATOM   1378  CD1 ILE A 180      16.973  34.240  26.378  1.00 17.47           C  
ATOM   1379  N   GLU A 181      16.372  36.216  31.580  1.00 20.50           N  
ATOM   1380  CA  GLU A 181      16.388  37.357  32.488  1.00 23.99           C  
ATOM   1381  C   GLU A 181      16.324  37.031  33.966  1.00 25.00           C  
ATOM   1382  O   GLU A 181      16.911  37.730  34.792  1.00 24.53           O  
ATOM   1383  CB  GLU A 181      15.215  38.270  32.171  1.00 22.92           C  
ATOM   1384  CG  GLU A 181      15.578  39.357  31.221  1.00 24.77           C  
ATOM   1385  CD  GLU A 181      14.381  40.051  30.669  1.00 21.50           C  
ATOM   1386  OE1 GLU A 181      13.346  40.121  31.348  1.00 22.53           O  
ATOM   1387  OE2 GLU A 181      14.483  40.531  29.539  1.00 27.32           O  
ATOM   1388  N   SER A 182      15.584  35.980  34.286  1.00 26.54           N  
ATOM   1389  CA  SER A 182      15.365  35.581  35.655  1.00 29.22           C  
ATOM   1390  C   SER A 182      15.179  34.071  35.764  1.00 28.52           C  
ATOM   1391  O   SER A 182      14.152  33.600  36.253  1.00 31.87           O  
ATOM   1392  CB  SER A 182      14.098  36.309  36.124  1.00 32.98           C  
ATOM   1393  OG  SER A 182      13.596  35.837  37.366  1.00 40.48           O  
ATOM   1394  N   GLY A 183      16.163  33.300  35.330  1.00 26.90           N  
ATOM   1395  CA  GLY A 183      16.000  31.865  35.410  1.00 25.08           C  
ATOM   1396  C   GLY A 183      17.243  31.064  35.150  1.00 24.58           C  
ATOM   1397  O   GLY A 183      18.360  31.548  35.358  1.00 22.58           O  
ATOM   1398  N   ASN A 184      17.026  29.884  34.572  1.00 25.68           N  
ATOM   1399  CA  ASN A 184      18.088  28.927  34.272  1.00 27.04           C  
ATOM   1400  C   ASN A 184      19.158  29.349  33.285  1.00 25.56           C  
ATOM   1401  O   ASN A 184      20.260  28.786  33.299  1.00 25.98           O  
ATOM   1402  CB  ASN A 184      17.492  27.611  33.786  1.00 31.57           C  
ATOM   1403  CG  ASN A 184      16.443  27.064  34.726  1.00 35.66           C  
ATOM   1404  OD1 ASN A 184      16.532  27.234  35.939  1.00 39.63           O  
ATOM   1405  ND2 ASN A 184      15.435  26.404  34.168  1.00 38.28           N  
ATOM   1406  N   TYR A 185      18.849  30.296  32.404  1.00 23.19           N  
ATOM   1407  CA  TYR A 185      19.848  30.727  31.428  1.00 21.54           C  
ATOM   1408  C   TYR A 185      20.608  31.986  31.796  1.00 20.95           C  
ATOM   1409  O   TYR A 185      21.620  32.293  31.178  1.00 19.67           O  
ATOM   1410  CB  TYR A 185      19.209  30.988  30.078  1.00 19.94           C  
ATOM   1411  CG  TYR A 185      18.514  29.814  29.456  1.00 18.19           C  
ATOM   1412  CD1 TYR A 185      19.080  28.540  29.475  1.00 18.33           C  
ATOM   1413  CD2 TYR A 185      17.308  29.993  28.789  1.00 18.44           C  
ATOM   1414  CE1 TYR A 185      18.444  27.475  28.845  1.00 17.44           C  
ATOM   1415  CE2 TYR A 185      16.672  28.951  28.168  1.00 18.31           C  
ATOM   1416  CZ  TYR A 185      17.248  27.700  28.192  1.00 18.32           C  
ATOM   1417  OH  TYR A 185      16.590  26.683  27.561  1.00 21.56           O  
ATOM   1418  N   THR A 186      20.127  32.696  32.809  1.00 21.89           N  
ATOM   1419  CA  THR A 186      20.719  33.968  33.228  1.00 22.09           C  
ATOM   1420  C   THR A 186      22.234  33.955  33.299  1.00 22.68           C  
ATOM   1421  O   THR A 186      22.910  34.777  32.689  1.00 22.09           O  
ATOM   1422  CB  THR A 186      20.147  34.422  34.591  1.00 22.23           C  
ATOM   1423  OG1 THR A 186      18.717  34.501  34.499  1.00 22.60           O  
ATOM   1424  CG2 THR A 186      20.707  35.804  35.002  1.00 19.34           C  
ATOM   1425  N   ALA A 187      22.772  32.947  33.964  1.00 23.17           N  
ATOM   1426  CA  ALA A 187      24.209  32.862  34.110  1.00 24.23           C  
ATOM   1427  C   ALA A 187      24.969  32.562  32.807  1.00 24.80           C  
ATOM   1428  O   ALA A 187      26.113  32.979  32.665  1.00 25.16           O  
ATOM   1429  CB  ALA A 187      24.549  31.853  35.211  1.00 23.29           C  
ATOM   1430  N   GLN A 188      24.306  31.887  31.860  1.00 24.75           N  
ATOM   1431  CA  GLN A 188      24.865  31.480  30.553  1.00 24.25           C  
ATOM   1432  C   GLN A 188      24.790  32.520  29.438  1.00 23.15           C  
ATOM   1433  O   GLN A 188      25.692  32.606  28.595  1.00 22.46           O  
ATOM   1434  CB  GLN A 188      24.106  30.267  30.017  1.00 26.88           C  
ATOM   1435  CG  GLN A 188      24.411  28.936  30.658  1.00 32.12           C  
ATOM   1436  CD  GLN A 188      23.587  27.829  30.028  1.00 33.14           C  
ATOM   1437  OE1 GLN A 188      23.931  27.322  28.975  1.00 35.96           O  
ATOM   1438  NE2 GLN A 188      22.466  27.500  30.641  1.00 33.62           N  
ATOM   1439  N   ALA A 189      23.660  33.225  29.390  1.00 21.56           N  
ATOM   1440  CA  ALA A 189      23.375  34.237  28.380  1.00 21.03           C  
ATOM   1441  C   ALA A 189      24.544  35.098  27.881  1.00 22.27           C  
ATOM   1442  O   ALA A 189      24.752  35.207  26.672  1.00 21.31           O  
ATOM   1443  CB  ALA A 189      22.235  35.116  28.840  1.00 20.37           C  
ATOM   1444  N   ILE A 190      25.341  35.674  28.779  1.00 22.33           N  
ATOM   1445  CA  ILE A 190      26.437  36.523  28.320  1.00 24.31           C  
ATOM   1446  C   ILE A 190      27.451  35.774  27.471  1.00 21.72           C  
ATOM   1447  O   ILE A 190      28.103  36.368  26.625  1.00 21.01           O  
ATOM   1448  CB  ILE A 190      27.195  37.241  29.482  1.00 29.25           C  
ATOM   1449  CG1 ILE A 190      28.267  36.330  30.088  1.00 31.78           C  
ATOM   1450  CG2 ILE A 190      26.244  37.651  30.578  1.00 32.12           C  
ATOM   1451  CD1 ILE A 190      29.629  37.004  30.208  1.00 35.47           C  
ATOM   1452  N   GLY A 191      27.615  34.484  27.732  1.00 20.43           N  
ATOM   1453  CA  GLY A 191      28.566  33.691  26.970  1.00 18.80           C  
ATOM   1454  C   GLY A 191      28.128  33.423  25.533  1.00 18.65           C  
ATOM   1455  O   GLY A 191      28.958  33.163  24.669  1.00 18.26           O  
ATOM   1456  N   TRP A 192      26.824  33.495  25.279  1.00 16.96           N  
ATOM   1457  CA  TRP A 192      26.279  33.272  23.943  1.00 14.94           C  
ATOM   1458  C   TRP A 192      26.726  34.348  22.945  1.00 15.85           C  
ATOM   1459  O   TRP A 192      26.804  34.085  21.746  1.00 15.16           O  
ATOM   1460  CB  TRP A 192      24.753  33.266  23.994  1.00 11.34           C  
ATOM   1461  CG  TRP A 192      24.177  32.201  24.851  1.00  8.10           C  
ATOM   1462  CD1 TRP A 192      24.810  31.091  25.310  1.00  7.83           C  
ATOM   1463  CD2 TRP A 192      22.829  32.130  25.335  1.00  8.76           C  
ATOM   1464  NE1 TRP A 192      23.935  30.321  26.049  1.00  8.81           N  
ATOM   1465  CE2 TRP A 192      22.716  30.935  26.079  1.00  9.11           C  
ATOM   1466  CE3 TRP A 192      21.711  32.964  25.209  1.00 10.42           C  
ATOM   1467  CZ2 TRP A 192      21.508  30.547  26.701  1.00  8.62           C  
ATOM   1468  CZ3 TRP A 192      20.515  32.581  25.826  1.00 10.84           C  
ATOM   1469  CH2 TRP A 192      20.428  31.379  26.564  1.00 10.25           C  
ATOM   1470  N   ILE A 193      26.971  35.568  23.425  1.00 15.11           N  
ATOM   1471  CA  ILE A 193      27.370  36.656  22.539  1.00 13.98           C  
ATOM   1472  C   ILE A 193      28.762  37.175  22.814  1.00 16.82           C  
ATOM   1473  O   ILE A 193      29.213  38.134  22.188  1.00 18.00           O  
ATOM   1474  CB  ILE A 193      26.403  37.839  22.650  1.00 15.31           C  
ATOM   1475  CG1 ILE A 193      26.440  38.422  24.073  1.00 14.95           C  
ATOM   1476  CG2 ILE A 193      24.995  37.402  22.267  1.00 15.36           C  
ATOM   1477  CD1 ILE A 193      25.537  39.608  24.287  1.00 14.49           C  
ATOM   1478  N   LYS A 194      29.470  36.518  23.711  1.00 19.15           N  
ATOM   1479  CA  LYS A 194      30.798  36.969  24.065  1.00 20.54           C  
ATOM   1480  C   LYS A 194      31.735  36.965  22.878  1.00 20.14           C  
ATOM   1481  O   LYS A 194      31.964  35.936  22.265  1.00 21.54           O  
ATOM   1482  CB  LYS A 194      31.350  36.119  25.204  1.00 23.26           C  
ATOM   1483  CG  LYS A 194      32.750  36.494  25.612  1.00 27.36           C  
ATOM   1484  CD  LYS A 194      32.855  36.649  27.105  1.00 31.52           C  
ATOM   1485  CE  LYS A 194      34.320  36.668  27.517  1.00 34.44           C  
ATOM   1486  NZ  LYS A 194      35.096  37.661  26.714  1.00 37.49           N  
ATOM   1487  N   GLY A 195      32.233  38.142  22.529  1.00 20.13           N  
ATOM   1488  CA  GLY A 195      33.150  38.262  21.413  1.00 20.86           C  
ATOM   1489  C   GLY A 195      32.532  38.627  20.076  1.00 20.11           C  
ATOM   1490  O   GLY A 195      33.258  39.050  19.177  1.00 22.22           O  
ATOM   1491  N   ASP A 196      31.217  38.472  19.937  1.00 18.27           N  
ATOM   1492  CA  ASP A 196      30.521  38.791  18.693  1.00 17.41           C  
ATOM   1493  C   ASP A 196      30.821  40.241  18.300  1.00 20.75           C  
ATOM   1494  O   ASP A 196      30.623  41.162  19.100  1.00 19.73           O  
ATOM   1495  CB  ASP A 196      29.007  38.585  18.852  1.00 16.63           C  
ATOM   1496  CG  ASP A 196      28.616  37.114  19.045  1.00 13.96           C  
ATOM   1497  OD1 ASP A 196      29.507  36.238  19.171  1.00 15.01           O  
ATOM   1498  OD2 ASP A 196      27.406  36.836  19.068  1.00 13.11           O  
ATOM   1499  N   ASN A 197      31.247  40.460  17.059  1.00 22.44           N  
ATOM   1500  CA  ASN A 197      31.621  41.812  16.611  1.00 24.51           C  
ATOM   1501  C   ASN A 197      31.223  41.973  15.158  1.00 23.91           C  
ATOM   1502  O   ASN A 197      31.757  41.271  14.308  1.00 23.58           O  
ATOM   1503  CB  ASN A 197      33.163  41.995  16.759  1.00 27.30           C  
ATOM   1504  CG  ASN A 197      33.620  43.484  16.722  1.00 33.20           C  
ATOM   1505  OD1 ASN A 197      33.003  44.269  15.987  1.00 31.18           O  
ATOM   1506  ND2 ASN A 197      34.683  43.823  17.497  1.00 39.04           N  
ATOM   1507  N   ILE A 198      30.329  42.908  14.852  1.00 24.20           N  
ATOM   1508  CA  ILE A 198      29.921  43.079  13.458  1.00 25.79           C  
ATOM   1509  C   ILE A 198      31.077  43.432  12.516  1.00 27.38           C  
ATOM   1510  O   ILE A 198      30.952  43.319  11.301  1.00 27.91           O  
ATOM   1511  CB  ILE A 198      28.804  44.125  13.257  1.00 25.97           C  
ATOM   1512  CG1 ILE A 198      29.306  45.528  13.584  1.00 25.50           C  
ATOM   1513  CG2 ILE A 198      27.558  43.753  14.035  1.00 25.14           C  
ATOM   1514  CD1 ILE A 198      28.301  46.574  13.194  1.00 26.12           C  
ATOM   1515  N   SER A 199      32.194  43.888  13.058  1.00 27.67           N  
ATOM   1516  CA  SER A 199      33.324  44.221  12.205  1.00 29.36           C  
ATOM   1517  C   SER A 199      34.180  42.980  11.958  1.00 29.38           C  
ATOM   1518  O   SER A 199      35.237  43.055  11.335  1.00 31.22           O  
ATOM   1519  CB  SER A 199      34.160  45.340  12.827  1.00 30.87           C  
ATOM   1520  OG  SER A 199      34.896  44.872  13.944  1.00 36.85           O  
ATOM   1521  N   GLU A 200      33.697  41.827  12.405  1.00 28.10           N  
ATOM   1522  CA  GLU A 200      34.420  40.566  12.233  1.00 27.31           C  
ATOM   1523  C   GLU A 200      33.362  39.480  12.026  1.00 23.74           C  
ATOM   1524  O   GLU A 200      33.379  38.449  12.694  1.00 23.98           O  
ATOM   1525  CB  GLU A 200      35.221  40.284  13.500  1.00 30.76           C  
ATOM   1526  CG  GLU A 200      36.638  39.869  13.275  1.00 39.44           C  
ATOM   1527  CD  GLU A 200      37.333  39.474  14.569  1.00 45.34           C  
ATOM   1528  OE1 GLU A 200      36.650  39.362  15.623  1.00 48.56           O  
ATOM   1529  OE2 GLU A 200      38.567  39.254  14.525  1.00 48.61           O  
ATOM   1530  N   PRO A 201      32.481  39.660  11.032  1.00 22.30           N  
ATOM   1531  CA  PRO A 201      31.416  38.689  10.768  1.00 21.24           C  
ATOM   1532  C   PRO A 201      31.811  37.256  10.455  1.00 20.21           C  
ATOM   1533  O   PRO A 201      31.096  36.350  10.838  1.00 17.81           O  
ATOM   1534  CB  PRO A 201      30.619  39.343   9.651  1.00 20.30           C  
ATOM   1535  CG  PRO A 201      31.673  40.102   8.890  1.00 22.27           C  
ATOM   1536  CD  PRO A 201      32.516  40.704   9.990  1.00 21.98           C  
ATOM   1537  N   ILE A 202      32.941  37.039   9.782  1.00 20.91           N  
ATOM   1538  CA  ILE A 202      33.360  35.669   9.469  1.00 21.19           C  
ATOM   1539  C   ILE A 202      33.804  34.950  10.740  1.00 20.87           C  
ATOM   1540  O   ILE A 202      33.332  33.857  11.034  1.00 21.11           O  
ATOM   1541  CB  ILE A 202      34.493  35.607   8.377  1.00 20.96           C  
ATOM   1542  CG1 ILE A 202      33.990  36.205   7.061  1.00 21.31           C  
ATOM   1543  CG2 ILE A 202      34.952  34.171   8.148  1.00 21.00           C  
ATOM   1544  CD1 ILE A 202      32.549  35.882   6.751  1.00 25.39           C  
ATOM   1545  N   THR A 203      34.673  35.583  11.524  1.00 21.31           N  
ATOM   1546  CA  THR A 203      35.157  34.978  12.771  1.00 20.53           C  
ATOM   1547  C   THR A 203      33.992  34.757  13.731  1.00 19.46           C  
ATOM   1548  O   THR A 203      33.895  33.715  14.361  1.00 19.68           O  
ATOM   1549  CB  THR A 203      36.214  35.863  13.472  1.00 23.00           C  
ATOM   1550  OG1 THR A 203      37.153  36.335  12.500  1.00 26.78           O  
ATOM   1551  CG2 THR A 203      36.970  35.066  14.527  1.00 23.73           C  
ATOM   1552  N   THR A 204      33.086  35.722  13.804  1.00 17.18           N  
ATOM   1553  CA  THR A 204      31.940  35.593  14.683  1.00 16.82           C  
ATOM   1554  C   THR A 204      31.043  34.433  14.250  1.00 16.54           C  
ATOM   1555  O   THR A 204      30.778  33.515  15.022  1.00 16.47           O  
ATOM   1556  CB  THR A 204      31.128  36.892  14.721  1.00 16.57           C  
ATOM   1557  OG1 THR A 204      31.939  37.929  15.281  1.00 15.12           O  
ATOM   1558  CG2 THR A 204      29.904  36.722  15.591  1.00 16.81           C  
ATOM   1559  N   ALA A 205      30.610  34.451  12.997  1.00 16.57           N  
ATOM   1560  CA  ALA A 205      29.736  33.397  12.480  1.00 15.48           C  
ATOM   1561  C   ALA A 205      30.362  32.010  12.533  1.00 15.60           C  
ATOM   1562  O   ALA A 205      29.659  31.027  12.762  1.00 16.52           O  
ATOM   1563  CB  ALA A 205      29.265  33.727  11.070  1.00 15.70           C  
ATOM   1564  N   THR A 206      31.668  31.907  12.309  1.00 14.79           N  
ATOM   1565  CA  THR A 206      32.329  30.601  12.402  1.00 14.53           C  
ATOM   1566  C   THR A 206      32.215  30.087  13.849  1.00 15.14           C  
ATOM   1567  O   THR A 206      32.117  28.882  14.085  1.00 12.76           O  
ATOM   1568  CB  THR A 206      33.819  30.684  12.028  1.00 13.11           C  
ATOM   1569  OG1 THR A 206      33.945  31.240  10.715  1.00 14.53           O  
ATOM   1570  CG2 THR A 206      34.445  29.312  12.034  1.00 15.32           C  
ATOM   1571  N   ARG A 207      32.210  31.014  14.806  1.00 14.39           N  
ATOM   1572  CA  ARG A 207      32.093  30.665  16.209  1.00 14.18           C  
ATOM   1573  C   ARG A 207      30.699  30.075  16.470  1.00 12.22           C  
ATOM   1574  O   ARG A 207      30.558  29.051  17.152  1.00 11.51           O  
ATOM   1575  CB  ARG A 207      32.294  31.916  17.046  1.00 17.25           C  
ATOM   1576  CG  ARG A 207      33.041  31.686  18.325  1.00 23.83           C  
ATOM   1577  CD  ARG A 207      32.357  32.421  19.473  1.00 27.37           C  
ATOM   1578  NE  ARG A 207      32.042  33.820  19.162  1.00 29.73           N  
ATOM   1579  CZ  ARG A 207      32.919  34.730  18.729  1.00 31.39           C  
ATOM   1580  NH1 ARG A 207      34.198  34.418  18.526  1.00 31.69           N  
ATOM   1581  NH2 ARG A 207      32.507  35.965  18.491  1.00 31.41           N  
ATOM   1582  N   TRP A 208      29.672  30.724  15.934  1.00 10.97           N  
ATOM   1583  CA  TRP A 208      28.288  30.264  16.082  1.00 10.62           C  
ATOM   1584  C   TRP A 208      28.160  28.868  15.460  1.00 12.14           C  
ATOM   1585  O   TRP A 208      27.478  28.001  16.012  1.00 12.87           O  
ATOM   1586  CB  TRP A 208      27.311  31.209  15.368  1.00 11.01           C  
ATOM   1587  CG  TRP A 208      27.279  32.638  15.883  1.00 10.44           C  
ATOM   1588  CD1 TRP A 208      27.752  33.095  17.090  1.00 11.14           C  
ATOM   1589  CD2 TRP A 208      26.709  33.780  15.211  1.00 11.54           C  
ATOM   1590  NE1 TRP A 208      27.499  34.446  17.207  1.00 10.79           N  
ATOM   1591  CE2 TRP A 208      26.864  34.886  16.080  1.00 11.80           C  
ATOM   1592  CE3 TRP A 208      26.090  33.970  13.962  1.00 11.33           C  
ATOM   1593  CZ2 TRP A 208      26.409  36.163  15.735  1.00 11.57           C  
ATOM   1594  CZ3 TRP A 208      25.641  35.247  13.624  1.00 12.87           C  
ATOM   1595  CH2 TRP A 208      25.805  36.326  14.511  1.00 12.27           C  
ATOM   1596  N   ALA A 209      28.806  28.660  14.309  1.00 12.18           N  
ATOM   1597  CA  ALA A 209      28.766  27.365  13.613  1.00 11.53           C  
ATOM   1598  C   ALA A 209      29.461  26.259  14.397  1.00 11.27           C  
ATOM   1599  O   ALA A 209      28.953  25.146  14.491  1.00 11.97           O  
ATOM   1600  CB  ALA A 209      29.382  27.485  12.216  1.00  9.77           C  
ATOM   1601  N   SER A 210      30.610  26.568  14.984  1.00 10.19           N  
ATOM   1602  CA  SER A 210      31.356  25.585  15.764  1.00 11.26           C  
ATOM   1603  C   SER A 210      30.614  25.193  17.044  1.00 10.66           C  
ATOM   1604  O   SER A 210      30.630  24.031  17.440  1.00 11.46           O  
ATOM   1605  CB  SER A 210      32.752  26.108  16.098  1.00 11.23           C  
ATOM   1606  OG  SER A 210      33.477  26.404  14.911  1.00 19.71           O  
ATOM   1607  N   ASP A 211      29.926  26.157  17.650  1.00 10.84           N  
ATOM   1608  CA  ASP A 211      29.157  25.934  18.876  1.00 10.22           C  
ATOM   1609  C   ASP A 211      28.022  24.948  18.603  1.00 10.59           C  
ATOM   1610  O   ASP A 211      27.784  24.026  19.389  1.00 10.04           O  
ATOM   1611  CB  ASP A 211      28.604  27.272  19.386  1.00 10.60           C  
ATOM   1612  CG  ASP A 211      27.738  27.124  20.627  1.00 12.42           C  
ATOM   1613  OD1 ASP A 211      28.267  26.774  21.707  1.00 16.83           O  
ATOM   1614  OD2 ASP A 211      26.522  27.359  20.511  1.00 12.48           O  
ATOM   1615  N   ALA A 212      27.318  25.138  17.487  1.00  9.54           N  
ATOM   1616  CA  ALA A 212      26.227  24.235  17.106  1.00  8.27           C  
ATOM   1617  C   ALA A 212      26.738  22.889  16.567  1.00  8.25           C  
ATOM   1618  O   ALA A 212      26.202  21.841  16.887  1.00  8.55           O  
ATOM   1619  CB  ALA A 212      25.328  24.896  16.088  1.00  8.48           C  
ATOM   1620  N   ASN A 213      27.814  22.921  15.793  1.00  9.00           N  
ATOM   1621  CA  ASN A 213      28.385  21.703  15.220  1.00 10.30           C  
ATOM   1622  C   ASN A 213      28.871  20.712  16.284  1.00 10.91           C  
ATOM   1623  O   ASN A 213      28.775  19.494  16.111  1.00 11.33           O  
ATOM   1624  CB  ASN A 213      29.527  22.042  14.238  1.00  9.78           C  
ATOM   1625  CG  ASN A 213      30.343  20.816  13.846  1.00 11.07           C  
ATOM   1626  OD1 ASN A 213      31.306  20.470  14.528  1.00 11.51           O  
ATOM   1627  ND2 ASN A 213      29.968  20.160  12.751  1.00 10.79           N  
ATOM   1628  N   ALA A 214      29.355  21.219  17.405  1.00 10.36           N  
ATOM   1629  CA  ALA A 214      29.844  20.347  18.468  1.00 10.06           C  
ATOM   1630  C   ALA A 214      28.729  19.455  19.016  1.00 10.24           C  
ATOM   1631  O   ALA A 214      28.983  18.327  19.440  1.00 11.61           O  
ATOM   1632  CB  ALA A 214      30.469  21.182  19.595  1.00  9.30           C  
ATOM   1633  N   LEU A 215      27.494  19.943  18.987  1.00  8.61           N  
ATOM   1634  CA  LEU A 215      26.361  19.180  19.496  1.00  9.80           C  
ATOM   1635  C   LEU A 215      26.019  17.971  18.638  1.00 11.32           C  
ATOM   1636  O   LEU A 215      25.284  17.092  19.075  1.00 10.69           O  
ATOM   1637  CB  LEU A 215      25.129  20.072  19.628  1.00 10.96           C  
ATOM   1638  CG  LEU A 215      25.312  21.268  20.559  1.00 13.79           C  
ATOM   1639  CD1 LEU A 215      24.126  22.188  20.400  1.00 11.84           C  
ATOM   1640  CD2 LEU A 215      25.467  20.795  21.993  1.00 13.48           C  
ATOM   1641  N   VAL A 216      26.526  17.924  17.411  1.00 10.18           N  
ATOM   1642  CA  VAL A 216      26.235  16.786  16.545  1.00  9.86           C  
ATOM   1643  C   VAL A 216      26.838  15.534  17.168  1.00 10.79           C  
ATOM   1644  O   VAL A 216      26.185  14.488  17.284  1.00 11.02           O  
ATOM   1645  CB  VAL A 216      26.802  16.998  15.129  1.00 11.76           C  
ATOM   1646  CG1 VAL A 216      26.692  15.708  14.309  1.00 10.56           C  
ATOM   1647  CG2 VAL A 216      26.042  18.140  14.448  1.00 13.24           C  
ATOM   1648  N   CYS A 217      28.062  15.680  17.651  1.00 12.35           N  
ATOM   1649  CA  CYS A 217      28.786  14.578  18.273  1.00 13.59           C  
ATOM   1650  C   CYS A 217      28.326  14.176  19.669  1.00 14.56           C  
ATOM   1651  O   CYS A 217      28.394  13.001  20.024  1.00 15.73           O  
ATOM   1652  CB  CYS A 217      30.276  14.901  18.331  1.00 13.69           C  
ATOM   1653  SG  CYS A 217      31.168  14.733  16.762  1.00 13.96           S  
ATOM   1654  N   THR A 218      27.855  15.132  20.459  1.00 14.11           N  
ATOM   1655  CA  THR A 218      27.456  14.822  21.823  1.00 14.15           C  
ATOM   1656  C   THR A 218      25.986  14.623  22.052  1.00 14.16           C  
ATOM   1657  O   THR A 218      25.605  13.870  22.949  1.00 15.04           O  
ATOM   1658  CB  THR A 218      27.937  15.902  22.816  1.00 13.06           C  
ATOM   1659  OG1 THR A 218      27.428  17.176  22.424  1.00 15.03           O  
ATOM   1660  CG2 THR A 218      29.443  15.966  22.846  1.00 14.50           C  
ATOM   1661  N   VAL A 219      25.152  15.252  21.230  1.00 11.16           N  
ATOM   1662  CA  VAL A 219      23.713  15.157  21.434  1.00 11.38           C  
ATOM   1663  C   VAL A 219      22.885  14.631  20.265  1.00 11.29           C  
ATOM   1664  O   VAL A 219      21.956  13.843  20.453  1.00 11.22           O  
ATOM   1665  CB  VAL A 219      23.142  16.543  21.860  1.00 12.02           C  
ATOM   1666  CG1 VAL A 219      21.634  16.492  22.010  1.00  9.60           C  
ATOM   1667  CG2 VAL A 219      23.789  16.994  23.154  1.00 13.15           C  
ATOM   1668  N   VAL A 220      23.214  15.051  19.049  1.00 11.48           N  
ATOM   1669  CA  VAL A 220      22.402  14.629  17.908  1.00  9.67           C  
ATOM   1670  C   VAL A 220      22.535  13.156  17.526  1.00  8.25           C  
ATOM   1671  O   VAL A 220      21.531  12.470  17.362  1.00  8.29           O  
ATOM   1672  CB  VAL A 220      22.657  15.525  16.674  1.00  9.93           C  
ATOM   1673  CG1 VAL A 220      21.684  15.153  15.538  1.00  8.24           C  
ATOM   1674  CG2 VAL A 220      22.507  16.979  17.063  1.00  8.75           C  
ATOM   1675  N   MET A 221      23.759  12.684  17.368  1.00  8.38           N  
ATOM   1676  CA  MET A 221      23.976  11.292  17.005  1.00 11.64           C  
ATOM   1677  C   MET A 221      25.246  10.801  17.697  1.00 11.43           C  
ATOM   1678  O   MET A 221      26.196  10.339  17.045  1.00 11.47           O  
ATOM   1679  CB  MET A 221      24.057  11.143  15.475  1.00 11.50           C  
ATOM   1680  CG  MET A 221      25.113  12.021  14.823  1.00 16.14           C  
ATOM   1681  SD  MET A 221      25.207  11.872  13.006  1.00 20.97           S  
ATOM   1682  CE  MET A 221      26.315  10.434  12.865  1.00 19.97           C  
ATOM   1683  N   PRO A 222      25.249  10.837  19.051  1.00 11.75           N  
ATOM   1684  CA  PRO A 222      26.390  10.408  19.872  1.00 12.77           C  
ATOM   1685  C   PRO A 222      26.809   8.947  19.697  1.00 13.35           C  
ATOM   1686  O   PRO A 222      27.920   8.571  20.064  1.00 15.25           O  
ATOM   1687  CB  PRO A 222      25.910  10.678  21.300  1.00 10.91           C  
ATOM   1688  CG  PRO A 222      24.419  10.547  21.206  1.00  8.92           C  
ATOM   1689  CD  PRO A 222      24.108  11.235  19.903  1.00 11.25           C  
ATOM   1690  N   HIS A 223      25.923   8.109  19.175  1.00 12.74           N  
ATOM   1691  CA  HIS A 223      26.267   6.706  18.994  1.00 13.63           C  
ATOM   1692  C   HIS A 223      26.094   6.209  17.551  1.00 14.96           C  
ATOM   1693  O   HIS A 223      25.961   4.998  17.320  1.00 14.29           O  
ATOM   1694  CB  HIS A 223      25.468   5.845  19.989  1.00 13.89           C  
ATOM   1695  CG  HIS A 223      25.630   6.279  21.430  1.00 13.19           C  
ATOM   1696  ND1 HIS A 223      26.801   6.101  22.135  1.00 11.44           N  
ATOM   1697  CD2 HIS A 223      24.797   6.960  22.245  1.00 12.49           C  
ATOM   1698  CE1 HIS A 223      26.689   6.669  23.325  1.00 10.65           C  
ATOM   1699  NE2 HIS A 223      25.477   7.200  23.421  1.00 12.75           N  
ATOM   1700  N   GLY A 224      26.241   7.126  16.595  1.00 14.25           N  
ATOM   1701  CA  GLY A 224      26.087   6.771  15.194  1.00 14.00           C  
ATOM   1702  C   GLY A 224      24.636   6.797  14.762  1.00 13.80           C  
ATOM   1703  O   GLY A 224      23.755   6.834  15.602  1.00 14.48           O  
ATOM   1704  N   ALA A 225      24.372   6.761  13.457  1.00 14.75           N  
ATOM   1705  CA  ALA A 225      23.003   6.809  12.957  1.00 15.10           C  
ATOM   1706  C   ALA A 225      22.227   5.508  13.064  1.00 15.00           C  
ATOM   1707  O   ALA A 225      21.017   5.528  13.258  1.00 15.55           O  
ATOM   1708  CB  ALA A 225      22.985   7.303  11.543  1.00 15.79           C  
ATOM   1709  N   ALA A 226      22.909   4.376  12.932  1.00 15.38           N  
ATOM   1710  CA  ALA A 226      22.230   3.085  13.032  1.00 16.34           C  
ATOM   1711  C   ALA A 226      21.469   2.966  14.352  1.00 16.39           C  
ATOM   1712  O   ALA A 226      20.365   2.413  14.387  1.00 16.75           O  
ATOM   1713  CB  ALA A 226      23.221   1.930  12.871  1.00 17.28           C  
ATOM   1714  N   ALA A 227      22.009   3.558  15.416  1.00 16.99           N  
ATOM   1715  CA  ALA A 227      21.349   3.535  16.728  1.00 16.89           C  
ATOM   1716  C   ALA A 227      20.008   4.283  16.731  1.00 18.21           C  
ATOM   1717  O   ALA A 227      19.124   3.973  17.535  1.00 19.37           O  
ATOM   1718  CB  ALA A 227      22.267   4.114  17.788  1.00 16.44           C  
ATOM   1719  N   LEU A 228      19.820   5.207  15.783  1.00 18.71           N  
ATOM   1720  CA  LEU A 228      18.588   5.994  15.697  1.00 18.27           C  
ATOM   1721  C   LEU A 228      17.499   5.443  14.764  1.00 20.27           C  
ATOM   1722  O   LEU A 228      16.348   5.878  14.819  1.00 19.35           O  
ATOM   1723  CB  LEU A 228      18.937   7.411  15.245  1.00 17.62           C  
ATOM   1724  CG  LEU A 228      19.891   8.187  16.145  1.00 17.65           C  
ATOM   1725  CD1 LEU A 228      20.308   9.471  15.469  1.00 18.26           C  
ATOM   1726  CD2 LEU A 228      19.198   8.464  17.447  1.00 16.79           C  
ATOM   1727  N   GLN A 229      17.865   4.508  13.896  1.00 22.57           N  
ATOM   1728  CA  GLN A 229      16.925   3.961  12.939  1.00 25.08           C  
ATOM   1729  C   GLN A 229      16.374   2.642  13.403  1.00 27.87           C  
ATOM   1730  O   GLN A 229      16.050   1.780  12.573  1.00 31.48           O  
ATOM   1731  CB  GLN A 229      17.629   3.752  11.603  1.00 25.00           C  
ATOM   1732  CG  GLN A 229      18.376   4.948  11.127  1.00 25.19           C  
ATOM   1733  CD  GLN A 229      18.939   4.736   9.752  1.00 24.13           C  
ATOM   1734  OE1 GLN A 229      20.103   4.398   9.601  1.00 25.49           O  
ATOM   1735  NE2 GLN A 229      18.108   4.911   8.735  1.00 25.01           N  
ATOM   1736  N   THR A 230      16.154   2.485  14.699  1.00 29.65           N  
ATOM   1737  CA  THR A 230      15.693   1.211  15.099  1.00 32.20           C  
ATOM   1738  C   THR A 230      14.513   1.111  16.045  1.00 32.00           C  
ATOM   1739  O   THR A 230      13.938   0.013  16.213  1.00 34.96           O  
ATOM   1740  CB  THR A 230      16.900   0.321  15.385  1.00 33.57           C  
ATOM   1741  OG1 THR A 230      16.627  -0.988  14.902  1.00 37.01           O  
ATOM   1742  CG2 THR A 230      17.244   0.327  16.817  1.00 32.90           C  
ATOM   1743  N   GLY A 231      14.093   2.218  16.645  1.00 30.39           N  
ATOM   1744  CA  GLY A 231      12.946   2.088  17.486  1.00 28.80           C  
ATOM   1745  C   GLY A 231      12.270   3.374  17.204  1.00 26.53           C  
ATOM   1746  O   GLY A 231      12.663   4.079  16.288  1.00 29.88           O  
ATOM   1747  N   ASP A 232      11.262   3.685  17.986  1.00 21.83           N  
ATOM   1748  CA  ASP A 232      10.625   4.964  17.834  1.00 19.88           C  
ATOM   1749  C   ASP A 232      11.514   5.909  18.659  1.00 19.28           C  
ATOM   1750  O   ASP A 232      12.035   5.520  19.703  1.00 17.61           O  
ATOM   1751  CB  ASP A 232       9.217   4.911  18.391  1.00 19.94           C  
ATOM   1752  CG  ASP A 232       8.393   6.130  18.019  1.00 20.58           C  
ATOM   1753  OD1 ASP A 232       8.879   7.249  18.228  1.00 19.83           O  
ATOM   1754  OD2 ASP A 232       7.252   5.977  17.537  1.00 20.11           O  
ATOM   1755  N   LEU A 233      11.725   7.129  18.180  1.00 16.40           N  
ATOM   1756  CA  LEU A 233      12.576   8.066  18.889  1.00 16.09           C  
ATOM   1757  C   LEU A 233      11.898   8.677  20.101  1.00 17.18           C  
ATOM   1758  O   LEU A 233      12.548   9.304  20.947  1.00 18.29           O  
ATOM   1759  CB  LEU A 233      13.085   9.156  17.947  1.00 16.48           C  
ATOM   1760  CG  LEU A 233      14.074   8.674  16.890  1.00 15.27           C  
ATOM   1761  CD1 LEU A 233      14.536   9.879  16.091  1.00 17.44           C  
ATOM   1762  CD2 LEU A 233      15.252   7.962  17.521  1.00 16.83           C  
ATOM   1763  N   TYR A 234      10.586   8.541  20.172  1.00 16.46           N  
ATOM   1764  CA  TYR A 234       9.843   9.069  21.309  1.00 18.28           C  
ATOM   1765  C   TYR A 234       9.629   7.887  22.267  1.00 18.48           C  
ATOM   1766  O   TYR A 234       9.181   6.829  21.842  1.00 17.21           O  
ATOM   1767  CB  TYR A 234       8.533   9.674  20.848  1.00 18.65           C  
ATOM   1768  CG  TYR A 234       7.757  10.335  21.955  1.00 21.83           C  
ATOM   1769  CD1 TYR A 234       8.162  11.561  22.480  1.00 22.54           C  
ATOM   1770  CD2 TYR A 234       6.619   9.734  22.481  1.00 22.76           C  
ATOM   1771  CE1 TYR A 234       7.443  12.181  23.497  1.00 25.37           C  
ATOM   1772  CE2 TYR A 234       5.892  10.338  23.498  1.00 25.59           C  
ATOM   1773  CZ  TYR A 234       6.304  11.562  24.007  1.00 26.89           C  
ATOM   1774  OH  TYR A 234       5.555  12.175  24.999  1.00 29.24           O  
ATOM   1775  N   PRO A 235       9.773   8.106  23.588  1.00 19.08           N  
ATOM   1776  CA  PRO A 235      10.213   9.338  24.247  1.00 16.79           C  
ATOM   1777  C   PRO A 235      11.659   9.404  24.646  1.00 15.48           C  
ATOM   1778  O   PRO A 235      12.128  10.462  25.028  1.00 16.47           O  
ATOM   1779  CB  PRO A 235       9.342   9.313  25.502  1.00 19.33           C  
ATOM   1780  CG  PRO A 235       9.503   7.863  25.918  1.00 20.91           C  
ATOM   1781  CD  PRO A 235       9.318   7.120  24.582  1.00 21.01           C  
ATOM   1782  N   THR A 236      12.383   8.297  24.551  1.00 13.57           N  
ATOM   1783  CA  THR A 236      13.778   8.275  24.987  1.00 15.09           C  
ATOM   1784  C   THR A 236      14.767   9.221  24.312  1.00 15.06           C  
ATOM   1785  O   THR A 236      15.516   9.931  24.995  1.00 14.68           O  
ATOM   1786  CB  THR A 236      14.310   6.841  25.009  1.00 15.14           C  
ATOM   1787  OG1 THR A 236      13.407   6.037  25.776  1.00 18.87           O  
ATOM   1788  CG2 THR A 236      15.695   6.774  25.657  1.00 16.10           C  
ATOM   1789  N   TYR A 237      14.815   9.204  22.982  1.00 13.13           N  
ATOM   1790  CA  TYR A 237      15.714  10.106  22.254  1.00 13.22           C  
ATOM   1791  C   TYR A 237      15.209  11.548  22.435  1.00 12.21           C  
ATOM   1792  O   TYR A 237      15.991  12.460  22.685  1.00 14.39           O  
ATOM   1793  CB  TYR A 237      15.756   9.745  20.767  1.00 10.79           C  
ATOM   1794  CG  TYR A 237      16.607  10.680  19.942  1.00 10.25           C  
ATOM   1795  CD1 TYR A 237      17.992  10.570  19.936  1.00  9.23           C  
ATOM   1796  CD2 TYR A 237      16.019  11.681  19.162  1.00 10.26           C  
ATOM   1797  CE1 TYR A 237      18.784  11.447  19.174  1.00 10.46           C  
ATOM   1798  CE2 TYR A 237      16.799  12.557  18.405  1.00  8.67           C  
ATOM   1799  CZ  TYR A 237      18.167  12.432  18.409  1.00  9.82           C  
ATOM   1800  OH  TYR A 237      18.909  13.290  17.632  1.00  9.99           O  
ATOM   1801  N   TYR A 238      13.895  11.725  22.337  1.00 14.42           N  
ATOM   1802  CA  TYR A 238      13.227  13.019  22.506  1.00 13.64           C  
ATOM   1803  C   TYR A 238      13.613  13.651  23.832  1.00 15.07           C  
ATOM   1804  O   TYR A 238      14.025  14.817  23.908  1.00 14.31           O  
ATOM   1805  CB  TYR A 238      11.714  12.808  22.466  1.00 14.82           C  
ATOM   1806  CG  TYR A 238      10.884  14.039  22.747  1.00 16.99           C  
ATOM   1807  CD1 TYR A 238      10.786  15.073  21.808  1.00 16.24           C  
ATOM   1808  CD2 TYR A 238      10.202  14.184  23.956  1.00 19.44           C  
ATOM   1809  CE1 TYR A 238      10.022  16.211  22.059  1.00 15.23           C  
ATOM   1810  CE2 TYR A 238       9.434  15.324  24.215  1.00 18.98           C  
ATOM   1811  CZ  TYR A 238       9.360  16.331  23.265  1.00 18.72           C  
ATOM   1812  OH  TYR A 238       8.612  17.447  23.531  1.00 19.32           O  
ATOM   1813  N   ASP A 239      13.503  12.868  24.891  1.00 16.44           N  
ATOM   1814  CA  ASP A 239      13.842  13.365  26.219  1.00 17.19           C  
ATOM   1815  C   ASP A 239      15.293  13.812  26.335  1.00 16.49           C  
ATOM   1816  O   ASP A 239      15.585  14.800  27.005  1.00 19.95           O  
ATOM   1817  CB  ASP A 239      13.528  12.310  27.291  1.00 18.11           C  
ATOM   1818  CG  ASP A 239      12.044  12.135  27.516  1.00 21.04           C  
ATOM   1819  OD1 ASP A 239      11.249  13.003  27.109  1.00 24.41           O  
ATOM   1820  OD2 ASP A 239      11.654  11.127  28.121  1.00 23.20           O  
ATOM   1821  N   SER A 240      16.202  13.121  25.661  1.00 14.62           N  
ATOM   1822  CA  SER A 240      17.614  13.477  25.741  1.00 14.98           C  
ATOM   1823  C   SER A 240      18.021  14.689  24.910  1.00 13.68           C  
ATOM   1824  O   SER A 240      19.133  15.176  25.067  1.00 14.20           O  
ATOM   1825  CB  SER A 240      18.494  12.293  25.324  1.00 16.42           C  
ATOM   1826  OG  SER A 240      18.555  12.193  23.908  1.00 20.26           O  
ATOM   1827  N   VAL A 241      17.148  15.173  24.025  1.00 12.08           N  
ATOM   1828  CA  VAL A 241      17.512  16.311  23.168  1.00 11.32           C  
ATOM   1829  C   VAL A 241      16.666  17.574  23.281  1.00 11.84           C  
ATOM   1830  O   VAL A 241      17.108  18.659  22.906  1.00 11.23           O  
ATOM   1831  CB  VAL A 241      17.533  15.926  21.653  1.00 11.46           C  
ATOM   1832  CG1 VAL A 241      18.420  14.718  21.405  1.00 11.03           C  
ATOM   1833  CG2 VAL A 241      16.113  15.705  21.116  1.00 11.81           C  
ATOM   1834  N   ILE A 242      15.471  17.457  23.833  1.00 12.21           N  
ATOM   1835  CA  ILE A 242      14.579  18.596  23.922  1.00 13.64           C  
ATOM   1836  C   ILE A 242      15.131  19.816  24.673  1.00 13.92           C  
ATOM   1837  O   ILE A 242      14.841  20.957  24.299  1.00 13.96           O  
ATOM   1838  CB  ILE A 242      13.197  18.145  24.438  1.00 14.40           C  
ATOM   1839  CG1 ILE A 242      12.146  19.191  24.098  1.00 16.16           C  
ATOM   1840  CG2 ILE A 242      13.259  17.772  25.930  1.00 17.96           C  
ATOM   1841  CD1 ILE A 242      11.955  19.366  22.580  1.00 17.80           C  
ATOM   1842  N   ASP A 243      15.997  19.589  25.661  1.00 13.16           N  
ATOM   1843  CA  ASP A 243      16.595  20.687  26.428  1.00 15.12           C  
ATOM   1844  C   ASP A 243      17.583  21.452  25.565  1.00 13.93           C  
ATOM   1845  O   ASP A 243      17.743  22.670  25.707  1.00 13.27           O  
ATOM   1846  CB  ASP A 243      17.321  20.172  27.672  1.00 18.14           C  
ATOM   1847  CG  ASP A 243      16.408  20.062  28.886  1.00 23.75           C  
ATOM   1848  OD1 ASP A 243      15.177  20.293  28.776  1.00 25.33           O  
ATOM   1849  OD2 ASP A 243      16.942  19.749  29.972  1.00 29.92           O  
ATOM   1850  N   THR A 244      18.255  20.725  24.678  1.00 11.41           N  
ATOM   1851  CA  THR A 244      19.215  21.326  23.753  1.00 11.01           C  
ATOM   1852  C   THR A 244      18.483  22.175  22.705  1.00 10.64           C  
ATOM   1853  O   THR A 244      18.959  23.247  22.335  1.00 12.59           O  
ATOM   1854  CB  THR A 244      20.068  20.251  23.049  1.00 10.93           C  
ATOM   1855  OG1 THR A 244      20.908  19.616  24.011  1.00 13.63           O  
ATOM   1856  CG2 THR A 244      20.954  20.855  21.982  1.00 10.25           C  
ATOM   1857  N   ILE A 245      17.319  21.720  22.251  1.00 10.64           N  
ATOM   1858  CA  ILE A 245      16.548  22.477  21.261  1.00 10.88           C  
ATOM   1859  C   ILE A 245      16.135  23.825  21.850  1.00 11.73           C  
ATOM   1860  O   ILE A 245      16.277  24.857  21.203  1.00 10.11           O  
ATOM   1861  CB  ILE A 245      15.304  21.700  20.737  1.00 12.04           C  
ATOM   1862  CG1 ILE A 245      15.758  20.543  19.837  1.00 14.36           C  
ATOM   1863  CG2 ILE A 245      14.379  22.634  19.940  1.00 12.07           C  
ATOM   1864  CD1 ILE A 245      14.628  19.587  19.385  1.00 15.12           C  
ATOM   1865  N   GLU A 246      15.655  23.830  23.089  1.00 11.16           N  
ATOM   1866  CA  GLU A 246      15.254  25.095  23.708  1.00 11.96           C  
ATOM   1867  C   GLU A 246      16.446  26.013  23.867  1.00 10.06           C  
ATOM   1868  O   GLU A 246      16.370  27.181  23.538  1.00 12.95           O  
ATOM   1869  CB  GLU A 246      14.586  24.856  25.048  1.00 15.12           C  
ATOM   1870  CG  GLU A 246      13.320  24.036  24.910  1.00 19.79           C  
ATOM   1871  CD  GLU A 246      12.442  24.105  26.129  1.00 25.97           C  
ATOM   1872  OE1 GLU A 246      11.612  25.047  26.204  1.00 27.85           O  
ATOM   1873  OE2 GLU A 246      12.570  23.208  26.992  1.00 27.97           O  
ATOM   1874  N   LEU A 247      17.568  25.452  24.297  1.00  9.10           N  
ATOM   1875  CA  LEU A 247      18.803  26.190  24.467  1.00  9.00           C  
ATOM   1876  C   LEU A 247      19.271  26.834  23.139  1.00  9.68           C  
ATOM   1877  O   LEU A 247      19.681  27.994  23.113  1.00  7.97           O  
ATOM   1878  CB  LEU A 247      19.892  25.258  25.002  1.00  9.96           C  
ATOM   1879  CG  LEU A 247      21.282  25.885  25.081  1.00 11.42           C  
ATOM   1880  CD1 LEU A 247      21.269  27.000  26.108  1.00 13.33           C  
ATOM   1881  CD2 LEU A 247      22.343  24.842  25.419  1.00 13.61           C  
ATOM   1882  N   GLN A 248      19.173  26.101  22.032  1.00  9.91           N  
ATOM   1883  CA  GLN A 248      19.613  26.623  20.734  1.00  8.47           C  
ATOM   1884  C   GLN A 248      18.690  27.718  20.182  1.00  7.46           C  
ATOM   1885  O   GLN A 248      19.143  28.639  19.526  1.00  7.46           O  
ATOM   1886  CB  GLN A 248      19.784  25.473  19.724  1.00  9.46           C  
ATOM   1887  CG  GLN A 248      20.945  24.513  20.030  1.00  7.37           C  
ATOM   1888  CD  GLN A 248      22.284  25.213  20.183  1.00 10.47           C  
ATOM   1889  OE1 GLN A 248      22.784  25.329  21.285  1.00 11.41           O  
ATOM   1890  NE2 GLN A 248      22.900  25.633  19.072  1.00  9.59           N  
ATOM   1891  N   ILE A 249      17.397  27.604  20.440  1.00  7.97           N  
ATOM   1892  CA  ILE A 249      16.431  28.607  20.004  1.00 10.81           C  
ATOM   1893  C   ILE A 249      16.718  29.892  20.801  1.00 11.14           C  
ATOM   1894  O   ILE A 249      16.699  30.996  20.234  1.00 12.71           O  
ATOM   1895  CB  ILE A 249      14.974  28.151  20.289  1.00 10.99           C  
ATOM   1896  CG1 ILE A 249      14.607  26.955  19.411  1.00 13.98           C  
ATOM   1897  CG2 ILE A 249      13.979  29.280  20.052  1.00 10.18           C  
ATOM   1898  CD1 ILE A 249      14.627  27.240  17.958  1.00 11.93           C  
ATOM   1899  N   ALA A 250      17.004  29.749  22.102  1.00 10.29           N  
ATOM   1900  CA  ALA A 250      17.293  30.903  22.953  1.00 10.23           C  
ATOM   1901  C   ALA A 250      18.580  31.623  22.523  1.00  9.98           C  
ATOM   1902  O   ALA A 250      18.628  32.863  22.487  1.00 11.69           O  
ATOM   1903  CB  ALA A 250      17.364  30.481  24.432  1.00 11.04           C  
ATOM   1904  N   LYS A 251      19.614  30.864  22.176  1.00  9.21           N  
ATOM   1905  CA  LYS A 251      20.869  31.462  21.723  1.00 11.08           C  
ATOM   1906  C   LYS A 251      20.653  32.280  20.442  1.00 12.09           C  
ATOM   1907  O   LYS A 251      21.201  33.380  20.307  1.00 12.50           O  
ATOM   1908  CB  LYS A 251      21.921  30.397  21.411  1.00 12.35           C  
ATOM   1909  CG  LYS A 251      22.577  29.704  22.591  1.00 12.70           C  
ATOM   1910  CD  LYS A 251      23.534  28.638  22.076  1.00 12.52           C  
ATOM   1911  CE  LYS A 251      24.230  27.923  23.206  1.00 12.03           C  
ATOM   1912  NZ  LYS A 251      24.997  26.723  22.749  1.00 11.84           N  
ATOM   1913  N   GLY A 252      19.897  31.716  19.490  1.00 11.00           N  
ATOM   1914  CA  GLY A 252      19.626  32.391  18.228  1.00 10.74           C  
ATOM   1915  C   GLY A 252      18.968  33.728  18.458  1.00 11.63           C  
ATOM   1916  O   GLY A 252      19.407  34.741  17.914  1.00 12.37           O  
ATOM   1917  N   GLY A 253      17.934  33.723  19.305  1.00 10.16           N  
ATOM   1918  CA  GLY A 253      17.211  34.936  19.639  1.00 10.27           C  
ATOM   1919  C   GLY A 253      18.088  35.991  20.293  1.00 10.71           C  
ATOM   1920  O   GLY A 253      18.078  37.155  19.886  1.00 12.39           O  
ATOM   1921  N   TYR A 254      18.885  35.586  21.276  1.00 10.29           N  
ATOM   1922  CA  TYR A 254      19.756  36.514  21.993  1.00 10.40           C  
ATOM   1923  C   TYR A 254      20.849  37.091  21.081  1.00 11.79           C  
ATOM   1924  O   TYR A 254      21.185  38.296  21.161  1.00 12.06           O  
ATOM   1925  CB  TYR A 254      20.386  35.792  23.172  1.00 10.58           C  
ATOM   1926  CG  TYR A 254      20.801  36.704  24.280  1.00  8.46           C  
ATOM   1927  CD1 TYR A 254      19.846  37.391  25.020  1.00 12.18           C  
ATOM   1928  CD2 TYR A 254      22.136  36.844  24.621  1.00  8.57           C  
ATOM   1929  CE1 TYR A 254      20.208  38.206  26.080  1.00 13.78           C  
ATOM   1930  CE2 TYR A 254      22.518  37.655  25.686  1.00 11.96           C  
ATOM   1931  CZ  TYR A 254      21.542  38.326  26.410  1.00 14.27           C  
ATOM   1932  OH  TYR A 254      21.898  39.123  27.472  1.00 20.15           O  
ATOM   1933  N   ARG A 255      21.416  36.242  20.222  1.00 10.21           N  
ATOM   1934  CA  ARG A 255      22.461  36.687  19.293  1.00 10.55           C  
ATOM   1935  C   ARG A 255      21.919  37.652  18.239  1.00 10.59           C  
ATOM   1936  O   ARG A 255      22.620  38.590  17.846  1.00 10.41           O  
ATOM   1937  CB  ARG A 255      23.115  35.492  18.601  1.00  9.46           C  
ATOM   1938  CG  ARG A 255      24.078  34.706  19.474  1.00  8.47           C  
ATOM   1939  CD  ARG A 255      24.429  33.415  18.769  1.00  9.76           C  
ATOM   1940  NE  ARG A 255      25.350  32.597  19.552  1.00  9.06           N  
ATOM   1941  CZ  ARG A 255      25.539  31.297  19.355  1.00 10.51           C  
ATOM   1942  NH1 ARG A 255      24.854  30.655  18.408  1.00  9.55           N  
ATOM   1943  NH2 ARG A 255      26.391  30.635  20.121  1.00 10.23           N  
ATOM   1944  N   LEU A 256      20.692  37.407  17.769  1.00  9.11           N  
ATOM   1945  CA  LEU A 256      20.066  38.272  16.765  1.00  9.61           C  
ATOM   1946  C   LEU A 256      19.832  39.665  17.363  1.00 11.61           C  
ATOM   1947  O   LEU A 256      20.122  40.688  16.715  1.00 10.11           O  
ATOM   1948  CB  LEU A 256      18.742  37.677  16.249  1.00  9.79           C  
ATOM   1949  CG  LEU A 256      17.889  38.480  15.242  1.00 11.20           C  
ATOM   1950  CD1 LEU A 256      18.653  38.828  13.941  1.00 11.65           C  
ATOM   1951  CD2 LEU A 256      16.660  37.693  14.901  1.00 10.38           C  
ATOM   1952  N   ALA A 257      19.316  39.711  18.593  1.00 12.15           N  
ATOM   1953  CA  ALA A 257      19.085  40.985  19.277  1.00 12.21           C  
ATOM   1954  C   ALA A 257      20.380  41.786  19.366  1.00 11.55           C  
ATOM   1955  O   ALA A 257      20.418  42.947  18.983  1.00 14.16           O  
ATOM   1956  CB  ALA A 257      18.519  40.754  20.665  1.00 10.19           C  
ATOM   1957  N   ASN A 258      21.457  41.163  19.837  1.00 12.98           N  
ATOM   1958  CA  ASN A 258      22.744  41.853  19.959  1.00 12.99           C  
ATOM   1959  C   ASN A 258      23.341  42.297  18.624  1.00 16.14           C  
ATOM   1960  O   ASN A 258      24.035  43.314  18.548  1.00 16.38           O  
ATOM   1961  CB  ASN A 258      23.780  40.987  20.709  1.00 13.23           C  
ATOM   1962  CG  ASN A 258      25.159  41.642  20.767  1.00 13.09           C  
ATOM   1963  OD1 ASN A 258      26.114  41.200  20.121  1.00 16.57           O  
ATOM   1964  ND2 ASN A 258      25.261  42.717  21.528  1.00 15.35           N  
ATOM   1965  N   TRP A 259      23.100  41.525  17.574  1.00 15.14           N  
ATOM   1966  CA  TRP A 259      23.635  41.861  16.262  1.00 15.26           C  
ATOM   1967  C   TRP A 259      22.973  43.134  15.762  1.00 14.52           C  
ATOM   1968  O   TRP A 259      23.652  44.050  15.310  1.00 15.63           O  
ATOM   1969  CB  TRP A 259      23.374  40.710  15.294  1.00 14.78           C  
ATOM   1970  CG  TRP A 259      24.252  40.726  14.112  1.00 15.75           C  
ATOM   1971  CD1 TRP A 259      23.863  40.896  12.817  1.00 14.33           C  
ATOM   1972  CD2 TRP A 259      25.659  40.466  14.080  1.00 14.98           C  
ATOM   1973  NE1 TRP A 259      24.935  40.744  11.983  1.00 13.66           N  
ATOM   1974  CE2 TRP A 259      26.055  40.474  12.731  1.00 14.29           C  
ATOM   1975  CE3 TRP A 259      26.627  40.213  15.067  1.00 16.17           C  
ATOM   1976  CZ2 TRP A 259      27.367  40.237  12.324  1.00 17.24           C  
ATOM   1977  CZ3 TRP A 259      27.942  39.974  14.666  1.00 19.69           C  
ATOM   1978  CH2 TRP A 259      28.297  39.987  13.299  1.00 18.71           C  
ATOM   1979  N   ILE A 260      21.653  43.196  15.868  1.00 13.28           N  
ATOM   1980  CA  ILE A 260      20.884  44.361  15.450  1.00 16.01           C  
ATOM   1981  C   ILE A 260      21.312  45.601  16.256  1.00 19.02           C  
ATOM   1982  O   ILE A 260      21.483  46.700  15.694  1.00 21.00           O  
ATOM   1983  CB  ILE A 260      19.367  44.121  15.642  1.00 16.22           C  
ATOM   1984  CG1 ILE A 260      18.848  43.093  14.630  1.00 17.92           C  
ATOM   1985  CG2 ILE A 260      18.574  45.414  15.505  1.00 16.29           C  
ATOM   1986  CD1 ILE A 260      17.390  42.708  14.855  1.00 17.68           C  
ATOM   1987  N   ASN A 261      21.502  45.429  17.562  1.00 18.56           N  
ATOM   1988  CA  ASN A 261      21.922  46.547  18.405  1.00 19.78           C  
ATOM   1989  C   ASN A 261      23.277  47.097  17.984  1.00 19.59           C  
ATOM   1990  O   ASN A 261      23.471  48.306  18.005  1.00 20.52           O  
ATOM   1991  CB  ASN A 261      21.959  46.167  19.896  1.00 18.29           C  
ATOM   1992  CG  ASN A 261      20.577  46.001  20.492  1.00 17.57           C  
ATOM   1993  OD1 ASN A 261      19.614  46.638  20.058  1.00 18.68           O  
ATOM   1994  ND2 ASN A 261      20.469  45.153  21.506  1.00 17.28           N  
ATOM   1995  N   GLU A 262      24.217  46.218  17.645  1.00 19.15           N  
ATOM   1996  CA  GLU A 262      25.546  46.654  17.214  1.00 21.03           C  
ATOM   1997  C   GLU A 262      25.522  47.396  15.880  1.00 22.82           C  
ATOM   1998  O   GLU A 262      26.304  48.319  15.662  1.00 22.36           O  
ATOM   1999  CB  GLU A 262      26.493  45.476  17.081  1.00 20.01           C  
ATOM   2000  CG  GLU A 262      26.953  44.898  18.396  1.00 24.50           C  
ATOM   2001  CD  GLU A 262      28.159  44.000  18.236  1.00 27.49           C  
ATOM   2002  OE1 GLU A 262      28.876  44.134  17.216  1.00 31.45           O  
ATOM   2003  OE2 GLU A 262      28.413  43.166  19.131  1.00 28.01           O  
ATOM   2004  N   ILE A 263      24.691  46.908  14.964  1.00 24.91           N  
ATOM   2005  CA  ILE A 263      24.538  47.493  13.639  1.00 26.92           C  
ATOM   2006  C   ILE A 263      23.942  48.875  13.774  1.00 28.94           C  
ATOM   2007  O   ILE A 263      24.344  49.792  13.068  1.00 28.77           O  
ATOM   2008  CB  ILE A 263      23.622  46.631  12.732  1.00 25.39           C  
ATOM   2009  CG1 ILE A 263      24.322  45.322  12.378  1.00 25.84           C  
ATOM   2010  CG2 ILE A 263      23.289  47.365  11.438  1.00 25.78           C  
ATOM   2011  CD1 ILE A 263      23.441  44.381  11.578  1.00 26.27           C  
ATOM   2012  N   HIS A 264      22.952  49.009  14.646  1.00 31.58           N  
ATOM   2013  CA  HIS A 264      22.339  50.305  14.847  1.00 35.02           C  
ATOM   2014  C   HIS A 264      23.259  51.295  15.552  1.00 34.68           C  
ATOM   2015  O   HIS A 264      23.199  52.477  15.195  1.00 37.19           O  
ATOM   2016  CB  HIS A 264      21.040  50.185  15.620  1.00 38.65           C  
ATOM   2017  CG  HIS A 264      20.308  51.469  15.702  1.00 44.67           C  
ATOM   2018  ND1 HIS A 264      19.849  52.015  16.904  1.00 47.32           N  
ATOM   2019  CD2 HIS A 264      19.986  52.378  14.757  1.00 46.93           C  
ATOM   2020  CE1 HIS A 264      19.299  53.176  16.671  1.00 48.65           C  
ATOM   2021  NE2 HIS A 264      19.365  53.428  15.372  1.00 49.16           N  
TER    2022      HIS A 264                                                      
HETATM 2023  C1  NAG B   1      24.955  39.189  -1.588  1.00 26.03           C  
HETATM 2024  C2  NAG B   1      25.166  38.012  -2.540  1.00 30.40           C  
HETATM 2025  C3  NAG B   1      24.649  38.350  -3.931  1.00 30.62           C  
HETATM 2026  C4  NAG B   1      23.185  38.693  -3.810  1.00 30.91           C  
HETATM 2027  C5  NAG B   1      23.046  39.898  -2.878  1.00 27.88           C  
HETATM 2028  C6  NAG B   1      21.608  40.344  -2.678  1.00 26.28           C  
HETATM 2029  C7  NAG B   1      27.075  36.724  -1.850  1.00 36.90           C  
HETATM 2030  C8  NAG B   1      28.567  36.531  -1.927  1.00 37.06           C  
HETATM 2031  N2  NAG B   1      26.584  37.720  -2.582  1.00 33.99           N  
HETATM 2032  O3  NAG B   1      24.817  37.244  -4.812  1.00 32.99           O  
HETATM 2033  O4  NAG B   1      22.689  39.017  -5.123  1.00 34.48           O  
HETATM 2034  O5  NAG B   1      23.582  39.590  -1.582  1.00 26.21           O  
HETATM 2035  O6  NAG B   1      20.767  39.263  -2.315  1.00 28.77           O  
HETATM 2036  O7  NAG B   1      26.372  35.910  -1.248  1.00 37.33           O  
HETATM 2037  C1  NAG B   2      21.961  38.063  -5.819  1.00 36.43           C  
HETATM 2038  C2  NAG B   2      21.208  38.763  -6.910  1.00 37.75           C  
HETATM 2039  C3  NAG B   2      20.464  37.726  -7.708  1.00 39.94           C  
HETATM 2040  C4  NAG B   2      21.468  36.756  -8.317  1.00 41.58           C  
HETATM 2041  C5  NAG B   2      22.221  36.093  -7.186  1.00 41.39           C  
HETATM 2042  C6  NAG B   2      23.284  35.109  -7.674  1.00 42.95           C  
HETATM 2043  C7  NAG B   2      20.587  41.010  -6.223  1.00 34.91           C  
HETATM 2044  C8  NAG B   2      19.504  41.898  -5.641  1.00 32.06           C  
HETATM 2045  N2  NAG B   2      20.278  39.717  -6.346  1.00 35.81           N  
HETATM 2046  O3  NAG B   2      19.721  38.375  -8.716  1.00 43.01           O  
HETATM 2047  O4  NAG B   2      20.796  35.784  -9.099  1.00 43.19           O  
HETATM 2048  O5  NAG B   2      22.873  37.119  -6.405  1.00 38.44           O  
HETATM 2049  O6  NAG B   2      24.412  35.779  -8.218  1.00 44.13           O  
HETATM 2050  O7  NAG B   2      21.695  41.491  -6.483  1.00 33.99           O  
HETATM 2051  C1  NAG A 285      35.332  45.143  17.496  1.00 46.55           C  
HETATM 2052  C2  NAG A 285      35.909  45.450  18.869  1.00 49.75           C  
HETATM 2053  C3  NAG A 285      36.291  46.915  18.899  1.00 51.81           C  
HETATM 2054  C4  NAG A 285      37.562  46.934  18.075  1.00 52.89           C  
HETATM 2055  C5  NAG A 285      37.331  46.346  16.635  1.00 52.83           C  
HETATM 2056  C6  NAG A 285      38.678  45.880  16.090  1.00 55.57           C  
HETATM 2057  C7  NAG A 285      33.881  45.297  20.224  1.00 49.72           C  
HETATM 2058  C8  NAG A 285      33.380  44.637  21.487  1.00 50.01           C  
HETATM 2059  N2  NAG A 285      35.148  44.993  20.016  1.00 50.02           N  
HETATM 2060  O3  NAG A 285      36.547  47.352  20.232  1.00 54.84           O  
HETATM 2061  O4  NAG A 285      38.107  48.257  18.012  1.00 54.60           O  
HETATM 2062  O5  NAG A 285      36.434  45.164  16.565  1.00 49.53           O  
HETATM 2063  O6  NAG A 285      38.685  45.851  14.669  1.00 60.28           O  
HETATM 2064  O7  NAG A 285      33.240  46.043  19.509  1.00 48.87           O  
HETATM 2065  C1  NAG A 287      15.260   3.334   6.174  1.00 46.93           C  
HETATM 2066  C2  NAG A 287      14.443   2.285   6.814  1.00 51.26           C  
HETATM 2067  C3  NAG A 287      14.763   0.918   6.422  1.00 54.12           C  
HETATM 2068  C4  NAG A 287      14.250   0.896   5.003  1.00 55.74           C  
HETATM 2069  C5  NAG A 287      14.926   1.962   4.123  1.00 55.35           C  
HETATM 2070  C6  NAG A 287      13.954   2.262   3.002  1.00 56.83           C  
HETATM 2071  C7  NAG A 287      13.201   2.608   8.691  1.00 54.40           C  
HETATM 2072  C8  NAG A 287      13.236   2.946  10.175  1.00 53.71           C  
HETATM 2073  N2  NAG A 287      14.382   2.466   8.225  1.00 52.47           N  
HETATM 2074  O3  NAG A 287      14.057  -0.016   7.236  1.00 55.10           O  
HETATM 2075  O4  NAG A 287      14.431  -0.390   4.425  1.00 58.00           O  
HETATM 2076  O5  NAG A 287      15.192   3.255   4.745  1.00 50.89           O  
HETATM 2077  O6  NAG A 287      12.722   2.778   3.506  1.00 60.13           O  
HETATM 2078  O7  NAG A 287      12.316   2.599   7.847  1.00 56.53           O  
HETATM 2079 ZN    ZN A 271      16.468  28.301   6.361  1.00 13.59          ZN  
HETATM 2080 ZN    ZN A 272      16.364  22.734   8.198  1.00 13.34          ZN  
HETATM 2081 ZN    ZN A 273      15.197  26.996   9.544  1.00 13.94          ZN  
HETATM 2082 ZN    ZN A 274      13.440  41.994  29.713  1.00 19.21          ZN  
HETATM 2083  O5' ADS A 292      18.688  18.950 -12.623  1.00 46.39           O  
HETATM 2084  C5' ADS A 292      19.875  19.656 -12.915  1.00 41.71           C  
HETATM 2085  C4' ADS A 292      20.027  20.526 -11.739  1.00 40.65           C  
HETATM 2086  O4' ADS A 292      21.368  20.667 -11.354  1.00 37.69           O  
HETATM 2087  C3' ADS A 292      19.363  21.849 -11.862  1.00 40.80           C  
HETATM 2088  O3' ADS A 292      19.028  22.147 -10.517  1.00 44.89           O  
HETATM 2089  C2' ADS A 292      20.511  22.714 -12.233  1.00 37.61           C  
HETATM 2090  C1' ADS A 292      21.670  22.040 -11.520  1.00 33.70           C  
HETATM 2091  N9  ADS A 292      22.897  22.247 -12.262  1.00 28.72           N  
HETATM 2092  C8  ADS A 292      23.134  22.247 -13.591  1.00 27.60           C  
HETATM 2093  N7  ADS A 292      24.326  22.631 -13.977  1.00 25.79           N  
HETATM 2094  C5  ADS A 292      24.948  22.897 -12.741  1.00 24.65           C  
HETATM 2095  C6  ADS A 292      26.240  23.352 -12.396  1.00 22.60           C  
HETATM 2096  N6  ADS A 292      27.158  23.621 -13.312  1.00 19.65           N  
HETATM 2097  N1  ADS A 292      26.497  23.548 -11.102  1.00 20.84           N  
HETATM 2098  C2  ADS A 292      25.565  23.285 -10.205  1.00 20.90           C  
HETATM 2099  N3  ADS A 292      24.342  22.860 -10.402  1.00 23.65           N  
HETATM 2100  C4  ADS A 292      24.086  22.668 -11.706  1.00 26.15           C  
HETATM 2101  P   THS A 293      17.579  22.071  -9.757  1.00 48.65           P  
HETATM 2102  S2P THS A 293      17.446  23.815  -8.952  1.00 46.44           S  
HETATM 2103  S3P THS A 293      16.223  21.383 -10.899  1.00 46.17           S  
HETATM 2104  O5' THS A 293      17.707  20.954  -8.705  1.00 50.70           O  
HETATM 2105  C5' THS A 293      18.948  21.023  -8.097  1.00 57.69           C  
HETATM 2106  C4' THS A 293      18.872  20.132  -6.916  1.00 61.56           C  
HETATM 2107  O4' THS A 293      18.744  18.842  -7.530  1.00 64.50           O  
HETATM 2108  C3' THS A 293      20.136  20.048  -6.035  1.00 63.58           C  
HETATM 2109  O3' THS A 293      19.705  19.283  -4.863  1.00 65.20           O  
HETATM 2110  C2' THS A 293      20.988  19.098  -6.887  1.00 65.38           C  
HETATM 2111  C1' THS A 293      19.935  18.054  -7.268  1.00 67.22           C  
HETATM 2112  N1  THS A 293      20.264  17.042  -8.328  1.00 70.44           N  
HETATM 2113  C2  THS A 293      20.320  15.722  -7.878  1.00 72.41           C  
HETATM 2114  O2  THS A 293      20.352  15.429  -6.676  1.00 74.46           O  
HETATM 2115  N3  THS A 293      20.323  14.722  -8.863  1.00 74.03           N  
HETATM 2116  C4  THS A 293      20.279  14.879 -10.261  1.00 74.48           C  
HETATM 2117  O4  THS A 293      20.289  13.862 -10.996  1.00 74.60           O  
HETATM 2118  C5  THS A 293      20.238  16.308 -10.670  1.00 74.15           C  
HETATM 2119  C5M THS A 293      20.198  16.629 -12.199  1.00 74.20           C  
HETATM 2120  C6  THS A 293      20.242  17.326  -9.704  1.00 72.50           C  
HETATM 2121  P   THS A 294      19.867  19.259  -3.202  1.00 65.64           P  
HETATM 2122  S2P THS A 294      21.262  18.004  -2.659  1.00 66.13           S  
HETATM 2123  S3P THS A 294      19.858  21.065  -2.455  1.00 68.66           S  
HETATM 2124  O5' THS A 294      18.486  18.544  -2.765  1.00 60.86           O  
HETATM 2125  C5' THS A 294      17.259  19.235  -2.961  1.00 52.95           C  
HETATM 2126  C4' THS A 294      16.433  19.067  -1.733  1.00 48.59           C  
HETATM 2127  O4' THS A 294      16.228  17.696  -1.507  1.00 47.49           O  
HETATM 2128  C3' THS A 294      17.065  19.590  -0.438  1.00 46.06           C  
HETATM 2129  O3' THS A 294      15.928  20.159   0.169  1.00 42.51           O  
HETATM 2130  C2' THS A 294      17.581  18.402   0.340  1.00 46.58           C  
HETATM 2131  C1' THS A 294      16.760  17.251  -0.230  1.00 47.31           C  
HETATM 2132  N1  THS A 294      17.506  15.959  -0.396  1.00 46.12           N  
HETATM 2133  C2  THS A 294      16.955  14.859   0.307  1.00 45.82           C  
HETATM 2134  O2  THS A 294      16.003  14.950   1.103  1.00 46.27           O  
HETATM 2135  N3  THS A 294      17.559  13.644   0.072  1.00 44.85           N  
HETATM 2136  C4  THS A 294      18.606  13.404  -0.775  1.00 45.80           C  
HETATM 2137  O4  THS A 294      19.029  12.250  -0.898  1.00 47.03           O  
HETATM 2138  C5  THS A 294      19.110  14.581  -1.456  1.00 45.77           C  
HETATM 2139  C5M THS A 294      20.298  14.379  -2.399  1.00 46.16           C  
HETATM 2140  C6  THS A 294      18.569  15.807  -1.261  1.00 45.00           C  
HETATM 2141  P   THS A 295      15.941  21.536   1.063  1.00 42.04           P  
HETATM 2142  S2P THS A 295      17.418  22.752   0.417  1.00 39.03           S  
HETATM 2143  S3P THS A 295      14.118  22.080   1.316  1.00 40.80           S  
HETATM 2144  O5' THS A 295      16.149  21.170   2.610  1.00 36.14           O  
HETATM 2145  C5' THS A 295      15.920  20.162   3.595  1.00 27.87           C  
HETATM 2146  C4' THS A 295      16.400  20.786   4.891  1.00 23.37           C  
HETATM 2147  O4' THS A 295      17.793  20.597   5.029  1.00 16.01           O  
HETATM 2148  C3' THS A 295      16.253  22.353   4.919  1.00 22.85           C  
HETATM 2149  O3' THS A 295      15.903  22.864   6.241  1.00 25.63           O  
HETATM 2150  C2' THS A 295      17.642  22.889   4.603  1.00 19.35           C  
HETATM 2151  C1' THS A 295      18.529  21.796   5.159  1.00 17.90           C  
HETATM 2152  N1  THS A 295      19.771  21.518   4.476  1.00 19.97           N  
HETATM 2153  C2  THS A 295      20.920  21.433   5.290  1.00 21.13           C  
HETATM 2154  O2  THS A 295      20.848  21.814   6.467  1.00 22.54           O  
HETATM 2155  N3  THS A 295      22.059  20.908   4.680  1.00 19.89           N  
HETATM 2156  C4  THS A 295      22.165  20.495   3.339  1.00 18.56           C  
HETATM 2157  O4  THS A 295      23.240  20.056   2.967  1.00 19.41           O  
HETATM 2158  C5  THS A 295      20.959  20.614   2.529  1.00 18.91           C  
HETATM 2159  C5M THS A 295      20.931  20.166   1.039  1.00 18.82           C  
HETATM 2160  C6  THS A 295      19.823  21.109   3.098  1.00 19.85           C  
HETATM 2161  O   HOH A 400       9.853  24.672  14.114  1.00 11.78           O  
HETATM 2162  O   HOH A 401       7.347  24.491  12.722  1.00 16.00           O  
HETATM 2163  O   HOH A 402       8.538  31.815  11.028  1.00 19.94           O  
HETATM 2164  O   HOH A 403      14.758  33.151  12.800  1.00 13.07           O  
HETATM 2165  O   HOH A 404      11.053  45.264  19.852  1.00 45.07           O  
HETATM 2166  O   HOH A 405      21.269  40.359  23.414  1.00 24.65           O  
HETATM 2167  O   HOH A 406       6.828  33.896  10.412  1.00 29.85           O  
HETATM 2168  O   HOH A 407       7.862  34.550   7.726  1.00 32.57           O  
HETATM 2169  O   HOH A 408      13.573  35.590   6.353  1.00 16.03           O  
HETATM 2170  O   HOH A 409      16.498  31.725   0.836  1.00 17.50           O  
HETATM 2171  O   HOH A 410      24.876  27.070   9.419  1.00 13.08           O  
HETATM 2172  O   HOH A 411      28.482  24.198   2.834  1.00 12.94           O  
HETATM 2173  O   HOH A 412      31.260  21.445   2.312  1.00 24.67           O  
HETATM 2174  O   HOH A 413      30.669  14.695   7.593  1.00 16.89           O  
HETATM 2175  O   HOH A 414      28.668  25.773  -1.441  1.00 30.20           O  
HETATM 2176  O   HOH A 415      23.491  31.923  15.742  1.00 12.41           O  
HETATM 2177  O   HOH A 416      25.190  27.922  17.827  1.00 14.09           O  
HETATM 2178  O   HOH A 417      13.868   5.292  14.208  1.00 14.29           O  
HETATM 2179  O   HOH A 418      29.533  33.546  20.194  1.00 21.68           O  
HETATM 2180  O   HOH A 419      25.421  38.729  18.518  1.00 15.85           O  
HETATM 2181  O   HOH A 420      29.540  41.039  21.838  1.00 29.62           O  
HETATM 2182  O   HOH A 421      34.919  23.573  15.068  1.00 21.41           O  
HETATM 2183  O   HOH A 422      32.533  21.957  16.360  1.00 14.11           O  
HETATM 2184  O   HOH A 423      23.371   8.054  18.113  1.00  9.99           O  
HETATM 2185  O   HOH A 424      24.990   3.447  15.408  1.00 21.28           O  
HETATM 2186  O   HOH A 425      12.162   5.260  22.710  1.00 38.73           O  
HETATM 2187  O   HOH A 426      19.645  17.950  25.814  1.00 25.83           O  
HETATM 2188  O   HOH A 427      17.091  17.231  27.227  1.00 32.68           O  
HETATM 2189  O   HOH A 428      24.466  18.879   0.785  1.00 44.65           O  
HETATM 2190  O   HOH A 429      24.005  20.891   6.930  1.00 13.63           O  
HETATM 2191  O   HOH A 430      10.260  28.080   8.217  1.00 36.59           O  
HETATM 2192  O   HOH A 431       7.715  24.292  10.044  1.00 32.05           O  
HETATM 2193  O   HOH A 432      10.168  14.179   6.998  1.00 30.17           O  
HETATM 2194  O   HOH A 433      12.846  20.540   7.267  1.00 35.76           O  
HETATM 2195  O   HOH A 434      21.460  50.497  19.210  1.00 33.06           O  
HETATM 2196  O   HOH A 435      18.490  55.729  15.009  1.00 37.36           O  
HETATM 2197  O   HOH A 436       7.291  35.622   5.148  1.00 46.04           O  
HETATM 2198  O   HOH A 437      18.161  25.400   1.990  1.00 21.40           O  
HETATM 2199  O   HOH A 438      26.649  25.822   1.642  1.00 20.28           O  
HETATM 2200  O   HOH A 439      30.631  44.372   8.526  1.00 47.60           O  
HETATM 2201  O   HOH A 440      11.279   6.799   8.056  1.00 27.27           O  
HETATM 2202  O   HOH A 441       4.869  14.123  16.234  1.00 26.45           O  
HETATM 2203  O   HOH A 442       0.578   8.282  16.549  1.00 36.52           O  
HETATM 2204  O   HOH A 443       4.377   7.970   8.163  1.00 26.71           O  
HETATM 2205  O   HOH A 444       5.120  16.869  16.384  1.00 19.84           O  
HETATM 2206  O   HOH A 445       3.391  18.266  14.810  1.00 30.84           O  
HETATM 2207  O   HOH A 446      28.329  23.401  22.092  1.00 25.22           O  
HETATM 2208  O   HOH A 447      31.942  17.682  19.918  1.00 19.77           O  
HETATM 2209  O   HOH A 448      34.640  16.228  18.555  1.00 33.44           O  
HETATM 2210  O   HOH A 449      21.027  12.200  22.532  1.00 18.14           O  
HETATM 2211  O   HOH A 450      21.227   9.291  22.264  1.00 24.95           O  
HETATM 2212  O   HOH A 451      21.706   7.367  20.188  1.00 23.87           O  
HETATM 2213  O   HOH A 452      23.196  12.976  24.766  1.00 47.05           O  
HETATM 2214  O   HOH A 453      26.606   6.934  11.700  1.00 28.03           O  
HETATM 2215  O   HOH A 454       7.205  17.455  26.043  1.00 37.74           O  
HETATM 2216  O   HOH A 455      17.272  24.063  28.086  1.00 25.85           O  
HETATM 2217  O   HOH A 456      14.464  18.893  31.419  1.00 41.40           O  
HETATM 2218  O   HOH A 457      26.996  18.726  24.995  1.00 50.92           O  
HETATM 2219  O   HOH A 458       6.692  25.366  -4.446  1.00 27.97           O  
HETATM 2220  O   HOH A 459       9.047  23.867  -5.196  1.00 32.65           O  
HETATM 2221  O   HOH A 460      37.453  28.285   9.998  1.00 23.28           O  
HETATM 2222  O   HOH A 461      30.649  37.177   1.967  1.00 33.96           O  
HETATM 2223  O   HOH A 462      26.146  16.760   2.116  1.00 36.45           O  
HETATM 2224  O   HOH A 463      28.663  17.728   1.377  1.00 34.06           O  
HETATM 2225  O   HOH A 464      30.091  15.501   1.725  1.00 59.52           O  
HETATM 2226  O   HOH A 465       8.487  26.747   7.064  1.00 58.71           O  
HETATM 2227  O   HOH A 466       8.891  39.394  22.666  1.00 47.47           O  
HETATM 2228  O   HOH A 467       8.579  40.471  25.166  1.00 51.05           O  
HETATM 2229  O   HOH A 468      20.278  41.476  28.890  1.00 38.89           O  
HETATM 2230  O   HOH A 469      16.138  45.852  25.627  1.00 32.82           O  
HETATM 2231  O   HOH A 470       6.477  28.656  -5.090  1.00 52.24           O  
HETATM 2232  O   HOH A 471      14.430  24.999  -3.387  1.00 58.24           O  
HETATM 2233  O   HOH A 472      23.118  44.031  22.626  1.00 26.33           O  
HETATM 2234  O   HOH A 473      33.632  21.934   0.548  1.00 56.45           O  
HETATM 2235  O   HOH A 474      30.849  11.561   7.339  1.00 55.92           O  
HETATM 2236  O   HOH A 475      25.902  12.833   2.422  1.00 45.61           O  
HETATM 2237  O   HOH A 476      28.132  30.548  22.564  1.00 33.52           O  
HETATM 2238  O   HOH A 477      31.900  40.694  23.954  1.00 32.21           O  
HETATM 2239  O   HOH A 478      27.794  43.527  22.634  1.00 40.62           O  
HETATM 2240  O   HOH A 479      34.339  20.734  18.173  1.00 55.42           O  
HETATM 2241  O   HOH A 480      35.139  28.846  15.851  1.00 56.19           O  
HETATM 2242  O   HOH A 481      19.543   5.534  20.503  1.00 53.90           O  
HETATM 2243  O   HOH A 482      14.064  18.169   5.937  1.00 24.33           O  
HETATM 2244  O   HOH A 483       2.456  17.079  18.034  1.00 36.69           O  
HETATM 2245  O   HOH A 484       2.331   6.815   9.747  1.00 45.81           O  
HETATM 2246  O   HOH A 485       8.428  15.755  28.208  1.00 49.89           O  
HETATM 2247  O   HOH A 486      36.880  31.431  10.212  1.00 27.27           O  
HETATM 2248  O   HOH A 487      39.006  28.485   7.202  1.00 39.39           O  
HETATM 2249  O   HOH A 488      14.595  37.733  -6.672  1.00 36.65           O  
HETATM 2250  O   HOH A 489      38.428  22.421  12.239  1.00 50.06           O  
HETATM 2251  O   HOH A 490      35.029  26.844   0.668  1.00 34.98           O  
HETATM 2252  O   HOH A 491      20.079  42.897  -0.039  1.00 30.46           O  
HETATM 2253  O   HOH A 492      12.549  44.151  -0.390  1.00 38.71           O  
HETATM 2254  O   HOH A 493      14.861  10.464   4.456  1.00 47.08           O  
HETATM 2255  O   HOH A 494       5.911   3.675  16.936  1.00 39.04           O  
HETATM 2256  O   HOH A 495       4.191   7.255  19.833  1.00 54.15           O  
HETATM 2257  O   HOH A 496       5.455  11.583   7.744  1.00 41.08           O  
HETATM 2258  O   HOH A 497       2.114  10.500   7.372  1.00 60.70           O  
HETATM 2259  O   HOH A 498      -1.656  33.378  15.635  1.00 50.89           O  
HETATM 2260  O   HOH A 499      20.896  37.722  31.282  1.00 35.26           O  
HETATM 2261  O   HOH A 500      25.228  27.595  27.042  1.00 29.02           O  
HETATM 2262  O   HOH A 501      27.644  30.261  28.165  1.00 32.63           O  
HETATM 2263  O   HOH A 502      35.921  31.804  15.089  1.00 34.45           O  
HETATM 2264  O   HOH A 503      19.799  -0.003  12.671  1.00 40.91           O  
HETATM 2265  O   HOH A 504      16.761   9.580  27.542  1.00 42.63           O  
HETATM 2266  O   HOH A 505      17.196  11.512  29.061  1.00 55.10           O  
HETATM 2267  O   HOH A 506      18.959   8.379  23.382  1.00 40.01           O  
HETATM 2268  O   HOH A 507      23.079  21.027  25.466  1.00 39.38           O  
HETATM 2269  O   HOH A 508      29.104  48.517  17.466  1.00 70.46           O  
HETATM 2270  O   HOH A 509      10.417  20.784   8.381  1.00 47.36           O  
HETATM 2271  O   HOH A 510      12.146  23.797   7.875  1.00 39.99           O  
HETATM 2272  O   HOH A 511      12.926  46.841  23.433  1.00 61.57           O  
HETATM 2273  O   HOH A 512       9.913  43.247   4.578  1.00 40.71           O  
HETATM 2274  O   HOH A 513       1.937  39.136  18.663  1.00 65.89           O  
HETATM 2275  O   HOH A 514      19.099  25.216  -5.157  1.00 30.96           O  
HETATM 2276  O   HOH A 515       8.260  29.423 -11.965  1.00 47.53           O  
HETATM 2277  O   HOH A 516      18.923  34.367 -10.213  1.00 44.14           O  
HETATM 2278  O   HOH A 517      17.096  36.232  -9.159  1.00 45.70           O  
HETATM 2279  O   HOH A 518      17.061  33.949 -12.319  1.00 41.61           O  
HETATM 2280  O   HOH A 519      19.677  25.610  -8.599  1.00 46.97           O  
HETATM 2281  O   HOH A 520      21.203  30.249 -11.479  1.00 45.87           O  
HETATM 2282  O   HOH A 521      17.220  23.329  -4.122  1.00 40.52           O  
HETATM 2283  O   HOH A 522      26.459  24.101  -0.697  1.00 48.87           O  
HETATM 2284  O   HOH A 523      31.600  35.339  -0.125  1.00 55.24           O  
HETATM 2285  O   HOH A 524      31.960  42.461   5.959  1.00 43.30           O  
HETATM 2286  O   HOH A 525      28.507  43.207   0.108  1.00 50.29           O  
HETATM 2287  O   HOH A 526      -1.432   6.694  16.060  1.00 48.69           O  
HETATM 2288  O   HOH A 527       7.179  15.173   6.940  1.00 40.92           O  
HETATM 2289  O   HOH A 528       2.334  19.225  11.033  1.00 41.93           O  
HETATM 2290  O   HOH A 529       4.535  22.871  10.512  1.00 52.84           O  
HETATM 2291  O   HOH A 530      -4.213  34.254  17.719  1.00 51.10           O  
HETATM 2292  O   HOH A 531       4.395  31.338  27.889  1.00 38.13           O  
HETATM 2293  O   HOH A 532      13.778  27.320  28.323  1.00 55.38           O  
HETATM 2294  O   HOH A 533      21.442  31.066  35.465  1.00 33.52           O  
HETATM 2295  O   HOH A 534      23.674  36.815  31.264  1.00 43.84           O  
HETATM 2296  O   HOH A 535      30.006  40.979  25.982  1.00 58.11           O  
HETATM 2297  O   HOH A 536      25.929   4.125  11.951  1.00 42.97           O  
HETATM 2298  O   HOH A 537      20.862  13.955  27.250  1.00 45.05           O  
HETATM 2299  O   HOH A 538      26.140  26.165  25.236  1.00 41.05           O  
HETATM 2300  O   HOH A 539      12.032  43.269  30.391  1.00 30.85           O  
HETATM 2301  O   HOH A 540      31.764  47.742  18.287  1.00 52.08           O  
HETATM 2302  O   HOH A 541      14.586   6.065  21.420  1.00 39.19           O  
HETATM 2303  O   HOH A 542      19.737  23.328  28.325  1.00 53.77           O  
HETATM 2304  O   HOH A 543      19.561  43.678  25.415  1.00 46.66           O  
HETATM 2305  O   HOH A 544      31.254   9.990  10.096  1.00 44.64           O  
HETATM 2306  O   HOH A 545      27.679  28.548  24.233  1.00 60.99           O  
HETATM 2307  O   HOH A 546      38.198  31.453  12.828  1.00 47.74           O  
HETATM 2308  O   HOH A 547       8.198  44.057   6.639  1.00 47.36           O  
HETATM 2309  O   HOH A 548      11.194  26.448   1.757  1.00 51.99           O  
HETATM 2310  O   HOH A 549      17.575  31.354  -8.879  1.00 49.19           O  
HETATM 2311  O   HOH A 550      32.844   8.649  13.115  1.00 49.07           O  
HETATM 2312  O   HOH A 551      24.317  35.930   0.153  1.00 38.41           O  
HETATM 2313  O   HOH A 552      11.696   4.424   8.888  1.00 49.62           O  
HETATM 2314  O   HOH A 553      12.607  21.738   4.577  1.00 54.12           O  
CONECT    1 2081                                                                
CONECT    4 2081                                                                
CONECT   45 2081                                                                
CONECT  112 2082                                                                
CONECT  327 2079                                                                
CONECT  445 2079                                                                
CONECT  540 1653                                                                
CONECT  609  635                                                                
CONECT  635  609                                                                
CONECT  681 2023                                                                
CONECT  874 2079                                                                
CONECT  904 2081                                                                
CONECT  905 2079                                                                
CONECT  954 2080                                                                
CONECT 1041 2065                                                                
CONECT 1134 2080                                                                
CONECT 1169 2080                                                                
CONECT 1170 2080                                                                
CONECT 1385 2082                                                                
CONECT 1386 2082                                                                
CONECT 1387 2082                                                                
CONECT 1506 2051                                                                
CONECT 1653  540                                                                
CONECT 2023  681 2024 2034                                                      
CONECT 2024 2023 2025 2031                                                      
CONECT 2025 2024 2026 2032                                                      
CONECT 2026 2025 2027 2033                                                      
CONECT 2027 2026 2028 2034                                                      
CONECT 2028 2027 2035                                                           
CONECT 2029 2030 2031 2036                                                      
CONECT 2030 2029                                                                
CONECT 2031 2024 2029                                                           
CONECT 2032 2025                                                                
CONECT 2033 2026 2037                                                           
CONECT 2034 2023 2027                                                           
CONECT 2035 2028                                                                
CONECT 2036 2029                                                                
CONECT 2037 2033 2038 2048                                                      
CONECT 2038 2037 2039 2045                                                      
CONECT 2039 2038 2040 2046                                                      
CONECT 2040 2039 2041 2047                                                      
CONECT 2041 2040 2042 2048                                                      
CONECT 2042 2041 2049                                                           
CONECT 2043 2044 2045 2050                                                      
CONECT 2044 2043                                                                
CONECT 2045 2038 2043                                                           
CONECT 2046 2039                                                                
CONECT 2047 2040                                                                
CONECT 2048 2037 2041                                                           
CONECT 2049 2042                                                                
CONECT 2050 2043                                                                
CONECT 2051 1506 2052 2062                                                      
CONECT 2052 2051 2053 2059                                                      
CONECT 2053 2052 2054 2060                                                      
CONECT 2054 2053 2055 2061                                                      
CONECT 2055 2054 2056 2062                                                      
CONECT 2056 2055 2063                                                           
CONECT 2057 2058 2059 2064                                                      
CONECT 2058 2057                                                                
CONECT 2059 2052 2057                                                           
CONECT 2060 2053                                                                
CONECT 2061 2054                                                                
CONECT 2062 2051 2055                                                           
CONECT 2063 2056                                                                
CONECT 2064 2057                                                                
CONECT 2065 1041 2066 2076                                                      
CONECT 2066 2065 2067 2073                                                      
CONECT 2067 2066 2068 2074                                                      
CONECT 2068 2067 2069 2075                                                      
CONECT 2069 2068 2070 2076                                                      
CONECT 2070 2069 2077                                                           
CONECT 2071 2072 2073 2078                                                      
CONECT 2072 2071                                                                
CONECT 2073 2066 2071                                                           
CONECT 2074 2067                                                                
CONECT 2075 2068                                                                
CONECT 2076 2065 2069                                                           
CONECT 2077 2070                                                                
CONECT 2078 2071                                                                
CONECT 2079  327  445  874  905                                                 
CONECT 2080  954 1134 1169 1170                                                 
CONECT 2080 2149                                                                
CONECT 2081    1    4   45  904                                                 
CONECT 2082  112 1385 1386 1387                                                 
CONECT 2082 2300                                                                
CONECT 2083 2084                                                                
CONECT 2084 2083 2085                                                           
CONECT 2085 2084 2086 2087                                                      
CONECT 2086 2085 2090                                                           
CONECT 2087 2085 2088 2089                                                      
CONECT 2088 2087 2101                                                           
CONECT 2089 2087 2090                                                           
CONECT 2090 2086 2089 2091                                                      
CONECT 2091 2090 2092 2100                                                      
CONECT 2092 2091 2093                                                           
CONECT 2093 2092 2094                                                           
CONECT 2094 2093 2095 2100                                                      
CONECT 2095 2094 2096 2097                                                      
CONECT 2096 2095                                                                
CONECT 2097 2095 2098                                                           
CONECT 2098 2097 2099                                                           
CONECT 2099 2098 2100                                                           
CONECT 2100 2091 2094 2099                                                      
CONECT 2101 2088 2102 2103 2104                                                 
CONECT 2102 2101                                                                
CONECT 2103 2101                                                                
CONECT 2104 2101 2105                                                           
CONECT 2105 2104 2106                                                           
CONECT 2106 2105 2107 2108                                                      
CONECT 2107 2106 2111                                                           
CONECT 2108 2106 2109 2110                                                      
CONECT 2109 2108 2121                                                           
CONECT 2110 2108 2111                                                           
CONECT 2111 2107 2110 2112                                                      
CONECT 2112 2111 2113 2120                                                      
CONECT 2113 2112 2114 2115                                                      
CONECT 2114 2113                                                                
CONECT 2115 2113 2116                                                           
CONECT 2116 2115 2117 2118                                                      
CONECT 2117 2116                                                                
CONECT 2118 2116 2119 2120                                                      
CONECT 2119 2118                                                                
CONECT 2120 2112 2118                                                           
CONECT 2121 2109 2122 2123 2124                                                 
CONECT 2122 2121                                                                
CONECT 2123 2121                                                                
CONECT 2124 2121 2125                                                           
CONECT 2125 2124 2126                                                           
CONECT 2126 2125 2127 2128                                                      
CONECT 2127 2126 2131                                                           
CONECT 2128 2126 2129 2130                                                      
CONECT 2129 2128 2141                                                           
CONECT 2130 2128 2131                                                           
CONECT 2131 2127 2130 2132                                                      
CONECT 2132 2131 2133 2140                                                      
CONECT 2133 2132 2134 2135                                                      
CONECT 2134 2133                                                                
CONECT 2135 2133 2136                                                           
CONECT 2136 2135 2137 2138                                                      
CONECT 2137 2136                                                                
CONECT 2138 2136 2139 2140                                                      
CONECT 2139 2138                                                                
CONECT 2140 2132 2138                                                           
CONECT 2141 2129 2142 2143 2144                                                 
CONECT 2142 2141                                                                
CONECT 2143 2141                                                                
CONECT 2144 2141 2145                                                           
CONECT 2145 2144 2146                                                           
CONECT 2146 2145 2147 2148                                                      
CONECT 2147 2146 2151                                                           
CONECT 2148 2146 2149 2150                                                      
CONECT 2149 2080 2148                                                           
CONECT 2150 2148 2151                                                           
CONECT 2151 2147 2150 2152                                                      
CONECT 2152 2151 2153 2160                                                      
CONECT 2153 2152 2154 2155                                                      
CONECT 2154 2153                                                                
CONECT 2155 2153 2156                                                           
CONECT 2156 2155 2157 2158                                                      
CONECT 2157 2156                                                                
CONECT 2158 2156 2159 2160                                                      
CONECT 2159 2158                                                                
CONECT 2160 2152 2158                                                           
CONECT 2300 2082                                                                
MASTER      328    0   12   17    2    0    0    6 2313    1  164   21          
END                                                                             
