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***  METALLOPROTEASE 26-NOV-02 1O8A  ***

elNémo ID: 20042220085887874

Job options:

ID        	=	 20042220085887874
JOBID     	=	 METALLOPROTEASE 26-NOV-02 1O8A
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    METALLOPROTEASE                         26-NOV-02   1O8A              
TITLE     CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME (NATIVE).    
CAVEAT     1O8A    NAG A 695 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 68-656;                                           
COMPND   5 SYNONYM: ACE-T, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II;          
COMPND   6 EC: 3.4.15.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: TESTIS;                                                       
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    METALLOPROTEASE, ACE, PEPTIDYL DIPEPTIDASE, TYPE-I MEMBRANE-ANCHORED  
KEYWDS   2 PROTEIN.                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.NATESH,S.L.U.SCHWAGER,E.D.STURROCK,K.R.ACHARYA                      
REVDAT   5   11-JUL-18 1O8A    1       CAVEAT COMPND JRNL   HET                 
REVDAT   5 2                   1       HETNAM FORMUL LINK   ATOM                
REVDAT   4   24-FEB-09 1O8A    1       VERSN                                    
REVDAT   3   06-MAR-06 1O8A    1       TITLE  REMARK                            
REVDAT   2   11-JUL-03 1O8A    1       JRNL                                     
REVDAT   1   07-FEB-03 1O8A    0                                                
JRNL        AUTH   R.NATESH,S.L.SCHWAGER,E.D.STURROCK,K.R.ACHARYA               
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN ANGIOTENSIN-CONVERTING        
JRNL        TITL 2 ENZYME-LISINOPRIL COMPLEX.                                   
JRNL        REF    NATURE                        V. 421   551 2003              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   12540854                                                     
JRNL        DOI    10.1038/NATURE01370                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 41402                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1675                            
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            : 4660                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 504                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.40                          
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) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.220                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.35                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.810                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1O8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290011783.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42782                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 22.4600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.440                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1O86                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000/SODIUM ACETATE., PH 4.70         
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       28.31000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.89500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.89500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.31000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.53000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CONVERTS ANGIOTENSIN I TO ANGIOTENSIN II BY RELEASE OF               
REMARK 400  THE TERMINAL HIS-LEU, THIS RESULTS IN AN INCREASE OF THE            
REMARK 400  VASOCONSTRICTOR ACTIVITY OF ANGIOTENSIN. ALSO ABLE TO INACTIVATE    
REMARK 400  BRADYKININ, A POTENT VASODILATOR  AND ACTS ON VARIOUS OTHER         
REMARK 400  OLIGOPEPTIDES WITH FREE C-TERMINUS.                                 
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     LEU A    37                                                      
REMARK 465     VAL A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     SER A   435                                                      
REMARK 465     GLU A   436                                                      
REMARK 465     GLY A   437                                                      
REMARK 465     GLY A   438                                                      
REMARK 465     TYR A   619                                                      
REMARK 465     ASN A   620                                                      
REMARK 465     TRP A   621                                                      
REMARK 465     THR A   622                                                      
REMARK 465     PRO A   623                                                      
REMARK 465     ASN A   624                                                      
REMARK 465     SER A   625                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A  40    CG   OD1  OD2                                       
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 117    CG   CD   CE   NZ                                   
REMARK 470     SER A 298    OG                                                  
REMARK 470     GLU A 303    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 307    CG   CD   CE   NZ                                   
REMARK 470     SER A 439    CB   OG                                             
REMARK 470     ASP A 440    CG   OD1  OD2                                       
REMARK 470     GLN A 618    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLN A 618    NE2                                                 
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    ASN A  72       76.67   -169.41                                   
REMARK 500    GLU A 123     -136.53     49.77                                   
REMARK 500    GLN A 308       33.14    -97.76                                   
REMARK 500    ASP A 346       -6.67    -53.05                                   
REMARK 500    LYS A 363      -39.81   -133.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 387   NE2                                                    
REMARK 620 2 GLU A 411   OE1 105.0                                              
REMARK 620 3 ACT A 700   OXT  89.5 153.1                                        
REMARK 620 4 ACT A 700   O   127.5  95.5  58.2                                  
REMARK 620 5 HIS A 383   NE2 106.6  95.6 101.8 118.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 691                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 692                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 693                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 694                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 696                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 704                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NXA A 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX  
REMARK 900 WITH LISINOPRIL.                                                     
DBREF  1O8A A   37   625  UNP    P22966   ACET_HUMAN      68    656             
SEQRES   1 A  589  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU          
SEQRES   2 A  589  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR          
SEQRES   3 A  589  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR          
SEQRES   4 A  589  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE          
SEQRES   5 A  589  ALA ASN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS          
SEQRES   6 A  589  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG          
SEQRES   7 A  589  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU          
SEQRES   8 A  589  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU          
SEQRES   9 A  589  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS          
SEQRES  10 A  589  PRO ASN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR          
SEQRES  11 A  589  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU          
SEQRES  12 A  589  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA          
SEQRES  13 A  589  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN          
SEQRES  14 A  589  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP          
SEQRES  15 A  589  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN          
SEQRES  16 A  589  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR          
SEQRES  17 A  589  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG          
SEQRES  18 A  589  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE          
SEQRES  19 A  589  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP          
SEQRES  20 A  589  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA          
SEQRES  21 A  589  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY          
SEQRES  22 A  589  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE          
SEQRES  23 A  589  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE          
SEQRES  24 A  589  TRP ASN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG          
SEQRES  25 A  589  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN          
SEQRES  26 A  589  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN          
SEQRES  27 A  589  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS          
SEQRES  28 A  589  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA          
SEQRES  29 A  589  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE          
SEQRES  30 A  589  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS          
SEQRES  31 A  589  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER          
SEQRES  32 A  589  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU          
SEQRES  33 A  589  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP          
SEQRES  34 A  589  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS          
SEQRES  35 A  589  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS          
SEQRES  36 A  589  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY          
SEQRES  37 A  589  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER          
SEQRES  38 A  589  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN          
SEQRES  39 A  589  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS          
SEQRES  40 A  589  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS          
SEQRES  41 A  589  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY          
SEQRES  42 A  589  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR          
SEQRES  43 A  589  GLY GLN PRO ASN MET SER ALA SER ALA MET LEU SER TYR          
SEQRES  44 A  589  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU          
SEQRES  45 A  589  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP          
SEQRES  46 A  589  THR PRO ASN SER                                              
MODRES 1O8A ASN A   72  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A   90  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  109  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  155  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  337  ASN  GLYCOSYLATION SITE                                 
MODRES 1O8A ASN A  586  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 691      14                                                       
HET    NAG  A 692      14                                                       
HET    NAG  A 693      14                                                       
HET    NAG  A 694      14                                                       
HET    NAG  A 695      14                                                       
HET    NAG  A 696      14                                                       
HET    ACT  A 700       4                                                       
HET     ZN  A 701       1                                                       
HET    NXA  A 702       9                                                       
HET     CL  A 703       1                                                       
HET     CL  A 704       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     ACT ACETATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     NXA N-CARBOXYALANINE                                                 
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  NAG    6(C8 H15 N O6)                                               
FORMUL   8  ACT    C2 H3 O2 1-                                                  
FORMUL   9   ZN    ZN 2+                                                        
FORMUL  10  NXA    C4 H7 N O4                                                   
FORMUL  11   CL    2(CL 1-)                                                     
FORMUL  13  HOH   *504(H2 O)                                                    
HELIX    1   1 ASP A   40  THR A   71  1                                  32    
HELIX    2   2 THR A   74  ARG A  100  1                                  27    
HELIX    3   3 LYS A  101  LEU A  107  5                                   7    
HELIX    4   4 ASN A  109  GLN A  120  1                                  12    
HELIX    5   5 LEU A  122  LEU A  127  5                                   6    
HELIX    6   6 PRO A  128  VAL A  148  1                                  21    
HELIX    7   7 PRO A  163  SER A  172  1                                  10    
HELIX    8   8 LYS A  174  LEU A  210  1                                  37    
HELIX    9   9 ASP A  215  SER A  222  1                                   8    
HELIX   10  10 MET A  223  GLU A  225  5                                   3    
HELIX   11  11 SER A  228  GLY A  260  1                                  33    
HELIX   12  12 TRP A  283  ASN A  285  5                                   3    
HELIX   13  13 ILE A  286  VAL A  291  1                                   6    
HELIX   14  14 ASP A  300  GLN A  308  1                                   9    
HELIX   15  15 THR A  311  LEU A  326  1                                  16    
HELIX   16  16 PRO A  332  SER A  339  1                                   8    
HELIX   17  17 ASN A  374  TYR A  394  1                                  21    
HELIX   18  18 PRO A  398  ARG A  402  5                                   5    
HELIX   19  19 ASN A  406  LEU A  430  1                                  25    
HELIX   20  20 SER A  439  ASP A  473  1                                  35    
HELIX   21  21 ASN A  480  GLY A  494  1                                  15    
HELIX   22  22 PHE A  506  LYS A  511  5                                   6    
HELIX   23  23 TYR A  520  ALA A  541  1                                  22    
HELIX   24  24 PRO A  546  CYS A  550  5                                   5    
HELIX   25  25 SER A  555  LEU A  568  1                                  14    
HELIX   26  26 PRO A  573  GLY A  583  1                                  11    
HELIX   27  27 ALA A  589  HIS A  610  1                                  22    
SHEET    1  AA 2 ALA A 149  HIS A 153  0                                        
SHEET    2  AA 2 SER A 157  LEU A 161 -1  O  LEU A 159   N  VAL A 151           
SHEET    1  AB 2 ILE A 270  ALA A 272  0                                        
SHEET    2  AB 2 LEU A 495  CYS A 496  1  N  CYS A 496   O  ILE A 270           
SHEET    1  AC 2 SER A 355  PHE A 359  0                                        
SHEET    2  AC 2 ASP A 364  LYS A 368 -1  O  ARG A 366   N  TRP A 357           
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.03  
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.03  
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03  
LINK         ND2 ASN A  72                 C1  NAG A 691     1555   1555  1.46  
LINK         ND2 ASN A  72                 O5  NAG A 691     1555   1555  1.88  
LINK         ND2 ASN A  90                 C1  NAG A 692     1555   1555  1.45  
LINK         ND2 ASN A 109                 C1  NAG A 693     1555   1555  1.45  
LINK         ND2 ASN A 155                 C1  NAG A 694     1555   1555  1.45  
LINK         ND2 ASN A 337                 C1  NAG A 695     1555   1555  1.46  
LINK         ND2 ASN A 586                 C1  NAG A 696     1555   1555  1.46  
LINK        ZN    ZN A 701                 NE2 HIS A 387     1555   1555  2.06  
LINK        ZN    ZN A 701                 OE1 GLU A 411     1555   1555  1.97  
LINK        ZN    ZN A 701                 OXT ACT A 700     1555   1555  2.60  
LINK        ZN    ZN A 701                 O   ACT A 700     1555   1555  2.06  
LINK        ZN    ZN A 701                 NE2 HIS A 383     1555   1555  2.02  
CISPEP   1 GLU A  162    PRO A  163          0         0.16                     
SITE     1 AC1  5 ASN A  72  THR A  74  GLU A  76  ASP A 346                    
SITE     2 AC1  5 ARG A 348                                                     
SITE     1 AC2  1 ASN A  90                                                     
SITE     1 AC3  2 ASN A 109  ILE A 112                                          
SITE     1 AC4  3 HIS A 153  ASN A 155  SER A 157                               
SITE     1 AC5  4 THR A 502  ASN A 586  HOH A2221  HOH A2503                    
SITE     1 AC6  1 ASN A 337                                                     
SITE     1 AC7  9 ALA A 354  HIS A 383  GLU A 384  HIS A 387                    
SITE     2 AC7  9 GLU A 411  TYR A 523   ZN A 701  NXA A 702                    
SITE     3 AC7  9 HOH A2317                                                     
SITE     1 AC8  4 HIS A 383  HIS A 387  GLU A 411  ACT A 700                    
SITE     1 AC9  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489                    
SITE     1 BC1  6 TYR A 224  PRO A 407  PRO A 519  ILE A 521                    
SITE     2 BC1  6 ARG A 522  HOH A2195                                          
SITE     1 BC2 10 GLN A 281  HIS A 353  GLU A 384  LYS A 511                    
SITE     2 BC2 10 HIS A 513  TYR A 520  TYR A 523  ACT A 700                    
SITE     3 BC2 10 HOH A2424  HOH A2504                                          
CRYST1   56.620   85.060  133.790  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      0.017662  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011756  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007474        0.00000                         
ATOM      1  N   ASP A  40      35.784  72.211  67.437  1.00 47.96           N  
ATOM      2  CA  ASP A  40      35.164  71.098  66.663  1.00 47.50           C  
ATOM      3  C   ASP A  40      36.244  70.263  65.985  1.00 47.34           C  
ATOM      4  O   ASP A  40      36.117  69.044  65.862  1.00 47.51           O  
ATOM      5  CB  ASP A  40      34.205  71.662  65.620  1.00 47.11           C  
ATOM      6  N   GLU A  41      37.307  70.929  65.547  1.00 46.68           N  
ATOM      7  CA  GLU A  41      38.419  70.260  64.882  1.00 46.09           C  
ATOM      8  C   GLU A  41      39.223  69.474  65.916  1.00 45.81           C  
ATOM      9  O   GLU A  41      39.862  68.466  65.594  1.00 45.67           O  
ATOM     10  CB  GLU A  41      39.315  71.298  64.200  1.00 46.87           C  
ATOM     11  CG  GLU A  41      40.370  70.727  63.262  1.00 47.65           C  
ATOM     12  CD  GLU A  41      39.776  70.111  62.005  1.00 48.95           C  
ATOM     13  OE1 GLU A  41      38.997  70.801  61.309  1.00 48.20           O  
ATOM     14  OE2 GLU A  41      40.096  68.939  61.708  1.00 49.03           O  
ATOM     15  N   ALA A  42      39.184  69.941  67.161  1.00 43.82           N  
ATOM     16  CA  ALA A  42      39.905  69.292  68.249  1.00 42.35           C  
ATOM     17  C   ALA A  42      39.210  67.996  68.646  1.00 40.96           C  
ATOM     18  O   ALA A  42      39.863  66.990  68.926  1.00 39.62           O  
ATOM     19  CB  ALA A  42      39.995  70.229  69.446  1.00 42.98           C  
ATOM     20  N   GLU A  43      37.881  68.028  68.680  1.00 40.60           N  
ATOM     21  CA  GLU A  43      37.104  66.844  69.025  1.00 40.79           C  
ATOM     22  C   GLU A  43      37.272  65.799  67.931  1.00 38.90           C  
ATOM     23  O   GLU A  43      37.217  64.597  68.192  1.00 38.20           O  
ATOM     24  CB  GLU A  43      35.620  67.190  69.157  1.00 42.97           C  
ATOM     25  CG  GLU A  43      35.138  67.389  70.581  1.00 48.05           C  
ATOM     26  CD  GLU A  43      33.642  67.644  70.649  1.00 51.91           C  
ATOM     27  OE1 GLU A  43      32.869  66.798  70.142  1.00 53.53           O  
ATOM     28  OE2 GLU A  43      33.239  68.687  71.210  1.00 53.71           O  
ATOM     29  N   ALA A  44      37.482  66.273  66.706  1.00 37.33           N  
ATOM     30  CA  ALA A  44      37.643  65.395  65.552  1.00 35.44           C  
ATOM     31  C   ALA A  44      38.917  64.558  65.613  1.00 33.72           C  
ATOM     32  O   ALA A  44      38.871  63.343  65.434  1.00 34.25           O  
ATOM     33  CB  ALA A  44      37.619  66.217  64.268  1.00 34.80           C  
ATOM     34  N   SER A  45      40.053  65.204  65.856  1.00 32.28           N  
ATOM     35  CA  SER A  45      41.319  64.486  65.932  1.00 32.11           C  
ATOM     36  C   SER A  45      41.326  63.562  67.148  1.00 30.77           C  
ATOM     37  O   SER A  45      41.948  62.501  67.126  1.00 30.49           O  
ATOM     38  CB  SER A  45      42.486  65.468  66.012  1.00 33.65           C  
ATOM     39  OG  SER A  45      42.391  66.266  67.175  1.00 40.00           O  
ATOM     40  N   LYS A  46      40.631  63.974  68.204  1.00 29.20           N  
ATOM     41  CA  LYS A  46      40.534  63.179  69.424  1.00 29.11           C  
ATOM     42  C   LYS A  46      39.662  61.952  69.160  1.00 28.16           C  
ATOM     43  O   LYS A  46      39.966  60.844  69.613  1.00 25.92           O  
ATOM     44  CB  LYS A  46      39.924  64.021  70.547  1.00 32.76           C  
ATOM     45  CG  LYS A  46      39.438  63.219  71.745  1.00 35.84           C  
ATOM     46  CD  LYS A  46      38.889  64.135  72.830  1.00 42.05           C  
ATOM     47  CE  LYS A  46      38.072  63.355  73.847  1.00 44.16           C  
ATOM     48  NZ  LYS A  46      36.868  62.741  73.208  1.00 47.21           N  
ATOM     49  N   PHE A  47      38.573  62.163  68.427  1.00 26.59           N  
ATOM     50  CA  PHE A  47      37.661  61.079  68.083  1.00 26.14           C  
ATOM     51  C   PHE A  47      38.407  60.018  67.281  1.00 24.51           C  
ATOM     52  O   PHE A  47      38.293  58.825  67.555  1.00 25.03           O  
ATOM     53  CB  PHE A  47      36.495  61.610  67.250  1.00 26.37           C  
ATOM     54  CG  PHE A  47      35.634  60.527  66.657  1.00 28.09           C  
ATOM     55  CD1 PHE A  47      34.772  59.788  67.459  1.00 27.07           C  
ATOM     56  CD2 PHE A  47      35.700  60.238  65.297  1.00 27.78           C  
ATOM     57  CE1 PHE A  47      33.983  58.776  66.916  1.00 28.93           C  
ATOM     58  CE2 PHE A  47      34.914  59.224  64.745  1.00 29.96           C  
ATOM     59  CZ  PHE A  47      34.055  58.493  65.558  1.00 27.46           C  
ATOM     60  N   VAL A  48      39.174  60.460  66.290  1.00 24.17           N  
ATOM     61  CA  VAL A  48      39.928  59.539  65.448  1.00 25.75           C  
ATOM     62  C   VAL A  48      40.944  58.732  66.255  1.00 26.10           C  
ATOM     63  O   VAL A  48      41.109  57.527  66.030  1.00 26.21           O  
ATOM     64  CB  VAL A  48      40.647  60.296  64.315  1.00 27.26           C  
ATOM     65  CG1 VAL A  48      41.588  59.362  63.574  1.00 29.96           C  
ATOM     66  CG2 VAL A  48      39.618  60.868  63.352  1.00 26.11           C  
ATOM     67  N   GLU A  49      41.624  59.390  67.191  1.00 25.41           N  
ATOM     68  CA  GLU A  49      42.605  58.707  68.031  1.00 26.15           C  
ATOM     69  C   GLU A  49      41.910  57.627  68.858  1.00 23.94           C  
ATOM     70  O   GLU A  49      42.408  56.504  68.979  1.00 22.22           O  
ATOM     71  CB  GLU A  49      43.302  59.699  68.974  1.00 30.36           C  
ATOM     72  CG  GLU A  49      44.036  60.832  68.267  1.00 34.75           C  
ATOM     73  CD  GLU A  49      44.759  61.760  69.233  1.00 39.99           C  
ATOM     74  OE1 GLU A  49      44.149  62.161  70.251  1.00 41.71           O  
ATOM     75  OE2 GLU A  49      45.934  62.096  68.971  1.00 40.92           O  
ATOM     76  N   GLU A  50      40.759  57.969  69.431  1.00 22.01           N  
ATOM     77  CA  GLU A  50      40.011  57.013  70.237  1.00 22.46           C  
ATOM     78  C   GLU A  50      39.524  55.860  69.369  1.00 21.38           C  
ATOM     79  O   GLU A  50      39.678  54.686  69.725  1.00 19.63           O  
ATOM     80  CB  GLU A  50      38.831  57.706  70.927  1.00 25.23           C  
ATOM     81  CG  GLU A  50      39.227  58.391  72.231  1.00 29.28           C  
ATOM     82  CD  GLU A  50      38.161  59.326  72.773  1.00 32.89           C  
ATOM     83  OE1 GLU A  50      36.960  58.986  72.693  1.00 34.63           O  
ATOM     84  OE2 GLU A  50      38.531  60.399  73.298  1.00 35.89           O  
ATOM     85  N   TYR A  51      38.948  56.197  68.220  1.00 19.43           N  
ATOM     86  CA  TYR A  51      38.461  55.179  67.303  1.00 19.72           C  
ATOM     87  C   TYR A  51      39.581  54.201  66.940  1.00 18.48           C  
ATOM     88  O   TYR A  51      39.382  52.987  66.944  1.00 19.79           O  
ATOM     89  CB  TYR A  51      37.927  55.832  66.024  1.00 19.77           C  
ATOM     90  CG  TYR A  51      37.545  54.837  64.951  1.00 20.35           C  
ATOM     91  CD1 TYR A  51      36.376  54.078  65.054  1.00 19.98           C  
ATOM     92  CD2 TYR A  51      38.363  54.638  63.842  1.00 20.13           C  
ATOM     93  CE1 TYR A  51      36.033  53.145  64.074  1.00 20.16           C  
ATOM     94  CE2 TYR A  51      38.033  53.708  62.858  1.00 21.53           C  
ATOM     95  CZ  TYR A  51      36.866  52.967  62.980  1.00 20.57           C  
ATOM     96  OH  TYR A  51      36.538  52.053  62.011  1.00 19.33           O  
ATOM     97  N   ASP A  52      40.760  54.734  66.637  1.00 20.94           N  
ATOM     98  CA  ASP A  52      41.889  53.897  66.236  1.00 23.21           C  
ATOM     99  C   ASP A  52      42.398  52.937  67.307  1.00 23.85           C  
ATOM    100  O   ASP A  52      42.600  51.751  67.037  1.00 23.74           O  
ATOM    101  CB  ASP A  52      43.052  54.766  65.748  1.00 25.46           C  
ATOM    102  CG  ASP A  52      44.149  53.945  65.092  1.00 31.10           C  
ATOM    103  OD1 ASP A  52      43.862  53.293  64.065  1.00 33.90           O  
ATOM    104  OD2 ASP A  52      45.293  53.941  65.597  1.00 31.88           O  
ATOM    105  N   ARG A  53      42.617  53.431  68.521  1.00 23.48           N  
ATOM    106  CA  ARG A  53      43.117  52.548  69.565  1.00 24.21           C  
ATOM    107  C   ARG A  53      42.107  51.474  69.959  1.00 22.21           C  
ATOM    108  O   ARG A  53      42.489  50.332  70.192  1.00 20.72           O  
ATOM    109  CB  ARG A  53      43.576  53.351  70.792  1.00 25.95           C  
ATOM    110  CG  ARG A  53      42.574  54.331  71.350  1.00 28.39           C  
ATOM    111  CD  ARG A  53      43.155  55.060  72.557  1.00 29.91           C  
ATOM    112  NE  ARG A  53      44.269  55.945  72.220  1.00 28.71           N  
ATOM    113  CZ  ARG A  53      44.211  57.273  72.280  1.00 29.24           C  
ATOM    114  NH1 ARG A  53      43.093  57.877  72.660  1.00 28.18           N  
ATOM    115  NH2 ARG A  53      45.278  58.001  71.982  1.00 30.94           N  
ATOM    116  N   THR A  54      40.824  51.823  70.010  1.00 20.97           N  
ATOM    117  CA  THR A  54      39.796  50.845  70.365  1.00 21.86           C  
ATOM    118  C   THR A  54      39.531  49.853  69.227  1.00 22.63           C  
ATOM    119  O   THR A  54      39.271  48.671  69.468  1.00 23.06           O  
ATOM    120  CB  THR A  54      38.457  51.528  70.752  1.00 22.90           C  
ATOM    121  OG1 THR A  54      37.996  52.349  69.673  1.00 24.14           O  
ATOM    122  CG2 THR A  54      38.637  52.389  72.006  1.00 22.66           C  
ATOM    123  N   SER A  55      39.597  50.331  67.988  1.00 22.84           N  
ATOM    124  CA  SER A  55      39.364  49.467  66.833  1.00 23.43           C  
ATOM    125  C   SER A  55      40.420  48.375  66.737  1.00 23.93           C  
ATOM    126  O   SER A  55      40.107  47.224  66.431  1.00 26.22           O  
ATOM    127  CB  SER A  55      39.358  50.290  65.542  1.00 20.63           C  
ATOM    128  OG  SER A  55      38.201  51.101  65.469  1.00 22.91           O  
ATOM    129  N   GLN A  56      41.671  48.739  66.996  1.00 25.11           N  
ATOM    130  CA  GLN A  56      42.764  47.777  66.934  1.00 27.65           C  
ATOM    131  C   GLN A  56      42.494  46.575  67.832  1.00 27.47           C  
ATOM    132  O   GLN A  56      42.700  45.430  67.430  1.00 27.09           O  
ATOM    133  CB  GLN A  56      44.076  48.441  67.349  1.00 29.31           C  
ATOM    134  CG  GLN A  56      44.611  49.434  66.340  1.00 34.89           C  
ATOM    135  CD  GLN A  56      45.901  50.079  66.797  1.00 38.51           C  
ATOM    136  OE1 GLN A  56      46.854  49.392  67.170  1.00 39.63           O  
ATOM    137  NE2 GLN A  56      45.942  51.407  66.766  1.00 40.39           N  
ATOM    138  N   VAL A  57      42.027  46.843  69.049  1.00 27.70           N  
ATOM    139  CA  VAL A  57      41.732  45.784  70.009  1.00 27.09           C  
ATOM    140  C   VAL A  57      40.531  44.933  69.597  1.00 26.88           C  
ATOM    141  O   VAL A  57      40.628  43.711  69.537  1.00 26.76           O  
ATOM    142  CB  VAL A  57      41.457  46.363  71.418  1.00 28.38           C  
ATOM    143  CG1 VAL A  57      41.137  45.231  72.392  1.00 28.68           C  
ATOM    144  CG2 VAL A  57      42.666  47.156  71.902  1.00 28.04           C  
ATOM    145  N   VAL A  58      39.403  45.577  69.318  1.00 25.88           N  
ATOM    146  CA  VAL A  58      38.199  44.852  68.928  1.00 26.99           C  
ATOM    147  C   VAL A  58      38.375  44.071  67.616  1.00 27.29           C  
ATOM    148  O   VAL A  58      37.906  42.937  67.497  1.00 25.50           O  
ATOM    149  CB  VAL A  58      36.985  45.813  68.803  1.00 27.18           C  
ATOM    150  CG1 VAL A  58      37.315  46.950  67.862  1.00 32.87           C  
ATOM    151  CG2 VAL A  58      35.765  45.060  68.306  1.00 31.36           C  
ATOM    152  N   TRP A  59      39.048  44.674  66.637  1.00 26.45           N  
ATOM    153  CA  TRP A  59      39.273  44.010  65.354  1.00 27.47           C  
ATOM    154  C   TRP A  59      40.243  42.846  65.510  1.00 27.07           C  
ATOM    155  O   TRP A  59      40.121  41.831  64.824  1.00 27.40           O  
ATOM    156  CB  TRP A  59      39.817  45.003  64.325  1.00 29.71           C  
ATOM    157  CG  TRP A  59      38.809  46.020  63.873  1.00 33.63           C  
ATOM    158  CD1 TRP A  59      37.656  46.375  64.513  1.00 34.94           C  
ATOM    159  CD2 TRP A  59      38.891  46.847  62.707  1.00 35.80           C  
ATOM    160  NE1 TRP A  59      37.015  47.373  63.819  1.00 36.40           N  
ATOM    161  CE2 TRP A  59      37.752  47.684  62.707  1.00 37.41           C  
ATOM    162  CE3 TRP A  59      39.817  46.965  61.663  1.00 37.42           C  
ATOM    163  CZ2 TRP A  59      37.514  48.629  61.700  1.00 38.33           C  
ATOM    164  CZ3 TRP A  59      39.582  47.906  60.661  1.00 39.67           C  
ATOM    165  CH2 TRP A  59      38.437  48.726  60.690  1.00 40.02           C  
ATOM    166  N   ASN A  60      41.210  42.991  66.409  1.00 25.74           N  
ATOM    167  CA  ASN A  60      42.167  41.920  66.634  1.00 26.47           C  
ATOM    168  C   ASN A  60      41.442  40.705  67.196  1.00 27.08           C  
ATOM    169  O   ASN A  60      41.697  39.574  66.780  1.00 26.40           O  
ATOM    170  CB  ASN A  60      43.271  42.364  67.597  1.00 26.15           C  
ATOM    171  CG  ASN A  60      44.156  41.212  68.033  1.00 29.44           C  
ATOM    172  OD1 ASN A  60      43.840  40.502  68.987  1.00 30.76           O  
ATOM    173  ND2 ASN A  60      45.261  41.005  67.319  1.00 28.75           N  
ATOM    174  N   GLU A  61      40.533  40.942  68.138  1.00 26.14           N  
ATOM    175  CA  GLU A  61      39.768  39.858  68.734  1.00 27.35           C  
ATOM    176  C   GLU A  61      38.881  39.174  67.705  1.00 25.71           C  
ATOM    177  O   GLU A  61      38.777  37.952  67.689  1.00 25.50           O  
ATOM    178  CB  GLU A  61      38.906  40.378  69.888  1.00 30.98           C  
ATOM    179  CG  GLU A  61      39.643  40.460  71.214  1.00 37.75           C  
ATOM    180  CD  GLU A  61      38.847  41.182  72.288  1.00 40.97           C  
ATOM    181  OE1 GLU A  61      37.654  40.855  72.466  1.00 43.05           O  
ATOM    182  OE2 GLU A  61      39.421  42.070  72.955  1.00 41.95           O  
ATOM    183  N   TYR A  62      38.238  39.961  66.849  1.00 25.38           N  
ATOM    184  CA  TYR A  62      37.367  39.396  65.825  1.00 25.52           C  
ATOM    185  C   TYR A  62      38.161  38.501  64.878  1.00 23.80           C  
ATOM    186  O   TYR A  62      37.725  37.404  64.528  1.00 24.56           O  
ATOM    187  CB  TYR A  62      36.693  40.503  65.012  1.00 25.32           C  
ATOM    188  CG  TYR A  62      35.790  39.961  63.929  1.00 28.08           C  
ATOM    189  CD1 TYR A  62      34.578  39.348  64.248  1.00 28.32           C  
ATOM    190  CD2 TYR A  62      36.165  40.021  62.588  1.00 29.39           C  
ATOM    191  CE1 TYR A  62      33.761  38.804  63.260  1.00 31.75           C  
ATOM    192  CE2 TYR A  62      35.355  39.477  61.589  1.00 33.01           C  
ATOM    193  CZ  TYR A  62      34.155  38.872  61.933  1.00 33.10           C  
ATOM    194  OH  TYR A  62      33.354  38.334  60.952  1.00 36.34           O  
ATOM    195  N   ALA A  63      39.325  38.984  64.461  1.00 23.33           N  
ATOM    196  CA  ALA A  63      40.184  38.241  63.552  1.00 24.84           C  
ATOM    197  C   ALA A  63      40.526  36.876  64.143  1.00 24.40           C  
ATOM    198  O   ALA A  63      40.589  35.876  63.427  1.00 23.49           O  
ATOM    199  CB  ALA A  63      41.461  39.034  63.274  1.00 22.84           C  
ATOM    200  N   GLU A  64      40.739  36.840  65.454  1.00 25.55           N  
ATOM    201  CA  GLU A  64      41.069  35.593  66.136  1.00 25.36           C  
ATOM    202  C   GLU A  64      39.928  34.593  66.007  1.00 24.83           C  
ATOM    203  O   GLU A  64      40.138  33.440  65.630  1.00 26.02           O  
ATOM    204  CB  GLU A  64      41.361  35.864  67.609  1.00 30.67           C  
ATOM    205  N   ALA A  65      38.718  35.038  66.326  1.00 23.74           N  
ATOM    206  CA  ALA A  65      37.547  34.177  66.244  1.00 23.43           C  
ATOM    207  C   ALA A  65      37.284  33.742  64.803  1.00 23.35           C  
ATOM    208  O   ALA A  65      36.934  32.589  64.545  1.00 22.60           O  
ATOM    209  CB  ALA A  65      36.329  34.904  66.794  1.00 22.21           C  
ATOM    210  N   ASN A  66      37.451  34.673  63.870  1.00 21.81           N  
ATOM    211  CA  ASN A  66      37.224  34.389  62.456  1.00 22.42           C  
ATOM    212  C   ASN A  66      38.257  33.373  61.965  1.00 21.42           C  
ATOM    213  O   ASN A  66      37.941  32.480  61.183  1.00 22.56           O  
ATOM    214  CB  ASN A  66      37.308  35.695  61.651  1.00 21.62           C  
ATOM    215  CG  ASN A  66      36.768  35.553  60.241  1.00 22.75           C  
ATOM    216  OD1 ASN A  66      35.968  34.660  59.955  1.00 22.10           O  
ATOM    217  ND2 ASN A  66      37.186  36.450  59.356  1.00 21.12           N  
ATOM    218  N   TRP A  67      39.490  33.502  62.447  1.00 22.34           N  
ATOM    219  CA  TRP A  67      40.552  32.585  62.059  1.00 22.66           C  
ATOM    220  C   TRP A  67      40.286  31.170  62.578  1.00 23.96           C  
ATOM    221  O   TRP A  67      40.444  30.190  61.840  1.00 22.16           O  
ATOM    222  CB  TRP A  67      41.901  33.085  62.583  1.00 22.16           C  
ATOM    223  CG  TRP A  67      43.016  32.098  62.384  1.00 23.43           C  
ATOM    224  CD1 TRP A  67      43.381  31.086  63.229  1.00 25.02           C  
ATOM    225  CD2 TRP A  67      43.883  32.003  61.246  1.00 22.99           C  
ATOM    226  NE1 TRP A  67      44.421  30.365  62.686  1.00 25.09           N  
ATOM    227  CE2 TRP A  67      44.749  30.907  61.470  1.00 24.37           C  
ATOM    228  CE3 TRP A  67      44.010  32.735  60.055  1.00 21.19           C  
ATOM    229  CZ2 TRP A  67      45.733  30.526  60.547  1.00 23.12           C  
ATOM    230  CZ3 TRP A  67      44.989  32.354  59.134  1.00 21.49           C  
ATOM    231  CH2 TRP A  67      45.837  31.258  59.389  1.00 20.86           C  
ATOM    232  N   ASN A  68      39.876  31.071  63.841  1.00 24.47           N  
ATOM    233  CA  ASN A  68      39.596  29.770  64.455  1.00 26.36           C  
ATOM    234  C   ASN A  68      38.480  29.026  63.724  1.00 25.35           C  
ATOM    235  O   ASN A  68      38.523  27.802  63.588  1.00 23.96           O  
ATOM    236  CB  ASN A  68      39.230  29.936  65.937  1.00 27.31           C  
ATOM    237  CG  ASN A  68      40.368  30.524  66.760  1.00 29.77           C  
ATOM    238  OD1 ASN A  68      41.537  30.432  66.382  1.00 28.77           O  
ATOM    239  ND2 ASN A  68      40.028  31.119  67.899  1.00 30.82           N  
ATOM    240  N   TYR A  69      37.477  29.762  63.258  1.00 24.11           N  
ATOM    241  CA  TYR A  69      36.380  29.145  62.518  1.00 24.41           C  
ATOM    242  C   TYR A  69      36.892  28.674  61.157  1.00 24.55           C  
ATOM    243  O   TYR A  69      36.698  27.521  60.770  1.00 23.28           O  
ATOM    244  CB  TYR A  69      35.242  30.153  62.308  1.00 27.59           C  
ATOM    245  CG  TYR A  69      34.348  29.829  61.127  1.00 28.29           C  
ATOM    246  CD1 TYR A  69      33.375  28.834  61.209  1.00 30.33           C  
ATOM    247  CD2 TYR A  69      34.508  30.494  59.912  1.00 31.13           C  
ATOM    248  CE1 TYR A  69      32.581  28.505  60.101  1.00 29.75           C  
ATOM    249  CE2 TYR A  69      33.725  30.174  58.800  1.00 31.87           C  
ATOM    250  CZ  TYR A  69      32.765  29.180  58.902  1.00 32.09           C  
ATOM    251  OH  TYR A  69      31.995  28.868  57.799  1.00 31.48           O  
ATOM    252  N   ASN A  70      37.538  29.588  60.436  1.00 22.98           N  
ATOM    253  CA  ASN A  70      38.083  29.312  59.111  1.00 21.52           C  
ATOM    254  C   ASN A  70      39.048  28.130  59.074  1.00 22.49           C  
ATOM    255  O   ASN A  70      39.092  27.398  58.085  1.00 22.22           O  
ATOM    256  CB  ASN A  70      38.799  30.555  58.573  1.00 22.42           C  
ATOM    257  CG  ASN A  70      37.883  31.452  57.766  1.00 20.70           C  
ATOM    258  OD1 ASN A  70      37.843  31.369  56.541  1.00 20.36           O  
ATOM    259  ND2 ASN A  70      37.131  32.307  58.452  1.00 20.18           N  
ATOM    260  N   THR A  71      39.821  27.953  60.144  1.00 21.87           N  
ATOM    261  CA  THR A  71      40.799  26.866  60.209  1.00 23.29           C  
ATOM    262  C   THR A  71      40.332  25.682  61.055  1.00 25.33           C  
ATOM    263  O   THR A  71      41.100  24.755  61.312  1.00 26.63           O  
ATOM    264  CB  THR A  71      42.153  27.364  60.773  1.00 22.46           C  
ATOM    265  OG1 THR A  71      41.985  27.779  62.132  1.00 21.26           O  
ATOM    266  CG2 THR A  71      42.675  28.544  59.956  1.00 22.88           C  
ATOM    267  N   ASN A  72      39.073  25.709  61.478  1.00 26.22           N  
ATOM    268  CA  ASN A  72      38.513  24.633  62.293  1.00 27.70           C  
ATOM    269  C   ASN A  72      37.005  24.834  62.382  1.00 26.39           C  
ATOM    270  O   ASN A  72      36.486  25.297  63.395  1.00 28.11           O  
ATOM    271  CB  ASN A  72      39.154  24.648  63.691  1.00 28.15           C  
ATOM    272  CG  ASN A  72      38.674  23.499  64.576  1.00 31.04           C  
ATOM    273  OD1 ASN A  72      38.244  22.457  64.074  1.00 29.17           O  
ATOM    274  ND2 ASN A  72      38.761  23.701  65.892  1.00 32.86           N  
ATOM    275  N   ILE A  73      36.312  24.487  61.304  1.00 27.62           N  
ATOM    276  CA  ILE A  73      34.864  24.640  61.225  1.00 28.58           C  
ATOM    277  C   ILE A  73      34.128  23.655  62.127  1.00 30.90           C  
ATOM    278  O   ILE A  73      34.063  22.460  61.839  1.00 31.19           O  
ATOM    279  CB  ILE A  73      34.370  24.456  59.770  1.00 28.41           C  
ATOM    280  CG1 ILE A  73      35.032  25.498  58.861  1.00 28.67           C  
ATOM    281  CG2 ILE A  73      32.849  24.581  59.710  1.00 29.27           C  
ATOM    282  CD1 ILE A  73      34.674  25.359  57.387  1.00 27.85           C  
ATOM    283  N   THR A  74      33.579  24.171  63.222  1.00 32.51           N  
ATOM    284  CA  THR A  74      32.831  23.360  64.177  1.00 33.92           C  
ATOM    285  C   THR A  74      31.649  24.176  64.677  1.00 34.62           C  
ATOM    286  O   THR A  74      31.575  25.384  64.450  1.00 34.35           O  
ATOM    287  CB  THR A  74      33.688  22.982  65.399  1.00 34.56           C  
ATOM    288  OG1 THR A  74      34.015  24.169  66.133  1.00 35.94           O  
ATOM    289  CG2 THR A  74      34.972  22.284  64.965  1.00 33.74           C  
ATOM    290  N   THR A  75      30.722  23.518  65.360  1.00 34.69           N  
ATOM    291  CA  THR A  75      29.564  24.220  65.889  1.00 35.91           C  
ATOM    292  C   THR A  75      30.041  25.219  66.945  1.00 35.21           C  
ATOM    293  O   THR A  75      29.499  26.318  67.069  1.00 34.43           O  
ATOM    294  CB  THR A  75      28.546  23.229  66.510  1.00 36.94           C  
ATOM    295  OG1 THR A  75      27.453  23.956  67.085  1.00 40.00           O  
ATOM    296  CG2 THR A  75      29.205  22.386  67.582  1.00 36.78           C  
ATOM    297  N   GLU A  76      31.084  24.840  67.679  1.00 35.12           N  
ATOM    298  CA  GLU A  76      31.638  25.692  68.725  1.00 35.53           C  
ATOM    299  C   GLU A  76      32.309  26.957  68.180  1.00 34.45           C  
ATOM    300  O   GLU A  76      32.003  28.066  68.623  1.00 32.19           O  
ATOM    301  CB  GLU A  76      32.640  24.905  69.576  1.00 38.54           C  
ATOM    302  CG  GLU A  76      32.084  23.613  70.185  1.00 44.28           C  
ATOM    303  CD  GLU A  76      32.317  22.385  69.310  1.00 47.02           C  
ATOM    304  OE1 GLU A  76      31.828  22.356  68.161  1.00 48.87           O  
ATOM    305  OE2 GLU A  76      32.998  21.444  69.775  1.00 50.21           O  
ATOM    306  N   THR A  77      33.227  26.796  67.229  1.00 33.18           N  
ATOM    307  CA  THR A  77      33.913  27.949  66.651  1.00 32.17           C  
ATOM    308  C   THR A  77      32.925  28.834  65.897  1.00 31.26           C  
ATOM    309  O   THR A  77      33.107  30.045  65.815  1.00 30.78           O  
ATOM    310  CB  THR A  77      35.048  27.527  65.687  1.00 31.68           C  
ATOM    311  OG1 THR A  77      34.528  26.660  64.673  1.00 31.48           O  
ATOM    312  CG2 THR A  77      36.157  26.818  66.452  1.00 31.84           C  
ATOM    313  N   SER A  78      31.878  28.228  65.347  1.00 31.59           N  
ATOM    314  CA  SER A  78      30.865  28.989  64.623  1.00 32.27           C  
ATOM    315  C   SER A  78      30.094  29.863  65.602  1.00 33.27           C  
ATOM    316  O   SER A  78      29.871  31.046  65.352  1.00 31.52           O  
ATOM    317  CB  SER A  78      29.888  28.054  63.905  1.00 32.03           C  
ATOM    318  OG  SER A  78      30.511  27.388  62.819  1.00 33.62           O  
ATOM    319  N   LYS A  79      29.695  29.268  66.722  1.00 34.58           N  
ATOM    320  CA  LYS A  79      28.943  29.985  67.741  1.00 36.62           C  
ATOM    321  C   LYS A  79      29.755  31.162  68.279  1.00 35.77           C  
ATOM    322  O   LYS A  79      29.234  32.264  68.449  1.00 36.40           O  
ATOM    323  CB  LYS A  79      28.570  29.031  68.880  1.00 39.13           C  
ATOM    324  CG  LYS A  79      27.494  29.561  69.819  1.00 43.25           C  
ATOM    325  CD  LYS A  79      27.052  28.487  70.807  1.00 46.60           C  
ATOM    326  CE  LYS A  79      25.859  28.943  71.639  1.00 48.32           C  
ATOM    327  NZ  LYS A  79      25.369  27.861  72.547  1.00 49.35           N  
ATOM    328  N   ILE A  80      31.037  30.927  68.535  1.00 34.36           N  
ATOM    329  CA  ILE A  80      31.909  31.974  69.054  1.00 33.18           C  
ATOM    330  C   ILE A  80      32.073  33.107  68.044  1.00 32.41           C  
ATOM    331  O   ILE A  80      32.075  34.284  68.410  1.00 32.05           O  
ATOM    332  CB  ILE A  80      33.296  31.410  69.408  1.00 33.61           C  
ATOM    333  CG1 ILE A  80      33.154  30.364  70.517  1.00 34.16           C  
ATOM    334  CG2 ILE A  80      34.226  32.537  69.837  1.00 33.24           C  
ATOM    335  CD1 ILE A  80      34.458  29.696  70.907  1.00 33.43           C  
ATOM    336  N   LEU A  81      32.212  32.749  66.772  1.00 30.05           N  
ATOM    337  CA  LEU A  81      32.364  33.752  65.731  1.00 28.87           C  
ATOM    338  C   LEU A  81      31.127  34.645  65.672  1.00 28.87           C  
ATOM    339  O   LEU A  81      31.243  35.867  65.612  1.00 27.96           O  
ATOM    340  CB  LEU A  81      32.591  33.084  64.371  1.00 28.19           C  
ATOM    341  CG  LEU A  81      32.709  34.015  63.157  1.00 28.67           C  
ATOM    342  CD1 LEU A  81      33.778  35.063  63.405  1.00 28.05           C  
ATOM    343  CD2 LEU A  81      33.035  33.198  61.918  1.00 27.39           C  
ATOM    344  N   LEU A  82      29.942  34.040  65.700  1.00 28.83           N  
ATOM    345  CA  LEU A  82      28.710  34.821  65.641  1.00 29.55           C  
ATOM    346  C   LEU A  82      28.595  35.772  66.827  1.00 30.99           C  
ATOM    347  O   LEU A  82      28.035  36.861  66.703  1.00 30.68           O  
ATOM    348  CB  LEU A  82      27.488  33.897  65.581  1.00 28.66           C  
ATOM    349  CG  LEU A  82      27.358  33.047  64.313  1.00 27.25           C  
ATOM    350  CD1 LEU A  82      26.146  32.144  64.423  1.00 28.60           C  
ATOM    351  CD2 LEU A  82      27.238  33.955  63.090  1.00 29.42           C  
ATOM    352  N   GLN A  83      29.134  35.364  67.973  1.00 32.59           N  
ATOM    353  CA  GLN A  83      29.096  36.205  69.164  1.00 34.05           C  
ATOM    354  C   GLN A  83      30.056  37.375  68.992  1.00 33.41           C  
ATOM    355  O   GLN A  83      29.746  38.500  69.380  1.00 33.15           O  
ATOM    356  CB  GLN A  83      29.461  35.393  70.414  1.00 35.86           C  
ATOM    357  CG  GLN A  83      28.397  34.363  70.797  1.00 41.83           C  
ATOM    358  CD  GLN A  83      28.802  33.483  71.970  1.00 44.71           C  
ATOM    359  OE1 GLN A  83      29.028  33.966  73.080  1.00 47.69           O  
ATOM    360  NE2 GLN A  83      28.892  32.180  71.726  1.00 47.51           N  
ATOM    361  N   LYS A  84      31.222  37.114  68.409  1.00 33.19           N  
ATOM    362  CA  LYS A  84      32.194  38.177  68.185  1.00 33.34           C  
ATOM    363  C   LYS A  84      31.655  39.180  67.172  1.00 32.53           C  
ATOM    364  O   LYS A  84      32.033  40.351  67.192  1.00 30.99           O  
ATOM    365  CB  LYS A  84      33.527  37.604  67.695  1.00 35.03           C  
ATOM    366  CG  LYS A  84      34.397  37.022  68.802  1.00 39.16           C  
ATOM    367  CD  LYS A  84      34.872  38.111  69.757  1.00 41.08           C  
ATOM    368  CE  LYS A  84      35.682  37.534  70.912  1.00 43.92           C  
ATOM    369  NZ  LYS A  84      36.142  38.597  71.855  1.00 43.32           N  
ATOM    370  N   ASN A  85      30.779  38.717  66.283  1.00 33.42           N  
ATOM    371  CA  ASN A  85      30.180  39.597  65.279  1.00 34.57           C  
ATOM    372  C   ASN A  85      29.404  40.694  66.001  1.00 34.49           C  
ATOM    373  O   ASN A  85      29.531  41.874  65.683  1.00 33.34           O  
ATOM    374  CB  ASN A  85      29.219  38.820  64.368  1.00 36.23           C  
ATOM    375  CG  ASN A  85      29.938  37.996  63.314  1.00 37.73           C  
ATOM    376  OD1 ASN A  85      30.671  38.530  62.479  1.00 37.42           O  
ATOM    377  ND2 ASN A  85      29.719  36.685  63.340  1.00 41.84           N  
ATOM    378  N   MET A  86      28.597  40.286  66.975  1.00 34.71           N  
ATOM    379  CA  MET A  86      27.794  41.217  67.757  1.00 36.39           C  
ATOM    380  C   MET A  86      28.670  42.228  68.488  1.00 35.39           C  
ATOM    381  O   MET A  86      28.320  43.402  68.590  1.00 34.85           O  
ATOM    382  CB  MET A  86      26.943  40.448  68.772  1.00 39.17           C  
ATOM    383  CG  MET A  86      25.518  40.138  68.319  1.00 43.08           C  
ATOM    384  SD  MET A  86      25.294  40.020  66.531  1.00 49.27           S  
ATOM    385  CE  MET A  86      23.829  41.035  66.302  1.00 47.42           C  
ATOM    386  N   GLN A  87      29.814  41.772  68.989  1.00 34.91           N  
ATOM    387  CA  GLN A  87      30.722  42.648  69.719  1.00 35.11           C  
ATOM    388  C   GLN A  87      31.352  43.714  68.831  1.00 32.85           C  
ATOM    389  O   GLN A  87      31.371  44.895  69.188  1.00 31.35           O  
ATOM    390  CB  GLN A  87      31.818  41.826  70.405  1.00 38.55           C  
ATOM    391  CG  GLN A  87      31.278  40.731  71.319  1.00 44.24           C  
ATOM    392  CD  GLN A  87      32.340  40.138  72.229  1.00 47.30           C  
ATOM    393  OE1 GLN A  87      33.397  39.702  71.771  1.00 49.53           O  
ATOM    394  NE2 GLN A  87      32.060  40.115  73.528  1.00 47.80           N  
ATOM    395  N   ILE A  88      31.869  43.308  67.676  1.00 29.57           N  
ATOM    396  CA  ILE A  88      32.492  44.269  66.776  1.00 28.83           C  
ATOM    397  C   ILE A  88      31.435  45.195  66.179  1.00 26.91           C  
ATOM    398  O   ILE A  88      31.709  46.358  65.872  1.00 25.48           O  
ATOM    399  CB  ILE A  88      33.274  43.563  65.644  1.00 29.00           C  
ATOM    400  CG1 ILE A  88      34.063  44.599  64.844  1.00 31.09           C  
ATOM    401  CG2 ILE A  88      32.319  42.794  64.742  1.00 29.58           C  
ATOM    402  CD1 ILE A  88      35.045  43.992  63.864  1.00 33.97           C  
ATOM    403  N   ALA A  89      30.220  44.683  66.024  1.00 25.38           N  
ATOM    404  CA  ALA A  89      29.135  45.492  65.482  1.00 26.14           C  
ATOM    405  C   ALA A  89      28.790  46.568  66.509  1.00 25.83           C  
ATOM    406  O   ALA A  89      28.566  47.727  66.165  1.00 25.53           O  
ATOM    407  CB  ALA A  89      27.918  44.623  65.202  1.00 24.25           C  
ATOM    408  N   ASN A  90      28.755  46.178  67.778  1.00 25.13           N  
ATOM    409  CA  ASN A  90      28.443  47.131  68.834  1.00 25.64           C  
ATOM    410  C   ASN A  90      29.474  48.256  68.843  1.00 23.48           C  
ATOM    411  O   ASN A  90      29.131  49.421  69.052  1.00 24.86           O  
ATOM    412  CB  ASN A  90      28.407  46.426  70.191  1.00 28.05           C  
ATOM    413  CG  ASN A  90      27.945  47.341  71.304  1.00 33.48           C  
ATOM    414  OD1 ASN A  90      28.666  48.256  71.704  1.00 37.03           O  
ATOM    415  ND2 ASN A  90      26.732  47.107  71.797  1.00 35.02           N  
ATOM    416  N   HIS A  91      30.735  47.910  68.603  1.00 21.49           N  
ATOM    417  CA  HIS A  91      31.799  48.908  68.565  1.00 21.72           C  
ATOM    418  C   HIS A  91      31.624  49.822  67.354  1.00 22.77           C  
ATOM    419  O   HIS A  91      31.801  51.041  67.445  1.00 21.87           O  
ATOM    420  CB  HIS A  91      33.171  48.227  68.499  1.00 21.96           C  
ATOM    421  CG  HIS A  91      34.297  49.165  68.190  1.00 23.78           C  
ATOM    422  ND1 HIS A  91      34.694  49.456  66.901  1.00 25.06           N  
ATOM    423  CD2 HIS A  91      35.094  49.902  69.002  1.00 22.69           C  
ATOM    424  CE1 HIS A  91      35.684  50.330  66.934  1.00 24.61           C  
ATOM    425  NE2 HIS A  91      35.946  50.618  68.197  1.00 22.29           N  
ATOM    426  N   THR A  92      31.278  49.224  66.218  1.00 20.58           N  
ATOM    427  CA  THR A  92      31.083  49.979  64.987  1.00 21.80           C  
ATOM    428  C   THR A  92      29.905  50.940  65.128  1.00 21.91           C  
ATOM    429  O   THR A  92      29.972  52.085  64.692  1.00 21.95           O  
ATOM    430  CB  THR A  92      30.823  49.034  63.795  1.00 22.75           C  
ATOM    431  OG1 THR A  92      31.945  48.155  63.632  1.00 22.95           O  
ATOM    432  CG2 THR A  92      30.618  49.832  62.509  1.00 23.24           C  
ATOM    433  N   LEU A  93      28.829  50.468  65.747  1.00 23.43           N  
ATOM    434  CA  LEU A  93      27.643  51.291  65.945  1.00 24.99           C  
ATOM    435  C   LEU A  93      27.953  52.501  66.830  1.00 25.57           C  
ATOM    436  O   LEU A  93      27.559  53.628  66.526  1.00 23.70           O  
ATOM    437  CB  LEU A  93      26.538  50.458  66.590  1.00 27.24           C  
ATOM    438  CG  LEU A  93      25.215  51.170  66.870  1.00 29.20           C  
ATOM    439  CD1 LEU A  93      24.575  51.621  65.556  1.00 31.28           C  
ATOM    440  CD2 LEU A  93      24.294  50.228  67.622  1.00 30.06           C  
ATOM    441  N   LYS A  94      28.664  52.256  67.924  1.00 24.93           N  
ATOM    442  CA  LYS A  94      29.018  53.316  68.855  1.00 26.17           C  
ATOM    443  C   LYS A  94      29.830  54.422  68.192  1.00 25.74           C  
ATOM    444  O   LYS A  94      29.455  55.593  68.244  1.00 25.50           O  
ATOM    445  CB  LYS A  94      29.818  52.747  70.026  1.00 27.56           C  
ATOM    446  CG  LYS A  94      30.174  53.788  71.072  1.00 32.44           C  
ATOM    447  CD  LYS A  94      31.157  53.249  72.093  1.00 34.92           C  
ATOM    448  CE  LYS A  94      31.464  54.302  73.144  1.00 38.23           C  
ATOM    449  NZ  LYS A  94      31.907  55.587  72.522  1.00 40.02           N  
ATOM    450  N   TYR A  95      30.948  54.053  67.575  1.00 23.64           N  
ATOM    451  CA  TYR A  95      31.793  55.044  66.930  1.00 23.63           C  
ATOM    452  C   TYR A  95      31.199  55.594  65.644  1.00 23.81           C  
ATOM    453  O   TYR A  95      31.426  56.756  65.303  1.00 24.01           O  
ATOM    454  CB  TYR A  95      33.193  54.477  66.688  1.00 23.98           C  
ATOM    455  CG  TYR A  95      34.005  54.436  67.961  1.00 24.33           C  
ATOM    456  CD1 TYR A  95      33.877  53.380  68.865  1.00 24.10           C  
ATOM    457  CD2 TYR A  95      34.822  55.509  68.314  1.00 25.19           C  
ATOM    458  CE1 TYR A  95      34.539  53.401  70.094  1.00 24.70           C  
ATOM    459  CE2 TYR A  95      35.484  55.540  69.534  1.00 25.45           C  
ATOM    460  CZ  TYR A  95      35.337  54.489  70.420  1.00 24.76           C  
ATOM    461  OH  TYR A  95      35.971  54.545  71.640  1.00 26.84           O  
ATOM    462  N   GLY A  96      30.426  54.764  64.945  1.00 23.08           N  
ATOM    463  CA  GLY A  96      29.791  55.198  63.713  1.00 22.50           C  
ATOM    464  C   GLY A  96      28.741  56.255  63.994  1.00 23.32           C  
ATOM    465  O   GLY A  96      28.616  57.237  63.259  1.00 21.48           O  
ATOM    466  N   THR A  97      27.981  56.050  65.066  1.00 24.15           N  
ATOM    467  CA  THR A  97      26.945  56.996  65.468  1.00 25.03           C  
ATOM    468  C   THR A  97      27.601  58.332  65.821  1.00 25.94           C  
ATOM    469  O   THR A  97      27.138  59.390  65.397  1.00 26.44           O  
ATOM    470  CB  THR A  97      26.166  56.474  66.687  1.00 24.73           C  
ATOM    471  OG1 THR A  97      25.558  55.221  66.357  1.00 25.50           O  
ATOM    472  CG2 THR A  97      25.088  57.468  67.103  1.00 23.72           C  
ATOM    473  N   GLN A  98      28.680  58.275  66.597  1.00 27.23           N  
ATOM    474  CA  GLN A  98      29.408  59.481  66.980  1.00 28.25           C  
ATOM    475  C   GLN A  98      29.943  60.182  65.737  1.00 27.53           C  
ATOM    476  O   GLN A  98      29.824  61.399  65.601  1.00 26.41           O  
ATOM    477  CB  GLN A  98      30.587  59.138  67.901  1.00 32.26           C  
ATOM    478  CG  GLN A  98      30.285  59.178  69.396  1.00 38.49           C  
ATOM    479  CD  GLN A  98      31.487  58.779  70.249  1.00 42.52           C  
ATOM    480  OE1 GLN A  98      31.786  57.594  70.412  1.00 44.86           O  
ATOM    481  NE2 GLN A  98      32.187  59.772  70.787  1.00 45.22           N  
ATOM    482  N   ALA A  99      30.531  59.405  64.831  1.00 25.80           N  
ATOM    483  CA  ALA A  99      31.104  59.944  63.600  1.00 24.69           C  
ATOM    484  C   ALA A  99      30.100  60.729  62.757  1.00 25.28           C  
ATOM    485  O   ALA A  99      30.448  61.739  62.141  1.00 24.63           O  
ATOM    486  CB  ALA A  99      31.699  58.810  62.766  1.00 25.45           C  
ATOM    487  N   ARG A 100      28.860  60.256  62.723  1.00 24.09           N  
ATOM    488  CA  ARG A 100      27.819  60.908  61.945  1.00 26.32           C  
ATOM    489  C   ARG A 100      27.398  62.254  62.519  1.00 27.69           C  
ATOM    490  O   ARG A 100      26.722  63.033  61.848  1.00 27.22           O  
ATOM    491  CB  ARG A 100      26.600  59.994  61.836  1.00 25.28           C  
ATOM    492  CG  ARG A 100      26.859  58.750  61.015  1.00 26.20           C  
ATOM    493  CD  ARG A 100      25.613  57.904  60.897  1.00 26.32           C  
ATOM    494  NE  ARG A 100      25.805  56.792  59.972  1.00 25.16           N  
ATOM    495  CZ  ARG A 100      24.853  55.925  59.648  1.00 26.49           C  
ATOM    496  NH1 ARG A 100      23.640  56.041  60.180  1.00 25.08           N  
ATOM    497  NH2 ARG A 100      25.108  54.953  58.780  1.00 27.31           N  
ATOM    498  N   LYS A 101      27.792  62.524  63.758  1.00 28.78           N  
ATOM    499  CA  LYS A 101      27.444  63.785  64.397  1.00 31.07           C  
ATOM    500  C   LYS A 101      28.371  64.906  63.946  1.00 30.99           C  
ATOM    501  O   LYS A 101      28.104  66.082  64.194  1.00 30.45           O  
ATOM    502  CB  LYS A 101      27.480  63.629  65.920  1.00 32.98           C  
ATOM    503  CG  LYS A 101      26.404  62.682  66.437  1.00 37.31           C  
ATOM    504  CD  LYS A 101      26.517  62.422  67.931  1.00 40.01           C  
ATOM    505  CE  LYS A 101      25.419  61.469  68.386  1.00 42.18           C  
ATOM    506  NZ  LYS A 101      25.551  61.088  69.821  1.00 44.23           N  
ATOM    507  N   PHE A 102      29.461  64.543  63.278  1.00 31.38           N  
ATOM    508  CA  PHE A 102      30.401  65.542  62.776  1.00 32.92           C  
ATOM    509  C   PHE A 102      29.970  65.978  61.390  1.00 33.66           C  
ATOM    510  O   PHE A 102      29.487  65.165  60.601  1.00 33.46           O  
ATOM    511  CB  PHE A 102      31.825  64.980  62.665  1.00 32.55           C  
ATOM    512  CG  PHE A 102      32.531  64.825  63.977  1.00 32.74           C  
ATOM    513  CD1 PHE A 102      32.357  63.682  64.746  1.00 33.65           C  
ATOM    514  CD2 PHE A 102      33.376  65.828  64.444  1.00 34.44           C  
ATOM    515  CE1 PHE A 102      33.017  63.535  65.965  1.00 35.01           C  
ATOM    516  CE2 PHE A 102      34.041  65.695  65.664  1.00 34.23           C  
ATOM    517  CZ  PHE A 102      33.861  64.546  66.425  1.00 35.80           C  
ATOM    518  N   ASP A 103      30.136  67.262  61.095  1.00 34.13           N  
ATOM    519  CA  ASP A 103      29.804  67.769  59.772  1.00 34.82           C  
ATOM    520  C   ASP A 103      31.121  67.737  59.014  1.00 34.27           C  
ATOM    521  O   ASP A 103      31.909  68.677  59.089  1.00 34.87           O  
ATOM    522  CB  ASP A 103      29.286  69.209  59.836  1.00 35.44           C  
ATOM    523  CG  ASP A 103      28.831  69.724  58.477  1.00 35.56           C  
ATOM    524  OD1 ASP A 103      29.439  69.336  57.459  1.00 36.13           O  
ATOM    525  OD2 ASP A 103      27.873  70.522  58.425  1.00 36.65           O  
ATOM    526  N   VAL A 104      31.361  66.644  58.298  1.00 35.15           N  
ATOM    527  CA  VAL A 104      32.595  66.478  57.540  1.00 35.95           C  
ATOM    528  C   VAL A 104      32.915  67.682  56.660  1.00 36.83           C  
ATOM    529  O   VAL A 104      34.084  67.983  56.415  1.00 36.31           O  
ATOM    530  CB  VAL A 104      32.530  65.218  56.657  1.00 36.58           C  
ATOM    531  CG1 VAL A 104      33.794  65.095  55.833  1.00 37.87           C  
ATOM    532  CG2 VAL A 104      32.355  63.988  57.530  1.00 36.85           C  
ATOM    533  N   ASN A 105      31.880  68.371  56.189  1.00 37.34           N  
ATOM    534  CA  ASN A 105      32.077  69.540  55.340  1.00 39.98           C  
ATOM    535  C   ASN A 105      32.851  70.639  56.061  1.00 41.21           C  
ATOM    536  O   ASN A 105      33.593  71.396  55.437  1.00 42.44           O  
ATOM    537  CB  ASN A 105      30.729  70.105  54.873  1.00 39.64           C  
ATOM    538  CG  ASN A 105      29.961  69.138  53.996  1.00 40.40           C  
ATOM    539  OD1 ASN A 105      30.488  68.633  53.004  1.00 39.43           O  
ATOM    540  ND2 ASN A 105      28.703  68.879  54.354  1.00 39.64           N  
ATOM    541  N   GLN A 106      32.684  70.716  57.377  1.00 42.26           N  
ATOM    542  CA  GLN A 106      33.354  71.741  58.173  1.00 43.46           C  
ATOM    543  C   GLN A 106      34.755  71.355  58.648  1.00 43.13           C  
ATOM    544  O   GLN A 106      35.518  72.209  59.101  1.00 42.91           O  
ATOM    545  CB  GLN A 106      32.486  72.104  59.381  1.00 44.53           C  
ATOM    546  CG  GLN A 106      31.077  72.557  59.023  1.00 47.29           C  
ATOM    547  CD  GLN A 106      31.064  73.786  58.130  1.00 49.81           C  
ATOM    548  OE1 GLN A 106      31.620  74.830  58.480  1.00 51.43           O  
ATOM    549  NE2 GLN A 106      30.424  73.668  56.971  1.00 50.55           N  
ATOM    550  N   LEU A 107      35.096  70.074  58.549  1.00 43.61           N  
ATOM    551  CA  LEU A 107      36.411  69.608  58.983  1.00 43.43           C  
ATOM    552  C   LEU A 107      37.530  70.124  58.087  1.00 43.49           C  
ATOM    553  O   LEU A 107      37.443  70.055  56.862  1.00 43.96           O  
ATOM    554  CB  LEU A 107      36.432  68.078  59.043  1.00 43.64           C  
ATOM    555  CG  LEU A 107      36.358  67.475  60.451  1.00 44.21           C  
ATOM    556  CD1 LEU A 107      35.308  68.189  61.286  1.00 44.64           C  
ATOM    557  CD2 LEU A 107      36.049  65.994  60.349  1.00 44.83           C  
ATOM    558  N   GLN A 108      38.585  70.635  58.716  1.00 43.92           N  
ATOM    559  CA  GLN A 108      39.729  71.199  58.005  1.00 44.02           C  
ATOM    560  C   GLN A 108      40.778  70.167  57.603  1.00 43.28           C  
ATOM    561  O   GLN A 108      41.149  70.075  56.434  1.00 44.53           O  
ATOM    562  CB  GLN A 108      40.392  72.275  58.867  1.00 46.53           C  
ATOM    563  CG  GLN A 108      40.683  73.572  58.137  1.00 49.82           C  
ATOM    564  CD  GLN A 108      39.418  74.318  57.762  1.00 52.02           C  
ATOM    565  OE1 GLN A 108      38.581  73.813  57.012  1.00 53.40           O  
ATOM    566  NE2 GLN A 108      39.269  75.530  58.288  1.00 53.64           N  
ATOM    567  N   ASN A 109      41.268  69.403  58.575  1.00 41.60           N  
ATOM    568  CA  ASN A 109      42.280  68.385  58.307  1.00 39.70           C  
ATOM    569  C   ASN A 109      41.715  67.336  57.353  1.00 39.03           C  
ATOM    570  O   ASN A 109      40.752  66.640  57.682  1.00 37.85           O  
ATOM    571  CB  ASN A 109      42.721  67.719  59.614  1.00 38.65           C  
ATOM    572  CG  ASN A 109      43.904  66.782  59.425  1.00 38.74           C  
ATOM    573  OD1 ASN A 109      43.860  65.877  58.587  1.00 39.03           O  
ATOM    574  ND2 ASN A 109      44.959  67.007  60.208  1.00 38.01           N  
ATOM    575  N   THR A 110      42.319  67.222  56.175  1.00 38.84           N  
ATOM    576  CA  THR A 110      41.862  66.265  55.175  1.00 39.36           C  
ATOM    577  C   THR A 110      41.910  64.820  55.673  1.00 38.70           C  
ATOM    578  O   THR A 110      40.965  64.060  55.469  1.00 39.63           O  
ATOM    579  CB  THR A 110      42.689  66.377  53.878  1.00 40.12           C  
ATOM    580  OG1 THR A 110      44.072  66.148  54.168  1.00 42.67           O  
ATOM    581  CG2 THR A 110      42.527  67.761  53.263  1.00 40.55           C  
ATOM    582  N   THR A 111      43.003  64.442  56.327  1.00 37.88           N  
ATOM    583  CA  THR A 111      43.141  63.082  56.843  1.00 36.04           C  
ATOM    584  C   THR A 111      42.045  62.770  57.857  1.00 35.01           C  
ATOM    585  O   THR A 111      41.465  61.686  57.836  1.00 34.20           O  
ATOM    586  CB  THR A 111      44.516  62.870  57.509  1.00 36.83           C  
ATOM    587  OG1 THR A 111      45.547  63.012  56.524  1.00 36.96           O  
ATOM    588  CG2 THR A 111      44.605  61.481  58.126  1.00 37.59           C  
ATOM    589  N   ILE A 112      41.770  63.719  58.747  1.00 33.02           N  
ATOM    590  CA  ILE A 112      40.728  63.538  59.754  1.00 32.35           C  
ATOM    591  C   ILE A 112      39.379  63.467  59.048  1.00 31.17           C  
ATOM    592  O   ILE A 112      38.503  62.679  59.413  1.00 29.34           O  
ATOM    593  CB  ILE A 112      40.706  64.721  60.754  1.00 33.52           C  
ATOM    594  CG1 ILE A 112      42.000  64.736  61.573  1.00 33.85           C  
ATOM    595  CG2 ILE A 112      39.488  64.620  61.664  1.00 31.47           C  
ATOM    596  CD1 ILE A 112      42.192  63.512  62.442  1.00 36.23           C  
ATOM    597  N   LYS A 113      39.231  64.306  58.028  1.00 30.98           N  
ATOM    598  CA  LYS A 113      38.016  64.386  57.228  1.00 30.73           C  
ATOM    599  C   LYS A 113      37.712  63.034  56.574  1.00 28.35           C  
ATOM    600  O   LYS A 113      36.590  62.526  56.645  1.00 27.74           O  
ATOM    601  CB  LYS A 113      38.208  65.462  56.153  1.00 33.49           C  
ATOM    602  CG  LYS A 113      36.993  65.776  55.306  1.00 37.03           C  
ATOM    603  CD  LYS A 113      37.360  66.779  54.219  1.00 40.12           C  
ATOM    604  CE  LYS A 113      36.174  67.118  53.325  1.00 42.45           C  
ATOM    605  NZ  LYS A 113      35.112  67.865  54.051  1.00 43.36           N  
ATOM    606  N   ARG A 114      38.734  62.459  55.951  1.00 26.86           N  
ATOM    607  CA  ARG A 114      38.631  61.179  55.254  1.00 24.41           C  
ATOM    608  C   ARG A 114      38.302  60.009  56.187  1.00 24.55           C  
ATOM    609  O   ARG A 114      37.457  59.168  55.871  1.00 22.27           O  
ATOM    610  CB  ARG A 114      39.943  60.913  54.512  1.00 24.91           C  
ATOM    611  CG  ARG A 114      39.934  59.733  53.549  1.00 23.83           C  
ATOM    612  CD  ARG A 114      41.194  59.763  52.692  1.00 24.48           C  
ATOM    613  NE  ARG A 114      41.334  58.608  51.806  1.00 23.26           N  
ATOM    614  CZ  ARG A 114      40.576  58.376  50.738  1.00 25.83           C  
ATOM    615  NH1 ARG A 114      39.606  59.221  50.410  1.00 23.61           N  
ATOM    616  NH2 ARG A 114      40.796  57.300  49.988  1.00 23.06           N  
ATOM    617  N   ILE A 115      38.971  59.949  57.333  1.00 23.82           N  
ATOM    618  CA  ILE A 115      38.720  58.876  58.288  1.00 24.41           C  
ATOM    619  C   ILE A 115      37.296  58.932  58.838  1.00 24.39           C  
ATOM    620  O   ILE A 115      36.591  57.922  58.858  1.00 24.78           O  
ATOM    621  CB  ILE A 115      39.720  58.935  59.468  1.00 25.21           C  
ATOM    622  CG1 ILE A 115      41.113  58.519  58.979  1.00 25.19           C  
ATOM    623  CG2 ILE A 115      39.251  58.033  60.600  1.00 22.70           C  
ATOM    624  CD1 ILE A 115      42.202  58.625  60.028  1.00 26.27           C  
ATOM    625  N   ILE A 116      36.874  60.116  59.274  1.00 23.99           N  
ATOM    626  CA  ILE A 116      35.539  60.283  59.832  1.00 24.23           C  
ATOM    627  C   ILE A 116      34.441  59.947  58.822  1.00 23.88           C  
ATOM    628  O   ILE A 116      33.459  59.293  59.168  1.00 22.19           O  
ATOM    629  CB  ILE A 116      35.337  61.724  60.381  1.00 24.80           C  
ATOM    630  CG1 ILE A 116      36.219  61.924  61.622  1.00 25.41           C  
ATOM    631  CG2 ILE A 116      33.871  61.960  60.733  1.00 25.96           C  
ATOM    632  CD1 ILE A 116      36.029  63.261  62.324  1.00 25.15           C  
ATOM    633  N   LYS A 117      34.603  60.392  57.579  1.00 25.35           N  
ATOM    634  CA  LYS A 117      33.610  60.099  56.549  1.00 26.35           C  
ATOM    635  C   LYS A 117      33.470  58.584  56.424  1.00 26.20           C  
ATOM    636  O   LYS A 117      32.366  58.055  56.296  1.00 26.64           O  
ATOM    637  CB  LYS A 117      34.041  60.704  55.206  1.00 26.72           C  
ATOM    638  N   LYS A 118      34.604  57.892  56.476  1.00 26.33           N  
ATOM    639  CA  LYS A 118      34.632  56.439  56.372  1.00 25.57           C  
ATOM    640  C   LYS A 118      33.989  55.754  57.581  1.00 24.69           C  
ATOM    641  O   LYS A 118      33.302  54.739  57.435  1.00 24.36           O  
ATOM    642  CB  LYS A 118      36.080  55.970  56.205  1.00 28.20           C  
ATOM    643  CG  LYS A 118      36.244  54.497  55.885  1.00 32.16           C  
ATOM    644  CD  LYS A 118      37.640  54.228  55.333  1.00 36.26           C  
ATOM    645  CE  LYS A 118      37.815  52.773  54.930  1.00 37.26           C  
ATOM    646  NZ  LYS A 118      37.763  51.868  56.105  1.00 39.38           N  
ATOM    647  N   VAL A 119      34.205  56.307  58.772  1.00 22.37           N  
ATOM    648  CA  VAL A 119      33.632  55.727  59.981  1.00 22.59           C  
ATOM    649  C   VAL A 119      32.111  55.899  60.035  1.00 21.68           C  
ATOM    650  O   VAL A 119      31.426  55.151  60.730  1.00 21.12           O  
ATOM    651  CB  VAL A 119      34.270  56.341  61.254  1.00 23.63           C  
ATOM    652  CG1 VAL A 119      33.651  55.723  62.502  1.00 20.79           C  
ATOM    653  CG2 VAL A 119      35.776  56.099  61.243  1.00 22.23           C  
ATOM    654  N   GLN A 120      31.581  56.871  59.294  1.00 20.83           N  
ATOM    655  CA  GLN A 120      30.133  57.097  59.267  1.00 21.36           C  
ATOM    656  C   GLN A 120      29.405  55.948  58.555  1.00 21.63           C  
ATOM    657  O   GLN A 120      28.178  55.831  58.637  1.00 21.51           O  
ATOM    658  CB  GLN A 120      29.804  58.423  58.566  1.00 21.83           C  
ATOM    659  CG  GLN A 120      30.424  59.658  59.216  1.00 22.21           C  
ATOM    660  CD  GLN A 120      30.025  60.949  58.514  1.00 26.18           C  
ATOM    661  OE1 GLN A 120      29.786  60.960  57.306  1.00 26.64           O  
ATOM    662  NE2 GLN A 120      29.969  62.046  59.266  1.00 23.87           N  
ATOM    663  N   ASP A 121      30.162  55.111  57.848  1.00 19.66           N  
ATOM    664  CA  ASP A 121      29.596  53.958  57.141  1.00 21.29           C  
ATOM    665  C   ASP A 121      29.690  52.781  58.109  1.00 20.99           C  
ATOM    666  O   ASP A 121      30.772  52.240  58.323  1.00 20.95           O  
ATOM    667  CB  ASP A 121      30.413  53.657  55.875  1.00 19.46           C  
ATOM    668  CG  ASP A 121      29.783  52.574  55.004  1.00 21.81           C  
ATOM    669  OD1 ASP A 121      29.034  51.724  55.528  1.00 21.84           O  
ATOM    670  OD2 ASP A 121      30.056  52.563  53.784  1.00 22.86           O  
ATOM    671  N   LEU A 122      28.558  52.386  58.688  1.00 22.58           N  
ATOM    672  CA  LEU A 122      28.535  51.292  59.661  1.00 22.39           C  
ATOM    673  C   LEU A 122      28.460  49.919  59.013  1.00 22.78           C  
ATOM    674  O   LEU A 122      28.512  48.902  59.704  1.00 21.91           O  
ATOM    675  CB  LEU A 122      27.330  51.433  60.593  1.00 22.04           C  
ATOM    676  CG  LEU A 122      26.824  52.837  60.927  1.00 25.61           C  
ATOM    677  CD1 LEU A 122      25.697  52.735  61.951  1.00 25.99           C  
ATOM    678  CD2 LEU A 122      27.956  53.680  61.460  1.00 22.76           C  
ATOM    679  N   GLU A 123      28.341  49.894  57.691  1.00 22.03           N  
ATOM    680  CA  GLU A 123      28.202  48.644  56.965  1.00 23.75           C  
ATOM    681  C   GLU A 123      27.103  47.792  57.603  1.00 21.61           C  
ATOM    682  O   GLU A 123      26.055  48.324  57.952  1.00 22.87           O  
ATOM    683  CB  GLU A 123      29.540  47.902  56.894  1.00 26.94           C  
ATOM    684  CG  GLU A 123      30.179  48.049  55.508  1.00 34.66           C  
ATOM    685  CD  GLU A 123      31.604  48.553  55.547  1.00 38.29           C  
ATOM    686  OE1 GLU A 123      32.505  47.776  55.938  1.00 41.36           O  
ATOM    687  OE2 GLU A 123      31.825  49.729  55.185  1.00 42.09           O  
ATOM    688  N   ARG A 124      27.323  46.493  57.773  1.00 20.09           N  
ATOM    689  CA  ARG A 124      26.275  45.646  58.340  1.00 21.46           C  
ATOM    690  C   ARG A 124      25.784  46.105  59.712  1.00 21.73           C  
ATOM    691  O   ARG A 124      24.638  45.846  60.084  1.00 21.61           O  
ATOM    692  CB  ARG A 124      26.742  44.192  58.430  1.00 20.77           C  
ATOM    693  CG  ARG A 124      27.718  43.918  59.551  1.00 19.96           C  
ATOM    694  CD  ARG A 124      28.186  42.480  59.509  1.00 23.32           C  
ATOM    695  NE  ARG A 124      28.950  42.205  58.299  1.00 25.43           N  
ATOM    696  CZ  ARG A 124      29.456  41.017  57.994  1.00 29.86           C  
ATOM    697  NH1 ARG A 124      29.274  39.987  58.814  1.00 28.71           N  
ATOM    698  NH2 ARG A 124      30.152  40.858  56.873  1.00 31.49           N  
ATOM    699  N   ALA A 125      26.645  46.787  60.461  1.00 21.87           N  
ATOM    700  CA  ALA A 125      26.270  47.264  61.789  1.00 24.11           C  
ATOM    701  C   ALA A 125      25.117  48.270  61.749  1.00 24.29           C  
ATOM    702  O   ALA A 125      24.566  48.620  62.788  1.00 24.68           O  
ATOM    703  CB  ALA A 125      27.478  47.878  62.490  1.00 24.00           C  
ATOM    704  N   ALA A 126      24.748  48.735  60.557  1.00 22.56           N  
ATOM    705  CA  ALA A 126      23.642  49.684  60.447  1.00 22.76           C  
ATOM    706  C   ALA A 126      22.297  48.966  60.554  1.00 22.55           C  
ATOM    707  O   ALA A 126      21.258  49.598  60.749  1.00 23.01           O  
ATOM    708  CB  ALA A 126      23.721  50.438  59.125  1.00 21.66           C  
ATOM    709  N   LEU A 127      22.322  47.642  60.429  1.00 22.24           N  
ATOM    710  CA  LEU A 127      21.103  46.834  60.490  1.00 21.40           C  
ATOM    711  C   LEU A 127      20.542  46.655  61.900  1.00 22.60           C  
ATOM    712  O   LEU A 127      21.296  46.550  62.861  1.00 21.61           O  
ATOM    713  CB  LEU A 127      21.365  45.441  59.912  1.00 19.45           C  
ATOM    714  CG  LEU A 127      21.629  45.249  58.418  1.00 16.15           C  
ATOM    715  CD1 LEU A 127      22.085  43.821  58.168  1.00 18.41           C  
ATOM    716  CD2 LEU A 127      20.357  45.554  57.632  1.00 14.90           C  
ATOM    717  N   PRO A 128      19.202  46.616  62.033  1.00 23.33           N  
ATOM    718  CA  PRO A 128      18.582  46.430  63.348  1.00 24.44           C  
ATOM    719  C   PRO A 128      19.122  45.111  63.897  1.00 25.67           C  
ATOM    720  O   PRO A 128      19.384  44.182  63.128  1.00 24.90           O  
ATOM    721  CB  PRO A 128      17.096  46.342  63.017  1.00 23.93           C  
ATOM    722  CG  PRO A 128      16.970  47.241  61.824  1.00 24.99           C  
ATOM    723  CD  PRO A 128      18.180  46.863  60.999  1.00 22.87           C  
ATOM    724  N   ALA A 129      19.289  45.035  65.213  1.00 25.35           N  
ATOM    725  CA  ALA A 129      19.818  43.841  65.866  1.00 26.14           C  
ATOM    726  C   ALA A 129      19.296  42.516  65.303  1.00 26.55           C  
ATOM    727  O   ALA A 129      20.071  41.584  65.078  1.00 23.79           O  
ATOM    728  CB  ALA A 129      19.536  43.909  67.366  1.00 26.95           C  
ATOM    729  N   GLN A 130      17.989  42.431  65.077  1.00 26.32           N  
ATOM    730  CA  GLN A 130      17.397  41.201  64.563  1.00 29.37           C  
ATOM    731  C   GLN A 130      17.909  40.844  63.169  1.00 28.25           C  
ATOM    732  O   GLN A 130      18.313  39.705  62.922  1.00 27.07           O  
ATOM    733  CB  GLN A 130      15.871  41.313  64.542  1.00 31.38           C  
ATOM    734  CG  GLN A 130      15.167  40.022  64.158  1.00 37.44           C  
ATOM    735  CD  GLN A 130      13.656  40.124  64.267  1.00 41.02           C  
ATOM    736  OE1 GLN A 130      13.114  40.363  65.349  1.00 43.87           O  
ATOM    737  NE2 GLN A 130      12.967  39.947  63.144  1.00 43.01           N  
ATOM    738  N   GLU A 131      17.884  41.815  62.262  1.00 27.58           N  
ATOM    739  CA  GLU A 131      18.353  41.595  60.898  1.00 28.12           C  
ATOM    740  C   GLU A 131      19.852  41.319  60.875  1.00 25.64           C  
ATOM    741  O   GLU A 131      20.338  40.564  60.036  1.00 24.67           O  
ATOM    742  CB  GLU A 131      18.056  42.812  60.014  1.00 30.05           C  
ATOM    743  CG  GLU A 131      16.648  42.872  59.439  1.00 36.16           C  
ATOM    744  CD  GLU A 131      15.596  43.218  60.474  1.00 40.46           C  
ATOM    745  OE1 GLU A 131      15.349  42.396  61.383  1.00 43.71           O  
ATOM    746  OE2 GLU A 131      15.015  44.320  60.376  1.00 42.20           O  
ATOM    747  N   LEU A 132      20.583  41.933  61.798  1.00 23.77           N  
ATOM    748  CA  LEU A 132      22.027  41.741  61.856  1.00 23.77           C  
ATOM    749  C   LEU A 132      22.382  40.299  62.192  1.00 24.03           C  
ATOM    750  O   LEU A 132      23.248  39.700  61.546  1.00 23.44           O  
ATOM    751  CB  LEU A 132      22.658  42.686  62.886  1.00 23.27           C  
ATOM    752  CG  LEU A 132      24.167  42.535  63.139  1.00 22.82           C  
ATOM    753  CD1 LEU A 132      24.947  42.725  61.843  1.00 24.01           C  
ATOM    754  CD2 LEU A 132      24.614  43.548  64.179  1.00 23.32           C  
ATOM    755  N   GLU A 133      21.717  39.728  63.192  1.00 23.75           N  
ATOM    756  CA  GLU A 133      22.031  38.356  63.562  1.00 25.00           C  
ATOM    757  C   GLU A 133      21.628  37.401  62.445  1.00 23.01           C  
ATOM    758  O   GLU A 133      22.319  36.414  62.185  1.00 22.51           O  
ATOM    759  CB  GLU A 133      21.362  37.974  64.893  1.00 28.77           C  
ATOM    760  CG  GLU A 133      19.950  37.445  64.807  1.00 35.39           C  
ATOM    761  CD  GLU A 133      19.405  37.035  66.171  1.00 40.22           C  
ATOM    762  OE1 GLU A 133      18.302  36.450  66.224  1.00 41.83           O  
ATOM    763  OE2 GLU A 133      20.080  37.303  67.193  1.00 41.78           O  
ATOM    764  N   GLU A 134      20.524  37.703  61.768  1.00 22.62           N  
ATOM    765  CA  GLU A 134      20.073  36.857  60.670  1.00 24.34           C  
ATOM    766  C   GLU A 134      21.065  36.968  59.509  1.00 24.93           C  
ATOM    767  O   GLU A 134      21.395  35.967  58.865  1.00 24.77           O  
ATOM    768  CB  GLU A 134      18.669  37.265  60.209  1.00 24.26           C  
ATOM    769  CG  GLU A 134      18.195  36.512  58.973  1.00 26.97           C  
ATOM    770  CD  GLU A 134      16.781  36.876  58.560  1.00 28.34           C  
ATOM    771  OE1 GLU A 134      16.329  37.996  58.886  1.00 28.72           O  
ATOM    772  OE2 GLU A 134      16.127  36.045  57.893  1.00 28.15           O  
ATOM    773  N   TYR A 135      21.552  38.181  59.260  1.00 23.07           N  
ATOM    774  CA  TYR A 135      22.514  38.402  58.188  1.00 23.12           C  
ATOM    775  C   TYR A 135      23.831  37.687  58.503  1.00 23.03           C  
ATOM    776  O   TYR A 135      24.412  37.040  57.633  1.00 23.00           O  
ATOM    777  CB  TYR A 135      22.764  39.903  57.993  1.00 21.91           C  
ATOM    778  CG  TYR A 135      23.736  40.235  56.875  1.00 21.83           C  
ATOM    779  CD1 TYR A 135      23.502  39.807  55.568  1.00 22.95           C  
ATOM    780  CD2 TYR A 135      24.886  40.985  57.125  1.00 21.46           C  
ATOM    781  CE1 TYR A 135      24.390  40.119  54.532  1.00 22.34           C  
ATOM    782  CE2 TYR A 135      25.780  41.301  56.102  1.00 22.52           C  
ATOM    783  CZ  TYR A 135      25.526  40.865  54.808  1.00 23.28           C  
ATOM    784  OH  TYR A 135      26.403  41.176  53.795  1.00 23.78           O  
ATOM    785  N   ASN A 136      24.302  37.794  59.743  1.00 22.34           N  
ATOM    786  CA  ASN A 136      25.551  37.129  60.112  1.00 22.66           C  
ATOM    787  C   ASN A 136      25.430  35.616  59.994  1.00 22.26           C  
ATOM    788  O   ASN A 136      26.363  34.950  59.552  1.00 21.60           O  
ATOM    789  CB  ASN A 136      25.979  37.493  61.539  1.00 23.67           C  
ATOM    790  CG  ASN A 136      26.499  38.915  61.649  1.00 24.93           C  
ATOM    791  OD1 ASN A 136      27.226  39.393  60.777  1.00 26.06           O  
ATOM    792  ND2 ASN A 136      26.140  39.594  62.731  1.00 25.88           N  
ATOM    793  N   LYS A 137      24.280  35.073  60.382  1.00 20.98           N  
ATOM    794  CA  LYS A 137      24.079  33.632  60.307  1.00 21.98           C  
ATOM    795  C   LYS A 137      24.006  33.159  58.860  1.00 20.98           C  
ATOM    796  O   LYS A 137      24.509  32.085  58.525  1.00 20.06           O  
ATOM    797  CB  LYS A 137      22.809  33.214  61.055  1.00 23.33           C  
ATOM    798  CG  LYS A 137      22.528  31.729  60.936  1.00 27.37           C  
ATOM    799  CD  LYS A 137      21.405  31.270  61.844  1.00 32.52           C  
ATOM    800  CE  LYS A 137      21.082  29.808  61.567  1.00 35.29           C  
ATOM    801  NZ  LYS A 137      22.320  28.969  61.554  1.00 35.98           N  
ATOM    802  N   ILE A 138      23.374  33.959  58.007  1.00 19.85           N  
ATOM    803  CA  ILE A 138      23.260  33.615  56.595  1.00 21.24           C  
ATOM    804  C   ILE A 138      24.643  33.554  55.944  1.00 19.54           C  
ATOM    805  O   ILE A 138      24.936  32.632  55.188  1.00 21.81           O  
ATOM    806  CB  ILE A 138      22.368  34.631  55.846  1.00 21.43           C  
ATOM    807  CG1 ILE A 138      20.900  34.340  56.159  1.00 24.06           C  
ATOM    808  CG2 ILE A 138      22.611  34.554  54.338  1.00 23.74           C  
ATOM    809  CD1 ILE A 138      19.930  35.302  55.515  1.00 24.63           C  
ATOM    810  N   LEU A 139      25.491  34.530  56.244  1.00 19.05           N  
ATOM    811  CA  LEU A 139      26.837  34.562  55.687  1.00 19.74           C  
ATOM    812  C   LEU A 139      27.620  33.332  56.140  1.00 21.61           C  
ATOM    813  O   LEU A 139      28.300  32.682  55.344  1.00 21.28           O  
ATOM    814  CB  LEU A 139      27.565  35.834  56.131  1.00 19.37           C  
ATOM    815  CG  LEU A 139      27.041  37.157  55.559  1.00 21.50           C  
ATOM    816  CD1 LEU A 139      27.810  38.328  56.170  1.00 20.18           C  
ATOM    817  CD2 LEU A 139      27.188  37.151  54.044  1.00 19.99           C  
ATOM    818  N   LEU A 140      27.511  33.009  57.423  1.00 21.65           N  
ATOM    819  CA  LEU A 140      28.217  31.862  57.969  1.00 23.32           C  
ATOM    820  C   LEU A 140      27.714  30.569  57.337  1.00 22.19           C  
ATOM    821  O   LEU A 140      28.511  29.705  56.975  1.00 22.62           O  
ATOM    822  CB  LEU A 140      28.042  31.811  59.490  1.00 25.33           C  
ATOM    823  CG  LEU A 140      28.968  30.869  60.262  1.00 28.92           C  
ATOM    824  CD1 LEU A 140      30.414  31.241  59.990  1.00 30.99           C  
ATOM    825  CD2 LEU A 140      28.681  30.977  61.756  1.00 32.45           C  
ATOM    826  N   ASP A 141      26.396  30.439  57.202  1.00 20.90           N  
ATOM    827  CA  ASP A 141      25.817  29.237  56.615  1.00 21.82           C  
ATOM    828  C   ASP A 141      26.244  29.060  55.161  1.00 22.04           C  
ATOM    829  O   ASP A 141      26.501  27.940  54.720  1.00 21.02           O  
ATOM    830  CB  ASP A 141      24.283  29.261  56.698  1.00 22.55           C  
ATOM    831  CG  ASP A 141      23.766  29.076  58.121  1.00 24.93           C  
ATOM    832  OD1 ASP A 141      24.489  28.493  58.952  1.00 24.24           O  
ATOM    833  OD2 ASP A 141      22.625  29.502  58.404  1.00 26.64           O  
ATOM    834  N   MET A 142      26.315  30.156  54.411  1.00 20.30           N  
ATOM    835  CA  MET A 142      26.731  30.057  53.014  1.00 20.02           C  
ATOM    836  C   MET A 142      28.195  29.639  52.925  1.00 19.90           C  
ATOM    837  O   MET A 142      28.560  28.773  52.129  1.00 18.15           O  
ATOM    838  CB  MET A 142      26.524  31.389  52.277  1.00 16.36           C  
ATOM    839  CG  MET A 142      25.055  31.743  52.047  1.00 14.73           C  
ATOM    840  SD  MET A 142      24.812  32.982  50.748  1.00 18.57           S  
ATOM    841  CE  MET A 142      25.587  34.426  51.501  1.00 15.06           C  
ATOM    842  N   GLU A 143      29.033  30.251  53.751  1.00 21.27           N  
ATOM    843  CA  GLU A 143      30.452  29.931  53.745  1.00 24.34           C  
ATOM    844  C   GLU A 143      30.686  28.477  54.122  1.00 23.73           C  
ATOM    845  O   GLU A 143      31.454  27.768  53.464  1.00 23.77           O  
ATOM    846  CB  GLU A 143      31.209  30.830  54.719  1.00 26.33           C  
ATOM    847  CG  GLU A 143      32.700  30.567  54.706  1.00 31.24           C  
ATOM    848  CD  GLU A 143      33.296  30.741  53.321  1.00 34.04           C  
ATOM    849  OE1 GLU A 143      33.424  31.900  52.874  1.00 33.83           O  
ATOM    850  OE2 GLU A 143      33.624  29.716  52.678  1.00 34.64           O  
ATOM    851  N   THR A 144      30.024  28.037  55.187  1.00 22.79           N  
ATOM    852  CA  THR A 144      30.166  26.664  55.650  1.00 23.63           C  
ATOM    853  C   THR A 144      29.693  25.671  54.593  1.00 22.90           C  
ATOM    854  O   THR A 144      30.391  24.701  54.279  1.00 24.74           O  
ATOM    855  CB  THR A 144      29.363  26.425  56.941  1.00 23.79           C  
ATOM    856  OG1 THR A 144      29.850  27.294  57.971  1.00 23.95           O  
ATOM    857  CG2 THR A 144      29.502  24.973  57.391  1.00 23.49           C  
ATOM    858  N   THR A 145      28.507  25.917  54.050  1.00 19.50           N  
ATOM    859  CA  THR A 145      27.937  25.052  53.025  1.00 21.93           C  
ATOM    860  C   THR A 145      28.884  24.870  51.842  1.00 21.08           C  
ATOM    861  O   THR A 145      29.060  23.761  51.342  1.00 22.40           O  
ATOM    862  CB  THR A 145      26.605  25.616  52.494  1.00 21.32           C  
ATOM    863  OG1 THR A 145      25.646  25.661  53.559  1.00 22.38           O  
ATOM    864  CG2 THR A 145      26.068  24.740  51.358  1.00 20.84           C  
ATOM    865  N   TYR A 146      29.492  25.963  51.395  1.00 20.72           N  
ATOM    866  CA  TYR A 146      30.406  25.906  50.260  1.00 19.26           C  
ATOM    867  C   TYR A 146      31.682  25.126  50.581  1.00 19.83           C  
ATOM    868  O   TYR A 146      32.089  24.244  49.826  1.00 19.73           O  
ATOM    869  CB  TYR A 146      30.784  27.327  49.816  1.00 18.41           C  
ATOM    870  CG  TYR A 146      31.707  27.374  48.610  1.00 18.79           C  
ATOM    871  CD1 TYR A 146      31.196  27.356  47.311  1.00 16.82           C  
ATOM    872  CD2 TYR A 146      33.094  27.410  48.770  1.00 17.18           C  
ATOM    873  CE1 TYR A 146      32.044  27.376  46.197  1.00 16.82           C  
ATOM    874  CE2 TYR A 146      33.954  27.424  47.662  1.00 17.14           C  
ATOM    875  CZ  TYR A 146      33.418  27.406  46.382  1.00 18.38           C  
ATOM    876  OH  TYR A 146      34.256  27.403  45.289  1.00 18.18           O  
ATOM    877  N   SER A 147      32.298  25.448  51.712  1.00 19.67           N  
ATOM    878  CA  SER A 147      33.555  24.828  52.117  1.00 22.76           C  
ATOM    879  C   SER A 147      33.543  23.363  52.556  1.00 22.80           C  
ATOM    880  O   SER A 147      34.606  22.752  52.672  1.00 22.47           O  
ATOM    881  CB  SER A 147      34.208  25.678  53.211  1.00 23.75           C  
ATOM    882  OG  SER A 147      34.560  26.953  52.702  1.00 28.52           O  
ATOM    883  N   VAL A 148      32.368  22.796  52.803  1.00 22.17           N  
ATOM    884  CA  VAL A 148      32.309  21.401  53.219  1.00 23.76           C  
ATOM    885  C   VAL A 148      31.527  20.541  52.231  1.00 23.17           C  
ATOM    886  O   VAL A 148      31.277  19.366  52.482  1.00 24.77           O  
ATOM    887  CB  VAL A 148      31.676  21.255  54.631  1.00 24.20           C  
ATOM    888  CG1 VAL A 148      32.400  22.160  55.617  1.00 23.61           C  
ATOM    889  CG2 VAL A 148      30.189  21.584  54.588  1.00 23.11           C  
ATOM    890  N   ALA A 149      31.153  21.122  51.098  1.00 22.77           N  
ATOM    891  CA  ALA A 149      30.395  20.384  50.093  1.00 21.75           C  
ATOM    892  C   ALA A 149      31.247  19.329  49.391  1.00 21.47           C  
ATOM    893  O   ALA A 149      32.429  19.549  49.121  1.00 20.99           O  
ATOM    894  CB  ALA A 149      29.810  21.352  49.064  1.00 19.82           C  
ATOM    895  N   THR A 150      30.644  18.179  49.106  1.00 21.38           N  
ATOM    896  CA  THR A 150      31.354  17.111  48.411  1.00 22.06           C  
ATOM    897  C   THR A 150      30.491  16.527  47.298  1.00 22.17           C  
ATOM    898  O   THR A 150      29.266  16.673  47.294  1.00 22.75           O  
ATOM    899  CB  THR A 150      31.768  15.957  49.371  1.00 23.05           C  
ATOM    900  OG1 THR A 150      30.598  15.325  49.901  1.00 25.28           O  
ATOM    901  CG2 THR A 150      32.615  16.487  50.520  1.00 22.65           C  
ATOM    902  N   VAL A 151      31.145  15.881  46.343  1.00 22.72           N  
ATOM    903  CA  VAL A 151      30.459  15.244  45.228  1.00 24.25           C  
ATOM    904  C   VAL A 151      30.819  13.767  45.329  1.00 26.05           C  
ATOM    905  O   VAL A 151      31.990  13.404  45.239  1.00 26.03           O  
ATOM    906  CB  VAL A 151      30.941  15.813  43.884  1.00 23.11           C  
ATOM    907  CG1 VAL A 151      30.204  15.133  42.738  1.00 23.43           C  
ATOM    908  CG2 VAL A 151      30.707  17.324  43.852  1.00 22.55           C  
ATOM    909  N   CYS A 152      29.813  12.920  45.522  1.00 30.03           N  
ATOM    910  CA  CYS A 152      30.051  11.489  45.689  1.00 34.00           C  
ATOM    911  C   CYS A 152      29.670  10.596  44.514  1.00 36.77           C  
ATOM    912  O   CYS A 152      28.800  10.927  43.711  1.00 37.04           O  
ATOM    913  CB  CYS A 152      29.301  10.976  46.916  1.00 33.01           C  
ATOM    914  SG  CYS A 152      29.491  11.922  48.460  1.00 34.26           S  
ATOM    915  N   HIS A 153      30.333   9.443  44.450  1.00 40.51           N  
ATOM    916  CA  HIS A 153      30.085   8.433  43.427  1.00 43.09           C  
ATOM    917  C   HIS A 153      29.141   7.394  44.027  1.00 45.42           C  
ATOM    918  O   HIS A 153      28.935   7.360  45.243  1.00 45.31           O  
ATOM    919  CB  HIS A 153      31.392   7.748  43.028  1.00 43.26           C  
ATOM    920  CG  HIS A 153      32.240   8.552  42.097  1.00 44.35           C  
ATOM    921  ND1 HIS A 153      31.902   8.761  40.777  1.00 45.33           N  
ATOM    922  CD2 HIS A 153      33.423   9.183  42.287  1.00 44.78           C  
ATOM    923  CE1 HIS A 153      32.842   9.483  40.194  1.00 45.93           C  
ATOM    924  NE2 HIS A 153      33.777   9.752  41.088  1.00 46.19           N  
ATOM    925  N   PRO A 154      28.554   6.531  43.181  1.00 47.60           N  
ATOM    926  CA  PRO A 154      27.632   5.493  43.654  1.00 48.59           C  
ATOM    927  C   PRO A 154      28.231   4.651  44.780  1.00 49.38           C  
ATOM    928  O   PRO A 154      27.577   4.403  45.795  1.00 49.51           O  
ATOM    929  CB  PRO A 154      27.370   4.674  42.394  1.00 48.70           C  
ATOM    930  CG  PRO A 154      27.411   5.721  41.320  1.00 48.86           C  
ATOM    931  CD  PRO A 154      28.637   6.523  41.709  1.00 48.72           C  
ATOM    932  N   ASN A 155      29.478   4.220  44.597  1.00 49.61           N  
ATOM    933  CA  ASN A 155      30.154   3.407  45.602  1.00 50.29           C  
ATOM    934  C   ASN A 155      30.164   4.072  46.974  1.00 50.98           C  
ATOM    935  O   ASN A 155      29.525   3.592  47.913  1.00 53.09           O  
ATOM    936  CB  ASN A 155      31.594   3.082  45.168  1.00 49.31           C  
ATOM    937  CG  ASN A 155      32.299   4.260  44.507  1.00 47.77           C  
ATOM    938  OD1 ASN A 155      32.262   5.384  45.012  1.00 47.20           O  
ATOM    939  ND2 ASN A 155      32.955   3.993  43.377  1.00 45.72           N  
ATOM    940  N   GLY A 156      30.885   5.180  47.086  1.00 50.22           N  
ATOM    941  CA  GLY A 156      30.964   5.881  48.353  1.00 47.28           C  
ATOM    942  C   GLY A 156      32.148   6.822  48.369  1.00 45.22           C  
ATOM    943  O   GLY A 156      32.458   7.432  49.392  1.00 46.04           O  
ATOM    944  N   SER A 157      32.824   6.927  47.232  1.00 42.88           N  
ATOM    945  CA  SER A 157      33.965   7.821  47.122  1.00 41.34           C  
ATOM    946  C   SER A 157      33.431   9.230  46.904  1.00 38.80           C  
ATOM    947  O   SER A 157      32.807   9.517  45.884  1.00 37.31           O  
ATOM    948  CB  SER A 157      34.855   7.415  45.948  1.00 41.68           C  
ATOM    949  OG  SER A 157      35.413   6.130  46.160  1.00 45.75           O  
ATOM    950  N   CYS A 158      33.655  10.096  47.883  1.00 36.07           N  
ATOM    951  CA  CYS A 158      33.202  11.471  47.793  1.00 33.90           C  
ATOM    952  C   CYS A 158      34.416  12.358  47.579  1.00 32.06           C  
ATOM    953  O   CYS A 158      35.459  12.159  48.202  1.00 33.88           O  
ATOM    954  CB  CYS A 158      32.479  11.883  49.070  1.00 34.32           C  
ATOM    955  SG  CYS A 158      30.963  10.949  49.464  1.00 35.61           S  
ATOM    956  N   LEU A 159      34.280  13.331  46.689  1.00 28.75           N  
ATOM    957  CA  LEU A 159      35.377  14.237  46.387  1.00 26.04           C  
ATOM    958  C   LEU A 159      35.107  15.659  46.866  1.00 24.84           C  
ATOM    959  O   LEU A 159      33.988  16.159  46.765  1.00 23.97           O  
ATOM    960  CB  LEU A 159      35.644  14.252  44.875  1.00 26.05           C  
ATOM    961  CG  LEU A 159      36.265  13.013  44.216  1.00 27.11           C  
ATOM    962  CD1 LEU A 159      35.318  11.828  44.314  1.00 28.50           C  
ATOM    963  CD2 LEU A 159      36.569  13.323  42.753  1.00 27.77           C  
ATOM    964  N   GLN A 160      36.138  16.297  47.405  1.00 24.09           N  
ATOM    965  CA  GLN A 160      36.028  17.677  47.857  1.00 25.37           C  
ATOM    966  C   GLN A 160      36.550  18.534  46.704  1.00 23.81           C  
ATOM    967  O   GLN A 160      37.239  18.024  45.818  1.00 21.41           O  
ATOM    968  CB  GLN A 160      36.881  17.902  49.109  1.00 27.00           C  
ATOM    969  CG  GLN A 160      36.405  17.122  50.329  1.00 31.92           C  
ATOM    970  CD  GLN A 160      37.279  17.348  51.546  1.00 34.94           C  
ATOM    971  OE1 GLN A 160      38.476  17.061  51.527  1.00 38.38           O  
ATOM    972  NE2 GLN A 160      36.684  17.862  52.614  1.00 37.18           N  
ATOM    973  N   LEU A 161      36.222  19.824  46.705  1.00 23.17           N  
ATOM    974  CA  LEU A 161      36.680  20.709  45.639  1.00 22.33           C  
ATOM    975  C   LEU A 161      38.206  20.719  45.582  1.00 23.46           C  
ATOM    976  O   LEU A 161      38.801  20.494  44.533  1.00 23.60           O  
ATOM    977  CB  LEU A 161      36.151  22.131  45.856  1.00 21.16           C  
ATOM    978  CG  LEU A 161      36.586  23.161  44.808  1.00 19.56           C  
ATOM    979  CD1 LEU A 161      36.115  22.726  43.425  1.00 19.50           C  
ATOM    980  CD2 LEU A 161      36.015  24.527  45.166  1.00 21.09           C  
ATOM    981  N   GLU A 162      38.844  20.973  46.716  1.00 25.17           N  
ATOM    982  CA  GLU A 162      40.297  20.989  46.751  1.00 27.25           C  
ATOM    983  C   GLU A 162      40.789  19.794  47.558  1.00 27.24           C  
ATOM    984  O   GLU A 162      40.398  19.614  48.710  1.00 28.55           O  
ATOM    985  CB  GLU A 162      40.796  22.297  47.367  1.00 31.24           C  
ATOM    986  CG  GLU A 162      40.244  23.527  46.662  1.00 37.45           C  
ATOM    987  CD  GLU A 162      41.081  24.769  46.892  1.00 43.41           C  
ATOM    988  OE1 GLU A 162      41.256  25.170  48.060  1.00 46.60           O  
ATOM    989  OE2 GLU A 162      41.564  25.348  45.896  1.00 48.13           O  
ATOM    990  N   PRO A 163      41.663  18.964  46.965  1.00 26.18           N  
ATOM    991  CA  PRO A 163      42.200  19.094  45.607  1.00 24.97           C  
ATOM    992  C   PRO A 163      41.558  18.143  44.595  1.00 23.91           C  
ATOM    993  O   PRO A 163      41.868  18.203  43.404  1.00 22.16           O  
ATOM    994  CB  PRO A 163      43.662  18.750  45.806  1.00 26.63           C  
ATOM    995  CG  PRO A 163      43.547  17.564  46.737  1.00 25.86           C  
ATOM    996  CD  PRO A 163      42.458  17.987  47.737  1.00 26.80           C  
ATOM    997  N   ASP A 164      40.672  17.273  45.072  1.00 22.30           N  
ATOM    998  CA  ASP A 164      40.037  16.269  44.225  1.00 21.76           C  
ATOM    999  C   ASP A 164      39.365  16.754  42.945  1.00 21.71           C  
ATOM   1000  O   ASP A 164      39.793  16.392  41.850  1.00 23.10           O  
ATOM   1001  CB  ASP A 164      39.029  15.452  45.036  1.00 22.60           C  
ATOM   1002  CG  ASP A 164      39.608  14.946  46.341  1.00 26.35           C  
ATOM   1003  OD1 ASP A 164      40.763  14.474  46.339  1.00 26.43           O  
ATOM   1004  OD2 ASP A 164      38.902  15.018  47.369  1.00 29.80           O  
ATOM   1005  N   LEU A 165      38.308  17.551  43.068  1.00 19.29           N  
ATOM   1006  CA  LEU A 165      37.604  18.027  41.875  1.00 19.93           C  
ATOM   1007  C   LEU A 165      38.473  18.933  41.020  1.00 18.92           C  
ATOM   1008  O   LEU A 165      38.405  18.887  39.794  1.00 19.13           O  
ATOM   1009  CB  LEU A 165      36.316  18.753  42.273  1.00 19.22           C  
ATOM   1010  CG  LEU A 165      35.288  17.859  42.971  1.00 21.05           C  
ATOM   1011  CD1 LEU A 165      34.177  18.719  43.553  1.00 21.19           C  
ATOM   1012  CD2 LEU A 165      34.726  16.834  41.978  1.00 18.71           C  
ATOM   1013  N   THR A 166      39.287  19.757  41.673  1.00 19.32           N  
ATOM   1014  CA  THR A 166      40.179  20.667  40.968  1.00 20.23           C  
ATOM   1015  C   THR A 166      41.138  19.855  40.103  1.00 20.96           C  
ATOM   1016  O   THR A 166      41.408  20.203  38.950  1.00 18.55           O  
ATOM   1017  CB  THR A 166      40.994  21.530  41.962  1.00 21.09           C  
ATOM   1018  OG1 THR A 166      40.098  22.333  42.739  1.00 23.68           O  
ATOM   1019  CG2 THR A 166      41.962  22.444  41.212  1.00 23.82           C  
ATOM   1020  N   ASN A 167      41.649  18.762  40.660  1.00 20.33           N  
ATOM   1021  CA  ASN A 167      42.566  17.916  39.910  1.00 21.82           C  
ATOM   1022  C   ASN A 167      41.876  17.272  38.706  1.00 19.19           C  
ATOM   1023  O   ASN A 167      42.457  17.200  37.624  1.00 21.70           O  
ATOM   1024  CB  ASN A 167      43.144  16.820  40.800  1.00 24.76           C  
ATOM   1025  CG  ASN A 167      44.158  15.971  40.068  1.00 29.65           C  
ATOM   1026  OD1 ASN A 167      45.283  16.409  39.812  1.00 31.73           O  
ATOM   1027  ND2 ASN A 167      43.759  14.757  39.701  1.00 31.98           N  
ATOM   1028  N   VAL A 168      40.645  16.800  38.893  1.00 18.96           N  
ATOM   1029  CA  VAL A 168      39.907  16.180  37.795  1.00 18.37           C  
ATOM   1030  C   VAL A 168      39.715  17.182  36.650  1.00 18.73           C  
ATOM   1031  O   VAL A 168      39.965  16.869  35.485  1.00 15.90           O  
ATOM   1032  CB  VAL A 168      38.516  15.666  38.257  1.00 19.57           C  
ATOM   1033  CG1 VAL A 168      37.680  15.275  37.048  1.00 18.46           C  
ATOM   1034  CG2 VAL A 168      38.682  14.451  39.187  1.00 20.39           C  
ATOM   1035  N   MET A 169      39.279  18.392  36.988  1.00 18.95           N  
ATOM   1036  CA  MET A 169      39.063  19.423  35.980  1.00 17.76           C  
ATOM   1037  C   MET A 169      40.353  19.794  35.244  1.00 16.67           C  
ATOM   1038  O   MET A 169      40.328  20.125  34.060  1.00 17.29           O  
ATOM   1039  CB  MET A 169      38.475  20.680  36.630  1.00 18.24           C  
ATOM   1040  CG  MET A 169      37.084  20.494  37.227  1.00 16.87           C  
ATOM   1041  SD  MET A 169      35.914  19.807  36.056  1.00 20.02           S  
ATOM   1042  CE  MET A 169      35.798  21.162  34.832  1.00 21.44           C  
ATOM   1043  N   ALA A 170      41.478  19.724  35.944  1.00 15.31           N  
ATOM   1044  CA  ALA A 170      42.764  20.088  35.356  1.00 16.45           C  
ATOM   1045  C   ALA A 170      43.473  19.014  34.530  1.00 17.34           C  
ATOM   1046  O   ALA A 170      44.191  19.336  33.580  1.00 18.65           O  
ATOM   1047  CB  ALA A 170      43.708  20.570  36.458  1.00 14.53           C  
ATOM   1048  N   THR A 171      43.263  17.750  34.875  1.00 14.75           N  
ATOM   1049  CA  THR A 171      43.963  16.665  34.199  1.00 15.77           C  
ATOM   1050  C   THR A 171      43.151  15.721  33.322  1.00 17.01           C  
ATOM   1051  O   THR A 171      43.680  15.157  32.364  1.00 17.58           O  
ATOM   1052  CB  THR A 171      44.717  15.818  35.230  1.00 16.12           C  
ATOM   1053  OG1 THR A 171      43.773  15.222  36.124  1.00 17.60           O  
ATOM   1054  CG2 THR A 171      45.669  16.694  36.042  1.00 16.30           C  
ATOM   1055  N   SER A 172      41.876  15.531  33.634  1.00 16.36           N  
ATOM   1056  CA  SER A 172      41.070  14.635  32.816  1.00 16.62           C  
ATOM   1057  C   SER A 172      40.841  15.190  31.411  1.00 17.76           C  
ATOM   1058  O   SER A 172      40.627  16.390  31.231  1.00 16.09           O  
ATOM   1059  CB  SER A 172      39.717  14.379  33.471  1.00 17.45           C  
ATOM   1060  OG  SER A 172      38.883  13.637  32.592  1.00 17.94           O  
ATOM   1061  N   ARG A 173      40.894  14.305  30.420  1.00 17.37           N  
ATOM   1062  CA  ARG A 173      40.656  14.675  29.029  1.00 18.83           C  
ATOM   1063  C   ARG A 173      39.473  13.859  28.510  1.00 18.41           C  
ATOM   1064  O   ARG A 173      39.333  13.648  27.306  1.00 18.06           O  
ATOM   1065  CB  ARG A 173      41.899  14.394  28.175  1.00 21.32           C  
ATOM   1066  CG  ARG A 173      42.806  15.601  27.910  1.00 25.72           C  
ATOM   1067  CD  ARG A 173      42.784  16.603  29.041  1.00 24.96           C  
ATOM   1068  NE  ARG A 173      44.009  17.391  29.117  1.00 25.28           N  
ATOM   1069  CZ  ARG A 173      44.224  18.329  30.035  1.00 25.48           C  
ATOM   1070  NH1 ARG A 173      45.366  18.998  30.055  1.00 27.49           N  
ATOM   1071  NH2 ARG A 173      43.287  18.610  30.928  1.00 26.72           N  
ATOM   1072  N   LYS A 174      38.629  13.394  29.427  1.00 19.07           N  
ATOM   1073  CA  LYS A 174      37.449  12.614  29.058  1.00 19.70           C  
ATOM   1074  C   LYS A 174      36.181  13.441  29.276  1.00 18.76           C  
ATOM   1075  O   LYS A 174      35.836  13.786  30.412  1.00 16.76           O  
ATOM   1076  CB  LYS A 174      37.396  11.320  29.876  1.00 20.49           C  
ATOM   1077  CG  LYS A 174      38.655  10.464  29.712  1.00 25.63           C  
ATOM   1078  CD  LYS A 174      38.499   9.071  30.304  1.00 27.27           C  
ATOM   1079  CE  LYS A 174      37.450   8.267  29.552  1.00 32.01           C  
ATOM   1080  NZ  LYS A 174      37.428   6.847  30.001  1.00 36.31           N  
ATOM   1081  N   TYR A 175      35.499  13.750  28.175  1.00 17.94           N  
ATOM   1082  CA  TYR A 175      34.280  14.564  28.187  1.00 18.82           C  
ATOM   1083  C   TYR A 175      33.298  14.209  29.303  1.00 18.43           C  
ATOM   1084  O   TYR A 175      32.820  15.092  30.016  1.00 18.33           O  
ATOM   1085  CB  TYR A 175      33.561  14.456  26.834  1.00 17.41           C  
ATOM   1086  CG  TYR A 175      32.581  15.582  26.551  1.00 17.19           C  
ATOM   1087  CD1 TYR A 175      32.960  16.682  25.782  1.00 17.56           C  
ATOM   1088  CD2 TYR A 175      31.276  15.546  27.049  1.00 18.96           C  
ATOM   1089  CE1 TYR A 175      32.068  17.718  25.509  1.00 17.54           C  
ATOM   1090  CE2 TYR A 175      30.373  16.581  26.787  1.00 19.27           C  
ATOM   1091  CZ  TYR A 175      30.778  17.666  26.015  1.00 20.83           C  
ATOM   1092  OH  TYR A 175      29.908  18.711  25.768  1.00 21.81           O  
ATOM   1093  N   GLU A 176      32.996  12.922  29.454  1.00 17.90           N  
ATOM   1094  CA  GLU A 176      32.049  12.492  30.479  1.00 18.16           C  
ATOM   1095  C   GLU A 176      32.548  12.619  31.917  1.00 17.41           C  
ATOM   1096  O   GLU A 176      31.752  12.866  32.821  1.00 16.71           O  
ATOM   1097  CB  GLU A 176      31.598  11.046  30.224  1.00 20.18           C  
ATOM   1098  CG  GLU A 176      30.791  10.830  28.943  1.00 20.70           C  
ATOM   1099  CD  GLU A 176      29.494  11.633  28.895  1.00 23.77           C  
ATOM   1100  OE1 GLU A 176      28.760  11.661  29.907  1.00 22.24           O  
ATOM   1101  OE2 GLU A 176      29.202  12.226  27.833  1.00 24.84           O  
ATOM   1102  N   ASP A 177      33.848  12.443  32.145  1.00 16.59           N  
ATOM   1103  CA  ASP A 177      34.373  12.560  33.506  1.00 17.48           C  
ATOM   1104  C   ASP A 177      34.416  14.033  33.906  1.00 16.55           C  
ATOM   1105  O   ASP A 177      34.133  14.389  35.052  1.00 13.04           O  
ATOM   1106  CB  ASP A 177      35.774  11.944  33.617  1.00 19.01           C  
ATOM   1107  CG  ASP A 177      35.779  10.440  33.362  1.00 24.16           C  
ATOM   1108  OD1 ASP A 177      34.689   9.830  33.331  1.00 26.06           O  
ATOM   1109  OD2 ASP A 177      36.875   9.865  33.201  1.00 23.40           O  
ATOM   1110  N   LEU A 178      34.769  14.885  32.951  1.00 15.38           N  
ATOM   1111  CA  LEU A 178      34.822  16.319  33.200  1.00 16.48           C  
ATOM   1112  C   LEU A 178      33.404  16.803  33.499  1.00 16.80           C  
ATOM   1113  O   LEU A 178      33.192  17.636  34.385  1.00 17.09           O  
ATOM   1114  CB  LEU A 178      35.386  17.048  31.974  1.00 14.57           C  
ATOM   1115  CG  LEU A 178      36.893  16.869  31.731  1.00 14.85           C  
ATOM   1116  CD1 LEU A 178      37.298  17.512  30.412  1.00 14.52           C  
ATOM   1117  CD2 LEU A 178      37.668  17.501  32.880  1.00 14.67           C  
ATOM   1118  N   LEU A 179      32.434  16.258  32.768  1.00 15.84           N  
ATOM   1119  CA  LEU A 179      31.037  16.631  32.955  1.00 15.80           C  
ATOM   1120  C   LEU A 179      30.530  16.250  34.342  1.00 16.05           C  
ATOM   1121  O   LEU A 179      29.840  17.037  34.998  1.00 16.25           O  
ATOM   1122  CB  LEU A 179      30.160  15.971  31.881  1.00 18.19           C  
ATOM   1123  CG  LEU A 179      28.670  16.336  31.924  1.00 18.57           C  
ATOM   1124  CD1 LEU A 179      28.524  17.850  31.917  1.00 23.32           C  
ATOM   1125  CD2 LEU A 179      27.942  15.731  30.735  1.00 22.22           C  
ATOM   1126  N   TRP A 180      30.869  15.042  34.784  1.00 15.85           N  
ATOM   1127  CA  TRP A 180      30.452  14.556  36.099  1.00 16.79           C  
ATOM   1128  C   TRP A 180      30.914  15.505  37.208  1.00 15.76           C  
ATOM   1129  O   TRP A 180      30.139  15.871  38.091  1.00 15.00           O  
ATOM   1130  CB  TRP A 180      31.033  13.159  36.362  1.00 19.10           C  
ATOM   1131  CG  TRP A 180      30.687  12.625  37.721  1.00 22.86           C  
ATOM   1132  CD1 TRP A 180      29.531  11.991  38.086  1.00 25.13           C  
ATOM   1133  CD2 TRP A 180      31.472  12.746  38.916  1.00 24.67           C  
ATOM   1134  NE1 TRP A 180      29.549  11.714  39.436  1.00 25.08           N  
ATOM   1135  CE2 TRP A 180      30.727  12.167  39.967  1.00 26.17           C  
ATOM   1136  CE3 TRP A 180      32.731  13.290  39.199  1.00 25.03           C  
ATOM   1137  CZ2 TRP A 180      31.202  12.119  41.284  1.00 27.62           C  
ATOM   1138  CZ3 TRP A 180      33.203  13.241  40.509  1.00 26.84           C  
ATOM   1139  CH2 TRP A 180      32.439  12.659  41.533  1.00 27.01           C  
ATOM   1140  N   ALA A 181      32.181  15.899  37.158  1.00 16.39           N  
ATOM   1141  CA  ALA A 181      32.739  16.796  38.162  1.00 15.16           C  
ATOM   1142  C   ALA A 181      32.142  18.200  38.063  1.00 15.48           C  
ATOM   1143  O   ALA A 181      31.839  18.826  39.080  1.00 16.14           O  
ATOM   1144  CB  ALA A 181      34.256  16.863  38.010  1.00 14.42           C  
ATOM   1145  N   TRP A 182      31.982  18.684  36.835  1.00 15.80           N  
ATOM   1146  CA  TRP A 182      31.436  20.019  36.581  1.00 16.29           C  
ATOM   1147  C   TRP A 182      29.985  20.138  37.057  1.00 15.56           C  
ATOM   1148  O   TRP A 182      29.634  21.070  37.779  1.00 13.86           O  
ATOM   1149  CB  TRP A 182      31.506  20.331  35.082  1.00 15.34           C  
ATOM   1150  CG  TRP A 182      31.110  21.741  34.725  1.00 15.79           C  
ATOM   1151  CD1 TRP A 182      31.929  22.837  34.666  1.00 16.30           C  
ATOM   1152  CD2 TRP A 182      29.792  22.209  34.413  1.00 15.16           C  
ATOM   1153  NE1 TRP A 182      31.199  23.958  34.338  1.00 15.53           N  
ATOM   1154  CE2 TRP A 182      29.885  23.601  34.179  1.00 16.51           C  
ATOM   1155  CE3 TRP A 182      28.538  21.588  34.312  1.00 16.54           C  
ATOM   1156  CZ2 TRP A 182      28.771  24.382  33.849  1.00 14.24           C  
ATOM   1157  CZ3 TRP A 182      27.432  22.366  33.985  1.00 16.40           C  
ATOM   1158  CH2 TRP A 182      27.558  23.748  33.756  1.00 15.28           C  
ATOM   1159  N   GLU A 183      29.149  19.192  36.639  1.00 15.67           N  
ATOM   1160  CA  GLU A 183      27.741  19.178  37.019  1.00 15.17           C  
ATOM   1161  C   GLU A 183      27.576  18.857  38.499  1.00 16.13           C  
ATOM   1162  O   GLU A 183      26.791  19.497  39.206  1.00 15.22           O  
ATOM   1163  CB  GLU A 183      26.982  18.139  36.187  1.00 17.45           C  
ATOM   1164  CG  GLU A 183      25.473  18.101  36.444  1.00 19.85           C  
ATOM   1165  CD  GLU A 183      24.785  19.410  36.087  1.00 23.48           C  
ATOM   1166  OE1 GLU A 183      25.012  19.911  34.968  1.00 25.84           O  
ATOM   1167  OE2 GLU A 183      24.012  19.938  36.918  1.00 26.74           O  
ATOM   1168  N   GLY A 184      28.321  17.858  38.962  1.00 17.03           N  
ATOM   1169  CA  GLY A 184      28.244  17.452  40.352  1.00 17.32           C  
ATOM   1170  C   GLY A 184      28.530  18.576  41.328  1.00 18.14           C  
ATOM   1171  O   GLY A 184      27.812  18.750  42.312  1.00 18.29           O  
ATOM   1172  N   TRP A 185      29.584  19.340  41.067  1.00 17.32           N  
ATOM   1173  CA  TRP A 185      29.940  20.440  41.952  1.00 16.83           C  
ATOM   1174  C   TRP A 185      28.796  21.441  42.028  1.00 15.17           C  
ATOM   1175  O   TRP A 185      28.422  21.900  43.105  1.00 17.84           O  
ATOM   1176  CB  TRP A 185      31.209  21.145  41.459  1.00 15.21           C  
ATOM   1177  CG  TRP A 185      31.605  22.288  42.345  1.00 16.54           C  
ATOM   1178  CD1 TRP A 185      31.716  23.603  41.991  1.00 14.98           C  
ATOM   1179  CD2 TRP A 185      31.879  22.226  43.751  1.00 17.16           C  
ATOM   1180  NE1 TRP A 185      32.036  24.364  43.092  1.00 17.71           N  
ATOM   1181  CE2 TRP A 185      32.141  23.544  44.185  1.00 16.95           C  
ATOM   1182  CE3 TRP A 185      31.924  21.182  44.689  1.00 17.45           C  
ATOM   1183  CZ2 TRP A 185      32.444  23.849  45.518  1.00 16.83           C  
ATOM   1184  CZ3 TRP A 185      32.225  21.487  46.016  1.00 17.47           C  
ATOM   1185  CH2 TRP A 185      32.480  22.811  46.415  1.00 18.90           C  
ATOM   1186  N   ARG A 186      28.234  21.779  40.878  1.00 15.34           N  
ATOM   1187  CA  ARG A 186      27.136  22.724  40.854  1.00 16.45           C  
ATOM   1188  C   ARG A 186      25.903  22.145  41.547  1.00 17.65           C  
ATOM   1189  O   ARG A 186      25.202  22.858  42.263  1.00 17.39           O  
ATOM   1190  CB  ARG A 186      26.868  23.142  39.407  1.00 13.86           C  
ATOM   1191  CG  ARG A 186      27.981  24.074  38.923  1.00 16.46           C  
ATOM   1192  CD  ARG A 186      28.079  24.265  37.416  1.00 15.80           C  
ATOM   1193  NE  ARG A 186      29.144  25.230  37.139  1.00 15.22           N  
ATOM   1194  CZ  ARG A 186      30.444  24.974  37.269  1.00 15.55           C  
ATOM   1195  NH1 ARG A 186      31.333  25.920  37.009  1.00 16.82           N  
ATOM   1196  NH2 ARG A 186      30.860  23.766  37.632  1.00 15.71           N  
ATOM   1197  N   ASP A 187      25.661  20.848  41.374  1.00 18.73           N  
ATOM   1198  CA  ASP A 187      24.513  20.215  42.021  1.00 20.64           C  
ATOM   1199  C   ASP A 187      24.610  20.272  43.545  1.00 19.56           C  
ATOM   1200  O   ASP A 187      23.619  20.520  44.227  1.00 19.81           O  
ATOM   1201  CB  ASP A 187      24.388  18.745  41.612  1.00 22.06           C  
ATOM   1202  CG  ASP A 187      24.011  18.570  40.161  1.00 24.98           C  
ATOM   1203  OD1 ASP A 187      23.555  19.550  39.537  1.00 24.48           O  
ATOM   1204  OD2 ASP A 187      24.158  17.437  39.648  1.00 26.98           O  
ATOM   1205  N   LYS A 188      25.807  20.043  44.077  1.00 20.45           N  
ATOM   1206  CA  LYS A 188      26.003  20.031  45.525  1.00 21.29           C  
ATOM   1207  C   LYS A 188      26.279  21.378  46.183  1.00 21.42           C  
ATOM   1208  O   LYS A 188      25.719  21.678  47.236  1.00 24.45           O  
ATOM   1209  CB  LYS A 188      27.121  19.051  45.890  1.00 21.65           C  
ATOM   1210  CG  LYS A 188      26.895  17.629  45.373  1.00 25.13           C  
ATOM   1211  CD  LYS A 188      25.543  17.058  45.813  1.00 28.05           C  
ATOM   1212  CE  LYS A 188      25.447  16.918  47.328  1.00 29.00           C  
ATOM   1213  NZ  LYS A 188      26.538  16.060  47.868  1.00 30.61           N  
ATOM   1214  N   ALA A 189      27.143  22.188  45.579  1.00 21.30           N  
ATOM   1215  CA  ALA A 189      27.468  23.492  46.153  1.00 20.70           C  
ATOM   1216  C   ALA A 189      26.504  24.578  45.685  1.00 19.99           C  
ATOM   1217  O   ALA A 189      25.902  25.276  46.501  1.00 21.16           O  
ATOM   1218  CB  ALA A 189      28.902  23.878  45.799  1.00 20.00           C  
ATOM   1219  N   GLY A 190      26.358  24.711  44.370  1.00 18.26           N  
ATOM   1220  CA  GLY A 190      25.476  25.722  43.819  1.00 18.25           C  
ATOM   1221  C   GLY A 190      24.028  25.653  44.275  1.00 19.99           C  
ATOM   1222  O   GLY A 190      23.496  26.628  44.808  1.00 19.79           O  
ATOM   1223  N   ARG A 191      23.378  24.512  44.067  1.00 17.04           N  
ATOM   1224  CA  ARG A 191      21.982  24.377  44.467  1.00 19.12           C  
ATOM   1225  C   ARG A 191      21.800  24.611  45.965  1.00 18.43           C  
ATOM   1226  O   ARG A 191      20.803  25.193  46.385  1.00 19.58           O  
ATOM   1227  CB  ARG A 191      21.443  22.989  44.091  1.00 17.89           C  
ATOM   1228  CG  ARG A 191      21.397  22.730  42.592  1.00 19.59           C  
ATOM   1229  CD  ARG A 191      20.767  21.367  42.283  1.00 24.35           C  
ATOM   1230  NE  ARG A 191      20.643  21.152  40.845  1.00 30.28           N  
ATOM   1231  CZ  ARG A 191      20.353  19.984  40.276  1.00 33.18           C  
ATOM   1232  NH1 ARG A 191      20.150  18.901  41.021  1.00 31.51           N  
ATOM   1233  NH2 ARG A 191      20.281  19.896  38.954  1.00 33.98           N  
ATOM   1234  N   ALA A 192      22.771  24.171  46.757  1.00 16.28           N  
ATOM   1235  CA  ALA A 192      22.715  24.317  48.210  1.00 19.92           C  
ATOM   1236  C   ALA A 192      22.815  25.767  48.681  1.00 19.46           C  
ATOM   1237  O   ALA A 192      22.435  26.089  49.806  1.00 22.30           O  
ATOM   1238  CB  ALA A 192      23.824  23.483  48.859  1.00 19.14           C  
ATOM   1239  N   ILE A 193      23.329  26.646  47.833  1.00 18.66           N  
ATOM   1240  CA  ILE A 193      23.457  28.045  48.222  1.00 17.34           C  
ATOM   1241  C   ILE A 193      22.187  28.830  47.897  1.00 17.43           C  
ATOM   1242  O   ILE A 193      21.883  29.825  48.550  1.00 18.29           O  
ATOM   1243  CB  ILE A 193      24.679  28.705  47.522  1.00 16.89           C  
ATOM   1244  CG1 ILE A 193      25.966  28.023  47.993  1.00 14.94           C  
ATOM   1245  CG2 ILE A 193      24.729  30.202  47.819  1.00 15.15           C  
ATOM   1246  CD1 ILE A 193      26.218  28.141  49.488  1.00 15.97           C  
ATOM   1247  N   LEU A 194      21.435  28.360  46.907  1.00 16.61           N  
ATOM   1248  CA  LEU A 194      20.217  29.044  46.480  1.00 18.87           C  
ATOM   1249  C   LEU A 194      19.208  29.387  47.582  1.00 20.30           C  
ATOM   1250  O   LEU A 194      18.573  30.440  47.529  1.00 21.05           O  
ATOM   1251  CB  LEU A 194      19.511  28.233  45.386  1.00 17.28           C  
ATOM   1252  CG  LEU A 194      18.251  28.880  44.803  1.00 17.62           C  
ATOM   1253  CD1 LEU A 194      18.591  30.250  44.247  1.00 15.98           C  
ATOM   1254  CD2 LEU A 194      17.664  27.993  43.712  1.00 17.36           C  
ATOM   1255  N   GLN A 195      19.054  28.522  48.582  1.00 20.59           N  
ATOM   1256  CA  GLN A 195      18.086  28.812  49.635  1.00 20.98           C  
ATOM   1257  C   GLN A 195      18.460  30.027  50.476  1.00 20.99           C  
ATOM   1258  O   GLN A 195      17.594  30.624  51.113  1.00 20.68           O  
ATOM   1259  CB  GLN A 195      17.887  27.602  50.554  1.00 22.39           C  
ATOM   1260  CG  GLN A 195      19.098  27.206  51.373  1.00 22.59           C  
ATOM   1261  CD  GLN A 195      18.743  26.255  52.506  1.00 28.86           C  
ATOM   1262  OE1 GLN A 195      19.401  25.236  52.708  1.00 29.99           O  
ATOM   1263  NE2 GLN A 195      17.702  26.594  53.259  1.00 30.07           N  
ATOM   1264  N   PHE A 196      19.738  30.402  50.472  1.00 17.78           N  
ATOM   1265  CA  PHE A 196      20.188  31.548  51.261  1.00 18.81           C  
ATOM   1266  C   PHE A 196      20.320  32.875  50.515  1.00 18.52           C  
ATOM   1267  O   PHE A 196      20.150  33.936  51.116  1.00 18.03           O  
ATOM   1268  CB  PHE A 196      21.555  31.278  51.901  1.00 18.57           C  
ATOM   1269  CG  PHE A 196      21.626  30.016  52.709  1.00 20.93           C  
ATOM   1270  CD1 PHE A 196      22.241  28.881  52.191  1.00 19.23           C  
ATOM   1271  CD2 PHE A 196      21.106  29.970  53.998  1.00 19.89           C  
ATOM   1272  CE1 PHE A 196      22.340  27.720  52.945  1.00 20.37           C  
ATOM   1273  CE2 PHE A 196      21.198  28.812  54.763  1.00 20.86           C  
ATOM   1274  CZ  PHE A 196      21.818  27.683  54.236  1.00 21.52           C  
ATOM   1275  N   TYR A 197      20.631  32.824  49.220  1.00 17.84           N  
ATOM   1276  CA  TYR A 197      20.870  34.046  48.458  1.00 15.89           C  
ATOM   1277  C   TYR A 197      19.817  35.146  48.437  1.00 16.77           C  
ATOM   1278  O   TYR A 197      20.143  36.313  48.645  1.00 16.17           O  
ATOM   1279  CB  TYR A 197      21.267  33.716  47.013  1.00 14.37           C  
ATOM   1280  CG  TYR A 197      22.396  34.599  46.526  1.00 13.39           C  
ATOM   1281  CD1 TYR A 197      23.678  34.485  47.068  1.00 11.77           C  
ATOM   1282  CD2 TYR A 197      22.178  35.573  45.555  1.00 14.08           C  
ATOM   1283  CE1 TYR A 197      24.720  35.322  46.653  1.00 12.65           C  
ATOM   1284  CE2 TYR A 197      23.207  36.420  45.134  1.00 13.53           C  
ATOM   1285  CZ  TYR A 197      24.472  36.289  45.685  1.00 14.24           C  
ATOM   1286  OH  TYR A 197      25.484  37.127  45.274  1.00 15.11           O  
ATOM   1287  N   PRO A 198      18.546  34.805  48.173  1.00 16.14           N  
ATOM   1288  CA  PRO A 198      17.556  35.887  48.156  1.00 16.22           C  
ATOM   1289  C   PRO A 198      17.525  36.702  49.451  1.00 16.67           C  
ATOM   1290  O   PRO A 198      17.395  37.924  49.414  1.00 18.90           O  
ATOM   1291  CB  PRO A 198      16.240  35.150  47.888  1.00 16.46           C  
ATOM   1292  CG  PRO A 198      16.688  33.982  47.027  1.00 16.36           C  
ATOM   1293  CD  PRO A 198      17.939  33.525  47.766  1.00 16.20           C  
ATOM   1294  N   LYS A 199      17.655  36.030  50.590  1.00 17.12           N  
ATOM   1295  CA  LYS A 199      17.629  36.717  51.881  1.00 18.28           C  
ATOM   1296  C   LYS A 199      18.909  37.525  52.090  1.00 17.96           C  
ATOM   1297  O   LYS A 199      18.886  38.617  52.662  1.00 15.33           O  
ATOM   1298  CB  LYS A 199      17.459  35.711  53.019  1.00 20.03           C  
ATOM   1299  CG  LYS A 199      16.968  36.337  54.314  1.00 24.93           C  
ATOM   1300  CD  LYS A 199      15.626  37.010  54.076  1.00 29.71           C  
ATOM   1301  CE  LYS A 199      14.991  37.481  55.356  1.00 33.08           C  
ATOM   1302  NZ  LYS A 199      13.687  38.138  55.078  1.00 33.19           N  
ATOM   1303  N   TYR A 200      20.022  36.971  51.627  1.00 16.71           N  
ATOM   1304  CA  TYR A 200      21.314  37.638  51.715  1.00 16.94           C  
ATOM   1305  C   TYR A 200      21.251  38.961  50.949  1.00 14.98           C  
ATOM   1306  O   TYR A 200      21.702  39.997  51.434  1.00 14.92           O  
ATOM   1307  CB  TYR A 200      22.383  36.730  51.107  1.00 14.95           C  
ATOM   1308  CG  TYR A 200      23.567  37.445  50.490  1.00 13.63           C  
ATOM   1309  CD1 TYR A 200      24.576  37.988  51.286  1.00 13.32           C  
ATOM   1310  CD2 TYR A 200      23.694  37.543  49.101  1.00 14.54           C  
ATOM   1311  CE1 TYR A 200      25.693  38.608  50.715  1.00 14.67           C  
ATOM   1312  CE2 TYR A 200      24.802  38.162  48.518  1.00 13.31           C  
ATOM   1313  CZ  TYR A 200      25.797  38.688  49.329  1.00 12.39           C  
ATOM   1314  OH  TYR A 200      26.899  39.279  48.764  1.00 13.70           O  
ATOM   1315  N   VAL A 201      20.695  38.910  49.742  1.00 16.25           N  
ATOM   1316  CA  VAL A 201      20.568  40.091  48.888  1.00 15.73           C  
ATOM   1317  C   VAL A 201      19.705  41.168  49.546  1.00 17.00           C  
ATOM   1318  O   VAL A 201      20.044  42.359  49.532  1.00 14.95           O  
ATOM   1319  CB  VAL A 201      19.978  39.693  47.511  1.00 16.32           C  
ATOM   1320  CG1 VAL A 201      19.518  40.922  46.744  1.00 14.95           C  
ATOM   1321  CG2 VAL A 201      21.041  38.931  46.706  1.00 14.49           C  
ATOM   1322  N   GLU A 202      18.596  40.742  50.136  1.00 16.77           N  
ATOM   1323  CA  GLU A 202      17.695  41.670  50.802  1.00 18.55           C  
ATOM   1324  C   GLU A 202      18.413  42.355  51.959  1.00 17.80           C  
ATOM   1325  O   GLU A 202      18.380  43.576  52.081  1.00 17.11           O  
ATOM   1326  CB  GLU A 202      16.459  40.919  51.315  1.00 20.59           C  
ATOM   1327  CG  GLU A 202      15.554  41.728  52.234  1.00 27.30           C  
ATOM   1328  CD  GLU A 202      14.310  40.956  52.658  1.00 32.53           C  
ATOM   1329  OE1 GLU A 202      14.424  39.751  52.977  1.00 32.64           O  
ATOM   1330  OE2 GLU A 202      13.217  41.561  52.679  1.00 38.43           O  
ATOM   1331  N   LEU A 203      19.084  41.566  52.791  1.00 17.72           N  
ATOM   1332  CA  LEU A 203      19.782  42.107  53.951  1.00 17.47           C  
ATOM   1333  C   LEU A 203      21.006  42.963  53.638  1.00 17.17           C  
ATOM   1334  O   LEU A 203      21.205  43.995  54.273  1.00 16.30           O  
ATOM   1335  CB  LEU A 203      20.161  40.971  54.906  1.00 17.40           C  
ATOM   1336  CG  LEU A 203      18.941  40.262  55.503  1.00 22.59           C  
ATOM   1337  CD1 LEU A 203      19.386  39.093  56.366  1.00 22.34           C  
ATOM   1338  CD2 LEU A 203      18.119  41.256  56.319  1.00 22.15           C  
ATOM   1339  N   ILE A 204      21.823  42.560  52.666  1.00 14.58           N  
ATOM   1340  CA  ILE A 204      23.000  43.363  52.355  1.00 14.01           C  
ATOM   1341  C   ILE A 204      22.563  44.661  51.679  1.00 14.36           C  
ATOM   1342  O   ILE A 204      23.193  45.705  51.857  1.00 13.51           O  
ATOM   1343  CB  ILE A 204      24.023  42.592  51.472  1.00 13.57           C  
ATOM   1344  CG1 ILE A 204      25.331  43.389  51.395  1.00 11.74           C  
ATOM   1345  CG2 ILE A 204      23.462  42.349  50.074  1.00 12.52           C  
ATOM   1346  CD1 ILE A 204      26.469  42.632  50.735  1.00 11.93           C  
ATOM   1347  N   ASN A 205      21.474  44.600  50.916  1.00 14.39           N  
ATOM   1348  CA  ASN A 205      20.951  45.798  50.261  1.00 15.23           C  
ATOM   1349  C   ASN A 205      20.394  46.751  51.322  1.00 15.66           C  
ATOM   1350  O   ASN A 205      20.570  47.964  51.231  1.00 16.15           O  
ATOM   1351  CB  ASN A 205      19.837  45.448  49.264  1.00 15.19           C  
ATOM   1352  CG  ASN A 205      20.365  45.201  47.862  1.00 15.72           C  
ATOM   1353  OD1 ASN A 205      21.519  45.501  47.560  1.00 15.27           O  
ATOM   1354  ND2 ASN A 205      19.512  44.667  46.992  1.00 18.17           N  
ATOM   1355  N   GLN A 206      19.721  46.190  52.322  1.00 17.57           N  
ATOM   1356  CA  GLN A 206      19.146  46.989  53.404  1.00 18.43           C  
ATOM   1357  C   GLN A 206      20.261  47.727  54.139  1.00 17.44           C  
ATOM   1358  O   GLN A 206      20.158  48.924  54.402  1.00 17.22           O  
ATOM   1359  CB  GLN A 206      18.391  46.090  54.391  1.00 19.68           C  
ATOM   1360  CG  GLN A 206      17.537  46.858  55.391  1.00 22.74           C  
ATOM   1361  CD  GLN A 206      16.845  45.947  56.397  1.00 25.62           C  
ATOM   1362  OE1 GLN A 206      16.460  44.821  56.073  1.00 25.13           O  
ATOM   1363  NE2 GLN A 206      16.667  46.441  57.620  1.00 25.08           N  
ATOM   1364  N   ALA A 207      21.323  47.003  54.478  1.00 15.64           N  
ATOM   1365  CA  ALA A 207      22.460  47.604  55.162  1.00 16.63           C  
ATOM   1366  C   ALA A 207      23.038  48.727  54.303  1.00 16.39           C  
ATOM   1367  O   ALA A 207      23.385  49.790  54.813  1.00 18.77           O  
ATOM   1368  CB  ALA A 207      23.530  46.549  55.436  1.00 14.09           C  
ATOM   1369  N   ALA A 208      23.142  48.484  52.998  1.00 15.79           N  
ATOM   1370  CA  ALA A 208      23.672  49.482  52.076  1.00 16.70           C  
ATOM   1371  C   ALA A 208      22.827  50.758  52.102  1.00 17.22           C  
ATOM   1372  O   ALA A 208      23.369  51.866  52.172  1.00 14.26           O  
ATOM   1373  CB  ALA A 208      23.725  48.921  50.650  1.00 14.56           C  
ATOM   1374  N   ARG A 209      21.505  50.606  52.043  1.00 15.36           N  
ATOM   1375  CA  ARG A 209      20.622  51.774  52.064  1.00 17.46           C  
ATOM   1376  C   ARG A 209      20.701  52.506  53.404  1.00 17.66           C  
ATOM   1377  O   ARG A 209      20.569  53.729  53.460  1.00 16.54           O  
ATOM   1378  CB  ARG A 209      19.162  51.376  51.793  1.00 15.33           C  
ATOM   1379  CG  ARG A 209      18.893  50.824  50.388  1.00 17.28           C  
ATOM   1380  CD  ARG A 209      17.393  50.778  50.080  1.00 16.93           C  
ATOM   1381  NE  ARG A 209      16.638  50.067  51.108  1.00 19.77           N  
ATOM   1382  CZ  ARG A 209      16.521  48.744  51.180  1.00 22.01           C  
ATOM   1383  NH1 ARG A 209      17.107  47.966  50.271  1.00 19.52           N  
ATOM   1384  NH2 ARG A 209      15.823  48.197  52.169  1.00 18.66           N  
ATOM   1385  N   LEU A 210      20.916  51.759  54.482  1.00 17.65           N  
ATOM   1386  CA  LEU A 210      21.005  52.374  55.800  1.00 19.55           C  
ATOM   1387  C   LEU A 210      22.326  53.117  55.973  1.00 19.27           C  
ATOM   1388  O   LEU A 210      22.548  53.783  56.986  1.00 20.50           O  
ATOM   1389  CB  LEU A 210      20.827  51.315  56.898  1.00 19.64           C  
ATOM   1390  CG  LEU A 210      19.413  50.726  57.017  1.00 19.83           C  
ATOM   1391  CD1 LEU A 210      19.416  49.573  57.999  1.00 20.06           C  
ATOM   1392  CD2 LEU A 210      18.434  51.804  57.470  1.00 22.50           C  
ATOM   1393  N   ASN A 211      23.202  53.001  54.980  1.00 16.73           N  
ATOM   1394  CA  ASN A 211      24.481  53.693  55.021  1.00 16.25           C  
ATOM   1395  C   ASN A 211      24.572  54.763  53.934  1.00 17.24           C  
ATOM   1396  O   ASN A 211      25.652  55.290  53.655  1.00 17.37           O  
ATOM   1397  CB  ASN A 211      25.636  52.697  54.897  1.00 15.12           C  
ATOM   1398  CG  ASN A 211      25.891  51.952  56.195  1.00 19.42           C  
ATOM   1399  OD1 ASN A 211      26.139  52.571  57.234  1.00 19.98           O  
ATOM   1400  ND2 ASN A 211      25.825  50.622  56.148  1.00 18.09           N  
ATOM   1401  N   GLY A 212      23.429  55.066  53.321  1.00 15.75           N  
ATOM   1402  CA  GLY A 212      23.373  56.099  52.299  1.00 16.87           C  
ATOM   1403  C   GLY A 212      23.543  55.696  50.844  1.00 15.89           C  
ATOM   1404  O   GLY A 212      23.626  56.565  49.978  1.00 15.97           O  
ATOM   1405  N   TYR A 213      23.608  54.398  50.565  1.00 16.21           N  
ATOM   1406  CA  TYR A 213      23.764  53.922  49.189  1.00 14.57           C  
ATOM   1407  C   TYR A 213      22.423  53.462  48.628  1.00 15.50           C  
ATOM   1408  O   TYR A 213      21.483  53.254  49.385  1.00 17.45           O  
ATOM   1409  CB  TYR A 213      24.761  52.757  49.135  1.00 14.48           C  
ATOM   1410  CG  TYR A 213      26.167  53.146  49.521  1.00 15.74           C  
ATOM   1411  CD1 TYR A 213      26.665  52.860  50.787  1.00 14.52           C  
ATOM   1412  CD2 TYR A 213      26.989  53.833  48.627  1.00 16.81           C  
ATOM   1413  CE1 TYR A 213      27.951  53.250  51.158  1.00 16.68           C  
ATOM   1414  CE2 TYR A 213      28.274  54.231  48.988  1.00 16.81           C  
ATOM   1415  CZ  TYR A 213      28.747  53.935  50.255  1.00 16.66           C  
ATOM   1416  OH  TYR A 213      30.013  54.329  50.619  1.00 20.02           O  
ATOM   1417  N   VAL A 214      22.325  53.308  47.307  1.00 15.80           N  
ATOM   1418  CA  VAL A 214      21.069  52.854  46.713  1.00 15.94           C  
ATOM   1419  C   VAL A 214      20.926  51.335  46.830  1.00 15.52           C  
ATOM   1420  O   VAL A 214      19.810  50.817  46.890  1.00 16.08           O  
ATOM   1421  CB  VAL A 214      20.945  53.283  45.227  1.00 19.25           C  
ATOM   1422  CG1 VAL A 214      20.843  54.804  45.137  1.00 21.35           C  
ATOM   1423  CG2 VAL A 214      22.133  52.795  44.436  1.00 19.37           C  
ATOM   1424  N   ASP A 215      22.057  50.630  46.871  1.00 12.67           N  
ATOM   1425  CA  ASP A 215      22.077  49.169  47.017  1.00 12.71           C  
ATOM   1426  C   ASP A 215      23.507  48.677  47.273  1.00 11.44           C  
ATOM   1427  O   ASP A 215      24.450  49.463  47.236  1.00 12.92           O  
ATOM   1428  CB  ASP A 215      21.487  48.477  45.776  1.00 10.13           C  
ATOM   1429  CG  ASP A 215      22.273  48.765  44.509  1.00 12.08           C  
ATOM   1430  OD1 ASP A 215      23.483  48.446  44.453  1.00 15.10           O  
ATOM   1431  OD2 ASP A 215      21.676  49.312  43.561  1.00 15.37           O  
ATOM   1432  N   ALA A 216      23.666  47.381  47.537  1.00 12.55           N  
ATOM   1433  CA  ALA A 216      24.986  46.813  47.819  1.00 12.99           C  
ATOM   1434  C   ALA A 216      26.016  47.011  46.704  1.00 11.82           C  
ATOM   1435  O   ALA A 216      27.204  47.218  46.975  1.00 12.97           O  
ATOM   1436  CB  ALA A 216      24.855  45.318  48.148  1.00 12.30           C  
ATOM   1437  N   GLY A 217      25.570  46.935  45.453  1.00 10.87           N  
ATOM   1438  CA  GLY A 217      26.484  47.116  44.335  1.00 10.26           C  
ATOM   1439  C   GLY A 217      27.077  48.512  44.352  1.00 13.13           C  
ATOM   1440  O   GLY A 217      28.277  48.708  44.134  1.00 13.09           O  
ATOM   1441  N   ASP A 218      26.214  49.490  44.606  1.00 14.71           N  
ATOM   1442  CA  ASP A 218      26.615  50.894  44.685  1.00 15.46           C  
ATOM   1443  C   ASP A 218      27.652  51.008  45.804  1.00 15.19           C  
ATOM   1444  O   ASP A 218      28.718  51.598  45.626  1.00 14.88           O  
ATOM   1445  CB  ASP A 218      25.369  51.744  44.977  1.00 15.97           C  
ATOM   1446  CG  ASP A 218      25.671  53.226  45.132  1.00 17.81           C  
ATOM   1447  OD1 ASP A 218      26.503  53.765  44.373  1.00 16.36           O  
ATOM   1448  OD2 ASP A 218      25.040  53.856  46.005  1.00 18.13           O  
ATOM   1449  N   SER A 219      27.346  50.418  46.954  1.00 15.48           N  
ATOM   1450  CA  SER A 219      28.267  50.448  48.083  1.00 15.85           C  
ATOM   1451  C   SER A 219      29.650  49.877  47.723  1.00 15.52           C  
ATOM   1452  O   SER A 219      30.680  50.479  48.036  1.00 13.65           O  
ATOM   1453  CB  SER A 219      27.669  49.667  49.257  1.00 18.56           C  
ATOM   1454  OG  SER A 219      28.534  49.703  50.376  1.00 19.16           O  
ATOM   1455  N   TRP A 220      29.676  48.718  47.065  1.00 14.06           N  
ATOM   1456  CA  TRP A 220      30.945  48.093  46.672  1.00 14.44           C  
ATOM   1457  C   TRP A 220      31.735  48.923  45.662  1.00 14.40           C  
ATOM   1458  O   TRP A 220      32.956  49.057  45.776  1.00 11.76           O  
ATOM   1459  CB  TRP A 220      30.700  46.698  46.082  1.00 13.11           C  
ATOM   1460  CG  TRP A 220      30.248  45.674  47.075  1.00 14.95           C  
ATOM   1461  CD1 TRP A 220      29.985  45.868  48.405  1.00 16.16           C  
ATOM   1462  CD2 TRP A 220      30.022  44.282  46.820  1.00 15.48           C  
ATOM   1463  NE1 TRP A 220      29.612  44.680  48.992  1.00 16.30           N  
ATOM   1464  CE2 TRP A 220      29.626  43.691  48.041  1.00 17.39           C  
ATOM   1465  CE3 TRP A 220      30.117  43.477  45.676  1.00 12.92           C  
ATOM   1466  CZ2 TRP A 220      29.323  42.323  48.151  1.00 16.20           C  
ATOM   1467  CZ3 TRP A 220      29.817  42.120  45.784  1.00 15.52           C  
ATOM   1468  CH2 TRP A 220      29.425  41.558  47.014  1.00 15.29           C  
ATOM   1469  N   ARG A 221      31.043  49.471  44.665  1.00 14.90           N  
ATOM   1470  CA  ARG A 221      31.714  50.272  43.655  1.00 13.31           C  
ATOM   1471  C   ARG A 221      32.337  51.527  44.267  1.00 16.12           C  
ATOM   1472  O   ARG A 221      33.361  52.004  43.787  1.00 14.85           O  
ATOM   1473  CB  ARG A 221      30.740  50.668  42.528  1.00 14.60           C  
ATOM   1474  CG  ARG A 221      30.243  49.494  41.672  1.00 14.42           C  
ATOM   1475  CD  ARG A 221      29.472  49.970  40.447  1.00 12.08           C  
ATOM   1476  NE  ARG A 221      28.233  50.687  40.771  1.00 13.50           N  
ATOM   1477  CZ  ARG A 221      27.063  50.107  41.037  1.00 14.82           C  
ATOM   1478  NH1 ARG A 221      26.002  50.854  41.319  1.00 13.27           N  
ATOM   1479  NH2 ARG A 221      26.942  48.783  41.011  1.00 13.16           N  
ATOM   1480  N   SER A 222      31.730  52.050  45.332  1.00 15.54           N  
ATOM   1481  CA  SER A 222      32.239  53.260  45.977  1.00 16.04           C  
ATOM   1482  C   SER A 222      33.652  53.086  46.527  1.00 14.43           C  
ATOM   1483  O   SER A 222      34.339  54.069  46.789  1.00 14.48           O  
ATOM   1484  CB  SER A 222      31.309  53.703  47.112  1.00 16.20           C  
ATOM   1485  OG  SER A 222      31.590  52.997  48.309  1.00 20.61           O  
ATOM   1486  N   MET A 223      34.085  51.840  46.697  1.00 14.27           N  
ATOM   1487  CA  MET A 223      35.429  51.562  47.209  1.00 16.48           C  
ATOM   1488  C   MET A 223      36.517  52.121  46.298  1.00 15.51           C  
ATOM   1489  O   MET A 223      37.666  52.265  46.714  1.00 16.06           O  
ATOM   1490  CB  MET A 223      35.657  50.051  47.360  1.00 17.80           C  
ATOM   1491  CG  MET A 223      34.740  49.358  48.359  1.00 21.06           C  
ATOM   1492  SD  MET A 223      35.187  47.614  48.574  1.00 31.02           S  
ATOM   1493  CE  MET A 223      34.226  46.857  47.338  1.00 27.13           C  
ATOM   1494  N   TYR A 224      36.163  52.423  45.053  1.00 14.88           N  
ATOM   1495  CA  TYR A 224      37.135  52.956  44.105  1.00 15.20           C  
ATOM   1496  C   TYR A 224      37.126  54.479  44.023  1.00 14.46           C  
ATOM   1497  O   TYR A 224      38.000  55.068  43.393  1.00 14.81           O  
ATOM   1498  CB  TYR A 224      36.904  52.360  42.704  1.00 15.30           C  
ATOM   1499  CG  TYR A 224      37.206  50.880  42.631  1.00 13.36           C  
ATOM   1500  CD1 TYR A 224      36.245  49.935  42.986  1.00 12.66           C  
ATOM   1501  CD2 TYR A 224      38.479  50.427  42.281  1.00 12.94           C  
ATOM   1502  CE1 TYR A 224      36.544  48.568  43.000  1.00 13.69           C  
ATOM   1503  CE2 TYR A 224      38.792  49.064  42.293  1.00 14.05           C  
ATOM   1504  CZ  TYR A 224      37.818  48.143  42.659  1.00 13.41           C  
ATOM   1505  OH  TYR A 224      38.129  46.806  42.721  1.00 13.11           O  
ATOM   1506  N   GLU A 225      36.139  55.111  44.654  1.00 15.24           N  
ATOM   1507  CA  GLU A 225      36.028  56.574  44.642  1.00 16.61           C  
ATOM   1508  C   GLU A 225      36.191  57.103  43.222  1.00 15.97           C  
ATOM   1509  O   GLU A 225      36.852  58.114  42.991  1.00 16.36           O  
ATOM   1510  CB  GLU A 225      37.103  57.195  45.539  1.00 17.37           C  
ATOM   1511  CG  GLU A 225      37.109  56.665  46.966  1.00 22.10           C  
ATOM   1512  CD  GLU A 225      38.044  57.453  47.878  1.00 23.83           C  
ATOM   1513  OE1 GLU A 225      39.253  57.535  47.579  1.00 26.54           O  
ATOM   1514  OE2 GLU A 225      37.565  57.988  48.894  1.00 26.05           O  
ATOM   1515  N   THR A 226      35.575  56.413  42.273  1.00 16.18           N  
ATOM   1516  CA  THR A 226      35.678  56.786  40.872  1.00 17.13           C  
ATOM   1517  C   THR A 226      34.309  56.761  40.201  1.00 16.00           C  
ATOM   1518  O   THR A 226      33.818  55.707  39.797  1.00 15.27           O  
ATOM   1519  CB  THR A 226      36.628  55.824  40.144  1.00 18.70           C  
ATOM   1520  OG1 THR A 226      37.905  55.848  40.796  1.00 17.37           O  
ATOM   1521  CG2 THR A 226      36.789  56.226  38.679  1.00 17.93           C  
ATOM   1522  N   PRO A 227      33.673  57.936  40.077  1.00 15.23           N  
ATOM   1523  CA  PRO A 227      32.349  58.057  39.456  1.00 15.97           C  
ATOM   1524  C   PRO A 227      32.254  57.434  38.064  1.00 15.58           C  
ATOM   1525  O   PRO A 227      31.208  56.909  37.683  1.00 16.29           O  
ATOM   1526  CB  PRO A 227      32.120  59.569  39.426  1.00 16.42           C  
ATOM   1527  CG  PRO A 227      32.851  60.041  40.663  1.00 16.92           C  
ATOM   1528  CD  PRO A 227      34.141  59.242  40.584  1.00 15.95           C  
ATOM   1529  N   SER A 228      33.348  57.487  37.310  1.00 15.31           N  
ATOM   1530  CA  SER A 228      33.355  56.939  35.953  1.00 15.70           C  
ATOM   1531  C   SER A 228      33.728  55.452  35.884  1.00 14.57           C  
ATOM   1532  O   SER A 228      33.917  54.913  34.798  1.00 13.39           O  
ATOM   1533  CB  SER A 228      34.330  57.740  35.085  1.00 17.61           C  
ATOM   1534  OG  SER A 228      35.657  57.612  35.573  1.00 18.28           O  
ATOM   1535  N   LEU A 229      33.810  54.790  37.036  1.00 13.86           N  
ATOM   1536  CA  LEU A 229      34.200  53.376  37.094  1.00 14.52           C  
ATOM   1537  C   LEU A 229      33.577  52.437  36.056  1.00 13.87           C  
ATOM   1538  O   LEU A 229      34.299  51.777  35.311  1.00  9.84           O  
ATOM   1539  CB  LEU A 229      33.936  52.806  38.497  1.00 14.33           C  
ATOM   1540  CG  LEU A 229      34.446  51.379  38.763  1.00 17.84           C  
ATOM   1541  CD1 LEU A 229      35.965  51.348  38.632  1.00 17.38           C  
ATOM   1542  CD2 LEU A 229      34.033  50.922  40.161  1.00 17.16           C  
ATOM   1543  N   GLU A 230      32.248  52.363  36.003  1.00 13.07           N  
ATOM   1544  CA  GLU A 230      31.607  51.448  35.061  1.00 14.77           C  
ATOM   1545  C   GLU A 230      32.030  51.664  33.618  1.00 14.11           C  
ATOM   1546  O   GLU A 230      32.295  50.704  32.895  1.00 14.05           O  
ATOM   1547  CB  GLU A 230      30.079  51.514  35.191  1.00 12.37           C  
ATOM   1548  CG  GLU A 230      29.591  51.176  36.596  1.00 15.59           C  
ATOM   1549  CD  GLU A 230      28.174  50.633  36.623  1.00 17.28           C  
ATOM   1550  OE1 GLU A 230      27.524  50.604  35.560  1.00 21.19           O  
ATOM   1551  OE2 GLU A 230      27.714  50.234  37.712  1.00 18.05           O  
ATOM   1552  N   GLN A 231      32.108  52.919  33.200  1.00 15.79           N  
ATOM   1553  CA  GLN A 231      32.522  53.232  31.839  1.00 16.53           C  
ATOM   1554  C   GLN A 231      34.001  52.901  31.642  1.00 17.20           C  
ATOM   1555  O   GLN A 231      34.382  52.314  30.625  1.00 15.46           O  
ATOM   1556  CB  GLN A 231      32.280  54.712  31.547  1.00 21.41           C  
ATOM   1557  CG  GLN A 231      30.809  55.095  31.459  1.00 27.97           C  
ATOM   1558  CD  GLN A 231      30.587  56.587  31.641  1.00 32.44           C  
ATOM   1559  OE1 GLN A 231      29.655  57.162  31.077  1.00 34.42           O  
ATOM   1560  NE2 GLN A 231      31.439  57.220  32.447  1.00 33.41           N  
ATOM   1561  N   ASP A 232      34.830  53.280  32.612  1.00 16.67           N  
ATOM   1562  CA  ASP A 232      36.263  53.011  32.524  1.00 15.94           C  
ATOM   1563  C   ASP A 232      36.535  51.519  32.346  1.00 16.31           C  
ATOM   1564  O   ASP A 232      37.341  51.121  31.507  1.00 17.06           O  
ATOM   1565  CB  ASP A 232      36.998  53.485  33.781  1.00 19.14           C  
ATOM   1566  CG  ASP A 232      37.032  54.998  33.914  1.00 22.47           C  
ATOM   1567  OD1 ASP A 232      37.016  55.698  32.878  1.00 21.52           O  
ATOM   1568  OD2 ASP A 232      37.097  55.486  35.060  1.00 22.10           O  
ATOM   1569  N   LEU A 233      35.866  50.696  33.146  1.00 15.79           N  
ATOM   1570  CA  LEU A 233      36.056  49.251  33.082  1.00 16.11           C  
ATOM   1571  C   LEU A 233      35.567  48.667  31.757  1.00 16.10           C  
ATOM   1572  O   LEU A 233      36.175  47.746  31.215  1.00 14.50           O  
ATOM   1573  CB  LEU A 233      35.334  48.585  34.258  1.00 17.87           C  
ATOM   1574  CG  LEU A 233      35.807  49.044  35.641  1.00 18.11           C  
ATOM   1575  CD1 LEU A 233      35.050  48.285  36.717  1.00 19.50           C  
ATOM   1576  CD2 LEU A 233      37.303  48.819  35.781  1.00 19.36           C  
ATOM   1577  N   GLU A 234      34.468  49.206  31.240  1.00 17.12           N  
ATOM   1578  CA  GLU A 234      33.911  48.745  29.970  1.00 18.85           C  
ATOM   1579  C   GLU A 234      34.890  49.034  28.830  1.00 19.85           C  
ATOM   1580  O   GLU A 234      35.077  48.207  27.935  1.00 19.78           O  
ATOM   1581  CB  GLU A 234      32.571  49.440  29.708  1.00 21.26           C  
ATOM   1582  CG  GLU A 234      31.924  49.123  28.364  1.00 27.69           C  
ATOM   1583  CD  GLU A 234      31.617  47.648  28.189  1.00 34.09           C  
ATOM   1584  OE1 GLU A 234      31.001  47.050  29.100  1.00 36.70           O  
ATOM   1585  OE2 GLU A 234      31.984  47.087  27.134  1.00 37.08           O  
ATOM   1586  N   ARG A 235      35.515  50.210  28.859  1.00 17.74           N  
ATOM   1587  CA  ARG A 235      36.475  50.567  27.822  1.00 17.75           C  
ATOM   1588  C   ARG A 235      37.686  49.645  27.894  1.00 16.78           C  
ATOM   1589  O   ARG A 235      38.203  49.206  26.867  1.00 15.67           O  
ATOM   1590  CB  ARG A 235      36.920  52.026  27.970  1.00 20.40           C  
ATOM   1591  CG  ARG A 235      35.885  53.041  27.507  1.00 25.02           C  
ATOM   1592  CD  ARG A 235      36.506  54.424  27.397  1.00 28.27           C  
ATOM   1593  NE  ARG A 235      36.724  55.042  28.701  1.00 34.44           N  
ATOM   1594  CZ  ARG A 235      35.776  55.660  29.401  1.00 36.31           C  
ATOM   1595  NH1 ARG A 235      34.541  55.747  28.920  1.00 36.59           N  
ATOM   1596  NH2 ARG A 235      36.061  56.191  30.582  1.00 36.92           N  
ATOM   1597  N   LEU A 236      38.140  49.352  29.108  1.00 15.01           N  
ATOM   1598  CA  LEU A 236      39.280  48.459  29.289  1.00 14.82           C  
ATOM   1599  C   LEU A 236      38.932  47.076  28.743  1.00 17.23           C  
ATOM   1600  O   LEU A 236      39.737  46.439  28.054  1.00 15.82           O  
ATOM   1601  CB  LEU A 236      39.646  48.362  30.773  1.00 16.36           C  
ATOM   1602  CG  LEU A 236      40.160  49.672  31.381  1.00 16.60           C  
ATOM   1603  CD1 LEU A 236      40.344  49.515  32.884  1.00 16.07           C  
ATOM   1604  CD2 LEU A 236      41.486  50.064  30.709  1.00 15.87           C  
ATOM   1605  N   PHE A 237      37.723  46.616  29.046  1.00 15.48           N  
ATOM   1606  CA  PHE A 237      37.286  45.314  28.569  1.00 16.55           C  
ATOM   1607  C   PHE A 237      37.291  45.258  27.043  1.00 17.17           C  
ATOM   1608  O   PHE A 237      37.776  44.295  26.445  1.00 15.21           O  
ATOM   1609  CB  PHE A 237      35.879  44.994  29.062  1.00 18.24           C  
ATOM   1610  CG  PHE A 237      35.345  43.707  28.512  1.00 21.70           C  
ATOM   1611  CD1 PHE A 237      35.826  42.488  28.981  1.00 22.36           C  
ATOM   1612  CD2 PHE A 237      34.425  43.711  27.468  1.00 21.62           C  
ATOM   1613  CE1 PHE A 237      35.403  41.292  28.415  1.00 24.19           C  
ATOM   1614  CE2 PHE A 237      33.996  42.517  26.894  1.00 23.63           C  
ATOM   1615  CZ  PHE A 237      34.489  41.306  27.371  1.00 22.93           C  
ATOM   1616  N   GLN A 238      36.739  46.292  26.416  1.00 16.96           N  
ATOM   1617  CA  GLN A 238      36.677  46.361  24.962  1.00 17.31           C  
ATOM   1618  C   GLN A 238      38.048  46.354  24.292  1.00 16.49           C  
ATOM   1619  O   GLN A 238      38.197  45.811  23.207  1.00 15.38           O  
ATOM   1620  CB  GLN A 238      35.905  47.606  24.517  1.00 19.68           C  
ATOM   1621  CG  GLN A 238      34.408  47.569  24.831  1.00 24.90           C  
ATOM   1622  CD  GLN A 238      33.706  46.381  24.198  1.00 28.78           C  
ATOM   1623  OE1 GLN A 238      33.938  46.057  23.032  1.00 31.92           O  
ATOM   1624  NE2 GLN A 238      32.832  45.732  24.960  1.00 30.59           N  
ATOM   1625  N   GLU A 239      39.046  46.960  24.926  1.00 16.98           N  
ATOM   1626  CA  GLU A 239      40.386  46.992  24.345  1.00 20.14           C  
ATOM   1627  C   GLU A 239      41.032  45.614  24.291  1.00 19.09           C  
ATOM   1628  O   GLU A 239      41.861  45.344  23.420  1.00 17.60           O  
ATOM   1629  CB  GLU A 239      41.288  47.941  25.129  1.00 23.65           C  
ATOM   1630  CG  GLU A 239      40.839  49.382  25.073  1.00 30.06           C  
ATOM   1631  CD  GLU A 239      41.821  50.306  25.743  1.00 35.93           C  
ATOM   1632  OE1 GLU A 239      42.956  50.432  25.234  1.00 40.83           O  
ATOM   1633  OE2 GLU A 239      41.465  50.903  26.779  1.00 39.30           O  
ATOM   1634  N   LEU A 240      40.652  44.745  25.222  1.00 17.35           N  
ATOM   1635  CA  LEU A 240      41.197  43.393  25.269  1.00 18.44           C  
ATOM   1636  C   LEU A 240      40.366  42.366  24.495  1.00 18.59           C  
ATOM   1637  O   LEU A 240      40.722  41.188  24.434  1.00 17.40           O  
ATOM   1638  CB  LEU A 240      41.356  42.961  26.726  1.00 20.14           C  
ATOM   1639  CG  LEU A 240      42.655  43.506  27.322  1.00 24.11           C  
ATOM   1640  CD1 LEU A 240      42.449  43.927  28.754  1.00 26.75           C  
ATOM   1641  CD2 LEU A 240      43.731  42.429  27.210  1.00 25.08           C  
ATOM   1642  N   GLN A 241      39.270  42.818  23.894  1.00 18.72           N  
ATOM   1643  CA  GLN A 241      38.395  41.941  23.117  1.00 21.08           C  
ATOM   1644  C   GLN A 241      39.098  41.233  21.960  1.00 21.24           C  
ATOM   1645  O   GLN A 241      39.024  40.010  21.835  1.00 23.38           O  
ATOM   1646  CB  GLN A 241      37.207  42.734  22.565  1.00 22.80           C  
ATOM   1647  CG  GLN A 241      35.993  42.745  23.461  1.00 24.90           C  
ATOM   1648  CD  GLN A 241      35.383  41.367  23.607  1.00 27.57           C  
ATOM   1649  OE1 GLN A 241      35.940  40.495  24.274  1.00 28.36           O  
ATOM   1650  NE2 GLN A 241      34.235  41.161  22.973  1.00 28.83           N  
ATOM   1651  N   PRO A 242      39.783  41.992  21.091  1.00 21.84           N  
ATOM   1652  CA  PRO A 242      40.476  41.364  19.961  1.00 22.92           C  
ATOM   1653  C   PRO A 242      41.398  40.223  20.381  1.00 22.91           C  
ATOM   1654  O   PRO A 242      41.432  39.162  19.745  1.00 23.26           O  
ATOM   1655  CB  PRO A 242      41.237  42.531  19.336  1.00 23.77           C  
ATOM   1656  CG  PRO A 242      40.304  43.685  19.570  1.00 21.85           C  
ATOM   1657  CD  PRO A 242      39.893  43.462  21.019  1.00 22.66           C  
ATOM   1658  N   LEU A 243      42.142  40.442  21.457  1.00 22.09           N  
ATOM   1659  CA  LEU A 243      43.062  39.433  21.951  1.00 19.44           C  
ATOM   1660  C   LEU A 243      42.294  38.234  22.511  1.00 18.52           C  
ATOM   1661  O   LEU A 243      42.607  37.087  22.186  1.00 16.12           O  
ATOM   1662  CB  LEU A 243      43.971  40.044  23.017  1.00 21.98           C  
ATOM   1663  CG  LEU A 243      45.175  39.249  23.520  1.00 26.32           C  
ATOM   1664  CD1 LEU A 243      45.869  38.537  22.366  1.00 25.68           C  
ATOM   1665  CD2 LEU A 243      46.138  40.216  24.215  1.00 26.73           C  
ATOM   1666  N   TYR A 244      41.286  38.487  23.345  1.00 15.05           N  
ATOM   1667  CA  TYR A 244      40.520  37.376  23.897  1.00 16.26           C  
ATOM   1668  C   TYR A 244      39.816  36.576  22.801  1.00 14.63           C  
ATOM   1669  O   TYR A 244      39.852  35.346  22.803  1.00 13.73           O  
ATOM   1670  CB  TYR A 244      39.462  37.844  24.898  1.00 14.51           C  
ATOM   1671  CG  TYR A 244      38.655  36.674  25.425  1.00 15.81           C  
ATOM   1672  CD1 TYR A 244      39.259  35.687  26.205  1.00 14.55           C  
ATOM   1673  CD2 TYR A 244      37.313  36.512  25.082  1.00 15.17           C  
ATOM   1674  CE1 TYR A 244      38.550  34.567  26.627  1.00 15.08           C  
ATOM   1675  CE2 TYR A 244      36.592  35.394  25.499  1.00 14.87           C  
ATOM   1676  CZ  TYR A 244      37.217  34.427  26.271  1.00 13.90           C  
ATOM   1677  OH  TYR A 244      36.513  33.326  26.697  1.00 13.75           O  
ATOM   1678  N   LEU A 245      39.174  37.268  21.865  1.00 14.03           N  
ATOM   1679  CA  LEU A 245      38.458  36.567  20.799  1.00 15.37           C  
ATOM   1680  C   LEU A 245      39.381  35.691  19.960  1.00 15.77           C  
ATOM   1681  O   LEU A 245      38.986  34.612  19.513  1.00 15.97           O  
ATOM   1682  CB  LEU A 245      37.718  37.563  19.906  1.00 15.87           C  
ATOM   1683  CG  LEU A 245      36.570  38.318  20.588  1.00 18.77           C  
ATOM   1684  CD1 LEU A 245      35.991  39.340  19.620  1.00 17.96           C  
ATOM   1685  CD2 LEU A 245      35.494  37.336  21.039  1.00 19.76           C  
ATOM   1686  N   ASN A 246      40.609  36.151  19.740  1.00 13.92           N  
ATOM   1687  CA  ASN A 246      41.558  35.367  18.965  1.00 14.44           C  
ATOM   1688  C   ASN A 246      42.044  34.158  19.760  1.00 14.54           C  
ATOM   1689  O   ASN A 246      42.272  33.090  19.199  1.00 12.53           O  
ATOM   1690  CB  ASN A 246      42.734  36.239  18.528  1.00 14.75           C  
ATOM   1691  CG  ASN A 246      42.463  36.954  17.219  1.00 17.20           C  
ATOM   1692  OD1 ASN A 246      42.442  36.330  16.157  1.00 16.39           O  
ATOM   1693  ND2 ASN A 246      42.239  38.266  17.288  1.00 16.71           N  
ATOM   1694  N   LEU A 247      42.192  34.319  21.071  1.00 12.24           N  
ATOM   1695  CA  LEU A 247      42.635  33.204  21.900  1.00 13.24           C  
ATOM   1696  C   LEU A 247      41.507  32.173  21.972  1.00 12.49           C  
ATOM   1697  O   LEU A 247      41.747  30.969  21.906  1.00 10.75           O  
ATOM   1698  CB  LEU A 247      42.986  33.691  23.311  1.00 12.96           C  
ATOM   1699  CG  LEU A 247      43.378  32.597  24.310  1.00 12.38           C  
ATOM   1700  CD1 LEU A 247      44.717  31.969  23.898  1.00 12.63           C  
ATOM   1701  CD2 LEU A 247      43.484  33.201  25.713  1.00 14.10           C  
ATOM   1702  N   HIS A 248      40.280  32.669  22.111  1.00 12.22           N  
ATOM   1703  CA  HIS A 248      39.080  31.837  22.190  1.00 13.07           C  
ATOM   1704  C   HIS A 248      38.946  30.972  20.936  1.00 13.49           C  
ATOM   1705  O   HIS A 248      38.766  29.759  21.026  1.00 14.71           O  
ATOM   1706  CB  HIS A 248      37.847  32.740  22.333  1.00 11.98           C  
ATOM   1707  CG  HIS A 248      36.539  32.007  22.308  1.00 12.16           C  
ATOM   1708  ND1 HIS A 248      35.844  31.678  23.454  1.00 14.66           N  
ATOM   1709  CD2 HIS A 248      35.775  31.586  21.273  1.00  9.43           C  
ATOM   1710  CE1 HIS A 248      34.707  31.091  23.126  1.00 10.50           C  
ATOM   1711  NE2 HIS A 248      34.641  31.022  21.808  1.00 16.46           N  
ATOM   1712  N   ALA A 249      39.037  31.603  19.769  1.00 11.17           N  
ATOM   1713  CA  ALA A 249      38.918  30.891  18.501  1.00 12.70           C  
ATOM   1714  C   ALA A 249      40.010  29.828  18.328  1.00 13.11           C  
ATOM   1715  O   ALA A 249      39.752  28.728  17.828  1.00 14.49           O  
ATOM   1716  CB  ALA A 249      38.966  31.887  17.342  1.00 11.01           C  
ATOM   1717  N   TYR A 250      41.231  30.161  18.734  1.00 14.23           N  
ATOM   1718  CA  TYR A 250      42.349  29.230  18.624  1.00 14.13           C  
ATOM   1719  C   TYR A 250      42.142  28.025  19.544  1.00 14.20           C  
ATOM   1720  O   TYR A 250      42.339  26.876  19.140  1.00 12.95           O  
ATOM   1721  CB  TYR A 250      43.658  29.942  18.979  1.00 13.18           C  
ATOM   1722  CG  TYR A 250      44.863  29.030  19.022  1.00 15.59           C  
ATOM   1723  CD1 TYR A 250      45.465  28.571  17.849  1.00 16.24           C  
ATOM   1724  CD2 TYR A 250      45.390  28.609  20.239  1.00 14.46           C  
ATOM   1725  CE1 TYR A 250      46.565  27.709  17.889  1.00 16.63           C  
ATOM   1726  CE2 TYR A 250      46.482  27.753  20.291  1.00 19.39           C  
ATOM   1727  CZ  TYR A 250      47.065  27.305  19.114  1.00 18.64           C  
ATOM   1728  OH  TYR A 250      48.143  26.448  19.182  1.00 19.16           O  
ATOM   1729  N   VAL A 251      41.747  28.291  20.785  1.00 13.42           N  
ATOM   1730  CA  VAL A 251      41.514  27.217  21.744  1.00 13.04           C  
ATOM   1731  C   VAL A 251      40.328  26.351  21.309  1.00 13.40           C  
ATOM   1732  O   VAL A 251      40.356  25.129  21.451  1.00 12.76           O  
ATOM   1733  CB  VAL A 251      41.263  27.790  23.156  1.00 12.69           C  
ATOM   1734  CG1 VAL A 251      40.806  26.681  24.113  1.00 10.82           C  
ATOM   1735  CG2 VAL A 251      42.544  28.439  23.674  1.00 11.44           C  
ATOM   1736  N   ARG A 252      39.294  26.989  20.770  1.00 12.27           N  
ATOM   1737  CA  ARG A 252      38.112  26.276  20.301  1.00 12.41           C  
ATOM   1738  C   ARG A 252      38.497  25.290  19.189  1.00 15.02           C  
ATOM   1739  O   ARG A 252      37.973  24.174  19.121  1.00 14.50           O  
ATOM   1740  CB  ARG A 252      37.073  27.280  19.788  1.00 10.58           C  
ATOM   1741  CG  ARG A 252      35.801  26.655  19.227  1.00 10.97           C  
ATOM   1742  CD  ARG A 252      34.793  27.732  18.829  1.00 11.14           C  
ATOM   1743  NE  ARG A 252      35.374  28.708  17.911  1.00 12.22           N  
ATOM   1744  CZ  ARG A 252      34.815  29.873  17.593  1.00 14.58           C  
ATOM   1745  NH1 ARG A 252      33.647  30.225  18.119  1.00 12.82           N  
ATOM   1746  NH2 ARG A 252      35.431  30.691  16.744  1.00 13.94           N  
ATOM   1747  N   ARG A 253      39.415  25.705  18.320  1.00 15.37           N  
ATOM   1748  CA  ARG A 253      39.865  24.842  17.231  1.00 16.53           C  
ATOM   1749  C   ARG A 253      40.592  23.615  17.793  1.00 17.62           C  
ATOM   1750  O   ARG A 253      40.369  22.490  17.340  1.00 16.82           O  
ATOM   1751  CB  ARG A 253      40.791  25.619  16.289  1.00 15.14           C  
ATOM   1752  CG  ARG A 253      41.532  24.771  15.262  1.00 17.18           C  
ATOM   1753  CD  ARG A 253      40.608  24.186  14.201  1.00 17.98           C  
ATOM   1754  NE  ARG A 253      39.899  25.226  13.458  1.00 17.50           N  
ATOM   1755  CZ  ARG A 253      39.121  24.987  12.406  1.00 20.20           C  
ATOM   1756  NH1 ARG A 253      38.505  25.989  11.789  1.00 17.52           N  
ATOM   1757  NH2 ARG A 253      38.967  23.742  11.963  1.00 18.66           N  
ATOM   1758  N   ALA A 254      41.456  23.838  18.782  1.00 16.05           N  
ATOM   1759  CA  ALA A 254      42.213  22.751  19.400  1.00 16.40           C  
ATOM   1760  C   ALA A 254      41.288  21.770  20.122  1.00 17.14           C  
ATOM   1761  O   ALA A 254      41.527  20.560  20.111  1.00 15.20           O  
ATOM   1762  CB  ALA A 254      43.247  23.312  20.369  1.00 15.81           C  
ATOM   1763  N   LEU A 255      40.237  22.289  20.748  1.00 14.27           N  
ATOM   1764  CA  LEU A 255      39.285  21.428  21.449  1.00 16.86           C  
ATOM   1765  C   LEU A 255      38.502  20.615  20.422  1.00 17.67           C  
ATOM   1766  O   LEU A 255      38.172  19.452  20.651  1.00 17.19           O  
ATOM   1767  CB  LEU A 255      38.331  22.266  22.301  1.00 15.32           C  
ATOM   1768  CG  LEU A 255      38.945  22.925  23.542  1.00 17.90           C  
ATOM   1769  CD1 LEU A 255      37.887  23.785  24.230  1.00 15.75           C  
ATOM   1770  CD2 LEU A 255      39.470  21.850  24.505  1.00 13.91           C  
ATOM   1771  N   HIS A 256      38.212  21.245  19.286  1.00 16.68           N  
ATOM   1772  CA  HIS A 256      37.494  20.601  18.196  1.00 18.26           C  
ATOM   1773  C   HIS A 256      38.361  19.421  17.740  1.00 19.03           C  
ATOM   1774  O   HIS A 256      37.866  18.327  17.471  1.00 17.36           O  
ATOM   1775  CB  HIS A 256      37.292  21.621  17.062  1.00 18.41           C  
ATOM   1776  CG  HIS A 256      36.648  21.061  15.831  1.00 18.72           C  
ATOM   1777  ND1 HIS A 256      37.351  20.359  14.875  1.00 18.34           N  
ATOM   1778  CD2 HIS A 256      35.373  21.137  15.380  1.00 17.00           C  
ATOM   1779  CE1 HIS A 256      36.537  20.031  13.887  1.00 14.90           C  
ATOM   1780  NE2 HIS A 256      35.332  20.492  14.169  1.00 16.90           N  
ATOM   1781  N   ARG A 257      39.666  19.659  17.700  1.00 18.55           N  
ATOM   1782  CA  ARG A 257      40.649  18.662  17.295  1.00 20.61           C  
ATOM   1783  C   ARG A 257      40.679  17.468  18.253  1.00 20.35           C  
ATOM   1784  O   ARG A 257      40.773  16.314  17.825  1.00 19.01           O  
ATOM   1785  CB  ARG A 257      42.028  19.320  17.254  1.00 23.74           C  
ATOM   1786  CG  ARG A 257      42.870  19.014  16.032  1.00 30.47           C  
ATOM   1787  CD  ARG A 257      43.922  20.102  15.857  1.00 33.76           C  
ATOM   1788  NE  ARG A 257      44.686  20.306  17.083  1.00 33.81           N  
ATOM   1789  CZ  ARG A 257      45.113  21.487  17.514  1.00 35.70           C  
ATOM   1790  NH1 ARG A 257      44.852  22.587  16.817  1.00 35.23           N  
ATOM   1791  NH2 ARG A 257      45.800  21.569  18.646  1.00 36.87           N  
ATOM   1792  N   HIS A 258      40.586  17.747  19.550  1.00 19.12           N  
ATOM   1793  CA  HIS A 258      40.641  16.692  20.559  1.00 20.16           C  
ATOM   1794  C   HIS A 258      39.327  15.997  20.903  1.00 20.43           C  
ATOM   1795  O   HIS A 258      39.276  14.768  20.978  1.00 20.43           O  
ATOM   1796  CB  HIS A 258      41.247  17.230  21.858  1.00 21.21           C  
ATOM   1797  CG  HIS A 258      41.407  16.184  22.916  1.00 23.81           C  
ATOM   1798  ND1 HIS A 258      42.440  15.270  22.909  1.00 26.00           N  
ATOM   1799  CD2 HIS A 258      40.632  15.866  23.980  1.00 24.22           C  
ATOM   1800  CE1 HIS A 258      42.292  14.433  23.921  1.00 24.08           C  
ATOM   1801  NE2 HIS A 258      41.202  14.772  24.585  1.00 27.58           N  
ATOM   1802  N   TYR A 259      38.270  16.772  21.123  1.00 19.15           N  
ATOM   1803  CA  TYR A 259      36.990  16.194  21.503  1.00 18.20           C  
ATOM   1804  C   TYR A 259      36.026  15.842  20.375  1.00 19.53           C  
ATOM   1805  O   TYR A 259      34.985  15.235  20.624  1.00 19.64           O  
ATOM   1806  CB  TYR A 259      36.298  17.098  22.527  1.00 17.79           C  
ATOM   1807  CG  TYR A 259      37.025  17.158  23.859  1.00 17.11           C  
ATOM   1808  CD1 TYR A 259      37.840  18.242  24.188  1.00 14.34           C  
ATOM   1809  CD2 TYR A 259      36.922  16.111  24.778  1.00 17.43           C  
ATOM   1810  CE1 TYR A 259      38.538  18.284  25.403  1.00 15.63           C  
ATOM   1811  CE2 TYR A 259      37.616  16.140  25.990  1.00 16.23           C  
ATOM   1812  CZ  TYR A 259      38.421  17.227  26.296  1.00 17.84           C  
ATOM   1813  OH  TYR A 259      39.117  17.242  27.485  1.00 16.73           O  
ATOM   1814  N   GLY A 260      36.359  16.224  19.145  1.00 19.76           N  
ATOM   1815  CA  GLY A 260      35.503  15.890  18.017  1.00 19.38           C  
ATOM   1816  C   GLY A 260      34.552  16.967  17.537  1.00 17.77           C  
ATOM   1817  O   GLY A 260      34.058  17.772  18.317  1.00 16.36           O  
ATOM   1818  N   ALA A 261      34.279  16.958  16.237  1.00 18.00           N  
ATOM   1819  CA  ALA A 261      33.392  17.939  15.620  1.00 17.85           C  
ATOM   1820  C   ALA A 261      31.961  17.871  16.142  1.00 17.75           C  
ATOM   1821  O   ALA A 261      31.235  18.859  16.095  1.00 17.45           O  
ATOM   1822  CB  ALA A 261      33.401  17.757  14.094  1.00 18.60           C  
ATOM   1823  N   GLN A 262      31.548  16.705  16.631  1.00 17.76           N  
ATOM   1824  CA  GLN A 262      30.194  16.544  17.149  1.00 17.65           C  
ATOM   1825  C   GLN A 262      30.005  17.229  18.503  1.00 18.04           C  
ATOM   1826  O   GLN A 262      28.873  17.405  18.960  1.00 17.48           O  
ATOM   1827  CB  GLN A 262      29.845  15.053  17.276  1.00 19.36           C  
ATOM   1828  CG  GLN A 262      29.784  14.287  15.947  1.00 18.52           C  
ATOM   1829  CD  GLN A 262      28.512  14.554  15.153  1.00 19.88           C  
ATOM   1830  OE1 GLN A 262      27.616  15.264  15.606  1.00 19.17           O  
ATOM   1831  NE2 GLN A 262      28.428  13.973  13.959  1.00 18.08           N  
ATOM   1832  N   HIS A 263      31.105  17.630  19.137  1.00 16.33           N  
ATOM   1833  CA  HIS A 263      31.021  18.277  20.446  1.00 17.25           C  
ATOM   1834  C   HIS A 263      31.519  19.720  20.480  1.00 18.08           C  
ATOM   1835  O   HIS A 263      31.356  20.409  21.488  1.00 19.39           O  
ATOM   1836  CB  HIS A 263      31.784  17.445  21.478  1.00 18.66           C  
ATOM   1837  CG  HIS A 263      31.345  16.014  21.532  1.00 21.25           C  
ATOM   1838  ND1 HIS A 263      30.114  15.631  22.021  1.00 22.71           N  
ATOM   1839  CD2 HIS A 263      31.954  14.879  21.111  1.00 21.69           C  
ATOM   1840  CE1 HIS A 263      29.982  14.322  21.894  1.00 23.73           C  
ATOM   1841  NE2 HIS A 263      31.084  13.842  21.344  1.00 24.62           N  
ATOM   1842  N   ILE A 264      32.122  20.180  19.387  1.00 17.59           N  
ATOM   1843  CA  ILE A 264      32.625  21.552  19.323  1.00 17.39           C  
ATOM   1844  C   ILE A 264      32.150  22.259  18.060  1.00 15.69           C  
ATOM   1845  O   ILE A 264      32.467  21.836  16.948  1.00 16.28           O  
ATOM   1846  CB  ILE A 264      34.177  21.600  19.335  1.00 18.25           C  
ATOM   1847  CG1 ILE A 264      34.724  20.998  20.634  1.00 19.74           C  
ATOM   1848  CG2 ILE A 264      34.650  23.050  19.161  1.00 19.44           C  
ATOM   1849  CD1 ILE A 264      34.452  21.827  21.889  1.00 19.50           C  
ATOM   1850  N   ASN A 265      31.381  23.328  18.234  1.00 14.98           N  
ATOM   1851  CA  ASN A 265      30.896  24.112  17.105  1.00 17.48           C  
ATOM   1852  C   ASN A 265      31.946  25.194  16.840  1.00 17.45           C  
ATOM   1853  O   ASN A 265      32.135  26.091  17.662  1.00 17.17           O  
ATOM   1854  CB  ASN A 265      29.559  24.766  17.450  1.00 18.21           C  
ATOM   1855  CG  ASN A 265      28.995  25.586  16.304  1.00 20.95           C  
ATOM   1856  OD1 ASN A 265      29.639  25.764  15.271  1.00 18.66           O  
ATOM   1857  ND2 ASN A 265      27.786  26.096  16.487  1.00 24.30           N  
ATOM   1858  N   LEU A 266      32.621  25.105  15.697  1.00 15.65           N  
ATOM   1859  CA  LEU A 266      33.670  26.060  15.333  1.00 17.18           C  
ATOM   1860  C   LEU A 266      33.192  27.502  15.182  1.00 17.65           C  
ATOM   1861  O   LEU A 266      34.006  28.418  15.037  1.00 15.95           O  
ATOM   1862  CB  LEU A 266      34.357  25.613  14.042  1.00 15.85           C  
ATOM   1863  CG  LEU A 266      35.202  24.338  14.136  1.00 15.74           C  
ATOM   1864  CD1 LEU A 266      35.632  23.934  12.741  1.00 17.98           C  
ATOM   1865  CD2 LEU A 266      36.415  24.565  15.032  1.00 15.34           C  
ATOM   1866  N   GLU A 267      31.877  27.702  15.214  1.00 17.41           N  
ATOM   1867  CA  GLU A 267      31.311  29.041  15.101  1.00 19.65           C  
ATOM   1868  C   GLU A 267      30.445  29.366  16.317  1.00 18.22           C  
ATOM   1869  O   GLU A 267      29.660  30.318  16.294  1.00 20.41           O  
ATOM   1870  CB  GLU A 267      30.460  29.158  13.830  1.00 22.80           C  
ATOM   1871  CG  GLU A 267      31.163  28.684  12.570  1.00 27.54           C  
ATOM   1872  CD  GLU A 267      30.365  28.977  11.309  1.00 31.19           C  
ATOM   1873  OE1 GLU A 267      29.148  28.692  11.282  1.00 32.45           O  
ATOM   1874  OE2 GLU A 267      30.961  29.488  10.342  1.00 32.93           O  
ATOM   1875  N   GLY A 268      30.588  28.581  17.381  1.00 14.98           N  
ATOM   1876  CA  GLY A 268      29.785  28.818  18.567  1.00 12.99           C  
ATOM   1877  C   GLY A 268      30.562  28.885  19.867  1.00 13.29           C  
ATOM   1878  O   GLY A 268      31.793  28.909  19.858  1.00 13.77           O  
ATOM   1879  N   PRO A 269      29.864  28.918  21.014  1.00 14.38           N  
ATOM   1880  CA  PRO A 269      30.539  28.982  22.311  1.00 15.04           C  
ATOM   1881  C   PRO A 269      31.217  27.660  22.676  1.00 15.92           C  
ATOM   1882  O   PRO A 269      30.914  26.614  22.100  1.00 14.68           O  
ATOM   1883  CB  PRO A 269      29.411  29.353  23.263  1.00 15.56           C  
ATOM   1884  CG  PRO A 269      28.232  28.651  22.661  1.00 16.94           C  
ATOM   1885  CD  PRO A 269      28.397  28.934  21.180  1.00 14.36           C  
ATOM   1886  N   ILE A 270      32.131  27.724  23.639  1.00 14.52           N  
ATOM   1887  CA  ILE A 270      32.885  26.560  24.090  1.00 13.49           C  
ATOM   1888  C   ILE A 270      32.275  25.957  25.351  1.00 13.55           C  
ATOM   1889  O   ILE A 270      31.946  26.681  26.288  1.00  9.28           O  
ATOM   1890  CB  ILE A 270      34.345  26.958  24.416  1.00 14.98           C  
ATOM   1891  CG1 ILE A 270      35.033  27.492  23.158  1.00 15.50           C  
ATOM   1892  CG2 ILE A 270      35.104  25.763  25.013  1.00 13.64           C  
ATOM   1893  CD1 ILE A 270      36.413  28.053  23.409  1.00 14.09           C  
ATOM   1894  N   PRO A 271      32.097  24.623  25.380  1.00 12.22           N  
ATOM   1895  CA  PRO A 271      31.528  23.966  26.562  1.00 13.66           C  
ATOM   1896  C   PRO A 271      32.387  24.325  27.777  1.00 12.95           C  
ATOM   1897  O   PRO A 271      33.606  24.133  27.772  1.00 10.63           O  
ATOM   1898  CB  PRO A 271      31.608  22.487  26.200  1.00 12.81           C  
ATOM   1899  CG  PRO A 271      31.360  22.510  24.733  1.00 13.21           C  
ATOM   1900  CD  PRO A 271      32.236  23.667  24.271  1.00 12.83           C  
ATOM   1901  N   ALA A 272      31.731  24.835  28.814  1.00 13.88           N  
ATOM   1902  CA  ALA A 272      32.386  25.304  30.033  1.00 13.20           C  
ATOM   1903  C   ALA A 272      33.197  24.326  30.876  1.00 14.39           C  
ATOM   1904  O   ALA A 272      33.897  24.752  31.798  1.00 14.70           O  
ATOM   1905  CB  ALA A 272      31.348  25.984  30.917  1.00 12.25           C  
ATOM   1906  N   HIS A 273      33.125  23.032  30.583  1.00 13.10           N  
ATOM   1907  CA  HIS A 273      33.861  22.065  31.391  1.00 15.86           C  
ATOM   1908  C   HIS A 273      35.175  21.596  30.772  1.00 15.34           C  
ATOM   1909  O   HIS A 273      35.876  20.776  31.362  1.00 13.95           O  
ATOM   1910  CB  HIS A 273      32.972  20.847  31.673  1.00 14.23           C  
ATOM   1911  CG  HIS A 273      32.622  20.057  30.448  1.00 16.26           C  
ATOM   1912  ND1 HIS A 273      32.138  20.644  29.297  1.00 16.27           N  
ATOM   1913  CD2 HIS A 273      32.663  18.725  30.202  1.00 14.69           C  
ATOM   1914  CE1 HIS A 273      31.896  19.708  28.396  1.00 16.80           C  
ATOM   1915  NE2 HIS A 273      32.205  18.534  28.920  1.00 16.57           N  
ATOM   1916  N   LEU A 274      35.519  22.136  29.605  1.00 14.97           N  
ATOM   1917  CA  LEU A 274      36.725  21.716  28.891  1.00 14.04           C  
ATOM   1918  C   LEU A 274      37.947  22.624  28.991  1.00 15.10           C  
ATOM   1919  O   LEU A 274      38.921  22.424  28.262  1.00 16.46           O  
ATOM   1920  CB  LEU A 274      36.383  21.531  27.405  1.00 12.83           C  
ATOM   1921  CG  LEU A 274      35.144  20.690  27.076  1.00 12.75           C  
ATOM   1922  CD1 LEU A 274      34.877  20.727  25.564  1.00  9.86           C  
ATOM   1923  CD2 LEU A 274      35.367  19.260  27.559  1.00 10.56           C  
ATOM   1924  N   LEU A 275      37.925  23.602  29.889  1.00 14.31           N  
ATOM   1925  CA  LEU A 275      39.047  24.527  29.972  1.00 15.42           C  
ATOM   1926  C   LEU A 275      40.080  24.275  31.070  1.00 15.84           C  
ATOM   1927  O   LEU A 275      40.937  25.124  31.313  1.00 15.82           O  
ATOM   1928  CB  LEU A 275      38.524  25.972  30.053  1.00 13.51           C  
ATOM   1929  CG  LEU A 275      37.764  26.550  28.848  1.00 14.73           C  
ATOM   1930  CD1 LEU A 275      38.592  26.362  27.577  1.00 14.30           C  
ATOM   1931  CD2 LEU A 275      36.410  25.870  28.694  1.00 15.38           C  
ATOM   1932  N   GLY A 276      39.997  23.120  31.728  1.00 16.01           N  
ATOM   1933  CA  GLY A 276      40.967  22.766  32.758  1.00 15.85           C  
ATOM   1934  C   GLY A 276      40.780  23.392  34.126  1.00 16.19           C  
ATOM   1935  O   GLY A 276      41.595  23.195  35.035  1.00 14.81           O  
ATOM   1936  N   ASN A 277      39.692  24.137  34.275  1.00 15.62           N  
ATOM   1937  CA  ASN A 277      39.381  24.815  35.522  1.00 15.37           C  
ATOM   1938  C   ASN A 277      37.869  24.734  35.769  1.00 14.00           C  
ATOM   1939  O   ASN A 277      37.072  24.858  34.842  1.00 12.08           O  
ATOM   1940  CB  ASN A 277      39.878  26.265  35.430  1.00 14.32           C  
ATOM   1941  CG  ASN A 277      39.391  27.132  36.570  1.00 15.28           C  
ATOM   1942  OD1 ASN A 277      38.277  27.654  36.530  1.00 15.45           O  
ATOM   1943  ND2 ASN A 277      40.226  27.292  37.598  1.00 13.64           N  
ATOM   1944  N   MET A 278      37.486  24.519  37.023  1.00 13.86           N  
ATOM   1945  CA  MET A 278      36.077  24.368  37.390  1.00 14.00           C  
ATOM   1946  C   MET A 278      35.155  25.478  36.884  1.00 14.78           C  
ATOM   1947  O   MET A 278      33.996  25.220  36.548  1.00 13.18           O  
ATOM   1948  CB  MET A 278      35.951  24.234  38.916  1.00 14.12           C  
ATOM   1949  CG  MET A 278      34.527  24.008  39.414  1.00 15.15           C  
ATOM   1950  SD  MET A 278      33.787  22.492  38.767  1.00 16.63           S  
ATOM   1951  CE  MET A 278      34.428  21.288  39.947  1.00 16.22           C  
ATOM   1952  N   TRP A 279      35.671  26.703  36.812  1.00 11.51           N  
ATOM   1953  CA  TRP A 279      34.872  27.843  36.366  1.00 14.25           C  
ATOM   1954  C   TRP A 279      35.309  28.360  35.001  1.00 13.97           C  
ATOM   1955  O   TRP A 279      34.772  29.348  34.508  1.00 12.98           O  
ATOM   1956  CB  TRP A 279      34.970  28.968  37.403  1.00 12.20           C  
ATOM   1957  CG  TRP A 279      34.625  28.480  38.772  1.00 12.52           C  
ATOM   1958  CD1 TRP A 279      33.373  28.295  39.283  1.00 11.84           C  
ATOM   1959  CD2 TRP A 279      35.538  27.959  39.745  1.00 12.82           C  
ATOM   1960  NE1 TRP A 279      33.447  27.681  40.509  1.00 12.66           N  
ATOM   1961  CE2 TRP A 279      34.764  27.461  40.817  1.00 13.24           C  
ATOM   1962  CE3 TRP A 279      36.937  27.855  39.810  1.00 13.78           C  
ATOM   1963  CZ2 TRP A 279      35.340  26.866  41.948  1.00 12.55           C  
ATOM   1964  CZ3 TRP A 279      37.513  27.260  40.934  1.00 13.31           C  
ATOM   1965  CH2 TRP A 279      36.708  26.773  41.990  1.00 12.52           C  
ATOM   1966  N   ALA A 280      36.269  27.670  34.388  1.00 14.15           N  
ATOM   1967  CA  ALA A 280      36.799  28.086  33.096  1.00 13.77           C  
ATOM   1968  C   ALA A 280      37.297  29.534  33.179  1.00 13.58           C  
ATOM   1969  O   ALA A 280      37.249  30.263  32.189  1.00 13.90           O  
ATOM   1970  CB  ALA A 280      35.719  27.964  32.021  1.00 14.05           C  
ATOM   1971  N   GLN A 281      37.761  29.952  34.358  1.00 13.19           N  
ATOM   1972  CA  GLN A 281      38.247  31.325  34.541  1.00 13.69           C  
ATOM   1973  C   GLN A 281      39.700  31.485  34.102  1.00 13.47           C  
ATOM   1974  O   GLN A 281      40.137  32.587  33.771  1.00 11.19           O  
ATOM   1975  CB  GLN A 281      38.088  31.770  36.000  1.00 12.28           C  
ATOM   1976  CG  GLN A 281      38.917  30.995  36.999  1.00 14.52           C  
ATOM   1977  CD  GLN A 281      38.542  31.318  38.433  1.00 17.57           C  
ATOM   1978  OE1 GLN A 281      37.382  31.187  38.828  1.00 15.61           O  
ATOM   1979  NE2 GLN A 281      39.522  31.739  39.220  1.00 19.96           N  
ATOM   1980  N   THR A 282      40.442  30.382  34.124  1.00 12.33           N  
ATOM   1981  CA  THR A 282      41.835  30.354  33.687  1.00 13.83           C  
ATOM   1982  C   THR A 282      41.964  29.040  32.918  1.00 16.52           C  
ATOM   1983  O   THR A 282      41.415  28.021  33.335  1.00 14.73           O  
ATOM   1984  CB  THR A 282      42.826  30.403  34.875  1.00 16.20           C  
ATOM   1985  OG1 THR A 282      42.468  29.425  35.858  1.00 16.40           O  
ATOM   1986  CG2 THR A 282      42.819  31.789  35.511  1.00 17.20           C  
ATOM   1987  N   TRP A 283      42.675  29.065  31.795  1.00 14.06           N  
ATOM   1988  CA  TRP A 283      42.788  27.881  30.948  1.00 15.86           C  
ATOM   1989  C   TRP A 283      44.171  27.255  30.816  1.00 17.18           C  
ATOM   1990  O   TRP A 283      44.363  26.402  29.950  1.00 16.26           O  
ATOM   1991  CB  TRP A 283      42.318  28.216  29.529  1.00 15.32           C  
ATOM   1992  CG  TRP A 283      40.991  28.934  29.408  1.00 13.99           C  
ATOM   1993  CD1 TRP A 283      40.032  29.079  30.372  1.00 14.30           C  
ATOM   1994  CD2 TRP A 283      40.457  29.529  28.219  1.00 13.70           C  
ATOM   1995  NE1 TRP A 283      38.929  29.725  29.854  1.00 13.72           N  
ATOM   1996  CE2 TRP A 283      39.164  30.012  28.534  1.00 14.95           C  
ATOM   1997  CE3 TRP A 283      40.943  29.698  26.915  1.00 12.93           C  
ATOM   1998  CZ2 TRP A 283      38.355  30.650  27.592  1.00 13.70           C  
ATOM   1999  CZ3 TRP A 283      40.137  30.332  25.979  1.00 16.03           C  
ATOM   2000  CH2 TRP A 283      38.853  30.800  26.325  1.00 16.16           C  
ATOM   2001  N   SER A 284      45.125  27.655  31.648  1.00 16.81           N  
ATOM   2002  CA  SER A 284      46.482  27.131  31.514  1.00 18.73           C  
ATOM   2003  C   SER A 284      46.628  25.618  31.658  1.00 17.43           C  
ATOM   2004  O   SER A 284      47.599  25.043  31.165  1.00 16.20           O  
ATOM   2005  CB  SER A 284      47.429  27.840  32.493  1.00 19.48           C  
ATOM   2006  OG  SER A 284      47.078  27.573  33.834  1.00 23.23           O  
ATOM   2007  N   ASN A 285      45.669  24.967  32.309  1.00 16.52           N  
ATOM   2008  CA  ASN A 285      45.758  23.526  32.487  1.00 16.72           C  
ATOM   2009  C   ASN A 285      45.540  22.700  31.219  1.00 17.50           C  
ATOM   2010  O   ASN A 285      45.834  21.508  31.210  1.00 17.87           O  
ATOM   2011  CB  ASN A 285      44.827  23.068  33.617  1.00 16.47           C  
ATOM   2012  CG  ASN A 285      45.342  23.494  34.991  1.00 18.32           C  
ATOM   2013  OD1 ASN A 285      46.504  23.262  35.323  1.00 19.09           O  
ATOM   2014  ND2 ASN A 285      44.484  24.116  35.788  1.00 15.86           N  
ATOM   2015  N   ILE A 286      45.028  23.311  30.150  1.00 17.39           N  
ATOM   2016  CA  ILE A 286      44.869  22.568  28.901  1.00 17.13           C  
ATOM   2017  C   ILE A 286      45.947  23.014  27.915  1.00 18.07           C  
ATOM   2018  O   ILE A 286      45.793  22.892  26.697  1.00 16.69           O  
ATOM   2019  CB  ILE A 286      43.479  22.759  28.246  1.00 16.82           C  
ATOM   2020  CG1 ILE A 286      43.242  24.230  27.902  1.00 17.65           C  
ATOM   2021  CG2 ILE A 286      42.394  22.220  29.170  1.00 16.53           C  
ATOM   2022  CD1 ILE A 286      42.036  24.444  27.019  1.00 18.86           C  
ATOM   2023  N   TYR A 287      47.047  23.536  28.454  1.00 18.93           N  
ATOM   2024  CA  TYR A 287      48.155  23.983  27.618  1.00 20.39           C  
ATOM   2025  C   TYR A 287      48.609  22.861  26.682  1.00 20.54           C  
ATOM   2026  O   TYR A 287      48.933  23.108  25.525  1.00 19.56           O  
ATOM   2027  CB  TYR A 287      49.337  24.421  28.479  1.00 21.07           C  
ATOM   2028  CG  TYR A 287      50.567  24.757  27.667  1.00 23.88           C  
ATOM   2029  CD1 TYR A 287      50.635  25.931  26.917  1.00 22.79           C  
ATOM   2030  CD2 TYR A 287      51.652  23.879  27.618  1.00 25.81           C  
ATOM   2031  CE1 TYR A 287      51.749  26.225  26.138  1.00 25.90           C  
ATOM   2032  CE2 TYR A 287      52.774  24.163  26.841  1.00 26.76           C  
ATOM   2033  CZ  TYR A 287      52.815  25.335  26.105  1.00 27.14           C  
ATOM   2034  OH  TYR A 287      53.919  25.616  25.338  1.00 27.90           O  
ATOM   2035  N   ASP A 288      48.624  21.634  27.194  1.00 21.68           N  
ATOM   2036  CA  ASP A 288      49.041  20.468  26.415  1.00 24.93           C  
ATOM   2037  C   ASP A 288      48.214  20.275  25.144  1.00 24.42           C  
ATOM   2038  O   ASP A 288      48.721  19.790  24.133  1.00 24.30           O  
ATOM   2039  CB  ASP A 288      48.942  19.205  27.273  1.00 27.75           C  
ATOM   2040  CG  ASP A 288      47.532  18.947  27.770  1.00 33.89           C  
ATOM   2041  OD1 ASP A 288      46.943  19.866  28.377  1.00 37.33           O  
ATOM   2042  OD2 ASP A 288      47.009  17.829  27.560  1.00 36.71           O  
ATOM   2043  N   LEU A 289      46.940  20.648  25.200  1.00 22.05           N  
ATOM   2044  CA  LEU A 289      46.057  20.502  24.048  1.00 21.65           C  
ATOM   2045  C   LEU A 289      46.190  21.626  23.023  1.00 20.30           C  
ATOM   2046  O   LEU A 289      45.750  21.476  21.884  1.00 20.89           O  
ATOM   2047  CB  LEU A 289      44.594  20.431  24.503  1.00 21.37           C  
ATOM   2048  CG  LEU A 289      44.138  19.298  25.429  1.00 20.50           C  
ATOM   2049  CD1 LEU A 289      42.647  19.458  25.712  1.00 20.57           C  
ATOM   2050  CD2 LEU A 289      44.414  17.946  24.780  1.00 20.05           C  
ATOM   2051  N   VAL A 290      46.803  22.743  23.411  1.00 18.20           N  
ATOM   2052  CA  VAL A 290      46.911  23.878  22.497  1.00 17.14           C  
ATOM   2053  C   VAL A 290      48.319  24.420  22.267  1.00 18.07           C  
ATOM   2054  O   VAL A 290      48.477  25.496  21.697  1.00 19.68           O  
ATOM   2055  CB  VAL A 290      46.014  25.051  22.986  1.00 15.95           C  
ATOM   2056  CG1 VAL A 290      44.637  24.529  23.358  1.00 16.89           C  
ATOM   2057  CG2 VAL A 290      46.648  25.737  24.182  1.00 13.25           C  
ATOM   2058  N   VAL A 291      49.342  23.689  22.699  1.00 20.47           N  
ATOM   2059  CA  VAL A 291      50.715  24.154  22.516  1.00 23.25           C  
ATOM   2060  C   VAL A 291      50.975  24.620  21.077  1.00 22.80           C  
ATOM   2061  O   VAL A 291      50.758  23.875  20.123  1.00 23.34           O  
ATOM   2062  CB  VAL A 291      51.735  23.050  22.893  1.00 25.43           C  
ATOM   2063  CG1 VAL A 291      51.487  21.801  22.069  1.00 27.69           C  
ATOM   2064  CG2 VAL A 291      53.156  23.561  22.680  1.00 27.11           C  
ATOM   2065  N   PRO A 292      51.432  25.874  20.904  1.00 23.14           N  
ATOM   2066  CA  PRO A 292      51.712  26.414  19.566  1.00 24.47           C  
ATOM   2067  C   PRO A 292      52.790  25.620  18.821  1.00 26.42           C  
ATOM   2068  O   PRO A 292      52.615  25.255  17.658  1.00 26.23           O  
ATOM   2069  CB  PRO A 292      52.152  27.848  19.855  1.00 23.04           C  
ATOM   2070  CG  PRO A 292      51.422  28.181  21.134  1.00 22.71           C  
ATOM   2071  CD  PRO A 292      51.589  26.917  21.934  1.00 21.86           C  
ATOM   2072  N   PHE A 293      53.905  25.359  19.494  1.00 27.57           N  
ATOM   2073  CA  PHE A 293      54.996  24.606  18.885  1.00 28.92           C  
ATOM   2074  C   PHE A 293      55.339  23.400  19.738  1.00 29.62           C  
ATOM   2075  O   PHE A 293      56.221  23.460  20.596  1.00 27.80           O  
ATOM   2076  CB  PHE A 293      56.232  25.494  18.707  1.00 29.24           C  
ATOM   2077  CG  PHE A 293      56.003  26.667  17.801  1.00 28.40           C  
ATOM   2078  CD1 PHE A 293      55.591  27.890  18.314  1.00 28.05           C  
ATOM   2079  CD2 PHE A 293      56.159  26.538  16.426  1.00 30.34           C  
ATOM   2080  CE1 PHE A 293      55.333  28.964  17.473  1.00 28.58           C  
ATOM   2081  CE2 PHE A 293      55.903  27.605  15.575  1.00 28.99           C  
ATOM   2082  CZ  PHE A 293      55.490  28.823  16.099  1.00 29.77           C  
ATOM   2083  N   PRO A 294      54.633  22.280  19.514  1.00 31.43           N  
ATOM   2084  CA  PRO A 294      54.855  21.042  20.263  1.00 34.46           C  
ATOM   2085  C   PRO A 294      56.257  20.463  20.083  1.00 36.18           C  
ATOM   2086  O   PRO A 294      56.677  19.593  20.849  1.00 37.18           O  
ATOM   2087  CB  PRO A 294      53.756  20.118  19.737  1.00 33.87           C  
ATOM   2088  CG  PRO A 294      53.560  20.595  18.336  1.00 33.40           C  
ATOM   2089  CD  PRO A 294      53.589  22.095  18.491  1.00 32.36           C  
ATOM   2090  N   SER A 295      56.980  20.947  19.077  1.00 37.49           N  
ATOM   2091  CA  SER A 295      58.337  20.473  18.832  1.00 41.11           C  
ATOM   2092  C   SER A 295      59.259  20.936  19.949  1.00 41.74           C  
ATOM   2093  O   SER A 295      60.210  20.246  20.300  1.00 42.06           O  
ATOM   2094  CB  SER A 295      58.858  20.989  17.490  1.00 42.68           C  
ATOM   2095  OG  SER A 295      58.218  20.326  16.416  1.00 46.06           O  
ATOM   2096  N   ALA A 296      58.974  22.113  20.498  1.00 42.81           N  
ATOM   2097  CA  ALA A 296      59.767  22.663  21.591  1.00 44.30           C  
ATOM   2098  C   ALA A 296      59.138  22.200  22.903  1.00 45.75           C  
ATOM   2099  O   ALA A 296      58.246  22.857  23.440  1.00 45.98           O  
ATOM   2100  CB  ALA A 296      59.778  24.183  21.516  1.00 44.00           C  
ATOM   2101  N   PRO A 297      59.601  21.059  23.439  1.00 46.83           N  
ATOM   2102  CA  PRO A 297      59.051  20.539  24.692  1.00 48.00           C  
ATOM   2103  C   PRO A 297      59.297  21.448  25.890  1.00 48.18           C  
ATOM   2104  O   PRO A 297      60.282  22.187  25.940  1.00 46.83           O  
ATOM   2105  CB  PRO A 297      59.746  19.189  24.834  1.00 48.21           C  
ATOM   2106  CG  PRO A 297      61.100  19.469  24.262  1.00 48.04           C  
ATOM   2107  CD  PRO A 297      60.768  20.265  23.013  1.00 47.01           C  
ATOM   2108  N   SER A 298      58.381  21.388  26.849  1.00 49.04           N  
ATOM   2109  CA  SER A 298      58.484  22.185  28.063  1.00 50.15           C  
ATOM   2110  C   SER A 298      58.521  21.222  29.240  1.00 49.64           C  
ATOM   2111  O   SER A 298      57.741  20.270  29.293  1.00 49.91           O  
ATOM   2112  CB  SER A 298      57.284  23.123  28.183  1.00 50.22           C  
ATOM   2113  N   MET A 299      59.432  21.462  30.177  1.00 49.53           N  
ATOM   2114  CA  MET A 299      59.547  20.599  31.340  1.00 49.53           C  
ATOM   2115  C   MET A 299      58.262  20.525  32.144  1.00 48.79           C  
ATOM   2116  O   MET A 299      57.481  21.475  32.183  1.00 49.29           O  
ATOM   2117  CB  MET A 299      60.673  21.070  32.257  1.00 51.15           C  
ATOM   2118  CG  MET A 299      62.029  20.527  31.884  1.00 53.03           C  
ATOM   2119  SD  MET A 299      63.171  20.647  33.253  1.00 57.37           S  
ATOM   2120  CE  MET A 299      62.679  19.231  34.226  1.00 55.84           C  
ATOM   2121  N   ASP A 300      58.048  19.381  32.781  1.00 47.29           N  
ATOM   2122  CA  ASP A 300      56.874  19.182  33.615  1.00 45.73           C  
ATOM   2123  C   ASP A 300      57.190  19.889  34.932  1.00 43.86           C  
ATOM   2124  O   ASP A 300      57.723  19.279  35.860  1.00 42.31           O  
ATOM   2125  CB  ASP A 300      56.656  17.689  33.862  1.00 47.61           C  
ATOM   2126  CG  ASP A 300      55.342  17.400  34.557  1.00 48.84           C  
ATOM   2127  OD1 ASP A 300      54.962  18.178  35.459  1.00 49.28           O  
ATOM   2128  OD2 ASP A 300      54.698  16.388  34.211  1.00 49.53           O  
ATOM   2129  N   THR A 301      56.872  21.178  34.999  1.00 41.74           N  
ATOM   2130  CA  THR A 301      57.140  21.978  36.191  1.00 40.58           C  
ATOM   2131  C   THR A 301      56.669  21.307  37.476  1.00 39.17           C  
ATOM   2132  O   THR A 301      57.411  21.245  38.457  1.00 37.70           O  
ATOM   2133  CB  THR A 301      56.484  23.371  36.090  1.00 41.27           C  
ATOM   2134  OG1 THR A 301      56.908  24.016  34.881  1.00 42.14           O  
ATOM   2135  CG2 THR A 301      56.896  24.236  37.275  1.00 42.66           C  
ATOM   2136  N   THR A 302      55.437  20.807  37.472  1.00 37.74           N  
ATOM   2137  CA  THR A 302      54.890  20.144  38.648  1.00 36.86           C  
ATOM   2138  C   THR A 302      55.722  18.914  38.981  1.00 36.88           C  
ATOM   2139  O   THR A 302      56.088  18.692  40.137  1.00 36.19           O  
ATOM   2140  CB  THR A 302      53.427  19.719  38.418  1.00 37.40           C  
ATOM   2141  OG1 THR A 302      52.628  20.882  38.169  1.00 36.62           O  
ATOM   2142  CG2 THR A 302      52.886  18.984  39.635  1.00 37.24           C  
ATOM   2143  N   GLU A 303      56.023  18.116  37.960  1.00 36.39           N  
ATOM   2144  CA  GLU A 303      56.826  16.917  38.153  1.00 35.82           C  
ATOM   2145  C   GLU A 303      58.176  17.327  38.725  1.00 35.55           C  
ATOM   2146  O   GLU A 303      58.707  16.666  39.618  1.00 36.24           O  
ATOM   2147  CB  GLU A 303      57.017  16.187  36.828  1.00 36.09           C  
ATOM   2148  N   ALA A 304      58.723  18.424  38.209  1.00 34.21           N  
ATOM   2149  CA  ALA A 304      60.009  18.923  38.675  1.00 33.61           C  
ATOM   2150  C   ALA A 304      59.901  19.304  40.146  1.00 33.27           C  
ATOM   2151  O   ALA A 304      60.704  18.866  40.965  1.00 31.41           O  
ATOM   2152  CB  ALA A 304      60.436  20.128  37.846  1.00 33.15           C  
ATOM   2153  N   MET A 305      58.894  20.107  40.482  1.00 34.57           N  
ATOM   2154  CA  MET A 305      58.688  20.531  41.866  1.00 34.78           C  
ATOM   2155  C   MET A 305      58.578  19.323  42.795  1.00 35.93           C  
ATOM   2156  O   MET A 305      59.274  19.241  43.810  1.00 35.89           O  
ATOM   2157  CB  MET A 305      57.427  21.394  41.975  1.00 32.50           C  
ATOM   2158  CG  MET A 305      57.541  22.735  41.264  1.00 29.70           C  
ATOM   2159  SD  MET A 305      56.074  23.759  41.452  1.00 28.38           S  
ATOM   2160  CE  MET A 305      56.194  24.182  43.188  1.00 22.94           C  
ATOM   2161  N   LEU A 306      57.706  18.384  42.440  1.00 37.76           N  
ATOM   2162  CA  LEU A 306      57.524  17.178  43.239  1.00 40.14           C  
ATOM   2163  C   LEU A 306      58.817  16.365  43.241  1.00 41.26           C  
ATOM   2164  O   LEU A 306      59.253  15.871  44.283  1.00 41.87           O  
ATOM   2165  CB  LEU A 306      56.380  16.334  42.666  1.00 40.76           C  
ATOM   2166  CG  LEU A 306      54.971  16.932  42.725  1.00 41.59           C  
ATOM   2167  CD1 LEU A 306      54.024  16.102  41.871  1.00 41.83           C  
ATOM   2168  CD2 LEU A 306      54.491  16.982  44.171  1.00 41.58           C  
ATOM   2169  N   LYS A 307      59.430  16.242  42.067  1.00 41.93           N  
ATOM   2170  CA  LYS A 307      60.671  15.490  41.913  1.00 42.20           C  
ATOM   2171  C   LYS A 307      61.736  15.922  42.909  1.00 42.52           C  
ATOM   2172  O   LYS A 307      62.386  15.081  43.530  1.00 42.44           O  
ATOM   2173  CB  LYS A 307      61.200  15.641  40.495  1.00 43.26           C  
ATOM   2174  N   GLN A 308      61.926  17.230  43.062  1.00 42.25           N  
ATOM   2175  CA  GLN A 308      62.928  17.713  44.001  1.00 41.65           C  
ATOM   2176  C   GLN A 308      62.357  18.113  45.350  1.00 40.44           C  
ATOM   2177  O   GLN A 308      62.847  19.031  46.004  1.00 41.27           O  
ATOM   2178  CB  GLN A 308      63.734  18.859  43.394  1.00 42.74           C  
ATOM   2179  CG  GLN A 308      63.026  19.643  42.327  1.00 44.14           C  
ATOM   2180  CD  GLN A 308      63.993  20.157  41.285  1.00 45.56           C  
ATOM   2181  OE1 GLN A 308      64.984  20.807  41.613  1.00 47.00           O  
ATOM   2182  NE2 GLN A 308      63.715  19.862  40.019  1.00 45.62           N  
ATOM   2183  N   GLY A 309      61.312  17.399  45.752  1.00 39.31           N  
ATOM   2184  CA  GLY A 309      60.678  17.619  47.038  1.00 38.16           C  
ATOM   2185  C   GLY A 309      60.257  19.015  47.451  1.00 35.80           C  
ATOM   2186  O   GLY A 309      60.453  19.396  48.603  1.00 35.38           O  
ATOM   2187  N   TRP A 310      59.690  19.788  46.533  1.00 34.88           N  
ATOM   2188  CA  TRP A 310      59.229  21.119  46.900  1.00 33.70           C  
ATOM   2189  C   TRP A 310      58.035  20.916  47.822  1.00 32.71           C  
ATOM   2190  O   TRP A 310      57.268  19.968  47.650  1.00 32.15           O  
ATOM   2191  CB  TRP A 310      58.805  21.916  45.663  1.00 32.35           C  
ATOM   2192  CG  TRP A 310      59.926  22.667  45.025  1.00 32.45           C  
ATOM   2193  CD1 TRP A 310      61.089  22.146  44.544  1.00 33.26           C  
ATOM   2194  CD2 TRP A 310      59.992  24.080  44.792  1.00 33.12           C  
ATOM   2195  NE1 TRP A 310      61.877  23.143  44.024  1.00 33.74           N  
ATOM   2196  CE2 TRP A 310      61.228  24.341  44.163  1.00 33.53           C  
ATOM   2197  CE3 TRP A 310      59.125  25.151  45.053  1.00 33.17           C  
ATOM   2198  CZ2 TRP A 310      61.624  25.632  43.788  1.00 33.86           C  
ATOM   2199  CZ3 TRP A 310      59.517  26.435  44.681  1.00 33.83           C  
ATOM   2200  CH2 TRP A 310      60.758  26.663  44.054  1.00 33.79           C  
ATOM   2201  N   THR A 311      57.892  21.790  48.812  1.00 31.61           N  
ATOM   2202  CA  THR A 311      56.782  21.697  49.754  1.00 30.86           C  
ATOM   2203  C   THR A 311      56.072  23.042  49.825  1.00 29.61           C  
ATOM   2204  O   THR A 311      56.577  24.044  49.324  1.00 28.37           O  
ATOM   2205  CB  THR A 311      57.271  21.368  51.176  1.00 31.36           C  
ATOM   2206  OG1 THR A 311      58.015  22.481  51.687  1.00 30.07           O  
ATOM   2207  CG2 THR A 311      58.158  20.128  51.170  1.00 32.63           C  
ATOM   2208  N   PRO A 312      54.882  23.078  50.442  1.00 29.45           N  
ATOM   2209  CA  PRO A 312      54.160  24.347  50.552  1.00 28.24           C  
ATOM   2210  C   PRO A 312      55.036  25.393  51.247  1.00 28.41           C  
ATOM   2211  O   PRO A 312      55.105  26.543  50.816  1.00 28.24           O  
ATOM   2212  CB  PRO A 312      52.937  23.969  51.378  1.00 27.42           C  
ATOM   2213  CG  PRO A 312      52.646  22.579  50.887  1.00 27.57           C  
ATOM   2214  CD  PRO A 312      54.024  21.946  50.843  1.00 27.29           C  
ATOM   2215  N   ARG A 313      55.721  24.982  52.311  1.00 29.01           N  
ATOM   2216  CA  ARG A 313      56.588  25.896  53.052  1.00 30.23           C  
ATOM   2217  C   ARG A 313      57.689  26.436  52.140  1.00 29.35           C  
ATOM   2218  O   ARG A 313      58.016  27.620  52.183  1.00 28.16           O  
ATOM   2219  CB  ARG A 313      57.207  25.183  54.260  1.00 32.72           C  
ATOM   2220  CG  ARG A 313      57.690  26.117  55.376  1.00 38.15           C  
ATOM   2221  CD  ARG A 313      58.192  25.317  56.580  1.00 41.91           C  
ATOM   2222  NE  ARG A 313      58.217  26.096  57.821  1.00 46.21           N  
ATOM   2223  CZ  ARG A 313      59.095  27.056  58.100  1.00 46.40           C  
ATOM   2224  NH1 ARG A 313      59.026  27.700  59.258  1.00 46.37           N  
ATOM   2225  NH2 ARG A 313      60.046  27.368  57.232  1.00 48.36           N  
ATOM   2226  N   ARG A 314      58.248  25.565  51.304  1.00 28.94           N  
ATOM   2227  CA  ARG A 314      59.302  25.968  50.378  1.00 28.91           C  
ATOM   2228  C   ARG A 314      58.771  27.020  49.414  1.00 26.66           C  
ATOM   2229  O   ARG A 314      59.443  28.008  49.117  1.00 25.29           O  
ATOM   2230  CB  ARG A 314      59.793  24.764  49.567  1.00 32.39           C  
ATOM   2231  CG  ARG A 314      61.304  24.601  49.543  1.00 38.26           C  
ATOM   2232  CD  ARG A 314      62.016  25.852  49.048  1.00 41.91           C  
ATOM   2233  NE  ARG A 314      62.441  25.769  47.650  1.00 47.14           N  
ATOM   2234  CZ  ARG A 314      63.250  24.830  47.163  1.00 48.30           C  
ATOM   2235  NH1 ARG A 314      63.724  23.877  47.955  1.00 50.47           N  
ATOM   2236  NH2 ARG A 314      63.609  24.858  45.888  1.00 48.82           N  
ATOM   2237  N   MET A 315      57.558  26.783  48.925  1.00 24.67           N  
ATOM   2238  CA  MET A 315      56.909  27.680  47.981  1.00 23.82           C  
ATOM   2239  C   MET A 315      56.776  29.087  48.548  1.00 22.51           C  
ATOM   2240  O   MET A 315      57.111  30.061  47.877  1.00 22.36           O  
ATOM   2241  CB  MET A 315      55.538  27.115  47.593  1.00 22.88           C  
ATOM   2242  CG  MET A 315      55.631  25.817  46.789  1.00 22.60           C  
ATOM   2243  SD  MET A 315      54.099  24.884  46.702  1.00 23.12           S  
ATOM   2244  CE  MET A 315      53.193  25.800  45.456  1.00 22.77           C  
ATOM   2245  N   PHE A 316      56.299  29.198  49.783  1.00 22.71           N  
ATOM   2246  CA  PHE A 316      56.154  30.512  50.397  1.00 23.33           C  
ATOM   2247  C   PHE A 316      57.521  31.109  50.731  1.00 24.58           C  
ATOM   2248  O   PHE A 316      57.698  32.329  50.701  1.00 23.58           O  
ATOM   2249  CB  PHE A 316      55.272  30.431  51.650  1.00 21.23           C  
ATOM   2250  CG  PHE A 316      53.810  30.232  51.344  1.00 20.37           C  
ATOM   2251  CD1 PHE A 316      53.280  28.957  51.191  1.00 20.90           C  
ATOM   2252  CD2 PHE A 316      52.974  31.328  51.156  1.00 20.68           C  
ATOM   2253  CE1 PHE A 316      51.937  28.775  50.855  1.00 22.83           C  
ATOM   2254  CE2 PHE A 316      51.633  31.158  50.820  1.00 19.46           C  
ATOM   2255  CZ  PHE A 316      51.113  29.879  50.668  1.00 20.69           C  
ATOM   2256  N   LYS A 317      58.489  30.248  51.039  1.00 25.53           N  
ATOM   2257  CA  LYS A 317      59.838  30.708  51.349  1.00 25.95           C  
ATOM   2258  C   LYS A 317      60.428  31.383  50.115  1.00 25.86           C  
ATOM   2259  O   LYS A 317      61.081  32.418  50.223  1.00 26.39           O  
ATOM   2260  CB  LYS A 317      60.726  29.531  51.772  1.00 29.39           C  
ATOM   2261  CG  LYS A 317      60.529  29.067  53.209  1.00 32.76           C  
ATOM   2262  CD  LYS A 317      61.020  30.117  54.201  1.00 37.96           C  
ATOM   2263  CE  LYS A 317      60.995  29.590  55.633  1.00 38.41           C  
ATOM   2264  NZ  LYS A 317      61.587  30.556  56.606  1.00 38.93           N  
ATOM   2265  N   GLU A 318      60.197  30.796  48.941  1.00 25.73           N  
ATOM   2266  CA  GLU A 318      60.701  31.375  47.696  1.00 25.00           C  
ATOM   2267  C   GLU A 318      60.031  32.727  47.446  1.00 24.44           C  
ATOM   2268  O   GLU A 318      60.679  33.684  47.018  1.00 23.97           O  
ATOM   2269  CB  GLU A 318      60.425  30.445  46.510  1.00 27.57           C  
ATOM   2270  CG  GLU A 318      61.252  29.163  46.476  1.00 32.10           C  
ATOM   2271  CD  GLU A 318      62.754  29.418  46.536  1.00 34.82           C  
ATOM   2272  OE1 GLU A 318      63.207  30.487  46.066  1.00 35.04           O  
ATOM   2273  OE2 GLU A 318      63.484  28.538  47.041  1.00 36.16           O  
ATOM   2274  N   ALA A 319      58.727  32.797  47.702  1.00 23.38           N  
ATOM   2275  CA  ALA A 319      57.985  34.043  47.522  1.00 22.42           C  
ATOM   2276  C   ALA A 319      58.579  35.104  48.444  1.00 21.24           C  
ATOM   2277  O   ALA A 319      58.844  36.233  48.027  1.00 21.74           O  
ATOM   2278  CB  ALA A 319      56.511  33.829  47.857  1.00 22.54           C  
ATOM   2279  N   ASP A 320      58.787  34.732  49.702  1.00 20.72           N  
ATOM   2280  CA  ASP A 320      59.353  35.652  50.682  1.00 21.66           C  
ATOM   2281  C   ASP A 320      60.708  36.163  50.198  1.00 22.19           C  
ATOM   2282  O   ASP A 320      61.051  37.330  50.392  1.00 22.86           O  
ATOM   2283  CB  ASP A 320      59.499  34.949  52.037  1.00 23.19           C  
ATOM   2284  CG  ASP A 320      59.901  35.900  53.150  1.00 26.89           C  
ATOM   2285  OD1 ASP A 320      59.198  36.914  53.364  1.00 26.58           O  
ATOM   2286  OD2 ASP A 320      60.921  35.633  53.818  1.00 26.96           O  
ATOM   2287  N   ASP A 321      61.472  35.289  49.548  1.00 23.64           N  
ATOM   2288  CA  ASP A 321      62.787  35.667  49.041  1.00 23.82           C  
ATOM   2289  C   ASP A 321      62.680  36.688  47.916  1.00 23.50           C  
ATOM   2290  O   ASP A 321      63.486  37.612  47.836  1.00 22.72           O  
ATOM   2291  CB  ASP A 321      63.553  34.430  48.548  1.00 23.91           C  
ATOM   2292  CG  ASP A 321      64.921  34.780  47.988  1.00 26.32           C  
ATOM   2293  OD1 ASP A 321      65.096  34.724  46.753  1.00 25.02           O  
ATOM   2294  OD2 ASP A 321      65.821  35.124  48.786  1.00 28.34           O  
ATOM   2295  N   PHE A 322      61.681  36.534  47.051  1.00 23.52           N  
ATOM   2296  CA  PHE A 322      61.522  37.475  45.953  1.00 22.24           C  
ATOM   2297  C   PHE A 322      61.237  38.870  46.504  1.00 20.90           C  
ATOM   2298  O   PHE A 322      61.837  39.849  46.059  1.00 22.16           O  
ATOM   2299  CB  PHE A 322      60.397  37.045  45.001  1.00 21.06           C  
ATOM   2300  CG  PHE A 322      60.542  37.609  43.607  1.00 19.58           C  
ATOM   2301  CD1 PHE A 322      60.744  36.767  42.516  1.00 21.35           C  
ATOM   2302  CD2 PHE A 322      60.528  38.984  43.392  1.00 19.63           C  
ATOM   2303  CE1 PHE A 322      60.935  37.288  41.230  1.00 19.63           C  
ATOM   2304  CE2 PHE A 322      60.718  39.513  42.115  1.00 19.63           C  
ATOM   2305  CZ  PHE A 322      60.923  38.660  41.029  1.00 19.46           C  
ATOM   2306  N   PHE A 323      60.329  38.968  47.471  1.00 20.76           N  
ATOM   2307  CA  PHE A 323      60.019  40.269  48.057  1.00 20.13           C  
ATOM   2308  C   PHE A 323      61.258  40.935  48.671  1.00 21.10           C  
ATOM   2309  O   PHE A 323      61.517  42.120  48.427  1.00 19.45           O  
ATOM   2310  CB  PHE A 323      58.915  40.143  49.115  1.00 20.30           C  
ATOM   2311  CG  PHE A 323      57.526  40.045  48.535  1.00 18.25           C  
ATOM   2312  CD1 PHE A 323      56.932  38.805  48.306  1.00 17.88           C  
ATOM   2313  CD2 PHE A 323      56.826  41.200  48.187  1.00 19.40           C  
ATOM   2314  CE1 PHE A 323      55.662  38.713  47.738  1.00 17.04           C  
ATOM   2315  CE2 PHE A 323      55.548  41.123  47.612  1.00 18.88           C  
ATOM   2316  CZ  PHE A 323      54.968  39.875  47.388  1.00 19.24           C  
ATOM   2317  N   THR A 324      62.028  40.184  49.456  1.00 22.06           N  
ATOM   2318  CA  THR A 324      63.224  40.748  50.081  1.00 24.14           C  
ATOM   2319  C   THR A 324      64.289  41.118  49.055  1.00 23.51           C  
ATOM   2320  O   THR A 324      65.042  42.070  49.257  1.00 25.42           O  
ATOM   2321  CB  THR A 324      63.849  39.787  51.126  1.00 24.56           C  
ATOM   2322  OG1 THR A 324      64.083  38.505  50.533  1.00 26.60           O  
ATOM   2323  CG2 THR A 324      62.926  39.633  52.326  1.00 25.22           C  
ATOM   2324  N   SER A 325      64.342  40.386  47.948  1.00 23.09           N  
ATOM   2325  CA  SER A 325      65.332  40.676  46.913  1.00 22.30           C  
ATOM   2326  C   SER A 325      65.088  42.068  46.345  1.00 22.33           C  
ATOM   2327  O   SER A 325      66.005  42.707  45.824  1.00 22.15           O  
ATOM   2328  CB  SER A 325      65.256  39.642  45.784  1.00 23.31           C  
ATOM   2329  OG  SER A 325      64.163  39.901  44.915  1.00 25.00           O  
ATOM   2330  N   LEU A 326      63.846  42.535  46.452  1.00 20.54           N  
ATOM   2331  CA  LEU A 326      63.477  43.855  45.951  1.00 21.18           C  
ATOM   2332  C   LEU A 326      63.687  44.929  47.015  1.00 21.10           C  
ATOM   2333  O   LEU A 326      63.448  46.113  46.769  1.00 21.69           O  
ATOM   2334  CB  LEU A 326      62.007  43.874  45.515  1.00 20.21           C  
ATOM   2335  CG  LEU A 326      61.567  42.939  44.386  1.00 22.18           C  
ATOM   2336  CD1 LEU A 326      60.089  43.169  44.092  1.00 20.93           C  
ATOM   2337  CD2 LEU A 326      62.391  43.197  43.140  1.00 19.15           C  
ATOM   2338  N   GLY A 327      64.133  44.513  48.193  1.00 20.78           N  
ATOM   2339  CA  GLY A 327      64.340  45.465  49.269  1.00 22.52           C  
ATOM   2340  C   GLY A 327      63.086  45.581  50.120  1.00 23.30           C  
ATOM   2341  O   GLY A 327      63.053  46.339  51.091  1.00 23.76           O  
ATOM   2342  N   LEU A 328      62.051  44.826  49.754  1.00 20.72           N  
ATOM   2343  CA  LEU A 328      60.792  44.844  50.487  1.00 21.07           C  
ATOM   2344  C   LEU A 328      60.909  44.062  51.797  1.00 21.60           C  
ATOM   2345  O   LEU A 328      61.932  43.424  52.058  1.00 21.13           O  
ATOM   2346  CB  LEU A 328      59.667  44.293  49.604  1.00 17.66           C  
ATOM   2347  CG  LEU A 328      59.417  45.174  48.371  1.00 19.03           C  
ATOM   2348  CD1 LEU A 328      58.362  44.551  47.459  1.00 16.52           C  
ATOM   2349  CD2 LEU A 328      58.977  46.563  48.829  1.00 16.74           C  
ATOM   2350  N   LEU A 329      59.863  44.112  52.616  1.00 21.11           N  
ATOM   2351  CA  LEU A 329      59.869  43.451  53.921  1.00 22.96           C  
ATOM   2352  C   LEU A 329      59.654  41.942  53.937  1.00 23.76           C  
ATOM   2353  O   LEU A 329      58.870  41.401  53.163  1.00 24.22           O  
ATOM   2354  CB  LEU A 329      58.815  44.093  54.830  1.00 23.88           C  
ATOM   2355  CG  LEU A 329      58.982  45.575  55.174  1.00 27.26           C  
ATOM   2356  CD1 LEU A 329      57.692  46.100  55.788  1.00 27.98           C  
ATOM   2357  CD2 LEU A 329      60.162  45.756  56.131  1.00 25.65           C  
ATOM   2358  N   PRO A 330      60.355  41.241  54.840  1.00 25.33           N  
ATOM   2359  CA  PRO A 330      60.217  39.791  54.953  1.00 25.45           C  
ATOM   2360  C   PRO A 330      59.071  39.538  55.926  1.00 25.74           C  
ATOM   2361  O   PRO A 330      58.773  40.394  56.759  1.00 26.40           O  
ATOM   2362  CB  PRO A 330      61.562  39.373  55.529  1.00 27.39           C  
ATOM   2363  CG  PRO A 330      61.851  40.492  56.480  1.00 27.59           C  
ATOM   2364  CD  PRO A 330      61.465  41.730  55.683  1.00 26.75           C  
ATOM   2365  N   VAL A 331      58.412  38.390  55.827  1.00 25.30           N  
ATOM   2366  CA  VAL A 331      57.323  38.115  56.757  1.00 25.65           C  
ATOM   2367  C   VAL A 331      57.926  37.820  58.127  1.00 27.19           C  
ATOM   2368  O   VAL A 331      59.013  37.247  58.221  1.00 27.05           O  
ATOM   2369  CB  VAL A 331      56.462  36.916  56.303  1.00 24.53           C  
ATOM   2370  CG1 VAL A 331      55.770  37.249  54.980  1.00 23.68           C  
ATOM   2371  CG2 VAL A 331      57.327  35.674  56.167  1.00 23.66           C  
ATOM   2372  N   PRO A 332      57.235  38.226  59.207  1.00 26.80           N  
ATOM   2373  CA  PRO A 332      57.726  37.995  60.570  1.00 27.57           C  
ATOM   2374  C   PRO A 332      57.826  36.513  60.911  1.00 27.67           C  
ATOM   2375  O   PRO A 332      57.114  35.684  60.340  1.00 27.28           O  
ATOM   2376  CB  PRO A 332      56.685  38.706  61.441  1.00 26.11           C  
ATOM   2377  CG  PRO A 332      56.169  39.793  60.545  1.00 27.52           C  
ATOM   2378  CD  PRO A 332      56.022  39.063  59.229  1.00 26.99           C  
ATOM   2379  N   PRO A 333      58.722  36.160  61.847  1.00 28.91           N  
ATOM   2380  CA  PRO A 333      58.888  34.761  62.252  1.00 27.66           C  
ATOM   2381  C   PRO A 333      57.537  34.165  62.650  1.00 27.12           C  
ATOM   2382  O   PRO A 333      57.245  33.003  62.369  1.00 25.49           O  
ATOM   2383  CB  PRO A 333      59.844  34.864  63.437  1.00 30.48           C  
ATOM   2384  CG  PRO A 333      60.707  36.037  63.061  1.00 31.62           C  
ATOM   2385  CD  PRO A 333      59.688  37.033  62.542  1.00 30.07           C  
ATOM   2386  N   GLU A 334      56.715  34.985  63.297  1.00 28.48           N  
ATOM   2387  CA  GLU A 334      55.387  34.578  63.755  1.00 29.40           C  
ATOM   2388  C   GLU A 334      54.511  34.039  62.617  1.00 29.17           C  
ATOM   2389  O   GLU A 334      53.653  33.178  62.832  1.00 29.47           O  
ATOM   2390  CB  GLU A 334      54.705  35.769  64.439  1.00 31.16           C  
ATOM   2391  CG  GLU A 334      53.287  35.524  64.907  1.00 34.46           C  
ATOM   2392  CD  GLU A 334      52.757  36.659  65.770  1.00 37.66           C  
ATOM   2393  OE1 GLU A 334      53.118  37.831  65.518  1.00 38.25           O  
ATOM   2394  OE2 GLU A 334      51.967  36.381  66.696  1.00 38.79           O  
ATOM   2395  N   PHE A 335      54.736  34.549  61.409  1.00 28.47           N  
ATOM   2396  CA  PHE A 335      53.990  34.128  60.222  1.00 26.31           C  
ATOM   2397  C   PHE A 335      54.162  32.632  59.965  1.00 25.92           C  
ATOM   2398  O   PHE A 335      53.190  31.899  59.774  1.00 24.62           O  
ATOM   2399  CB  PHE A 335      54.487  34.904  58.997  1.00 25.09           C  
ATOM   2400  CG  PHE A 335      53.986  34.361  57.680  1.00 23.73           C  
ATOM   2401  CD1 PHE A 335      52.829  34.865  57.096  1.00 22.77           C  
ATOM   2402  CD2 PHE A 335      54.681  33.348  57.023  1.00 24.15           C  
ATOM   2403  CE1 PHE A 335      52.368  34.371  55.873  1.00 21.92           C  
ATOM   2404  CE2 PHE A 335      54.228  32.845  55.799  1.00 22.88           C  
ATOM   2405  CZ  PHE A 335      53.071  33.358  55.225  1.00 22.34           C  
ATOM   2406  N   TRP A 336      55.414  32.189  59.948  1.00 26.49           N  
ATOM   2407  CA  TRP A 336      55.724  30.788  59.699  1.00 28.05           C  
ATOM   2408  C   TRP A 336      55.128  29.845  60.737  1.00 28.77           C  
ATOM   2409  O   TRP A 336      54.818  28.693  60.436  1.00 29.68           O  
ATOM   2410  CB  TRP A 336      57.242  30.605  59.640  1.00 27.25           C  
ATOM   2411  CG  TRP A 336      57.869  31.421  58.559  1.00 26.72           C  
ATOM   2412  CD1 TRP A 336      58.678  32.507  58.713  1.00 26.27           C  
ATOM   2413  CD2 TRP A 336      57.708  31.235  57.148  1.00 24.28           C  
ATOM   2414  NE1 TRP A 336      59.032  33.011  57.486  1.00 24.78           N  
ATOM   2415  CE2 TRP A 336      58.450  32.249  56.508  1.00 24.53           C  
ATOM   2416  CE3 TRP A 336      57.007  30.308  56.363  1.00 25.77           C  
ATOM   2417  CZ2 TRP A 336      58.515  32.367  55.115  1.00 25.59           C  
ATOM   2418  CZ3 TRP A 336      57.070  30.423  54.975  1.00 25.39           C  
ATOM   2419  CH2 TRP A 336      57.820  31.446  54.368  1.00 26.81           C  
ATOM   2420  N   ASN A 337      54.948  30.341  61.955  1.00 29.29           N  
ATOM   2421  CA  ASN A 337      54.407  29.517  63.023  1.00 30.04           C  
ATOM   2422  C   ASN A 337      52.882  29.448  63.097  1.00 30.01           C  
ATOM   2423  O   ASN A 337      52.323  28.404  63.431  1.00 27.10           O  
ATOM   2424  CB  ASN A 337      54.955  29.999  64.369  1.00 33.90           C  
ATOM   2425  CG  ASN A 337      54.405  29.197  65.545  1.00 37.17           C  
ATOM   2426  OD1 ASN A 337      53.214  29.307  65.846  1.00 41.44           O  
ATOM   2427  ND2 ASN A 337      55.233  28.397  66.223  1.00 37.16           N  
ATOM   2428  N   LYS A 338      52.206  30.547  62.780  1.00 28.47           N  
ATOM   2429  CA  LYS A 338      50.753  30.567  62.870  1.00 29.06           C  
ATOM   2430  C   LYS A 338      49.964  30.320  61.584  1.00 28.08           C  
ATOM   2431  O   LYS A 338      48.788  29.961  61.645  1.00 29.11           O  
ATOM   2432  CB  LYS A 338      50.308  31.882  63.513  1.00 30.23           C  
ATOM   2433  CG  LYS A 338      50.848  32.067  64.931  1.00 32.99           C  
ATOM   2434  CD  LYS A 338      50.314  33.335  65.573  1.00 38.01           C  
ATOM   2435  CE  LYS A 338      50.831  33.502  66.996  1.00 40.47           C  
ATOM   2436  NZ  LYS A 338      50.244  34.711  67.648  1.00 43.23           N  
ATOM   2437  N   SER A 339      50.594  30.498  60.426  1.00 27.36           N  
ATOM   2438  CA  SER A 339      49.904  30.288  59.151  1.00 26.35           C  
ATOM   2439  C   SER A 339      49.524  28.830  58.908  1.00 27.44           C  
ATOM   2440  O   SER A 339      50.158  27.911  59.430  1.00 27.46           O  
ATOM   2441  CB  SER A 339      50.774  30.764  57.977  1.00 24.78           C  
ATOM   2442  OG  SER A 339      50.954  32.171  57.991  1.00 22.65           O  
ATOM   2443  N   MET A 340      48.475  28.628  58.117  1.00 27.03           N  
ATOM   2444  CA  MET A 340      48.029  27.288  57.749  1.00 27.37           C  
ATOM   2445  C   MET A 340      48.336  27.186  56.259  1.00 28.01           C  
ATOM   2446  O   MET A 340      47.493  27.511  55.419  1.00 27.83           O  
ATOM   2447  CB  MET A 340      46.524  27.117  57.973  1.00 25.87           C  
ATOM   2448  CG  MET A 340      46.028  25.700  57.695  1.00 23.55           C  
ATOM   2449  SD  MET A 340      44.257  25.591  57.365  1.00 24.62           S  
ATOM   2450  CE  MET A 340      44.241  25.865  55.602  1.00 23.28           C  
ATOM   2451  N   LEU A 341      49.547  26.742  55.935  1.00 28.67           N  
ATOM   2452  CA  LEU A 341      49.976  26.636  54.544  1.00 27.98           C  
ATOM   2453  C   LEU A 341      49.597  25.325  53.861  1.00 29.45           C  
ATOM   2454  O   LEU A 341      49.835  25.154  52.664  1.00 29.43           O  
ATOM   2455  CB  LEU A 341      51.488  26.849  54.463  1.00 26.09           C  
ATOM   2456  CG  LEU A 341      52.000  28.142  55.109  1.00 26.99           C  
ATOM   2457  CD1 LEU A 341      53.516  28.186  55.014  1.00 25.50           C  
ATOM   2458  CD2 LEU A 341      51.382  29.362  54.421  1.00 25.38           C  
ATOM   2459  N   GLU A 342      49.002  24.407  54.618  1.00 30.71           N  
ATOM   2460  CA  GLU A 342      48.589  23.115  54.074  1.00 33.88           C  
ATOM   2461  C   GLU A 342      47.230  22.718  54.622  1.00 33.50           C  
ATOM   2462  O   GLU A 342      46.854  23.115  55.726  1.00 32.75           O  
ATOM   2463  CB  GLU A 342      49.576  22.012  54.460  1.00 36.25           C  
ATOM   2464  CG  GLU A 342      51.022  22.277  54.127  1.00 43.43           C  
ATOM   2465  CD  GLU A 342      51.929  21.197  54.686  1.00 46.04           C  
ATOM   2466  OE1 GLU A 342      51.953  21.025  55.924  1.00 49.71           O  
ATOM   2467  OE2 GLU A 342      52.609  20.515  53.892  1.00 48.87           O  
ATOM   2468  N   LYS A 343      46.506  21.917  53.851  1.00 33.65           N  
ATOM   2469  CA  LYS A 343      45.200  21.429  54.271  1.00 35.26           C  
ATOM   2470  C   LYS A 343      45.432  20.474  55.435  1.00 36.99           C  
ATOM   2471  O   LYS A 343      46.171  19.496  55.307  1.00 37.40           O  
ATOM   2472  CB  LYS A 343      44.523  20.687  53.121  1.00 35.25           C  
ATOM   2473  CG  LYS A 343      43.155  20.120  53.456  1.00 35.45           C  
ATOM   2474  CD  LYS A 343      42.518  19.531  52.208  1.00 35.40           C  
ATOM   2475  CE  LYS A 343      41.132  18.994  52.483  1.00 36.09           C  
ATOM   2476  NZ  LYS A 343      40.514  18.496  51.224  1.00 36.76           N  
ATOM   2477  N   PRO A 344      44.813  20.747  56.591  1.00 38.18           N  
ATOM   2478  CA  PRO A 344      44.992  19.873  57.753  1.00 40.05           C  
ATOM   2479  C   PRO A 344      44.570  18.427  57.509  1.00 41.45           C  
ATOM   2480  O   PRO A 344      43.595  18.159  56.808  1.00 40.45           O  
ATOM   2481  CB  PRO A 344      44.133  20.545  58.822  1.00 39.71           C  
ATOM   2482  CG  PRO A 344      44.209  21.993  58.451  1.00 39.38           C  
ATOM   2483  CD  PRO A 344      44.031  21.941  56.951  1.00 38.24           C  
ATOM   2484  N   THR A 345      45.330  17.502  58.084  1.00 43.87           N  
ATOM   2485  CA  THR A 345      45.042  16.077  57.989  1.00 46.82           C  
ATOM   2486  C   THR A 345      44.450  15.750  59.355  1.00 48.06           C  
ATOM   2487  O   THR A 345      44.102  14.612  59.664  1.00 49.50           O  
ATOM   2488  CB  THR A 345      46.331  15.268  57.766  1.00 47.11           C  
ATOM   2489  OG1 THR A 345      47.272  15.569  58.804  1.00 48.76           O  
ATOM   2490  CG2 THR A 345      46.946  15.622  56.425  1.00 46.74           C  
ATOM   2491  N   ASP A 346      44.345  16.808  60.151  1.00 49.79           N  
ATOM   2492  CA  ASP A 346      43.821  16.801  61.510  1.00 50.68           C  
ATOM   2493  C   ASP A 346      42.439  16.162  61.607  1.00 50.48           C  
ATOM   2494  O   ASP A 346      41.919  15.965  62.705  1.00 50.57           O  
ATOM   2495  CB  ASP A 346      43.722  18.252  61.991  1.00 51.52           C  
ATOM   2496  CG  ASP A 346      44.084  18.416  63.445  1.00 53.90           C  
ATOM   2497  OD1 ASP A 346      43.505  17.705  64.293  1.00 56.14           O  
ATOM   2498  OD2 ASP A 346      44.950  19.267  63.737  1.00 54.87           O  
ATOM   2499  N   GLY A 347      41.845  15.831  60.465  1.00 50.81           N  
ATOM   2500  CA  GLY A 347      40.504  15.280  60.486  1.00 50.66           C  
ATOM   2501  C   GLY A 347      39.635  16.487  60.795  1.00 50.28           C  
ATOM   2502  O   GLY A 347      38.488  16.379  61.230  1.00 51.71           O  
ATOM   2503  N   ARG A 348      40.231  17.653  60.560  1.00 48.17           N  
ATOM   2504  CA  ARG A 348      39.613  18.954  60.788  1.00 45.10           C  
ATOM   2505  C   ARG A 348      39.013  19.464  59.477  1.00 41.98           C  
ATOM   2506  O   ARG A 348      39.522  19.167  58.398  1.00 42.26           O  
ATOM   2507  CB  ARG A 348      40.688  19.934  61.261  1.00 45.50           C  
ATOM   2508  CG  ARG A 348      40.269  20.913  62.332  1.00 44.65           C  
ATOM   2509  CD  ARG A 348      41.270  22.052  62.408  1.00 44.87           C  
ATOM   2510  NE  ARG A 348      42.651  21.577  62.397  1.00 44.55           N  
ATOM   2511  CZ  ARG A 348      43.705  22.356  62.170  1.00 44.28           C  
ATOM   2512  NH1 ARG A 348      43.540  23.651  61.933  1.00 42.73           N  
ATOM   2513  NH2 ARG A 348      44.927  21.841  62.174  1.00 44.56           N  
ATOM   2514  N   GLU A 349      37.932  20.227  59.573  1.00 38.86           N  
ATOM   2515  CA  GLU A 349      37.286  20.788  58.390  1.00 35.74           C  
ATOM   2516  C   GLU A 349      37.681  22.266  58.330  1.00 31.68           C  
ATOM   2517  O   GLU A 349      37.643  22.958  59.346  1.00 28.60           O  
ATOM   2518  CB  GLU A 349      35.767  20.654  58.508  1.00 37.72           C  
ATOM   2519  CG  GLU A 349      35.008  20.940  57.225  1.00 41.39           C  
ATOM   2520  CD  GLU A 349      34.671  19.679  56.439  1.00 44.40           C  
ATOM   2521  OE1 GLU A 349      33.991  18.792  57.003  1.00 45.17           O  
ATOM   2522  OE2 GLU A 349      35.075  19.577  55.260  1.00 43.36           O  
ATOM   2523  N   VAL A 350      38.066  22.749  57.150  1.00 29.12           N  
ATOM   2524  CA  VAL A 350      38.480  24.145  57.013  1.00 25.82           C  
ATOM   2525  C   VAL A 350      38.041  24.806  55.708  1.00 25.16           C  
ATOM   2526  O   VAL A 350      37.528  24.150  54.799  1.00 24.70           O  
ATOM   2527  CB  VAL A 350      40.022  24.281  57.096  1.00 26.30           C  
ATOM   2528  CG1 VAL A 350      40.546  23.600  58.347  1.00 26.29           C  
ATOM   2529  CG2 VAL A 350      40.669  23.673  55.855  1.00 26.07           C  
ATOM   2530  N   VAL A 351      38.238  26.120  55.637  1.00 22.13           N  
ATOM   2531  CA  VAL A 351      37.929  26.879  54.433  1.00 22.57           C  
ATOM   2532  C   VAL A 351      39.254  26.864  53.679  1.00 22.05           C  
ATOM   2533  O   VAL A 351      40.199  27.551  54.056  1.00 22.15           O  
ATOM   2534  CB  VAL A 351      37.533  28.341  54.764  1.00 23.19           C  
ATOM   2535  CG1 VAL A 351      37.289  29.122  53.479  1.00 22.36           C  
ATOM   2536  CG2 VAL A 351      36.279  28.355  55.636  1.00 21.95           C  
ATOM   2537  N   CYS A 352      39.331  26.059  52.626  1.00 22.87           N  
ATOM   2538  CA  CYS A 352      40.561  25.937  51.857  1.00 22.31           C  
ATOM   2539  C   CYS A 352      40.946  27.106  50.957  1.00 22.33           C  
ATOM   2540  O   CYS A 352      42.134  27.335  50.723  1.00 22.41           O  
ATOM   2541  CB  CYS A 352      40.521  24.664  51.018  1.00 23.58           C  
ATOM   2542  SG  CYS A 352      41.168  23.197  51.879  1.00 25.88           S  
ATOM   2543  N   HIS A 353      39.958  27.841  50.456  1.00 21.14           N  
ATOM   2544  CA  HIS A 353      40.231  28.961  49.558  1.00 19.98           C  
ATOM   2545  C   HIS A 353      41.309  29.884  50.124  1.00 19.92           C  
ATOM   2546  O   HIS A 353      41.173  30.412  51.226  1.00 19.94           O  
ATOM   2547  CB  HIS A 353      38.954  29.761  49.286  1.00 17.69           C  
ATOM   2548  CG  HIS A 353      39.075  30.695  48.123  1.00 16.80           C  
ATOM   2549  ND1 HIS A 353      38.954  30.273  46.816  1.00 17.45           N  
ATOM   2550  CD2 HIS A 353      39.392  32.009  48.067  1.00 16.85           C  
ATOM   2551  CE1 HIS A 353      39.196  31.287  46.004  1.00 17.61           C  
ATOM   2552  NE2 HIS A 353      39.466  32.352  46.737  1.00 20.78           N  
ATOM   2553  N   ALA A 354      42.376  30.080  49.355  1.00 19.69           N  
ATOM   2554  CA  ALA A 354      43.497  30.917  49.779  1.00 18.75           C  
ATOM   2555  C   ALA A 354      43.110  32.322  50.228  1.00 17.94           C  
ATOM   2556  O   ALA A 354      42.298  32.990  49.589  1.00 16.36           O  
ATOM   2557  CB  ALA A 354      44.529  31.007  48.657  1.00 16.28           C  
ATOM   2558  N   SER A 355      43.708  32.769  51.328  1.00 19.03           N  
ATOM   2559  CA  SER A 355      43.450  34.110  51.847  1.00 19.74           C  
ATOM   2560  C   SER A 355      44.576  34.584  52.767  1.00 19.49           C  
ATOM   2561  O   SER A 355      45.305  33.775  53.355  1.00 20.16           O  
ATOM   2562  CB  SER A 355      42.098  34.163  52.581  1.00 20.01           C  
ATOM   2563  OG  SER A 355      42.041  33.244  53.656  1.00 24.98           O  
ATOM   2564  N   ALA A 356      44.721  35.903  52.860  1.00 19.32           N  
ATOM   2565  CA  ALA A 356      45.744  36.541  53.682  1.00 18.05           C  
ATOM   2566  C   ALA A 356      45.048  37.292  54.804  1.00 19.41           C  
ATOM   2567  O   ALA A 356      44.006  37.922  54.594  1.00 18.50           O  
ATOM   2568  CB  ALA A 356      46.571  37.502  52.840  1.00 18.53           C  
ATOM   2569  N   TRP A 357      45.641  37.243  55.988  1.00 18.57           N  
ATOM   2570  CA  TRP A 357      45.043  37.862  57.157  1.00 20.63           C  
ATOM   2571  C   TRP A 357      45.873  38.923  57.877  1.00 21.09           C  
ATOM   2572  O   TRP A 357      47.062  38.734  58.148  1.00 20.91           O  
ATOM   2573  CB  TRP A 357      44.672  36.764  58.158  1.00 20.94           C  
ATOM   2574  CG  TRP A 357      43.693  35.759  57.626  1.00 20.63           C  
ATOM   2575  CD1 TRP A 357      43.834  34.974  56.513  1.00 21.13           C  
ATOM   2576  CD2 TRP A 357      42.423  35.424  58.195  1.00 20.38           C  
ATOM   2577  NE1 TRP A 357      42.728  34.171  56.356  1.00 19.97           N  
ATOM   2578  CE2 TRP A 357      41.847  34.427  57.374  1.00 20.45           C  
ATOM   2579  CE3 TRP A 357      41.715  35.872  59.321  1.00 20.78           C  
ATOM   2580  CZ2 TRP A 357      40.591  33.867  57.645  1.00 21.53           C  
ATOM   2581  CZ3 TRP A 357      40.464  35.315  59.590  1.00 22.62           C  
ATOM   2582  CH2 TRP A 357      39.917  34.323  58.754  1.00 22.52           C  
ATOM   2583  N   ASP A 358      45.222  40.040  58.183  1.00 20.21           N  
ATOM   2584  CA  ASP A 358      45.845  41.127  58.922  1.00 20.18           C  
ATOM   2585  C   ASP A 358      45.140  41.091  60.283  1.00 21.39           C  
ATOM   2586  O   ASP A 358      43.913  41.234  60.350  1.00 19.21           O  
ATOM   2587  CB  ASP A 358      45.577  42.472  58.241  1.00 18.75           C  
ATOM   2588  CG  ASP A 358      46.327  43.615  58.900  1.00 19.53           C  
ATOM   2589  OD1 ASP A 358      46.749  43.451  60.065  1.00 19.53           O  
ATOM   2590  OD2 ASP A 358      46.492  44.676  58.261  1.00 18.57           O  
ATOM   2591  N   PHE A 359      45.894  40.875  61.358  1.00 21.15           N  
ATOM   2592  CA  PHE A 359      45.286  40.819  62.687  1.00 23.78           C  
ATOM   2593  C   PHE A 359      45.289  42.159  63.414  1.00 24.86           C  
ATOM   2594  O   PHE A 359      45.079  42.226  64.627  1.00 26.08           O  
ATOM   2595  CB  PHE A 359      45.959  39.741  63.546  1.00 22.15           C  
ATOM   2596  CG  PHE A 359      45.567  38.341  63.165  1.00 23.26           C  
ATOM   2597  CD1 PHE A 359      46.029  37.771  61.983  1.00 21.17           C  
ATOM   2598  CD2 PHE A 359      44.707  37.604  63.974  1.00 23.14           C  
ATOM   2599  CE1 PHE A 359      45.640  36.490  61.608  1.00 22.67           C  
ATOM   2600  CE2 PHE A 359      44.310  36.321  63.610  1.00 25.19           C  
ATOM   2601  CZ  PHE A 359      44.780  35.761  62.420  1.00 24.11           C  
ATOM   2602  N   TYR A 360      45.529  43.218  62.649  1.00 26.25           N  
ATOM   2603  CA  TYR A 360      45.535  44.597  63.133  1.00 29.34           C  
ATOM   2604  C   TYR A 360      46.334  44.960  64.382  1.00 29.54           C  
ATOM   2605  O   TYR A 360      45.897  45.802  65.166  1.00 30.88           O  
ATOM   2606  CB  TYR A 360      44.097  45.083  63.329  1.00 32.35           C  
ATOM   2607  CG  TYR A 360      43.174  44.734  62.188  1.00 36.14           C  
ATOM   2608  CD1 TYR A 360      42.490  43.521  62.172  1.00 38.33           C  
ATOM   2609  CD2 TYR A 360      42.992  45.609  61.118  1.00 39.05           C  
ATOM   2610  CE1 TYR A 360      41.645  43.185  61.126  1.00 41.84           C  
ATOM   2611  CE2 TYR A 360      42.148  45.281  60.059  1.00 42.44           C  
ATOM   2612  CZ  TYR A 360      41.477  44.068  60.074  1.00 42.85           C  
ATOM   2613  OH  TYR A 360      40.630  43.737  59.042  1.00 48.25           O  
ATOM   2614  N   ASN A 361      47.492  44.342  64.583  1.00 28.09           N  
ATOM   2615  CA  ASN A 361      48.317  44.697  65.732  1.00 26.46           C  
ATOM   2616  C   ASN A 361      49.703  45.042  65.208  1.00 26.86           C  
ATOM   2617  O   ASN A 361      50.630  45.301  65.974  1.00 26.07           O  
ATOM   2618  CB  ASN A 361      48.375  43.554  66.762  1.00 25.72           C  
ATOM   2619  CG  ASN A 361      49.069  42.311  66.238  1.00 24.13           C  
ATOM   2620  OD1 ASN A 361      49.450  42.234  65.074  1.00 19.92           O  
ATOM   2621  ND2 ASN A 361      49.232  41.324  67.110  1.00 24.99           N  
ATOM   2622  N   GLY A 362      49.820  45.051  63.880  1.00 26.09           N  
ATOM   2623  CA  GLY A 362      51.075  45.371  63.225  1.00 24.15           C  
ATOM   2624  C   GLY A 362      52.155  44.325  63.404  1.00 24.36           C  
ATOM   2625  O   GLY A 362      53.313  44.560  63.061  1.00 25.32           O  
ATOM   2626  N   LYS A 363      51.784  43.159  63.916  1.00 23.94           N  
ATOM   2627  CA  LYS A 363      52.763  42.107  64.147  1.00 26.37           C  
ATOM   2628  C   LYS A 363      52.336  40.732  63.647  1.00 25.74           C  
ATOM   2629  O   LYS A 363      53.145  39.984  63.097  1.00 26.30           O  
ATOM   2630  CB  LYS A 363      53.069  42.017  65.645  1.00 29.65           C  
ATOM   2631  CG  LYS A 363      54.522  42.251  65.990  1.00 35.63           C  
ATOM   2632  CD  LYS A 363      54.954  43.660  65.631  1.00 38.94           C  
ATOM   2633  CE  LYS A 363      54.438  44.665  66.640  1.00 42.85           C  
ATOM   2634  NZ  LYS A 363      55.031  44.415  67.988  1.00 44.66           N  
ATOM   2635  N   ASP A 364      51.062  40.413  63.839  1.00 24.66           N  
ATOM   2636  CA  ASP A 364      50.514  39.117  63.461  1.00 24.69           C  
ATOM   2637  C   ASP A 364      49.830  39.102  62.086  1.00 25.11           C  
ATOM   2638  O   ASP A 364      48.725  39.631  61.919  1.00 23.47           O  
ATOM   2639  CB  ASP A 364      49.529  38.674  64.549  1.00 22.82           C  
ATOM   2640  CG  ASP A 364      49.088  37.237  64.402  1.00 24.52           C  
ATOM   2641  OD1 ASP A 364      49.389  36.602  63.368  1.00 24.94           O  
ATOM   2642  OD2 ASP A 364      48.424  36.738  65.333  1.00 27.00           O  
ATOM   2643  N   PHE A 365      50.498  38.498  61.106  1.00 24.32           N  
ATOM   2644  CA  PHE A 365      49.955  38.383  59.750  1.00 23.41           C  
ATOM   2645  C   PHE A 365      50.027  36.910  59.379  1.00 23.79           C  
ATOM   2646  O   PHE A 365      51.023  36.246  59.670  1.00 24.61           O  
ATOM   2647  CB  PHE A 365      50.783  39.188  58.743  1.00 23.60           C  
ATOM   2648  CG  PHE A 365      51.136  40.571  59.203  1.00 24.38           C  
ATOM   2649  CD1 PHE A 365      52.341  40.813  59.858  1.00 25.69           C  
ATOM   2650  CD2 PHE A 365      50.274  41.641  58.965  1.00 25.33           C  
ATOM   2651  CE1 PHE A 365      52.687  42.104  60.267  1.00 23.83           C  
ATOM   2652  CE2 PHE A 365      50.611  42.934  59.371  1.00 23.41           C  
ATOM   2653  CZ  PHE A 365      51.821  43.164  60.023  1.00 23.93           C  
ATOM   2654  N   ARG A 366      48.984  36.394  58.736  1.00 23.34           N  
ATOM   2655  CA  ARG A 366      48.973  34.984  58.371  1.00 21.97           C  
ATOM   2656  C   ARG A 366      48.312  34.679  57.035  1.00 22.32           C  
ATOM   2657  O   ARG A 366      47.522  35.468  56.507  1.00 20.61           O  
ATOM   2658  CB  ARG A 366      48.245  34.166  59.443  1.00 22.90           C  
ATOM   2659  CG  ARG A 366      48.555  34.552  60.881  1.00 23.65           C  
ATOM   2660  CD  ARG A 366      47.710  33.717  61.832  1.00 24.02           C  
ATOM   2661  NE  ARG A 366      47.685  34.268  63.183  1.00 24.58           N  
ATOM   2662  CZ  ARG A 366      46.977  33.755  64.184  1.00 25.68           C  
ATOM   2663  NH1 ARG A 366      46.235  32.672  63.988  1.00 24.67           N  
ATOM   2664  NH2 ARG A 366      46.998  34.333  65.377  1.00 25.68           N  
ATOM   2665  N   ILE A 367      48.636  33.504  56.505  1.00 22.29           N  
ATOM   2666  CA  ILE A 367      48.057  33.029  55.260  1.00 20.95           C  
ATOM   2667  C   ILE A 367      47.400  31.679  55.544  1.00 21.59           C  
ATOM   2668  O   ILE A 367      47.938  30.862  56.300  1.00 21.62           O  
ATOM   2669  CB  ILE A 367      49.137  32.891  54.154  1.00 20.55           C  
ATOM   2670  CG1 ILE A 367      49.502  34.282  53.625  1.00 18.02           C  
ATOM   2671  CG2 ILE A 367      48.629  32.009  53.016  1.00 21.09           C  
ATOM   2672  CD1 ILE A 367      50.575  34.283  52.548  1.00 17.26           C  
ATOM   2673  N   LYS A 368      46.214  31.478  54.971  1.00 20.68           N  
ATOM   2674  CA  LYS A 368      45.453  30.239  55.115  1.00 19.59           C  
ATOM   2675  C   LYS A 368      45.188  29.723  53.704  1.00 20.32           C  
ATOM   2676  O   LYS A 368      44.379  30.291  52.966  1.00 17.80           O  
ATOM   2677  CB  LYS A 368      44.115  30.495  55.818  1.00 19.25           C  
ATOM   2678  CG  LYS A 368      43.236  29.248  55.912  1.00 20.50           C  
ATOM   2679  CD  LYS A 368      41.796  29.585  56.296  1.00 20.84           C  
ATOM   2680  CE  LYS A 368      41.143  30.517  55.274  1.00 19.03           C  
ATOM   2681  NZ  LYS A 368      41.207  29.974  53.882  1.00 17.95           N  
ATOM   2682  N   GLN A 369      45.857  28.638  53.335  1.00 19.73           N  
ATOM   2683  CA  GLN A 369      45.716  28.092  51.993  1.00 19.81           C  
ATOM   2684  C   GLN A 369      46.013  26.601  51.986  1.00 20.97           C  
ATOM   2685  O   GLN A 369      47.011  26.173  52.559  1.00 19.21           O  
ATOM   2686  CB  GLN A 369      46.701  28.819  51.074  1.00 20.96           C  
ATOM   2687  CG  GLN A 369      46.652  28.439  49.606  1.00 22.65           C  
ATOM   2688  CD  GLN A 369      47.679  29.200  48.788  1.00 23.34           C  
ATOM   2689  OE1 GLN A 369      47.979  30.360  49.073  1.00 23.98           O  
ATOM   2690  NE2 GLN A 369      48.213  28.556  47.757  1.00 25.85           N  
ATOM   2691  N   CYS A 370      45.148  25.810  51.356  1.00 22.51           N  
ATOM   2692  CA  CYS A 370      45.389  24.372  51.268  1.00 24.18           C  
ATOM   2693  C   CYS A 370      46.241  24.204  50.017  1.00 24.54           C  
ATOM   2694  O   CYS A 370      45.795  23.703  48.982  1.00 24.83           O  
ATOM   2695  CB  CYS A 370      44.077  23.602  51.144  1.00 24.18           C  
ATOM   2696  SG  CYS A 370      42.962  23.853  52.560  1.00 26.68           S  
ATOM   2697  N   THR A 371      47.481  24.653  50.145  1.00 23.39           N  
ATOM   2698  CA  THR A 371      48.455  24.649  49.072  1.00 23.83           C  
ATOM   2699  C   THR A 371      48.789  23.295  48.468  1.00 23.55           C  
ATOM   2700  O   THR A 371      49.037  22.323  49.178  1.00 22.36           O  
ATOM   2701  CB  THR A 371      49.761  25.296  49.553  1.00 24.60           C  
ATOM   2702  OG1 THR A 371      49.458  26.532  50.214  1.00 24.98           O  
ATOM   2703  CG2 THR A 371      50.694  25.564  48.377  1.00 24.72           C  
ATOM   2704  N   THR A 372      48.790  23.250  47.142  1.00 24.22           N  
ATOM   2705  CA  THR A 372      49.142  22.044  46.407  1.00 25.66           C  
ATOM   2706  C   THR A 372      50.482  22.350  45.752  1.00 24.67           C  
ATOM   2707  O   THR A 372      50.747  23.494  45.377  1.00 24.35           O  
ATOM   2708  CB  THR A 372      48.096  21.716  45.323  1.00 26.94           C  
ATOM   2709  OG1 THR A 372      46.879  21.298  45.953  1.00 31.08           O  
ATOM   2710  CG2 THR A 372      48.589  20.597  44.421  1.00 30.68           C  
ATOM   2711  N   VAL A 373      51.329  21.337  45.618  1.00 25.92           N  
ATOM   2712  CA  VAL A 373      52.644  21.533  45.021  1.00 25.04           C  
ATOM   2713  C   VAL A 373      52.632  21.494  43.493  1.00 25.52           C  
ATOM   2714  O   VAL A 373      52.737  20.429  42.881  1.00 26.04           O  
ATOM   2715  CB  VAL A 373      53.648  20.485  45.549  1.00 25.96           C  
ATOM   2716  CG1 VAL A 373      55.024  20.725  44.949  1.00 24.79           C  
ATOM   2717  CG2 VAL A 373      53.716  20.557  47.068  1.00 24.67           C  
ATOM   2718  N   ASN A 374      52.491  22.671  42.893  1.00 24.32           N  
ATOM   2719  CA  ASN A 374      52.490  22.835  41.440  1.00 24.14           C  
ATOM   2720  C   ASN A 374      52.702  24.311  41.133  1.00 24.79           C  
ATOM   2721  O   ASN A 374      52.667  25.150  42.041  1.00 22.13           O  
ATOM   2722  CB  ASN A 374      51.176  22.345  40.818  1.00 24.83           C  
ATOM   2723  CG  ASN A 374      49.954  22.969  41.456  1.00 27.35           C  
ATOM   2724  OD1 ASN A 374      49.858  24.187  41.591  1.00 29.21           O  
ATOM   2725  ND2 ASN A 374      49.004  22.132  41.842  1.00 28.69           N  
ATOM   2726  N   LEU A 375      52.922  24.629  39.862  1.00 22.38           N  
ATOM   2727  CA  LEU A 375      53.167  26.005  39.459  1.00 24.32           C  
ATOM   2728  C   LEU A 375      51.978  26.931  39.691  1.00 24.77           C  
ATOM   2729  O   LEU A 375      52.152  28.082  40.082  1.00 24.88           O  
ATOM   2730  CB  LEU A 375      53.582  26.056  37.986  1.00 24.24           C  
ATOM   2731  CG  LEU A 375      53.912  27.439  37.417  1.00 26.51           C  
ATOM   2732  CD1 LEU A 375      54.969  28.127  38.280  1.00 25.09           C  
ATOM   2733  CD2 LEU A 375      54.403  27.288  35.980  1.00 27.04           C  
ATOM   2734  N   GLU A 376      50.773  26.428  39.452  1.00 24.97           N  
ATOM   2735  CA  GLU A 376      49.571  27.231  39.635  1.00 27.47           C  
ATOM   2736  C   GLU A 376      49.482  27.767  41.066  1.00 26.40           C  
ATOM   2737  O   GLU A 376      49.209  28.948  41.278  1.00 27.12           O  
ATOM   2738  CB  GLU A 376      48.334  26.392  39.285  1.00 29.90           C  
ATOM   2739  CG  GLU A 376      47.011  27.143  39.341  1.00 33.59           C  
ATOM   2740  CD  GLU A 376      45.921  26.457  38.527  1.00 36.42           C  
ATOM   2741  OE1 GLU A 376      45.788  25.218  38.627  1.00 36.53           O  
ATOM   2742  OE2 GLU A 376      45.193  27.159  37.791  1.00 37.68           O  
ATOM   2743  N   ASP A 377      49.729  26.901  42.043  1.00 25.56           N  
ATOM   2744  CA  ASP A 377      49.683  27.303  43.448  1.00 26.24           C  
ATOM   2745  C   ASP A 377      50.895  28.132  43.866  1.00 25.11           C  
ATOM   2746  O   ASP A 377      50.853  28.837  44.873  1.00 23.90           O  
ATOM   2747  CB  ASP A 377      49.567  26.070  44.345  1.00 28.50           C  
ATOM   2748  CG  ASP A 377      48.160  25.857  44.850  1.00 32.70           C  
ATOM   2749  OD1 ASP A 377      47.216  26.002  44.047  1.00 38.19           O  
ATOM   2750  OD2 ASP A 377      47.992  25.541  46.046  1.00 36.12           O  
ATOM   2751  N   LEU A 378      51.980  28.039  43.103  1.00 22.82           N  
ATOM   2752  CA  LEU A 378      53.170  28.819  43.416  1.00 22.42           C  
ATOM   2753  C   LEU A 378      52.811  30.274  43.140  1.00 21.63           C  
ATOM   2754  O   LEU A 378      53.165  31.175  43.906  1.00 19.27           O  
ATOM   2755  CB  LEU A 378      54.349  28.401  42.532  1.00 23.11           C  
ATOM   2756  CG  LEU A 378      55.660  29.142  42.815  1.00 23.64           C  
ATOM   2757  CD1 LEU A 378      56.084  28.889  44.253  1.00 23.67           C  
ATOM   2758  CD2 LEU A 378      56.739  28.674  41.855  1.00 23.00           C  
ATOM   2759  N   VAL A 379      52.100  30.491  42.037  1.00 19.69           N  
ATOM   2760  CA  VAL A 379      51.664  31.829  41.666  1.00 20.55           C  
ATOM   2761  C   VAL A 379      50.678  32.332  42.717  1.00 19.32           C  
ATOM   2762  O   VAL A 379      50.747  33.485  43.138  1.00 20.39           O  
ATOM   2763  CB  VAL A 379      50.977  31.834  40.282  1.00 21.61           C  
ATOM   2764  CG1 VAL A 379      50.409  33.215  39.983  1.00 20.73           C  
ATOM   2765  CG2 VAL A 379      51.981  31.433  39.209  1.00 24.65           C  
ATOM   2766  N   VAL A 380      49.766  31.465  43.150  1.00 19.65           N  
ATOM   2767  CA  VAL A 380      48.790  31.858  44.163  1.00 20.22           C  
ATOM   2768  C   VAL A 380      49.497  32.226  45.466  1.00 21.47           C  
ATOM   2769  O   VAL A 380      49.085  33.150  46.171  1.00 20.05           O  
ATOM   2770  CB  VAL A 380      47.767  30.730  44.439  1.00 20.61           C  
ATOM   2771  CG1 VAL A 380      46.824  31.137  45.578  1.00 19.72           C  
ATOM   2772  CG2 VAL A 380      46.957  30.447  43.174  1.00 18.85           C  
ATOM   2773  N   ALA A 381      50.572  31.510  45.776  1.00 20.65           N  
ATOM   2774  CA  ALA A 381      51.332  31.781  46.989  1.00 20.54           C  
ATOM   2775  C   ALA A 381      51.912  33.196  46.935  1.00 20.50           C  
ATOM   2776  O   ALA A 381      51.902  33.915  47.934  1.00 20.25           O  
ATOM   2777  CB  ALA A 381      52.448  30.755  47.145  1.00 20.33           C  
ATOM   2778  N   HIS A 382      52.422  33.591  45.769  1.00 19.01           N  
ATOM   2779  CA  HIS A 382      52.979  34.931  45.605  1.00 18.24           C  
ATOM   2780  C   HIS A 382      51.861  35.950  45.736  1.00 16.58           C  
ATOM   2781  O   HIS A 382      52.041  37.005  46.339  1.00 15.66           O  
ATOM   2782  CB  HIS A 382      53.653  35.084  44.236  1.00 18.06           C  
ATOM   2783  CG  HIS A 382      55.006  34.452  44.161  1.00 17.97           C  
ATOM   2784  ND1 HIS A 382      55.193  33.087  44.199  1.00 18.68           N  
ATOM   2785  CD2 HIS A 382      56.243  35.001  44.109  1.00 17.44           C  
ATOM   2786  CE1 HIS A 382      56.488  32.822  44.176  1.00 17.45           C  
ATOM   2787  NE2 HIS A 382      57.146  33.965  44.123  1.00 17.19           N  
ATOM   2788  N   HIS A 383      50.708  35.623  45.158  1.00 16.88           N  
ATOM   2789  CA  HIS A 383      49.534  36.492  45.212  1.00 16.63           C  
ATOM   2790  C   HIS A 383      49.218  36.835  46.662  1.00 16.06           C  
ATOM   2791  O   HIS A 383      49.070  38.006  47.017  1.00 17.09           O  
ATOM   2792  CB  HIS A 383      48.320  35.785  44.596  1.00 17.03           C  
ATOM   2793  CG  HIS A 383      47.034  36.539  44.760  1.00 17.66           C  
ATOM   2794  ND1 HIS A 383      46.612  37.497  43.863  1.00 17.56           N  
ATOM   2795  CD2 HIS A 383      46.091  36.491  45.732  1.00 16.85           C  
ATOM   2796  CE1 HIS A 383      45.463  38.005  44.275  1.00 17.61           C  
ATOM   2797  NE2 HIS A 383      45.125  37.411  45.406  1.00 17.08           N  
ATOM   2798  N   GLU A 384      49.118  35.799  47.493  1.00 15.07           N  
ATOM   2799  CA  GLU A 384      48.807  35.964  48.910  1.00 16.06           C  
ATOM   2800  C   GLU A 384      49.920  36.679  49.676  1.00 17.92           C  
ATOM   2801  O   GLU A 384      49.642  37.486  50.570  1.00 18.35           O  
ATOM   2802  CB  GLU A 384      48.527  34.600  49.553  1.00 16.75           C  
ATOM   2803  CG  GLU A 384      47.327  33.845  48.972  1.00 16.11           C  
ATOM   2804  CD  GLU A 384      46.013  34.599  49.145  1.00 16.59           C  
ATOM   2805  OE1 GLU A 384      45.878  35.334  50.142  1.00 17.28           O  
ATOM   2806  OE2 GLU A 384      45.109  34.444  48.292  1.00 15.42           O  
ATOM   2807  N   MET A 385      51.174  36.383  49.338  1.00 16.54           N  
ATOM   2808  CA  MET A 385      52.295  37.034  50.008  1.00 17.95           C  
ATOM   2809  C   MET A 385      52.280  38.522  49.670  1.00 18.12           C  
ATOM   2810  O   MET A 385      52.789  39.356  50.427  1.00 15.13           O  
ATOM   2811  CB  MET A 385      53.619  36.392  49.583  1.00 17.54           C  
ATOM   2812  CG  MET A 385      53.855  35.041  50.243  1.00 19.19           C  
ATOM   2813  SD  MET A 385      54.175  35.197  52.034  1.00 21.75           S  
ATOM   2814  CE  MET A 385      55.966  35.333  52.015  1.00 20.55           C  
ATOM   2815  N   GLY A 386      51.680  38.840  48.526  1.00 17.95           N  
ATOM   2816  CA  GLY A 386      51.561  40.222  48.109  1.00 15.72           C  
ATOM   2817  C   GLY A 386      50.621  40.942  49.066  1.00 15.92           C  
ATOM   2818  O   GLY A 386      50.856  42.094  49.413  1.00 14.01           O  
ATOM   2819  N   HIS A 387      49.551  40.268  49.487  1.00 16.50           N  
ATOM   2820  CA  HIS A 387      48.603  40.861  50.434  1.00 17.17           C  
ATOM   2821  C   HIS A 387      49.320  41.110  51.758  1.00 17.69           C  
ATOM   2822  O   HIS A 387      49.163  42.167  52.370  1.00 16.65           O  
ATOM   2823  CB  HIS A 387      47.415  39.931  50.697  1.00 15.51           C  
ATOM   2824  CG  HIS A 387      46.421  39.866  49.578  1.00 17.03           C  
ATOM   2825  ND1 HIS A 387      45.848  40.991  49.022  1.00 19.32           N  
ATOM   2826  CD2 HIS A 387      45.843  38.807  48.963  1.00 15.43           C  
ATOM   2827  CE1 HIS A 387      44.958  40.626  48.115  1.00 17.79           C  
ATOM   2828  NE2 HIS A 387      44.935  39.306  48.060  1.00 17.55           N  
ATOM   2829  N   ILE A 388      50.100  40.126  52.199  1.00 16.39           N  
ATOM   2830  CA  ILE A 388      50.848  40.239  53.450  1.00 18.31           C  
ATOM   2831  C   ILE A 388      51.821  41.417  53.410  1.00 17.09           C  
ATOM   2832  O   ILE A 388      51.988  42.127  54.403  1.00 18.17           O  
ATOM   2833  CB  ILE A 388      51.640  38.941  53.745  1.00 17.86           C  
ATOM   2834  CG1 ILE A 388      50.668  37.767  53.910  1.00 17.08           C  
ATOM   2835  CG2 ILE A 388      52.498  39.115  54.995  1.00 17.98           C  
ATOM   2836  CD1 ILE A 388      49.723  37.907  55.078  1.00 16.70           C  
ATOM   2837  N   GLN A 389      52.457  41.628  52.260  1.00 17.68           N  
ATOM   2838  CA  GLN A 389      53.404  42.728  52.115  1.00 16.85           C  
ATOM   2839  C   GLN A 389      52.671  44.054  52.274  1.00 17.71           C  
ATOM   2840  O   GLN A 389      53.171  44.985  52.909  1.00 17.12           O  
ATOM   2841  CB  GLN A 389      54.093  42.677  50.746  1.00 17.05           C  
ATOM   2842  CG  GLN A 389      55.148  43.766  50.562  1.00 17.55           C  
ATOM   2843  CD  GLN A 389      56.380  43.547  51.428  1.00 18.80           C  
ATOM   2844  OE1 GLN A 389      57.049  44.501  51.824  1.00 17.97           O  
ATOM   2845  NE2 GLN A 389      56.694  42.286  51.710  1.00 18.82           N  
ATOM   2846  N   TYR A 390      51.479  44.138  51.695  1.00 18.42           N  
ATOM   2847  CA  TYR A 390      50.688  45.356  51.792  1.00 18.42           C  
ATOM   2848  C   TYR A 390      50.344  45.619  53.266  1.00 19.47           C  
ATOM   2849  O   TYR A 390      50.473  46.746  53.744  1.00 19.23           O  
ATOM   2850  CB  TYR A 390      49.418  45.217  50.943  1.00 16.41           C  
ATOM   2851  CG  TYR A 390      49.113  46.419  50.075  1.00 15.65           C  
ATOM   2852  CD1 TYR A 390      48.661  46.257  48.764  1.00 14.49           C  
ATOM   2853  CD2 TYR A 390      49.237  47.717  50.570  1.00 16.14           C  
ATOM   2854  CE1 TYR A 390      48.335  47.352  47.973  1.00 14.23           C  
ATOM   2855  CE2 TYR A 390      48.913  48.825  49.783  1.00 15.24           C  
ATOM   2856  CZ  TYR A 390      48.459  48.633  48.486  1.00 16.86           C  
ATOM   2857  OH  TYR A 390      48.108  49.718  47.703  1.00 14.61           O  
ATOM   2858  N   PHE A 391      49.928  44.577  53.986  1.00 19.13           N  
ATOM   2859  CA  PHE A 391      49.591  44.716  55.407  1.00 20.97           C  
ATOM   2860  C   PHE A 391      50.771  45.314  56.170  1.00 21.67           C  
ATOM   2861  O   PHE A 391      50.619  46.274  56.923  1.00 21.52           O  
ATOM   2862  CB  PHE A 391      49.260  43.353  56.029  1.00 19.61           C  
ATOM   2863  CG  PHE A 391      48.029  42.690  55.463  1.00 19.85           C  
ATOM   2864  CD1 PHE A 391      47.863  41.309  55.574  1.00 20.06           C  
ATOM   2865  CD2 PHE A 391      47.038  43.434  54.829  1.00 18.91           C  
ATOM   2866  CE1 PHE A 391      46.731  40.675  55.058  1.00 19.40           C  
ATOM   2867  CE2 PHE A 391      45.898  42.807  54.312  1.00 18.30           C  
ATOM   2868  CZ  PHE A 391      45.748  41.425  54.427  1.00 18.76           C  
ATOM   2869  N   MET A 392      51.950  44.737  55.964  1.00 21.08           N  
ATOM   2870  CA  MET A 392      53.153  45.196  56.644  1.00 21.47           C  
ATOM   2871  C   MET A 392      53.560  46.610  56.257  1.00 22.13           C  
ATOM   2872  O   MET A 392      54.024  47.375  57.104  1.00 21.14           O  
ATOM   2873  CB  MET A 392      54.316  44.237  56.373  1.00 21.55           C  
ATOM   2874  CG  MET A 392      54.057  42.811  56.820  1.00 23.09           C  
ATOM   2875  SD  MET A 392      55.572  41.828  56.883  1.00 26.45           S  
ATOM   2876  CE  MET A 392      55.812  41.441  55.121  1.00 20.52           C  
ATOM   2877  N   GLN A 393      53.381  46.957  54.985  1.00 21.08           N  
ATOM   2878  CA  GLN A 393      53.747  48.281  54.499  1.00 21.09           C  
ATOM   2879  C   GLN A 393      52.921  49.431  55.082  1.00 22.17           C  
ATOM   2880  O   GLN A 393      53.460  50.514  55.319  1.00 21.22           O  
ATOM   2881  CB  GLN A 393      53.668  48.326  52.967  1.00 21.81           C  
ATOM   2882  CG  GLN A 393      54.783  47.570  52.238  1.00 20.30           C  
ATOM   2883  CD  GLN A 393      56.145  48.214  52.419  1.00 21.34           C  
ATOM   2884  OE1 GLN A 393      56.248  49.415  52.677  1.00 21.87           O  
ATOM   2885  NE2 GLN A 393      57.200  47.422  52.262  1.00 20.74           N  
ATOM   2886  N   TYR A 394      51.624  49.219  55.308  1.00 21.31           N  
ATOM   2887  CA  TYR A 394      50.791  50.293  55.861  1.00 20.51           C  
ATOM   2888  C   TYR A 394      50.354  50.082  57.310  1.00 21.09           C  
ATOM   2889  O   TYR A 394      49.447  50.758  57.795  1.00 21.46           O  
ATOM   2890  CB  TYR A 394      49.551  50.538  54.975  1.00 18.49           C  
ATOM   2891  CG  TYR A 394      48.603  49.360  54.753  1.00 18.46           C  
ATOM   2892  CD1 TYR A 394      48.144  48.581  55.820  1.00 16.90           C  
ATOM   2893  CD2 TYR A 394      48.091  49.089  53.478  1.00 16.81           C  
ATOM   2894  CE1 TYR A 394      47.193  47.564  55.624  1.00 16.58           C  
ATOM   2895  CE2 TYR A 394      47.139  48.083  53.272  1.00 16.87           C  
ATOM   2896  CZ  TYR A 394      46.694  47.324  54.349  1.00 18.42           C  
ATOM   2897  OH  TYR A 394      45.744  46.342  54.150  1.00 17.95           O  
ATOM   2898  N   LYS A 395      51.018  49.162  58.003  1.00 21.85           N  
ATOM   2899  CA  LYS A 395      50.678  48.840  59.391  1.00 24.15           C  
ATOM   2900  C   LYS A 395      50.708  50.007  60.383  1.00 24.45           C  
ATOM   2901  O   LYS A 395      50.117  49.914  61.460  1.00 24.16           O  
ATOM   2902  CB  LYS A 395      51.593  47.727  59.912  1.00 23.65           C  
ATOM   2903  CG  LYS A 395      53.048  48.138  60.077  1.00 27.12           C  
ATOM   2904  CD  LYS A 395      53.883  46.986  60.636  1.00 29.68           C  
ATOM   2905  CE  LYS A 395      55.337  47.396  60.853  1.00 32.06           C  
ATOM   2906  NZ  LYS A 395      55.457  48.484  61.862  1.00 35.07           N  
ATOM   2907  N   ASP A 396      51.385  51.098  60.033  1.00 25.44           N  
ATOM   2908  CA  ASP A 396      51.473  52.238  60.941  1.00 27.31           C  
ATOM   2909  C   ASP A 396      50.466  53.354  60.686  1.00 27.40           C  
ATOM   2910  O   ASP A 396      50.487  54.382  61.362  1.00 27.53           O  
ATOM   2911  CB  ASP A 396      52.888  52.816  60.921  1.00 29.17           C  
ATOM   2912  CG  ASP A 396      53.919  51.824  61.410  1.00 32.66           C  
ATOM   2913  OD1 ASP A 396      53.697  51.226  62.484  1.00 34.11           O  
ATOM   2914  OD2 ASP A 396      54.948  51.644  60.727  1.00 35.93           O  
ATOM   2915  N   LEU A 397      49.586  53.163  59.711  1.00 26.71           N  
ATOM   2916  CA  LEU A 397      48.581  54.175  59.417  1.00 25.14           C  
ATOM   2917  C   LEU A 397      47.356  53.897  60.271  1.00 23.90           C  
ATOM   2918  O   LEU A 397      47.199  52.798  60.801  1.00 23.96           O  
ATOM   2919  CB  LEU A 397      48.159  54.110  57.946  1.00 25.72           C  
ATOM   2920  CG  LEU A 397      49.169  54.334  56.819  1.00 24.48           C  
ATOM   2921  CD1 LEU A 397      48.466  54.097  55.487  1.00 23.73           C  
ATOM   2922  CD2 LEU A 397      49.731  55.743  56.878  1.00 24.31           C  
ATOM   2923  N   PRO A 398      46.477  54.897  60.433  1.00 23.83           N  
ATOM   2924  CA  PRO A 398      45.267  54.676  61.232  1.00 24.74           C  
ATOM   2925  C   PRO A 398      44.555  53.484  60.584  1.00 25.64           C  
ATOM   2926  O   PRO A 398      44.529  53.380  59.356  1.00 25.40           O  
ATOM   2927  CB  PRO A 398      44.497  55.977  61.046  1.00 22.89           C  
ATOM   2928  CG  PRO A 398      45.593  56.993  60.911  1.00 23.44           C  
ATOM   2929  CD  PRO A 398      46.585  56.303  60.003  1.00 22.86           C  
ATOM   2930  N   VAL A 399      43.986  52.590  61.390  1.00 26.24           N  
ATOM   2931  CA  VAL A 399      43.320  51.404  60.854  1.00 26.47           C  
ATOM   2932  C   VAL A 399      42.307  51.672  59.743  1.00 25.82           C  
ATOM   2933  O   VAL A 399      42.148  50.856  58.837  1.00 24.60           O  
ATOM   2934  CB  VAL A 399      42.621  50.590  61.972  1.00 29.13           C  
ATOM   2935  CG1 VAL A 399      43.660  50.035  62.933  1.00 28.70           C  
ATOM   2936  CG2 VAL A 399      41.620  51.467  62.708  1.00 30.53           C  
ATOM   2937  N   ALA A 400      41.629  52.812  59.802  1.00 24.76           N  
ATOM   2938  CA  ALA A 400      40.639  53.143  58.786  1.00 24.41           C  
ATOM   2939  C   ALA A 400      41.286  53.313  57.419  1.00 23.48           C  
ATOM   2940  O   ALA A 400      40.623  53.198  56.391  1.00 23.10           O  
ATOM   2941  CB  ALA A 400      39.898  54.419  59.171  1.00 26.53           C  
ATOM   2942  N   LEU A 401      42.587  53.583  57.407  1.00 23.44           N  
ATOM   2943  CA  LEU A 401      43.297  53.785  56.153  1.00 22.88           C  
ATOM   2944  C   LEU A 401      44.178  52.595  55.787  1.00 23.45           C  
ATOM   2945  O   LEU A 401      44.974  52.666  54.844  1.00 23.80           O  
ATOM   2946  CB  LEU A 401      44.143  55.059  56.236  1.00 23.01           C  
ATOM   2947  CG  LEU A 401      43.365  56.321  56.628  1.00 22.58           C  
ATOM   2948  CD1 LEU A 401      44.321  57.500  56.716  1.00 21.61           C  
ATOM   2949  CD2 LEU A 401      42.267  56.597  55.606  1.00 24.25           C  
ATOM   2950  N   ARG A 402      44.030  51.501  56.529  1.00 22.08           N  
ATOM   2951  CA  ARG A 402      44.815  50.303  56.260  1.00 22.75           C  
ATOM   2952  C   ARG A 402      44.162  49.424  55.188  1.00 21.02           C  
ATOM   2953  O   ARG A 402      43.635  48.347  55.474  1.00 19.37           O  
ATOM   2954  CB  ARG A 402      45.026  49.497  57.546  1.00 23.50           C  
ATOM   2955  CG  ARG A 402      45.849  50.225  58.607  1.00 26.73           C  
ATOM   2956  CD  ARG A 402      46.193  49.307  59.779  1.00 29.04           C  
ATOM   2957  NE  ARG A 402      46.793  50.044  60.888  1.00 32.42           N  
ATOM   2958  CZ  ARG A 402      47.191  49.492  62.031  1.00 33.50           C  
ATOM   2959  NH1 ARG A 402      47.061  48.187  62.229  1.00 33.63           N  
ATOM   2960  NH2 ARG A 402      47.710  50.252  62.986  1.00 35.11           N  
ATOM   2961  N   GLU A 403      44.188  49.914  53.954  1.00 20.40           N  
ATOM   2962  CA  GLU A 403      43.644  49.196  52.803  1.00 21.33           C  
ATOM   2963  C   GLU A 403      44.476  49.606  51.604  1.00 18.30           C  
ATOM   2964  O   GLU A 403      45.303  50.507  51.713  1.00 16.88           O  
ATOM   2965  CB  GLU A 403      42.172  49.560  52.567  1.00 24.12           C  
ATOM   2966  CG  GLU A 403      41.226  49.009  53.624  1.00 34.46           C  
ATOM   2967  CD  GLU A 403      40.542  50.099  54.420  1.00 38.95           C  
ATOM   2968  OE1 GLU A 403      41.253  50.975  54.958  1.00 42.61           O  
ATOM   2969  OE2 GLU A 403      39.295  50.078  54.515  1.00 42.67           O  
ATOM   2970  N   GLY A 404      44.271  48.945  50.466  1.00 19.36           N  
ATOM   2971  CA  GLY A 404      45.031  49.296  49.276  1.00 18.55           C  
ATOM   2972  C   GLY A 404      44.491  50.578  48.679  1.00 18.67           C  
ATOM   2973  O   GLY A 404      43.400  51.005  49.055  1.00 17.09           O  
ATOM   2974  N   ALA A 405      45.246  51.204  47.775  1.00 19.08           N  
ATOM   2975  CA  ALA A 405      44.799  52.442  47.123  1.00 17.26           C  
ATOM   2976  C   ALA A 405      43.336  52.215  46.722  1.00 16.59           C  
ATOM   2977  O   ALA A 405      42.493  53.097  46.842  1.00 16.06           O  
ATOM   2978  CB  ALA A 405      45.667  52.731  45.906  1.00 17.85           C  
ATOM   2979  N   ASN A 406      43.066  51.020  46.212  1.00 16.87           N  
ATOM   2980  CA  ASN A 406      41.712  50.570  45.889  1.00 16.03           C  
ATOM   2981  C   ASN A 406      41.865  49.054  45.948  1.00 16.39           C  
ATOM   2982  O   ASN A 406      42.988  48.551  45.956  1.00 15.77           O  
ATOM   2983  CB  ASN A 406      41.185  51.088  44.526  1.00 14.52           C  
ATOM   2984  CG  ASN A 406      41.872  50.474  43.324  1.00 14.43           C  
ATOM   2985  OD1 ASN A 406      42.105  49.269  43.261  1.00 15.44           O  
ATOM   2986  ND2 ASN A 406      42.162  51.311  42.335  1.00 13.55           N  
ATOM   2987  N   PRO A 407      40.756  48.306  46.030  1.00 15.87           N  
ATOM   2988  CA  PRO A 407      40.869  46.846  46.105  1.00 13.68           C  
ATOM   2989  C   PRO A 407      41.737  46.185  45.039  1.00 14.27           C  
ATOM   2990  O   PRO A 407      42.379  45.170  45.306  1.00 14.30           O  
ATOM   2991  CB  PRO A 407      39.413  46.391  46.059  1.00 14.60           C  
ATOM   2992  CG  PRO A 407      38.712  47.508  46.793  1.00 16.23           C  
ATOM   2993  CD  PRO A 407      39.350  48.730  46.157  1.00 14.94           C  
ATOM   2994  N   GLY A 408      41.760  46.760  43.840  1.00 13.68           N  
ATOM   2995  CA  GLY A 408      42.563  46.201  42.766  1.00 13.77           C  
ATOM   2996  C   GLY A 408      44.051  46.182  43.070  1.00 14.65           C  
ATOM   2997  O   GLY A 408      44.741  45.203  42.776  1.00 12.71           O  
ATOM   2998  N   PHE A 409      44.553  47.269  43.649  1.00 14.29           N  
ATOM   2999  CA  PHE A 409      45.968  47.364  44.006  1.00 14.09           C  
ATOM   3000  C   PHE A 409      46.369  46.235  44.954  1.00 13.76           C  
ATOM   3001  O   PHE A 409      47.432  45.629  44.807  1.00 12.46           O  
ATOM   3002  CB  PHE A 409      46.262  48.708  44.691  1.00 14.69           C  
ATOM   3003  CG  PHE A 409      46.467  49.856  43.736  1.00 17.06           C  
ATOM   3004  CD1 PHE A 409      45.474  50.226  42.836  1.00 16.87           C  
ATOM   3005  CD2 PHE A 409      47.658  50.580  43.753  1.00 16.76           C  
ATOM   3006  CE1 PHE A 409      45.663  51.307  41.962  1.00 16.34           C  
ATOM   3007  CE2 PHE A 409      47.856  51.655  42.890  1.00 16.34           C  
ATOM   3008  CZ  PHE A 409      46.857  52.019  41.993  1.00 16.50           C  
ATOM   3009  N   HIS A 410      45.521  45.962  45.940  1.00 14.94           N  
ATOM   3010  CA  HIS A 410      45.813  44.911  46.910  1.00 15.78           C  
ATOM   3011  C   HIS A 410      45.958  43.555  46.220  1.00 16.92           C  
ATOM   3012  O   HIS A 410      46.813  42.747  46.592  1.00 15.31           O  
ATOM   3013  CB  HIS A 410      44.703  44.833  47.964  1.00 17.07           C  
ATOM   3014  CG  HIS A 410      45.209  44.750  49.374  1.00 15.66           C  
ATOM   3015  ND1 HIS A 410      46.073  43.763  49.802  1.00 16.88           N  
ATOM   3016  CD2 HIS A 410      44.960  45.526  50.456  1.00 15.15           C  
ATOM   3017  CE1 HIS A 410      46.332  43.935  51.087  1.00 14.94           C  
ATOM   3018  NE2 HIS A 410      45.669  44.998  51.508  1.00 15.07           N  
ATOM   3019  N   GLU A 411      45.122  43.311  45.214  1.00 16.74           N  
ATOM   3020  CA  GLU A 411      45.162  42.049  44.482  1.00 15.92           C  
ATOM   3021  C   GLU A 411      46.329  41.955  43.497  1.00 17.24           C  
ATOM   3022  O   GLU A 411      46.778  40.859  43.162  1.00 16.84           O  
ATOM   3023  CB  GLU A 411      43.861  41.851  43.701  1.00 15.02           C  
ATOM   3024  CG  GLU A 411      42.590  41.822  44.542  1.00 11.10           C  
ATOM   3025  CD  GLU A 411      42.635  40.757  45.617  1.00 11.15           C  
ATOM   3026  OE1 GLU A 411      43.250  39.697  45.371  1.00 14.00           O  
ATOM   3027  OE2 GLU A 411      42.055  40.975  46.699  1.00 11.81           O  
ATOM   3028  N   ALA A 412      46.826  43.100  43.039  1.00 15.95           N  
ATOM   3029  CA  ALA A 412      47.894  43.114  42.041  1.00 17.36           C  
ATOM   3030  C   ALA A 412      49.343  42.907  42.491  1.00 16.95           C  
ATOM   3031  O   ALA A 412      50.135  42.328  41.750  1.00 17.94           O  
ATOM   3032  CB  ALA A 412      47.799  44.404  41.221  1.00 15.87           C  
ATOM   3033  N   ILE A 413      49.692  43.374  43.686  1.00 16.73           N  
ATOM   3034  CA  ILE A 413      51.070  43.264  44.176  1.00 15.92           C  
ATOM   3035  C   ILE A 413      51.744  41.902  43.980  1.00 16.43           C  
ATOM   3036  O   ILE A 413      52.792  41.807  43.332  1.00 15.13           O  
ATOM   3037  CB  ILE A 413      51.166  43.630  45.671  1.00 15.04           C  
ATOM   3038  CG1 ILE A 413      50.502  44.990  45.927  1.00 14.90           C  
ATOM   3039  CG2 ILE A 413      52.631  43.664  46.095  1.00 16.89           C  
ATOM   3040  CD1 ILE A 413      51.112  46.139  45.153  1.00 15.89           C  
ATOM   3041  N   GLY A 414      51.155  40.858  44.554  1.00 15.53           N  
ATOM   3042  CA  GLY A 414      51.724  39.528  44.427  1.00 16.88           C  
ATOM   3043  C   GLY A 414      51.844  39.072  42.985  1.00 18.50           C  
ATOM   3044  O   GLY A 414      52.866  38.512  42.581  1.00 17.19           O  
ATOM   3045  N   ASP A 415      50.796  39.317  42.205  1.00 16.96           N  
ATOM   3046  CA  ASP A 415      50.775  38.935  40.795  1.00 17.24           C  
ATOM   3047  C   ASP A 415      51.919  39.572  40.016  1.00 18.31           C  
ATOM   3048  O   ASP A 415      52.503  38.939  39.132  1.00 16.77           O  
ATOM   3049  CB  ASP A 415      49.438  39.334  40.157  1.00 15.35           C  
ATOM   3050  CG  ASP A 415      48.291  38.426  40.579  1.00 17.38           C  
ATOM   3051  OD1 ASP A 415      48.298  37.936  41.728  1.00 14.96           O  
ATOM   3052  OD2 ASP A 415      47.370  38.212  39.761  1.00 16.72           O  
ATOM   3053  N   VAL A 416      52.234  40.829  40.328  1.00 18.18           N  
ATOM   3054  CA  VAL A 416      53.314  41.508  39.629  1.00 18.02           C  
ATOM   3055  C   VAL A 416      54.611  40.716  39.765  1.00 18.36           C  
ATOM   3056  O   VAL A 416      55.293  40.471  38.773  1.00 17.66           O  
ATOM   3057  CB  VAL A 416      53.542  42.935  40.158  1.00 17.59           C  
ATOM   3058  CG1 VAL A 416      54.795  43.520  39.514  1.00 20.25           C  
ATOM   3059  CG2 VAL A 416      52.330  43.816  39.831  1.00 15.79           C  
ATOM   3060  N   LEU A 417      54.948  40.312  40.986  1.00 18.09           N  
ATOM   3061  CA  LEU A 417      56.167  39.543  41.194  1.00 18.49           C  
ATOM   3062  C   LEU A 417      56.053  38.170  40.529  1.00 19.50           C  
ATOM   3063  O   LEU A 417      57.011  37.682  39.930  1.00 20.72           O  
ATOM   3064  CB  LEU A 417      56.464  39.378  42.691  1.00 17.75           C  
ATOM   3065  CG  LEU A 417      57.233  40.500  43.405  1.00 18.33           C  
ATOM   3066  CD1 LEU A 417      56.458  41.811  43.359  1.00 17.13           C  
ATOM   3067  CD2 LEU A 417      57.487  40.082  44.848  1.00 18.72           C  
ATOM   3068  N   ALA A 418      54.879  37.551  40.627  1.00 18.48           N  
ATOM   3069  CA  ALA A 418      54.671  36.240  40.028  1.00 18.81           C  
ATOM   3070  C   ALA A 418      54.905  36.272  38.518  1.00 17.58           C  
ATOM   3071  O   ALA A 418      55.285  35.261  37.925  1.00 17.76           O  
ATOM   3072  CB  ALA A 418      53.260  35.731  40.337  1.00 18.00           C  
ATOM   3073  N   LEU A 419      54.677  37.424  37.890  1.00 16.49           N  
ATOM   3074  CA  LEU A 419      54.898  37.536  36.449  1.00 16.51           C  
ATOM   3075  C   LEU A 419      56.376  37.262  36.150  1.00 18.30           C  
ATOM   3076  O   LEU A 419      56.702  36.552  35.196  1.00 17.45           O  
ATOM   3077  CB  LEU A 419      54.516  38.933  35.935  1.00 15.69           C  
ATOM   3078  CG  LEU A 419      53.027  39.294  35.797  1.00 14.12           C  
ATOM   3079  CD1 LEU A 419      52.887  40.749  35.374  1.00 12.95           C  
ATOM   3080  CD2 LEU A 419      52.356  38.385  34.770  1.00 15.02           C  
ATOM   3081  N   SER A 420      57.266  37.824  36.966  1.00 18.19           N  
ATOM   3082  CA  SER A 420      58.701  37.617  36.777  1.00 18.99           C  
ATOM   3083  C   SER A 420      59.092  36.178  37.092  1.00 19.71           C  
ATOM   3084  O   SER A 420      59.896  35.575  36.383  1.00 20.72           O  
ATOM   3085  CB  SER A 420      59.507  38.572  37.663  1.00 16.95           C  
ATOM   3086  OG  SER A 420      59.480  39.890  37.141  1.00 17.53           O  
ATOM   3087  N   VAL A 421      58.520  35.635  38.160  1.00 21.54           N  
ATOM   3088  CA  VAL A 421      58.798  34.263  38.574  1.00 22.76           C  
ATOM   3089  C   VAL A 421      58.435  33.259  37.482  1.00 24.01           C  
ATOM   3090  O   VAL A 421      59.112  32.243  37.307  1.00 23.13           O  
ATOM   3091  CB  VAL A 421      57.997  33.893  39.843  1.00 22.77           C  
ATOM   3092  CG1 VAL A 421      58.217  32.428  40.195  1.00 25.58           C  
ATOM   3093  CG2 VAL A 421      58.419  34.781  40.997  1.00 25.93           C  
ATOM   3094  N   SER A 422      57.358  33.552  36.757  1.00 22.60           N  
ATOM   3095  CA  SER A 422      56.870  32.678  35.693  1.00 23.40           C  
ATOM   3096  C   SER A 422      57.715  32.622  34.424  1.00 22.87           C  
ATOM   3097  O   SER A 422      57.563  31.697  33.631  1.00 22.16           O  
ATOM   3098  CB  SER A 422      55.434  33.067  35.317  1.00 21.89           C  
ATOM   3099  OG  SER A 422      54.546  32.810  36.393  1.00 20.22           O  
ATOM   3100  N   THR A 423      58.592  33.602  34.219  1.00 23.18           N  
ATOM   3101  CA  THR A 423      59.420  33.601  33.016  1.00 24.33           C  
ATOM   3102  C   THR A 423      60.240  32.313  32.940  1.00 25.55           C  
ATOM   3103  O   THR A 423      60.749  31.827  33.949  1.00 25.28           O  
ATOM   3104  CB  THR A 423      60.373  34.817  32.972  1.00 23.24           C  
ATOM   3105  OG1 THR A 423      61.199  34.827  34.143  1.00 24.32           O  
ATOM   3106  CG2 THR A 423      59.576  36.115  32.894  1.00 24.49           C  
ATOM   3107  N   PRO A 424      60.368  31.738  31.734  1.00 25.92           N  
ATOM   3108  CA  PRO A 424      61.134  30.499  31.574  1.00 27.37           C  
ATOM   3109  C   PRO A 424      62.499  30.573  32.245  1.00 27.20           C  
ATOM   3110  O   PRO A 424      62.909  29.646  32.946  1.00 26.66           O  
ATOM   3111  CB  PRO A 424      61.238  30.351  30.058  1.00 27.14           C  
ATOM   3112  CG  PRO A 424      59.949  30.959  29.578  1.00 25.75           C  
ATOM   3113  CD  PRO A 424      59.860  32.211  30.433  1.00 26.48           C  
ATOM   3114  N   LYS A 425      63.193  31.688  32.045  1.00 28.50           N  
ATOM   3115  CA  LYS A 425      64.513  31.851  32.626  1.00 29.18           C  
ATOM   3116  C   LYS A 425      64.501  31.795  34.151  1.00 29.42           C  
ATOM   3117  O   LYS A 425      65.366  31.151  34.753  1.00 28.75           O  
ATOM   3118  CB  LYS A 425      65.150  33.161  32.164  1.00 31.89           C  
ATOM   3119  CG  LYS A 425      66.669  33.142  32.280  1.00 36.40           C  
ATOM   3120  CD  LYS A 425      67.296  34.487  31.959  1.00 39.36           C  
ATOM   3121  CE  LYS A 425      68.815  34.374  31.932  1.00 40.98           C  
ATOM   3122  NZ  LYS A 425      69.335  33.657  33.129  1.00 43.02           N  
ATOM   3123  N   HIS A 426      63.534  32.458  34.785  1.00 24.85           N  
ATOM   3124  CA  HIS A 426      63.486  32.427  36.242  1.00 23.20           C  
ATOM   3125  C   HIS A 426      63.167  31.019  36.738  1.00 23.20           C  
ATOM   3126  O   HIS A 426      63.768  30.541  37.701  1.00 21.36           O  
ATOM   3127  CB  HIS A 426      62.439  33.397  36.791  1.00 23.95           C  
ATOM   3128  CG  HIS A 426      62.503  33.558  38.278  1.00 23.17           C  
ATOM   3129  ND1 HIS A 426      63.300  34.501  38.892  1.00 24.07           N  
ATOM   3130  CD2 HIS A 426      61.930  32.846  39.277  1.00 23.50           C  
ATOM   3131  CE1 HIS A 426      63.218  34.360  40.203  1.00 25.29           C  
ATOM   3132  NE2 HIS A 426      62.393  33.361  40.463  1.00 25.90           N  
ATOM   3133  N   LEU A 427      62.208  30.362  36.089  1.00 24.06           N  
ATOM   3134  CA  LEU A 427      61.835  29.010  36.481  1.00 25.22           C  
ATOM   3135  C   LEU A 427      63.058  28.105  36.350  1.00 26.11           C  
ATOM   3136  O   LEU A 427      63.265  27.204  37.157  1.00 24.93           O  
ATOM   3137  CB  LEU A 427      60.694  28.486  35.600  1.00 25.32           C  
ATOM   3138  CG  LEU A 427      59.302  29.096  35.812  1.00 24.79           C  
ATOM   3139  CD1 LEU A 427      58.314  28.482  34.827  1.00 24.94           C  
ATOM   3140  CD2 LEU A 427      58.848  28.852  37.249  1.00 24.07           C  
ATOM   3141  N   HIS A 428      63.875  28.356  35.334  1.00 28.43           N  
ATOM   3142  CA  HIS A 428      65.070  27.548  35.140  1.00 31.28           C  
ATOM   3143  C   HIS A 428      66.053  27.782  36.283  1.00 30.04           C  
ATOM   3144  O   HIS A 428      66.755  26.861  36.699  1.00 29.57           O  
ATOM   3145  CB  HIS A 428      65.731  27.872  33.799  1.00 33.71           C  
ATOM   3146  CG  HIS A 428      66.959  27.060  33.521  1.00 39.54           C  
ATOM   3147  ND1 HIS A 428      68.174  27.316  34.120  1.00 42.70           N  
ATOM   3148  CD2 HIS A 428      67.152  25.977  32.730  1.00 40.92           C  
ATOM   3149  CE1 HIS A 428      69.062  26.427  33.711  1.00 42.68           C  
ATOM   3150  NE2 HIS A 428      68.467  25.603  32.867  1.00 43.45           N  
ATOM   3151  N   SER A 429      66.087  29.008  36.803  1.00 28.70           N  
ATOM   3152  CA  SER A 429      66.997  29.335  37.897  1.00 27.62           C  
ATOM   3153  C   SER A 429      66.579  28.613  39.174  1.00 27.55           C  
ATOM   3154  O   SER A 429      67.380  28.446  40.091  1.00 26.24           O  
ATOM   3155  CB  SER A 429      67.034  30.850  38.142  1.00 27.69           C  
ATOM   3156  OG  SER A 429      65.945  31.283  38.942  1.00 27.73           O  
ATOM   3157  N   LEU A 430      65.321  28.186  39.228  1.00 26.91           N  
ATOM   3158  CA  LEU A 430      64.808  27.463  40.388  1.00 29.43           C  
ATOM   3159  C   LEU A 430      64.931  25.971  40.119  1.00 30.51           C  
ATOM   3160  O   LEU A 430      64.528  25.142  40.938  1.00 31.19           O  
ATOM   3161  CB  LEU A 430      63.337  27.813  40.641  1.00 27.64           C  
ATOM   3162  CG  LEU A 430      63.027  29.239  41.101  1.00 28.24           C  
ATOM   3163  CD1 LEU A 430      61.523  29.462  41.111  1.00 28.05           C  
ATOM   3164  CD2 LEU A 430      63.611  29.461  42.488  1.00 27.97           C  
ATOM   3165  N   ASN A 431      65.491  25.649  38.957  1.00 32.47           N  
ATOM   3166  CA  ASN A 431      65.684  24.272  38.523  1.00 34.80           C  
ATOM   3167  C   ASN A 431      64.337  23.607  38.222  1.00 36.15           C  
ATOM   3168  O   ASN A 431      64.154  22.414  38.466  1.00 35.72           O  
ATOM   3169  CB  ASN A 431      66.447  23.484  39.594  1.00 35.75           C  
ATOM   3170  CG  ASN A 431      67.114  22.241  39.036  1.00 38.55           C  
ATOM   3171  OD1 ASN A 431      67.732  22.283  37.973  1.00 38.16           O  
ATOM   3172  ND2 ASN A 431      67.006  21.132  39.758  1.00 39.43           N  
ATOM   3173  N   LEU A 432      63.402  24.391  37.689  1.00 36.82           N  
ATOM   3174  CA  LEU A 432      62.074  23.886  37.345  1.00 39.43           C  
ATOM   3175  C   LEU A 432      61.851  23.900  35.839  1.00 41.12           C  
ATOM   3176  O   LEU A 432      60.771  23.568  35.355  1.00 42.26           O  
ATOM   3177  CB  LEU A 432      60.987  24.713  38.038  1.00 37.66           C  
ATOM   3178  CG  LEU A 432      60.997  24.667  39.569  1.00 37.31           C  
ATOM   3179  CD1 LEU A 432      59.836  25.492  40.111  1.00 36.51           C  
ATOM   3180  CD2 LEU A 432      60.898  23.227  40.046  1.00 36.47           C  
ATOM   3181  N   LEU A 433      62.880  24.307  35.105  1.00 43.53           N  
ATOM   3182  CA  LEU A 433      62.832  24.341  33.647  1.00 46.78           C  
ATOM   3183  C   LEU A 433      64.217  24.032  33.097  1.00 47.91           C  
ATOM   3184  O   LEU A 433      65.208  24.081  33.830  1.00 48.74           O  
ATOM   3185  CB  LEU A 433      62.358  25.707  33.131  1.00 47.15           C  
ATOM   3186  CG  LEU A 433      60.846  25.963  33.126  1.00 47.86           C  
ATOM   3187  CD1 LEU A 433      60.553  27.253  32.374  1.00 48.43           C  
ATOM   3188  CD2 LEU A 433      60.122  24.801  32.457  1.00 48.04           C  
ATOM   3189  N   SER A 434      64.282  23.702  31.812  1.00 49.72           N  
ATOM   3190  CA  SER A 434      65.552  23.375  31.173  1.00 51.10           C  
ATOM   3191  C   SER A 434      65.745  24.157  29.879  1.00 51.56           C  
ATOM   3192  O   SER A 434      66.428  25.182  29.860  1.00 52.18           O  
ATOM   3193  CB  SER A 434      65.619  21.873  30.887  1.00 51.49           C  
ATOM   3194  OG  SER A 434      64.505  21.452  30.117  1.00 52.92           O  
ATOM   3195  N   SER A 439      64.653  32.326  21.785  1.00 48.10           N  
ATOM   3196  CA  SER A 439      63.950  31.478  20.839  1.00 48.51           C  
ATOM   3197  C   SER A 439      62.522  31.928  20.591  1.00 47.84           C  
ATOM   3198  O   SER A 439      61.718  31.998  21.520  1.00 48.31           O  
ATOM   3199  N   ASP A 440      62.202  32.229  19.336  1.00 46.54           N  
ATOM   3200  CA  ASP A 440      60.864  32.681  18.976  1.00 45.12           C  
ATOM   3201  C   ASP A 440      59.799  31.654  19.351  1.00 44.20           C  
ATOM   3202  O   ASP A 440      58.843  31.976  20.056  1.00 44.05           O  
ATOM   3203  CB  ASP A 440      60.799  32.979  17.485  1.00 46.24           C  
ATOM   3204  N   GLU A 441      59.965  30.420  18.883  1.00 41.85           N  
ATOM   3205  CA  GLU A 441      59.002  29.367  19.178  1.00 40.72           C  
ATOM   3206  C   GLU A 441      58.810  29.146  20.672  1.00 39.99           C  
ATOM   3207  O   GLU A 441      57.724  28.762  21.111  1.00 37.39           O  
ATOM   3208  CB  GLU A 441      59.411  28.062  18.492  1.00 40.77           C  
ATOM   3209  CG  GLU A 441      59.039  28.041  17.019  1.00 43.32           C  
ATOM   3210  CD  GLU A 441      59.363  26.728  16.336  1.00 44.64           C  
ATOM   3211  OE1 GLU A 441      59.319  25.675  17.008  1.00 44.66           O  
ATOM   3212  OE2 GLU A 441      59.641  26.753  15.117  1.00 46.17           O  
ATOM   3213  N   HIS A 442      59.859  29.380  21.454  1.00 39.00           N  
ATOM   3214  CA  HIS A 442      59.746  29.226  22.896  1.00 38.09           C  
ATOM   3215  C   HIS A 442      59.032  30.449  23.453  1.00 36.31           C  
ATOM   3216  O   HIS A 442      58.367  30.368  24.482  1.00 36.98           O  
ATOM   3217  CB  HIS A 442      61.121  29.080  23.551  1.00 40.74           C  
ATOM   3218  CG  HIS A 442      61.664  27.684  23.510  1.00 43.40           C  
ATOM   3219  ND1 HIS A 442      62.501  27.236  22.510  1.00 45.60           N  
ATOM   3220  CD2 HIS A 442      61.475  26.632  24.341  1.00 44.06           C  
ATOM   3221  CE1 HIS A 442      62.805  25.969  22.729  1.00 45.16           C  
ATOM   3222  NE2 HIS A 442      62.195  25.578  23.833  1.00 45.60           N  
ATOM   3223  N   ASP A 443      59.172  31.581  22.766  1.00 34.37           N  
ATOM   3224  CA  ASP A 443      58.516  32.810  23.187  1.00 34.17           C  
ATOM   3225  C   ASP A 443      57.007  32.692  23.021  1.00 32.16           C  
ATOM   3226  O   ASP A 443      56.248  33.095  23.903  1.00 30.43           O  
ATOM   3227  CB  ASP A 443      59.000  34.009  22.365  1.00 38.03           C  
ATOM   3228  CG  ASP A 443      60.243  34.647  22.937  1.00 41.09           C  
ATOM   3229  OD1 ASP A 443      60.257  34.930  24.154  1.00 42.53           O  
ATOM   3230  OD2 ASP A 443      61.202  34.878  22.169  1.00 43.99           O  
ATOM   3231  N   ILE A 444      56.580  32.153  21.880  1.00 28.89           N  
ATOM   3232  CA  ILE A 444      55.159  31.996  21.595  1.00 25.76           C  
ATOM   3233  C   ILE A 444      54.539  30.962  22.526  1.00 24.56           C  
ATOM   3234  O   ILE A 444      53.422  31.150  23.009  1.00 23.51           O  
ATOM   3235  CB  ILE A 444      54.922  31.577  20.122  1.00 26.10           C  
ATOM   3236  CG1 ILE A 444      55.544  32.613  19.183  1.00 23.79           C  
ATOM   3237  CG2 ILE A 444      53.425  31.456  19.838  1.00 22.06           C  
ATOM   3238  CD1 ILE A 444      54.998  34.015  19.363  1.00 25.45           C  
ATOM   3239  N   ASN A 445      55.258  29.869  22.775  1.00 22.07           N  
ATOM   3240  CA  ASN A 445      54.749  28.843  23.673  1.00 22.59           C  
ATOM   3241  C   ASN A 445      54.564  29.465  25.057  1.00 22.14           C  
ATOM   3242  O   ASN A 445      53.554  29.231  25.721  1.00 20.32           O  
ATOM   3243  CB  ASN A 445      55.718  27.658  23.777  1.00 22.82           C  
ATOM   3244  CG  ASN A 445      55.557  26.656  22.640  1.00 23.84           C  
ATOM   3245  OD1 ASN A 445      54.640  26.756  21.822  1.00 23.67           O  
ATOM   3246  ND2 ASN A 445      56.451  25.674  22.595  1.00 22.00           N  
ATOM   3247  N   PHE A 446      55.544  30.258  25.487  1.00 19.74           N  
ATOM   3248  CA  PHE A 446      55.473  30.907  26.795  1.00 20.07           C  
ATOM   3249  C   PHE A 446      54.327  31.910  26.879  1.00 18.41           C  
ATOM   3250  O   PHE A 446      53.558  31.907  27.840  1.00 17.57           O  
ATOM   3251  CB  PHE A 446      56.779  31.630  27.118  1.00 19.28           C  
ATOM   3252  CG  PHE A 446      56.697  32.491  28.348  1.00 19.26           C  
ATOM   3253  CD1 PHE A 446      56.387  31.930  29.582  1.00 19.77           C  
ATOM   3254  CD2 PHE A 446      56.908  33.861  28.270  1.00 18.99           C  
ATOM   3255  CE1 PHE A 446      56.288  32.721  30.723  1.00 20.49           C  
ATOM   3256  CE2 PHE A 446      56.811  34.664  29.404  1.00 21.68           C  
ATOM   3257  CZ  PHE A 446      56.501  34.091  30.634  1.00 20.79           C  
ATOM   3258  N   LEU A 447      54.230  32.782  25.882  1.00 16.70           N  
ATOM   3259  CA  LEU A 447      53.171  33.778  25.858  1.00 17.73           C  
ATOM   3260  C   LEU A 447      51.808  33.094  25.857  1.00 17.77           C  
ATOM   3261  O   LEU A 447      50.859  33.602  26.454  1.00 16.81           O  
ATOM   3262  CB  LEU A 447      53.315  34.692  24.634  1.00 18.54           C  
ATOM   3263  CG  LEU A 447      54.441  35.733  24.725  1.00 18.88           C  
ATOM   3264  CD1 LEU A 447      54.594  36.453  23.399  1.00 20.51           C  
ATOM   3265  CD2 LEU A 447      54.133  36.732  25.835  1.00 21.13           C  
ATOM   3266  N   MET A 448      51.710  31.943  25.192  1.00 16.85           N  
ATOM   3267  CA  MET A 448      50.447  31.207  25.155  1.00 16.42           C  
ATOM   3268  C   MET A 448      50.112  30.697  26.552  1.00 18.16           C  
ATOM   3269  O   MET A 448      48.965  30.772  26.987  1.00 16.49           O  
ATOM   3270  CB  MET A 448      50.523  30.020  24.187  1.00 16.54           C  
ATOM   3271  CG  MET A 448      49.265  29.145  24.170  1.00 15.90           C  
ATOM   3272  SD  MET A 448      47.741  30.068  23.800  1.00 20.51           S  
ATOM   3273  CE  MET A 448      47.978  30.453  22.101  1.00 14.74           C  
ATOM   3274  N   LYS A 449      51.108  30.169  27.257  1.00 17.20           N  
ATOM   3275  CA  LYS A 449      50.852  29.673  28.600  1.00 19.57           C  
ATOM   3276  C   LYS A 449      50.368  30.835  29.478  1.00 17.85           C  
ATOM   3277  O   LYS A 449      49.420  30.689  30.247  1.00 18.61           O  
ATOM   3278  CB  LYS A 449      52.117  29.038  29.191  1.00 22.36           C  
ATOM   3279  CG  LYS A 449      51.837  28.140  30.387  1.00 27.80           C  
ATOM   3280  CD  LYS A 449      53.012  27.221  30.741  1.00 33.74           C  
ATOM   3281  CE  LYS A 449      54.250  28.002  31.184  1.00 37.33           C  
ATOM   3282  NZ  LYS A 449      55.332  27.126  31.746  1.00 39.64           N  
ATOM   3283  N   MET A 450      51.006  31.992  29.343  1.00 15.91           N  
ATOM   3284  CA  MET A 450      50.619  33.165  30.123  1.00 16.21           C  
ATOM   3285  C   MET A 450      49.224  33.662  29.740  1.00 14.73           C  
ATOM   3286  O   MET A 450      48.430  34.029  30.605  1.00 15.28           O  
ATOM   3287  CB  MET A 450      51.627  34.302  29.925  1.00 15.78           C  
ATOM   3288  CG  MET A 450      53.019  34.045  30.504  1.00 17.36           C  
ATOM   3289  SD  MET A 450      53.024  33.719  32.288  1.00 23.53           S  
ATOM   3290  CE  MET A 450      52.210  35.205  32.913  1.00 14.65           C  
ATOM   3291  N   ALA A 451      48.930  33.672  28.444  1.00 12.83           N  
ATOM   3292  CA  ALA A 451      47.635  34.144  27.966  1.00 14.42           C  
ATOM   3293  C   ALA A 451      46.485  33.254  28.432  1.00 13.98           C  
ATOM   3294  O   ALA A 451      45.404  33.737  28.742  1.00 12.54           O  
ATOM   3295  CB  ALA A 451      47.640  34.229  26.440  1.00 12.60           C  
ATOM   3296  N   LEU A 452      46.721  31.950  28.469  1.00 12.96           N  
ATOM   3297  CA  LEU A 452      45.687  31.019  28.889  1.00 15.49           C  
ATOM   3298  C   LEU A 452      45.172  31.377  30.286  1.00 15.60           C  
ATOM   3299  O   LEU A 452      44.029  31.076  30.633  1.00 13.79           O  
ATOM   3300  CB  LEU A 452      46.221  29.581  28.845  1.00 13.86           C  
ATOM   3301  CG  LEU A 452      46.433  29.004  27.438  1.00 12.19           C  
ATOM   3302  CD1 LEU A 452      47.119  27.645  27.522  1.00 12.00           C  
ATOM   3303  CD2 LEU A 452      45.099  28.868  26.744  1.00 11.05           C  
ATOM   3304  N   ASP A 453      46.011  32.026  31.088  1.00 17.99           N  
ATOM   3305  CA  ASP A 453      45.579  32.432  32.421  1.00 19.85           C  
ATOM   3306  C   ASP A 453      45.159  33.900  32.469  1.00 19.15           C  
ATOM   3307  O   ASP A 453      44.016  34.205  32.801  1.00 19.40           O  
ATOM   3308  CB  ASP A 453      46.675  32.186  33.457  1.00 23.35           C  
ATOM   3309  CG  ASP A 453      46.697  30.752  33.950  1.00 31.47           C  
ATOM   3310  OD1 ASP A 453      45.708  30.017  33.703  1.00 32.89           O  
ATOM   3311  OD2 ASP A 453      47.692  30.358  34.590  1.00 35.68           O  
ATOM   3312  N   LYS A 454      46.074  34.797  32.106  1.00 15.90           N  
ATOM   3313  CA  LYS A 454      45.809  36.233  32.153  1.00 15.26           C  
ATOM   3314  C   LYS A 454      44.743  36.792  31.207  1.00 15.09           C  
ATOM   3315  O   LYS A 454      43.963  37.655  31.608  1.00 14.86           O  
ATOM   3316  CB  LYS A 454      47.115  37.013  31.937  1.00 16.44           C  
ATOM   3317  CG  LYS A 454      48.221  36.683  32.935  1.00 17.03           C  
ATOM   3318  CD  LYS A 454      47.780  36.925  34.376  1.00 16.07           C  
ATOM   3319  CE  LYS A 454      48.914  36.634  35.355  1.00 16.43           C  
ATOM   3320  NZ  LYS A 454      48.526  36.873  36.774  1.00 15.12           N  
ATOM   3321  N   ILE A 455      44.720  36.338  29.954  1.00 12.89           N  
ATOM   3322  CA  ILE A 455      43.738  36.845  28.997  1.00 12.96           C  
ATOM   3323  C   ILE A 455      42.370  36.185  29.177  1.00 13.40           C  
ATOM   3324  O   ILE A 455      41.339  36.856  29.155  1.00 13.09           O  
ATOM   3325  CB  ILE A 455      44.206  36.634  27.534  1.00 12.31           C  
ATOM   3326  CG1 ILE A 455      45.492  37.431  27.269  1.00 14.69           C  
ATOM   3327  CG2 ILE A 455      43.111  37.083  26.564  1.00 11.47           C  
ATOM   3328  CD1 ILE A 455      45.378  38.921  27.561  1.00 14.14           C  
ATOM   3329  N   ALA A 456      42.363  34.868  29.343  1.00 13.68           N  
ATOM   3330  CA  ALA A 456      41.108  34.143  29.523  1.00 13.77           C  
ATOM   3331  C   ALA A 456      40.356  34.655  30.746  1.00 12.99           C  
ATOM   3332  O   ALA A 456      39.130  34.653  30.773  1.00 14.04           O  
ATOM   3333  CB  ALA A 456      41.381  32.640  29.672  1.00 13.45           C  
ATOM   3334  N   PHE A 457      41.095  35.111  31.750  1.00 11.52           N  
ATOM   3335  CA  PHE A 457      40.488  35.595  32.984  1.00 12.47           C  
ATOM   3336  C   PHE A 457      39.806  36.957  32.858  1.00 12.87           C  
ATOM   3337  O   PHE A 457      38.944  37.290  33.669  1.00 14.49           O  
ATOM   3338  CB  PHE A 457      41.548  35.663  34.079  1.00 10.72           C  
ATOM   3339  CG  PHE A 457      41.002  35.979  35.445  1.00 13.51           C  
ATOM   3340  CD1 PHE A 457      40.295  35.019  36.172  1.00 11.90           C  
ATOM   3341  CD2 PHE A 457      41.245  37.216  36.031  1.00 12.70           C  
ATOM   3342  CE1 PHE A 457      39.850  35.286  37.467  1.00 12.84           C  
ATOM   3343  CE2 PHE A 457      40.803  37.492  37.324  1.00 12.47           C  
ATOM   3344  CZ  PHE A 457      40.106  36.524  38.043  1.00 11.48           C  
ATOM   3345  N   ILE A 458      40.190  37.738  31.851  1.00 13.59           N  
ATOM   3346  CA  ILE A 458      39.616  39.064  31.661  1.00 12.89           C  
ATOM   3347  C   ILE A 458      38.083  39.080  31.581  1.00 14.01           C  
ATOM   3348  O   ILE A 458      37.433  39.771  32.361  1.00 13.07           O  
ATOM   3349  CB  ILE A 458      40.200  39.758  30.404  1.00 14.05           C  
ATOM   3350  CG1 ILE A 458      41.677  40.100  30.636  1.00 15.42           C  
ATOM   3351  CG2 ILE A 458      39.399  41.024  30.076  1.00 11.51           C  
ATOM   3352  CD1 ILE A 458      41.931  41.022  31.840  1.00 16.62           C  
ATOM   3353  N   PRO A 459      37.486  38.340  30.630  1.00 11.60           N  
ATOM   3354  CA  PRO A 459      36.022  38.377  30.580  1.00 12.27           C  
ATOM   3355  C   PRO A 459      35.339  37.767  31.802  1.00 11.71           C  
ATOM   3356  O   PRO A 459      34.267  38.218  32.202  1.00 11.51           O  
ATOM   3357  CB  PRO A 459      35.694  37.643  29.276  1.00 12.12           C  
ATOM   3358  CG  PRO A 459      36.876  36.749  29.062  1.00 14.13           C  
ATOM   3359  CD  PRO A 459      38.036  37.616  29.470  1.00 12.38           C  
ATOM   3360  N   PHE A 460      35.950  36.747  32.401  1.00 10.88           N  
ATOM   3361  CA  PHE A 460      35.346  36.126  33.581  1.00 10.74           C  
ATOM   3362  C   PHE A 460      35.337  37.110  34.745  1.00 10.49           C  
ATOM   3363  O   PHE A 460      34.308  37.310  35.390  1.00 11.46           O  
ATOM   3364  CB  PHE A 460      36.113  34.871  34.017  1.00  9.32           C  
ATOM   3365  CG  PHE A 460      35.556  34.230  35.269  1.00  9.41           C  
ATOM   3366  CD1 PHE A 460      34.443  33.396  35.206  1.00 10.06           C  
ATOM   3367  CD2 PHE A 460      36.121  34.492  36.511  1.00  9.76           C  
ATOM   3368  CE1 PHE A 460      33.901  32.834  36.365  1.00 12.14           C  
ATOM   3369  CE2 PHE A 460      35.589  33.937  37.679  1.00 11.37           C  
ATOM   3370  CZ  PHE A 460      34.476  33.104  37.606  1.00 11.49           C  
ATOM   3371  N   SER A 461      36.482  37.732  35.005  1.00 10.88           N  
ATOM   3372  CA  SER A 461      36.584  38.673  36.117  1.00 12.32           C  
ATOM   3373  C   SER A 461      35.679  39.888  35.940  1.00 13.79           C  
ATOM   3374  O   SER A 461      35.297  40.533  36.919  1.00 15.69           O  
ATOM   3375  CB  SER A 461      38.031  39.125  36.308  1.00 11.29           C  
ATOM   3376  OG  SER A 461      38.510  39.836  35.181  1.00 11.99           O  
ATOM   3377  N   TYR A 462      35.340  40.190  34.693  1.00 12.01           N  
ATOM   3378  CA  TYR A 462      34.468  41.320  34.374  1.00 12.81           C  
ATOM   3379  C   TYR A 462      33.010  40.948  34.621  1.00 13.40           C  
ATOM   3380  O   TYR A 462      32.227  41.727  35.162  1.00 13.85           O  
ATOM   3381  CB  TYR A 462      34.633  41.700  32.897  1.00 14.65           C  
ATOM   3382  CG  TYR A 462      33.937  42.983  32.493  1.00 16.68           C  
ATOM   3383  CD1 TYR A 462      34.362  44.214  32.989  1.00 18.71           C  
ATOM   3384  CD2 TYR A 462      32.852  42.966  31.617  1.00 17.79           C  
ATOM   3385  CE1 TYR A 462      33.724  45.398  32.624  1.00 20.68           C  
ATOM   3386  CE2 TYR A 462      32.207  44.147  31.245  1.00 20.59           C  
ATOM   3387  CZ  TYR A 462      32.649  45.357  31.753  1.00 19.58           C  
ATOM   3388  OH  TYR A 462      32.014  46.526  31.400  1.00 18.46           O  
ATOM   3389  N   LEU A 463      32.666  39.733  34.217  1.00 12.33           N  
ATOM   3390  CA  LEU A 463      31.313  39.197  34.311  1.00 13.77           C  
ATOM   3391  C   LEU A 463      30.713  39.016  35.704  1.00 11.84           C  
ATOM   3392  O   LEU A 463      29.542  39.330  35.925  1.00 13.02           O  
ATOM   3393  CB  LEU A 463      31.293  37.864  33.551  1.00 16.44           C  
ATOM   3394  CG  LEU A 463      30.246  36.756  33.614  1.00 23.07           C  
ATOM   3395  CD1 LEU A 463      30.665  35.692  32.600  1.00 23.72           C  
ATOM   3396  CD2 LEU A 463      30.142  36.150  34.994  1.00 18.70           C  
ATOM   3397  N   VAL A 464      31.505  38.516  36.643  1.00 10.62           N  
ATOM   3398  CA  VAL A 464      30.990  38.236  37.979  1.00 11.98           C  
ATOM   3399  C   VAL A 464      30.207  39.360  38.642  1.00 12.05           C  
ATOM   3400  O   VAL A 464      29.064  39.150  39.050  1.00  8.92           O  
ATOM   3401  CB  VAL A 464      32.112  37.768  38.922  1.00 11.36           C  
ATOM   3402  CG1 VAL A 464      31.552  37.498  40.309  1.00  9.21           C  
ATOM   3403  CG2 VAL A 464      32.751  36.504  38.362  1.00 13.56           C  
ATOM   3404  N   ASP A 465      30.802  40.543  38.760  1.00 11.08           N  
ATOM   3405  CA  ASP A 465      30.086  41.641  39.391  1.00 11.99           C  
ATOM   3406  C   ASP A 465      29.120  42.358  38.453  1.00 13.14           C  
ATOM   3407  O   ASP A 465      28.297  43.151  38.906  1.00 12.97           O  
ATOM   3408  CB  ASP A 465      31.056  42.624  40.061  1.00 11.20           C  
ATOM   3409  CG  ASP A 465      31.579  42.096  41.400  1.00 12.07           C  
ATOM   3410  OD1 ASP A 465      31.048  41.069  41.881  1.00 13.72           O  
ATOM   3411  OD2 ASP A 465      32.507  42.695  41.980  1.00 10.70           O  
ATOM   3412  N   GLN A 466      29.207  42.096  37.151  1.00 12.75           N  
ATOM   3413  CA  GLN A 466      28.234  42.711  36.255  1.00 12.19           C  
ATOM   3414  C   GLN A 466      26.926  42.008  36.633  1.00 14.20           C  
ATOM   3415  O   GLN A 466      25.857  42.615  36.640  1.00 12.70           O  
ATOM   3416  CB  GLN A 466      28.561  42.447  34.781  1.00 14.86           C  
ATOM   3417  CG  GLN A 466      29.789  43.181  34.232  1.00 15.25           C  
ATOM   3418  CD  GLN A 466      29.717  44.698  34.383  1.00 19.00           C  
ATOM   3419  OE1 GLN A 466      28.641  45.290  34.356  1.00 17.62           O  
ATOM   3420  NE2 GLN A 466      30.875  45.330  34.526  1.00 19.82           N  
ATOM   3421  N   TRP A 467      27.033  40.720  36.964  1.00 12.15           N  
ATOM   3422  CA  TRP A 467      25.876  39.927  37.371  1.00 13.21           C  
ATOM   3423  C   TRP A 467      25.388  40.363  38.757  1.00 12.74           C  
ATOM   3424  O   TRP A 467      24.202  40.609  38.945  1.00 12.76           O  
ATOM   3425  CB  TRP A 467      26.230  38.435  37.414  1.00 12.05           C  
ATOM   3426  CG  TRP A 467      25.081  37.551  37.820  1.00 12.38           C  
ATOM   3427  CD1 TRP A 467      24.068  37.091  37.018  1.00 13.82           C  
ATOM   3428  CD2 TRP A 467      24.828  37.025  39.124  1.00 11.96           C  
ATOM   3429  NE1 TRP A 467      23.204  36.309  37.747  1.00 13.23           N  
ATOM   3430  CE2 TRP A 467      23.647  36.251  39.043  1.00 14.37           C  
ATOM   3431  CE3 TRP A 467      25.487  37.129  40.357  1.00 12.53           C  
ATOM   3432  CZ2 TRP A 467      23.111  35.584  40.150  1.00 12.76           C  
ATOM   3433  CZ3 TRP A 467      24.953  36.463  41.458  1.00 14.42           C  
ATOM   3434  CH2 TRP A 467      23.777  35.702  41.345  1.00 12.98           C  
ATOM   3435  N   ARG A 468      26.297  40.458  39.726  1.00 14.02           N  
ATOM   3436  CA  ARG A 468      25.907  40.862  41.080  1.00 14.05           C  
ATOM   3437  C   ARG A 468      25.362  42.289  41.177  1.00 15.06           C  
ATOM   3438  O   ARG A 468      24.423  42.539  41.936  1.00 13.96           O  
ATOM   3439  CB  ARG A 468      27.069  40.693  42.066  1.00 13.99           C  
ATOM   3440  CG  ARG A 468      27.111  39.317  42.732  1.00 15.24           C  
ATOM   3441  CD  ARG A 468      28.018  39.283  43.967  1.00 14.11           C  
ATOM   3442  NE  ARG A 468      29.427  39.442  43.618  1.00 12.25           N  
ATOM   3443  CZ  ARG A 468      30.435  38.959  44.333  1.00 14.41           C  
ATOM   3444  NH1 ARG A 468      30.195  38.280  45.453  1.00 13.25           N  
ATOM   3445  NH2 ARG A 468      31.686  39.137  43.917  1.00 12.95           N  
ATOM   3446  N   TRP A 469      25.942  43.223  40.427  1.00 12.32           N  
ATOM   3447  CA  TRP A 469      25.454  44.600  40.469  1.00 14.74           C  
ATOM   3448  C   TRP A 469      23.997  44.651  40.015  1.00 15.43           C  
ATOM   3449  O   TRP A 469      23.213  45.457  40.513  1.00 14.95           O  
ATOM   3450  CB  TRP A 469      26.277  45.529  39.561  1.00 11.23           C  
ATOM   3451  CG  TRP A 469      27.692  45.753  39.989  1.00 12.02           C  
ATOM   3452  CD1 TRP A 469      28.233  45.495  41.214  1.00 10.03           C  
ATOM   3453  CD2 TRP A 469      28.757  46.277  39.181  1.00 11.01           C  
ATOM   3454  NE1 TRP A 469      29.567  45.819  41.218  1.00 10.74           N  
ATOM   3455  CE2 TRP A 469      29.916  46.302  39.984  1.00 10.87           C  
ATOM   3456  CE3 TRP A 469      28.841  46.728  37.855  1.00 13.39           C  
ATOM   3457  CZ2 TRP A 469      31.153  46.759  39.508  1.00  8.74           C  
ATOM   3458  CZ3 TRP A 469      30.073  47.186  37.378  1.00 11.68           C  
ATOM   3459  CH2 TRP A 469      31.210  47.195  38.205  1.00 11.27           C  
ATOM   3460  N   ARG A 470      23.643  43.799  39.056  1.00 15.05           N  
ATOM   3461  CA  ARG A 470      22.275  43.769  38.551  1.00 15.13           C  
ATOM   3462  C   ARG A 470      21.346  43.006  39.493  1.00 15.12           C  
ATOM   3463  O   ARG A 470      20.129  43.222  39.497  1.00 13.20           O  
ATOM   3464  CB  ARG A 470      22.249  43.170  37.142  1.00 17.81           C  
ATOM   3465  CG  ARG A 470      22.833  44.107  36.088  1.00 22.48           C  
ATOM   3466  CD  ARG A 470      22.988  43.403  34.751  1.00 29.90           C  
ATOM   3467  NE  ARG A 470      21.713  42.901  34.245  1.00 35.03           N  
ATOM   3468  CZ  ARG A 470      21.596  41.864  33.422  1.00 37.06           C  
ATOM   3469  NH1 ARG A 470      22.678  41.213  33.012  1.00 37.13           N  
ATOM   3470  NH2 ARG A 470      20.397  41.481  33.004  1.00 36.72           N  
ATOM   3471  N   VAL A 471      21.917  42.102  40.284  1.00 13.23           N  
ATOM   3472  CA  VAL A 471      21.126  41.367  41.262  1.00 14.21           C  
ATOM   3473  C   VAL A 471      20.820  42.369  42.373  1.00 14.19           C  
ATOM   3474  O   VAL A 471      19.678  42.513  42.813  1.00 14.12           O  
ATOM   3475  CB  VAL A 471      21.910  40.175  41.854  1.00 10.98           C  
ATOM   3476  CG1 VAL A 471      21.207  39.660  43.102  1.00 11.32           C  
ATOM   3477  CG2 VAL A 471      22.003  39.052  40.816  1.00 14.99           C  
ATOM   3478  N   PHE A 472      21.862  43.072  42.802  1.00 14.50           N  
ATOM   3479  CA  PHE A 472      21.749  44.070  43.856  1.00 15.39           C  
ATOM   3480  C   PHE A 472      20.802  45.221  43.509  1.00 15.02           C  
ATOM   3481  O   PHE A 472      20.022  45.650  44.359  1.00 14.79           O  
ATOM   3482  CB  PHE A 472      23.139  44.614  44.197  1.00 14.83           C  
ATOM   3483  CG  PHE A 472      23.999  43.647  44.971  1.00 14.46           C  
ATOM   3484  CD1 PHE A 472      25.383  43.722  44.901  1.00 14.93           C  
ATOM   3485  CD2 PHE A 472      23.422  42.677  45.793  1.00 16.22           C  
ATOM   3486  CE1 PHE A 472      26.186  42.848  45.640  1.00 14.36           C  
ATOM   3487  CE2 PHE A 472      24.218  41.797  46.537  1.00 12.05           C  
ATOM   3488  CZ  PHE A 472      25.598  41.886  46.459  1.00 15.10           C  
ATOM   3489  N   ASP A 473      20.853  45.722  42.274  1.00 14.97           N  
ATOM   3490  CA  ASP A 473      19.963  46.820  41.916  1.00 15.11           C  
ATOM   3491  C   ASP A 473      18.565  46.356  41.516  1.00 16.58           C  
ATOM   3492  O   ASP A 473      17.756  47.153  41.044  1.00 17.20           O  
ATOM   3493  CB  ASP A 473      20.575  47.716  40.819  1.00 15.57           C  
ATOM   3494  CG  ASP A 473      20.520  47.100  39.426  1.00 16.33           C  
ATOM   3495  OD1 ASP A 473      19.860  46.057  39.220  1.00 17.34           O  
ATOM   3496  OD2 ASP A 473      21.144  47.689  38.522  1.00 17.52           O  
ATOM   3497  N   GLY A 474      18.287  45.067  41.708  1.00 16.74           N  
ATOM   3498  CA  GLY A 474      16.971  44.527  41.400  1.00 17.30           C  
ATOM   3499  C   GLY A 474      16.636  44.167  39.961  1.00 17.93           C  
ATOM   3500  O   GLY A 474      15.520  43.732  39.693  1.00 18.99           O  
ATOM   3501  N   SER A 475      17.578  44.341  39.039  1.00 17.16           N  
ATOM   3502  CA  SER A 475      17.350  44.013  37.630  1.00 18.82           C  
ATOM   3503  C   SER A 475      17.185  42.509  37.401  1.00 18.71           C  
ATOM   3504  O   SER A 475      16.500  42.089  36.470  1.00 19.68           O  
ATOM   3505  CB  SER A 475      18.514  44.514  36.771  1.00 19.99           C  
ATOM   3506  OG  SER A 475      18.605  45.920  36.805  1.00 25.35           O  
ATOM   3507  N   ILE A 476      17.837  41.709  38.241  1.00 17.20           N  
ATOM   3508  CA  ILE A 476      17.767  40.253  38.147  1.00 17.19           C  
ATOM   3509  C   ILE A 476      17.123  39.695  39.420  1.00 17.07           C  
ATOM   3510  O   ILE A 476      17.689  39.807  40.509  1.00 16.98           O  
ATOM   3511  CB  ILE A 476      19.184  39.630  38.004  1.00 16.86           C  
ATOM   3512  CG1 ILE A 476      19.890  40.193  36.767  1.00 17.34           C  
ATOM   3513  CG2 ILE A 476      19.076  38.112  37.912  1.00 15.71           C  
ATOM   3514  CD1 ILE A 476      21.357  39.746  36.640  1.00 15.06           C  
ATOM   3515  N   THR A 477      15.940  39.105  39.281  1.00 17.01           N  
ATOM   3516  CA  THR A 477      15.227  38.531  40.421  1.00 18.33           C  
ATOM   3517  C   THR A 477      15.671  37.088  40.581  1.00 18.12           C  
ATOM   3518  O   THR A 477      16.318  36.540  39.689  1.00 17.12           O  
ATOM   3519  CB  THR A 477      13.710  38.551  40.196  1.00 18.44           C  
ATOM   3520  OG1 THR A 477      13.365  37.586  39.191  1.00 20.70           O  
ATOM   3521  CG2 THR A 477      13.263  39.931  39.734  1.00 20.95           C  
ATOM   3522  N   LYS A 478      15.312  36.469  41.703  1.00 20.57           N  
ATOM   3523  CA  LYS A 478      15.702  35.087  41.961  1.00 23.09           C  
ATOM   3524  C   LYS A 478      15.142  34.148  40.909  1.00 24.36           C  
ATOM   3525  O   LYS A 478      15.601  33.018  40.769  1.00 25.76           O  
ATOM   3526  CB  LYS A 478      15.240  34.637  43.352  1.00 24.96           C  
ATOM   3527  CG  LYS A 478      13.763  34.281  43.465  1.00 29.41           C  
ATOM   3528  CD  LYS A 478      13.455  33.746  44.859  1.00 32.03           C  
ATOM   3529  CE  LYS A 478      12.017  33.278  44.988  1.00 33.33           C  
ATOM   3530  NZ  LYS A 478      11.724  32.824  46.378  1.00 34.91           N  
ATOM   3531  N   GLU A 479      14.146  34.619  40.169  1.00 25.33           N  
ATOM   3532  CA  GLU A 479      13.534  33.819  39.116  1.00 26.94           C  
ATOM   3533  C   GLU A 479      14.489  33.726  37.927  1.00 26.01           C  
ATOM   3534  O   GLU A 479      14.458  32.758  37.163  1.00 25.45           O  
ATOM   3535  CB  GLU A 479      12.240  34.481  38.649  1.00 31.14           C  
ATOM   3536  CG  GLU A 479      11.420  35.078  39.776  1.00 39.75           C  
ATOM   3537  CD  GLU A 479      10.187  34.265  40.094  1.00 42.36           C  
ATOM   3538  OE1 GLU A 479       9.312  34.169  39.212  1.00 46.25           O  
ATOM   3539  OE2 GLU A 479      10.094  33.725  41.217  1.00 45.33           O  
ATOM   3540  N   ASN A 480      15.343  34.736  37.780  1.00 22.90           N  
ATOM   3541  CA  ASN A 480      16.271  34.785  36.657  1.00 21.40           C  
ATOM   3542  C   ASN A 480      17.759  34.747  37.000  1.00 18.64           C  
ATOM   3543  O   ASN A 480      18.593  34.993  36.131  1.00 16.50           O  
ATOM   3544  CB  ASN A 480      15.973  36.028  35.811  1.00 23.82           C  
ATOM   3545  CG  ASN A 480      14.538  36.057  35.315  1.00 29.85           C  
ATOM   3546  OD1 ASN A 480      14.086  35.126  34.646  1.00 30.15           O  
ATOM   3547  ND2 ASN A 480      13.811  37.122  35.647  1.00 28.53           N  
ATOM   3548  N   TYR A 481      18.089  34.441  38.251  1.00 15.85           N  
ATOM   3549  CA  TYR A 481      19.487  34.360  38.681  1.00 15.32           C  
ATOM   3550  C   TYR A 481      20.378  33.613  37.688  1.00 16.40           C  
ATOM   3551  O   TYR A 481      21.318  34.171  37.108  1.00 13.43           O  
ATOM   3552  CB  TYR A 481      19.604  33.604  40.007  1.00 14.72           C  
ATOM   3553  CG  TYR A 481      19.244  34.359  41.266  1.00 14.45           C  
ATOM   3554  CD1 TYR A 481      19.008  33.667  42.450  1.00 14.67           C  
ATOM   3555  CD2 TYR A 481      19.194  35.753  41.295  1.00 14.34           C  
ATOM   3556  CE1 TYR A 481      18.736  34.335  43.637  1.00 16.30           C  
ATOM   3557  CE2 TYR A 481      18.920  36.435  42.484  1.00 17.16           C  
ATOM   3558  CZ  TYR A 481      18.695  35.714  43.648  1.00 18.10           C  
ATOM   3559  OH  TYR A 481      18.451  36.361  44.837  1.00 21.96           O  
ATOM   3560  N   ASN A 482      20.077  32.328  37.521  1.00 15.11           N  
ATOM   3561  CA  ASN A 482      20.877  31.461  36.673  1.00 14.44           C  
ATOM   3562  C   ASN A 482      20.840  31.778  35.198  1.00 14.91           C  
ATOM   3563  O   ASN A 482      21.865  31.701  34.517  1.00 12.27           O  
ATOM   3564  CB  ASN A 482      20.478  29.999  36.894  1.00 14.83           C  
ATOM   3565  CG  ASN A 482      21.677  29.073  36.872  1.00 13.79           C  
ATOM   3566  OD1 ASN A 482      22.620  29.261  37.634  1.00 15.96           O  
ATOM   3567  ND2 ASN A 482      21.652  28.078  35.993  1.00 13.24           N  
ATOM   3568  N   GLN A 483      19.664  32.133  34.697  1.00 13.28           N  
ATOM   3569  CA  GLN A 483      19.539  32.441  33.285  1.00 16.41           C  
ATOM   3570  C   GLN A 483      20.378  33.660  32.900  1.00 16.35           C  
ATOM   3571  O   GLN A 483      21.004  33.682  31.830  1.00 14.47           O  
ATOM   3572  CB  GLN A 483      18.062  32.642  32.924  1.00 18.43           C  
ATOM   3573  CG  GLN A 483      17.219  31.363  33.087  1.00 25.86           C  
ATOM   3574  CD  GLN A 483      16.628  31.163  34.492  1.00 27.97           C  
ATOM   3575  OE1 GLN A 483      17.184  31.606  35.501  1.00 22.77           O  
ATOM   3576  NE2 GLN A 483      15.493  30.468  34.551  1.00 32.36           N  
ATOM   3577  N   GLU A 484      20.406  34.668  33.769  1.00 14.45           N  
ATOM   3578  CA  GLU A 484      21.188  35.872  33.486  1.00 15.60           C  
ATOM   3579  C   GLU A 484      22.680  35.591  33.656  1.00 13.08           C  
ATOM   3580  O   GLU A 484      23.512  36.209  32.992  1.00 14.72           O  
ATOM   3581  CB  GLU A 484      20.762  37.023  34.398  1.00 17.63           C  
ATOM   3582  CG  GLU A 484      19.361  37.553  34.107  1.00 23.50           C  
ATOM   3583  CD  GLU A 484      19.200  37.998  32.663  1.00 29.39           C  
ATOM   3584  OE1 GLU A 484      20.051  38.776  32.177  1.00 29.30           O  
ATOM   3585  OE2 GLU A 484      18.220  37.570  32.016  1.00 31.22           O  
ATOM   3586  N   TRP A 485      23.018  34.671  34.555  1.00 11.64           N  
ATOM   3587  CA  TRP A 485      24.423  34.303  34.752  1.00 12.26           C  
ATOM   3588  C   TRP A 485      24.945  33.701  33.450  1.00 12.53           C  
ATOM   3589  O   TRP A 485      26.014  34.081  32.967  1.00 15.24           O  
ATOM   3590  CB  TRP A 485      24.559  33.298  35.901  1.00 10.60           C  
ATOM   3591  CG  TRP A 485      25.924  32.648  36.038  1.00 13.26           C  
ATOM   3592  CD1 TRP A 485      26.281  31.402  35.612  1.00 15.30           C  
ATOM   3593  CD2 TRP A 485      27.086  33.201  36.671  1.00 13.09           C  
ATOM   3594  NE1 TRP A 485      27.593  31.140  35.943  1.00 14.97           N  
ATOM   3595  CE2 TRP A 485      28.110  32.228  36.593  1.00 14.57           C  
ATOM   3596  CE3 TRP A 485      27.362  34.423  37.300  1.00 14.40           C  
ATOM   3597  CZ2 TRP A 485      29.392  32.438  37.119  1.00 14.78           C  
ATOM   3598  CZ3 TRP A 485      28.640  34.632  37.827  1.00 15.38           C  
ATOM   3599  CH2 TRP A 485      29.636  33.642  37.731  1.00 16.29           C  
ATOM   3600  N   TRP A 486      24.186  32.778  32.864  1.00 11.64           N  
ATOM   3601  CA  TRP A 486      24.631  32.169  31.618  1.00 12.88           C  
ATOM   3602  C   TRP A 486      24.571  33.092  30.402  1.00 13.68           C  
ATOM   3603  O   TRP A 486      25.360  32.937  29.473  1.00 13.23           O  
ATOM   3604  CB  TRP A 486      23.892  30.850  31.371  1.00 11.74           C  
ATOM   3605  CG  TRP A 486      24.494  29.780  32.238  1.00 11.07           C  
ATOM   3606  CD1 TRP A 486      24.028  29.338  33.442  1.00 10.52           C  
ATOM   3607  CD2 TRP A 486      25.768  29.150  32.047  1.00 10.34           C  
ATOM   3608  NE1 TRP A 486      24.937  28.480  34.019  1.00 12.71           N  
ATOM   3609  CE2 TRP A 486      26.014  28.349  33.182  1.00 11.07           C  
ATOM   3610  CE3 TRP A 486      26.730  29.193  31.028  1.00 13.21           C  
ATOM   3611  CZ2 TRP A 486      27.185  27.596  33.328  1.00 11.38           C  
ATOM   3612  CZ3 TRP A 486      27.899  28.441  31.174  1.00 13.92           C  
ATOM   3613  CH2 TRP A 486      28.112  27.657  32.315  1.00 11.19           C  
ATOM   3614  N   SER A 487      23.662  34.063  30.403  1.00 13.61           N  
ATOM   3615  CA  SER A 487      23.606  35.001  29.289  1.00 13.77           C  
ATOM   3616  C   SER A 487      24.908  35.812  29.306  1.00 13.80           C  
ATOM   3617  O   SER A 487      25.438  36.174  28.261  1.00 11.73           O  
ATOM   3618  CB  SER A 487      22.406  35.938  29.429  1.00 16.27           C  
ATOM   3619  OG  SER A 487      21.198  35.215  29.273  1.00 25.55           O  
ATOM   3620  N   LEU A 488      25.420  36.085  30.503  1.00 12.48           N  
ATOM   3621  CA  LEU A 488      26.664  36.835  30.642  1.00 13.86           C  
ATOM   3622  C   LEU A 488      27.854  35.936  30.315  1.00 14.53           C  
ATOM   3623  O   LEU A 488      28.833  36.374  29.701  1.00 13.21           O  
ATOM   3624  CB  LEU A 488      26.792  37.386  32.065  1.00 13.18           C  
ATOM   3625  CG  LEU A 488      25.820  38.521  32.408  1.00 17.32           C  
ATOM   3626  CD1 LEU A 488      25.996  38.936  33.869  1.00 15.81           C  
ATOM   3627  CD2 LEU A 488      26.082  39.706  31.497  1.00 18.32           C  
ATOM   3628  N   ARG A 489      27.763  34.680  30.740  1.00 12.53           N  
ATOM   3629  CA  ARG A 489      28.811  33.698  30.483  1.00 14.43           C  
ATOM   3630  C   ARG A 489      29.018  33.581  28.975  1.00 15.32           C  
ATOM   3631  O   ARG A 489      30.154  33.479  28.499  1.00 14.29           O  
ATOM   3632  CB  ARG A 489      28.415  32.342  31.080  1.00 12.24           C  
ATOM   3633  CG  ARG A 489      28.505  32.295  32.602  1.00 10.71           C  
ATOM   3634  CD  ARG A 489      29.933  32.016  33.047  1.00 11.25           C  
ATOM   3635  NE  ARG A 489      30.126  30.601  33.360  1.00 11.37           N  
ATOM   3636  CZ  ARG A 489      31.309  30.021  33.547  1.00 14.25           C  
ATOM   3637  NH1 ARG A 489      31.364  28.728  33.843  1.00 11.46           N  
ATOM   3638  NH2 ARG A 489      32.435  30.722  33.418  1.00  8.82           N  
ATOM   3639  N   LEU A 490      27.914  33.602  28.232  1.00 14.48           N  
ATOM   3640  CA  LEU A 490      27.964  33.534  26.775  1.00 15.03           C  
ATOM   3641  C   LEU A 490      28.463  34.862  26.195  1.00 15.14           C  
ATOM   3642  O   LEU A 490      29.426  34.901  25.433  1.00 16.02           O  
ATOM   3643  CB  LEU A 490      26.570  33.237  26.197  1.00 14.34           C  
ATOM   3644  CG  LEU A 490      26.464  33.320  24.663  1.00 17.99           C  
ATOM   3645  CD1 LEU A 490      27.277  32.193  24.036  1.00 14.70           C  
ATOM   3646  CD2 LEU A 490      25.003  33.225  24.221  1.00 19.69           C  
ATOM   3647  N   LYS A 491      27.800  35.952  26.564  1.00 15.84           N  
ATOM   3648  CA  LYS A 491      28.156  37.273  26.053  1.00 16.80           C  
ATOM   3649  C   LYS A 491      29.618  37.664  26.245  1.00 15.29           C  
ATOM   3650  O   LYS A 491      30.254  38.159  25.322  1.00 15.94           O  
ATOM   3651  CB  LYS A 491      27.257  38.340  26.691  1.00 20.30           C  
ATOM   3652  CG  LYS A 491      27.614  39.767  26.290  1.00 25.17           C  
ATOM   3653  CD  LYS A 491      26.641  40.777  26.885  1.00 25.79           C  
ATOM   3654  CE  LYS A 491      27.035  42.197  26.505  1.00 27.00           C  
ATOM   3655  NZ  LYS A 491      26.061  43.202  27.014  1.00 29.07           N  
ATOM   3656  N   TYR A 492      30.159  37.446  27.437  1.00 14.11           N  
ATOM   3657  CA  TYR A 492      31.545  37.823  27.689  1.00 14.39           C  
ATOM   3658  C   TYR A 492      32.605  36.752  27.437  1.00 14.99           C  
ATOM   3659  O   TYR A 492      33.610  37.023  26.781  1.00 12.52           O  
ATOM   3660  CB  TYR A 492      31.672  38.370  29.115  1.00 16.01           C  
ATOM   3661  CG  TYR A 492      30.969  39.699  29.274  1.00 19.66           C  
ATOM   3662  CD1 TYR A 492      29.842  39.833  30.085  1.00 22.54           C  
ATOM   3663  CD2 TYR A 492      31.400  40.816  28.560  1.00 21.80           C  
ATOM   3664  CE1 TYR A 492      29.159  41.054  30.173  1.00 24.34           C  
ATOM   3665  CE2 TYR A 492      30.730  42.029  28.641  1.00 24.56           C  
ATOM   3666  CZ  TYR A 492      29.611  42.142  29.444  1.00 24.26           C  
ATOM   3667  OH  TYR A 492      28.946  43.346  29.493  1.00 30.82           O  
ATOM   3668  N   GLN A 493      32.389  35.537  27.935  1.00 13.32           N  
ATOM   3669  CA  GLN A 493      33.382  34.470  27.751  1.00 12.95           C  
ATOM   3670  C   GLN A 493      33.162  33.584  26.534  1.00 11.74           C  
ATOM   3671  O   GLN A 493      34.059  32.845  26.137  1.00 12.11           O  
ATOM   3672  CB  GLN A 493      33.425  33.566  28.980  1.00 11.02           C  
ATOM   3673  CG  GLN A 493      33.970  34.205  30.230  1.00 12.37           C  
ATOM   3674  CD  GLN A 493      34.033  33.207  31.356  1.00 10.81           C  
ATOM   3675  OE1 GLN A 493      33.043  32.974  32.049  1.00 12.38           O  
ATOM   3676  NE2 GLN A 493      35.191  32.577  31.520  1.00 10.48           N  
ATOM   3677  N   GLY A 494      31.973  33.637  25.949  1.00 12.72           N  
ATOM   3678  CA  GLY A 494      31.709  32.785  24.804  1.00 13.19           C  
ATOM   3679  C   GLY A 494      31.674  31.328  25.237  1.00 13.82           C  
ATOM   3680  O   GLY A 494      32.180  30.444  24.540  1.00 12.99           O  
ATOM   3681  N   LEU A 495      31.087  31.074  26.403  1.00 12.01           N  
ATOM   3682  CA  LEU A 495      30.975  29.710  26.913  1.00 11.37           C  
ATOM   3683  C   LEU A 495      29.515  29.289  26.989  1.00 14.13           C  
ATOM   3684  O   LEU A 495      28.617  30.134  27.059  1.00 14.75           O  
ATOM   3685  CB  LEU A 495      31.581  29.598  28.317  1.00 11.79           C  
ATOM   3686  CG  LEU A 495      33.052  29.983  28.498  1.00 11.39           C  
ATOM   3687  CD1 LEU A 495      33.439  29.852  29.978  1.00 12.76           C  
ATOM   3688  CD2 LEU A 495      33.926  29.084  27.625  1.00  9.67           C  
ATOM   3689  N   CYS A 496      29.284  27.978  26.963  1.00 13.45           N  
ATOM   3690  CA  CYS A 496      27.939  27.429  27.078  1.00 15.05           C  
ATOM   3691  C   CYS A 496      27.978  26.287  28.091  1.00 15.94           C  
ATOM   3692  O   CYS A 496      29.019  25.653  28.289  1.00 15.05           O  
ATOM   3693  CB  CYS A 496      27.424  26.919  25.722  1.00 15.05           C  
ATOM   3694  SG  CYS A 496      28.474  25.702  24.876  1.00 19.74           S  
ATOM   3695  N   PRO A 497      26.854  26.034  28.773  1.00 15.16           N  
ATOM   3696  CA  PRO A 497      26.816  24.952  29.761  1.00 15.93           C  
ATOM   3697  C   PRO A 497      26.706  23.606  29.040  1.00 16.28           C  
ATOM   3698  O   PRO A 497      25.832  23.426  28.195  1.00 16.69           O  
ATOM   3699  CB  PRO A 497      25.579  25.291  30.588  1.00 15.52           C  
ATOM   3700  CG  PRO A 497      24.653  25.904  29.560  1.00 17.39           C  
ATOM   3701  CD  PRO A 497      25.587  26.794  28.757  1.00 16.64           C  
ATOM   3702  N   PRO A 498      27.602  22.650  29.359  1.00 15.89           N  
ATOM   3703  CA  PRO A 498      27.595  21.325  28.728  1.00 16.53           C  
ATOM   3704  C   PRO A 498      26.299  20.564  28.979  1.00 16.93           C  
ATOM   3705  O   PRO A 498      25.929  19.675  28.214  1.00 19.21           O  
ATOM   3706  CB  PRO A 498      28.813  20.646  29.347  1.00 16.86           C  
ATOM   3707  CG  PRO A 498      28.864  21.250  30.719  1.00 17.60           C  
ATOM   3708  CD  PRO A 498      28.620  22.713  30.423  1.00 17.16           C  
ATOM   3709  N   VAL A 499      25.620  20.919  30.064  1.00 15.31           N  
ATOM   3710  CA  VAL A 499      24.345  20.309  30.421  1.00 18.95           C  
ATOM   3711  C   VAL A 499      23.331  21.439  30.591  1.00 18.93           C  
ATOM   3712  O   VAL A 499      23.586  22.402  31.320  1.00 17.96           O  
ATOM   3713  CB  VAL A 499      24.447  19.514  31.747  1.00 18.21           C  
ATOM   3714  CG1 VAL A 499      23.057  19.197  32.277  1.00 20.68           C  
ATOM   3715  CG2 VAL A 499      25.221  18.216  31.516  1.00 20.27           C  
ATOM   3716  N   PRO A 500      22.179  21.351  29.908  1.00 19.85           N  
ATOM   3717  CA  PRO A 500      21.186  22.422  30.055  1.00 20.04           C  
ATOM   3718  C   PRO A 500      20.806  22.624  31.519  1.00 20.47           C  
ATOM   3719  O   PRO A 500      20.590  21.660  32.258  1.00 19.22           O  
ATOM   3720  CB  PRO A 500      20.019  21.940  29.186  1.00 23.88           C  
ATOM   3721  CG  PRO A 500      20.207  20.436  29.134  1.00 24.49           C  
ATOM   3722  CD  PRO A 500      21.701  20.311  28.982  1.00 21.08           C  
ATOM   3723  N   ARG A 501      20.748  23.880  31.946  1.00 17.94           N  
ATOM   3724  CA  ARG A 501      20.408  24.173  33.331  1.00 19.58           C  
ATOM   3725  C   ARG A 501      18.903  24.018  33.538  1.00 20.97           C  
ATOM   3726  O   ARG A 501      18.125  24.148  32.593  1.00 21.91           O  
ATOM   3727  CB  ARG A 501      20.850  25.597  33.698  1.00 17.12           C  
ATOM   3728  CG  ARG A 501      22.203  26.006  33.109  1.00 17.15           C  
ATOM   3729  CD  ARG A 501      23.261  24.916  33.259  1.00 14.33           C  
ATOM   3730  NE  ARG A 501      23.625  24.670  34.650  1.00 16.72           N  
ATOM   3731  CZ  ARG A 501      23.756  23.457  35.175  1.00 18.54           C  
ATOM   3732  NH1 ARG A 501      23.548  22.382  34.418  1.00 18.00           N  
ATOM   3733  NH2 ARG A 501      24.100  23.316  36.447  1.00 16.39           N  
ATOM   3734  N   THR A 502      18.502  23.735  34.773  1.00 21.56           N  
ATOM   3735  CA  THR A 502      17.089  23.560  35.099  1.00 23.91           C  
ATOM   3736  C   THR A 502      16.734  24.342  36.354  1.00 24.49           C  
ATOM   3737  O   THR A 502      17.622  24.792  37.088  1.00 22.75           O  
ATOM   3738  CB  THR A 502      16.743  22.075  35.337  1.00 24.39           C  
ATOM   3739  OG1 THR A 502      17.593  21.542  36.363  1.00 26.32           O  
ATOM   3740  CG2 THR A 502      16.930  21.273  34.054  1.00 26.00           C  
ATOM   3741  N   GLN A 503      15.436  24.494  36.601  1.00 25.56           N  
ATOM   3742  CA  GLN A 503      14.963  25.227  37.769  1.00 27.46           C  
ATOM   3743  C   GLN A 503      15.589  24.628  39.023  1.00 26.85           C  
ATOM   3744  O   GLN A 503      15.630  23.410  39.195  1.00 28.91           O  
ATOM   3745  CB  GLN A 503      13.429  25.173  37.845  1.00 29.98           C  
ATOM   3746  CG  GLN A 503      12.834  26.077  38.917  1.00 34.85           C  
ATOM   3747  CD  GLN A 503      12.498  25.332  40.196  1.00 38.40           C  
ATOM   3748  OE1 GLN A 503      13.144  24.341  40.542  1.00 39.55           O  
ATOM   3749  NE2 GLN A 503      11.487  25.815  40.914  1.00 40.66           N  
ATOM   3750  N   GLY A 504      16.088  25.486  39.900  1.00 26.04           N  
ATOM   3751  CA  GLY A 504      16.722  24.988  41.103  1.00 22.99           C  
ATOM   3752  C   GLY A 504      18.230  25.145  41.032  1.00 20.56           C  
ATOM   3753  O   GLY A 504      18.893  25.172  42.062  1.00 21.12           O  
ATOM   3754  N   ASP A 505      18.783  25.236  39.824  1.00 19.34           N  
ATOM   3755  CA  ASP A 505      20.229  25.412  39.690  1.00 18.42           C  
ATOM   3756  C   ASP A 505      20.617  26.845  40.039  1.00 17.25           C  
ATOM   3757  O   ASP A 505      19.893  27.786  39.722  1.00 17.90           O  
ATOM   3758  CB  ASP A 505      20.710  25.126  38.262  1.00 18.23           C  
ATOM   3759  CG  ASP A 505      20.693  23.647  37.917  1.00 17.73           C  
ATOM   3760  OD1 ASP A 505      20.885  22.814  38.829  1.00 16.38           O  
ATOM   3761  OD2 ASP A 505      20.509  23.326  36.726  1.00 18.51           O  
ATOM   3762  N   PHE A 506      21.761  26.996  40.694  1.00 15.41           N  
ATOM   3763  CA  PHE A 506      22.285  28.309  41.069  1.00 15.10           C  
ATOM   3764  C   PHE A 506      23.798  28.188  40.929  1.00 14.34           C  
ATOM   3765  O   PHE A 506      24.534  28.107  41.910  1.00 11.59           O  
ATOM   3766  CB  PHE A 506      21.914  28.654  42.511  1.00 13.69           C  
ATOM   3767  CG  PHE A 506      22.344  30.031  42.934  1.00 14.67           C  
ATOM   3768  CD1 PHE A 506      21.970  31.150  42.190  1.00 14.51           C  
ATOM   3769  CD2 PHE A 506      23.127  30.211  44.073  1.00 14.42           C  
ATOM   3770  CE1 PHE A 506      22.372  32.434  42.576  1.00 16.76           C  
ATOM   3771  CE2 PHE A 506      23.535  31.490  44.469  1.00 16.13           C  
ATOM   3772  CZ  PHE A 506      23.155  32.602  43.717  1.00 16.55           C  
ATOM   3773  N   ASP A 507      24.246  28.160  39.683  1.00 13.08           N  
ATOM   3774  CA  ASP A 507      25.656  28.013  39.380  1.00 12.91           C  
ATOM   3775  C   ASP A 507      26.546  29.093  40.005  1.00 13.57           C  
ATOM   3776  O   ASP A 507      27.680  28.814  40.391  1.00 14.25           O  
ATOM   3777  CB  ASP A 507      25.812  27.915  37.858  1.00 14.42           C  
ATOM   3778  CG  ASP A 507      24.984  26.761  37.275  1.00 13.98           C  
ATOM   3779  OD1 ASP A 507      24.869  25.725  37.959  1.00 15.77           O  
ATOM   3780  OD2 ASP A 507      24.456  26.875  36.148  1.00 16.17           O  
ATOM   3781  N   PRO A 508      26.049  30.336  40.125  1.00 12.45           N  
ATOM   3782  CA  PRO A 508      26.903  31.362  40.738  1.00 14.07           C  
ATOM   3783  C   PRO A 508      27.318  30.945  42.149  1.00 14.32           C  
ATOM   3784  O   PRO A 508      28.405  31.290  42.620  1.00 15.96           O  
ATOM   3785  CB  PRO A 508      25.998  32.596  40.760  1.00 13.43           C  
ATOM   3786  CG  PRO A 508      25.203  32.428  39.495  1.00 14.83           C  
ATOM   3787  CD  PRO A 508      24.833  30.944  39.554  1.00 12.63           C  
ATOM   3788  N   GLY A 509      26.443  30.201  42.818  1.00 13.56           N  
ATOM   3789  CA  GLY A 509      26.726  29.759  44.173  1.00 13.06           C  
ATOM   3790  C   GLY A 509      27.880  28.779  44.262  1.00 14.35           C  
ATOM   3791  O   GLY A 509      28.410  28.530  45.350  1.00 14.78           O  
ATOM   3792  N   ALA A 510      28.278  28.233  43.116  1.00 13.27           N  
ATOM   3793  CA  ALA A 510      29.374  27.268  43.057  1.00 13.82           C  
ATOM   3794  C   ALA A 510      30.736  27.948  42.899  1.00 14.23           C  
ATOM   3795  O   ALA A 510      31.755  27.277  42.723  1.00 14.48           O  
ATOM   3796  CB  ALA A 510      29.142  26.282  41.908  1.00 13.95           C  
ATOM   3797  N   LYS A 511      30.744  29.278  42.950  1.00 13.31           N  
ATOM   3798  CA  LYS A 511      31.981  30.051  42.845  1.00 13.43           C  
ATOM   3799  C   LYS A 511      32.195  30.690  44.215  1.00 14.23           C  
ATOM   3800  O   LYS A 511      31.363  31.472  44.678  1.00 13.83           O  
ATOM   3801  CB  LYS A 511      31.854  31.131  41.758  1.00 11.46           C  
ATOM   3802  CG  LYS A 511      33.080  32.052  41.629  1.00 11.83           C  
ATOM   3803  CD  LYS A 511      34.363  31.258  41.356  1.00 11.07           C  
ATOM   3804  CE  LYS A 511      35.594  32.152  41.434  1.00 13.88           C  
ATOM   3805  NZ  LYS A 511      36.866  31.380  41.387  1.00 13.39           N  
ATOM   3806  N   PHE A 512      33.309  30.346  44.857  1.00 14.52           N  
ATOM   3807  CA  PHE A 512      33.640  30.842  46.197  1.00 15.65           C  
ATOM   3808  C   PHE A 512      33.159  32.242  46.577  1.00 16.50           C  
ATOM   3809  O   PHE A 512      32.411  32.411  47.540  1.00 17.35           O  
ATOM   3810  CB  PHE A 512      35.156  30.803  46.422  1.00 16.34           C  
ATOM   3811  CG  PHE A 512      35.581  31.353  47.760  1.00 16.35           C  
ATOM   3812  CD1 PHE A 512      35.489  30.574  48.909  1.00 18.40           C  
ATOM   3813  CD2 PHE A 512      36.047  32.661  47.875  1.00 19.53           C  
ATOM   3814  CE1 PHE A 512      35.858  31.090  50.161  1.00 18.32           C  
ATOM   3815  CE2 PHE A 512      36.418  33.188  49.120  1.00 18.19           C  
ATOM   3816  CZ  PHE A 512      36.323  32.399  50.263  1.00 18.52           C  
ATOM   3817  N   HIS A 513      33.603  33.242  45.822  1.00 13.72           N  
ATOM   3818  CA  HIS A 513      33.284  34.635  46.119  1.00 14.78           C  
ATOM   3819  C   HIS A 513      31.808  35.016  46.213  1.00 14.84           C  
ATOM   3820  O   HIS A 513      31.470  36.034  46.826  1.00 14.80           O  
ATOM   3821  CB  HIS A 513      34.006  35.543  45.116  1.00 13.88           C  
ATOM   3822  CG  HIS A 513      35.484  35.298  45.050  1.00 13.02           C  
ATOM   3823  ND1 HIS A 513      36.017  34.106  44.606  1.00 14.71           N  
ATOM   3824  CD2 HIS A 513      36.536  36.070  45.408  1.00 10.61           C  
ATOM   3825  CE1 HIS A 513      37.335  34.155  44.693  1.00 13.70           C  
ATOM   3826  NE2 HIS A 513      37.678  35.335  45.176  1.00 13.80           N  
ATOM   3827  N   ILE A 514      30.930  34.212  45.622  1.00 14.32           N  
ATOM   3828  CA  ILE A 514      29.504  34.511  45.670  1.00 13.72           C  
ATOM   3829  C   ILE A 514      28.954  34.249  47.079  1.00 14.60           C  
ATOM   3830  O   ILE A 514      28.518  35.182  47.757  1.00 13.03           O  
ATOM   3831  CB  ILE A 514      28.733  33.701  44.598  1.00 14.44           C  
ATOM   3832  CG1 ILE A 514      29.190  34.138  43.199  1.00 16.16           C  
ATOM   3833  CG2 ILE A 514      27.234  33.908  44.749  1.00 12.67           C  
ATOM   3834  CD1 ILE A 514      29.032  35.621  42.922  1.00 16.96           C  
ATOM   3835  N   PRO A 515      28.976  32.986  47.549  1.00 15.66           N  
ATOM   3836  CA  PRO A 515      28.457  32.750  48.903  1.00 15.17           C  
ATOM   3837  C   PRO A 515      29.305  33.419  49.990  1.00 16.68           C  
ATOM   3838  O   PRO A 515      28.799  33.732  51.074  1.00 15.08           O  
ATOM   3839  CB  PRO A 515      28.453  31.222  49.014  1.00 16.53           C  
ATOM   3840  CG  PRO A 515      29.579  30.812  48.111  1.00 17.51           C  
ATOM   3841  CD  PRO A 515      29.355  31.713  46.909  1.00 13.25           C  
ATOM   3842  N   SER A 516      30.589  33.641  49.701  1.00 13.81           N  
ATOM   3843  CA  SER A 516      31.488  34.284  50.659  1.00 15.60           C  
ATOM   3844  C   SER A 516      31.342  35.803  50.646  1.00 13.58           C  
ATOM   3845  O   SER A 516      31.965  36.499  51.443  1.00 13.34           O  
ATOM   3846  CB  SER A 516      32.947  33.918  50.362  1.00 18.79           C  
ATOM   3847  OG  SER A 516      33.183  32.536  50.565  1.00 22.02           O  
ATOM   3848  N   SER A 517      30.529  36.312  49.727  1.00 13.46           N  
ATOM   3849  CA  SER A 517      30.288  37.751  49.617  1.00 13.96           C  
ATOM   3850  C   SER A 517      31.571  38.587  49.542  1.00 15.62           C  
ATOM   3851  O   SER A 517      31.743  39.553  50.288  1.00 15.61           O  
ATOM   3852  CB  SER A 517      29.427  38.231  50.791  1.00 14.80           C  
ATOM   3853  OG  SER A 517      28.929  39.544  50.566  1.00 14.76           O  
ATOM   3854  N   VAL A 518      32.464  38.201  48.637  1.00 14.22           N  
ATOM   3855  CA  VAL A 518      33.718  38.914  48.413  1.00 14.31           C  
ATOM   3856  C   VAL A 518      33.611  39.538  47.023  1.00 13.23           C  
ATOM   3857  O   VAL A 518      33.448  38.826  46.034  1.00 14.20           O  
ATOM   3858  CB  VAL A 518      34.936  37.957  48.426  1.00 14.24           C  
ATOM   3859  CG1 VAL A 518      36.200  38.716  48.029  1.00 15.66           C  
ATOM   3860  CG2 VAL A 518      35.105  37.337  49.813  1.00 15.47           C  
ATOM   3861  N   PRO A 519      33.680  40.877  46.931  1.00 13.00           N  
ATOM   3862  CA  PRO A 519      33.588  41.572  45.637  1.00 13.72           C  
ATOM   3863  C   PRO A 519      34.597  41.006  44.640  1.00 13.40           C  
ATOM   3864  O   PRO A 519      35.694  40.602  45.027  1.00 12.68           O  
ATOM   3865  CB  PRO A 519      33.870  43.026  46.007  1.00 12.92           C  
ATOM   3866  CG  PRO A 519      33.282  43.120  47.399  1.00 13.93           C  
ATOM   3867  CD  PRO A 519      33.789  41.840  48.040  1.00 12.51           C  
ATOM   3868  N   TYR A 520      34.238  40.996  43.357  1.00 12.51           N  
ATOM   3869  CA  TYR A 520      35.111  40.419  42.337  1.00 11.74           C  
ATOM   3870  C   TYR A 520      35.758  41.362  41.316  1.00 12.92           C  
ATOM   3871  O   TYR A 520      36.772  41.009  40.713  1.00 12.28           O  
ATOM   3872  CB  TYR A 520      34.343  39.339  41.565  1.00 12.26           C  
ATOM   3873  CG  TYR A 520      35.216  38.181  41.146  1.00 11.10           C  
ATOM   3874  CD1 TYR A 520      35.589  37.201  42.069  1.00 12.21           C  
ATOM   3875  CD2 TYR A 520      35.717  38.092  39.849  1.00 10.70           C  
ATOM   3876  CE1 TYR A 520      36.445  36.163  41.716  1.00 11.38           C  
ATOM   3877  CE2 TYR A 520      36.578  37.052  39.479  1.00 11.88           C  
ATOM   3878  CZ  TYR A 520      36.936  36.095  40.422  1.00 12.73           C  
ATOM   3879  OH  TYR A 520      37.789  35.078  40.077  1.00 12.21           O  
ATOM   3880  N   ILE A 521      35.182  42.543  41.106  1.00 10.57           N  
ATOM   3881  CA  ILE A 521      35.729  43.474  40.123  1.00 10.70           C  
ATOM   3882  C   ILE A 521      37.195  43.826  40.404  1.00 11.68           C  
ATOM   3883  O   ILE A 521      37.940  44.198  39.499  1.00 12.19           O  
ATOM   3884  CB  ILE A 521      34.866  44.760  40.042  1.00 10.46           C  
ATOM   3885  CG1 ILE A 521      35.111  45.464  38.706  1.00 11.02           C  
ATOM   3886  CG2 ILE A 521      35.175  45.681  41.219  1.00 10.81           C  
ATOM   3887  CD1 ILE A 521      34.654  44.656  37.494  1.00 11.29           C  
ATOM   3888  N   ARG A 522      37.607  43.692  41.660  1.00 11.17           N  
ATOM   3889  CA  ARG A 522      38.989  43.952  42.055  1.00 10.89           C  
ATOM   3890  C   ARG A 522      39.971  43.071  41.260  1.00 12.16           C  
ATOM   3891  O   ARG A 522      41.105  43.478  40.990  1.00 11.49           O  
ATOM   3892  CB  ARG A 522      39.156  43.668  43.549  1.00 11.30           C  
ATOM   3893  CG  ARG A 522      38.686  42.265  43.958  1.00 13.00           C  
ATOM   3894  CD  ARG A 522      38.704  42.074  45.474  1.00 13.72           C  
ATOM   3895  NE  ARG A 522      37.886  43.088  46.134  1.00 10.87           N  
ATOM   3896  CZ  ARG A 522      37.634  43.123  47.439  1.00 13.84           C  
ATOM   3897  NH1 ARG A 522      38.132  42.196  48.247  1.00 11.15           N  
ATOM   3898  NH2 ARG A 522      36.889  44.100  47.941  1.00 13.85           N  
ATOM   3899  N   TYR A 523      39.539  41.871  40.881  1.00 10.69           N  
ATOM   3900  CA  TYR A 523      40.408  40.965  40.130  1.00 12.89           C  
ATOM   3901  C   TYR A 523      40.558  41.394  38.672  1.00 12.72           C  
ATOM   3902  O   TYR A 523      41.599  41.152  38.051  1.00 12.24           O  
ATOM   3903  CB  TYR A 523      39.882  39.525  40.215  1.00 10.20           C  
ATOM   3904  CG  TYR A 523      39.814  39.009  41.640  1.00 12.03           C  
ATOM   3905  CD1 TYR A 523      38.586  38.818  42.274  1.00 14.17           C  
ATOM   3906  CD2 TYR A 523      40.978  38.750  42.367  1.00 12.66           C  
ATOM   3907  CE1 TYR A 523      38.515  38.381  43.599  1.00 13.54           C  
ATOM   3908  CE2 TYR A 523      40.920  38.317  43.695  1.00 13.05           C  
ATOM   3909  CZ  TYR A 523      39.683  38.133  44.302  1.00 13.70           C  
ATOM   3910  OH  TYR A 523      39.603  37.697  45.610  1.00 13.05           O  
ATOM   3911  N   PHE A 524      39.515  42.016  38.128  1.00 10.68           N  
ATOM   3912  CA  PHE A 524      39.550  42.509  36.750  1.00 11.93           C  
ATOM   3913  C   PHE A 524      40.527  43.689  36.735  1.00 13.11           C  
ATOM   3914  O   PHE A 524      41.400  43.779  35.872  1.00 13.19           O  
ATOM   3915  CB  PHE A 524      38.154  42.980  36.317  1.00 11.21           C  
ATOM   3916  CG  PHE A 524      38.125  43.646  34.968  1.00 14.00           C  
ATOM   3917  CD1 PHE A 524      38.050  42.892  33.801  1.00 14.57           C  
ATOM   3918  CD2 PHE A 524      38.193  45.031  34.867  1.00 15.09           C  
ATOM   3919  CE1 PHE A 524      38.043  43.510  32.549  1.00 16.67           C  
ATOM   3920  CE2 PHE A 524      38.189  45.660  33.619  1.00 17.16           C  
ATOM   3921  CZ  PHE A 524      38.113  44.899  32.458  1.00 17.19           C  
ATOM   3922  N   VAL A 525      40.366  44.592  37.698  1.00 10.88           N  
ATOM   3923  CA  VAL A 525      41.239  45.753  37.809  1.00 11.92           C  
ATOM   3924  C   VAL A 525      42.683  45.276  37.989  1.00 12.43           C  
ATOM   3925  O   VAL A 525      43.590  45.746  37.308  1.00 12.45           O  
ATOM   3926  CB  VAL A 525      40.830  46.642  39.004  1.00 11.44           C  
ATOM   3927  CG1 VAL A 525      41.847  47.767  39.202  1.00 13.68           C  
ATOM   3928  CG2 VAL A 525      39.433  47.226  38.757  1.00 12.64           C  
ATOM   3929  N   SER A 526      42.882  44.325  38.895  1.00 12.83           N  
ATOM   3930  CA  SER A 526      44.211  43.781  39.156  1.00 13.38           C  
ATOM   3931  C   SER A 526      44.915  43.252  37.908  1.00 14.80           C  
ATOM   3932  O   SER A 526      46.080  43.567  37.659  1.00 13.56           O  
ATOM   3933  CB  SER A 526      44.124  42.658  40.195  1.00 14.45           C  
ATOM   3934  OG  SER A 526      45.366  41.981  40.321  1.00 15.47           O  
ATOM   3935  N   PHE A 527      44.220  42.438  37.123  1.00 13.85           N  
ATOM   3936  CA  PHE A 527      44.843  41.878  35.936  1.00 16.13           C  
ATOM   3937  C   PHE A 527      45.265  42.937  34.923  1.00 17.21           C  
ATOM   3938  O   PHE A 527      46.248  42.757  34.210  1.00 18.29           O  
ATOM   3939  CB  PHE A 527      43.930  40.813  35.311  1.00 14.35           C  
ATOM   3940  CG  PHE A 527      44.109  39.446  35.921  1.00 12.86           C  
ATOM   3941  CD1 PHE A 527      44.081  39.279  37.304  1.00 14.64           C  
ATOM   3942  CD2 PHE A 527      44.352  38.336  35.116  1.00 12.97           C  
ATOM   3943  CE1 PHE A 527      44.301  38.021  37.881  1.00 14.77           C  
ATOM   3944  CE2 PHE A 527      44.570  37.081  35.674  1.00 14.28           C  
ATOM   3945  CZ  PHE A 527      44.546  36.921  37.061  1.00 14.43           C  
ATOM   3946  N   ILE A 528      44.545  44.052  34.875  1.00 17.72           N  
ATOM   3947  CA  ILE A 528      44.907  45.124  33.956  1.00 17.85           C  
ATOM   3948  C   ILE A 528      46.120  45.891  34.491  1.00 16.91           C  
ATOM   3949  O   ILE A 528      47.155  45.991  33.826  1.00 18.09           O  
ATOM   3950  CB  ILE A 528      43.754  46.148  33.780  1.00 19.20           C  
ATOM   3951  CG1 ILE A 528      42.564  45.502  33.064  1.00 21.05           C  
ATOM   3952  CG2 ILE A 528      44.260  47.363  33.011  1.00 19.44           C  
ATOM   3953  CD1 ILE A 528      42.807  45.211  31.605  1.00 22.66           C  
ATOM   3954  N   ILE A 529      45.991  46.417  35.704  1.00 15.99           N  
ATOM   3955  CA  ILE A 529      47.056  47.221  36.294  1.00 14.87           C  
ATOM   3956  C   ILE A 529      48.337  46.467  36.639  1.00 16.49           C  
ATOM   3957  O   ILE A 529      49.415  47.060  36.666  1.00 14.18           O  
ATOM   3958  CB  ILE A 529      46.560  47.971  37.563  1.00 15.25           C  
ATOM   3959  CG1 ILE A 529      46.366  46.996  38.725  1.00 14.28           C  
ATOM   3960  CG2 ILE A 529      45.253  48.708  37.249  1.00 13.63           C  
ATOM   3961  CD1 ILE A 529      45.970  47.678  40.039  1.00 14.84           C  
ATOM   3962  N   GLN A 530      48.245  45.167  36.900  1.00 15.61           N  
ATOM   3963  CA  GLN A 530      49.461  44.443  37.233  1.00 16.41           C  
ATOM   3964  C   GLN A 530      50.450  44.476  36.064  1.00 16.86           C  
ATOM   3965  O   GLN A 530      51.664  44.434  36.273  1.00 16.40           O  
ATOM   3966  CB  GLN A 530      49.152  43.001  37.663  1.00 15.73           C  
ATOM   3967  CG  GLN A 530      48.557  42.090  36.604  1.00 14.21           C  
ATOM   3968  CD  GLN A 530      48.239  40.715  37.171  1.00 17.73           C  
ATOM   3969  OE1 GLN A 530      48.834  39.715  36.771  1.00 16.09           O  
ATOM   3970  NE2 GLN A 530      47.300  40.664  38.121  1.00 14.54           N  
ATOM   3971  N   PHE A 531      49.939  44.565  34.836  1.00 15.77           N  
ATOM   3972  CA  PHE A 531      50.824  44.631  33.684  1.00 16.79           C  
ATOM   3973  C   PHE A 531      51.385  46.042  33.579  1.00 17.19           C  
ATOM   3974  O   PHE A 531      52.517  46.238  33.143  1.00 15.79           O  
ATOM   3975  CB  PHE A 531      50.096  44.217  32.399  1.00 15.11           C  
ATOM   3976  CG  PHE A 531      49.994  42.729  32.236  1.00 16.63           C  
ATOM   3977  CD1 PHE A 531      48.911  42.029  32.757  1.00 14.63           C  
ATOM   3978  CD2 PHE A 531      51.037  42.012  31.648  1.00 18.81           C  
ATOM   3979  CE1 PHE A 531      48.865  40.637  32.705  1.00 18.62           C  
ATOM   3980  CE2 PHE A 531      51.006  40.615  31.589  1.00 18.29           C  
ATOM   3981  CZ  PHE A 531      49.915  39.927  32.121  1.00 17.80           C  
ATOM   3982  N   GLN A 532      50.592  47.022  33.998  1.00 16.85           N  
ATOM   3983  CA  GLN A 532      51.043  48.407  34.001  1.00 18.71           C  
ATOM   3984  C   GLN A 532      52.184  48.528  35.011  1.00 18.91           C  
ATOM   3985  O   GLN A 532      53.159  49.237  34.773  1.00 21.62           O  
ATOM   3986  CB  GLN A 532      49.909  49.347  34.418  1.00 18.72           C  
ATOM   3987  CG  GLN A 532      48.890  49.651  33.335  1.00 16.23           C  
ATOM   3988  CD  GLN A 532      47.819  50.607  33.825  1.00 18.40           C  
ATOM   3989  OE1 GLN A 532      46.777  50.188  34.326  1.00 16.56           O  
ATOM   3990  NE2 GLN A 532      48.084  51.908  33.700  1.00 15.19           N  
ATOM   3991  N   PHE A 533      52.048  47.846  36.148  1.00 17.60           N  
ATOM   3992  CA  PHE A 533      53.082  47.879  37.179  1.00 17.70           C  
ATOM   3993  C   PHE A 533      54.320  47.132  36.682  1.00 18.19           C  
ATOM   3994  O   PHE A 533      55.448  47.583  36.866  1.00 16.35           O  
ATOM   3995  CB  PHE A 533      52.576  47.237  38.479  1.00 16.56           C  
ATOM   3996  CG  PHE A 533      51.412  47.961  39.114  1.00 16.88           C  
ATOM   3997  CD1 PHE A 533      51.009  49.216  38.655  1.00 17.26           C  
ATOM   3998  CD2 PHE A 533      50.732  47.393  40.193  1.00 17.51           C  
ATOM   3999  CE1 PHE A 533      49.948  49.896  39.262  1.00 17.30           C  
ATOM   4000  CE2 PHE A 533      49.668  48.065  40.811  1.00 16.87           C  
ATOM   4001  CZ  PHE A 533      49.275  49.316  40.346  1.00 17.82           C  
ATOM   4002  N   HIS A 534      54.103  45.980  36.058  1.00 18.26           N  
ATOM   4003  CA  HIS A 534      55.201  45.191  35.523  1.00 17.93           C  
ATOM   4004  C   HIS A 534      56.001  46.053  34.536  1.00 19.62           C  
ATOM   4005  O   HIS A 534      57.224  46.140  34.623  1.00 19.79           O  
ATOM   4006  CB  HIS A 534      54.652  43.948  34.813  1.00 16.92           C  
ATOM   4007  CG  HIS A 534      55.712  43.026  34.290  1.00 19.54           C  
ATOM   4008  ND1 HIS A 534      56.645  42.424  35.106  1.00 19.14           N  
ATOM   4009  CD2 HIS A 534      55.963  42.577  33.036  1.00 18.23           C  
ATOM   4010  CE1 HIS A 534      57.423  41.641  34.379  1.00 19.86           C  
ATOM   4011  NE2 HIS A 534      57.030  41.716  33.120  1.00 18.37           N  
ATOM   4012  N   GLU A 535      55.299  46.692  33.605  1.00 19.55           N  
ATOM   4013  CA  GLU A 535      55.938  47.546  32.607  1.00 21.41           C  
ATOM   4014  C   GLU A 535      56.781  48.645  33.259  1.00 22.27           C  
ATOM   4015  O   GLU A 535      57.954  48.823  32.920  1.00 22.02           O  
ATOM   4016  CB  GLU A 535      54.874  48.175  31.702  1.00 21.29           C  
ATOM   4017  CG  GLU A 535      55.420  49.067  30.595  1.00 22.84           C  
ATOM   4018  CD  GLU A 535      54.320  49.736  29.798  1.00 23.16           C  
ATOM   4019  OE1 GLU A 535      53.587  50.571  30.370  1.00 25.71           O  
ATOM   4020  OE2 GLU A 535      54.180  49.423  28.599  1.00 24.72           O  
ATOM   4021  N   ALA A 536      56.185  49.375  34.199  1.00 22.14           N  
ATOM   4022  CA  ALA A 536      56.884  50.457  34.887  1.00 22.62           C  
ATOM   4023  C   ALA A 536      58.081  49.966  35.698  1.00 23.23           C  
ATOM   4024  O   ALA A 536      59.165  50.544  35.633  1.00 21.96           O  
ATOM   4025  CB  ALA A 536      55.918  51.206  35.794  1.00 21.46           C  
ATOM   4026  N   LEU A 537      57.884  48.898  36.463  1.00 23.52           N  
ATOM   4027  CA  LEU A 537      58.953  48.353  37.287  1.00 24.49           C  
ATOM   4028  C   LEU A 537      60.129  47.874  36.444  1.00 26.12           C  
ATOM   4029  O   LEU A 537      61.287  48.041  36.835  1.00 25.53           O  
ATOM   4030  CB  LEU A 537      58.427  47.204  38.149  1.00 23.80           C  
ATOM   4031  CG  LEU A 537      57.319  47.563  39.146  1.00 25.68           C  
ATOM   4032  CD1 LEU A 537      56.974  46.337  39.976  1.00 24.01           C  
ATOM   4033  CD2 LEU A 537      57.770  48.705  40.047  1.00 24.11           C  
ATOM   4034  N   CYS A 538      59.829  47.277  35.293  1.00 26.09           N  
ATOM   4035  CA  CYS A 538      60.866  46.785  34.394  1.00 26.84           C  
ATOM   4036  C   CYS A 538      61.662  47.954  33.833  1.00 29.17           C  
ATOM   4037  O   CYS A 538      62.888  47.891  33.735  1.00 29.21           O  
ATOM   4038  CB  CYS A 538      60.245  45.983  33.251  1.00 24.41           C  
ATOM   4039  SG  CYS A 538      59.479  44.440  33.829  1.00 23.54           S  
ATOM   4040  N   GLN A 539      60.958  49.018  33.461  1.00 30.60           N  
ATOM   4041  CA  GLN A 539      61.609  50.205  32.929  1.00 33.85           C  
ATOM   4042  C   GLN A 539      62.518  50.774  34.018  1.00 34.13           C  
ATOM   4043  O   GLN A 539      63.651  51.168  33.750  1.00 35.84           O  
ATOM   4044  CB  GLN A 539      60.560  51.241  32.508  1.00 36.01           C  
ATOM   4045  CG  GLN A 539      61.123  52.471  31.797  1.00 40.86           C  
ATOM   4046  CD  GLN A 539      61.634  53.535  32.755  1.00 44.93           C  
ATOM   4047  OE1 GLN A 539      62.251  54.518  32.338  1.00 47.36           O  
ATOM   4048  NE2 GLN A 539      61.370  53.349  34.044  1.00 46.77           N  
ATOM   4049  N   ALA A 540      62.023  50.793  35.252  1.00 33.88           N  
ATOM   4050  CA  ALA A 540      62.798  51.308  36.376  1.00 33.88           C  
ATOM   4051  C   ALA A 540      64.008  50.421  36.655  1.00 34.68           C  
ATOM   4052  O   ALA A 540      65.025  50.891  37.168  1.00 33.79           O  
ATOM   4053  CB  ALA A 540      61.922  51.397  37.616  1.00 33.43           C  
ATOM   4054  N   ALA A 541      63.894  49.140  36.314  1.00 34.10           N  
ATOM   4055  CA  ALA A 541      64.979  48.187  36.529  1.00 34.04           C  
ATOM   4056  C   ALA A 541      65.987  48.209  35.381  1.00 34.28           C  
ATOM   4057  O   ALA A 541      66.963  47.456  35.387  1.00 33.48           O  
ATOM   4058  CB  ALA A 541      64.414  46.781  36.698  1.00 31.78           C  
ATOM   4059  N   GLY A 542      65.740  49.067  34.396  1.00 35.90           N  
ATOM   4060  CA  GLY A 542      66.639  49.173  33.261  1.00 36.02           C  
ATOM   4061  C   GLY A 542      66.486  48.083  32.214  1.00 36.88           C  
ATOM   4062  O   GLY A 542      67.380  47.876  31.391  1.00 36.25           O  
ATOM   4063  N   HIS A 543      65.357  47.381  32.232  1.00 36.48           N  
ATOM   4064  CA  HIS A 543      65.124  46.320  31.262  1.00 34.33           C  
ATOM   4065  C   HIS A 543      64.874  46.906  29.881  1.00 33.60           C  
ATOM   4066  O   HIS A 543      64.237  47.946  29.743  1.00 33.03           O  
ATOM   4067  CB  HIS A 543      63.916  45.472  31.661  1.00 35.35           C  
ATOM   4068  CG  HIS A 543      63.584  44.400  30.670  1.00 36.05           C  
ATOM   4069  ND1 HIS A 543      64.327  43.245  30.547  1.00 36.78           N  
ATOM   4070  CD2 HIS A 543      62.614  44.325  29.727  1.00 36.62           C  
ATOM   4071  CE1 HIS A 543      63.829  42.506  29.571  1.00 36.45           C  
ATOM   4072  NE2 HIS A 543      62.790  43.138  29.057  1.00 35.54           N  
ATOM   4073  N   THR A 544      65.380  46.227  28.859  1.00 32.54           N  
ATOM   4074  CA  THR A 544      65.192  46.671  27.488  1.00 33.83           C  
ATOM   4075  C   THR A 544      64.751  45.462  26.676  1.00 33.06           C  
ATOM   4076  O   THR A 544      65.060  44.322  27.030  1.00 33.26           O  
ATOM   4077  CB  THR A 544      66.501  47.234  26.889  1.00 34.38           C  
ATOM   4078  OG1 THR A 544      67.435  46.166  26.684  1.00 35.54           O  
ATOM   4079  CG2 THR A 544      67.115  48.261  27.831  1.00 35.04           C  
ATOM   4080  N   GLY A 545      64.023  45.711  25.594  1.00 32.96           N  
ATOM   4081  CA  GLY A 545      63.554  44.618  24.764  1.00 32.46           C  
ATOM   4082  C   GLY A 545      62.144  44.192  25.125  1.00 32.04           C  
ATOM   4083  O   GLY A 545      61.479  44.862  25.915  1.00 32.23           O  
ATOM   4084  N   PRO A 546      61.663  43.068  24.571  1.00 31.90           N  
ATOM   4085  CA  PRO A 546      60.314  42.558  24.841  1.00 29.53           C  
ATOM   4086  C   PRO A 546      59.972  42.538  26.329  1.00 28.72           C  
ATOM   4087  O   PRO A 546      60.709  41.981  27.143  1.00 28.66           O  
ATOM   4088  CB  PRO A 546      60.351  41.158  24.235  1.00 30.83           C  
ATOM   4089  CG  PRO A 546      61.297  41.321  23.087  1.00 32.27           C  
ATOM   4090  CD  PRO A 546      62.410  42.136  23.709  1.00 30.59           C  
ATOM   4091  N   LEU A 547      58.842  43.146  26.672  1.00 27.32           N  
ATOM   4092  CA  LEU A 547      58.393  43.211  28.055  1.00 25.47           C  
ATOM   4093  C   LEU A 547      58.224  41.831  28.695  1.00 24.37           C  
ATOM   4094  O   LEU A 547      58.540  41.646  29.874  1.00 25.18           O  
ATOM   4095  CB  LEU A 547      57.073  43.990  28.135  1.00 24.84           C  
ATOM   4096  CG  LEU A 547      56.462  44.208  29.523  1.00 23.79           C  
ATOM   4097  CD1 LEU A 547      57.435  44.990  30.395  1.00 23.05           C  
ATOM   4098  CD2 LEU A 547      55.141  44.962  29.390  1.00 24.13           C  
ATOM   4099  N   HIS A 548      57.743  40.855  27.927  1.00 22.93           N  
ATOM   4100  CA  HIS A 548      57.533  39.521  28.482  1.00 22.45           C  
ATOM   4101  C   HIS A 548      58.810  38.796  28.900  1.00 23.53           C  
ATOM   4102  O   HIS A 548      58.744  37.743  29.535  1.00 24.05           O  
ATOM   4103  CB  HIS A 548      56.736  38.635  27.511  1.00 22.24           C  
ATOM   4104  CG  HIS A 548      57.512  38.181  26.313  1.00 22.10           C  
ATOM   4105  ND1 HIS A 548      57.627  38.938  25.166  1.00 24.64           N  
ATOM   4106  CD2 HIS A 548      58.201  37.038  26.080  1.00 23.76           C  
ATOM   4107  CE1 HIS A 548      58.350  38.279  24.277  1.00 25.23           C  
ATOM   4108  NE2 HIS A 548      58.711  37.123  24.807  1.00 25.73           N  
ATOM   4109  N   LYS A 549      59.968  39.348  28.547  1.00 23.73           N  
ATOM   4110  CA  LYS A 549      61.244  38.734  28.919  1.00 26.19           C  
ATOM   4111  C   LYS A 549      61.811  39.340  30.206  1.00 26.16           C  
ATOM   4112  O   LYS A 549      62.850  38.903  30.706  1.00 23.22           O  
ATOM   4113  CB  LYS A 549      62.272  38.902  27.794  1.00 27.71           C  
ATOM   4114  CG  LYS A 549      61.993  38.075  26.553  1.00 31.25           C  
ATOM   4115  CD  LYS A 549      63.043  38.351  25.481  1.00 34.78           C  
ATOM   4116  CE  LYS A 549      62.733  37.611  24.191  1.00 37.22           C  
ATOM   4117  NZ  LYS A 549      63.671  37.995  23.096  1.00 40.53           N  
ATOM   4118  N   CYS A 550      61.124  40.344  30.739  1.00 24.41           N  
ATOM   4119  CA  CYS A 550      61.569  41.006  31.959  1.00 23.52           C  
ATOM   4120  C   CYS A 550      61.407  40.186  33.240  1.00 24.04           C  
ATOM   4121  O   CYS A 550      60.418  39.469  33.419  1.00 21.53           O  
ATOM   4122  CB  CYS A 550      60.838  42.342  32.119  1.00 23.29           C  
ATOM   4123  SG  CYS A 550      61.004  43.098  33.770  1.00 24.70           S  
ATOM   4124  N   ASP A 551      62.400  40.306  34.121  1.00 21.19           N  
ATOM   4125  CA  ASP A 551      62.419  39.637  35.421  1.00 22.50           C  
ATOM   4126  C   ASP A 551      63.010  40.680  36.360  1.00 24.44           C  
ATOM   4127  O   ASP A 551      64.211  40.968  36.302  1.00 24.08           O  
ATOM   4128  CB  ASP A 551      63.317  38.394  35.392  1.00 22.61           C  
ATOM   4129  CG  ASP A 551      63.390  37.685  36.742  1.00 23.83           C  
ATOM   4130  OD1 ASP A 551      62.906  38.239  37.758  1.00 24.26           O  
ATOM   4131  OD2 ASP A 551      63.947  36.567  36.793  1.00 23.11           O  
ATOM   4132  N   ILE A 552      62.165  41.253  37.213  1.00 22.22           N  
ATOM   4133  CA  ILE A 552      62.601  42.294  38.138  1.00 21.09           C  
ATOM   4134  C   ILE A 552      63.279  41.779  39.401  1.00 21.02           C  
ATOM   4135  O   ILE A 552      63.533  42.552  40.325  1.00 21.75           O  
ATOM   4136  CB  ILE A 552      61.413  43.184  38.568  1.00 19.80           C  
ATOM   4137  CG1 ILE A 552      60.408  42.355  39.369  1.00 19.27           C  
ATOM   4138  CG2 ILE A 552      60.751  43.796  37.340  1.00 18.47           C  
ATOM   4139  CD1 ILE A 552      59.301  43.181  40.010  1.00 21.03           C  
ATOM   4140  N   TYR A 553      63.575  40.484  39.445  1.00 21.19           N  
ATOM   4141  CA  TYR A 553      64.220  39.906  40.620  1.00 22.52           C  
ATOM   4142  C   TYR A 553      65.434  40.721  41.068  1.00 22.10           C  
ATOM   4143  O   TYR A 553      66.273  41.102  40.252  1.00 19.45           O  
ATOM   4144  CB  TYR A 553      64.660  38.466  40.346  1.00 23.63           C  
ATOM   4145  CG  TYR A 553      65.245  37.787  41.565  1.00 25.38           C  
ATOM   4146  CD1 TYR A 553      64.420  37.304  42.576  1.00 24.65           C  
ATOM   4147  CD2 TYR A 553      66.625  37.672  41.731  1.00 25.96           C  
ATOM   4148  CE1 TYR A 553      64.951  36.724  43.725  1.00 26.30           C  
ATOM   4149  CE2 TYR A 553      67.167  37.095  42.878  1.00 27.41           C  
ATOM   4150  CZ  TYR A 553      66.325  36.624  43.869  1.00 27.35           C  
ATOM   4151  OH  TYR A 553      66.852  36.048  45.003  1.00 29.28           O  
ATOM   4152  N   GLN A 554      65.501  40.980  42.373  1.00 24.34           N  
ATOM   4153  CA  GLN A 554      66.581  41.736  43.014  1.00 25.79           C  
ATOM   4154  C   GLN A 554      66.666  43.231  42.687  1.00 25.96           C  
ATOM   4155  O   GLN A 554      67.585  43.919  43.139  1.00 27.28           O  
ATOM   4156  CB  GLN A 554      67.937  41.063  42.740  1.00 27.46           C  
ATOM   4157  CG  GLN A 554      69.106  41.754  43.433  1.00 30.44           C  
ATOM   4158  CD  GLN A 554      70.383  40.939  43.418  1.00 32.54           C  
ATOM   4159  OE1 GLN A 554      71.474  41.474  43.621  1.00 33.54           O  
ATOM   4160  NE2 GLN A 554      70.253  39.636  43.194  1.00 31.30           N  
ATOM   4161  N   SER A 555      65.707  43.747  41.924  1.00 24.70           N  
ATOM   4162  CA  SER A 555      65.716  45.165  41.577  1.00 25.28           C  
ATOM   4163  C   SER A 555      65.247  46.047  42.728  1.00 26.57           C  
ATOM   4164  O   SER A 555      64.072  46.026  43.103  1.00 26.45           O  
ATOM   4165  CB  SER A 555      64.829  45.436  40.365  1.00 24.97           C  
ATOM   4166  OG  SER A 555      64.667  46.834  40.178  1.00 25.13           O  
ATOM   4167  N   LYS A 556      66.167  46.832  43.277  1.00 25.12           N  
ATOM   4168  CA  LYS A 556      65.843  47.724  44.378  1.00 26.77           C  
ATOM   4169  C   LYS A 556      65.022  48.918  43.897  1.00 25.59           C  
ATOM   4170  O   LYS A 556      64.201  49.448  44.642  1.00 26.97           O  
ATOM   4171  CB  LYS A 556      67.126  48.207  45.067  1.00 26.74           C  
ATOM   4172  CG  LYS A 556      67.944  47.087  45.702  1.00 27.54           C  
ATOM   4173  CD  LYS A 556      67.119  46.297  46.712  1.00 27.45           C  
ATOM   4174  CE  LYS A 556      67.925  45.161  47.332  1.00 26.21           C  
ATOM   4175  NZ  LYS A 556      68.401  44.190  46.311  1.00 25.90           N  
ATOM   4176  N   GLU A 557      65.245  49.344  42.657  1.00 24.23           N  
ATOM   4177  CA  GLU A 557      64.496  50.467  42.104  1.00 25.34           C  
ATOM   4178  C   GLU A 557      63.021  50.071  41.987  1.00 25.42           C  
ATOM   4179  O   GLU A 557      62.125  50.880  42.238  1.00 22.32           O  
ATOM   4180  CB  GLU A 557      65.025  50.849  40.718  1.00 29.07           C  
ATOM   4181  CG  GLU A 557      66.440  51.417  40.693  1.00 34.67           C  
ATOM   4182  CD  GLU A 557      67.496  50.393  41.060  1.00 38.21           C  
ATOM   4183  OE1 GLU A 557      67.482  49.283  40.480  1.00 38.94           O  
ATOM   4184  OE2 GLU A 557      68.348  50.704  41.921  1.00 41.97           O  
ATOM   4185  N   ALA A 558      62.783  48.822  41.596  1.00 24.18           N  
ATOM   4186  CA  ALA A 558      61.426  48.306  41.452  1.00 24.57           C  
ATOM   4187  C   ALA A 558      60.761  48.271  42.822  1.00 24.55           C  
ATOM   4188  O   ALA A 558      59.665  48.801  43.009  1.00 24.25           O  
ATOM   4189  CB  ALA A 558      61.455  46.903  40.851  1.00 24.39           C  
ATOM   4190  N   GLY A 559      61.439  47.646  43.778  1.00 23.98           N  
ATOM   4191  CA  GLY A 559      60.902  47.551  45.121  1.00 26.42           C  
ATOM   4192  C   GLY A 559      60.582  48.897  45.746  1.00 27.69           C  
ATOM   4193  O   GLY A 559      59.577  49.039  46.442  1.00 28.18           O  
ATOM   4194  N   GLN A 560      61.429  49.890  45.500  1.00 27.79           N  
ATOM   4195  CA  GLN A 560      61.214  51.214  46.066  1.00 29.11           C  
ATOM   4196  C   GLN A 560      59.904  51.843  45.600  1.00 28.84           C  
ATOM   4197  O   GLN A 560      59.228  52.522  46.371  1.00 26.01           O  
ATOM   4198  CB  GLN A 560      62.376  52.143  45.715  1.00 31.76           C  
ATOM   4199  CG  GLN A 560      62.271  53.502  46.384  1.00 36.94           C  
ATOM   4200  CD  GLN A 560      62.181  53.386  47.896  1.00 41.21           C  
ATOM   4201  OE1 GLN A 560      63.116  52.925  48.554  1.00 44.17           O  
ATOM   4202  NE2 GLN A 560      61.048  53.795  48.454  1.00 43.27           N  
ATOM   4203  N   ARG A 561      59.547  51.625  44.340  1.00 28.52           N  
ATOM   4204  CA  ARG A 561      58.307  52.191  43.823  1.00 29.49           C  
ATOM   4205  C   ARG A 561      57.086  51.515  44.428  1.00 28.08           C  
ATOM   4206  O   ARG A 561      56.103  52.177  44.758  1.00 30.13           O  
ATOM   4207  CB  ARG A 561      58.258  52.089  42.298  1.00 30.74           C  
ATOM   4208  CG  ARG A 561      59.232  53.022  41.610  1.00 33.59           C  
ATOM   4209  CD  ARG A 561      58.864  53.215  40.162  1.00 34.84           C  
ATOM   4210  NE  ARG A 561      59.817  54.071  39.469  1.00 36.89           N  
ATOM   4211  CZ  ARG A 561      59.720  54.401  38.187  1.00 39.66           C  
ATOM   4212  NH1 ARG A 561      58.706  53.948  37.460  1.00 40.17           N  
ATOM   4213  NH2 ARG A 561      60.641  55.173  37.628  1.00 40.49           N  
ATOM   4214  N   LEU A 562      57.144  50.197  44.576  1.00 25.72           N  
ATOM   4215  CA  LEU A 562      56.028  49.468  45.162  1.00 24.31           C  
ATOM   4216  C   LEU A 562      55.856  49.851  46.630  1.00 24.61           C  
ATOM   4217  O   LEU A 562      54.734  50.014  47.113  1.00 22.28           O  
ATOM   4218  CB  LEU A 562      56.257  47.960  45.061  1.00 23.41           C  
ATOM   4219  CG  LEU A 562      56.003  47.293  43.710  1.00 24.09           C  
ATOM   4220  CD1 LEU A 562      56.340  45.814  43.814  1.00 22.31           C  
ATOM   4221  CD2 LEU A 562      54.541  47.482  43.309  1.00 24.13           C  
ATOM   4222  N   ALA A 563      56.979  49.994  47.327  1.00 22.88           N  
ATOM   4223  CA  ALA A 563      56.975  50.342  48.743  1.00 24.40           C  
ATOM   4224  C   ALA A 563      56.350  51.704  49.016  1.00 23.79           C  
ATOM   4225  O   ALA A 563      55.480  51.824  49.878  1.00 24.99           O  
ATOM   4226  CB  ALA A 563      58.400  50.304  49.299  1.00 23.81           C  
ATOM   4227  N   THR A 564      56.784  52.729  48.288  1.00 23.07           N  
ATOM   4228  CA  THR A 564      56.244  54.065  48.506  1.00 26.20           C  
ATOM   4229  C   THR A 564      54.745  54.092  48.218  1.00 25.47           C  
ATOM   4230  O   THR A 564      53.983  54.780  48.901  1.00 24.49           O  
ATOM   4231  CB  THR A 564      56.956  55.126  47.627  1.00 28.03           C  
ATOM   4232  OG1 THR A 564      56.705  54.861  46.242  1.00 35.56           O  
ATOM   4233  CG2 THR A 564      58.457  55.094  47.873  1.00 28.43           C  
ATOM   4234  N   ALA A 565      54.326  53.331  47.211  1.00 23.19           N  
ATOM   4235  CA  ALA A 565      52.918  53.265  46.846  1.00 22.32           C  
ATOM   4236  C   ALA A 565      52.123  52.530  47.919  1.00 20.86           C  
ATOM   4237  O   ALA A 565      51.067  52.993  48.347  1.00 21.03           O  
ATOM   4238  CB  ALA A 565      52.756  52.563  45.496  1.00 22.20           C  
ATOM   4239  N   MET A 566      52.631  51.385  48.362  1.00 20.23           N  
ATOM   4240  CA  MET A 566      51.930  50.608  49.376  1.00 20.17           C  
ATOM   4241  C   MET A 566      51.824  51.338  50.710  1.00 21.22           C  
ATOM   4242  O   MET A 566      50.834  51.194  51.426  1.00 19.46           O  
ATOM   4243  CB  MET A 566      52.610  49.249  49.581  1.00 18.97           C  
ATOM   4244  CG  MET A 566      52.435  48.280  48.412  1.00 18.62           C  
ATOM   4245  SD  MET A 566      53.001  46.611  48.797  1.00 20.81           S  
ATOM   4246  CE  MET A 566      54.714  46.755  48.344  1.00 18.21           C  
ATOM   4247  N   LYS A 567      52.839  52.128  51.039  1.00 22.34           N  
ATOM   4248  CA  LYS A 567      52.845  52.863  52.298  1.00 23.65           C  
ATOM   4249  C   LYS A 567      51.706  53.875  52.417  1.00 22.67           C  
ATOM   4250  O   LYS A 567      51.337  54.267  53.522  1.00 23.02           O  
ATOM   4251  CB  LYS A 567      54.194  53.565  52.492  1.00 23.93           C  
ATOM   4252  CG  LYS A 567      55.328  52.609  52.830  1.00 28.85           C  
ATOM   4253  CD  LYS A 567      56.610  53.354  53.162  1.00 31.84           C  
ATOM   4254  CE  LYS A 567      57.625  52.428  53.822  1.00 35.46           C  
ATOM   4255  NZ  LYS A 567      58.006  51.266  52.967  1.00 38.87           N  
ATOM   4256  N   LEU A 568      51.154  54.299  51.284  1.00 20.77           N  
ATOM   4257  CA  LEU A 568      50.050  55.257  51.290  1.00 20.03           C  
ATOM   4258  C   LEU A 568      48.757  54.614  51.784  1.00 20.21           C  
ATOM   4259  O   LEU A 568      47.834  55.306  52.219  1.00 19.40           O  
ATOM   4260  CB  LEU A 568      49.807  55.812  49.883  1.00 21.69           C  
ATOM   4261  CG  LEU A 568      50.838  56.754  49.260  1.00 22.59           C  
ATOM   4262  CD1 LEU A 568      50.420  57.074  47.835  1.00 22.70           C  
ATOM   4263  CD2 LEU A 568      50.947  58.026  50.085  1.00 22.77           C  
ATOM   4264  N   GLY A 569      48.690  53.290  51.717  1.00 20.15           N  
ATOM   4265  CA  GLY A 569      47.478  52.611  52.134  1.00 20.16           C  
ATOM   4266  C   GLY A 569      46.297  53.228  51.402  1.00 20.63           C  
ATOM   4267  O   GLY A 569      46.347  53.438  50.185  1.00 20.76           O  
ATOM   4268  N   PHE A 570      45.245  53.544  52.150  1.00 20.86           N  
ATOM   4269  CA  PHE A 570      44.031  54.143  51.593  1.00 21.23           C  
ATOM   4270  C   PHE A 570      43.972  55.632  51.961  1.00 20.30           C  
ATOM   4271  O   PHE A 570      42.899  56.230  51.999  1.00 21.85           O  
ATOM   4272  CB  PHE A 570      42.807  53.406  52.161  1.00 20.65           C  
ATOM   4273  CG  PHE A 570      41.509  53.733  51.470  1.00 24.23           C  
ATOM   4274  CD1 PHE A 570      41.340  53.471  50.115  1.00 25.84           C  
ATOM   4275  CD2 PHE A 570      40.449  54.283  52.183  1.00 24.34           C  
ATOM   4276  CE1 PHE A 570      40.130  53.751  49.479  1.00 28.01           C  
ATOM   4277  CE2 PHE A 570      39.233  54.568  51.557  1.00 27.29           C  
ATOM   4278  CZ  PHE A 570      39.075  54.300  50.202  1.00 26.47           C  
ATOM   4279  N   SER A 571      45.133  56.231  52.209  1.00 21.00           N  
ATOM   4280  CA  SER A 571      45.208  57.641  52.609  1.00 22.21           C  
ATOM   4281  C   SER A 571      44.982  58.679  51.506  1.00 23.68           C  
ATOM   4282  O   SER A 571      44.636  59.827  51.795  1.00 23.46           O  
ATOM   4283  CB  SER A 571      46.560  57.918  53.270  1.00 22.60           C  
ATOM   4284  OG  SER A 571      47.619  57.789  52.338  1.00 20.98           O  
ATOM   4285  N   ARG A 572      45.177  58.285  50.252  1.00 22.88           N  
ATOM   4286  CA  ARG A 572      45.005  59.207  49.130  1.00 25.54           C  
ATOM   4287  C   ARG A 572      44.243  58.549  47.981  1.00 23.92           C  
ATOM   4288  O   ARG A 572      44.199  57.330  47.884  1.00 24.89           O  
ATOM   4289  CB  ARG A 572      46.380  59.662  48.620  1.00 27.34           C  
ATOM   4290  CG  ARG A 572      47.247  60.373  49.654  1.00 31.36           C  
ATOM   4291  CD  ARG A 572      46.692  61.748  49.980  1.00 35.45           C  
ATOM   4292  NE  ARG A 572      46.606  62.585  48.784  1.00 40.01           N  
ATOM   4293  CZ  ARG A 572      46.063  63.799  48.754  1.00 42.24           C  
ATOM   4294  NH1 ARG A 572      45.552  64.329  49.857  1.00 44.20           N  
ATOM   4295  NH2 ARG A 572      46.029  64.483  47.618  1.00 41.85           N  
ATOM   4296  N   PRO A 573      43.623  59.353  47.101  1.00 24.43           N  
ATOM   4297  CA  PRO A 573      42.881  58.785  45.967  1.00 23.43           C  
ATOM   4298  C   PRO A 573      43.856  57.874  45.217  1.00 22.52           C  
ATOM   4299  O   PRO A 573      45.017  58.241  45.026  1.00 19.66           O  
ATOM   4300  CB  PRO A 573      42.495  60.021  45.161  1.00 24.04           C  
ATOM   4301  CG  PRO A 573      42.327  61.076  46.235  1.00 24.67           C  
ATOM   4302  CD  PRO A 573      43.538  60.825  47.105  1.00 24.47           C  
ATOM   4303  N   TRP A 574      43.397  56.702  44.784  1.00 21.06           N  
ATOM   4304  CA  TRP A 574      44.295  55.761  44.115  1.00 19.74           C  
ATOM   4305  C   TRP A 574      45.110  56.278  42.928  1.00 18.46           C  
ATOM   4306  O   TRP A 574      46.203  55.777  42.671  1.00 19.34           O  
ATOM   4307  CB  TRP A 574      43.547  54.478  43.719  1.00 17.20           C  
ATOM   4308  CG  TRP A 574      42.556  54.624  42.617  1.00 16.80           C  
ATOM   4309  CD1 TRP A 574      41.198  54.716  42.736  1.00 16.73           C  
ATOM   4310  CD2 TRP A 574      42.839  54.662  41.218  1.00 13.73           C  
ATOM   4311  NE1 TRP A 574      40.619  54.802  41.496  1.00 15.70           N  
ATOM   4312  CE2 TRP A 574      41.604  54.771  40.545  1.00 13.99           C  
ATOM   4313  CE3 TRP A 574      44.019  54.611  40.465  1.00 14.13           C  
ATOM   4314  CZ2 TRP A 574      41.514  54.835  39.153  1.00 12.90           C  
ATOM   4315  CZ3 TRP A 574      43.929  54.674  39.083  1.00 15.39           C  
ATOM   4316  CH2 TRP A 574      42.684  54.783  38.442  1.00 15.57           C  
ATOM   4317  N   PRO A 575      44.599  57.271  42.179  1.00 19.18           N  
ATOM   4318  CA  PRO A 575      45.409  57.748  41.052  1.00 20.80           C  
ATOM   4319  C   PRO A 575      46.813  58.182  41.485  1.00 21.70           C  
ATOM   4320  O   PRO A 575      47.751  58.138  40.697  1.00 20.53           O  
ATOM   4321  CB  PRO A 575      44.583  58.910  40.507  1.00 20.75           C  
ATOM   4322  CG  PRO A 575      43.184  58.426  40.733  1.00 20.74           C  
ATOM   4323  CD  PRO A 575      43.257  57.880  42.148  1.00 18.96           C  
ATOM   4324  N   GLU A 576      46.951  58.596  42.742  1.00 22.05           N  
ATOM   4325  CA  GLU A 576      48.250  59.020  43.250  1.00 23.78           C  
ATOM   4326  C   GLU A 576      49.197  57.838  43.367  1.00 23.11           C  
ATOM   4327  O   GLU A 576      50.370  57.949  43.017  1.00 22.68           O  
ATOM   4328  CB  GLU A 576      48.102  59.712  44.606  1.00 24.14           C  
ATOM   4329  CG  GLU A 576      47.576  61.128  44.482  1.00 30.40           C  
ATOM   4330  CD  GLU A 576      47.542  61.858  45.811  1.00 32.85           C  
ATOM   4331  OE1 GLU A 576      48.566  61.837  46.530  1.00 33.25           O  
ATOM   4332  OE2 GLU A 576      46.493  62.457  46.127  1.00 34.78           O  
ATOM   4333  N   ALA A 577      48.691  56.711  43.861  1.00 20.59           N  
ATOM   4334  CA  ALA A 577      49.514  55.513  43.984  1.00 21.79           C  
ATOM   4335  C   ALA A 577      49.854  55.014  42.575  1.00 20.36           C  
ATOM   4336  O   ALA A 577      50.941  54.484  42.341  1.00 20.96           O  
ATOM   4337  CB  ALA A 577      48.766  54.431  44.770  1.00 19.65           C  
ATOM   4338  N   MET A 578      48.922  55.191  41.641  1.00 19.66           N  
ATOM   4339  CA  MET A 578      49.139  54.772  40.257  1.00 19.69           C  
ATOM   4340  C   MET A 578      50.266  55.601  39.658  1.00 21.29           C  
ATOM   4341  O   MET A 578      51.131  55.080  38.956  1.00 21.89           O  
ATOM   4342  CB  MET A 578      47.873  54.978  39.425  1.00 19.14           C  
ATOM   4343  CG  MET A 578      48.052  54.689  37.933  1.00 17.12           C  
ATOM   4344  SD  MET A 578      48.510  52.964  37.574  1.00 19.73           S  
ATOM   4345  CE  MET A 578      46.861  52.188  37.611  1.00 15.34           C  
ATOM   4346  N   GLN A 579      50.244  56.899  39.945  1.00 22.60           N  
ATOM   4347  CA  GLN A 579      51.254  57.820  39.444  1.00 24.68           C  
ATOM   4348  C   GLN A 579      52.628  57.493  40.018  1.00 25.43           C  
ATOM   4349  O   GLN A 579      53.626  57.492  39.297  1.00 26.39           O  
ATOM   4350  CB  GLN A 579      50.880  59.253  39.810  1.00 28.02           C  
ATOM   4351  CG  GLN A 579      51.680  60.294  39.059  1.00 32.26           C  
ATOM   4352  CD  GLN A 579      50.791  61.215  38.261  1.00 34.82           C  
ATOM   4353  OE1 GLN A 579      50.166  62.126  38.805  1.00 37.92           O  
ATOM   4354  NE2 GLN A 579      50.709  60.969  36.962  1.00 39.74           N  
ATOM   4355  N   LEU A 580      52.677  57.221  41.318  1.00 25.09           N  
ATOM   4356  CA  LEU A 580      53.936  56.889  41.976  1.00 26.89           C  
ATOM   4357  C   LEU A 580      54.624  55.677  41.357  1.00 25.11           C  
ATOM   4358  O   LEU A 580      55.850  55.622  41.271  1.00 25.06           O  
ATOM   4359  CB  LEU A 580      53.704  56.624  43.466  1.00 28.27           C  
ATOM   4360  CG  LEU A 580      53.394  57.852  44.319  1.00 30.25           C  
ATOM   4361  CD1 LEU A 580      53.105  57.417  45.742  1.00 30.76           C  
ATOM   4362  CD2 LEU A 580      54.577  58.818  44.279  1.00 30.95           C  
ATOM   4363  N   ILE A 581      53.834  54.703  40.928  1.00 23.32           N  
ATOM   4364  CA  ILE A 581      54.394  53.497  40.339  1.00 22.85           C  
ATOM   4365  C   ILE A 581      54.678  53.607  38.844  1.00 22.85           C  
ATOM   4366  O   ILE A 581      55.739  53.187  38.380  1.00 23.82           O  
ATOM   4367  CB  ILE A 581      53.449  52.286  40.530  1.00 23.45           C  
ATOM   4368  CG1 ILE A 581      53.216  52.018  42.017  1.00 24.83           C  
ATOM   4369  CG2 ILE A 581      54.042  51.054  39.856  1.00 24.69           C  
ATOM   4370  CD1 ILE A 581      52.078  51.033  42.285  1.00 23.21           C  
ATOM   4371  N   THR A 582      53.736  54.179  38.099  1.00 22.01           N  
ATOM   4372  CA  THR A 582      53.846  54.262  36.642  1.00 22.05           C  
ATOM   4373  C   THR A 582      54.164  55.608  35.989  1.00 22.43           C  
ATOM   4374  O   THR A 582      54.456  55.660  34.796  1.00 22.71           O  
ATOM   4375  CB  THR A 582      52.552  53.740  35.993  1.00 20.57           C  
ATOM   4376  OG1 THR A 582      51.498  54.680  36.225  1.00 19.96           O  
ATOM   4377  CG2 THR A 582      52.151  52.397  36.600  1.00 17.72           C  
ATOM   4378  N   GLY A 583      54.095  56.696  36.743  1.00 24.21           N  
ATOM   4379  CA  GLY A 583      54.392  57.987  36.150  1.00 22.90           C  
ATOM   4380  C   GLY A 583      53.188  58.640  35.501  1.00 22.97           C  
ATOM   4381  O   GLY A 583      53.294  59.729  34.937  1.00 21.49           O  
ATOM   4382  N   GLN A 584      52.046  57.962  35.554  1.00 23.88           N  
ATOM   4383  CA  GLN A 584      50.802  58.502  35.012  1.00 21.95           C  
ATOM   4384  C   GLN A 584      49.689  58.095  35.989  1.00 20.81           C  
ATOM   4385  O   GLN A 584      49.891  57.215  36.825  1.00 20.69           O  
ATOM   4386  CB  GLN A 584      50.581  58.015  33.574  1.00 22.47           C  
ATOM   4387  CG  GLN A 584      50.505  56.523  33.379  1.00 22.03           C  
ATOM   4388  CD  GLN A 584      49.156  55.988  33.763  1.00 19.05           C  
ATOM   4389  OE1 GLN A 584      48.129  56.540  33.362  1.00 19.51           O  
ATOM   4390  NE2 GLN A 584      49.141  54.908  34.537  1.00 16.18           N  
ATOM   4391  N   PRO A 585      48.502  58.716  35.897  1.00 19.66           N  
ATOM   4392  CA  PRO A 585      47.427  58.379  36.836  1.00 20.55           C  
ATOM   4393  C   PRO A 585      46.267  57.457  36.457  1.00 19.89           C  
ATOM   4394  O   PRO A 585      45.445  57.136  37.314  1.00 19.50           O  
ATOM   4395  CB  PRO A 585      46.908  59.751  37.209  1.00 20.89           C  
ATOM   4396  CG  PRO A 585      46.873  60.418  35.835  1.00 20.78           C  
ATOM   4397  CD  PRO A 585      48.157  59.932  35.138  1.00 21.70           C  
ATOM   4398  N   ASN A 586      46.183  57.029  35.206  1.00 18.92           N  
ATOM   4399  CA  ASN A 586      45.051  56.199  34.799  1.00 20.34           C  
ATOM   4400  C   ASN A 586      45.303  54.708  34.664  1.00 17.45           C  
ATOM   4401  O   ASN A 586      46.445  54.250  34.621  1.00 17.50           O  
ATOM   4402  CB  ASN A 586      44.498  56.699  33.462  1.00 23.41           C  
ATOM   4403  CG  ASN A 586      44.426  58.205  33.391  1.00 26.99           C  
ATOM   4404  OD1 ASN A 586      44.083  58.855  34.377  1.00 31.32           O  
ATOM   4405  ND2 ASN A 586      44.732  58.761  32.219  1.00 31.42           N  
ATOM   4406  N   MET A 587      44.208  53.957  34.603  1.00 16.22           N  
ATOM   4407  CA  MET A 587      44.279  52.520  34.387  1.00 17.60           C  
ATOM   4408  C   MET A 587      44.402  52.465  32.872  1.00 16.95           C  
ATOM   4409  O   MET A 587      43.843  53.315  32.178  1.00 16.75           O  
ATOM   4410  CB  MET A 587      42.982  51.821  34.807  1.00 14.99           C  
ATOM   4411  CG  MET A 587      42.792  51.646  36.305  1.00 15.84           C  
ATOM   4412  SD  MET A 587      41.282  50.709  36.700  1.00 17.39           S  
ATOM   4413  CE  MET A 587      40.045  51.984  36.543  1.00 20.05           C  
ATOM   4414  N   SER A 588      45.117  51.480  32.351  1.00 16.04           N  
ATOM   4415  CA  SER A 588      45.286  51.385  30.904  1.00 16.02           C  
ATOM   4416  C   SER A 588      45.617  49.965  30.495  1.00 15.40           C  
ATOM   4417  O   SER A 588      46.400  49.297  31.161  1.00 14.10           O  
ATOM   4418  CB  SER A 588      46.420  52.314  30.449  1.00 16.02           C  
ATOM   4419  OG  SER A 588      46.691  52.155  29.067  1.00 19.66           O  
ATOM   4420  N   ALA A 589      45.024  49.516  29.392  1.00 15.67           N  
ATOM   4421  CA  ALA A 589      45.265  48.173  28.880  1.00 17.19           C  
ATOM   4422  C   ALA A 589      46.509  48.124  27.991  1.00 17.50           C  
ATOM   4423  O   ALA A 589      46.909  47.052  27.533  1.00 16.59           O  
ATOM   4424  CB  ALA A 589      44.053  47.695  28.092  1.00 15.24           C  
ATOM   4425  N   SER A 590      47.124  49.282  27.755  1.00 19.02           N  
ATOM   4426  CA  SER A 590      48.310  49.356  26.896  1.00 20.17           C  
ATOM   4427  C   SER A 590      49.443  48.420  27.296  1.00 18.71           C  
ATOM   4428  O   SER A 590      50.023  47.752  26.448  1.00 19.01           O  
ATOM   4429  CB  SER A 590      48.839  50.791  26.838  1.00 19.94           C  
ATOM   4430  OG  SER A 590      47.940  51.611  26.112  1.00 28.11           O  
ATOM   4431  N   ALA A 591      49.761  48.373  28.584  1.00 18.30           N  
ATOM   4432  CA  ALA A 591      50.841  47.513  29.060  1.00 17.71           C  
ATOM   4433  C   ALA A 591      50.554  46.034  28.784  1.00 16.19           C  
ATOM   4434  O   ALA A 591      51.410  45.305  28.271  1.00 16.07           O  
ATOM   4435  CB  ALA A 591      51.067  47.741  30.557  1.00 17.13           C  
ATOM   4436  N   MET A 592      49.350  45.591  29.122  1.00 15.56           N  
ATOM   4437  CA  MET A 592      48.974  44.202  28.899  1.00 15.10           C  
ATOM   4438  C   MET A 592      49.008  43.868  27.402  1.00 16.05           C  
ATOM   4439  O   MET A 592      49.480  42.802  27.012  1.00 17.32           O  
ATOM   4440  CB  MET A 592      47.580  43.931  29.475  1.00 15.03           C  
ATOM   4441  CG  MET A 592      47.133  42.489  29.348  1.00 18.59           C  
ATOM   4442  SD  MET A 592      45.530  42.188  30.123  1.00 19.23           S  
ATOM   4443  CE  MET A 592      45.854  40.606  30.925  1.00 19.84           C  
ATOM   4444  N   LEU A 593      48.508  44.774  26.566  1.00 15.21           N  
ATOM   4445  CA  LEU A 593      48.515  44.543  25.120  1.00 18.46           C  
ATOM   4446  C   LEU A 593      49.956  44.487  24.598  1.00 19.43           C  
ATOM   4447  O   LEU A 593      50.295  43.655  23.751  1.00 18.79           O  
ATOM   4448  CB  LEU A 593      47.735  45.649  24.396  1.00 19.41           C  
ATOM   4449  CG  LEU A 593      46.220  45.664  24.628  1.00 22.76           C  
ATOM   4450  CD1 LEU A 593      45.576  46.786  23.827  1.00 21.15           C  
ATOM   4451  CD2 LEU A 593      45.634  44.315  24.214  1.00 24.62           C  
ATOM   4452  N   SER A 594      50.802  45.375  25.112  1.00 19.19           N  
ATOM   4453  CA  SER A 594      52.208  45.418  24.717  1.00 19.92           C  
ATOM   4454  C   SER A 594      52.892  44.100  25.113  1.00 18.98           C  
ATOM   4455  O   SER A 594      53.667  43.525  24.345  1.00 19.48           O  
ATOM   4456  CB  SER A 594      52.891  46.612  25.402  1.00 22.10           C  
ATOM   4457  OG  SER A 594      54.286  46.618  25.176  1.00 27.80           O  
ATOM   4458  N   TYR A 595      52.600  43.623  26.316  1.00 17.23           N  
ATOM   4459  CA  TYR A 595      53.169  42.370  26.803  1.00 17.45           C  
ATOM   4460  C   TYR A 595      52.820  41.206  25.858  1.00 18.35           C  
ATOM   4461  O   TYR A 595      53.676  40.379  25.534  1.00 17.96           O  
ATOM   4462  CB  TYR A 595      52.626  42.070  28.203  1.00 17.03           C  
ATOM   4463  CG  TYR A 595      53.131  40.783  28.824  1.00 16.24           C  
ATOM   4464  CD1 TYR A 595      54.122  40.798  29.806  1.00 18.36           C  
ATOM   4465  CD2 TYR A 595      52.590  39.551  28.454  1.00 16.60           C  
ATOM   4466  CE1 TYR A 595      54.560  39.612  30.412  1.00 16.21           C  
ATOM   4467  CE2 TYR A 595      53.018  38.367  29.046  1.00 15.67           C  
ATOM   4468  CZ  TYR A 595      53.998  38.402  30.026  1.00 17.59           C  
ATOM   4469  OH  TYR A 595      54.385  37.225  30.630  1.00 17.16           O  
ATOM   4470  N   PHE A 596      51.564  41.151  25.416  1.00 17.36           N  
ATOM   4471  CA  PHE A 596      51.108  40.071  24.538  1.00 18.59           C  
ATOM   4472  C   PHE A 596      51.151  40.323  23.030  1.00 18.84           C  
ATOM   4473  O   PHE A 596      50.741  39.464  22.254  1.00 19.04           O  
ATOM   4474  CB  PHE A 596      49.679  39.657  24.914  1.00 15.88           C  
ATOM   4475  CG  PHE A 596      49.585  38.913  26.208  1.00 15.40           C  
ATOM   4476  CD1 PHE A 596      49.150  39.552  27.366  1.00 15.71           C  
ATOM   4477  CD2 PHE A 596      49.952  37.573  26.278  1.00 15.04           C  
ATOM   4478  CE1 PHE A 596      49.081  38.864  28.579  1.00 14.00           C  
ATOM   4479  CE2 PHE A 596      49.889  36.874  27.483  1.00 15.01           C  
ATOM   4480  CZ  PHE A 596      49.453  37.519  28.636  1.00 14.97           C  
ATOM   4481  N   LYS A 597      51.644  41.484  22.612  1.00 19.54           N  
ATOM   4482  CA  LYS A 597      51.705  41.819  21.190  1.00 19.75           C  
ATOM   4483  C   LYS A 597      52.217  40.692  20.283  1.00 20.01           C  
ATOM   4484  O   LYS A 597      51.584  40.365  19.281  1.00 21.94           O  
ATOM   4485  CB  LYS A 597      52.556  43.079  20.989  1.00 22.03           C  
ATOM   4486  CG  LYS A 597      52.868  43.419  19.532  1.00 23.91           C  
ATOM   4487  CD  LYS A 597      51.621  43.760  18.727  1.00 27.23           C  
ATOM   4488  CE  LYS A 597      52.002  44.196  17.306  1.00 30.31           C  
ATOM   4489  NZ  LYS A 597      50.817  44.449  16.440  1.00 30.49           N  
ATOM   4490  N   PRO A 598      53.369  40.087  20.611  1.00 20.55           N  
ATOM   4491  CA  PRO A 598      53.867  39.008  19.749  1.00 21.49           C  
ATOM   4492  C   PRO A 598      52.857  37.867  19.613  1.00 20.35           C  
ATOM   4493  O   PRO A 598      52.732  37.256  18.553  1.00 19.97           O  
ATOM   4494  CB  PRO A 598      55.151  38.566  20.450  1.00 21.82           C  
ATOM   4495  CG  PRO A 598      55.607  39.818  21.155  1.00 23.13           C  
ATOM   4496  CD  PRO A 598      54.306  40.351  21.717  1.00 22.46           C  
ATOM   4497  N   LEU A 599      52.131  37.583  20.687  1.00 19.10           N  
ATOM   4498  CA  LEU A 599      51.150  36.510  20.649  1.00 18.86           C  
ATOM   4499  C   LEU A 599      49.945  36.906  19.807  1.00 18.76           C  
ATOM   4500  O   LEU A 599      49.448  36.106  19.016  1.00 20.28           O  
ATOM   4501  CB  LEU A 599      50.695  36.135  22.059  1.00 17.73           C  
ATOM   4502  CG  LEU A 599      49.725  34.946  22.116  1.00 18.16           C  
ATOM   4503  CD1 LEU A 599      50.447  33.682  21.698  1.00 17.06           C  
ATOM   4504  CD2 LEU A 599      49.167  34.789  23.525  1.00 17.08           C  
ATOM   4505  N   LEU A 600      49.480  38.140  19.972  1.00 18.81           N  
ATOM   4506  CA  LEU A 600      48.332  38.617  19.207  1.00 19.95           C  
ATOM   4507  C   LEU A 600      48.599  38.482  17.709  1.00 21.61           C  
ATOM   4508  O   LEU A 600      47.725  38.048  16.955  1.00 18.83           O  
ATOM   4509  CB  LEU A 600      48.025  40.079  19.543  1.00 18.70           C  
ATOM   4510  CG  LEU A 600      46.896  40.731  18.735  1.00 21.74           C  
ATOM   4511  CD1 LEU A 600      45.584  40.002  18.990  1.00 23.52           C  
ATOM   4512  CD2 LEU A 600      46.766  42.196  19.119  1.00 22.39           C  
ATOM   4513  N   ASP A 601      49.804  38.855  17.281  1.00 21.33           N  
ATOM   4514  CA  ASP A 601      50.160  38.756  15.869  1.00 21.95           C  
ATOM   4515  C   ASP A 601      50.197  37.293  15.425  1.00 21.32           C  
ATOM   4516  O   ASP A 601      49.742  36.964  14.330  1.00 20.49           O  
ATOM   4517  CB  ASP A 601      51.525  39.405  15.604  1.00 23.60           C  
ATOM   4518  CG  ASP A 601      51.516  40.903  15.839  1.00 24.22           C  
ATOM   4519  OD1 ASP A 601      50.469  41.541  15.604  1.00 26.63           O  
ATOM   4520  OD2 ASP A 601      52.562  41.447  16.243  1.00 26.55           O  
ATOM   4521  N   TRP A 602      50.736  36.418  16.271  1.00 19.81           N  
ATOM   4522  CA  TRP A 602      50.808  34.998  15.929  1.00 20.07           C  
ATOM   4523  C   TRP A 602      49.402  34.407  15.817  1.00 20.16           C  
ATOM   4524  O   TRP A 602      49.120  33.624  14.908  1.00 20.21           O  
ATOM   4525  CB  TRP A 602      51.595  34.213  16.987  1.00 19.94           C  
ATOM   4526  CG  TRP A 602      51.761  32.756  16.632  1.00 21.13           C  
ATOM   4527  CD1 TRP A 602      52.712  32.211  15.807  1.00 22.30           C  
ATOM   4528  CD2 TRP A 602      50.902  31.674  17.019  1.00 21.92           C  
ATOM   4529  NE1 TRP A 602      52.492  30.860  15.656  1.00 21.61           N  
ATOM   4530  CE2 TRP A 602      51.389  30.505  16.388  1.00 22.13           C  
ATOM   4531  CE3 TRP A 602      49.766  31.578  17.836  1.00 22.40           C  
ATOM   4532  CZ2 TRP A 602      50.779  29.255  16.549  1.00 22.73           C  
ATOM   4533  CZ3 TRP A 602      49.158  30.333  17.996  1.00 23.58           C  
ATOM   4534  CH2 TRP A 602      49.669  29.189  17.354  1.00 24.12           C  
ATOM   4535  N   LEU A 603      48.528  34.788  16.745  1.00 18.10           N  
ATOM   4536  CA  LEU A 603      47.152  34.291  16.767  1.00 17.96           C  
ATOM   4537  C   LEU A 603      46.358  34.720  15.543  1.00 17.44           C  
ATOM   4538  O   LEU A 603      45.597  33.934  14.982  1.00 18.04           O  
ATOM   4539  CB  LEU A 603      46.433  34.766  18.033  1.00 13.19           C  
ATOM   4540  CG  LEU A 603      46.823  34.058  19.331  1.00 15.98           C  
ATOM   4541  CD1 LEU A 603      46.121  34.731  20.512  1.00 15.76           C  
ATOM   4542  CD2 LEU A 603      46.433  32.585  19.242  1.00 17.65           C  
ATOM   4543  N   ARG A 604      46.522  35.971  15.135  1.00 19.17           N  
ATOM   4544  CA  ARG A 604      45.809  36.459  13.965  1.00 20.10           C  
ATOM   4545  C   ARG A 604      46.240  35.688  12.728  1.00 19.78           C  
ATOM   4546  O   ARG A 604      45.404  35.275  11.930  1.00 19.55           O  
ATOM   4547  CB  ARG A 604      46.057  37.955  13.776  1.00 21.85           C  
ATOM   4548  CG  ARG A 604      45.154  38.812  14.644  1.00 25.01           C  
ATOM   4549  CD  ARG A 604      45.529  40.272  14.572  1.00 29.62           C  
ATOM   4550  NE  ARG A 604      44.548  41.106  15.260  1.00 33.26           N  
ATOM   4551  CZ  ARG A 604      44.745  42.381  15.571  1.00 34.54           C  
ATOM   4552  NH1 ARG A 604      45.895  42.969  15.259  1.00 35.00           N  
ATOM   4553  NH2 ARG A 604      43.791  43.069  16.185  1.00 36.75           N  
ATOM   4554  N   THR A 605      47.544  35.485  12.577  1.00 20.54           N  
ATOM   4555  CA  THR A 605      48.067  34.745  11.431  1.00 21.78           C  
ATOM   4556  C   THR A 605      47.579  33.296  11.463  1.00 20.62           C  
ATOM   4557  O   THR A 605      47.170  32.747  10.439  1.00 19.63           O  
ATOM   4558  CB  THR A 605      49.604  34.749  11.430  1.00 22.60           C  
ATOM   4559  OG1 THR A 605      50.072  36.101  11.362  1.00 26.06           O  
ATOM   4560  CG2 THR A 605      50.142  33.960  10.241  1.00 23.85           C  
ATOM   4561  N   GLU A 606      47.619  32.684  12.643  1.00 19.42           N  
ATOM   4562  CA  GLU A 606      47.176  31.299  12.804  1.00 18.86           C  
ATOM   4563  C   GLU A 606      45.676  31.152  12.553  1.00 17.40           C  
ATOM   4564  O   GLU A 606      45.258  30.279  11.794  1.00 18.84           O  
ATOM   4565  CB  GLU A 606      47.517  30.791  14.211  1.00 19.68           C  
ATOM   4566  CG  GLU A 606      46.993  29.385  14.533  1.00 20.95           C  
ATOM   4567  CD  GLU A 606      47.704  28.278  13.757  1.00 24.76           C  
ATOM   4568  OE1 GLU A 606      48.584  28.589  12.924  1.00 25.29           O  
ATOM   4569  OE2 GLU A 606      47.379  27.091  13.984  1.00 25.20           O  
ATOM   4570  N   ASN A 607      44.867  32.001  13.183  1.00 17.45           N  
ATOM   4571  CA  ASN A 607      43.416  31.928  13.006  1.00 17.49           C  
ATOM   4572  C   ASN A 607      43.015  32.235  11.571  1.00 18.74           C  
ATOM   4573  O   ASN A 607      42.067  31.655  11.039  1.00 16.61           O  
ATOM   4574  CB  ASN A 607      42.691  32.889  13.962  1.00 15.50           C  
ATOM   4575  CG  ASN A 607      42.730  32.411  15.408  1.00 16.54           C  
ATOM   4576  OD1 ASN A 607      42.820  31.209  15.674  1.00 15.31           O  
ATOM   4577  ND2 ASN A 607      42.652  33.348  16.348  1.00 12.94           N  
ATOM   4578  N   GLU A 608      43.748  33.147  10.944  1.00 20.32           N  
ATOM   4579  CA  GLU A 608      43.468  33.530   9.566  1.00 22.55           C  
ATOM   4580  C   GLU A 608      43.703  32.382   8.581  1.00 22.09           C  
ATOM   4581  O   GLU A 608      42.873  32.118   7.712  1.00 21.43           O  
ATOM   4582  CB  GLU A 608      44.335  34.729   9.178  1.00 23.65           C  
ATOM   4583  CG  GLU A 608      44.290  35.079   7.704  1.00 30.44           C  
ATOM   4584  CD  GLU A 608      45.149  36.284   7.386  1.00 33.49           C  
ATOM   4585  OE1 GLU A 608      44.809  37.389   7.863  1.00 34.20           O  
ATOM   4586  OE2 GLU A 608      46.166  36.122   6.675  1.00 33.48           O  
ATOM   4587  N   LEU A 609      44.825  31.688   8.722  1.00 22.49           N  
ATOM   4588  CA  LEU A 609      45.118  30.600   7.801  1.00 24.32           C  
ATOM   4589  C   LEU A 609      44.149  29.426   7.953  1.00 23.29           C  
ATOM   4590  O   LEU A 609      43.985  28.631   7.027  1.00 22.55           O  
ATOM   4591  CB  LEU A 609      46.576  30.150   7.956  1.00 25.56           C  
ATOM   4592  CG  LEU A 609      47.046  29.348   9.162  1.00 26.95           C  
ATOM   4593  CD1 LEU A 609      46.720  27.878   8.949  1.00 27.03           C  
ATOM   4594  CD2 LEU A 609      48.555  29.519   9.316  1.00 29.34           C  
ATOM   4595  N   HIS A 610      43.495  29.327   9.110  1.00 21.91           N  
ATOM   4596  CA  HIS A 610      42.524  28.263   9.339  1.00 22.74           C  
ATOM   4597  C   HIS A 610      41.106  28.747   9.071  1.00 23.10           C  
ATOM   4598  O   HIS A 610      40.145  27.988   9.217  1.00 22.01           O  
ATOM   4599  CB  HIS A 610      42.622  27.728  10.772  1.00 23.20           C  
ATOM   4600  CG  HIS A 610      43.812  26.856  11.000  1.00 24.45           C  
ATOM   4601  ND1 HIS A 610      44.894  27.252  11.756  1.00 28.28           N  
ATOM   4602  CD2 HIS A 610      44.112  25.623  10.530  1.00 25.66           C  
ATOM   4603  CE1 HIS A 610      45.810  26.301  11.742  1.00 26.29           C  
ATOM   4604  NE2 HIS A 610      45.360  25.302  11.005  1.00 29.81           N  
ATOM   4605  N   GLY A 611      40.986  30.012   8.678  1.00 22.53           N  
ATOM   4606  CA  GLY A 611      39.683  30.582   8.381  1.00 22.30           C  
ATOM   4607  C   GLY A 611      38.729  30.590   9.561  1.00 23.68           C  
ATOM   4608  O   GLY A 611      37.544  30.277   9.416  1.00 22.74           O  
ATOM   4609  N   GLU A 612      39.233  30.950  10.735  1.00 21.41           N  
ATOM   4610  CA  GLU A 612      38.386  30.981  11.919  1.00 21.09           C  
ATOM   4611  C   GLU A 612      37.407  32.147  11.872  1.00 22.46           C  
ATOM   4612  O   GLU A 612      37.727  33.230  11.371  1.00 23.79           O  
ATOM   4613  CB  GLU A 612      39.235  31.103  13.188  1.00 18.57           C  
ATOM   4614  CG  GLU A 612      40.322  30.051  13.336  1.00 18.36           C  
ATOM   4615  CD  GLU A 612      39.780  28.639  13.541  1.00 16.54           C  
ATOM   4616  OE1 GLU A 612      38.545  28.441  13.509  1.00 16.76           O  
ATOM   4617  OE2 GLU A 612      40.604  27.724  13.733  1.00 18.63           O  
ATOM   4618  N   LYS A 613      36.207  31.910  12.386  1.00 21.56           N  
ATOM   4619  CA  LYS A 613      35.180  32.938  12.472  1.00 22.52           C  
ATOM   4620  C   LYS A 613      35.170  33.347  13.940  1.00 22.34           C  
ATOM   4621  O   LYS A 613      34.633  32.626  14.779  1.00 22.63           O  
ATOM   4622  CB  LYS A 613      33.816  32.367  12.090  1.00 25.95           C  
ATOM   4623  CG  LYS A 613      32.662  33.335  12.296  1.00 32.66           C  
ATOM   4624  CD  LYS A 613      31.336  32.666  11.974  1.00 37.37           C  
ATOM   4625  CE  LYS A 613      30.164  33.603  12.192  1.00 38.64           C  
ATOM   4626  NZ  LYS A 613      28.883  32.959  11.777  1.00 42.06           N  
ATOM   4627  N   LEU A 614      35.777  34.490  14.250  1.00 21.01           N  
ATOM   4628  CA  LEU A 614      35.846  34.965  15.630  1.00 21.37           C  
ATOM   4629  C   LEU A 614      34.470  35.217  16.215  1.00 21.96           C  
ATOM   4630  O   LEU A 614      33.546  35.613  15.508  1.00 20.21           O  
ATOM   4631  CB  LEU A 614      36.662  36.251  15.721  1.00 19.95           C  
ATOM   4632  CG  LEU A 614      38.110  36.202  15.233  1.00 21.57           C  
ATOM   4633  CD1 LEU A 614      38.774  37.542  15.513  1.00 22.47           C  
ATOM   4634  CD2 LEU A 614      38.859  35.084  15.927  1.00 19.75           C  
ATOM   4635  N   GLY A 615      34.339  34.987  17.517  1.00 21.25           N  
ATOM   4636  CA  GLY A 615      33.065  35.214  18.167  1.00 20.02           C  
ATOM   4637  C   GLY A 615      32.117  34.037  18.080  1.00 21.85           C  
ATOM   4638  O   GLY A 615      32.516  32.919  17.748  1.00 19.09           O  
ATOM   4639  N   TRP A 616      30.850  34.302  18.369  1.00 22.45           N  
ATOM   4640  CA  TRP A 616      29.828  33.268  18.356  1.00 28.97           C  
ATOM   4641  C   TRP A 616      28.462  33.843  17.983  1.00 34.48           C  
ATOM   4642  O   TRP A 616      27.676  34.217  18.849  1.00 35.78           O  
ATOM   4643  CB  TRP A 616      29.778  32.601  19.734  1.00 23.61           C  
ATOM   4644  CG  TRP A 616      29.902  33.584  20.866  1.00 21.96           C  
ATOM   4645  CD1 TRP A 616      28.883  34.238  21.507  1.00 20.08           C  
ATOM   4646  CD2 TRP A 616      31.119  34.062  21.459  1.00 19.96           C  
ATOM   4647  NE1 TRP A 616      29.392  35.089  22.460  1.00 19.39           N  
ATOM   4648  CE2 TRP A 616      30.761  35.004  22.452  1.00 19.26           C  
ATOM   4649  CE3 TRP A 616      32.480  33.787  21.247  1.00 18.03           C  
ATOM   4650  CZ2 TRP A 616      31.713  35.675  23.231  1.00 17.35           C  
ATOM   4651  CZ3 TRP A 616      33.428  34.453  22.022  1.00 19.00           C  
ATOM   4652  CH2 TRP A 616      33.037  35.389  23.005  1.00 18.89           C  
ATOM   4653  N   PRO A 617      28.166  33.914  16.675  1.00 41.48           N  
ATOM   4654  CA  PRO A 617      26.895  34.443  16.166  1.00 44.45           C  
ATOM   4655  C   PRO A 617      25.679  33.707  16.726  1.00 46.65           C  
ATOM   4656  O   PRO A 617      24.898  34.348  17.458  1.00 48.64           O  
ATOM   4657  CB  PRO A 617      27.033  34.263  14.656  1.00 45.15           C  
ATOM   4658  CG  PRO A 617      27.883  33.024  14.556  1.00 44.87           C  
ATOM   4659  CD  PRO A 617      28.952  33.316  15.580  1.00 42.76           C  
ATOM   4660  N   GLN A 618      25.526  32.501  16.429  1.00 48.70           N  
TER    4661      GLN A 618                                                      
HETATM 4662  C1  NAG A 691      38.666  22.463  66.650  0.50 29.58           C  
HETATM 4663  C2  NAG A 691      39.962  22.246  67.525  0.50 29.55           C  
HETATM 4664  C3  NAG A 691      39.524  21.408  68.772  0.50 29.52           C  
HETATM 4665  C4  NAG A 691      38.496  22.259  69.550  0.50 29.70           C  
HETATM 4666  C5  NAG A 691      37.241  22.504  68.605  0.50 30.07           C  
HETATM 4667  C6  NAG A 691      36.157  23.293  69.219  0.50 28.97           C  
HETATM 4668  C7  NAG A 691      42.209  21.838  66.543  0.50 29.68           C  
HETATM 4669  C8  NAG A 691      43.027  20.911  65.781  0.50 29.38           C  
HETATM 4670  N2  NAG A 691      40.925  21.438  66.776  0.50 28.28           N  
HETATM 4671  O3  NAG A 691      40.679  21.179  69.596  0.50 29.08           O  
HETATM 4672  O4  NAG A 691      38.067  21.525  70.710  0.50 31.81           O  
HETATM 4673  O5  NAG A 691      37.742  23.245  67.408  0.50 28.44           O  
HETATM 4674  O6  NAG A 691      34.965  23.182  68.486  0.50 29.28           O  
HETATM 4675  O7  NAG A 691      42.632  22.844  66.920  0.50 30.40           O  
HETATM 4676  C1  NAG A 692      26.823  46.501  73.110  0.25 30.78           C  
HETATM 4677  C2  NAG A 692      26.060  47.367  74.194  0.25 29.79           C  
HETATM 4678  C3  NAG A 692      26.339  46.684  75.578  0.25 28.68           C  
HETATM 4679  C4  NAG A 692      25.778  45.248  75.517  0.25 28.12           C  
HETATM 4680  C5  NAG A 692      26.546  44.463  74.365  0.25 28.47           C  
HETATM 4681  C6  NAG A 692      26.141  43.054  74.189  0.25 27.89           C  
HETATM 4682  C7  NAG A 692      27.924  49.127  74.485  0.25 29.38           C  
HETATM 4683  C8  NAG A 692      28.176  50.560  74.479  0.25 29.34           C  
HETATM 4684  N2  NAG A 692      26.610  48.755  74.247  0.25 29.38           N  
HETATM 4685  O3  NAG A 692      25.663  47.437  76.598  0.25 28.79           O  
HETATM 4686  O4  NAG A 692      26.031  44.601  76.779  0.25 26.69           O  
HETATM 4687  O5  NAG A 692      26.263  45.191  73.097  0.25 29.85           O  
HETATM 4688  O6  NAG A 692      26.884  42.425  73.176  0.25 25.82           O  
HETATM 4689  O7  NAG A 692      28.778  48.376  74.677  0.25 28.91           O  
HETATM 4690  C1  NAG A 693      45.844  65.857  60.275  0.50 34.64           C  
HETATM 4691  C2  NAG A 693      47.343  66.335  60.338  0.50 33.61           C  
HETATM 4692  C3  NAG A 693      48.225  65.046  60.320  0.50 33.54           C  
HETATM 4693  C4  NAG A 693      47.874  64.228  61.582  0.50 33.12           C  
HETATM 4694  C5  NAG A 693      46.335  63.825  61.490  0.50 32.64           C  
HETATM 4695  C6  NAG A 693      45.829  63.006  62.614  0.50 32.29           C  
HETATM 4696  C7  NAG A 693      47.847  68.449  59.114  0.50 33.80           C  
HETATM 4697  C8  NAG A 693      48.147  69.026  57.814  0.50 33.51           C  
HETATM 4698  N2  NAG A 693      47.658  67.096  59.127  0.50 33.78           N  
HETATM 4699  O3  NAG A 693      49.604  65.442  60.373  0.50 34.37           O  
HETATM 4700  O4  NAG A 693      48.672  63.030  61.597  0.50 32.73           O  
HETATM 4701  O5  NAG A 693      45.563  65.105  61.455  0.50 32.95           O  
HETATM 4702  O6  NAG A 693      46.059  63.613  63.861  0.50 33.79           O  
HETATM 4703  O7  NAG A 693      47.775  69.104  60.061  0.50 34.69           O  
HETATM 4704  C1  NAG A 694      34.333   4.445  43.451  0.50 42.09           C  
HETATM 4705  C2  NAG A 694      35.344   3.237  43.321  0.50 40.59           C  
HETATM 4706  C3  NAG A 694      36.776   3.873  43.266  0.50 40.44           C  
HETATM 4707  C4  NAG A 694      36.837   4.763  42.008  0.50 39.57           C  
HETATM 4708  C5  NAG A 694      35.747   5.912  42.160  0.50 40.19           C  
HETATM 4709  C6  NAG A 694      35.697   6.867  41.038  0.50 39.67           C  
HETATM 4710  C7  NAG A 694      35.390   1.041  44.522  0.50 38.40           C  
HETATM 4711  C8  NAG A 694      35.318   0.390  45.820  0.50 37.85           C  
HETATM 4712  N2  NAG A 694      35.289   2.407  44.534  0.50 39.83           N  
HETATM 4713  O3  NAG A 694      37.745   2.817  43.151  0.50 41.14           O  
HETATM 4714  O4  NAG A 694      38.143   5.361  41.930  0.50 39.45           O  
HETATM 4715  O5  NAG A 694      34.422   5.231  42.261  0.50 40.94           O  
HETATM 4716  O6  NAG A 694      36.230   8.118  41.399  0.50 40.94           O  
HETATM 4717  O7  NAG A 694      35.527   0.432  43.553  0.50 39.01           O  
HETATM 4718  C1  NAG A 695      56.458  28.072  65.509  0.25 31.56           C  
HETATM 4719  C2  NAG A 695      56.666  26.508  65.432  0.25 30.72           C  
HETATM 4720  C3  NAG A 695      56.499  25.969  66.893  0.25 29.54           C  
HETATM 4721  C4  NAG A 695      57.609  26.616  67.754  0.25 29.02           C  
HETATM 4722  C5  NAG A 695      57.392  28.194  67.738  0.25 28.93           C  
HETATM 4723  C6  NAG A 695      58.361  28.972  68.535  0.25 29.26           C  
HETATM 4724  C7  NAG A 695      55.782  25.465  63.341  0.25 29.26           C  
HETATM 4725  C8  NAG A 695      54.608  24.896  62.697  0.25 29.00           C  
HETATM 4726  N2  NAG A 695      55.599  25.907  64.623  0.25 29.43           N  
HETATM 4727  O3  NAG A 695      56.674  24.544  66.875  0.25 30.87           O  
HETATM 4728  O4  NAG A 695      57.485  26.137  69.107  0.25 27.69           O  
HETATM 4729  O5  NAG A 695      57.504  28.627  66.310  0.25 30.15           O  
HETATM 4730  O6  NAG A 695      57.844  30.233  68.885  0.25 30.07           O  
HETATM 4731  O7  NAG A 695      56.794  25.529  62.791  0.25 29.27           O  
HETATM 4732  C1  NAG A 696      43.763  59.783  31.843  0.50 32.65           C  
HETATM 4733  C2  NAG A 696      43.513  59.801  30.283  0.50 33.89           C  
HETATM 4734  C3  NAG A 696      42.464  60.933  30.025  0.50 34.52           C  
HETATM 4735  C4  NAG A 696      41.169  60.556  30.774  0.50 34.29           C  
HETATM 4736  C5  NAG A 696      41.517  60.476  32.322  0.50 33.83           C  
HETATM 4737  C6  NAG A 696      40.400  60.153  33.216  0.50 33.87           C  
HETATM 4738  C7  NAG A 696      45.496  59.327  28.856  0.50 33.72           C  
HETATM 4739  C8  NAG A 696      46.660  59.906  28.211  0.50 33.27           C  
HETATM 4740  N2  NAG A 696      44.730  60.198  29.572  0.50 33.67           N  
HETATM 4741  O3  NAG A 696      42.197  61.001  28.614  0.50 36.84           O  
HETATM 4742  O4  NAG A 696      40.196  61.589  30.553  0.50 36.06           O  
HETATM 4743  O5  NAG A 696      42.537  59.408  32.458  0.50 34.67           O  
HETATM 4744  O6  NAG A 696      40.731  60.434  34.555  0.50 33.99           O  
HETATM 4745  O7  NAG A 696      45.250  58.204  28.755  0.50 33.63           O  
HETATM 4746  C   ACT A 700      42.190  36.698  47.868  1.00 17.87           C  
HETATM 4747  O   ACT A 700      41.942  37.484  46.891  1.00 16.00           O  
HETATM 4748  OXT ACT A 700      43.358  36.429  48.383  1.00 17.41           O  
HETATM 4749  CH3 ACT A 700      41.037  35.966  48.550  1.00 16.17           C  
HETATM 4750 ZN    ZN A 701      43.817  38.308  46.652  1.00 16.34          ZN  
HETATM 4751  N   NXA A 702      41.988  34.537  43.491  1.00 23.47           N  
HETATM 4752  CA  NXA A 702      40.825  34.645  42.578  1.00 24.59           C  
HETATM 4753  C   NXA A 702      39.846  33.467  42.340  1.00 22.86           C  
HETATM 4754  O   NXA A 702      40.179  32.410  43.024  1.00 21.93           O  
HETATM 4755  CB  NXA A 702      41.603  34.810  41.280  1.00 26.22           C  
HETATM 4756  OD1 NXA A 702      42.778  34.136  45.475  1.00 27.34           O  
HETATM 4757  OD2 NXA A 702      40.494  34.478  45.311  1.00 21.85           O  
HETATM 4758  C1  NXA A 702      41.675  34.389  44.805  1.00 25.81           C  
HETATM 4759  OXT NXA A 702      38.793  33.259  41.647  1.00 21.49           O  
HETATM 4760 CL    CL A 703      29.185  28.250  36.073  1.00 16.51          CL  
HETATM 4761 CL    CL A 704      36.287  45.320  44.617  1.00 16.56          CL  
HETATM 4762  O   HOH A2001      45.416  56.601  68.328  1.00 39.64           O  
HETATM 4763  O   HOH A2002      40.962  60.463  74.404  1.00 45.01           O  
HETATM 4764  O   HOH A2003      34.219  51.188  61.855  1.00 27.39           O  
HETATM 4765  O   HOH A2004      41.647  54.559  62.566  1.00 39.79           O  
HETATM 4766  O   HOH A2005      47.542  53.259  64.127  1.00 45.51           O  
HETATM 4767  O   HOH A2006      47.342  55.129  71.525  1.00 41.35           O  
HETATM 4768  O   HOH A2007      44.952  50.165  71.454  1.00 36.16           O  
HETATM 4769  O   HOH A2008      48.253  57.473  71.974  1.00 43.72           O  
HETATM 4770  O   HOH A2009      47.101  46.897  68.781  1.00 45.45           O  
HETATM 4771  O   HOH A2010      48.210  48.061  65.137  1.00 47.07           O  
HETATM 4772  O   HOH A2011      46.946  51.783  70.089  1.00 52.87           O  
HETATM 4773  O   HOH A2012      45.433  45.115  68.057  1.00 34.28           O  
HETATM 4774  O   HOH A2013      34.617  51.206  58.460  1.00 49.36           O  
HETATM 4775  O   HOH A2014      35.351  41.501  68.026  1.00 45.11           O  
HETATM 4776  O   HOH A2015      47.109  42.149  69.895  1.00 45.88           O  
HETATM 4777  O   HOH A2016      39.624  36.468  69.824  1.00 40.01           O  
HETATM 4778  O   HOH A2017      37.884  28.719  70.368  1.00 50.75           O  
HETATM 4779  O   HOH A2018      37.762  33.656  69.811  1.00 40.47           O  
HETATM 4780  O   HOH A2019      35.513  31.206  66.336  1.00 25.73           O  
HETATM 4781  O   HOH A2020      38.960  38.628  60.048  1.00 40.06           O  
HETATM 4782  O   HOH A2021      33.909  34.365  58.131  1.00 39.46           O  
HETATM 4783  O   HOH A2022      37.216  31.175  68.418  1.00 28.64           O  
HETATM 4784  O   HOH A2023      37.195  32.835  54.383  1.00 28.68           O  
HETATM 4785  O   HOH A2024      34.405  49.957  71.786  1.00 35.15           O  
HETATM 4786  O   HOH A2025      42.854  26.577  64.396  1.00 40.89           O  
HETATM 4787  O   HOH A2026      22.934  60.561  60.251  1.00 49.35           O  
HETATM 4788  O   HOH A2027      30.693  20.715  65.019  1.00 32.06           O  
HETATM 4789  O   HOH A2028      36.463  61.861  41.741  1.00 31.97           O  
HETATM 4790  O   HOH A2029      26.653  32.630  69.093  1.00 36.31           O  
HETATM 4791  O   HOH A2030      21.758  53.622  63.516  1.00 46.95           O  
HETATM 4792  O   HOH A2031      26.175  37.519  64.945  1.00 35.81           O  
HETATM 4793  O   HOH A2032      15.347  36.178  62.387  1.00 48.01           O  
HETATM 4794  O   HOH A2033      18.673  33.165  61.660  1.00 40.84           O  
HETATM 4795  O   HOH A2034      15.708  33.122  54.732  1.00 44.11           O  
HETATM 4796  O   HOH A2035      17.907  30.515  55.600  1.00 52.02           O  
HETATM 4797  O   HOH A2036      32.053  46.154  71.549  1.00 34.74           O  
HETATM 4798  O   HOH A2037      35.232  41.723  71.023  1.00 46.74           O  
HETATM 4799  O   HOH A2038      26.442  21.223  54.177  1.00 26.91           O  
HETATM 4800  O   HOH A2039      23.863  21.524  53.424  1.00 45.78           O  
HETATM 4801  O   HOH A2040      26.970  50.327  70.960  1.00 48.12           O  
HETATM 4802  O   HOH A2041      34.529  49.050  63.729  1.00 32.80           O  
HETATM 4803  O   HOH A2042      30.780  45.800  61.426  1.00 46.24           O  
HETATM 4804  O   HOH A2043      37.328  23.957  49.049  1.00 45.36           O  
HETATM 4805  O   HOH A2044      44.801  17.250  50.502  1.00 43.13           O  
HETATM 4806  O   HOH A2045      27.864  56.624  70.138  1.00 27.58           O  
HETATM 4807  O   HOH A2046      35.280  52.569  73.408  1.00 30.56           O  
HETATM 4808  O   HOH A2047      47.611  17.171  32.905  1.00 43.63           O  
HETATM 4809  O   HOH A2048      24.548  59.962  64.794  1.00 38.37           O  
HETATM 4810  O   HOH A2049      41.767  10.738  28.096  1.00 41.34           O  
HETATM 4811  O   HOH A2050      29.617  62.035  68.933  1.00 44.43           O  
HETATM 4812  O   HOH A2051      39.040  11.571  36.195  1.00 42.49           O  
HETATM 4813  O   HOH A2052      41.241   9.964  32.536  1.00 31.00           O  
HETATM 4814  O   HOH A2053      33.636  10.725  25.760  1.00 26.11           O  
HETATM 4815  O   HOH A2054      27.158  15.637  24.932  1.00 39.41           O  
HETATM 4816  O   HOH A2055      23.539  62.135  63.215  1.00 37.75           O  
HETATM 4817  O   HOH A2056      22.997  57.578  62.984  1.00 48.56           O  
HETATM 4818  O   HOH A2057      23.670  20.267  50.750  1.00 41.28           O  
HETATM 4819  O   HOH A2058      26.829  13.900  42.000  1.00 51.60           O  
HETATM 4820  O   HOH A2059      29.220  64.769  57.769  1.00 33.69           O  
HETATM 4821  O   HOH A2060      14.280  32.060  49.325  1.00 38.28           O  
HETATM 4822  O   HOH A2061      21.105  21.857  50.569  1.00 43.38           O  
HETATM 4823  O   HOH A2062      14.570  30.169  45.086  1.00 42.30           O  
HETATM 4824  O   HOH A2063      15.358  27.450  47.492  1.00 49.59           O  
HETATM 4825  O   HOH A2064      18.223  23.257  49.730  1.00 49.11           O  
HETATM 4826  O   HOH A2065      15.603  41.927  47.692  1.00 28.52           O  
HETATM 4827  O   HOH A2066      13.964  38.077  47.755  1.00 37.02           O  
HETATM 4828  O   HOH A2067      24.717  29.196  23.868  1.00 34.46           O  
HETATM 4829  O   HOH A2068      28.513  45.956  53.486  1.00 46.34           O  
HETATM 4830  O   HOH A2069      12.571  50.793  52.116  0.50 33.17           O  
HETATM 4831  O   HOH A2070      14.863  50.906  47.090  1.00 49.79           O  
HETATM 4832  O   HOH A2071      44.630  68.730  56.107  1.00 44.36           O  
HETATM 4833  O   HOH A2072      43.806  63.606  53.022  1.00 40.90           O  
HETATM 4834  O   HOH A2073      39.632  64.246  53.049  1.00 38.41           O  
HETATM 4835  O   HOH A2074      29.885  56.396  44.858  1.00 36.90           O  
HETATM 4836  O   HOH A2075      47.217  61.277  55.003  1.00 50.60           O  
HETATM 4837  O   HOH A2076      31.973  57.138  43.492  1.00 43.69           O  
HETATM 4838  O   HOH A2077      33.925  58.939  47.024  1.00 34.77           O  
HETATM 4839  O   HOH A2078      37.687  60.192  39.575  1.00 27.92           O  
HETATM 4840  O   HOH A2079      40.345  57.934  37.750  1.00 22.44           O  
HETATM 4841  O   HOH A2080      38.408  61.853  51.628  1.00 49.43           O  
HETATM 4842  O   HOH A2081      24.692  47.272  35.502  1.00 33.10           O  
HETATM 4843  O   HOH A2082      29.160  51.597  30.888  1.00 35.51           O  
HETATM 4844  O   HOH A2083      35.115  51.055  23.889  1.00 51.05           O  
HETATM 4845  O   HOH A2084      30.541  57.150  54.431  1.00 24.55           O  
HETATM 4846  O   HOH A2085      37.483  51.842  59.120  1.00 44.97           O  
HETATM 4847  O   HOH A2086      44.282  44.869  20.284  1.00 42.34           O  
HETATM 4848  O   HOH A2087      40.319  47.450  20.023  1.00 43.96           O  
HETATM 4849  O   HOH A2088      31.959  52.844  61.725  1.00 48.88           O  
HETATM 4850  O   HOH A2089      28.989  59.107  55.188  1.00 46.96           O  
HETATM 4851  O   HOH A2090      30.997  50.156  52.375  1.00 35.44           O  
HETATM 4852  O   HOH A2091      27.658  50.202  53.322  1.00 36.66           O  
HETATM 4853  O   HOH A2092      29.328  44.418  56.243  1.00 29.76           O  
HETATM 4854  O   HOH A2093      30.841  37.131  59.111  1.00 46.56           O  
HETATM 4855  O   HOH A2094      28.164  21.093  19.000  1.00 34.17           O  
HETATM 4856  O   HOH A2095      32.611  15.277  10.991  1.00 42.44           O  
HETATM 4857  O   HOH A2096      20.943  52.359  61.162  1.00 36.05           O  
HETATM 4858  O   HOH A2097      18.820  50.334  62.005  1.00 36.58           O  
HETATM 4859  O   HOH A2098      17.538  36.873  63.382  1.00 49.19           O  
HETATM 4860  O   HOH A2099      15.582  44.034  65.703  1.00 31.07           O  
HETATM 4861  O   HOH A2100      13.998  44.255  63.276  1.00 37.79           O  
HETATM 4862  O   HOH A2101      24.093  35.444  64.264  1.00 35.01           O  
HETATM 4863  O   HOH A2102      14.328  39.153  57.579  1.00 40.69           O  
HETATM 4864  O   HOH A2103      17.332  33.459  57.443  1.00 41.72           O  
HETATM 4865  O   HOH A2104      20.021  33.589  59.004  1.00 30.36           O  
HETATM 4866  O   HOH A2105      15.164  38.822  61.336  1.00 46.35           O  
HETATM 4867  O   HOH A2106      13.466  35.511  57.867  1.00 42.68           O  
HETATM 4868  O   HOH A2107      28.448  42.954  54.380  1.00 36.53           O  
HETATM 4869  O   HOH A2108      28.874  35.834  60.109  1.00 39.03           O  
HETATM 4870  O   HOH A2109      20.479  31.153  57.519  1.00 37.20           O  
HETATM 4871  O   HOH A2110      25.317  25.265  57.780  1.00 47.77           O  
HETATM 4872  O   HOH A2111      28.976  26.719  60.440  1.00 42.03           O  
HETATM 4873  O   HOH A2112      23.466  24.199  53.649  1.00 29.72           O  
HETATM 4874  O   HOH A2113      27.472  21.519  51.557  1.00 21.90           O  
HETATM 4875  O   HOH A2114      26.547  23.240  56.068  1.00 41.06           O  
HETATM 4876  O   HOH A2115      34.742  23.791  49.020  1.00 25.74           O  
HETATM 4877  O   HOH A2116      37.109  27.771  45.829  1.00 18.94           O  
HETATM 4878  O   HOH A2117      34.677  20.856  49.093  1.00 29.57           O  
HETATM 4879  O   HOH A2118      56.432  43.982  59.555  1.00 39.42           O  
HETATM 4880  O   HOH A2119      61.241  43.880  58.980  1.00 42.97           O  
HETATM 4881  O   HOH A2120      27.817  17.957  50.119  1.00 32.04           O  
HETATM 4882  O   HOH A2121      27.001  13.873  45.582  1.00 34.49           O  
HETATM 4883  O   HOH A2122      25.841   9.552  44.564  1.00 55.17           O  
HETATM 4884  O   HOH A2123      44.856  27.880  46.189  1.00 30.95           O  
HETATM 4885  O   HOH A2124      35.611   9.588  50.038  1.00 41.90           O  
HETATM 4886  O   HOH A2125      38.498  35.628  50.765  1.00 26.69           O  
HETATM 4887  O   HOH A2126      39.244  37.381  55.807  1.00 42.76           O  
HETATM 4888  O   HOH A2127      33.944  18.283  53.032  1.00 48.79           O  
HETATM 4889  O   HOH A2128      36.501  20.637  51.705  1.00 45.60           O  
HETATM 4890  O   HOH A2129      42.787  43.334  56.083  1.00 40.09           O  
HETATM 4891  O   HOH A2130      56.968  41.831  63.701  1.00 42.73           O  
HETATM 4892  O   HOH A2131      39.272  27.243  44.281  1.00 44.92           O  
HETATM 4893  O   HOH A2132      37.964  21.411  49.414  1.00 30.06           O  
HETATM 4894  O   HOH A2133      37.958  26.212  47.790  1.00 44.98           O  
HETATM 4895  O   HOH A2134      41.181  13.664  41.675  1.00 36.85           O  
HETATM 4896  O   HOH A2135      45.395  19.823  49.333  1.00 48.96           O  
HETATM 4897  O   HOH A2136      50.830  26.069  35.611  1.00 40.02           O  
HETATM 4898  O   HOH A2137      46.816  19.829  38.612  1.00 41.12           O  
HETATM 4899  O   HOH A2138      47.096  19.628  33.301  1.00 39.63           O  
HETATM 4900  O   HOH A2139      46.247  15.458  31.504  1.00 29.44           O  
HETATM 4901  O   HOH A2140      41.690  12.743  36.520  1.00 45.23           O  
HETATM 4902  O   HOH A2141      40.553  19.067  31.054  1.00 31.19           O  
HETATM 4903  O   HOH A2142      61.336  50.541  51.337  1.00 45.61           O  
HETATM 4904  O   HOH A2143      41.870  11.724  30.722  1.00 27.02           O  
HETATM 4905  O   HOH A2144      38.381  12.374  24.731  1.00 44.11           O  
HETATM 4906  O   HOH A2145      35.907  12.552  25.672  1.00 25.39           O  
HETATM 4907  O   HOH A2146      27.295  18.819  26.051  1.00 23.88           O  
HETATM 4908  O   HOH A2147      29.291  19.889  23.346  1.00 24.18           O  
HETATM 4909  O   HOH A2148      27.500  14.226  27.489  1.00 25.41           O  
HETATM 4910  O   HOH A2149      34.181  10.599  28.257  1.00 20.76           O  
HETATM 4911  O   HOH A2150      28.970  12.153  32.723  1.00 24.55           O  
HETATM 4912  O   HOH A2151      34.018   8.575  30.162  1.00 43.04           O  
HETATM 4913  O   HOH A2152      37.732   7.064  33.535  1.00 48.68           O  
HETATM 4914  O   HOH A2153      39.102  11.125  33.545  1.00 21.19           O  
HETATM 4915  O   HOH A2154      40.750  44.964  49.691  1.00 25.17           O  
HETATM 4916  O   HOH A2155      27.725  14.522  39.223  1.00 39.88           O  
HETATM 4917  O   HOH A2156      50.433  32.980  35.395  1.00 27.78           O  
HETATM 4918  O   HOH A2157      23.764  15.417  41.216  1.00 45.57           O  
HETATM 4919  O   HOH A2158      22.412  16.803  37.659  1.00 43.70           O  
HETATM 4920  O   HOH A2159      26.101  20.243  49.585  1.00 24.90           O  
HETATM 4921  O   HOH A2160      19.163  25.611  48.320  1.00 25.80           O  
HETATM 4922  O   HOH A2161      19.590  16.455  39.634  1.00 45.25           O  
HETATM 4923  O   HOH A2162      20.296  21.770  47.578  1.00 38.44           O  
HETATM 4924  O   HOH A2163      15.876  30.521  47.253  1.00 31.86           O  
HETATM 4925  O   HOH A2164      21.461  24.555  51.822  1.00 33.72           O  
HETATM 4926  O   HOH A2165      16.729  33.274  50.986  1.00 24.98           O  
HETATM 4927  O   HOH A2166      16.355  39.332  47.441  1.00 16.61           O  
HETATM 4928  O   HOH A2167      11.141  37.010  54.220  1.00 43.27           O  
HETATM 4929  O   HOH A2168      16.540  45.049  50.781  1.00 15.93           O  
HETATM 4930  O   HOH A2169      14.118  37.523  50.894  1.00 39.63           O  
HETATM 4931  O   HOH A2170      22.996  38.949  26.371  1.00 38.28           O  
HETATM 4932  O   HOH A2171      23.939  29.659  26.509  1.00 42.88           O  
HETATM 4933  O   HOH A2172      16.756  44.276  47.836  1.00 17.52           O  
HETATM 4934  O   HOH A2173      31.240  38.559  20.375  1.00 47.94           O  
HETATM 4935  O   HOH A2174      15.339  49.780  56.964  1.00 42.68           O  
HETATM 4936  O   HOH A2175      23.293  21.221  25.162  1.00 40.04           O  
HETATM 4937  O   HOH A2176      26.547  47.649  53.571  1.00 39.97           O  
HETATM 4938  O   HOH A2177      15.161  50.744  53.893  1.00 46.81           O  
HETATM 4939  O   HOH A2178      14.381  45.600  52.809  1.00 44.10           O  
HETATM 4940  O   HOH A2179      20.277  29.204  31.044  1.00 31.69           O  
HETATM 4941  O   HOH A2180      21.476  24.864  27.340  1.00 34.36           O  
HETATM 4942  O   HOH A2181      20.274  17.838  34.214  1.00 44.34           O  
HETATM 4943  O   HOH A2182      13.556  47.284  49.126  1.00 53.43           O  
HETATM 4944  O   HOH A2183      21.501  54.137  59.417  1.00 23.27           O  
HETATM 4945  O   HOH A2184      31.307  56.780  49.243  1.00 27.95           O  
HETATM 4946  O   HOH A2185      19.911  55.424  50.600  1.00 37.80           O  
HETATM 4947  O   HOH A2186      17.540  52.182  46.933  1.00 26.43           O  
HETATM 4948  O   HOH A2187      18.652  48.396  47.732  1.00 19.58           O  
HETATM 4949  O   HOH A2188      19.069  49.921  43.313  1.00 22.26           O  
HETATM 4950  O   HOH A2189      24.332  47.645  41.904  1.00 11.04           O  
HETATM 4951  O   HOH A2190      25.816  53.804  41.542  1.00 36.15           O  
HETATM 4952  O   HOH A2191      29.507  54.047  43.644  1.00 35.52           O  
HETATM 4953  O   HOH A2192      30.779  47.918  51.067  1.00 35.49           O  
HETATM 4954  O   HOH A2193      50.589  53.935  30.727  1.00 41.87           O  
HETATM 4955  O   HOH A2194      29.811  44.316  51.775  1.00 29.84           O  
HETATM 4956  O   HOH A2195      33.725  46.851  44.246  1.00 15.53           O  
HETATM 4957  O   HOH A2196      58.379  48.121  27.949  1.00 43.58           O  
HETATM 4958  O   HOH A2197      33.726  54.353  42.506  1.00 17.24           O  
HETATM 4959  O   HOH A2198      28.547  53.383  41.232  1.00 40.56           O  
HETATM 4960  O   HOH A2199      23.288  50.618  41.612  1.00 18.93           O  
HETATM 4961  O   HOH A2200      33.749  56.149  48.597  1.00 30.36           O  
HETATM 4962  O   HOH A2201      38.428  50.689  49.680  1.00 38.37           O  
HETATM 4963  O   HOH A2202      38.503  60.152  44.332  1.00 32.68           O  
HETATM 4964  O   HOH A2203      39.778  58.278  43.142  1.00 32.41           O  
HETATM 4965  O   HOH A2204      33.586  58.999  44.339  1.00 41.52           O  
HETATM 4966  O   HOH A2205      40.602  56.391  45.574  1.00 29.30           O  
HETATM 4967  O   HOH A2206      31.122  54.022  40.983  1.00 40.95           O  
HETATM 4968  O   HOH A2207      39.487  58.074  40.481  1.00 19.31           O  
HETATM 4969  O   HOH A2208      68.409  39.510  47.837  1.00 41.69           O  
HETATM 4970  O   HOH A2209      30.477  54.512  37.203  1.00 19.17           O  
HETATM 4971  O   HOH A2210      35.645  59.479  37.510  1.00 31.45           O  
HETATM 4972  O   HOH A2211      31.453  48.234  33.459  1.00 20.09           O  
HETATM 4973  O   HOH A2212      25.177  49.091  37.779  1.00 23.88           O  
HETATM 4974  O   HOH A2213      27.049  52.187  32.598  1.00 39.24           O  
HETATM 4975  O   HOH A2214      54.691  59.362  48.731  1.00 33.75           O  
HETATM 4976  O   HOH A2215      53.736  57.789  52.852  1.00 40.58           O  
HETATM 4977  O   HOH A2216      57.293  56.491  51.361  1.00 36.42           O  
HETATM 4978  O   HOH A2217      30.633  55.275  34.413  1.00 26.28           O  
HETATM 4979  O   HOH A2218      33.951  58.019  31.506  1.00 26.89           O  
HETATM 4980  O   HOH A2219      51.193  61.127  51.030  1.00 39.94           O  
HETATM 4981  O   HOH A2220      39.592  55.524  36.450  1.00 25.79           O  
HETATM 4982  O   HOH A2221      38.082  58.167  33.104  1.00 35.67           O  
HETATM 4983  O   HOH A2222      30.122  45.125  27.224  1.00 41.19           O  
HETATM 4984  O   HOH A2223      57.488  59.756  41.894  1.00 54.98           O  
HETATM 4985  O   HOH A2224      37.858  50.757  24.526  1.00 31.62           O  
HETATM 4986  O   HOH A2225      33.404  55.021  25.847  1.00 52.41           O  
HETATM 4987  O   HOH A2226      43.109  61.103  37.679  1.00 41.65           O  
HETATM 4988  O   HOH A2227      50.931  47.015  21.718  1.00 41.76           O  
HETATM 4989  O   HOH A2228      30.518  43.634  25.079  1.00 47.04           O  
HETATM 4990  O   HOH A2229      47.248  45.427  20.268  1.00 40.26           O  
HETATM 4991  O   HOH A2230      43.520  51.469  28.053  1.00 23.51           O  
HETATM 4992  O   HOH A2231      42.654  46.736  21.378  1.00 21.89           O  
HETATM 4993  O   HOH A2232      40.837  53.265  28.588  1.00 34.92           O  
HETATM 4994  O   HOH A2233      43.139  43.055  22.306  1.00 14.35           O  
HETATM 4995  O   HOH A2234      45.443  50.731  25.094  1.00 46.95           O  
HETATM 4996  O   HOH A2235      34.157  38.583  24.573  1.00 28.21           O  
HETATM 4997  O   HOH A2236      32.376  39.513  22.416  1.00 42.97           O  
HETATM 4998  O   HOH A2237      34.183  42.608  20.745  1.00 46.91           O  
HETATM 4999  O   HOH A2238      41.440  40.204  15.200  1.00 25.63           O  
HETATM 5000  O   HOH A2239      41.447  36.486  13.521  1.00 40.39           O  
HETATM 5001  O   HOH A2240      25.504  31.112  20.438  1.00 38.34           O  
HETATM 5002  O   HOH A2241      37.616  28.428  16.196  1.00 14.22           O  
HETATM 5003  O   HOH A2242      40.781  21.352  12.247  1.00 34.63           O  
HETATM 5004  O   HOH A2243      37.372  23.617   9.556  1.00 39.44           O  
HETATM 5005  O   HOH A2244      36.989  26.821   9.501  1.00 47.61           O  
HETATM 5006  O   HOH A2245      43.929  19.517  20.685  1.00 25.16           O  
HETATM 5007  O   HOH A2246      33.913  20.122  11.496  1.00 24.77           O  
HETATM 5008  O   HOH A2247      38.400  16.790  14.876  1.00 37.75           O  
HETATM 5009  O   HOH A2248      39.805  19.953  14.067  1.00 34.19           O  
HETATM 5010  O   HOH A2249      44.543  23.939  14.013  1.00 24.17           O  
HETATM 5011  O   HOH A2250      44.253  25.373  17.456  1.00 17.05           O  
HETATM 5012  O   HOH A2251      44.519  16.873  20.860  1.00 43.15           O  
HETATM 5013  O   HOH A2252      39.938  19.646  28.365  1.00 16.90           O  
HETATM 5014  O   HOH A2253      32.135  20.873  14.262  1.00 29.57           O  
HETATM 5015  O   HOH A2254      29.162  20.497  16.594  1.00 43.76           O  
HETATM 5016  O   HOH A2255      36.157  15.297  14.633  1.00 24.52           O  
HETATM 5017  O   HOH A2256      30.316  16.227  11.943  1.00 54.54           O  
HETATM 5018  O   HOH A2257      24.489  15.323  15.117  1.00 46.62           O  
HETATM 5019  O   HOH A2258      26.778  17.598  17.107  1.00 39.40           O  
HETATM 5020  O   HOH A2259      29.470  22.597  20.692  1.00 48.08           O  
HETATM 5021  O   HOH A2260      28.206  17.559  22.902  1.00 32.76           O  
HETATM 5022  O   HOH A2261      25.950  27.760  17.747  1.00 47.76           O  
HETATM 5023  O   HOH A2262      32.503  25.207  20.281  1.00 30.43           O  
HETATM 5024  O   HOH A2263      35.895  29.226  13.339  1.00 19.08           O  
HETATM 5025  O   HOH A2264      31.749  23.341  13.589  1.00 21.93           O  
HETATM 5026  O   HOH A2265      28.676  25.375  20.616  1.00 37.11           O  
HETATM 5027  O   HOH A2266      36.434  24.093  32.323  1.00 12.11           O  
HETATM 5028  O   HOH A2267      38.591  20.686  31.734  1.00 19.19           O  
HETATM 5029  O   HOH A2268      41.493  22.764  37.711  1.00 14.46           O  
HETATM 5030  O   HOH A2269      40.575  28.769  39.893  1.00 24.17           O  
HETATM 5031  O   HOH A2270      40.975  25.862  40.806  1.00 24.48           O  
HETATM 5032  O   HOH A2271      32.992  26.241  34.112  1.00 12.73           O  
HETATM 5033  O   HOH A2272      39.385  24.084  39.045  1.00 16.57           O  
HETATM 5034  O   HOH A2273      43.493  27.126  35.565  1.00 48.96           O  
HETATM 5035  O   HOH A2274      42.886  25.680  33.406  1.00 14.64           O  
HETATM 5036  O   HOH A2275      49.866  23.754  32.094  1.00 47.08           O  
HETATM 5037  O   HOH A2276      56.042  23.489  25.469  1.00 43.75           O  
HETATM 5038  O   HOH A2277      48.817  20.944  30.325  1.00 27.83           O  
HETATM 5039  O   HOH A2278      50.893  18.450  23.970  1.00 27.60           O  
HETATM 5040  O   HOH A2279      50.197  23.766  16.468  1.00 47.21           O  
HETATM 5041  O   HOH A2280      56.486  22.481  16.758  1.00 35.62           O  
HETATM 5042  O   HOH A2281      60.152  17.493  35.180  1.00 31.13           O  
HETATM 5043  O   HOH A2282      53.705  20.324  34.584  1.00 46.72           O  
HETATM 5044  O   HOH A2283      64.060  23.004  42.589  1.00 32.90           O  
HETATM 5045  O   HOH A2284      56.373  17.507  47.814  1.00 44.29           O  
HETATM 5046  O   HOH A2285      55.500  25.818  58.095  1.00 44.59           O  
HETATM 5047  O   HOH A2286      63.827  32.863  45.133  1.00 49.52           O  
HETATM 5048  O   HOH A2287      57.915  38.932  52.077  1.00 23.38           O  
HETATM 5049  O   HOH A2288      62.169  33.114  54.016  1.00 38.38           O  
HETATM 5050  O   HOH A2289      65.633  34.803  51.451  1.00 38.53           O  
HETATM 5051  O   HOH A2290      66.327  38.147  49.052  1.00 26.67           O  
HETATM 5052  O   HOH A2291      64.162  36.713  52.481  1.00 35.08           O  
HETATM 5053  O   HOH A2292      64.071  48.661  47.710  1.00 36.23           O  
HETATM 5054  O   HOH A2293      62.045  46.674  53.517  1.00 33.21           O  
HETATM 5055  O   HOH A2294      64.290  43.553  53.436  1.00 38.01           O  
HETATM 5056  O   HOH A2295      59.040  42.353  59.062  1.00 33.96           O  
HETATM 5057  O   HOH A2296      61.462  37.840  59.404  1.00 32.38           O  
HETATM 5058  O   HOH A2297      60.554  35.356  56.976  1.00 42.99           O  
HETATM 5059  O   HOH A2298      58.449  30.554  63.214  1.00 46.73           O  
HETATM 5060  O   HOH A2299      50.726  38.377  68.058  1.00 47.19           O  
HETATM 5061  O   HOH A2300      57.378  37.209  64.736  1.00 28.61           O  
HETATM 5062  O   HOH A2301      47.127  28.967  63.758  1.00 39.75           O  
HETATM 5063  O   HOH A2302      52.375  26.835  60.266  1.00 44.32           O  
HETATM 5064  O   HOH A2303      50.943  24.947  57.867  1.00 32.14           O  
HETATM 5065  O   HOH A2304      54.863  22.503  53.859  1.00 37.14           O  
HETATM 5066  O   HOH A2305      55.760  18.990  54.253  1.00 46.82           O  
HETATM 5067  O   HOH A2306      48.046  22.565  58.100  1.00 30.58           O  
HETATM 5068  O   HOH A2307      47.786  18.173  53.594  1.00 33.24           O  
HETATM 5069  O   HOH A2308      47.029  18.253  59.807  1.00 47.20           O  
HETATM 5070  O   HOH A2309      47.382  23.700  60.586  1.00 42.72           O  
HETATM 5071  O   HOH A2310      45.839  26.154  61.550  1.00 36.80           O  
HETATM 5072  O   HOH A2311      43.735  26.720  48.439  1.00 32.56           O  
HETATM 5073  O   HOH A2312      37.233  24.170  51.843  1.00 33.85           O  
HETATM 5074  O   HOH A2313      37.118  27.351  50.493  1.00 21.88           O  
HETATM 5075  O   HOH A2314      39.668  33.298  50.610  1.00 33.61           O  
HETATM 5076  O   HOH A2315      42.441  29.122  46.515  1.00 39.18           O  
HETATM 5077  O   HOH A2316      41.335  38.420  54.710  0.50 29.72           O  
HETATM 5078  O   HOH A2317      43.065  37.312  51.242  1.00 19.15           O  
HETATM 5079  O   HOH A2318      44.624  45.246  56.395  1.00 17.22           O  
HETATM 5080  O   HOH A2319      42.686  40.690  57.070  1.00 26.52           O  
HETATM 5081  O   HOH A2320      48.469  46.405  58.796  1.00 20.34           O  
HETATM 5082  O   HOH A2321      47.972  45.541  61.312  1.00 27.55           O  
HETATM 5083  O   HOH A2322      37.428  43.614  61.340  1.00 41.53           O  
HETATM 5084  O   HOH A2323      48.595  42.613  62.331  1.00 19.33           O  
HETATM 5085  O   HOH A2324      55.900  43.483  62.013  1.00 33.17           O  
HETATM 5086  O   HOH A2325      53.403  37.618  61.414  1.00 27.12           O  
HETATM 5087  O   HOH A2326      55.826  39.714  64.610  1.00 34.66           O  
HETATM 5088  O   HOH A2327      51.809  35.631  62.337  1.00 31.87           O  
HETATM 5089  O   HOH A2328      46.903  38.348  67.243  1.00 32.49           O  
HETATM 5090  O   HOH A2329      46.981  33.979  68.748  1.00 49.24           O  
HETATM 5091  O   HOH A2330      44.854  34.535  67.215  1.00 48.50           O  
HETATM 5092  O   HOH A2331      39.543  32.050  52.976  1.00 16.43           O  
HETATM 5093  O   HOH A2332      44.042  21.496  47.701  1.00 33.63           O  
HETATM 5094  O   HOH A2333      47.029  21.316  50.899  1.00 28.63           O  
HETATM 5095  O   HOH A2334      49.969  19.920  49.613  1.00 44.84           O  
HETATM 5096  O   HOH A2335      44.819  20.699  43.312  1.00 49.10           O  
HETATM 5097  O   HOH A2336      50.956  18.524  42.578  1.00 40.01           O  
HETATM 5098  O   HOH A2337      50.752  18.550  46.573  1.00 33.31           O  
HETATM 5099  O   HOH A2338      46.362  23.481  42.021  1.00 38.59           O  
HETATM 5100  O   HOH A2339      42.825  25.879  37.780  1.00 23.21           O  
HETATM 5101  O   HOH A2340      44.975  29.368  39.403  1.00 43.65           O  
HETATM 5102  O   HOH A2341      44.601  23.087  39.455  1.00 47.23           O  
HETATM 5103  O   HOH A2342      50.268  24.002  37.829  1.00 31.48           O  
HETATM 5104  O   HOH A2343      47.554  30.392  39.434  1.00 32.91           O  
HETATM 5105  O   HOH A2344      59.869  33.554  44.206  1.00 24.54           O  
HETATM 5106  O   HOH A2345      42.766  41.142  51.475  1.00 46.99           O  
HETATM 5107  O   HOH A2346      55.349  39.853  51.988  1.00 21.56           O  
HETATM 5108  O   HOH A2347      48.355  52.277  48.594  1.00 16.39           O  
HETATM 5109  O   HOH A2348      56.000  49.811  57.192  1.00 33.19           O  
HETATM 5110  O   HOH A2349      60.149  48.327  52.415  1.00 42.30           O  
HETATM 5111  O   HOH A2350      50.546  48.552  64.034  1.00 38.09           O  
HETATM 5112  O   HOH A2351      52.883  51.977  57.763  1.00 29.06           O  
HETATM 5113  O   HOH A2352      40.454  49.523  57.495  1.00 35.41           O  
HETATM 5114  O   HOH A2353      42.129  47.247  49.577  1.00 21.96           O  
HETATM 5115  O   HOH A2354      40.996  49.596  48.874  1.00 12.40           O  
HETATM 5116  O   HOH A2355      40.065  53.867  45.877  1.00 28.99           O  
HETATM 5117  O   HOH A2356      43.086  51.380  39.452  1.00 19.50           O  
HETATM 5118  O   HOH A2357      41.437  43.591  47.417  1.00 17.87           O  
HETATM 5119  O   HOH A2358      39.736  39.843  47.740  1.00 17.61           O  
HETATM 5120  O   HOH A2359      48.929  40.765  46.120  1.00 16.42           O  
HETATM 5121  O   HOH A2360      46.544  35.226  40.439  1.00 40.06           O  
HETATM 5122  O   HOH A2361      51.141  36.659  37.992  1.00 13.96           O  
HETATM 5123  O   HOH A2362      56.121  37.459  32.732  1.00 21.41           O  
HETATM 5124  O   HOH A2363      57.554  41.574  37.486  1.00 16.47           O  
HETATM 5125  O   HOH A2364      55.772  29.777  32.992  1.00 44.58           O  
HETATM 5126  O   HOH A2365      52.416  34.580  36.566  1.00 18.04           O  
HETATM 5127  O   HOH A2366      72.360  33.792  31.449  1.00 55.70           O  
HETATM 5128  O   HOH A2367      62.649  34.290  30.290  1.00 24.83           O  
HETATM 5129  O   HOH A2368      68.047  30.945  34.093  1.00 36.91           O  
HETATM 5130  O   HOH A2369      62.109  32.898  43.133  1.00 29.76           O  
HETATM 5131  O   HOH A2370      70.354  22.884  32.301  1.00 45.44           O  
HETATM 5132  O   HOH A2371      61.892  29.586  16.389  1.00 40.21           O  
HETATM 5133  O   HOH A2372      63.085  28.921  19.779  1.00 53.97           O  
HETATM 5134  O   HOH A2373      60.188  33.756  26.674  1.00 37.96           O  
HETATM 5135  O   HOH A2374      58.272  25.539  24.981  1.00 32.58           O  
HETATM 5136  O   HOH A2375      57.297  28.427  29.996  1.00 42.70           O  
HETATM 5137  O   HOH A2376      48.110  31.839  37.064  1.00 42.29           O  
HETATM 5138  O   HOH A2377      49.709  30.628  33.104  1.00 41.21           O  
HETATM 5139  O   HOH A2378      47.167  34.527  37.872  1.00 27.27           O  
HETATM 5140  O   HOH A2379      37.232  33.021  29.678  1.00 13.93           O  
HETATM 5141  O   HOH A2380      33.205  41.739  37.987  1.00 14.76           O  
HETATM 5142  O   HOH A2381      31.807  45.250  42.894  1.00 12.95           O  
HETATM 5143  O   HOH A2382      28.580  48.024  33.877  1.00 34.88           O  
HETATM 5144  O   HOH A2383      26.055  45.081  34.982  1.00 35.09           O  
HETATM 5145  O   HOH A2384      17.760  41.993  33.261  1.00 55.66           O  
HETATM 5146  O   HOH A2385      25.206  43.505  32.164  1.00 33.23           O  
HETATM 5147  O   HOH A2386      17.829  47.302  45.052  1.00 19.63           O  
HETATM 5148  O   HOH A2387      16.760  48.273  38.728  1.00 43.33           O  
HETATM 5149  O   HOH A2388      21.095  47.604  35.786  1.00 41.37           O  
HETATM 5150  O   HOH A2389      22.957  49.917  38.951  1.00 28.18           O  
HETATM 5151  O   HOH A2390      13.307  43.102  37.676  1.00 40.57           O  
HETATM 5152  O   HOH A2391      13.343  44.562  41.439  1.00 32.79           O  
HETATM 5153  O   HOH A2392      14.997  43.707  34.454  1.00 43.03           O  
HETATM 5154  O   HOH A2393      17.460  40.837  43.030  1.00 16.41           O  
HETATM 5155  O   HOH A2394      10.864  37.430  37.980  1.00 28.15           O  
HETATM 5156  O   HOH A2395      11.989  35.114  47.917  1.00 33.35           O  
HETATM 5157  O   HOH A2396       9.453  31.180  47.871  1.00 51.79           O  
HETATM 5158  O   HOH A2397       9.502  32.218  43.068  1.00 46.26           O  
HETATM 5159  O   HOH A2398      13.854  29.610  37.456  1.00 44.84           O  
HETATM 5160  O   HOH A2399      11.053  37.371  34.418  1.00 31.32           O  
HETATM 5161  O   HOH A2400      14.847  39.443  36.394  1.00 22.09           O  
HETATM 5162  O   HOH A2401      17.325  38.625  44.796  1.00 17.92           O  
HETATM 5163  O   HOH A2402      19.913  28.817  33.764  1.00 31.28           O  
HETATM 5164  O   HOH A2403      17.419  31.215  38.280  1.00 27.38           O  
HETATM 5165  O   HOH A2404      20.536  32.124  29.526  1.00 31.13           O  
HETATM 5166  O   HOH A2405      22.552  38.833  31.917  1.00 48.29           O  
HETATM 5167  O   HOH A2406      21.716  34.736  25.915  1.00 39.70           O  
HETATM 5168  O   HOH A2407      22.243  32.265  27.402  1.00 38.80           O  
HETATM 5169  O   HOH A2408      23.983  36.615  25.955  1.00 28.20           O  
HETATM 5170  O   HOH A2409      24.104  41.582  29.552  1.00 45.40           O  
HETATM 5171  O   HOH A2410      29.512  38.685  22.833  1.00 39.63           O  
HETATM 5172  O   HOH A2411      26.090  30.612  28.125  1.00 36.91           O  
HETATM 5173  O   HOH A2412      23.399  22.619  27.338  1.00 34.56           O  
HETATM 5174  O   HOH A2413      19.473  19.176  31.910  1.00 31.54           O  
HETATM 5175  O   HOH A2414      20.741  25.871  29.764  1.00 25.31           O  
HETATM 5176  O   HOH A2415      18.398  27.449  35.882  1.00 37.64           O  
HETATM 5177  O   HOH A2416      13.567  22.992  35.251  1.00 36.22           O  
HETATM 5178  O   HOH A2417      18.264  24.599  44.498  1.00 27.65           O  
HETATM 5179  O   HOH A2418      23.341  22.303  39.374  1.00 19.80           O  
HETATM 5180  O   HOH A2419      17.119  28.668  38.825  1.00 36.01           O  
HETATM 5181  O   HOH A2420      20.479  20.811  35.650  1.00 28.10           O  
HETATM 5182  O   HOH A2421      18.696  30.214  40.372  1.00 32.39           O  
HETATM 5183  O   HOH A2422      30.153  29.098  39.015  1.00 13.90           O  
HETATM 5184  O   HOH A2423      23.902  25.063  40.491  1.00 17.23           O  
HETATM 5185  O   HOH A2424      39.109  29.949  42.113  1.00 17.81           O  
HETATM 5186  O   HOH A2425      36.377  29.551  43.539  1.00 26.33           O  
HETATM 5187  O   HOH A2426      27.725  37.511  46.838  1.00 11.65           O  
HETATM 5188  O   HOH A2427      29.779  34.319  53.582  1.00 28.70           O  
HETATM 5189  O   HOH A2428      34.011  36.177  53.463  1.00 33.13           O  
HETATM 5190  O   HOH A2429      29.634  41.348  52.346  1.00 40.29           O  
HETATM 5191  O   HOH A2430      35.943  44.155  50.435  1.00 35.21           O  
HETATM 5192  O   HOH A2431      45.223  39.419  41.235  1.00 17.97           O  
HETATM 5193  O   HOH A2432      53.148  51.275  33.059  1.00 23.13           O  
HETATM 5194  O   HOH A2433      50.833  52.475  32.781  1.00 22.48           O  
HETATM 5195  O   HOH A2434      59.084  48.736  30.360  1.00 45.92           O  
HETATM 5196  O   HOH A2435      55.833  48.047  27.058  1.00 38.88           O  
HETATM 5197  O   HOH A2436      52.129  50.355  27.209  1.00 31.95           O  
HETATM 5198  O   HOH A2437      65.406  53.318  38.129  1.00 42.46           O  
HETATM 5199  O   HOH A2438      67.639  44.821  28.942  1.00 56.38           O  
HETATM 5200  O   HOH A2439      57.413  45.071  24.624  1.00 33.81           O  
HETATM 5201  O   HOH A2440      60.312  35.422  29.042  1.00 30.62           O  
HETATM 5202  O   HOH A2441      58.053  39.110  31.973  1.00 18.62           O  
HETATM 5203  O   HOH A2442      65.445  43.712  34.681  1.00 47.01           O  
HETATM 5204  O   HOH A2443      65.770  35.555  35.108  1.00 50.64           O  
HETATM 5205  O   HOH A2444      64.968  41.202  32.910  1.00 30.16           O  
HETATM 5206  O   HOH A2445      67.928  43.317  39.467  1.00 25.41           O  
HETATM 5207  O   HOH A2446      66.482  40.320  37.672  1.00 26.30           O  
HETATM 5208  O   HOH A2447      71.095  37.535  44.165  1.00 41.47           O  
HETATM 5209  O   HOH A2448      68.950  47.081  42.243  1.00 32.59           O  
HETATM 5210  O   HOH A2449      70.708  44.445  44.502  1.00 35.87           O  
HETATM 5211  O   HOH A2450      69.474  42.046  47.848  1.00 40.45           O  
HETATM 5212  O   HOH A2451      70.605  49.268  42.736  1.00 49.49           O  
HETATM 5213  O   HOH A2452      62.721  54.186  39.777  1.00 38.87           O  
HETATM 5214  O   HOH A2453      59.410  55.437  44.599  1.00 42.16           O  
HETATM 5215  O   HOH A2454      54.743  56.961  50.478  1.00 26.75           O  
HETATM 5216  O   HOH A2455      51.509  56.989  54.192  1.00 38.61           O  
HETATM 5217  O   HOH A2456      53.065  54.350  56.726  1.00 53.35           O  
HETATM 5218  O   HOH A2457      46.245  55.817  48.913  1.00 17.11           O  
HETATM 5219  O   HOH A2458      49.430  59.955  52.495  1.00 37.32           O  
HETATM 5220  O   HOH A2459      46.798  63.405  52.749  1.00 51.44           O  
HETATM 5221  O   HOH A2460      46.870  56.616  46.429  1.00 26.71           O  
HETATM 5222  O   HOH A2461      56.604  58.656  39.499  1.00 34.67           O  
HETATM 5223  O   HOH A2462      55.158  53.328  33.223  1.00 28.59           O  
HETATM 5224  O   HOH A2463      54.548  57.173  32.638  1.00 33.64           O  
HETATM 5225  O   HOH A2464      48.005  58.792  30.965  1.00 45.93           O  
HETATM 5226  O   HOH A2465      43.022  58.359  37.108  1.00 24.23           O  
HETATM 5227  O   HOH A2466      40.544  53.741  32.431  1.00 34.46           O  
HETATM 5228  O   HOH A2467      41.617  55.292  34.623  1.00 19.28           O  
HETATM 5229  O   HOH A2468      45.090  53.796  27.563  1.00 44.12           O  
HETATM 5230  O   HOH A2469      47.597  46.867  31.105  1.00 15.09           O  
HETATM 5231  O   HOH A2470      48.556  54.366  25.635  1.00 42.49           O  
HETATM 5232  O   HOH A2471      47.355  49.826  23.205  1.00 38.07           O  
HETATM 5233  O   HOH A2472      50.065  48.521  23.797  1.00 22.69           O  
HETATM 5234  O   HOH A2473      49.801  51.068  30.170  1.00 33.40           O  
HETATM 5235  O   HOH A2474      48.361  43.396  21.748  1.00 40.73           O  
HETATM 5236  O   HOH A2475      56.608  42.974  23.109  1.00 36.47           O  
HETATM 5237  O   HOH A2476      56.133  41.425  25.091  1.00 22.31           O  
HETATM 5238  O   HOH A2477      54.737  36.999  16.598  1.00 28.84           O  
HETATM 5239  O   HOH A2478      48.548  41.547  13.592  1.00 46.21           O  
HETATM 5240  O   HOH A2479      49.479  39.080  12.500  1.00 30.28           O  
HETATM 5241  O   HOH A2480      53.052  28.858  13.534  1.00 29.07           O  
HETATM 5242  O   HOH A2481      51.017  32.405  13.102  1.00 23.70           O  
HETATM 5243  O   HOH A2482      43.560  45.405  17.563  1.00 36.62           O  
HETATM 5244  O   HOH A2483      47.727  33.598   7.895  1.00 35.65           O  
HETATM 5245  O   HOH A2484      48.612  24.905  14.847  1.00 36.12           O  
HETATM 5246  O   HOH A2485      50.799  29.874  12.353  1.00 25.54           O  
HETATM 5247  O   HOH A2486      44.790  26.439  15.055  1.00 18.95           O  
HETATM 5248  O   HOH A2487      49.665  26.157  11.610  1.00 31.59           O  
HETATM 5249  O   HOH A2488      49.030  36.730   6.520  1.00 45.48           O  
HETATM 5250  O   HOH A2489      47.328  38.726   9.716  1.00 49.35           O  
HETATM 5251  O   HOH A2490      40.838  33.568   7.092  1.00 29.87           O  
HETATM 5252  O   HOH A2491      47.546  23.630  12.714  1.00 51.51           O  
HETATM 5253  O   HOH A2492      41.026  24.976   9.369  1.00 38.69           O  
HETATM 5254  O   HOH A2493      36.217  29.075   7.223  1.00 43.08           O  
HETATM 5255  O   HOH A2494      35.150  28.150  10.834  1.00 28.45           O  
HETATM 5256  O   HOH A2495      40.088  34.807  11.689  1.00 31.73           O  
HETATM 5257  O   HOH A2496      43.001  28.525  14.577  1.00 19.16           O  
HETATM 5258  O   HOH A2497      31.996  32.524  15.060  1.00 27.33           O  
HETATM 5259  O   HOH A2498      36.197  36.508  12.204  1.00 33.71           O  
HETATM 5260  O   HOH A2499      36.297  33.649  19.024  1.00 16.26           O  
HETATM 5261  O   HOH A2500      30.116  36.834  19.045  1.00 39.93           O  
HETATM 5262  O   HOH A2501      27.053  36.974  22.607  1.00 38.10           O  
HETATM 5263  O   HOH A2502      26.254  30.191  18.160  1.00 47.30           O  
HETATM 5264  O   HOH A2503      39.657  61.914  36.475  1.00 49.48           O  
HETATM 5265  O   HOH A2504      42.687  31.048  44.149  1.00 40.21           O  
CONECT  274 4662 4673                                                           
CONECT  415 4676                                                                
CONECT  574 4690                                                                
CONECT  914  955                                                                
CONECT  939 4704                                                                
CONECT  955  914                                                                
CONECT 2427 4718                                                                
CONECT 2542 2696                                                                
CONECT 2696 2542                                                                
CONECT 2797 4750                                                                
CONECT 2828 4750                                                                
CONECT 3026 4750                                                                
CONECT 4039 4123                                                                
CONECT 4123 4039                                                                
CONECT 4405 4732                                                                
CONECT 4662  274 4663 4673                                                      
CONECT 4663 4662 4664 4670                                                      
CONECT 4664 4663 4665 4671                                                      
CONECT 4665 4664 4666 4672                                                      
CONECT 4666 4665 4667 4673                                                      
CONECT 4667 4666 4674                                                           
CONECT 4668 4669 4670 4675                                                      
CONECT 4669 4668                                                                
CONECT 4670 4663 4668                                                           
CONECT 4671 4664                                                                
CONECT 4672 4665                                                                
CONECT 4673  274 4662 4666                                                      
CONECT 4674 4667                                                                
CONECT 4675 4668                                                                
CONECT 4676  415 4677 4687                                                      
CONECT 4677 4676 4678 4684                                                      
CONECT 4678 4677 4679 4685                                                      
CONECT 4679 4678 4680 4686                                                      
CONECT 4680 4679 4681 4687                                                      
CONECT 4681 4680 4688                                                           
CONECT 4682 4683 4684 4689                                                      
CONECT 4683 4682                                                                
CONECT 4684 4677 4682                                                           
CONECT 4685 4678                                                                
CONECT 4686 4679                                                                
CONECT 4687 4676 4680                                                           
CONECT 4688 4681                                                                
CONECT 4689 4682                                                                
CONECT 4690  574 4691 4701                                                      
CONECT 4691 4690 4692 4698                                                      
CONECT 4692 4691 4693 4699                                                      
CONECT 4693 4692 4694 4700                                                      
CONECT 4694 4693 4695 4701                                                      
CONECT 4695 4694 4702                                                           
CONECT 4696 4697 4698 4703                                                      
CONECT 4697 4696                                                                
CONECT 4698 4691 4696                                                           
CONECT 4699 4692                                                                
CONECT 4700 4693                                                                
CONECT 4701 4690 4694                                                           
CONECT 4702 4695                                                                
CONECT 4703 4696                                                                
CONECT 4704  939 4705 4715                                                      
CONECT 4705 4704 4706 4712                                                      
CONECT 4706 4705 4707 4713                                                      
CONECT 4707 4706 4708 4714                                                      
CONECT 4708 4707 4709 4715                                                      
CONECT 4709 4708 4716                                                           
CONECT 4710 4711 4712 4717                                                      
CONECT 4711 4710                                                                
CONECT 4712 4705 4710                                                           
CONECT 4713 4706                                                                
CONECT 4714 4707                                                                
CONECT 4715 4704 4708                                                           
CONECT 4716 4709                                                                
CONECT 4717 4710                                                                
CONECT 4718 2427 4719 4729                                                      
CONECT 4719 4718 4720 4726                                                      
CONECT 4720 4719 4721 4727                                                      
CONECT 4721 4720 4722 4728                                                      
CONECT 4722 4721 4723 4729                                                      
CONECT 4723 4722 4730                                                           
CONECT 4724 4725 4726 4731                                                      
CONECT 4725 4724                                                                
CONECT 4726 4719 4724                                                           
CONECT 4727 4720                                                                
CONECT 4728 4721                                                                
CONECT 4729 4718 4722                                                           
CONECT 4730 4723                                                                
CONECT 4731 4724                                                                
CONECT 4732 4405 4733 4743                                                      
CONECT 4733 4732 4734 4740                                                      
CONECT 4734 4733 4735 4741                                                      
CONECT 4735 4734 4736 4742                                                      
CONECT 4736 4735 4737 4743                                                      
CONECT 4737 4736 4744                                                           
CONECT 4738 4739 4740 4745                                                      
CONECT 4739 4738                                                                
CONECT 4740 4733 4738                                                           
CONECT 4741 4734                                                                
CONECT 4742 4735                                                                
CONECT 4743 4732 4736                                                           
CONECT 4744 4737                                                                
CONECT 4745 4738                                                                
CONECT 4746 4747 4748 4749                                                      
CONECT 4747 4746 4750                                                           
CONECT 4748 4746 4750                                                           
CONECT 4749 4746                                                                
CONECT 4750 2797 2828 3026 4747                                                 
CONECT 4750 4748                                                                
CONECT 4751 4752 4758                                                           
CONECT 4752 4751 4753 4755                                                      
CONECT 4753 4752 4754 4759                                                      
CONECT 4754 4753                                                                
CONECT 4755 4752                                                                
CONECT 4756 4758                                                                
CONECT 4757 4758                                                                
CONECT 4758 4751 4756 4757                                                      
CONECT 4759 4753                                                                
MASTER      351    0   11   27    6    0   17    6 5264    1  114   46          
HEADER    VIRAL PROTEIN                           25-FEB-20   6VXX              
TITLE     STRUCTURE OF THE SARS-COV-2 SPIKE GLYCOPROTEIN (CLOSED STATE)         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SARS-COV-2 SPIKE GLYCOPROTEIN;                             
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: ECTODOMAIN;                                                
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: SARS-COV-2;                                         
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    CORONAVIRUS, SARS-COV-2, SARS-COV, SPIKE GLYCOPROTEIN, FUSION         
KEYWDS   2 PROTEIN, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR 
KEYWDS   3 INFECTIOUS DISEASE, SSGCID, VIRAL PROTEIN                            
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.C.WALLS,Y.J.PARK,M.A.TORTORICI,A.WALL,SEATTLE STRUCTURAL GENOMICS   
AUTHOR   2 CENTER FOR INFECTIOUS DISEASE (SSGCID),A.T.MCGUIRE,D.VEESLER         
REVDAT   3   01-APR-20 6VXX    1       COMPND                                   
REVDAT   2   25-MAR-20 6VXX    1       JRNL                                     
REVDAT   1   11-MAR-20 6VXX    0                                                
JRNL        AUTH   A.C.WALLS,Y.J.PARK,M.A.TORTORICI,A.WALL,A.T.MCGUIRE,         
JRNL        AUTH 2 D.VEESLER                                                    
JRNL        TITL   STRUCTURE, FUNCTION, AND ANTIGENICITY OF THE SARS-COV-2      
JRNL        TITL 2 SPIKE GLYCOPROTEIN.                                          
JRNL        REF    CELL                                       2020              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   32155444                                                     
JRNL        DOI    10.1016/J.CELL.2020.02.058                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : WARP, LEGINON, RELION, CRYOSPARC          
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 2.800                          
REMARK   3   NUMBER OF PARTICLES               : 172693                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6VXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247293.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : SARS-COV-2 PREFUSION SPIKE        
REMARK 245                                    ECTODOMAIN                        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : UNSPECIFIED                       
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 70.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     ILE A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     PRO A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     PRO A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     MET A   -10                                                      
REMARK 465     PRO A    -9                                                      
REMARK 465     ALA A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     VAL A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     LEU A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     VAL A    16                                                      
REMARK 465     ASN A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     GLN A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     THR A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     GLY A    75                                                      
REMARK 465     THR A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     PHE A    79                                                      
REMARK 465     TYR A   144                                                      
REMARK 465     TYR A   145                                                      
REMARK 465     HIS A   146                                                      
REMARK 465     LYS A   147                                                      
REMARK 465     ASN A   148                                                      
REMARK 465     ASN A   149                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     TRP A   152                                                      
REMARK 465     MET A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     PHE A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     VAL A   159                                                      
REMARK 465     TYR A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     GLN A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     PHE A   175                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     MET A   177                                                      
REMARK 465     ASP A   178                                                      
REMARK 465     LEU A   179                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     GLN A   183                                                      
REMARK 465     GLY A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     ARG A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     TYR A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     PRO A   251                                                      
REMARK 465     GLY A   252                                                      
REMARK 465     ASP A   253                                                      
REMARK 465     SER A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     TRP A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     VAL A   445                                                      
REMARK 465     GLY A   446                                                      
REMARK 465     LEU A   455                                                      
REMARK 465     PHE A   456                                                      
REMARK 465     ARG A   457                                                      
REMARK 465     LYS A   458                                                      
REMARK 465     SER A   459                                                      
REMARK 465     ASN A   460                                                      
REMARK 465     LEU A   461                                                      
REMARK 465     SER A   469                                                      
REMARK 465     THR A   470                                                      
REMARK 465     GLU A   471                                                      
REMARK 465     ILE A   472                                                      
REMARK 465     TYR A   473                                                      
REMARK 465     GLN A   474                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     THR A   478                                                      
REMARK 465     PRO A   479                                                      
REMARK 465     CYS A   480                                                      
REMARK 465     ASN A   481                                                      
REMARK 465     GLY A   482                                                      
REMARK 465     VAL A   483                                                      
REMARK 465     GLU A   484                                                      
REMARK 465     GLY A   485                                                      
REMARK 465     PHE A   486                                                      
REMARK 465     ASN A   487                                                      
REMARK 465     CYS A   488                                                      
REMARK 465     GLY A   502                                                      
REMARK 465     PRO A   621                                                      
REMARK 465     VAL A   622                                                      
REMARK 465     ALA A   623                                                      
REMARK 465     ILE A   624                                                      
REMARK 465     HIS A   625                                                      
REMARK 465     ALA A   626                                                      
REMARK 465     ASP A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     THR A   630                                                      
REMARK 465     PRO A   631                                                      
REMARK 465     THR A   632                                                      
REMARK 465     TRP A   633                                                      
REMARK 465     ARG A   634                                                      
REMARK 465     VAL A   635                                                      
REMARK 465     TYR A   636                                                      
REMARK 465     SER A   637                                                      
REMARK 465     THR A   638                                                      
REMARK 465     GLY A   639                                                      
REMARK 465     SER A   640                                                      
REMARK 465     GLN A   677                                                      
REMARK 465     THR A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     SER A   680                                                      
REMARK 465     PRO A   681                                                      
REMARK 465     SER A   682                                                      
REMARK 465     GLY A   683                                                      
REMARK 465     ALA A   684                                                      
REMARK 465     GLY A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     VAL A   687                                                      
REMARK 465     ALA A   688                                                      
REMARK 465     LEU A   828                                                      
REMARK 465     ALA A   829                                                      
REMARK 465     ASP A   830                                                      
REMARK 465     ALA A   831                                                      
REMARK 465     GLY A   832                                                      
REMARK 465     PHE A   833                                                      
REMARK 465     ILE A   834                                                      
REMARK 465     LYS A   835                                                      
REMARK 465     GLN A   836                                                      
REMARK 465     TYR A   837                                                      
REMARK 465     GLY A   838                                                      
REMARK 465     ASP A   839                                                      
REMARK 465     CYS A   840                                                      
REMARK 465     LEU A   841                                                      
REMARK 465     GLY A   842                                                      
REMARK 465     ASP A   843                                                      
REMARK 465     ILE A   844                                                      
REMARK 465     ALA A   845                                                      
REMARK 465     ALA A   846                                                      
REMARK 465     ARG A   847                                                      
REMARK 465     ASP A   848                                                      
REMARK 465     LEU A   849                                                      
REMARK 465     ILE A   850                                                      
REMARK 465     CYS A   851                                                      
REMARK 465     ALA A   852                                                      
REMARK 465     GLN A   853                                                      
REMARK 465     PHE A  1148                                                      
REMARK 465     LYS A  1149                                                      
REMARK 465     GLU A  1150                                                      
REMARK 465     GLU A  1151                                                      
REMARK 465     LEU A  1152                                                      
REMARK 465     ASP A  1153                                                      
REMARK 465     LYS A  1154                                                      
REMARK 465     TYR A  1155                                                      
REMARK 465     PHE A  1156                                                      
REMARK 465     LYS A  1157                                                      
REMARK 465     ASN A  1158                                                      
REMARK 465     HIS A  1159                                                      
REMARK 465     THR A  1160                                                      
REMARK 465     SER A  1161                                                      
REMARK 465     PRO A  1162                                                      
REMARK 465     ASP A  1163                                                      
REMARK 465     VAL A  1164                                                      
REMARK 465     ASP A  1165                                                      
REMARK 465     LEU A  1166                                                      
REMARK 465     GLY A  1167                                                      
REMARK 465     ASP A  1168                                                      
REMARK 465     ILE A  1169                                                      
REMARK 465     SER A  1170                                                      
REMARK 465     GLY A  1171                                                      
REMARK 465     ILE A  1172                                                      
REMARK 465     ASN A  1173                                                      
REMARK 465     ALA A  1174                                                      
REMARK 465     SER A  1175                                                      
REMARK 465     VAL A  1176                                                      
REMARK 465     VAL A  1177                                                      
REMARK 465     ASN A  1178                                                      
REMARK 465     ILE A  1179                                                      
REMARK 465     GLN A  1180                                                      
REMARK 465     LYS A  1181                                                      
REMARK 465     GLU A  1182                                                      
REMARK 465     ILE A  1183                                                      
REMARK 465     ASP A  1184                                                      
REMARK 465     ARG A  1185                                                      
REMARK 465     LEU A  1186                                                      
REMARK 465     ASN A  1187                                                      
REMARK 465     GLU A  1188                                                      
REMARK 465     VAL A  1189                                                      
REMARK 465     ALA A  1190                                                      
REMARK 465     LYS A  1191                                                      
REMARK 465     ASN A  1192                                                      
REMARK 465     LEU A  1193                                                      
REMARK 465     ASN A  1194                                                      
REMARK 465     GLU A  1195                                                      
REMARK 465     SER A  1196                                                      
REMARK 465     LEU A  1197                                                      
REMARK 465     ILE A  1198                                                      
REMARK 465     ASP A  1199                                                      
REMARK 465     LEU A  1200                                                      
REMARK 465     GLN A  1201                                                      
REMARK 465     GLU A  1202                                                      
REMARK 465     LEU A  1203                                                      
REMARK 465     GLY A  1204                                                      
REMARK 465     LYS A  1205                                                      
REMARK 465     TYR A  1206                                                      
REMARK 465     GLU A  1207                                                      
REMARK 465     GLN A  1208                                                      
REMARK 465     TYR A  1209                                                      
REMARK 465     ILE A  1210                                                      
REMARK 465     LYS A  1211                                                      
REMARK 465     GLY A  1212                                                      
REMARK 465     SER A  1213                                                      
REMARK 465     GLY A  1214                                                      
REMARK 465     ARG A  1215                                                      
REMARK 465     GLU A  1216                                                      
REMARK 465     ASN A  1217                                                      
REMARK 465     LEU A  1218                                                      
REMARK 465     TYR A  1219                                                      
REMARK 465     PHE A  1220                                                      
REMARK 465     GLN A  1221                                                      
REMARK 465     GLY A  1222                                                      
REMARK 465     GLY A  1223                                                      
REMARK 465     GLY A  1224                                                      
REMARK 465     GLY A  1225                                                      
REMARK 465     SER A  1226                                                      
REMARK 465     GLY A  1227                                                      
REMARK 465     TYR A  1228                                                      
REMARK 465     ILE A  1229                                                      
REMARK 465     PRO A  1230                                                      
REMARK 465     GLU A  1231                                                      
REMARK 465     ALA A  1232                                                      
REMARK 465     PRO A  1233                                                      
REMARK 465     ARG A  1234                                                      
REMARK 465     ASP A  1235                                                      
REMARK 465     GLY A  1236                                                      
REMARK 465     GLN A  1237                                                      
REMARK 465     ALA A  1238                                                      
REMARK 465     TYR A  1239                                                      
REMARK 465     VAL A  1240                                                      
REMARK 465     ARG A  1241                                                      
REMARK 465     LYS A  1242                                                      
REMARK 465     ASP A  1243                                                      
REMARK 465     GLY A  1244                                                      
REMARK 465     GLU A  1245                                                      
REMARK 465     TRP A  1246                                                      
REMARK 465     VAL A  1247                                                      
REMARK 465     LEU A  1248                                                      
REMARK 465     LEU A  1249                                                      
REMARK 465     SER A  1250                                                      
REMARK 465     THR A  1251                                                      
REMARK 465     PHE A  1252                                                      
REMARK 465     LEU A  1253                                                      
REMARK 465     GLY A  1254                                                      
REMARK 465     HIS A  1255                                                      
REMARK 465     HIS A  1256                                                      
REMARK 465     HIS A  1257                                                      
REMARK 465     HIS A  1258                                                      
REMARK 465     HIS A  1259                                                      
REMARK 465     HIS A  1260                                                      
REMARK 465     HIS A  1261                                                      
REMARK 465     HIS A  1262                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     ILE B   -16                                                      
REMARK 465     LEU B   -15                                                      
REMARK 465     PRO B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     PRO B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     PRO B    -9                                                      
REMARK 465     ALA B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     VAL B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     CYS B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     CYS B    15                                                      
REMARK 465     VAL B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     THR B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     GLN B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     PRO B    26                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     SER B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     THR B    73                                                      
REMARK 465     ASN B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     THR B    76                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     PHE B    79                                                      
REMARK 465     TYR B   144                                                      
REMARK 465     TYR B   145                                                      
REMARK 465     HIS B   146                                                      
REMARK 465     LYS B   147                                                      
REMARK 465     ASN B   148                                                      
REMARK 465     ASN B   149                                                      
REMARK 465     LYS B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     TRP B   152                                                      
REMARK 465     MET B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     SER B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     PHE B   157                                                      
REMARK 465     ARG B   158                                                      
REMARK 465     VAL B   159                                                      
REMARK 465     TYR B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     ASN B   164                                                      
REMARK 465     GLN B   173                                                      
REMARK 465     PRO B   174                                                      
REMARK 465     PHE B   175                                                      
REMARK 465     LEU B   176                                                      
REMARK 465     MET B   177                                                      
REMARK 465     ASP B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     GLY B   181                                                      
REMARK 465     LYS B   182                                                      
REMARK 465     GLN B   183                                                      
REMARK 465     GLY B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     ARG B   246                                                      
REMARK 465     SER B   247                                                      
REMARK 465     TYR B   248                                                      
REMARK 465     LEU B   249                                                      
REMARK 465     THR B   250                                                      
REMARK 465     PRO B   251                                                      
REMARK 465     GLY B   252                                                      
REMARK 465     ASP B   253                                                      
REMARK 465     SER B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     GLY B   257                                                      
REMARK 465     TRP B   258                                                      
REMARK 465     THR B   259                                                      
REMARK 465     ALA B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     VAL B   445                                                      
REMARK 465     GLY B   446                                                      
REMARK 465     LEU B   455                                                      
REMARK 465     PHE B   456                                                      
REMARK 465     ARG B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     SER B   459                                                      
REMARK 465     ASN B   460                                                      
REMARK 465     LEU B   461                                                      
REMARK 465     SER B   469                                                      
REMARK 465     THR B   470                                                      
REMARK 465     GLU B   471                                                      
REMARK 465     ILE B   472                                                      
REMARK 465     TYR B   473                                                      
REMARK 465     GLN B   474                                                      
REMARK 465     ALA B   475                                                      
REMARK 465     GLY B   476                                                      
REMARK 465     SER B   477                                                      
REMARK 465     THR B   478                                                      
REMARK 465     PRO B   479                                                      
REMARK 465     CYS B   480                                                      
REMARK 465     ASN B   481                                                      
REMARK 465     GLY B   482                                                      
REMARK 465     VAL B   483                                                      
REMARK 465     GLU B   484                                                      
REMARK 465     GLY B   485                                                      
REMARK 465     PHE B   486                                                      
REMARK 465     ASN B   487                                                      
REMARK 465     CYS B   488                                                      
REMARK 465     GLY B   502                                                      
REMARK 465     PRO B   621                                                      
REMARK 465     VAL B   622                                                      
REMARK 465     ALA B   623                                                      
REMARK 465     ILE B   624                                                      
REMARK 465     HIS B   625                                                      
REMARK 465     ALA B   626                                                      
REMARK 465     ASP B   627                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     LEU B   629                                                      
REMARK 465     THR B   630                                                      
REMARK 465     PRO B   631                                                      
REMARK 465     THR B   632                                                      
REMARK 465     TRP B   633                                                      
REMARK 465     ARG B   634                                                      
REMARK 465     VAL B   635                                                      
REMARK 465     TYR B   636                                                      
REMARK 465     SER B   637                                                      
REMARK 465     THR B   638                                                      
REMARK 465     GLY B   639                                                      
REMARK 465     SER B   640                                                      
REMARK 465     GLN B   677                                                      
REMARK 465     THR B   678                                                      
REMARK 465     ASN B   679                                                      
REMARK 465     SER B   680                                                      
REMARK 465     PRO B   681                                                      
REMARK 465     SER B   682                                                      
REMARK 465     GLY B   683                                                      
REMARK 465     ALA B   684                                                      
REMARK 465     GLY B   685                                                      
REMARK 465     SER B   686                                                      
REMARK 465     VAL B   687                                                      
REMARK 465     ALA B   688                                                      
REMARK 465     LEU B   828                                                      
REMARK 465     ALA B   829                                                      
REMARK 465     ASP B   830                                                      
REMARK 465     ALA B   831                                                      
REMARK 465     GLY B   832                                                      
REMARK 465     PHE B   833                                                      
REMARK 465     ILE B   834                                                      
REMARK 465     LYS B   835                                                      
REMARK 465     GLN B   836                                                      
REMARK 465     TYR B   837                                                      
REMARK 465     GLY B   838                                                      
REMARK 465     ASP B   839                                                      
REMARK 465     CYS B   840                                                      
REMARK 465     LEU B   841                                                      
REMARK 465     GLY B   842                                                      
REMARK 465     ASP B   843                                                      
REMARK 465     ILE B   844                                                      
REMARK 465     ALA B   845                                                      
REMARK 465     ALA B   846                                                      
REMARK 465     ARG B   847                                                      
REMARK 465     ASP B   848                                                      
REMARK 465     LEU B   849                                                      
REMARK 465     ILE B   850                                                      
REMARK 465     CYS B   851                                                      
REMARK 465     ALA B   852                                                      
REMARK 465     GLN B   853                                                      
REMARK 465     PHE B  1148                                                      
REMARK 465     LYS B  1149                                                      
REMARK 465     GLU B  1150                                                      
REMARK 465     GLU B  1151                                                      
REMARK 465     LEU B  1152                                                      
REMARK 465     ASP B  1153                                                      
REMARK 465     LYS B  1154                                                      
REMARK 465     TYR B  1155                                                      
REMARK 465     PHE B  1156                                                      
REMARK 465     LYS B  1157                                                      
REMARK 465     ASN B  1158                                                      
REMARK 465     HIS B  1159                                                      
REMARK 465     THR B  1160                                                      
REMARK 465     SER B  1161                                                      
REMARK 465     PRO B  1162                                                      
REMARK 465     ASP B  1163                                                      
REMARK 465     VAL B  1164                                                      
REMARK 465     ASP B  1165                                                      
REMARK 465     LEU B  1166                                                      
REMARK 465     GLY B  1167                                                      
REMARK 465     ASP B  1168                                                      
REMARK 465     ILE B  1169                                                      
REMARK 465     SER B  1170                                                      
REMARK 465     GLY B  1171                                                      
REMARK 465     ILE B  1172                                                      
REMARK 465     ASN B  1173                                                      
REMARK 465     ALA B  1174                                                      
REMARK 465     SER B  1175                                                      
REMARK 465     VAL B  1176                                                      
REMARK 465     VAL B  1177                                                      
REMARK 465     ASN B  1178                                                      
REMARK 465     ILE B  1179                                                      
REMARK 465     GLN B  1180                                                      
REMARK 465     LYS B  1181                                                      
REMARK 465     GLU B  1182                                                      
REMARK 465     ILE B  1183                                                      
REMARK 465     ASP B  1184                                                      
REMARK 465     ARG B  1185                                                      
REMARK 465     LEU B  1186                                                      
REMARK 465     ASN B  1187                                                      
REMARK 465     GLU B  1188                                                      
REMARK 465     VAL B  1189                                                      
REMARK 465     ALA B  1190                                                      
REMARK 465     LYS B  1191                                                      
REMARK 465     ASN B  1192                                                      
REMARK 465     LEU B  1193                                                      
REMARK 465     ASN B  1194                                                      
REMARK 465     GLU B  1195                                                      
REMARK 465     SER B  1196                                                      
REMARK 465     LEU B  1197                                                      
REMARK 465     ILE B  1198                                                      
REMARK 465     ASP B  1199                                                      
REMARK 465     LEU B  1200                                                      
REMARK 465     GLN B  1201                                                      
REMARK 465     GLU B  1202                                                      
REMARK 465     LEU B  1203                                                      
REMARK 465     GLY B  1204                                                      
REMARK 465     LYS B  1205                                                      
REMARK 465     TYR B  1206                                                      
REMARK 465     GLU B  1207                                                      
REMARK 465     GLN B  1208                                                      
REMARK 465     TYR B  1209                                                      
REMARK 465     ILE B  1210                                                      
REMARK 465     LYS B  1211                                                      
REMARK 465     GLY B  1212                                                      
REMARK 465     SER B  1213                                                      
REMARK 465     GLY B  1214                                                      
REMARK 465     ARG B  1215                                                      
REMARK 465     GLU B  1216                                                      
REMARK 465     ASN B  1217                                                      
REMARK 465     LEU B  1218                                                      
REMARK 465     TYR B  1219                                                      
REMARK 465     PHE B  1220                                                      
REMARK 465     GLN B  1221                                                      
REMARK 465     GLY B  1222                                                      
REMARK 465     GLY B  1223                                                      
REMARK 465     GLY B  1224                                                      
REMARK 465     GLY B  1225                                                      
REMARK 465     SER B  1226                                                      
REMARK 465     GLY B  1227                                                      
REMARK 465     TYR B  1228                                                      
REMARK 465     ILE B  1229                                                      
REMARK 465     PRO B  1230                                                      
REMARK 465     GLU B  1231                                                      
REMARK 465     ALA B  1232                                                      
REMARK 465     PRO B  1233                                                      
REMARK 465     ARG B  1234                                                      
REMARK 465     ASP B  1235                                                      
REMARK 465     GLY B  1236                                                      
REMARK 465     GLN B  1237                                                      
REMARK 465     ALA B  1238                                                      
REMARK 465     TYR B  1239                                                      
REMARK 465     VAL B  1240                                                      
REMARK 465     ARG B  1241                                                      
REMARK 465     LYS B  1242                                                      
REMARK 465     ASP B  1243                                                      
REMARK 465     GLY B  1244                                                      
REMARK 465     GLU B  1245                                                      
REMARK 465     TRP B  1246                                                      
REMARK 465     VAL B  1247                                                      
REMARK 465     LEU B  1248                                                      
REMARK 465     LEU B  1249                                                      
REMARK 465     SER B  1250                                                      
REMARK 465     THR B  1251                                                      
REMARK 465     PHE B  1252                                                      
REMARK 465     LEU B  1253                                                      
REMARK 465     GLY B  1254                                                      
REMARK 465     HIS B  1255                                                      
REMARK 465     HIS B  1256                                                      
REMARK 465     HIS B  1257                                                      
REMARK 465     HIS B  1258                                                      
REMARK 465     HIS B  1259                                                      
REMARK 465     HIS B  1260                                                      
REMARK 465     HIS B  1261                                                      
REMARK 465     HIS B  1262                                                      
REMARK 465     MET C   -18                                                      
REMARK 465     GLY C   -17                                                      
REMARK 465     ILE C   -16                                                      
REMARK 465     LEU C   -15                                                      
REMARK 465     PRO C   -14                                                      
REMARK 465     SER C   -13                                                      
REMARK 465     PRO C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     MET C   -10                                                      
REMARK 465     PRO C    -9                                                      
REMARK 465     ALA C    -8                                                      
REMARK 465     LEU C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     SER C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     VAL C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     LEU C    -1                                                      
REMARK 465     LEU C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     MET C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     CYS C     7                                                      
REMARK 465     VAL C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     THR C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     GLN C    14                                                      
REMARK 465     CYS C    15                                                      
REMARK 465     VAL C    16                                                      
REMARK 465     ASN C    17                                                      
REMARK 465     LEU C    18                                                      
REMARK 465     THR C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     ARG C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     GLN C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     PRO C    25                                                      
REMARK 465     PRO C    26                                                      
REMARK 465     VAL C    70                                                      
REMARK 465     SER C    71                                                      
REMARK 465     GLY C    72                                                      
REMARK 465     THR C    73                                                      
REMARK 465     ASN C    74                                                      
REMARK 465     GLY C    75                                                      
REMARK 465     THR C    76                                                      
REMARK 465     LYS C    77                                                      
REMARK 465     ARG C    78                                                      
REMARK 465     PHE C    79                                                      
REMARK 465     TYR C   144                                                      
REMARK 465     TYR C   145                                                      
REMARK 465     HIS C   146                                                      
REMARK 465     LYS C   147                                                      
REMARK 465     ASN C   148                                                      
REMARK 465     ASN C   149                                                      
REMARK 465     LYS C   150                                                      
REMARK 465     SER C   151                                                      
REMARK 465     TRP C   152                                                      
REMARK 465     MET C   153                                                      
REMARK 465     GLU C   154                                                      
REMARK 465     SER C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     PHE C   157                                                      
REMARK 465     ARG C   158                                                      
REMARK 465     VAL C   159                                                      
REMARK 465     TYR C   160                                                      
REMARK 465     SER C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     ALA C   163                                                      
REMARK 465     ASN C   164                                                      
REMARK 465     GLN C   173                                                      
REMARK 465     PRO C   174                                                      
REMARK 465     PHE C   175                                                      
REMARK 465     LEU C   176                                                      
REMARK 465     MET C   177                                                      
REMARK 465     ASP C   178                                                      
REMARK 465     LEU C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     GLY C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     GLN C   183                                                      
REMARK 465     GLY C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     ARG C   246                                                      
REMARK 465     SER C   247                                                      
REMARK 465     TYR C   248                                                      
REMARK 465     LEU C   249                                                      
REMARK 465     THR C   250                                                      
REMARK 465     PRO C   251                                                      
REMARK 465     GLY C   252                                                      
REMARK 465     ASP C   253                                                      
REMARK 465     SER C   254                                                      
REMARK 465     SER C   255                                                      
REMARK 465     SER C   256                                                      
REMARK 465     GLY C   257                                                      
REMARK 465     TRP C   258                                                      
REMARK 465     THR C   259                                                      
REMARK 465     ALA C   260                                                      
REMARK 465     GLY C   261                                                      
REMARK 465     ALA C   262                                                      
REMARK 465     VAL C   445                                                      
REMARK 465     GLY C   446                                                      
REMARK 465     LEU C   455                                                      
REMARK 465     PHE C   456                                                      
REMARK 465     ARG C   457                                                      
REMARK 465     LYS C   458                                                      
REMARK 465     SER C   459                                                      
REMARK 465     ASN C   460                                                      
REMARK 465     LEU C   461                                                      
REMARK 465     SER C   469                                                      
REMARK 465     THR C   470                                                      
REMARK 465     GLU C   471                                                      
REMARK 465     ILE C   472                                                      
REMARK 465     TYR C   473                                                      
REMARK 465     GLN C   474                                                      
REMARK 465     ALA C   475                                                      
REMARK 465     GLY C   476                                                      
REMARK 465     SER C   477                                                      
REMARK 465     THR C   478                                                      
REMARK 465     PRO C   479                                                      
REMARK 465     CYS C   480                                                      
REMARK 465     ASN C   481                                                      
REMARK 465     GLY C   482                                                      
REMARK 465     VAL C   483                                                      
REMARK 465     GLU C   484                                                      
REMARK 465     GLY C   485                                                      
REMARK 465     PHE C   486                                                      
REMARK 465     ASN C   487                                                      
REMARK 465     CYS C   488                                                      
REMARK 465     GLY C   502                                                      
REMARK 465     PRO C   621                                                      
REMARK 465     VAL C   622                                                      
REMARK 465     ALA C   623                                                      
REMARK 465     ILE C   624                                                      
REMARK 465     HIS C   625                                                      
REMARK 465     ALA C   626                                                      
REMARK 465     ASP C   627                                                      
REMARK 465     GLN C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     THR C   630                                                      
REMARK 465     PRO C   631                                                      
REMARK 465     THR C   632                                                      
REMARK 465     TRP C   633                                                      
REMARK 465     ARG C   634                                                      
REMARK 465     VAL C   635                                                      
REMARK 465     TYR C   636                                                      
REMARK 465     SER C   637                                                      
REMARK 465     THR C   638                                                      
REMARK 465     GLY C   639                                                      
REMARK 465     SER C   640                                                      
REMARK 465     GLN C   677                                                      
REMARK 465     THR C   678                                                      
REMARK 465     ASN C   679                                                      
REMARK 465     SER C   680                                                      
REMARK 465     PRO C   681                                                      
REMARK 465     SER C   682                                                      
REMARK 465     GLY C   683                                                      
REMARK 465     ALA C   684                                                      
REMARK 465     GLY C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     VAL C   687                                                      
REMARK 465     ALA C   688                                                      
REMARK 465     LEU C   828                                                      
REMARK 465     ALA C   829                                                      
REMARK 465     ASP C   830                                                      
REMARK 465     ALA C   831                                                      
REMARK 465     GLY C   832                                                      
REMARK 465     PHE C   833                                                      
REMARK 465     ILE C   834                                                      
REMARK 465     LYS C   835                                                      
REMARK 465     GLN C   836                                                      
REMARK 465     TYR C   837                                                      
REMARK 465     GLY C   838                                                      
REMARK 465     ASP C   839                                                      
REMARK 465     CYS C   840                                                      
REMARK 465     LEU C   841                                                      
REMARK 465     GLY C   842                                                      
REMARK 465     ASP C   843                                                      
REMARK 465     ILE C   844                                                      
REMARK 465     ALA C   845                                                      
REMARK 465     ALA C   846                                                      
REMARK 465     ARG C   847                                                      
REMARK 465     ASP C   848                                                      
REMARK 465     LEU C   849                                                      
REMARK 465     ILE C   850                                                      
REMARK 465     CYS C   851                                                      
REMARK 465     ALA C   852                                                      
REMARK 465     GLN C   853                                                      
REMARK 465     PHE C  1148                                                      
REMARK 465     LYS C  1149                                                      
REMARK 465     GLU C  1150                                                      
REMARK 465     GLU C  1151                                                      
REMARK 465     LEU C  1152                                                      
REMARK 465     ASP C  1153                                                      
REMARK 465     LYS C  1154                                                      
REMARK 465     TYR C  1155                                                      
REMARK 465     PHE C  1156                                                      
REMARK 465     LYS C  1157                                                      
REMARK 465     ASN C  1158                                                      
REMARK 465     HIS C  1159                                                      
REMARK 465     THR C  1160                                                      
REMARK 465     SER C  1161                                                      
REMARK 465     PRO C  1162                                                      
REMARK 465     ASP C  1163                                                      
REMARK 465     VAL C  1164                                                      
REMARK 465     ASP C  1165                                                      
REMARK 465     LEU C  1166                                                      
REMARK 465     GLY C  1167                                                      
REMARK 465     ASP C  1168                                                      
REMARK 465     ILE C  1169                                                      
REMARK 465     SER C  1170                                                      
REMARK 465     GLY C  1171                                                      
REMARK 465     ILE C  1172                                                      
REMARK 465     ASN C  1173                                                      
REMARK 465     ALA C  1174                                                      
REMARK 465     SER C  1175                                                      
REMARK 465     VAL C  1176                                                      
REMARK 465     VAL C  1177                                                      
REMARK 465     ASN C  1178                                                      
REMARK 465     ILE C  1179                                                      
REMARK 465     GLN C  1180                                                      
REMARK 465     LYS C  1181                                                      
REMARK 465     GLU C  1182                                                      
REMARK 465     ILE C  1183                                                      
REMARK 465     ASP C  1184                                                      
REMARK 465     ARG C  1185                                                      
REMARK 465     LEU C  1186                                                      
REMARK 465     ASN C  1187                                                      
REMARK 465     GLU C  1188                                                      
REMARK 465     VAL C  1189                                                      
REMARK 465     ALA C  1190                                                      
REMARK 465     LYS C  1191                                                      
REMARK 465     ASN C  1192                                                      
REMARK 465     LEU C  1193                                                      
REMARK 465     ASN C  1194                                                      
REMARK 465     GLU C  1195                                                      
REMARK 465     SER C  1196                                                      
REMARK 465     LEU C  1197                                                      
REMARK 465     ILE C  1198                                                      
REMARK 465     ASP C  1199                                                      
REMARK 465     LEU C  1200                                                      
REMARK 465     GLN C  1201                                                      
REMARK 465     GLU C  1202                                                      
REMARK 465     LEU C  1203                                                      
REMARK 465     GLY C  1204                                                      
REMARK 465     LYS C  1205                                                      
REMARK 465     TYR C  1206                                                      
REMARK 465     GLU C  1207                                                      
REMARK 465     GLN C  1208                                                      
REMARK 465     TYR C  1209                                                      
REMARK 465     ILE C  1210                                                      
REMARK 465     LYS C  1211                                                      
REMARK 465     GLY C  1212                                                      
REMARK 465     SER C  1213                                                      
REMARK 465     GLY C  1214                                                      
REMARK 465     ARG C  1215                                                      
REMARK 465     GLU C  1216                                                      
REMARK 465     ASN C  1217                                                      
REMARK 465     LEU C  1218                                                      
REMARK 465     TYR C  1219                                                      
REMARK 465     PHE C  1220                                                      
REMARK 465     GLN C  1221                                                      
REMARK 465     GLY C  1222                                                      
REMARK 465     GLY C  1223                                                      
REMARK 465     GLY C  1224                                                      
REMARK 465     GLY C  1225                                                      
REMARK 465     SER C  1226                                                      
REMARK 465     GLY C  1227                                                      
REMARK 465     TYR C  1228                                                      
REMARK 465     ILE C  1229                                                      
REMARK 465     PRO C  1230                                                      
REMARK 465     GLU C  1231                                                      
REMARK 465     ALA C  1232                                                      
REMARK 465     PRO C  1233                                                      
REMARK 465     ARG C  1234                                                      
REMARK 465     ASP C  1235                                                      
REMARK 465     GLY C  1236                                                      
REMARK 465     GLN C  1237                                                      
REMARK 465     ALA C  1238                                                      
REMARK 465     TYR C  1239                                                      
REMARK 465     VAL C  1240                                                      
REMARK 465     ARG C  1241                                                      
REMARK 465     LYS C  1242                                                      
REMARK 465     ASP C  1243                                                      
REMARK 465     GLY C  1244                                                      
REMARK 465     GLU C  1245                                                      
REMARK 465     TRP C  1246                                                      
REMARK 465     VAL C  1247                                                      
REMARK 465     LEU C  1248                                                      
REMARK 465     LEU C  1249                                                      
REMARK 465     SER C  1250                                                      
REMARK 465     THR C  1251                                                      
REMARK 465     PHE C  1252                                                      
REMARK 465     LEU C  1253                                                      
REMARK 465     GLY C  1254                                                      
REMARK 465     HIS C  1255                                                      
REMARK 465     HIS C  1256                                                      
REMARK 465     HIS C  1257                                                      
REMARK 465     HIS C  1258                                                      
REMARK 465     HIS C  1259                                                      
REMARK 465     HIS C  1260                                                      
REMARK 465     HIS C  1261                                                      
REMARK 465     HIS C  1262                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 525   CB    CYS A 525   SG      0.117                       
REMARK 500    CYS B 525   CB    CYS B 525   SG      0.117                       
REMARK 500    CYS C 525   CB    CYS C 525   SG      0.117                       
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    TYR A 451   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TYR A 904   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    TYR B 451   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TYR B 904   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    TYR C 451   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TYR C 904   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  32     -117.39     51.72                                   
REMARK 500    PHE A  59       19.87     59.97                                   
REMARK 500    ASN A  87     -124.39     53.91                                   
REMARK 500    SER A  98       17.80   -143.63                                   
REMARK 500    ALA A 123     -104.45     64.89                                   
REMARK 500    LEU A 441      -54.36   -142.34                                   
REMARK 500    THR A 618      -75.07   -131.72                                   
REMARK 500    ASP A 663      -80.93   -118.00                                   
REMARK 500    CYS A1032      -52.46   -139.61                                   
REMARK 500    ASP A1041       15.64     58.22                                   
REMARK 500    CYS A1043       51.70   -119.14                                   
REMARK 500    LEU A1049      -66.28   -106.63                                   
REMARK 500    HIS A1083      -80.93   -119.13                                   
REMARK 500    GLU A1111       79.73   -153.98                                   
REMARK 500    PHE B  32     -117.42     51.82                                   
REMARK 500    ASN B  87     -124.38     53.89                                   
REMARK 500    SER B  98       17.87   -143.61                                   
REMARK 500    ALA B 123     -104.46     64.95                                   
REMARK 500    LEU B 441      -54.37   -142.34                                   
REMARK 500    THR B 618      -75.06   -131.68                                   
REMARK 500    ASP B 663      -80.97   -117.98                                   
REMARK 500    CYS B1032      -52.48   -139.61                                   
REMARK 500    ASP B1041       15.55     58.27                                   
REMARK 500    CYS B1043       51.71   -119.14                                   
REMARK 500    LEU B1049      -66.24   -106.63                                   
REMARK 500    HIS B1083      -80.88   -119.19                                   
REMARK 500    GLU B1111       79.73   -154.03                                   
REMARK 500    PHE C  32     -117.37     51.70                                   
REMARK 500    ASN C  87     -124.35     53.88                                   
REMARK 500    SER C  98       17.77   -143.64                                   
REMARK 500    ALA C 123     -104.46     64.91                                   
REMARK 500    LEU C 441      -54.39   -142.35                                   
REMARK 500    THR C 618      -75.02   -131.68                                   
REMARK 500    ASP C 663      -80.90   -118.00                                   
REMARK 500    CYS C1032      -52.44   -139.62                                   
REMARK 500    ASP C1041       15.64     58.22                                   
REMARK 500    CYS C1043       51.67   -119.13                                   
REMARK 500    LEU C1049      -66.27   -106.59                                   
REMARK 500    HIS C1083      -80.89   -119.17                                   
REMARK 500    GLU C1111       79.72   -153.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1301        
REMARK 800  bound to ASN A 61                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1302        
REMARK 800  bound to ASN A 122                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1321        
REMARK 800  bound to ASN A 165                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1303 through NAG A 1304 bound to ASN A 234                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1305        
REMARK 800  bound to ASN A 282                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1306        
REMARK 800  bound to ASN A 331                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1307        
REMARK 800  bound to ASN A 343                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1308        
REMARK 800  bound to ASN A 603                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1309        
REMARK 800  bound to ASN A 616                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1310        
REMARK 800  bound to ASN A 657                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1311        
REMARK 800  bound to ASN A 709                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1312 through NAG A 1313 bound to ASN A 717                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1314 through NAG A 1315 bound to ASN A 801                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1316        
REMARK 800  bound to ASN A 1074                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1317 through NAG A 1318 bound to ASN A 1098                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1319 through NAG A 1320 bound to ASN A 1134                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1301        
REMARK 800  bound to ASN B 61                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1302        
REMARK 800  bound to ASN B 122                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1321        
REMARK 800  bound to ASN B 165                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  1303 through NAG B 1304 bound to ASN B 234                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1305        
REMARK 800  bound to ASN B 282                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1306        
REMARK 800  bound to ASN B 331                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1307        
REMARK 800  bound to ASN B 343                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1308        
REMARK 800  bound to ASN B 603                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1309        
REMARK 800  bound to ASN B 616                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1310        
REMARK 800  bound to ASN B 657                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1311        
REMARK 800  bound to ASN B 709                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  1312 through NAG B 1313 bound to ASN B 717                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  1314 through NAG B 1315 bound to ASN B 801                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1316        
REMARK 800  bound to ASN B 1074                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  1317 through NAG B 1318 bound to ASN B 1098                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  1319 through NAG B 1320 bound to ASN B 1134                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1301        
REMARK 800  bound to ASN C 61                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1302        
REMARK 800  bound to ASN C 122                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1321        
REMARK 800  bound to ASN C 165                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  1303 through NAG C 1304 bound to ASN C 234                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1305        
REMARK 800  bound to ASN C 282                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1306        
REMARK 800  bound to ASN C 331                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1307        
REMARK 800  bound to ASN C 343                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1308        
REMARK 800  bound to ASN C 603                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1309        
REMARK 800  bound to ASN C 616                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1310        
REMARK 800  bound to ASN C 657                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1311        
REMARK 800  bound to ASN C 709                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  1312 through NAG C 1313 bound to ASN C 717                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  1314 through NAG C 1315 bound to ASN C 801                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 1316        
REMARK 800  bound to ASN C 1074                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  1317 through NAG C 1318 bound to ASN C 1098                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  1319 through NAG C 1320 bound to ASN C 1134                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-21452   RELATED DB: EMDB                             
REMARK 900 STRUCTURE OF THE SARS-COV-2 SPIKE GLYCOPROTEIN (CLOSED STATE)        
REMARK 900 RELATED ID: EMD-21457   RELATED DB: EMDB                             
REMARK 900 STRUCTURE OF THE SARS-COV-2 SPIKE GLYCOPROTEIN (OPEN STATE)          
DBREF  6VXX A  -18  1262  PDB    6VXX     6VXX           -18   1262             
DBREF  6VXX B  -18  1262  PDB    6VXX     6VXX           -18   1262             
DBREF  6VXX C  -18  1262  PDB    6VXX     6VXX           -18   1262             
SEQRES   1 A 1281  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU          
SEQRES   2 A 1281  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS          
SEQRES   3 A 1281  VAL ALA GLU THR GLY THR GLN CYS VAL ASN LEU THR THR          
SEQRES   4 A 1281  ARG THR GLN LEU PRO PRO ALA TYR THR ASN SER PHE THR          
SEQRES   5 A 1281  ARG GLY VAL TYR TYR PRO ASP LYS VAL PHE ARG SER SER          
SEQRES   6 A 1281  VAL LEU HIS SER THR GLN ASP LEU PHE LEU PRO PHE PHE          
SEQRES   7 A 1281  SER ASN VAL THR TRP PHE HIS ALA ILE HIS VAL SER GLY          
SEQRES   8 A 1281  THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL LEU PRO          
SEQRES   9 A 1281  PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU LYS SER          
SEQRES  10 A 1281  ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR LEU ASP          
SEQRES  11 A 1281  SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN ALA THR          
SEQRES  12 A 1281  ASN VAL VAL ILE LYS VAL CYS GLU PHE GLN PHE CYS ASN          
SEQRES  13 A 1281  ASP PRO PHE LEU GLY VAL TYR TYR HIS LYS ASN ASN LYS          
SEQRES  14 A 1281  SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SER ALA          
SEQRES  15 A 1281  ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE LEU          
SEQRES  16 A 1281  MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN LEU          
SEQRES  17 A 1281  ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE LYS          
SEQRES  18 A 1281  ILE TYR SER LYS HIS THR PRO ILE ASN LEU VAL ARG ASP          
SEQRES  19 A 1281  LEU PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP          
SEQRES  20 A 1281  LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU          
SEQRES  21 A 1281  LEU ALA LEU HIS ARG SER TYR LEU THR PRO GLY ASP SER          
SEQRES  22 A 1281  SER SER GLY TRP THR ALA GLY ALA ALA ALA TYR TYR VAL          
SEQRES  23 A 1281  GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN          
SEQRES  24 A 1281  GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU          
SEQRES  25 A 1281  ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE          
SEQRES  26 A 1281  THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG          
SEQRES  27 A 1281  VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE          
SEQRES  28 A 1281  THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR          
SEQRES  29 A 1281  ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE          
SEQRES  30 A 1281  SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER          
SEQRES  31 A 1281  ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO          
SEQRES  32 A 1281  THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA          
SEQRES  33 A 1281  ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE          
SEQRES  34 A 1281  ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR          
SEQRES  35 A 1281  LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP          
SEQRES  36 A 1281  ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR          
SEQRES  37 A 1281  ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS          
SEQRES  38 A 1281  PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA          
SEQRES  39 A 1281  GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS          
SEQRES  40 A 1281  TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN          
SEQRES  41 A 1281  GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER          
SEQRES  42 A 1281  PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO          
SEQRES  43 A 1281  LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN          
SEQRES  44 A 1281  PHE ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR          
SEQRES  45 A 1281  GLU SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY          
SEQRES  46 A 1281  ARG ASP ILE ALA ASP THR THR ASP ALA VAL ARG ASP PRO          
SEQRES  47 A 1281  GLN THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE          
SEQRES  48 A 1281  GLY GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER          
SEQRES  49 A 1281  ASN GLN VAL ALA VAL LEU TYR GLN ASP VAL ASN CYS THR          
SEQRES  50 A 1281  GLU VAL PRO VAL ALA ILE HIS ALA ASP GLN LEU THR PRO          
SEQRES  51 A 1281  THR TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN          
SEQRES  52 A 1281  THR ARG ALA GLY CYS LEU ILE GLY ALA GLU HIS VAL ASN          
SEQRES  53 A 1281  ASN SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE          
SEQRES  54 A 1281  CYS ALA SER TYR GLN THR GLN THR ASN SER PRO SER GLY          
SEQRES  55 A 1281  ALA GLY SER VAL ALA SER GLN SER ILE ILE ALA TYR THR          
SEQRES  56 A 1281  MET SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN          
SEQRES  57 A 1281  ASN SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL          
SEQRES  58 A 1281  THR THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER          
SEQRES  59 A 1281  VAL ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU          
SEQRES  60 A 1281  CYS SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR          
SEQRES  61 A 1281  GLN LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN          
SEQRES  62 A 1281  ASP LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN          
SEQRES  63 A 1281  ILE TYR LYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE          
SEQRES  64 A 1281  ASN PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER          
SEQRES  65 A 1281  LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL          
SEQRES  66 A 1281  THR LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP          
SEQRES  67 A 1281  CYS LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA          
SEQRES  68 A 1281  GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU          
SEQRES  69 A 1281  THR ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU          
SEQRES  70 A 1281  ALA GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY          
SEQRES  71 A 1281  ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET ALA TYR          
SEQRES  72 A 1281  ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR          
SEQRES  73 A 1281  GLU ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA          
SEQRES  74 A 1281  ILE GLY LYS ILE GLN ASP SER LEU SER SER THR ALA SER          
SEQRES  75 A 1281  ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA          
SEQRES  76 A 1281  GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER ASN          
SEQRES  77 A 1281  PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER          
SEQRES  78 A 1281  ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG          
SEQRES  79 A 1281  LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL          
SEQRES  80 A 1281  THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER          
SEQRES  81 A 1281  ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU          
SEQRES  82 A 1281  GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR          
SEQRES  83 A 1281  HIS LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL          
SEQRES  84 A 1281  VAL PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS          
SEQRES  85 A 1281  ASN PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS          
SEQRES  86 A 1281  ALA HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY          
SEQRES  87 A 1281  THR HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO          
SEQRES  88 A 1281  GLN ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN          
SEQRES  89 A 1281  CYS ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR          
SEQRES  90 A 1281  ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU          
SEQRES  91 A 1281  LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL          
SEQRES  92 A 1281  ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL          
SEQRES  93 A 1281  ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA          
SEQRES  94 A 1281  LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU          
SEQRES  95 A 1281  GLY LYS TYR GLU GLN TYR ILE LYS GLY SER GLY ARG GLU          
SEQRES  96 A 1281  ASN LEU TYR PHE GLN GLY GLY GLY GLY SER GLY TYR ILE          
SEQRES  97 A 1281  PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS          
SEQRES  98 A 1281  ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY HIS          
SEQRES  99 A 1281  HIS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B 1281  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU          
SEQRES   2 B 1281  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS          
SEQRES   3 B 1281  VAL ALA GLU THR GLY THR GLN CYS VAL ASN LEU THR THR          
SEQRES   4 B 1281  ARG THR GLN LEU PRO PRO ALA TYR THR ASN SER PHE THR          
SEQRES   5 B 1281  ARG GLY VAL TYR TYR PRO ASP LYS VAL PHE ARG SER SER          
SEQRES   6 B 1281  VAL LEU HIS SER THR GLN ASP LEU PHE LEU PRO PHE PHE          
SEQRES   7 B 1281  SER ASN VAL THR TRP PHE HIS ALA ILE HIS VAL SER GLY          
SEQRES   8 B 1281  THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL LEU PRO          
SEQRES   9 B 1281  PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU LYS SER          
SEQRES  10 B 1281  ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR LEU ASP          
SEQRES  11 B 1281  SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN ALA THR          
SEQRES  12 B 1281  ASN VAL VAL ILE LYS VAL CYS GLU PHE GLN PHE CYS ASN          
SEQRES  13 B 1281  ASP PRO PHE LEU GLY VAL TYR TYR HIS LYS ASN ASN LYS          
SEQRES  14 B 1281  SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SER ALA          
SEQRES  15 B 1281  ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE LEU          
SEQRES  16 B 1281  MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN LEU          
SEQRES  17 B 1281  ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE LYS          
SEQRES  18 B 1281  ILE TYR SER LYS HIS THR PRO ILE ASN LEU VAL ARG ASP          
SEQRES  19 B 1281  LEU PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP          
SEQRES  20 B 1281  LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU          
SEQRES  21 B 1281  LEU ALA LEU HIS ARG SER TYR LEU THR PRO GLY ASP SER          
SEQRES  22 B 1281  SER SER GLY TRP THR ALA GLY ALA ALA ALA TYR TYR VAL          
SEQRES  23 B 1281  GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN          
SEQRES  24 B 1281  GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU          
SEQRES  25 B 1281  ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE          
SEQRES  26 B 1281  THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG          
SEQRES  27 B 1281  VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE          
SEQRES  28 B 1281  THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR          
SEQRES  29 B 1281  ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE          
SEQRES  30 B 1281  SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER          
SEQRES  31 B 1281  ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO          
SEQRES  32 B 1281  THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA          
SEQRES  33 B 1281  ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE          
SEQRES  34 B 1281  ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR          
SEQRES  35 B 1281  LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP          
SEQRES  36 B 1281  ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR          
SEQRES  37 B 1281  ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS          
SEQRES  38 B 1281  PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA          
SEQRES  39 B 1281  GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS          
SEQRES  40 B 1281  TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN          
SEQRES  41 B 1281  GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER          
SEQRES  42 B 1281  PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO          
SEQRES  43 B 1281  LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN          
SEQRES  44 B 1281  PHE ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR          
SEQRES  45 B 1281  GLU SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY          
SEQRES  46 B 1281  ARG ASP ILE ALA ASP THR THR ASP ALA VAL ARG ASP PRO          
SEQRES  47 B 1281  GLN THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE          
SEQRES  48 B 1281  GLY GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER          
SEQRES  49 B 1281  ASN GLN VAL ALA VAL LEU TYR GLN ASP VAL ASN CYS THR          
SEQRES  50 B 1281  GLU VAL PRO VAL ALA ILE HIS ALA ASP GLN LEU THR PRO          
SEQRES  51 B 1281  THR TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN          
SEQRES  52 B 1281  THR ARG ALA GLY CYS LEU ILE GLY ALA GLU HIS VAL ASN          
SEQRES  53 B 1281  ASN SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE          
SEQRES  54 B 1281  CYS ALA SER TYR GLN THR GLN THR ASN SER PRO SER GLY          
SEQRES  55 B 1281  ALA GLY SER VAL ALA SER GLN SER ILE ILE ALA TYR THR          
SEQRES  56 B 1281  MET SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN          
SEQRES  57 B 1281  ASN SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL          
SEQRES  58 B 1281  THR THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER          
SEQRES  59 B 1281  VAL ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU          
SEQRES  60 B 1281  CYS SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR          
SEQRES  61 B 1281  GLN LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN          
SEQRES  62 B 1281  ASP LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN          
SEQRES  63 B 1281  ILE TYR LYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE          
SEQRES  64 B 1281  ASN PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER          
SEQRES  65 B 1281  LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL          
SEQRES  66 B 1281  THR LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP          
SEQRES  67 B 1281  CYS LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA          
SEQRES  68 B 1281  GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU          
SEQRES  69 B 1281  THR ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU          
SEQRES  70 B 1281  ALA GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY          
SEQRES  71 B 1281  ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET ALA TYR          
SEQRES  72 B 1281  ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR          
SEQRES  73 B 1281  GLU ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA          
SEQRES  74 B 1281  ILE GLY LYS ILE GLN ASP SER LEU SER SER THR ALA SER          
SEQRES  75 B 1281  ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA          
SEQRES  76 B 1281  GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER ASN          
SEQRES  77 B 1281  PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER          
SEQRES  78 B 1281  ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG          
SEQRES  79 B 1281  LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL          
SEQRES  80 B 1281  THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER          
SEQRES  81 B 1281  ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU          
SEQRES  82 B 1281  GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR          
SEQRES  83 B 1281  HIS LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL          
SEQRES  84 B 1281  VAL PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS          
SEQRES  85 B 1281  ASN PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS          
SEQRES  86 B 1281  ALA HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY          
SEQRES  87 B 1281  THR HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO          
SEQRES  88 B 1281  GLN ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN          
SEQRES  89 B 1281  CYS ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR          
SEQRES  90 B 1281  ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU          
SEQRES  91 B 1281  LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL          
SEQRES  92 B 1281  ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL          
SEQRES  93 B 1281  ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA          
SEQRES  94 B 1281  LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU          
SEQRES  95 B 1281  GLY LYS TYR GLU GLN TYR ILE LYS GLY SER GLY ARG GLU          
SEQRES  96 B 1281  ASN LEU TYR PHE GLN GLY GLY GLY GLY SER GLY TYR ILE          
SEQRES  97 B 1281  PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS          
SEQRES  98 B 1281  ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY HIS          
SEQRES  99 B 1281  HIS HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C 1281  MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU          
SEQRES   2 C 1281  SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS          
SEQRES   3 C 1281  VAL ALA GLU THR GLY THR GLN CYS VAL ASN LEU THR THR          
SEQRES   4 C 1281  ARG THR GLN LEU PRO PRO ALA TYR THR ASN SER PHE THR          
SEQRES   5 C 1281  ARG GLY VAL TYR TYR PRO ASP LYS VAL PHE ARG SER SER          
SEQRES   6 C 1281  VAL LEU HIS SER THR GLN ASP LEU PHE LEU PRO PHE PHE          
SEQRES   7 C 1281  SER ASN VAL THR TRP PHE HIS ALA ILE HIS VAL SER GLY          
SEQRES   8 C 1281  THR ASN GLY THR LYS ARG PHE ASP ASN PRO VAL LEU PRO          
SEQRES   9 C 1281  PHE ASN ASP GLY VAL TYR PHE ALA SER THR GLU LYS SER          
SEQRES  10 C 1281  ASN ILE ILE ARG GLY TRP ILE PHE GLY THR THR LEU ASP          
SEQRES  11 C 1281  SER LYS THR GLN SER LEU LEU ILE VAL ASN ASN ALA THR          
SEQRES  12 C 1281  ASN VAL VAL ILE LYS VAL CYS GLU PHE GLN PHE CYS ASN          
SEQRES  13 C 1281  ASP PRO PHE LEU GLY VAL TYR TYR HIS LYS ASN ASN LYS          
SEQRES  14 C 1281  SER TRP MET GLU SER GLU PHE ARG VAL TYR SER SER ALA          
SEQRES  15 C 1281  ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO PHE LEU          
SEQRES  16 C 1281  MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS ASN LEU          
SEQRES  17 C 1281  ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR PHE LYS          
SEQRES  18 C 1281  ILE TYR SER LYS HIS THR PRO ILE ASN LEU VAL ARG ASP          
SEQRES  19 C 1281  LEU PRO GLN GLY PHE SER ALA LEU GLU PRO LEU VAL ASP          
SEQRES  20 C 1281  LEU PRO ILE GLY ILE ASN ILE THR ARG PHE GLN THR LEU          
SEQRES  21 C 1281  LEU ALA LEU HIS ARG SER TYR LEU THR PRO GLY ASP SER          
SEQRES  22 C 1281  SER SER GLY TRP THR ALA GLY ALA ALA ALA TYR TYR VAL          
SEQRES  23 C 1281  GLY TYR LEU GLN PRO ARG THR PHE LEU LEU LYS TYR ASN          
SEQRES  24 C 1281  GLU ASN GLY THR ILE THR ASP ALA VAL ASP CYS ALA LEU          
SEQRES  25 C 1281  ASP PRO LEU SER GLU THR LYS CYS THR LEU LYS SER PHE          
SEQRES  26 C 1281  THR VAL GLU LYS GLY ILE TYR GLN THR SER ASN PHE ARG          
SEQRES  27 C 1281  VAL GLN PRO THR GLU SER ILE VAL ARG PHE PRO ASN ILE          
SEQRES  28 C 1281  THR ASN LEU CYS PRO PHE GLY GLU VAL PHE ASN ALA THR          
SEQRES  29 C 1281  ARG PHE ALA SER VAL TYR ALA TRP ASN ARG LYS ARG ILE          
SEQRES  30 C 1281  SER ASN CYS VAL ALA ASP TYR SER VAL LEU TYR ASN SER          
SEQRES  31 C 1281  ALA SER PHE SER THR PHE LYS CYS TYR GLY VAL SER PRO          
SEQRES  32 C 1281  THR LYS LEU ASN ASP LEU CYS PHE THR ASN VAL TYR ALA          
SEQRES  33 C 1281  ASP SER PHE VAL ILE ARG GLY ASP GLU VAL ARG GLN ILE          
SEQRES  34 C 1281  ALA PRO GLY GLN THR GLY LYS ILE ALA ASP TYR ASN TYR          
SEQRES  35 C 1281  LYS LEU PRO ASP ASP PHE THR GLY CYS VAL ILE ALA TRP          
SEQRES  36 C 1281  ASN SER ASN ASN LEU ASP SER LYS VAL GLY GLY ASN TYR          
SEQRES  37 C 1281  ASN TYR LEU TYR ARG LEU PHE ARG LYS SER ASN LEU LYS          
SEQRES  38 C 1281  PRO PHE GLU ARG ASP ILE SER THR GLU ILE TYR GLN ALA          
SEQRES  39 C 1281  GLY SER THR PRO CYS ASN GLY VAL GLU GLY PHE ASN CYS          
SEQRES  40 C 1281  TYR PHE PRO LEU GLN SER TYR GLY PHE GLN PRO THR ASN          
SEQRES  41 C 1281  GLY VAL GLY TYR GLN PRO TYR ARG VAL VAL VAL LEU SER          
SEQRES  42 C 1281  PHE GLU LEU LEU HIS ALA PRO ALA THR VAL CYS GLY PRO          
SEQRES  43 C 1281  LYS LYS SER THR ASN LEU VAL LYS ASN LYS CYS VAL ASN          
SEQRES  44 C 1281  PHE ASN PHE ASN GLY LEU THR GLY THR GLY VAL LEU THR          
SEQRES  45 C 1281  GLU SER ASN LYS LYS PHE LEU PRO PHE GLN GLN PHE GLY          
SEQRES  46 C 1281  ARG ASP ILE ALA ASP THR THR ASP ALA VAL ARG ASP PRO          
SEQRES  47 C 1281  GLN THR LEU GLU ILE LEU ASP ILE THR PRO CYS SER PHE          
SEQRES  48 C 1281  GLY GLY VAL SER VAL ILE THR PRO GLY THR ASN THR SER          
SEQRES  49 C 1281  ASN GLN VAL ALA VAL LEU TYR GLN ASP VAL ASN CYS THR          
SEQRES  50 C 1281  GLU VAL PRO VAL ALA ILE HIS ALA ASP GLN LEU THR PRO          
SEQRES  51 C 1281  THR TRP ARG VAL TYR SER THR GLY SER ASN VAL PHE GLN          
SEQRES  52 C 1281  THR ARG ALA GLY CYS LEU ILE GLY ALA GLU HIS VAL ASN          
SEQRES  53 C 1281  ASN SER TYR GLU CYS ASP ILE PRO ILE GLY ALA GLY ILE          
SEQRES  54 C 1281  CYS ALA SER TYR GLN THR GLN THR ASN SER PRO SER GLY          
SEQRES  55 C 1281  ALA GLY SER VAL ALA SER GLN SER ILE ILE ALA TYR THR          
SEQRES  56 C 1281  MET SER LEU GLY ALA GLU ASN SER VAL ALA TYR SER ASN          
SEQRES  57 C 1281  ASN SER ILE ALA ILE PRO THR ASN PHE THR ILE SER VAL          
SEQRES  58 C 1281  THR THR GLU ILE LEU PRO VAL SER MET THR LYS THR SER          
SEQRES  59 C 1281  VAL ASP CYS THR MET TYR ILE CYS GLY ASP SER THR GLU          
SEQRES  60 C 1281  CYS SER ASN LEU LEU LEU GLN TYR GLY SER PHE CYS THR          
SEQRES  61 C 1281  GLN LEU ASN ARG ALA LEU THR GLY ILE ALA VAL GLU GLN          
SEQRES  62 C 1281  ASP LYS ASN THR GLN GLU VAL PHE ALA GLN VAL LYS GLN          
SEQRES  63 C 1281  ILE TYR LYS THR PRO PRO ILE LYS ASP PHE GLY GLY PHE          
SEQRES  64 C 1281  ASN PHE SER GLN ILE LEU PRO ASP PRO SER LYS PRO SER          
SEQRES  65 C 1281  LYS ARG SER PHE ILE GLU ASP LEU LEU PHE ASN LYS VAL          
SEQRES  66 C 1281  THR LEU ALA ASP ALA GLY PHE ILE LYS GLN TYR GLY ASP          
SEQRES  67 C 1281  CYS LEU GLY ASP ILE ALA ALA ARG ASP LEU ILE CYS ALA          
SEQRES  68 C 1281  GLN LYS PHE ASN GLY LEU THR VAL LEU PRO PRO LEU LEU          
SEQRES  69 C 1281  THR ASP GLU MET ILE ALA GLN TYR THR SER ALA LEU LEU          
SEQRES  70 C 1281  ALA GLY THR ILE THR SER GLY TRP THR PHE GLY ALA GLY          
SEQRES  71 C 1281  ALA ALA LEU GLN ILE PRO PHE ALA MET GLN MET ALA TYR          
SEQRES  72 C 1281  ARG PHE ASN GLY ILE GLY VAL THR GLN ASN VAL LEU TYR          
SEQRES  73 C 1281  GLU ASN GLN LYS LEU ILE ALA ASN GLN PHE ASN SER ALA          
SEQRES  74 C 1281  ILE GLY LYS ILE GLN ASP SER LEU SER SER THR ALA SER          
SEQRES  75 C 1281  ALA LEU GLY LYS LEU GLN ASP VAL VAL ASN GLN ASN ALA          
SEQRES  76 C 1281  GLN ALA LEU ASN THR LEU VAL LYS GLN LEU SER SER ASN          
SEQRES  77 C 1281  PHE GLY ALA ILE SER SER VAL LEU ASN ASP ILE LEU SER          
SEQRES  78 C 1281  ARG LEU ASP PRO PRO GLU ALA GLU VAL GLN ILE ASP ARG          
SEQRES  79 C 1281  LEU ILE THR GLY ARG LEU GLN SER LEU GLN THR TYR VAL          
SEQRES  80 C 1281  THR GLN GLN LEU ILE ARG ALA ALA GLU ILE ARG ALA SER          
SEQRES  81 C 1281  ALA ASN LEU ALA ALA THR LYS MET SER GLU CYS VAL LEU          
SEQRES  82 C 1281  GLY GLN SER LYS ARG VAL ASP PHE CYS GLY LYS GLY TYR          
SEQRES  83 C 1281  HIS LEU MET SER PHE PRO GLN SER ALA PRO HIS GLY VAL          
SEQRES  84 C 1281  VAL PHE LEU HIS VAL THR TYR VAL PRO ALA GLN GLU LYS          
SEQRES  85 C 1281  ASN PHE THR THR ALA PRO ALA ILE CYS HIS ASP GLY LYS          
SEQRES  86 C 1281  ALA HIS PHE PRO ARG GLU GLY VAL PHE VAL SER ASN GLY          
SEQRES  87 C 1281  THR HIS TRP PHE VAL THR GLN ARG ASN PHE TYR GLU PRO          
SEQRES  88 C 1281  GLN ILE ILE THR THR ASP ASN THR PHE VAL SER GLY ASN          
SEQRES  89 C 1281  CYS ASP VAL VAL ILE GLY ILE VAL ASN ASN THR VAL TYR          
SEQRES  90 C 1281  ASP PRO LEU GLN PRO GLU LEU ASP SER PHE LYS GLU GLU          
SEQRES  91 C 1281  LEU ASP LYS TYR PHE LYS ASN HIS THR SER PRO ASP VAL          
SEQRES  92 C 1281  ASP LEU GLY ASP ILE SER GLY ILE ASN ALA SER VAL VAL          
SEQRES  93 C 1281  ASN ILE GLN LYS GLU ILE ASP ARG LEU ASN GLU VAL ALA          
SEQRES  94 C 1281  LYS ASN LEU ASN GLU SER LEU ILE ASP LEU GLN GLU LEU          
SEQRES  95 C 1281  GLY LYS TYR GLU GLN TYR ILE LYS GLY SER GLY ARG GLU          
SEQRES  96 C 1281  ASN LEU TYR PHE GLN GLY GLY GLY GLY SER GLY TYR ILE          
SEQRES  97 C 1281  PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG LYS          
SEQRES  98 C 1281  ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY HIS          
SEQRES  99 C 1281  HIS HIS HIS HIS HIS HIS HIS                                  
HET    NAG  A1301      14                                                       
HET    NAG  A1302      14                                                       
HET    NAG  A1303      14                                                       
HET    NAG  A1304      14                                                       
HET    NAG  A1305      14                                                       
HET    NAG  A1306      14                                                       
HET    NAG  A1307      14                                                       
HET    NAG  A1308      14                                                       
HET    NAG  A1309      14                                                       
HET    NAG  A1310      14                                                       
HET    NAG  A1311      14                                                       
HET    NAG  A1312      14                                                       
HET    NAG  A1313      14                                                       
HET    NAG  A1314      14                                                       
HET    NAG  A1315      14                                                       
HET    NAG  A1316      14                                                       
HET    NAG  A1317      14                                                       
HET    NAG  A1318      14                                                       
HET    NAG  A1319      14                                                       
HET    NAG  A1320      14                                                       
HET    NAG  A1321      14                                                       
HET    NAG  B1301      14                                                       
HET    NAG  B1302      14                                                       
HET    NAG  B1303      14                                                       
HET    NAG  B1304      14                                                       
HET    NAG  B1305      14                                                       
HET    NAG  B1306      14                                                       
HET    NAG  B1307      14                                                       
HET    NAG  B1308      14                                                       
HET    NAG  B1309      14                                                       
HET    NAG  B1310      14                                                       
HET    NAG  B1311      14                                                       
HET    NAG  B1312      14                                                       
HET    NAG  B1313      14                                                       
HET    NAG  B1314      14                                                       
HET    NAG  B1315      14                                                       
HET    NAG  B1316      14                                                       
HET    NAG  B1317      14                                                       
HET    NAG  B1318      14                                                       
HET    NAG  B1319      14                                                       
HET    NAG  B1320      14                                                       
HET    NAG  B1321      14                                                       
HET    NAG  C1301      14                                                       
HET    NAG  C1302      14                                                       
HET    NAG  C1303      14                                                       
HET    NAG  C1304      14                                                       
HET    NAG  C1305      14                                                       
HET    NAG  C1306      14                                                       
HET    NAG  C1307      14                                                       
HET    NAG  C1308      14                                                       
HET    NAG  C1309      14                                                       
HET    NAG  C1310      14                                                       
HET    NAG  C1311      14                                                       
HET    NAG  C1312      14                                                       
HET    NAG  C1313      14                                                       
HET    NAG  C1314      14                                                       
HET    NAG  C1315      14                                                       
HET    NAG  C1316      14                                                       
HET    NAG  C1317      14                                                       
HET    NAG  C1318      14                                                       
HET    NAG  C1319      14                                                       
HET    NAG  C1320      14                                                       
HET    NAG  C1321      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   4  NAG    63(C8 H15 N O6)                                              
HELIX    1 AA1 ASP A  294  LEU A  303  1                                  10    
HELIX    2 AA2 PHE A  338  ASN A  343  1                                   6    
HELIX    3 AA3 SER A  349  TRP A  353  5                                   5    
HELIX    4 AA4 ASP A  364  SER A  371  1                                   8    
HELIX    5 AA5 ASP A  405  ILE A  410  5                                   6    
HELIX    6 AA6 ASP A  737  CYS A  743  1                                   7    
HELIX    7 AA7 SER A  746  LEU A  754  1                                   9    
HELIX    8 AA8 GLN A  755  PHE A  759  5                                   5    
HELIX    9 AA9 CYS A  760  ALA A  783  1                                  24    
HELIX   10 AB1 SER A  816  ASN A  824  1                                   9    
HELIX   11 AB2 THR A  866  GLY A  885  1                                  20    
HELIX   12 AB3 TRP A  886  GLY A  891  1                                   6    
HELIX   13 AB4 PRO A  897  GLY A  908  1                                  12    
HELIX   14 AB5 GLN A  913  ASN A  919  1                                   7    
HELIX   15 AB6 ASN A  919  THR A  941  1                                  23    
HELIX   16 AB7 ALA A  942  ALA A  944  5                                   3    
HELIX   17 AB8 LEU A  945  GLN A  965  1                                  21    
HELIX   18 AB9 LEU A  966  SER A  968  5                                   3    
HELIX   19 AC1 VAL A  976  SER A  982  1                                   7    
HELIX   20 AC2 ASP A  985  VAL A 1033  1                                  49    
HELIX   21 AC3 LEU A 1141  SER A 1147  1                                   7    
HELIX   22 AC4 ASP B  294  LEU B  303  1                                  10    
HELIX   23 AC5 PHE B  338  ASN B  343  1                                   6    
HELIX   24 AC6 SER B  349  TRP B  353  5                                   5    
HELIX   25 AC7 ASP B  364  SER B  371  1                                   8    
HELIX   26 AC8 ASP B  405  ILE B  410  5                                   6    
HELIX   27 AC9 ASP B  737  CYS B  743  1                                   7    
HELIX   28 AD1 SER B  746  LEU B  754  1                                   9    
HELIX   29 AD2 GLN B  755  PHE B  759  5                                   5    
HELIX   30 AD3 CYS B  760  ALA B  783  1                                  24    
HELIX   31 AD4 SER B  816  ASN B  824  1                                   9    
HELIX   32 AD5 THR B  866  GLY B  885  1                                  20    
HELIX   33 AD6 TRP B  886  GLY B  891  1                                   6    
HELIX   34 AD7 PRO B  897  GLY B  908  1                                  12    
HELIX   35 AD8 GLN B  913  ASN B  919  1                                   7    
HELIX   36 AD9 ASN B  919  THR B  941  1                                  23    
HELIX   37 AE1 ALA B  942  ALA B  944  5                                   3    
HELIX   38 AE2 LEU B  945  GLN B  965  1                                  21    
HELIX   39 AE3 LEU B  966  SER B  968  5                                   3    
HELIX   40 AE4 VAL B  976  SER B  982  1                                   7    
HELIX   41 AE5 ASP B  985  VAL B 1033  1                                  49    
HELIX   42 AE6 LEU B 1141  SER B 1147  1                                   7    
HELIX   43 AE7 ASP C  294  LEU C  303  1                                  10    
HELIX   44 AE8 PHE C  338  ASN C  343  1                                   6    
HELIX   45 AE9 SER C  349  TRP C  353  5                                   5    
HELIX   46 AF1 ASP C  364  SER C  371  1                                   8    
HELIX   47 AF2 ASP C  405  ILE C  410  5                                   6    
HELIX   48 AF3 ASP C  737  CYS C  743  1                                   7    
HELIX   49 AF4 SER C  746  LEU C  754  1                                   9    
HELIX   50 AF5 GLN C  755  PHE C  759  5                                   5    
HELIX   51 AF6 CYS C  760  ALA C  783  1                                  24    
HELIX   52 AF7 SER C  816  ASN C  824  1                                   9    
HELIX   53 AF8 THR C  866  GLY C  885  1                                  20    
HELIX   54 AF9 TRP C  886  GLY C  891  1                                   6    
HELIX   55 AG1 PRO C  897  GLY C  908  1                                  12    
HELIX   56 AG2 GLN C  913  ASN C  919  1                                   7    
HELIX   57 AG3 ASN C  919  THR C  941  1                                  23    
HELIX   58 AG4 ALA C  942  ALA C  944  5                                   3    
HELIX   59 AG5 LEU C  945  GLN C  965  1                                  21    
HELIX   60 AG6 LEU C  966  SER C  968  5                                   3    
HELIX   61 AG7 VAL C  976  SER C  982  1                                   7    
HELIX   62 AG8 ASP C  985  VAL C 1033  1                                  49    
HELIX   63 AG9 LEU C 1141  SER C 1147  1                                   7    
SHEET    1 AA1 7 TYR A  28  ASN A  30  0                                        
SHEET    2 AA1 7 ASN A  61  PHE A  65 -1  O  VAL A  62   N  THR A  29           
SHEET    3 AA1 7 TYR A 265  TYR A 269 -1  O  TYR A 265   N  PHE A  65           
SHEET    4 AA1 7 VAL A  90  GLU A  96 -1  N  ALA A  93   O  TYR A 266           
SHEET    5 AA1 7 ASN A 188  ILE A 197 -1  O  PHE A 192   N  PHE A  92           
SHEET    6 AA1 7 TYR A 200  PRO A 209 -1  O  THR A 208   N  LEU A 189           
SHEET    7 AA1 7 GLU A 224  LEU A 229 -1  O  LEU A 226   N  ILE A 203           
SHEET    1 AA2 7 VAL A  42  PHE A  43  0                                        
SHEET    2 AA2 7 PHE C 565  ARG C 567  1  O  PHE C 565   N  PHE A  43           
SHEET    3 AA2 7 THR C 573  ARG C 577 -1  O  ALA C 575   N  GLY C 566           
SHEET    4 AA2 7 ILE C 584  THR C 588 -1  O  LEU C 585   N  VAL C 576           
SHEET    5 AA2 7 LEU C 546  GLU C 554 -1  N  VAL C 551   O  THR C 588           
SHEET    6 AA2 7 CYS C 538  PHE C 543 -1  N  PHE C 543   O  LEU C 546           
SHEET    7 AA2 7 SER C 325  ARG C 328  1  N  ARG C 328   O  ASN C 542           
SHEET    1 AA3 3 VAL A  47  PHE A  55  0                                        
SHEET    2 AA3 3 GLN A 271  TYR A 279 -1  O  LEU A 277   N  HIS A  49           
SHEET    3 AA3 3 ILE A 285  ASP A 290 -1  O  THR A 286   N  LYS A 278           
SHEET    1 AA4 3 VAL A  83  PRO A  85  0                                        
SHEET    2 AA4 3 ARG A 237  LEU A 244 -1  O  PHE A 238   N  LEU A  84           
SHEET    3 AA4 3 LEU A 141  GLY A 142  1  N  LEU A 141   O  LEU A 244           
SHEET    1 AA5 6 VAL A  83  PRO A  85  0                                        
SHEET    2 AA5 6 ARG A 237  LEU A 244 -1  O  PHE A 238   N  LEU A  84           
SHEET    3 AA5 6 ILE A 101  GLY A 107 -1  N  ILE A 105   O  GLN A 239           
SHEET    4 AA5 6 LEU A 117  ASN A 122 -1  O  ASN A 121   N  ARG A 102           
SHEET    5 AA5 6 ASN A 125  LYS A 129 -1  O  LYS A 129   N  LEU A 118           
SHEET    6 AA5 6 GLU A 169  VAL A 171 -1  O  TYR A 170   N  ILE A 128           
SHEET    1 AA6 5 GLY A 311  ARG A 319  0                                        
SHEET    2 AA6 5 PHE A 592  THR A 599 -1  O  GLY A 593   N  PHE A 318           
SHEET    3 AA6 5 ALA A 609  GLN A 613 -1  O  ALA A 609   N  ILE A 598           
SHEET    4 AA6 5 GLY A 648  ILE A 651 -1  O  ILE A 651   N  VAL A 610           
SHEET    5 AA6 5 VAL A 642  THR A 645 -1  N  PHE A 643   O  LEU A 650           
SHEET    1 AA7 7 SER A 325  ARG A 328  0                                        
SHEET    2 AA7 7 CYS A 538  PHE A 543  1  O  ASN A 542   N  ARG A 328           
SHEET    3 AA7 7 LEU A 546  GLU A 554 -1  O  LEU A 546   N  PHE A 543           
SHEET    4 AA7 7 ILE A 584  THR A 588 -1  O  THR A 588   N  VAL A 551           
SHEET    5 AA7 7 THR A 573  ARG A 577 -1  N  VAL A 576   O  LEU A 585           
SHEET    6 AA7 7 PHE A 565  ARG A 567 -1  N  GLY A 566   O  ALA A 575           
SHEET    7 AA7 7 VAL B  42  PHE B  43  1  O  PHE B  43   N  PHE A 565           
SHEET    1 AA8 5 ASN A 354  ILE A 358  0                                        
SHEET    2 AA8 5 ASN A 394  ARG A 403 -1  O  VAL A 395   N  ILE A 358           
SHEET    3 AA8 5 PRO A 507  GLU A 516 -1  O  TYR A 508   N  ILE A 402           
SHEET    4 AA8 5 GLY A 431  ASN A 437 -1  N  CYS A 432   O  LEU A 513           
SHEET    5 AA8 5 THR A 376  CYS A 379 -1  N  LYS A 378   O  VAL A 433           
SHEET    1 AA9 2 CYS A 361  VAL A 362  0                                        
SHEET    2 AA9 2 VAL A 524  CYS A 525  1  O  CYS A 525   N  CYS A 361           
SHEET    1 AB1 2 ASN A 448  TYR A 453  0                                        
SHEET    2 AB1 2 GLN A 493  PHE A 497 -1  O  GLN A 493   N  TYR A 453           
SHEET    1 AB2 4 GLU A 654  HIS A 655  0                                        
SHEET    2 AB2 4 SER A 691  THR A 696  1  O  ALA A 694   N  GLU A 654           
SHEET    3 AB2 4 ILE A 670  GLN A 675 -1  N  SER A 673   O  ILE A 693           
SHEET    4 AB2 4 ILE A 664  GLY A 667 -1  N  ILE A 664   O  ALA A 672           
SHEET    1 AB3 2 ALA A 701  GLU A 702  0                                        
SHEET    2 AB3 2 GLN B 787  ILE B 788  1  O  ILE B 788   N  ALA A 701           
SHEET    1 AB4 3 SER A 711  PRO A 728  0                                        
SHEET    2 AB4 3 GLY A1059  ALA A1078 -1  O  PHE A1062   N  GLU A 725           
SHEET    3 AB4 3 TYR A1047  ALA A1056 -1  N  GLN A1054   O  VAL A1061           
SHEET    1 AB5 5 SER A 711  PRO A 728  0                                        
SHEET    2 AB5 5 GLY A1059  ALA A1078 -1  O  PHE A1062   N  GLU A 725           
SHEET    3 AB5 5 VAL A1094  SER A1097 -1  O  SER A1097   N  THR A1076           
SHEET    4 AB5 5 TRP A1102  THR A1105 -1  O  PHE A1103   N  VAL A1096           
SHEET    5 AB5 5 GLN A1113  ILE A1114 -1  O  GLN A1113   N  VAL A1104           
SHEET    1 AB6 2 LYS A 733  VAL A 736  0                                        
SHEET    2 AB6 2 LEU A 858  LEU A 861 -1  O  LEU A 861   N  LYS A 733           
SHEET    1 AB7 2 GLN A 787  ILE A 788  0                                        
SHEET    2 AB7 2 ALA C 701  GLU C 702  1  O  ALA C 701   N  ILE A 788           
SHEET    1 AB8 4 THR A1120  ASN A1125  0                                        
SHEET    2 AB8 4 LYS A1086  PRO A1090 -1  N  PHE A1089   O  PHE A1121           
SHEET    3 AB8 4 ILE A1081  CYS A1082 -1  N  ILE A1081   O  HIS A1088           
SHEET    4 AB8 4 VAL A1133  ASN A1134  1  O  VAL A1133   N  CYS A1082           
SHEET    1 AB9 7 TYR B  28  ASN B  30  0                                        
SHEET    2 AB9 7 ASN B  61  PHE B  65 -1  O  VAL B  62   N  THR B  29           
SHEET    3 AB9 7 TYR B 265  TYR B 269 -1  O  TYR B 265   N  PHE B  65           
SHEET    4 AB9 7 VAL B  90  GLU B  96 -1  N  ALA B  93   O  TYR B 266           
SHEET    5 AB9 7 ASN B 188  ILE B 197 -1  O  PHE B 192   N  PHE B  92           
SHEET    6 AB9 7 TYR B 200  PRO B 209 -1  O  THR B 208   N  LEU B 189           
SHEET    7 AB9 7 GLU B 224  LEU B 229 -1  O  LEU B 226   N  ILE B 203           
SHEET    1 AC1 3 VAL B  47  PHE B  55  0                                        
SHEET    2 AC1 3 GLN B 271  TYR B 279 -1  O  LEU B 277   N  HIS B  49           
SHEET    3 AC1 3 ILE B 285  ASP B 290 -1  O  THR B 286   N  LYS B 278           
SHEET    1 AC2 3 VAL B  83  PRO B  85  0                                        
SHEET    2 AC2 3 ARG B 237  LEU B 244 -1  O  PHE B 238   N  LEU B  84           
SHEET    3 AC2 3 LEU B 141  GLY B 142  1  N  LEU B 141   O  LEU B 244           
SHEET    1 AC3 6 VAL B  83  PRO B  85  0                                        
SHEET    2 AC3 6 ARG B 237  LEU B 244 -1  O  PHE B 238   N  LEU B  84           
SHEET    3 AC3 6 ILE B 101  GLY B 107 -1  N  ILE B 105   O  GLN B 239           
SHEET    4 AC3 6 LEU B 117  ASN B 122 -1  O  ASN B 121   N  ARG B 102           
SHEET    5 AC3 6 ASN B 125  LYS B 129 -1  O  LYS B 129   N  LEU B 118           
SHEET    6 AC3 6 GLU B 169  VAL B 171 -1  O  TYR B 170   N  ILE B 128           
SHEET    1 AC4 5 GLY B 311  ARG B 319  0                                        
SHEET    2 AC4 5 PHE B 592  THR B 599 -1  O  GLY B 593   N  PHE B 318           
SHEET    3 AC4 5 ALA B 609  GLN B 613 -1  O  ALA B 609   N  ILE B 598           
SHEET    4 AC4 5 GLY B 648  ILE B 651 -1  O  ILE B 651   N  VAL B 610           
SHEET    5 AC4 5 VAL B 642  THR B 645 -1  N  PHE B 643   O  LEU B 650           
SHEET    1 AC5 7 SER B 325  ARG B 328  0                                        
SHEET    2 AC5 7 CYS B 538  PHE B 543  1  O  ASN B 542   N  ARG B 328           
SHEET    3 AC5 7 LEU B 546  GLU B 554 -1  O  LEU B 546   N  PHE B 543           
SHEET    4 AC5 7 ILE B 584  THR B 588 -1  O  THR B 588   N  VAL B 551           
SHEET    5 AC5 7 THR B 573  ARG B 577 -1  N  VAL B 576   O  LEU B 585           
SHEET    6 AC5 7 PHE B 565  ARG B 567 -1  N  GLY B 566   O  ALA B 575           
SHEET    7 AC5 7 VAL C  42  PHE C  43  1  O  PHE C  43   N  PHE B 565           
SHEET    1 AC6 5 ASN B 354  ILE B 358  0                                        
SHEET    2 AC6 5 ASN B 394  ARG B 403 -1  O  VAL B 395   N  ILE B 358           
SHEET    3 AC6 5 PRO B 507  GLU B 516 -1  O  TYR B 508   N  ILE B 402           
SHEET    4 AC6 5 GLY B 431  ASN B 437 -1  N  CYS B 432   O  LEU B 513           
SHEET    5 AC6 5 THR B 376  CYS B 379 -1  N  LYS B 378   O  VAL B 433           
SHEET    1 AC7 2 CYS B 361  VAL B 362  0                                        
SHEET    2 AC7 2 VAL B 524  CYS B 525  1  O  CYS B 525   N  CYS B 361           
SHEET    1 AC8 2 ASN B 448  TYR B 453  0                                        
SHEET    2 AC8 2 GLN B 493  PHE B 497 -1  O  GLN B 493   N  TYR B 453           
SHEET    1 AC9 4 GLU B 654  HIS B 655  0                                        
SHEET    2 AC9 4 SER B 691  THR B 696  1  O  ALA B 694   N  GLU B 654           
SHEET    3 AC9 4 ILE B 670  GLN B 675 -1  N  SER B 673   O  ILE B 693           
SHEET    4 AC9 4 ILE B 664  GLY B 667 -1  N  ILE B 664   O  ALA B 672           
SHEET    1 AD1 2 ALA B 701  GLU B 702  0                                        
SHEET    2 AD1 2 GLN C 787  ILE C 788  1  O  ILE C 788   N  ALA B 701           
SHEET    1 AD2 3 SER B 711  PRO B 728  0                                        
SHEET    2 AD2 3 GLY B1059  ALA B1078 -1  O  PHE B1062   N  GLU B 725           
SHEET    3 AD2 3 TYR B1047  ALA B1056 -1  N  GLN B1054   O  VAL B1061           
SHEET    1 AD3 5 SER B 711  PRO B 728  0                                        
SHEET    2 AD3 5 GLY B1059  ALA B1078 -1  O  PHE B1062   N  GLU B 725           
SHEET    3 AD3 5 VAL B1094  SER B1097 -1  O  SER B1097   N  THR B1076           
SHEET    4 AD3 5 TRP B1102  THR B1105 -1  O  PHE B1103   N  VAL B1096           
SHEET    5 AD3 5 GLN B1113  ILE B1114 -1  O  GLN B1113   N  VAL B1104           
SHEET    1 AD4 2 LYS B 733  VAL B 736  0                                        
SHEET    2 AD4 2 LEU B 858  LEU B 861 -1  O  LEU B 861   N  LYS B 733           
SHEET    1 AD5 4 THR B1120  ASN B1125  0                                        
SHEET    2 AD5 4 LYS B1086  PRO B1090 -1  N  PHE B1089   O  PHE B1121           
SHEET    3 AD5 4 ILE B1081  CYS B1082 -1  N  ILE B1081   O  HIS B1088           
SHEET    4 AD5 4 VAL B1133  ASN B1134  1  O  VAL B1133   N  CYS B1082           
SHEET    1 AD6 7 TYR C  28  ASN C  30  0                                        
SHEET    2 AD6 7 ASN C  61  PHE C  65 -1  O  VAL C  62   N  THR C  29           
SHEET    3 AD6 7 TYR C 265  TYR C 269 -1  O  TYR C 265   N  PHE C  65           
SHEET    4 AD6 7 VAL C  90  GLU C  96 -1  N  ALA C  93   O  TYR C 266           
SHEET    5 AD6 7 ASN C 188  ILE C 197 -1  O  PHE C 192   N  PHE C  92           
SHEET    6 AD6 7 TYR C 200  PRO C 209 -1  O  THR C 208   N  LEU C 189           
SHEET    7 AD6 7 GLU C 224  LEU C 229 -1  O  LEU C 226   N  ILE C 203           
SHEET    1 AD7 3 VAL C  47  PHE C  55  0                                        
SHEET    2 AD7 3 GLN C 271  TYR C 279 -1  O  LEU C 277   N  HIS C  49           
SHEET    3 AD7 3 ILE C 285  ASP C 290 -1  O  THR C 286   N  LYS C 278           
SHEET    1 AD8 3 VAL C  83  PRO C  85  0                                        
SHEET    2 AD8 3 ARG C 237  LEU C 244 -1  O  PHE C 238   N  LEU C  84           
SHEET    3 AD8 3 LEU C 141  GLY C 142  1  N  LEU C 141   O  LEU C 244           
SHEET    1 AD9 6 VAL C  83  PRO C  85  0                                        
SHEET    2 AD9 6 ARG C 237  LEU C 244 -1  O  PHE C 238   N  LEU C  84           
SHEET    3 AD9 6 ILE C 101  GLY C 107 -1  N  ILE C 105   O  GLN C 239           
SHEET    4 AD9 6 LEU C 117  ASN C 122 -1  O  ASN C 121   N  ARG C 102           
SHEET    5 AD9 6 ASN C 125  LYS C 129 -1  O  LYS C 129   N  LEU C 118           
SHEET    6 AD9 6 GLU C 169  VAL C 171 -1  O  TYR C 170   N  ILE C 128           
SHEET    1 AE1 5 GLY C 311  ARG C 319  0                                        
SHEET    2 AE1 5 PHE C 592  THR C 599 -1  O  GLY C 593   N  PHE C 318           
SHEET    3 AE1 5 ALA C 609  GLN C 613 -1  O  ALA C 609   N  ILE C 598           
SHEET    4 AE1 5 GLY C 648  ILE C 651 -1  O  ILE C 651   N  VAL C 610           
SHEET    5 AE1 5 VAL C 642  THR C 645 -1  N  PHE C 643   O  LEU C 650           
SHEET    1 AE2 5 ASN C 354  ILE C 358  0                                        
SHEET    2 AE2 5 ASN C 394  ARG C 403 -1  O  VAL C 395   N  ILE C 358           
SHEET    3 AE2 5 PRO C 507  GLU C 516 -1  O  TYR C 508   N  ILE C 402           
SHEET    4 AE2 5 GLY C 431  ASN C 437 -1  N  CYS C 432   O  LEU C 513           
SHEET    5 AE2 5 THR C 376  CYS C 379 -1  N  LYS C 378   O  VAL C 433           
SHEET    1 AE3 2 CYS C 361  VAL C 362  0                                        
SHEET    2 AE3 2 VAL C 524  CYS C 525  1  O  CYS C 525   N  CYS C 361           
SHEET    1 AE4 2 ASN C 448  TYR C 453  0                                        
SHEET    2 AE4 2 GLN C 493  PHE C 497 -1  O  GLN C 493   N  TYR C 453           
SHEET    1 AE5 4 GLU C 654  HIS C 655  0                                        
SHEET    2 AE5 4 SER C 691  THR C 696  1  O  ALA C 694   N  GLU C 654           
SHEET    3 AE5 4 ILE C 670  GLN C 675 -1  N  SER C 673   O  ILE C 693           
SHEET    4 AE5 4 ILE C 664  GLY C 667 -1  N  ILE C 664   O  ALA C 672           
SHEET    1 AE6 3 SER C 711  PRO C 728  0                                        
SHEET    2 AE6 3 GLY C1059  ALA C1078 -1  O  PHE C1062   N  GLU C 725           
SHEET    3 AE6 3 TYR C1047  ALA C1056 -1  N  GLN C1054   O  VAL C1061           
SHEET    1 AE7 5 SER C 711  PRO C 728  0                                        
SHEET    2 AE7 5 GLY C1059  ALA C1078 -1  O  PHE C1062   N  GLU C 725           
SHEET    3 AE7 5 VAL C1094  SER C1097 -1  O  SER C1097   N  THR C1076           
SHEET    4 AE7 5 TRP C1102  THR C1105 -1  O  PHE C1103   N  VAL C1096           
SHEET    5 AE7 5 GLN C1113  ILE C1114 -1  O  GLN C1113   N  VAL C1104           
SHEET    1 AE8 2 LYS C 733  VAL C 736  0                                        
SHEET    2 AE8 2 LEU C 858  LEU C 861 -1  O  LEU C 861   N  LYS C 733           
SHEET    1 AE9 4 THR C1120  ASN C1125  0                                        
SHEET    2 AE9 4 LYS C1086  PRO C1090 -1  N  PHE C1089   O  PHE C1121           
SHEET    3 AE9 4 ILE C1081  CYS C1082 -1  N  ILE C1081   O  HIS C1088           
SHEET    4 AE9 4 VAL C1133  ASN C1134  1  O  VAL C1133   N  CYS C1082           
SSBOND   1 CYS A  131    CYS A  166                          1555   1555  2.03  
SSBOND   2 CYS A  291    CYS A  301                          1555   1555  2.02  
SSBOND   3 CYS A  336    CYS A  361                          1555   1555  2.02  
SSBOND   4 CYS A  379    CYS A  432                          1555   1555  2.05  
SSBOND   5 CYS A  391    CYS A  525                          1555   1555  2.36  
SSBOND   6 CYS A  538    CYS A  590                          1555   1555  2.02  
SSBOND   7 CYS A  617    CYS A  649                          1555   1555  2.04  
SSBOND   8 CYS A  662    CYS A  671                          1555   1555  2.06  
SSBOND   9 CYS A  738    CYS A  760                          1555   1555  2.03  
SSBOND  10 CYS A  743    CYS A  749                          1555   1555  2.04  
SSBOND  11 CYS A 1032    CYS A 1043                          1555   1555  2.03  
SSBOND  12 CYS A 1082    CYS A 1126                          1555   1555  2.02  
SSBOND  13 CYS B  131    CYS B  166                          1555   1555  2.03  
SSBOND  14 CYS B  291    CYS B  301                          1555   1555  2.02  
SSBOND  15 CYS B  336    CYS B  361                          1555   1555  2.02  
SSBOND  16 CYS B  379    CYS B  432                          1555   1555  2.05  
SSBOND  17 CYS B  391    CYS B  525                          1555   1555  2.36  
SSBOND  18 CYS B  538    CYS B  590                          1555   1555  2.02  
SSBOND  19 CYS B  617    CYS B  649                          1555   1555  2.04  
SSBOND  20 CYS B  662    CYS B  671                          1555   1555  2.06  
SSBOND  21 CYS B  738    CYS B  760                          1555   1555  2.03  
SSBOND  22 CYS B  743    CYS B  749                          1555   1555  2.04  
SSBOND  23 CYS B 1032    CYS B 1043                          1555   1555  2.03  
SSBOND  24 CYS B 1082    CYS B 1126                          1555   1555  2.02  
SSBOND  25 CYS C  131    CYS C  166                          1555   1555  2.03  
SSBOND  26 CYS C  291    CYS C  301                          1555   1555  2.02  
SSBOND  27 CYS C  336    CYS C  361                          1555   1555  2.02  
SSBOND  28 CYS C  379    CYS C  432                          1555   1555  2.05  
SSBOND  29 CYS C  391    CYS C  525                          1555   1555  2.36  
SSBOND  30 CYS C  538    CYS C  590                          1555   1555  2.02  
SSBOND  31 CYS C  617    CYS C  649                          1555   1555  2.04  
SSBOND  32 CYS C  662    CYS C  671                          1555   1555  2.06  
SSBOND  33 CYS C  738    CYS C  760                          1555   1555  2.03  
SSBOND  34 CYS C  743    CYS C  749                          1555   1555  2.04  
SSBOND  35 CYS C 1032    CYS C 1043                          1555   1555  2.03  
SSBOND  36 CYS C 1082    CYS C 1126                          1555   1555  2.02  
LINK         ND2 ASN A  61                 C1  NAG A1301     1555   1555  1.51  
LINK         ND2 ASN A 122                 C1  NAG A1302     1555   1555  1.51  
LINK         ND2 ASN A 165                 C1  NAG A1321     1555   1555  1.53  
LINK         ND2 ASN A 234                 C1  NAG A1303     1555   1555  1.51  
LINK         ND2 ASN A 282                 C1  NAG A1305     1555   1555  1.51  
LINK         ND2 ASN A 331                 C1  NAG A1306     1555   1555  1.52  
LINK         ND2 ASN A 343                 C1  NAG A1307     1555   1555  1.51  
LINK         ND2 ASN A 603                 C1  NAG A1308     1555   1555  1.50  
LINK         ND2 ASN A 616                 C1  NAG A1309     1555   1555  1.51  
LINK         ND2 ASN A 657                 C1  NAG A1310     1555   1555  1.51  
LINK         ND2 ASN A 709                 C1  NAG A1311     1555   1555  1.50  
LINK         ND2 ASN A 717                 C1  NAG A1312     1555   1555  1.50  
LINK         ND2 ASN A 801                 C1  NAG A1314     1555   1555  1.50  
LINK         ND2 ASN A1074                 C1  NAG A1316     1555   1555  1.51  
LINK         ND2 ASN A1098                 C1  NAG A1317     1555   1555  1.51  
LINK         ND2 ASN A1134                 C1  NAG A1319     1555   1555  1.50  
LINK         ND2 ASN B  61                 C1  NAG B1301     1555   1555  1.51  
LINK         ND2 ASN B 122                 C1  NAG B1302     1555   1555  1.51  
LINK         ND2 ASN B 165                 C1  NAG B1321     1555   1555  1.53  
LINK         ND2 ASN B 234                 C1  NAG B1303     1555   1555  1.51  
LINK         ND2 ASN B 282                 C1  NAG B1305     1555   1555  1.51  
LINK         ND2 ASN B 331                 C1  NAG B1306     1555   1555  1.52  
LINK         ND2 ASN B 343                 C1  NAG B1307     1555   1555  1.51  
LINK         ND2 ASN B 603                 C1  NAG B1308     1555   1555  1.50  
LINK         ND2 ASN B 616                 C1  NAG B1309     1555   1555  1.51  
LINK         ND2 ASN B 657                 C1  NAG B1310     1555   1555  1.51  
LINK         ND2 ASN B 709                 C1  NAG B1311     1555   1555  1.50  
LINK         ND2 ASN B 717                 C1  NAG B1312     1555   1555  1.50  
LINK         ND2 ASN B 801                 C1  NAG B1314     1555   1555  1.50  
LINK         ND2 ASN B1074                 C1  NAG B1316     1555   1555  1.51  
LINK         ND2 ASN B1098                 C1  NAG B1317     1555   1555  1.51  
LINK         ND2 ASN B1134                 C1  NAG B1319     1555   1555  1.50  
LINK         ND2 ASN C  61                 C1  NAG C1301     1555   1555  1.51  
LINK         ND2 ASN C 122                 C1  NAG C1302     1555   1555  1.51  
LINK         ND2 ASN C 165                 C1  NAG C1321     1555   1555  1.53  
LINK         ND2 ASN C 234                 C1  NAG C1303     1555   1555  1.51  
LINK         ND2 ASN C 282                 C1  NAG C1305     1555   1555  1.51  
LINK         ND2 ASN C 331                 C1  NAG C1306     1555   1555  1.52  
LINK         ND2 ASN C 343                 C1  NAG C1307     1555   1555  1.51  
LINK         ND2 ASN C 603                 C1  NAG C1308     1555   1555  1.50  
LINK         ND2 ASN C 616                 C1  NAG C1309     1555   1555  1.51  
LINK         ND2 ASN C 657                 C1  NAG C1310     1555   1555  1.51  
LINK         ND2 ASN C 709                 C1  NAG C1311     1555   1555  1.50  
LINK         ND2 ASN C 717                 C1  NAG C1312     1555   1555  1.50  
LINK         ND2 ASN C 801                 C1  NAG C1314     1555   1555  1.50  
LINK         ND2 ASN C1074                 C1  NAG C1316     1555   1555  1.51  
LINK         ND2 ASN C1098                 C1  NAG C1317     1555   1555  1.51  
LINK         ND2 ASN C1134                 C1  NAG C1319     1555   1555  1.50  
LINK         O4  NAG A1303                 C1  NAG A1304     1555   1555  1.51  
LINK         O4  NAG A1312                 C1  NAG A1313     1555   1555  1.50  
LINK         O4  NAG A1314                 C1  NAG A1315     1555   1555  1.51  
LINK         O4  NAG A1317                 C1  NAG A1318     1555   1555  1.50  
LINK         O4  NAG A1319                 C1  NAG A1320     1555   1555  1.52  
LINK         O4  NAG B1303                 C1  NAG B1304     1555   1555  1.51  
LINK         O4  NAG B1312                 C1  NAG B1313     1555   1555  1.50  
LINK         O4  NAG B1314                 C1  NAG B1315     1555   1555  1.51  
LINK         O4  NAG B1317                 C1  NAG B1318     1555   1555  1.50  
LINK         O4  NAG B1319                 C1  NAG B1320     1555   1555  1.52  
LINK         O4  NAG C1303                 C1  NAG C1304     1555   1555  1.51  
LINK         O4  NAG C1312                 C1  NAG C1313     1555   1555  1.50  
LINK         O4  NAG C1314                 C1  NAG C1315     1555   1555  1.50  
LINK         O4  NAG C1317                 C1  NAG C1318     1555   1555  1.50  
LINK         O4  NAG C1319                 C1  NAG C1320     1555   1555  1.52  
SITE     1 AC1  1 ASN A  61                                                     
SITE     1 AC2  3 ASN A 122  ASN A 125  LYS A 129                               
SITE     1 AC3  2 GLU A 132  ASN A 165                                          
SITE     1 AC4  2 ASN A 234  GLU C 465                                          
SITE     1 AC5  3 ASN A 280  GLU A 281  ASN A 282                               
SITE     1 AC6  3 ASN A 331  PRO A 579  GLN A 580                               
SITE     1 AC7  4 GLY A 339  ASN A 343  VAL A 367  LEU A 368                    
SITE     1 AC8  1 ASN A 603                                                     
SITE     1 AC9  2 ASN A 616  GLN A 644                                          
SITE     1 AD1  2 HIS A 655  ASN A 657                                          
SITE     1 AD2  2 ASN A 709  GLY A1131                                          
SITE     1 AD3  2 ASN A 717  LEU A 922                                          
SITE     1 AD4  3 ASN A 801  SER A 803  GLN A 804                               
SITE     1 AD5  2 GLU A1072  ASN A1074                                          
SITE     1 AD6  4 ASN A1098  THR A1100  HIS A1101  PHE A1103                    
SITE     1 AD7  1 ASN A1134                                                     
SITE     1 AD8  1 ASN B  61                                                     
SITE     1 AD9  3 ASN B 122  ASN B 125  LYS B 129                               
SITE     1 AE1  2 GLU B 132  ASN B 165                                          
SITE     1 AE2  2 GLU A 465  ASN B 234                                          
SITE     1 AE3  3 ASN B 280  GLU B 281  ASN B 282                               
SITE     1 AE4  3 ASN B 331  PRO B 579  GLN B 580                               
SITE     1 AE5  4 GLY B 339  ASN B 343  VAL B 367  LEU B 368                    
SITE     1 AE6  1 ASN B 603                                                     
SITE     1 AE7  2 ASN B 616  GLN B 644                                          
SITE     1 AE8  2 HIS B 655  ASN B 657                                          
SITE     1 AE9  2 ASN B 709  GLY B1131                                          
SITE     1 AF1  2 ASN B 717  LEU B 922                                          
SITE     1 AF2  3 ASN B 801  SER B 803  GLN B 804                               
SITE     1 AF3  2 GLU B1072  ASN B1074                                          
SITE     1 AF4  4 ASN B1098  THR B1100  HIS B1101  PHE B1103                    
SITE     1 AF5  1 ASN B1134                                                     
SITE     1 AF6  1 ASN C  61                                                     
SITE     1 AF7  3 ASN C 122  ASN C 125  LYS C 129                               
SITE     1 AF8  2 GLU C 132  ASN C 165                                          
SITE     1 AF9  2 GLU B 465  ASN C 234                                          
SITE     1 AG1  3 ASN C 280  GLU C 281  ASN C 282                               
SITE     1 AG2  3 ASN C 331  PRO C 579  GLN C 580                               
SITE     1 AG3  4 GLY C 339  ASN C 343  VAL C 367  LEU C 368                    
SITE     1 AG4  1 ASN C 603                                                     
SITE     1 AG5  2 ASN C 616  GLN C 644                                          
SITE     1 AG6  2 HIS C 655  ASN C 657                                          
SITE     1 AG7  2 ASN C 709  GLY C1131                                          
SITE     1 AG8  2 ASN C 717  LEU C 922                                          
SITE     1 AG9  3 ASN C 801  SER C 803  GLN C 804                               
SITE     1 AH1  2 GLU C1072  ASN C1074                                          
SITE     1 AH2  4 ASN C1098  THR C1100  HIS C1101  PHE C1103                    
SITE     1 AH3  1 ASN C1134                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   ALA A  27     100.574  92.381   2.601  1.00 34.23           N  
ATOM      2  CA  ALA A  27     100.652  92.036   4.012  1.00 34.95           C  
ATOM      3  C   ALA A  27     100.201  90.593   4.228  1.00 34.25           C  
ATOM      4  O   ALA A  27      99.325  90.101   3.510  1.00 34.30           O  
ATOM      5  CB  ALA A  27      99.788  92.989   4.854  1.00 35.54           C  
ATOM      6  N   TYR A  28     100.816  89.921   5.213  1.00 34.21           N  
ATOM      7  CA  TYR A  28     100.511  88.544   5.610  1.00 34.20           C  
ATOM      8  C   TYR A  28     100.414  88.427   7.110  1.00 34.22           C  
ATOM      9  O   TYR A  28     101.071  89.171   7.838  1.00 34.22           O  
ATOM     10  CB  TYR A  28     101.581  87.579   5.111  1.00 33.92           C  
ATOM     11  CG  TYR A  28     101.633  87.445   3.639  1.00 33.85           C  
ATOM     12  CD1 TYR A  28     102.304  88.369   2.881  1.00 33.70           C  
ATOM     13  CD2 TYR A  28     101.011  86.379   3.044  1.00 33.75           C  
ATOM     14  CE1 TYR A  28     102.349  88.229   1.520  1.00 34.52           C  
ATOM     15  CE2 TYR A  28     101.056  86.231   1.688  1.00 33.56           C  
ATOM     16  CZ  TYR A  28     101.721  87.154   0.923  1.00 34.54           C  
ATOM     17  OH  TYR A  28     101.770  87.011  -0.443  1.00 33.14           O  
ATOM     18  N   THR A  29      99.633  87.464   7.573  1.00 34.15           N  
ATOM     19  CA  THR A  29      99.617  87.155   8.992  1.00 34.30           C  
ATOM     20  C   THR A  29      99.691  85.659   9.260  1.00 34.04           C  
ATOM     21  O   THR A  29      99.667  84.833   8.343  1.00 33.65           O  
ATOM     22  CB  THR A  29      98.398  87.736   9.713  1.00 34.33           C  
ATOM     23  OG1 THR A  29      98.587  87.585  11.122  1.00 34.97           O  
ATOM     24  CG2 THR A  29      97.155  87.020   9.304  1.00 34.02           C  
ATOM     25  N   ASN A  30      99.773  85.344  10.544  1.00 34.14           N  
ATOM     26  CA  ASN A  30      99.875  83.999  11.081  1.00 33.68           C  
ATOM     27  C   ASN A  30      98.491  83.417  11.347  1.00 33.32           C  
ATOM     28  O   ASN A  30      97.721  83.965  12.132  1.00 33.47           O  
ATOM     29  CB  ASN A  30     100.712  84.042  12.348  1.00 33.83           C  
ATOM     30  CG  ASN A  30     101.100  82.708  12.902  1.00 33.28           C  
ATOM     31  OD1 ASN A  30     100.438  81.684  12.713  1.00 33.56           O  
ATOM     32  ND2 ASN A  30     102.205  82.703  13.606  1.00 33.97           N  
ATOM     33  N   SER A  31      98.155  82.333  10.657  1.00 32.76           N  
ATOM     34  CA  SER A  31      96.853  81.693  10.809  1.00 32.51           C  
ATOM     35  C   SER A  31      96.699  80.977  12.142  1.00 32.15           C  
ATOM     36  O   SER A  31      95.590  80.612  12.535  1.00 31.64           O  
ATOM     37  CB  SER A  31      96.649  80.677   9.724  1.00 31.96           C  
ATOM     38  OG  SER A  31      97.554  79.636   9.870  1.00 31.98           O  
ATOM     39  N   PHE A  32      97.808  80.760  12.824  1.00 32.37           N  
ATOM     40  CA  PHE A  32      97.828  80.042  14.083  1.00 32.18           C  
ATOM     41  C   PHE A  32      97.119  78.703  13.977  1.00 32.00           C  
ATOM     42  O   PHE A  32      97.533  77.829  13.219  1.00 31.42           O  
ATOM     43  CB  PHE A  32      97.193  80.880  15.185  1.00 32.70           C  
ATOM     44  CG  PHE A  32      97.940  82.111  15.483  1.00 33.43           C  
ATOM     45  CD1 PHE A  32      97.470  83.328  15.059  1.00 33.52           C  
ATOM     46  CD2 PHE A  32      99.118  82.065  16.183  1.00 33.68           C  
ATOM     47  CE1 PHE A  32      98.159  84.479  15.332  1.00 33.91           C  
ATOM     48  CE2 PHE A  32      99.815  83.210  16.462  1.00 33.97           C  
ATOM     49  CZ  PHE A  32      99.334  84.422  16.036  1.00 34.24           C  
ATOM     50  N   THR A  33      96.045  78.541  14.739  1.00 32.19           N  
ATOM     51  CA  THR A  33      95.319  77.284  14.785  1.00 31.98           C  
ATOM     52  C   THR A  33      93.903  77.414  14.232  1.00 31.61           C  
ATOM     53  O   THR A  33      93.030  76.598  14.527  1.00 31.80           O  
ATOM     54  CB  THR A  33      95.283  76.759  16.222  1.00 32.58           C  
ATOM     55  OG1 THR A  33      94.669  77.734  17.067  1.00 33.21           O  
ATOM     56  CG2 THR A  33      96.700  76.509  16.707  1.00 32.99           C  
ATOM     57  N   ARG A  34      93.671  78.459  13.450  1.00 31.44           N  
ATOM     58  CA  ARG A  34      92.371  78.713  12.846  1.00 31.13           C  
ATOM     59  C   ARG A  34      92.183  77.845  11.606  1.00 30.99           C  
ATOM     60  O   ARG A  34      93.153  77.353  11.037  1.00 30.87           O  
ATOM     61  CB  ARG A  34      92.236  80.182  12.459  1.00 31.38           C  
ATOM     62  CG  ARG A  34      92.420  81.192  13.605  1.00 32.03           C  
ATOM     63  CD  ARG A  34      91.350  81.088  14.622  1.00 32.45           C  
ATOM     64  NE  ARG A  34      91.435  82.136  15.630  1.00 33.96           N  
ATOM     65  CZ  ARG A  34      90.564  82.297  16.639  1.00 34.42           C  
ATOM     66  NH1 ARG A  34      89.533  81.495  16.783  1.00 34.33           N  
ATOM     67  NH2 ARG A  34      90.764  83.270  17.481  1.00 34.87           N  
ATOM     68  N   GLY A  35      90.934  77.667  11.173  1.00 30.93           N  
ATOM     69  CA  GLY A  35      90.672  76.927   9.938  1.00 31.55           C  
ATOM     70  C   GLY A  35      90.296  75.461  10.128  1.00 31.62           C  
ATOM     71  O   GLY A  35      90.466  74.641   9.217  1.00 31.61           O  
ATOM     72  N   VAL A  36      89.805  75.127  11.316  1.00 31.57           N  
ATOM     73  CA  VAL A  36      89.329  73.783  11.605  1.00 32.09           C  
ATOM     74  C   VAL A  36      87.812  73.771  11.679  1.00 32.43           C  
ATOM     75  O   VAL A  36      87.203  74.579  12.373  1.00 32.47           O  
ATOM     76  CB  VAL A  36      89.942  73.238  12.901  1.00 31.87           C  
ATOM     77  CG1 VAL A  36      89.355  71.870  13.240  1.00 31.97           C  
ATOM     78  CG2 VAL A  36      91.439  73.117  12.703  1.00 31.36           C  
ATOM     79  N   TYR A  37      87.217  72.855  10.948  1.00 32.39           N  
ATOM     80  CA  TYR A  37      85.778  72.715  10.857  1.00 32.43           C  
ATOM     81  C   TYR A  37      85.377  71.271  11.074  1.00 32.76           C  
ATOM     82  O   TYR A  37      86.201  70.366  10.956  1.00 32.64           O  
ATOM     83  CB  TYR A  37      85.304  73.212   9.505  1.00 33.27           C  
ATOM     84  CG  TYR A  37      85.893  72.458   8.408  1.00 33.05           C  
ATOM     85  CD1 TYR A  37      85.292  71.328   7.952  1.00 33.54           C  
ATOM     86  CD2 TYR A  37      87.050  72.895   7.851  1.00 32.89           C  
ATOM     87  CE1 TYR A  37      85.849  70.629   6.936  1.00 33.32           C  
ATOM     88  CE2 TYR A  37      87.608  72.205   6.836  1.00 32.59           C  
ATOM     89  CZ  TYR A  37      87.009  71.073   6.378  1.00 32.79           C  
ATOM     90  OH  TYR A  37      87.563  70.383   5.360  1.00 32.55           O  
ATOM     91  N   TYR A  38      84.113  71.053  11.397  1.00 32.70           N  
ATOM     92  CA  TYR A  38      83.610  69.704  11.593  1.00 32.38           C  
ATOM     93  C   TYR A  38      83.548  69.003  10.237  1.00 32.56           C  
ATOM     94  O   TYR A  38      82.784  69.430   9.379  1.00 33.11           O  
ATOM     95  CB  TYR A  38      82.214  69.750  12.205  1.00 32.48           C  
ATOM     96  CG  TYR A  38      82.168  70.258  13.613  1.00 32.30           C  
ATOM     97  CD1 TYR A  38      82.203  71.602  13.842  1.00 32.70           C  
ATOM     98  CD2 TYR A  38      82.055  69.388  14.665  1.00 32.77           C  
ATOM     99  CE1 TYR A  38      82.136  72.094  15.106  1.00 32.60           C  
ATOM    100  CE2 TYR A  38      81.983  69.880  15.948  1.00 32.45           C  
ATOM    101  CZ  TYR A  38      82.026  71.231  16.162  1.00 31.85           C  
ATOM    102  OH  TYR A  38      81.948  71.729  17.429  1.00 31.86           O  
ATOM    103  N   PRO A  39      84.315  67.924  10.019  1.00 32.78           N  
ATOM    104  CA  PRO A  39      84.474  67.242   8.745  1.00 32.71           C  
ATOM    105  C   PRO A  39      83.206  66.559   8.240  1.00 32.77           C  
ATOM    106  O   PRO A  39      83.052  66.344   7.038  1.00 33.09           O  
ATOM    107  CB  PRO A  39      85.558  66.207   9.063  1.00 32.57           C  
ATOM    108  CG  PRO A  39      85.450  65.982  10.554  1.00 32.70           C  
ATOM    109  CD  PRO A  39      85.044  67.314  11.129  1.00 32.64           C  
ATOM    110  N   ASP A  40      82.290  66.230   9.144  1.00 32.90           N  
ATOM    111  CA  ASP A  40      81.051  65.575   8.753  1.00 33.24           C  
ATOM    112  C   ASP A  40      79.917  65.947   9.699  1.00 33.47           C  
ATOM    113  O   ASP A  40      80.023  66.906  10.465  1.00 33.53           O  
ATOM    114  CB  ASP A  40      81.234  64.059   8.654  1.00 33.09           C  
ATOM    115  CG  ASP A  40      81.605  63.386   9.951  1.00 33.02           C  
ATOM    116  OD1 ASP A  40      81.365  63.941  11.005  1.00 32.75           O  
ATOM    117  OD2 ASP A  40      82.133  62.295   9.884  1.00 32.98           O  
ATOM    118  N   LYS A  41      78.812  65.217   9.607  1.00 33.92           N  
ATOM    119  CA  LYS A  41      77.618  65.526  10.376  1.00 32.58           C  
ATOM    120  C   LYS A  41      77.338  64.473  11.441  1.00 35.09           C  
ATOM    121  O   LYS A  41      76.185  64.239  11.824  1.00 35.35           O  
ATOM    122  CB  LYS A  41      76.436  65.692   9.431  1.00 35.11           C  
ATOM    123  CG  LYS A  41      76.613  66.850   8.447  1.00 35.13           C  
ATOM    124  CD  LYS A  41      75.386  67.052   7.601  1.00 36.97           C  
ATOM    125  CE  LYS A  41      75.460  68.337   6.792  1.00 37.65           C  
ATOM    126  NZ  LYS A  41      76.460  68.252   5.692  1.00 35.69           N  
ATOM    127  N   VAL A  42      78.398  63.810  11.895  1.00 36.58           N  
ATOM    128  CA  VAL A  42      78.281  62.797  12.929  1.00 34.51           C  
ATOM    129  C   VAL A  42      78.660  63.318  14.299  1.00 37.69           C  
ATOM    130  O   VAL A  42      79.709  63.933  14.483  1.00 37.37           O  
ATOM    131  CB  VAL A  42      79.150  61.583  12.586  1.00 31.64           C  
ATOM    132  CG1 VAL A  42      79.145  60.589  13.726  1.00 29.68           C  
ATOM    133  CG2 VAL A  42      78.610  60.935  11.344  1.00 32.20           C  
ATOM    134  N   PHE A  43      77.809  63.057  15.272  1.00 36.23           N  
ATOM    135  CA  PHE A  43      78.101  63.454  16.629  1.00 43.61           C  
ATOM    136  C   PHE A  43      79.115  62.518  17.248  1.00 35.21           C  
ATOM    137  O   PHE A  43      78.968  61.292  17.215  1.00 26.72           O  
ATOM    138  CB  PHE A  43      76.843  63.475  17.479  1.00 34.17           C  
ATOM    139  CG  PHE A  43      77.093  63.829  18.905  1.00 44.50           C  
ATOM    140  CD1 PHE A  43      77.227  65.132  19.303  1.00 35.39           C  
ATOM    141  CD2 PHE A  43      77.196  62.843  19.855  1.00 31.83           C  
ATOM    142  CE1 PHE A  43      77.450  65.446  20.619  1.00 31.74           C  
ATOM    143  CE2 PHE A  43      77.424  63.153  21.170  1.00 33.35           C  
ATOM    144  CZ  PHE A  43      77.548  64.458  21.551  1.00 32.43           C  
ATOM    145  N   ARG A  44      80.144  63.105  17.820  1.00 31.87           N  
ATOM    146  CA  ARG A  44      81.185  62.373  18.511  1.00 30.89           C  
ATOM    147  C   ARG A  44      81.462  63.100  19.792  1.00 31.86           C  
ATOM    148  O   ARG A  44      81.303  64.311  19.837  1.00 32.06           O  
ATOM    149  CB  ARG A  44      82.456  62.307  17.693  1.00 32.07           C  
ATOM    150  CG  ARG A  44      82.356  61.566  16.398  1.00 31.69           C  
ATOM    151  CD  ARG A  44      83.663  61.541  15.704  1.00 31.24           C  
ATOM    152  NE  ARG A  44      83.598  60.833  14.447  1.00 30.94           N  
ATOM    153  CZ  ARG A  44      83.139  61.379  13.306  1.00 31.67           C  
ATOM    154  NH1 ARG A  44      82.702  62.621  13.309  1.00 32.15           N  
ATOM    155  NH2 ARG A  44      83.116  60.681  12.187  1.00 31.63           N  
ATOM    156  N   SER A  45      81.889  62.390  20.819  1.00 32.34           N  
ATOM    157  CA  SER A  45      82.245  63.044  22.067  1.00 31.21           C  
ATOM    158  C   SER A  45      83.322  62.274  22.797  1.00 30.49           C  
ATOM    159  O   SER A  45      83.434  61.057  22.647  1.00 29.98           O  
ATOM    160  CB  SER A  45      81.021  63.183  22.942  1.00 31.94           C  
ATOM    161  OG  SER A  45      80.509  61.922  23.297  1.00 32.68           O  
ATOM    162  N   SER A  46      84.096  62.986  23.607  1.00 30.42           N  
ATOM    163  CA  SER A  46      85.141  62.381  24.431  1.00 30.06           C  
ATOM    164  C   SER A  46      86.024  61.450  23.608  1.00 29.51           C  
ATOM    165  O   SER A  46      86.241  60.296  23.978  1.00 29.36           O  
ATOM    166  CB  SER A  46      84.520  61.610  25.576  1.00 30.14           C  
ATOM    167  OG  SER A  46      83.747  62.452  26.385  1.00 30.68           O  
ATOM    168  N   VAL A  47      86.493  61.935  22.469  1.00 29.46           N  
ATOM    169  CA  VAL A  47      87.268  61.097  21.566  1.00 29.02           C  
ATOM    170  C   VAL A  47      88.251  61.888  20.725  1.00 28.69           C  
ATOM    171  O   VAL A  47      87.981  63.024  20.338  1.00 29.28           O  
ATOM    172  CB  VAL A  47      86.305  60.304  20.654  1.00 28.69           C  
ATOM    173  CG1 VAL A  47      85.519  61.248  19.783  1.00 29.76           C  
ATOM    174  CG2 VAL A  47      87.068  59.311  19.782  1.00 28.44           C  
ATOM    175  N   LEU A  48      89.378  61.267  20.403  1.00 28.46           N  
ATOM    176  CA  LEU A  48      90.321  61.861  19.474  1.00 28.60           C  
ATOM    177  C   LEU A  48      90.154  61.176  18.127  1.00 28.44           C  
ATOM    178  O   LEU A  48      90.396  59.976  18.000  1.00 28.45           O  
ATOM    179  CB  LEU A  48      91.748  61.698  19.983  1.00 28.37           C  
ATOM    180  CG  LEU A  48      92.005  62.159  21.417  1.00 28.45           C  
ATOM    181  CD1 LEU A  48      93.443  61.958  21.724  1.00 27.55           C  
ATOM    182  CD2 LEU A  48      91.614  63.596  21.584  1.00 28.77           C  
ATOM    183  N   HIS A  49      89.701  61.924  17.136  1.00 28.56           N  
ATOM    184  CA  HIS A  49      89.383  61.350  15.832  1.00 28.64           C  
ATOM    185  C   HIS A  49      90.322  61.821  14.736  1.00 28.69           C  
ATOM    186  O   HIS A  49      90.541  63.017  14.564  1.00 29.15           O  
ATOM    187  CB  HIS A  49      87.947  61.690  15.449  1.00 28.70           C  
ATOM    188  CG  HIS A  49      87.549  61.175  14.123  1.00 29.04           C  
ATOM    189  ND1 HIS A  49      87.382  59.836  13.868  1.00 28.97           N  
ATOM    190  CD2 HIS A  49      87.278  61.817  12.969  1.00 29.37           C  
ATOM    191  CE1 HIS A  49      87.029  59.676  12.606  1.00 29.40           C  
ATOM    192  NE2 HIS A  49      86.956  60.862  12.041  1.00 29.51           N  
ATOM    193  N   SER A  50      90.888  60.874  14.001  1.00 28.77           N  
ATOM    194  CA  SER A  50      91.808  61.192  12.915  1.00 29.00           C  
ATOM    195  C   SER A  50      91.098  61.235  11.576  1.00 29.11           C  
ATOM    196  O   SER A  50      90.480  60.255  11.160  1.00 28.90           O  
ATOM    197  CB  SER A  50      92.925  60.180  12.855  1.00 28.74           C  
ATOM    198  OG  SER A  50      93.732  60.401  11.733  1.00 29.44           O  
ATOM    199  N   THR A  51      91.192  62.370  10.899  1.00 29.20           N  
ATOM    200  CA  THR A  51      90.521  62.548   9.618  1.00 29.50           C  
ATOM    201  C   THR A  51      91.364  63.306   8.603  1.00 29.90           C  
ATOM    202  O   THR A  51      92.139  64.194   8.958  1.00 30.22           O  
ATOM    203  CB  THR A  51      89.199  63.299   9.820  1.00 29.83           C  
ATOM    204  OG1 THR A  51      88.517  63.405   8.571  1.00 30.55           O  
ATOM    205  CG2 THR A  51      89.467  64.693  10.378  1.00 29.90           C  
ATOM    206  N   GLN A  52      91.184  62.983   7.327  1.00 30.09           N  
ATOM    207  CA  GLN A  52      91.871  63.713   6.270  1.00 30.20           C  
ATOM    208  C   GLN A  52      90.882  64.501   5.442  1.00 30.78           C  
ATOM    209  O   GLN A  52      89.930  63.941   4.899  1.00 30.84           O  
ATOM    210  CB  GLN A  52      92.666  62.781   5.365  1.00 30.31           C  
ATOM    211  CG  GLN A  52      93.435  63.522   4.281  1.00 30.38           C  
ATOM    212  CD  GLN A  52      94.271  62.613   3.431  1.00 31.04           C  
ATOM    213  OE1 GLN A  52      93.991  61.414   3.326  1.00 30.53           O  
ATOM    214  NE2 GLN A  52      95.312  63.164   2.809  1.00 31.30           N  
ATOM    215  N   ASP A  53      91.100  65.802   5.369  1.00 30.82           N  
ATOM    216  CA  ASP A  53      90.204  66.689   4.641  1.00 31.42           C  
ATOM    217  C   ASP A  53      90.945  67.960   4.294  1.00 31.66           C  
ATOM    218  O   ASP A  53      92.102  68.121   4.666  1.00 31.51           O  
ATOM    219  CB  ASP A  53      88.945  66.993   5.475  1.00 31.77           C  
ATOM    220  CG  ASP A  53      87.672  67.313   4.657  1.00 32.24           C  
ATOM    221  OD1 ASP A  53      87.780  67.850   3.562  1.00 32.35           O  
ATOM    222  OD2 ASP A  53      86.607  67.029   5.143  1.00 32.58           O  
ATOM    223  N   LEU A  54      90.281  68.878   3.622  1.00 31.95           N  
ATOM    224  CA  LEU A  54      90.918  70.126   3.254  1.00 32.04           C  
ATOM    225  C   LEU A  54      90.808  71.141   4.378  1.00 32.40           C  
ATOM    226  O   LEU A  54      89.776  71.781   4.556  1.00 32.75           O  
ATOM    227  CB  LEU A  54      90.266  70.679   1.989  1.00 32.80           C  
ATOM    228  CG  LEU A  54      90.288  69.771   0.756  1.00 32.17           C  
ATOM    229  CD1 LEU A  54      89.503  70.446  -0.345  1.00 33.19           C  
ATOM    230  CD2 LEU A  54      91.725  69.525   0.319  1.00 32.05           C  
ATOM    231  N   PHE A  55      91.887  71.282   5.134  1.00 32.39           N  
ATOM    232  CA  PHE A  55      91.943  72.146   6.309  1.00 32.13           C  
ATOM    233  C   PHE A  55      92.988  73.211   6.099  1.00 32.45           C  
ATOM    234  O   PHE A  55      93.889  73.033   5.283  1.00 32.64           O  
ATOM    235  CB  PHE A  55      92.328  71.379   7.563  1.00 31.30           C  
ATOM    236  CG  PHE A  55      91.360  70.366   8.085  1.00 31.31           C  
ATOM    237  CD1 PHE A  55      91.479  69.034   7.750  1.00 30.89           C  
ATOM    238  CD2 PHE A  55      90.351  70.744   8.943  1.00 31.57           C  
ATOM    239  CE1 PHE A  55      90.613  68.104   8.260  1.00 30.77           C  
ATOM    240  CE2 PHE A  55      89.475  69.814   9.455  1.00 31.47           C  
ATOM    241  CZ  PHE A  55      89.609  68.492   9.111  1.00 31.01           C  
ATOM    242  N   LEU A  56      92.886  74.319   6.820  1.00 32.47           N  
ATOM    243  CA  LEU A  56      93.938  75.318   6.722  1.00 32.24           C  
ATOM    244  C   LEU A  56      95.127  74.829   7.552  1.00 31.94           C  
ATOM    245  O   LEU A  56      94.966  74.612   8.751  1.00 31.72           O  
ATOM    246  CB  LEU A  56      93.452  76.645   7.293  1.00 32.47           C  
ATOM    247  CG  LEU A  56      94.372  77.853   7.164  1.00 32.38           C  
ATOM    248  CD1 LEU A  56      94.507  78.244   5.717  1.00 32.77           C  
ATOM    249  CD2 LEU A  56      93.792  78.987   7.966  1.00 32.16           C  
ATOM    250  N   PRO A  57      96.321  74.622   6.976  1.00 31.73           N  
ATOM    251  CA  PRO A  57      97.490  74.142   7.680  1.00 31.34           C  
ATOM    252  C   PRO A  57      97.816  75.068   8.833  1.00 31.22           C  
ATOM    253  O   PRO A  57      97.722  76.292   8.701  1.00 31.55           O  
ATOM    254  CB  PRO A  57      98.571  74.183   6.606  1.00 31.68           C  
ATOM    255  CG  PRO A  57      97.825  74.059   5.316  1.00 31.38           C  
ATOM    256  CD  PRO A  57      96.534  74.822   5.539  1.00 32.07           C  
ATOM    257  N   PHE A  58      98.216  74.492   9.953  1.00 30.80           N  
ATOM    258  CA  PHE A  58      98.522  75.303  11.116  1.00 30.74           C  
ATOM    259  C   PHE A  58      99.752  76.153  10.910  1.00 31.17           C  
ATOM    260  O   PHE A  58     100.722  75.744  10.272  1.00 30.54           O  
ATOM    261  CB  PHE A  58      98.667  74.442  12.366  1.00 30.68           C  
ATOM    262  CG  PHE A  58      97.372  74.084  13.058  1.00 30.96           C  
ATOM    263  CD1 PHE A  58      96.128  74.336  12.487  1.00 31.53           C  
ATOM    264  CD2 PHE A  58      97.400  73.523  14.317  1.00 31.38           C  
ATOM    265  CE1 PHE A  58      94.978  74.045  13.164  1.00 31.67           C  
ATOM    266  CE2 PHE A  58      96.235  73.226  14.987  1.00 30.95           C  
ATOM    267  CZ  PHE A  58      95.030  73.493  14.410  1.00 31.63           C  
ATOM    268  N   PHE A  59      99.657  77.372  11.421  1.00 31.64           N  
ATOM    269  CA  PHE A  59     100.687  78.393  11.377  1.00 31.56           C  
ATOM    270  C   PHE A  59     101.095  78.791   9.968  1.00 31.75           C  
ATOM    271  O   PHE A  59     102.146  79.400   9.778  1.00 31.96           O  
ATOM    272  CB  PHE A  59     101.894  77.948  12.192  1.00 31.54           C  
ATOM    273  CG  PHE A  59     101.554  77.768  13.633  1.00 31.62           C  
ATOM    274  CD1 PHE A  59     101.284  76.529  14.140  1.00 31.20           C  
ATOM    275  CD2 PHE A  59     101.496  78.851  14.477  1.00 32.34           C  
ATOM    276  CE1 PHE A  59     100.953  76.363  15.460  1.00 31.30           C  
ATOM    277  CE2 PHE A  59     101.172  78.694  15.800  1.00 32.39           C  
ATOM    278  CZ  PHE A  59     100.897  77.447  16.292  1.00 33.09           C  
ATOM    279  N   SER A  60     100.241  78.507   8.986  1.00 31.74           N  
ATOM    280  CA  SER A  60     100.494  78.934   7.619  1.00 31.90           C  
ATOM    281  C   SER A  60     100.236  80.429   7.447  1.00 32.68           C  
ATOM    282  O   SER A  60      99.640  81.072   8.325  1.00 32.50           O  
ATOM    283  CB  SER A  60      99.643  78.139   6.646  1.00 31.94           C  
ATOM    284  OG  SER A  60      98.281  78.424   6.806  1.00 31.76           O  
ATOM    285  N   ASN A  61     100.707  80.981   6.317  1.00 32.97           N  
ATOM    286  CA  ASN A  61     100.543  82.372   5.919  1.00 33.05           C  
ATOM    287  C   ASN A  61      99.210  82.592   5.210  1.00 32.90           C  
ATOM    288  O   ASN A  61      98.899  81.872   4.234  1.00 32.82           O  
ATOM    289  CB  ASN A  61     101.699  82.841   5.041  1.00 33.67           C  
ATOM    290  CG  ASN A  61     102.990  83.174   5.800  1.00 33.75           C  
ATOM    291  OD1 ASN A  61     102.994  83.319   7.035  1.00 33.88           O  
ATOM    292  ND2 ASN A  61     104.081  83.301   5.061  1.00 34.08           N  
ATOM    293  N   VAL A  62      98.438  83.585   5.652  1.00 33.09           N  
ATOM    294  CA  VAL A  62      97.185  83.991   5.020  1.00 33.11           C  
ATOM    295  C   VAL A  62      97.330  85.441   4.617  1.00 33.38           C  
ATOM    296  O   VAL A  62      97.895  86.247   5.361  1.00 33.97           O  
ATOM    297  CB  VAL A  62      95.982  83.770   5.952  1.00 32.96           C  
ATOM    298  CG1 VAL A  62      95.898  82.308   6.298  1.00 32.42           C  
ATOM    299  CG2 VAL A  62      96.110  84.600   7.194  1.00 33.19           C  
ATOM    300  N   THR A  63      96.864  85.772   3.427  1.00 33.62           N  
ATOM    301  CA  THR A  63      97.045  87.117   2.928  1.00 34.10           C  
ATOM    302  C   THR A  63      96.113  88.064   3.648  1.00 34.23           C  
ATOM    303  O   THR A  63      94.933  87.777   3.812  1.00 35.65           O  
ATOM    304  CB  THR A  63      96.822  87.177   1.418  1.00 34.80           C  
ATOM    305  OG1 THR A  63      97.690  86.241   0.774  1.00 34.12           O  
ATOM    306  CG2 THR A  63      97.153  88.563   0.906  1.00 35.26           C  
ATOM    307  N   TRP A  64      96.658  89.174   4.107  1.00 34.45           N  
ATOM    308  CA  TRP A  64      95.928  90.163   4.885  1.00 35.09           C  
ATOM    309  C   TRP A  64      95.556  91.395   4.060  1.00 35.66           C  
ATOM    310  O   TRP A  64      96.427  92.110   3.568  1.00 35.54           O  
ATOM    311  CB  TRP A  64      96.784  90.534   6.085  1.00 34.89           C  
ATOM    312  CG  TRP A  64      96.233  91.538   6.999  1.00 35.19           C  
ATOM    313  CD1 TRP A  64      94.984  92.044   7.059  1.00 35.46           C  
ATOM    314  CD2 TRP A  64      96.958  92.157   8.055  1.00 35.22           C  
ATOM    315  NE1 TRP A  64      94.897  92.941   8.071  1.00 35.19           N  
ATOM    316  CE2 TRP A  64      96.087  93.019   8.693  1.00 35.41           C  
ATOM    317  CE3 TRP A  64      98.269  92.044   8.513  1.00 35.13           C  
ATOM    318  CZ2 TRP A  64      96.468  93.775   9.762  1.00 35.75           C  
ATOM    319  CZ3 TRP A  64      98.657  92.806   9.596  1.00 35.03           C  
ATOM    320  CH2 TRP A  64      97.777  93.651  10.206  1.00 34.96           C  
ATOM    321  N   PHE A  65      94.253  91.626   3.903  1.00 36.03           N  
ATOM    322  CA  PHE A  65      93.722  92.727   3.105  1.00 35.86           C  
ATOM    323  C   PHE A  65      93.126  93.787   4.017  1.00 36.58           C  
ATOM    324  O   PHE A  65      92.683  93.471   5.119  1.00 36.49           O  
ATOM    325  CB  PHE A  65      92.665  92.202   2.173  1.00 36.41           C  
ATOM    326  CG  PHE A  65      93.178  91.171   1.275  1.00 36.17           C  
ATOM    327  CD1 PHE A  65      93.152  89.862   1.672  1.00 36.26           C  
ATOM    328  CD2 PHE A  65      93.680  91.476   0.039  1.00 37.08           C  
ATOM    329  CE1 PHE A  65      93.612  88.878   0.862  1.00 36.44           C  
ATOM    330  CE2 PHE A  65      94.146  90.483  -0.783  1.00 37.23           C  
ATOM    331  CZ  PHE A  65      94.108  89.179  -0.365  1.00 36.85           C  
ATOM    332  N   HIS A  66      93.098  95.041   3.564  1.00 36.40           N  
ATOM    333  CA  HIS A  66      92.614  96.145   4.411  1.00 36.61           C  
ATOM    334  C   HIS A  66      91.442  96.925   3.818  1.00 36.89           C  
ATOM    335  O   HIS A  66      91.287  97.013   2.610  1.00 37.18           O  
ATOM    336  CB  HIS A  66      93.747  97.130   4.677  1.00 36.60           C  
ATOM    337  CG  HIS A  66      94.875  96.563   5.436  1.00 36.11           C  
ATOM    338  ND1 HIS A  66      95.018  96.739   6.789  1.00 35.86           N  
ATOM    339  CD2 HIS A  66      95.929  95.818   5.038  1.00 35.80           C  
ATOM    340  CE1 HIS A  66      96.117  96.132   7.191  1.00 35.77           C  
ATOM    341  NE2 HIS A  66      96.687  95.566   6.146  1.00 35.53           N  
ATOM    342  N   ALA A  67      90.638  97.548   4.671  1.00 37.24           N  
ATOM    343  CA  ALA A  67      89.521  98.352   4.186  1.00 37.88           C  
ATOM    344  C   ALA A  67      89.480  99.709   4.877  1.00 37.87           C  
ATOM    345  O   ALA A  67      88.491 100.064   5.518  1.00 38.34           O  
ATOM    346  CB  ALA A  67      88.212  97.617   4.398  1.00 37.67           C  
ATOM    347  N   ILE A  68      90.573 100.456   4.748  1.00 38.37           N  
ATOM    348  CA  ILE A  68      90.709 101.770   5.361  1.00 39.44           C  
ATOM    349  C   ILE A  68      91.162 102.806   4.323  1.00 39.43           C  
ATOM    350  O   ILE A  68      91.728 102.438   3.292  1.00 39.25           O  
ATOM    351  CB  ILE A  68      91.707 101.699   6.536  1.00 39.65           C  
ATOM    352  CG1 ILE A  68      93.112 101.296   6.014  1.00 39.41           C  
ATOM    353  CG2 ILE A  68      91.196 100.697   7.573  1.00 40.52           C  
ATOM    354  CD1 ILE A  68      94.216 101.370   7.049  1.00 39.84           C  
ATOM    355  N   HIS A  69      90.934 104.105   4.613  1.00 39.49           N  
ATOM    356  CA  HIS A  69      91.356 105.253   3.785  1.00 39.50           C  
ATOM    357  C   HIS A  69      90.998 105.077   2.305  1.00 40.16           C  
ATOM    358  O   HIS A  69      90.896 106.055   1.559  1.00 39.45           O  
ATOM    359  CB  HIS A  69      92.879 105.521   3.924  1.00 39.56           C  
ATOM    360  CG  HIS A  69      93.325 105.964   5.312  1.00 39.34           C  
ATOM    361  ND1 HIS A  69      92.967 107.181   5.851  1.00 38.74           N  
ATOM    362  CD2 HIS A  69      94.103 105.354   6.240  1.00 39.51           C  
ATOM    363  CE1 HIS A  69      93.503 107.299   7.056  1.00 38.23           C  
ATOM    364  NE2 HIS A  69      94.198 106.203   7.314  1.00 39.16           N  
ATOM    365  N   ASP A  80      90.014  97.433  -1.010  1.00 36.80           N  
ATOM    366  CA  ASP A  80      90.944  96.333  -1.239  1.00 37.71           C  
ATOM    367  C   ASP A  80      90.125  95.048  -1.442  1.00 37.57           C  
ATOM    368  O   ASP A  80      89.990  94.219  -0.536  1.00 37.53           O  
ATOM    369  CB  ASP A  80      91.940  96.196  -0.057  1.00 37.77           C  
ATOM    370  CG  ASP A  80      93.193  95.307  -0.293  1.00 37.34           C  
ATOM    371  OD1 ASP A  80      93.460  94.924  -1.410  1.00 38.12           O  
ATOM    372  OD2 ASP A  80      93.866  95.042   0.686  1.00 36.99           O  
ATOM    373  N   ASN A  81      89.559  94.909  -2.643  1.00 37.96           N  
ATOM    374  CA  ASN A  81      88.712  93.793  -3.060  1.00 38.19           C  
ATOM    375  C   ASN A  81      89.166  93.180  -4.386  1.00 38.40           C  
ATOM    376  O   ASN A  81      88.391  93.169  -5.339  1.00 39.13           O  
ATOM    377  CB  ASN A  81      87.290  94.283  -3.183  1.00 38.95           C  
ATOM    378  CG  ASN A  81      87.225  95.378  -4.188  1.00 39.93           C  
ATOM    379  OD1 ASN A  81      88.256  96.018  -4.449  1.00 39.26           O  
ATOM    380  ND2 ASN A  81      86.085  95.613  -4.765  1.00 41.34           N  
ATOM    381  N   PRO A  82      90.411  92.700  -4.489  1.00 38.27           N  
ATOM    382  CA  PRO A  82      91.009  92.106  -5.663  1.00 38.55           C  
ATOM    383  C   PRO A  82      90.424  90.741  -5.918  1.00 38.52           C  
ATOM    384  O   PRO A  82      89.730  90.188  -5.067  1.00 39.15           O  
ATOM    385  CB  PRO A  82      92.483  92.006  -5.275  1.00 38.22           C  
ATOM    386  CG  PRO A  82      92.457  91.866  -3.775  1.00 37.47           C  
ATOM    387  CD  PRO A  82      91.318  92.740  -3.331  1.00 37.90           C  
ATOM    388  N   VAL A  83      90.688  90.201  -7.091  1.00 38.87           N  
ATOM    389  CA  VAL A  83      90.276  88.840  -7.367  1.00 38.99           C  
ATOM    390  C   VAL A  83      91.386  87.897  -6.933  1.00 38.80           C  
ATOM    391  O   VAL A  83      92.539  88.066  -7.329  1.00 38.40           O  
ATOM    392  CB  VAL A  83      89.964  88.663  -8.865  1.00 39.25           C  
ATOM    393  CG1 VAL A  83      89.595  87.230  -9.160  1.00 39.98           C  
ATOM    394  CG2 VAL A  83      88.820  89.577  -9.247  1.00 40.35           C  
ATOM    395  N   LEU A  84      91.043  86.918  -6.110  1.00 39.00           N  
ATOM    396  CA  LEU A  84      92.022  85.971  -5.605  1.00 38.57           C  
ATOM    397  C   LEU A  84      91.763  84.610  -6.233  1.00 39.02           C  
ATOM    398  O   LEU A  84      90.630  84.318  -6.608  1.00 40.32           O  
ATOM    399  CB  LEU A  84      91.929  85.821  -4.075  1.00 38.86           C  
ATOM    400  CG  LEU A  84      92.307  87.036  -3.171  1.00 38.41           C  
ATOM    401  CD1 LEU A  84      93.499  87.781  -3.763  1.00 38.90           C  
ATOM    402  CD2 LEU A  84      91.099  87.939  -2.975  1.00 38.42           C  
ATOM    403  N   PRO A  85      92.778  83.762  -6.379  1.00 38.84           N  
ATOM    404  CA  PRO A  85      92.654  82.371  -6.748  1.00 39.18           C  
ATOM    405  C   PRO A  85      91.827  81.647  -5.710  1.00 39.33           C  
ATOM    406  O   PRO A  85      91.861  82.005  -4.537  1.00 38.51           O  
ATOM    407  CB  PRO A  85      94.104  81.880  -6.726  1.00 38.84           C  
ATOM    408  CG  PRO A  85      94.933  83.120  -6.926  1.00 38.89           C  
ATOM    409  CD  PRO A  85      94.158  84.232  -6.249  1.00 38.46           C  
ATOM    410  N   PHE A  86      91.104  80.623  -6.132  1.00 39.60           N  
ATOM    411  CA  PHE A  86      90.343  79.785  -5.214  1.00 39.27           C  
ATOM    412  C   PHE A  86      91.141  78.530  -4.865  1.00 38.65           C  
ATOM    413  O   PHE A  86      90.982  77.949  -3.791  1.00 38.55           O  
ATOM    414  CB  PHE A  86      89.007  79.395  -5.836  1.00 40.27           C  
ATOM    415  CG  PHE A  86      88.062  78.730  -4.904  1.00 39.73           C  
ATOM    416  CD1 PHE A  86      87.323  79.477  -3.991  1.00 39.26           C  
ATOM    417  CD2 PHE A  86      87.897  77.365  -4.933  1.00 39.69           C  
ATOM    418  CE1 PHE A  86      86.442  78.865  -3.132  1.00 38.85           C  
ATOM    419  CE2 PHE A  86      87.019  76.755  -4.075  1.00 39.38           C  
ATOM    420  CZ  PHE A  86      86.289  77.509  -3.174  1.00 38.87           C  
ATOM    421  N   ASN A  87      91.990  78.110  -5.798  1.00 39.00           N  
ATOM    422  CA  ASN A  87      92.784  76.897  -5.671  1.00 38.96           C  
ATOM    423  C   ASN A  87      91.907  75.691  -5.367  1.00 38.78           C  
ATOM    424  O   ASN A  87      90.975  75.404  -6.116  1.00 38.89           O  
ATOM    425  CB  ASN A  87      93.884  77.076  -4.638  1.00 38.31           C  
ATOM    426  CG  ASN A  87      94.865  78.150  -5.033  1.00 38.37           C  
ATOM    427  OD1 ASN A  87      95.004  78.466  -6.220  1.00 39.17           O  
ATOM    428  ND2 ASN A  87      95.556  78.702  -4.075  1.00 37.10           N  
ATOM    429  N   ASP A  88      92.194  74.980  -4.281  1.00 38.45           N  
ATOM    430  CA  ASP A  88      91.440  73.780  -3.946  1.00 38.03           C  
ATOM    431  C   ASP A  88      90.471  74.018  -2.808  1.00 37.43           C  
ATOM    432  O   ASP A  88      89.926  73.075  -2.242  1.00 36.54           O  
ATOM    433  CB  ASP A  88      92.384  72.638  -3.574  1.00 37.70           C  
ATOM    434  CG  ASP A  88      93.253  72.174  -4.740  1.00 38.73           C  
ATOM    435  OD1 ASP A  88      92.768  72.121  -5.845  1.00 38.35           O  
ATOM    436  OD2 ASP A  88      94.401  71.876  -4.508  1.00 37.22           O  
ATOM    437  N   GLY A  89      90.256  75.272  -2.467  1.00 37.84           N  
ATOM    438  CA  GLY A  89      89.386  75.619  -1.361  1.00 37.24           C  
ATOM    439  C   GLY A  89      89.963  76.795  -0.617  1.00 35.87           C  
ATOM    440  O   GLY A  89      91.181  76.982  -0.562  1.00 36.45           O  
ATOM    441  N   VAL A  90      89.086  77.591  -0.041  1.00 36.40           N  
ATOM    442  CA  VAL A  90      89.491  78.812   0.616  1.00 35.78           C  
ATOM    443  C   VAL A  90      89.036  78.983   2.038  1.00 35.40           C  
ATOM    444  O   VAL A  90      87.867  78.810   2.372  1.00 35.71           O  
ATOM    445  CB  VAL A  90      88.978  80.011  -0.194  1.00 36.48           C  
ATOM    446  CG1 VAL A  90      89.264  81.316   0.523  1.00 36.08           C  
ATOM    447  CG2 VAL A  90      89.655  80.012  -1.529  1.00 37.41           C  
ATOM    448  N   TYR A  91      89.966  79.384   2.869  1.00 35.05           N  
ATOM    449  CA  TYR A  91      89.635  79.795   4.210  1.00 34.65           C  
ATOM    450  C   TYR A  91      89.455  81.289   4.173  1.00 33.77           C  
ATOM    451  O   TYR A  91      90.300  82.000   3.638  1.00 35.76           O  
ATOM    452  CB  TYR A  91      90.717  79.453   5.209  1.00 34.40           C  
ATOM    453  CG  TYR A  91      90.428  80.044   6.539  1.00 33.86           C  
ATOM    454  CD1 TYR A  91      89.538  79.438   7.362  1.00 33.70           C  
ATOM    455  CD2 TYR A  91      91.049  81.208   6.931  1.00 33.72           C  
ATOM    456  CE1 TYR A  91      89.254  79.978   8.581  1.00 33.36           C  
ATOM    457  CE2 TYR A  91      90.770  81.746   8.156  1.00 33.58           C  
ATOM    458  CZ  TYR A  91      89.872  81.126   8.975  1.00 33.37           C  
ATOM    459  OH  TYR A  91      89.576  81.639  10.191  1.00 33.25           O  
ATOM    460  N   PHE A  92      88.385  81.784   4.735  1.00 34.46           N  
ATOM    461  CA  PHE A  92      88.171  83.213   4.723  1.00 34.39           C  
ATOM    462  C   PHE A  92      87.869  83.689   6.119  1.00 33.80           C  
ATOM    463  O   PHE A  92      87.154  83.031   6.861  1.00 35.51           O  
ATOM    464  CB  PHE A  92      87.020  83.567   3.792  1.00 34.75           C  
ATOM    465  CG  PHE A  92      86.770  85.031   3.626  1.00 34.94           C  
ATOM    466  CD1 PHE A  92      87.276  85.704   2.537  1.00 35.83           C  
ATOM    467  CD2 PHE A  92      86.038  85.743   4.560  1.00 34.78           C  
ATOM    468  CE1 PHE A  92      87.049  87.049   2.379  1.00 36.40           C  
ATOM    469  CE2 PHE A  92      85.815  87.089   4.410  1.00 35.30           C  
ATOM    470  CZ  PHE A  92      86.320  87.743   3.317  1.00 36.36           C  
ATOM    471  N   ALA A  93      88.391  84.829   6.489  1.00 34.31           N  
ATOM    472  CA  ALA A  93      88.032  85.365   7.785  1.00 34.14           C  
ATOM    473  C   ALA A  93      87.977  86.852   7.727  1.00 34.08           C  
ATOM    474  O   ALA A  93      88.714  87.481   6.979  1.00 37.22           O  
ATOM    475  CB  ALA A  93      89.020  84.929   8.844  1.00 34.12           C  
ATOM    476  N   SER A  94      87.142  87.440   8.546  1.00 35.14           N  
ATOM    477  CA  SER A  94      87.113  88.881   8.578  1.00 35.69           C  
ATOM    478  C   SER A  94      86.829  89.445   9.937  1.00 36.06           C  
ATOM    479  O   SER A  94      86.191  88.810  10.779  1.00 36.64           O  
ATOM    480  CB  SER A  94      86.082  89.378   7.613  1.00 36.10           C  
ATOM    481  OG  SER A  94      84.802  88.935   7.974  1.00 36.22           O  
ATOM    482  N   THR A  95      87.278  90.668  10.140  1.00 36.95           N  
ATOM    483  CA  THR A  95      87.026  91.354  11.388  1.00 37.08           C  
ATOM    484  C   THR A  95      86.168  92.576  11.127  1.00 37.79           C  
ATOM    485  O   THR A  95      86.433  93.350  10.208  1.00 37.61           O  
ATOM    486  CB  THR A  95      88.344  91.747  12.053  1.00 37.42           C  
ATOM    487  OG1 THR A  95      89.085  92.579  11.153  1.00 37.09           O  
ATOM    488  CG2 THR A  95      89.162  90.510  12.391  1.00 37.47           C  
ATOM    489  N   GLU A  96      85.147  92.742  11.956  1.00 37.82           N  
ATOM    490  CA  GLU A  96      84.157  93.790  11.779  1.00 38.26           C  
ATOM    491  C   GLU A  96      83.879  94.637  13.002  1.00 38.69           C  
ATOM    492  O   GLU A  96      84.055  94.214  14.152  1.00 38.17           O  
ATOM    493  CB  GLU A  96      82.835  93.164  11.366  1.00 38.44           C  
ATOM    494  CG  GLU A  96      82.817  92.533  10.022  1.00 38.80           C  
ATOM    495  CD  GLU A  96      82.781  93.515   8.940  1.00 39.00           C  
ATOM    496  OE1 GLU A  96      82.732  94.700   9.216  1.00 39.57           O  
ATOM    497  OE2 GLU A  96      82.759  93.090   7.822  1.00 38.93           O  
ATOM    498  N   LYS A  97      83.413  95.848  12.727  1.00 39.27           N  
ATOM    499  CA  LYS A  97      82.932  96.760  13.744  1.00 39.52           C  
ATOM    500  C   LYS A  97      81.668  97.439  13.232  1.00 39.58           C  
ATOM    501  O   LYS A  97      80.903  98.025  13.999  1.00 39.61           O  
ATOM    502  CB  LYS A  97      84.026  97.763  14.116  1.00 39.43           C  
ATOM    503  CG  LYS A  97      84.465  98.688  12.984  1.00 39.97           C  
ATOM    504  CD  LYS A  97      85.630  99.570  13.415  1.00 39.55           C  
ATOM    505  CE  LYS A  97      86.072 100.497  12.289  1.00 40.95           C  
ATOM    506  NZ  LYS A  97      87.214 101.362  12.695  1.00 40.77           N  
ATOM    507  N   SER A  98      81.469  97.367  11.912  1.00 39.97           N  
ATOM    508  CA  SER A  98      80.349  98.043  11.262  1.00 40.62           C  
ATOM    509  C   SER A  98      79.736  97.267  10.093  1.00 40.08           C  
ATOM    510  O   SER A  98      79.020  97.845   9.276  1.00 40.07           O  
ATOM    511  CB  SER A  98      80.775  99.420  10.797  1.00 40.86           C  
ATOM    512  OG  SER A  98      81.846  99.346   9.897  1.00 40.29           O  
ATOM    513  N   ASN A  99      80.004  95.966  10.016  1.00 39.71           N  
ATOM    514  CA  ASN A  99      79.452  95.113   8.957  1.00 39.74           C  
ATOM    515  C   ASN A  99      79.742  95.617   7.538  1.00 39.80           C  
ATOM    516  O   ASN A  99      78.830  95.725   6.712  1.00 40.17           O  
ATOM    517  CB  ASN A  99      77.957  94.938   9.166  1.00 39.39           C  
ATOM    518  CG  ASN A  99      77.380  93.788   8.396  1.00 39.67           C  
ATOM    519  OD1 ASN A  99      78.063  92.795   8.120  1.00 39.39           O  
ATOM    520  ND2 ASN A  99      76.121  93.899   8.052  1.00 40.57           N  
ATOM    521  N   ILE A 100      81.009  95.923   7.264  1.00 39.52           N  
ATOM    522  CA  ILE A 100      81.442  96.389   5.947  1.00 40.35           C  
ATOM    523  C   ILE A 100      81.463  95.273   4.915  1.00 39.75           C  
ATOM    524  O   ILE A 100      81.109  95.480   3.757  1.00 39.92           O  
ATOM    525  CB  ILE A 100      82.840  97.012   6.007  1.00 39.59           C  
ATOM    526  CG1 ILE A 100      82.846  98.269   6.926  1.00 39.77           C  
ATOM    527  CG2 ILE A 100      83.379  97.335   4.587  1.00 40.03           C  
ATOM    528  CD1 ILE A 100      81.892  99.394   6.523  1.00 40.77           C  
ATOM    529  N   ILE A 101      81.940  94.102   5.295  1.00 39.80           N  
ATOM    530  CA  ILE A 101      82.000  93.019   4.334  1.00 39.39           C  
ATOM    531  C   ILE A 101      80.645  92.369   4.269  1.00 39.45           C  
ATOM    532  O   ILE A 101      80.124  91.875   5.270  1.00 39.16           O  
ATOM    533  CB  ILE A 101      83.073  92.001   4.722  1.00 39.32           C  
ATOM    534  CG1 ILE A 101      84.423  92.708   4.715  1.00 39.18           C  
ATOM    535  CG2 ILE A 101      83.052  90.816   3.731  1.00 38.73           C  
ATOM    536  CD1 ILE A 101      85.495  91.997   5.416  1.00 38.26           C  
ATOM    537  N   ARG A 102      80.043  92.399   3.093  1.00 39.10           N  
ATOM    538  CA  ARG A 102      78.697  91.887   2.981  1.00 39.50           C  
ATOM    539  C   ARG A 102      78.537  90.784   1.964  1.00 39.61           C  
ATOM    540  O   ARG A 102      77.452  90.229   1.836  1.00 40.01           O  
ATOM    541  CB  ARG A 102      77.735  93.022   2.700  1.00 39.85           C  
ATOM    542  CG  ARG A 102      77.658  94.030   3.840  1.00 39.98           C  
ATOM    543  CD  ARG A 102      76.666  95.057   3.590  1.00 40.12           C  
ATOM    544  NE  ARG A 102      76.677  96.085   4.612  1.00 40.44           N  
ATOM    545  CZ  ARG A 102      75.901  97.190   4.594  1.00 41.38           C  
ATOM    546  NH1 ARG A 102      75.051  97.391   3.607  1.00 41.19           N  
ATOM    547  NH2 ARG A 102      75.995  98.077   5.567  1.00 42.42           N  
ATOM    548  N   GLY A 103      79.590  90.423   1.245  1.00 39.29           N  
ATOM    549  CA  GLY A 103      79.366  89.356   0.285  1.00 39.05           C  
ATOM    550  C   GLY A 103      80.584  88.805  -0.425  1.00 38.42           C  
ATOM    551  O   GLY A 103      81.721  89.215  -0.182  1.00 39.23           O  
ATOM    552  N   TRP A 104      80.310  87.815  -1.269  1.00 38.54           N  
ATOM    553  CA  TRP A 104      81.314  87.092  -2.038  1.00 38.50           C  
ATOM    554  C   TRP A 104      80.863  86.777  -3.460  1.00 38.88           C  
ATOM    555  O   TRP A 104      79.682  86.543  -3.711  1.00 41.19           O  
ATOM    556  CB  TRP A 104      81.659  85.766  -1.358  1.00 37.62           C  
ATOM    557  CG  TRP A 104      82.266  85.877   0.002  1.00 36.69           C  
ATOM    558  CD1 TRP A 104      83.591  85.852   0.291  1.00 36.71           C  
ATOM    559  CD2 TRP A 104      81.587  86.025   1.266  1.00 35.88           C  
ATOM    560  NE1 TRP A 104      83.780  85.986   1.631  1.00 35.98           N  
ATOM    561  CE2 TRP A 104      82.567  86.095   2.244  1.00 35.93           C  
ATOM    562  CE3 TRP A 104      80.248  86.108   1.639  1.00 36.65           C  
ATOM    563  CZ2 TRP A 104      82.257  86.248   3.583  1.00 34.88           C  
ATOM    564  CZ3 TRP A 104      79.938  86.264   2.982  1.00 36.00           C  
ATOM    565  CH2 TRP A 104      80.918  86.334   3.927  1.00 34.48           C  
ATOM    566  N   ILE A 105      81.822  86.705  -4.380  1.00 40.15           N  
ATOM    567  CA  ILE A 105      81.578  86.287  -5.756  1.00 40.49           C  
ATOM    568  C   ILE A 105      82.480  85.109  -6.115  1.00 41.64           C  
ATOM    569  O   ILE A 105      83.693  85.209  -5.963  1.00 40.63           O  
ATOM    570  CB  ILE A 105      81.911  87.406  -6.751  1.00 40.79           C  
ATOM    571  CG1 ILE A 105      81.149  88.680  -6.435  1.00 41.00           C  
ATOM    572  CG2 ILE A 105      81.537  86.920  -8.129  1.00 41.97           C  
ATOM    573  CD1 ILE A 105      81.664  89.887  -7.207  1.00 41.92           C  
ATOM    574  N   PHE A 106      81.926  84.016  -6.631  1.00 40.65           N  
ATOM    575  CA  PHE A 106      82.782  82.888  -7.017  1.00 41.03           C  
ATOM    576  C   PHE A 106      82.552  82.453  -8.461  1.00 42.19           C  
ATOM    577  O   PHE A 106      81.413  82.259  -8.884  1.00 42.51           O  
ATOM    578  CB  PHE A 106      82.520  81.690  -6.117  1.00 41.31           C  
ATOM    579  CG  PHE A 106      82.730  81.936  -4.675  1.00 40.78           C  
ATOM    580  CD1 PHE A 106      81.715  82.462  -3.910  1.00 40.18           C  
ATOM    581  CD2 PHE A 106      83.924  81.634  -4.069  1.00 40.08           C  
ATOM    582  CE1 PHE A 106      81.883  82.687  -2.576  1.00 39.32           C  
ATOM    583  CE2 PHE A 106      84.103  81.868  -2.721  1.00 39.17           C  
ATOM    584  CZ  PHE A 106      83.075  82.398  -1.976  1.00 38.21           C  
ATOM    585  N   GLY A 107      83.627  82.223  -9.206  1.00 42.73           N  
ATOM    586  CA  GLY A 107      83.500  81.788 -10.599  1.00 43.38           C  
ATOM    587  C   GLY A 107      84.860  81.732 -11.285  1.00 42.64           C  
ATOM    588  O   GLY A 107      85.881  81.525 -10.628  1.00 44.18           O  
ATOM    589  N   THR A 108      84.880  81.869 -12.610  1.00 43.41           N  
ATOM    590  CA  THR A 108      86.152  81.838 -13.331  1.00 43.90           C  
ATOM    591  C   THR A 108      86.486  83.201 -13.927  1.00 43.61           C  
ATOM    592  O   THR A 108      87.633  83.647 -13.868  1.00 43.78           O  
ATOM    593  CB  THR A 108      86.128  80.810 -14.467  1.00 44.22           C  
ATOM    594  OG1 THR A 108      85.099  81.157 -15.405  1.00 44.10           O  
ATOM    595  CG2 THR A 108      85.841  79.470 -13.916  1.00 45.24           C  
ATOM    596  N   THR A 109      85.481  83.865 -14.498  1.00 43.86           N  
ATOM    597  CA  THR A 109      85.687  85.166 -15.124  1.00 44.78           C  
ATOM    598  C   THR A 109      84.904  86.296 -14.448  1.00 44.49           C  
ATOM    599  O   THR A 109      85.268  87.464 -14.579  1.00 44.45           O  
ATOM    600  CB  THR A 109      85.366  85.083 -16.625  1.00 44.15           C  
ATOM    601  OG1 THR A 109      84.013  84.665 -16.811  1.00 45.08           O  
ATOM    602  CG2 THR A 109      86.300  84.089 -17.295  1.00 44.25           C  
ATOM    603  N   LEU A 110      83.849  85.951 -13.702  1.00 44.37           N  
ATOM    604  CA  LEU A 110      83.053  86.931 -12.947  1.00 44.26           C  
ATOM    605  C   LEU A 110      82.587  88.137 -13.790  1.00 44.65           C  
ATOM    606  O   LEU A 110      82.620  89.273 -13.319  1.00 44.99           O  
ATOM    607  CB  LEU A 110      83.902  87.465 -11.769  1.00 44.67           C  
ATOM    608  CG  LEU A 110      84.128  86.527 -10.535  1.00 43.76           C  
ATOM    609  CD1 LEU A 110      85.106  85.368 -10.859  1.00 43.28           C  
ATOM    610  CD2 LEU A 110      84.693  87.373  -9.392  1.00 42.33           C  
ATOM    611  N   ASP A 111      82.169  87.896 -15.026  1.00 45.26           N  
ATOM    612  CA  ASP A 111      81.815  88.982 -15.949  1.00 45.03           C  
ATOM    613  C   ASP A 111      80.583  88.735 -16.816  1.00 45.99           C  
ATOM    614  O   ASP A 111      80.521  89.238 -17.945  1.00 45.29           O  
ATOM    615  CB  ASP A 111      83.007  89.218 -16.848  1.00 45.27           C  
ATOM    616  CG  ASP A 111      83.319  87.947 -17.562  1.00 45.50           C  
ATOM    617  OD1 ASP A 111      82.598  86.975 -17.294  1.00 45.58           O  
ATOM    618  OD2 ASP A 111      84.250  87.898 -18.346  1.00 45.09           O  
ATOM    619  N   SER A 112      79.625  87.946 -16.334  1.00 45.13           N  
ATOM    620  CA  SER A 112      78.404  87.580 -17.064  1.00 44.81           C  
ATOM    621  C   SER A 112      78.638  86.563 -18.173  1.00 45.80           C  
ATOM    622  O   SER A 112      77.695  86.191 -18.872  1.00 45.52           O  
ATOM    623  CB  SER A 112      77.754  88.791 -17.719  1.00 45.81           C  
ATOM    624  OG  SER A 112      76.444  88.505 -18.126  1.00 45.13           O  
ATOM    625  N   LYS A 113      79.868  86.072 -18.329  1.00 45.59           N  
ATOM    626  CA  LYS A 113      80.130  85.065 -19.351  1.00 46.35           C  
ATOM    627  C   LYS A 113      79.935  83.650 -18.815  1.00 46.15           C  
ATOM    628  O   LYS A 113      79.761  82.705 -19.585  1.00 46.84           O  
ATOM    629  CB  LYS A 113      81.538  85.224 -19.907  1.00 46.50           C  
ATOM    630  CG  LYS A 113      81.762  86.527 -20.644  1.00 46.29           C  
ATOM    631  CD  LYS A 113      83.188  86.634 -21.151  1.00 46.92           C  
ATOM    632  CE  LYS A 113      83.458  88.020 -21.715  1.00 46.87           C  
ATOM    633  NZ  LYS A 113      84.879  88.192 -22.121  1.00 46.69           N  
ATOM    634  N   THR A 114      79.989  83.500 -17.500  1.00 46.06           N  
ATOM    635  CA  THR A 114      79.802  82.202 -16.863  1.00 45.92           C  
ATOM    636  C   THR A 114      78.920  82.357 -15.647  1.00 47.04           C  
ATOM    637  O   THR A 114      78.623  83.481 -15.231  1.00 46.09           O  
ATOM    638  CB  THR A 114      81.145  81.560 -16.454  1.00 45.75           C  
ATOM    639  OG1 THR A 114      80.918  80.198 -16.071  1.00 45.94           O  
ATOM    640  CG2 THR A 114      81.774  82.323 -15.279  1.00 45.31           C  
ATOM    641  N   GLN A 115      78.531  81.242 -15.047  1.00 45.92           N  
ATOM    642  CA  GLN A 115      77.704  81.312 -13.852  1.00 45.78           C  
ATOM    643  C   GLN A 115      78.594  81.650 -12.675  1.00 44.72           C  
ATOM    644  O   GLN A 115      79.698  81.123 -12.555  1.00 45.43           O  
ATOM    645  CB  GLN A 115      76.977  79.991 -13.598  1.00 45.57           C  
ATOM    646  CG  GLN A 115      76.053  79.567 -14.711  1.00 46.66           C  
ATOM    647  CD  GLN A 115      76.779  78.787 -15.786  1.00 46.60           C  
ATOM    648  OE1 GLN A 115      77.538  77.864 -15.482  1.00 46.38           O  
ATOM    649  NE2 GLN A 115      76.566  79.144 -17.046  1.00 47.07           N  
ATOM    650  N   SER A 116      78.128  82.543 -11.818  1.00 44.50           N  
ATOM    651  CA  SER A 116      78.930  82.955 -10.684  1.00 44.61           C  
ATOM    652  C   SER A 116      78.113  83.077  -9.416  1.00 43.34           C  
ATOM    653  O   SER A 116      77.109  83.786  -9.367  1.00 43.24           O  
ATOM    654  CB  SER A 116      79.602  84.267 -11.003  1.00 43.83           C  
ATOM    655  OG  SER A 116      80.316  84.731  -9.905  1.00 42.86           O  
ATOM    656  N   LEU A 117      78.539  82.362  -8.390  1.00 43.35           N  
ATOM    657  CA  LEU A 117      77.834  82.370  -7.122  1.00 42.87           C  
ATOM    658  C   LEU A 117      77.970  83.711  -6.441  1.00 42.05           C  
ATOM    659  O   LEU A 117      79.073  84.232  -6.301  1.00 42.49           O  
ATOM    660  CB  LEU A 117      78.372  81.264  -6.208  1.00 42.64           C  
ATOM    661  CG  LEU A 117      77.835  81.229  -4.756  1.00 41.68           C  
ATOM    662  CD1 LEU A 117      76.374  80.891  -4.728  1.00 42.20           C  
ATOM    663  CD2 LEU A 117      78.614  80.208  -3.982  1.00 41.42           C  
ATOM    664  N   LEU A 118      76.851  84.268  -6.025  1.00 42.10           N  
ATOM    665  CA  LEU A 118      76.818  85.542  -5.348  1.00 41.66           C  
ATOM    666  C   LEU A 118      76.126  85.450  -4.008  1.00 41.23           C  
ATOM    667  O   LEU A 118      74.965  85.054  -3.918  1.00 43.02           O  
ATOM    668  CB  LEU A 118      76.082  86.560  -6.219  1.00 42.26           C  
ATOM    669  CG  LEU A 118      75.806  87.926  -5.585  1.00 42.59           C  
ATOM    670  CD1 LEU A 118      77.105  88.634  -5.302  1.00 42.19           C  
ATOM    671  CD2 LEU A 118      74.946  88.733  -6.523  1.00 43.26           C  
ATOM    672  N   ILE A 119      76.829  85.832  -2.963  1.00 41.55           N  
ATOM    673  CA  ILE A 119      76.249  85.826  -1.630  1.00 42.06           C  
ATOM    674  C   ILE A 119      76.275  87.239  -1.074  1.00 40.69           C  
ATOM    675  O   ILE A 119      77.341  87.845  -1.000  1.00 42.14           O  
ATOM    676  CB  ILE A 119      77.041  84.881  -0.702  1.00 40.64           C  
ATOM    677  CG1 ILE A 119      77.023  83.445  -1.277  1.00 41.57           C  
ATOM    678  CG2 ILE A 119      76.450  84.932   0.717  1.00 41.63           C  
ATOM    679  CD1 ILE A 119      77.972  82.489  -0.595  1.00 39.89           C  
ATOM    680  N   VAL A 120      75.114  87.773  -0.697  1.00 42.36           N  
ATOM    681  CA  VAL A 120      75.037  89.125  -0.140  1.00 42.44           C  
ATOM    682  C   VAL A 120      74.206  89.194   1.129  1.00 41.86           C  
ATOM    683  O   VAL A 120      73.099  88.676   1.180  1.00 43.73           O  
ATOM    684  CB  VAL A 120      74.452  90.108  -1.166  1.00 42.74           C  
ATOM    685  CG1 VAL A 120      74.363  91.521  -0.547  1.00 42.31           C  
ATOM    686  CG2 VAL A 120      75.327  90.108  -2.405  1.00 42.71           C  
ATOM    687  N   ASN A 121      74.709  89.857   2.151  1.00 42.71           N  
ATOM    688  CA  ASN A 121      73.929  90.034   3.370  1.00 43.38           C  
ATOM    689  C   ASN A 121      73.649  91.517   3.631  1.00 43.05           C  
ATOM    690  O   ASN A 121      74.537  92.231   4.107  1.00 42.26           O  
ATOM    691  CB  ASN A 121      74.657  89.428   4.546  1.00 42.97           C  
ATOM    692  CG  ASN A 121      73.825  89.442   5.793  1.00 43.62           C  
ATOM    693  OD1 ASN A 121      72.593  89.402   5.730  1.00 43.97           O  
ATOM    694  ND2 ASN A 121      74.471  89.503   6.930  1.00 43.86           N  
ATOM    695  N   ASN A 122      72.431  91.994   3.286  1.00 43.86           N  
ATOM    696  CA  ASN A 122      72.056  93.397   3.388  1.00 43.87           C  
ATOM    697  C   ASN A 122      71.013  93.604   4.508  1.00 44.47           C  
ATOM    698  O   ASN A 122      69.872  93.180   4.392  1.00 44.69           O  
ATOM    699  CB  ASN A 122      71.575  93.954   2.035  1.00 44.33           C  
ATOM    700  CG  ASN A 122      70.431  93.164   1.355  1.00 45.06           C  
ATOM    701  OD1 ASN A 122      69.973  92.136   1.852  1.00 44.42           O  
ATOM    702  ND2 ASN A 122      69.959  93.668   0.231  1.00 45.50           N  
ATOM    703  N   ALA A 123      71.447  94.248   5.622  1.00 44.52           N  
ATOM    704  CA  ALA A 123      70.651  94.430   6.852  1.00 45.31           C  
ATOM    705  C   ALA A 123      70.369  93.077   7.497  1.00 45.42           C  
ATOM    706  O   ALA A 123      71.252  92.498   8.130  1.00 45.73           O  
ATOM    707  CB  ALA A 123      69.348  95.179   6.581  1.00 44.82           C  
ATOM    708  N   THR A 124      69.145  92.588   7.357  1.00 45.35           N  
ATOM    709  CA  THR A 124      68.760  91.321   7.955  1.00 45.71           C  
ATOM    710  C   THR A 124      68.433  90.242   6.925  1.00 45.31           C  
ATOM    711  O   THR A 124      67.880  89.201   7.277  1.00 45.10           O  
ATOM    712  CB  THR A 124      67.552  91.517   8.884  1.00 45.71           C  
ATOM    713  OG1 THR A 124      66.452  92.043   8.131  1.00 45.46           O  
ATOM    714  CG2 THR A 124      67.915  92.488   9.997  1.00 46.74           C  
ATOM    715  N   ASN A 125      68.732  90.476   5.647  1.00 44.98           N  
ATOM    716  CA  ASN A 125      68.382  89.483   4.632  1.00 44.29           C  
ATOM    717  C   ASN A 125      69.548  88.909   3.843  1.00 43.97           C  
ATOM    718  O   ASN A 125      70.137  89.568   2.987  1.00 44.45           O  
ATOM    719  CB  ASN A 125      67.373  90.046   3.652  1.00 44.97           C  
ATOM    720  CG  ASN A 125      65.977  90.227   4.213  1.00 45.01           C  
ATOM    721  OD1 ASN A 125      65.129  90.798   3.520  1.00 46.08           O  
ATOM    722  ND2 ASN A 125      65.705  89.750   5.410  1.00 45.02           N  
ATOM    723  N   VAL A 126      69.819  87.635   4.081  1.00 44.12           N  
ATOM    724  CA  VAL A 126      70.851  86.926   3.341  1.00 43.97           C  
ATOM    725  C   VAL A 126      70.309  86.485   1.989  1.00 43.82           C  
ATOM    726  O   VAL A 126      69.269  85.836   1.905  1.00 45.08           O  
ATOM    727  CB  VAL A 126      71.341  85.693   4.124  1.00 43.89           C  
ATOM    728  CG1 VAL A 126      72.355  84.901   3.287  1.00 44.52           C  
ATOM    729  CG2 VAL A 126      71.965  86.149   5.426  1.00 44.08           C  
ATOM    730  N   VAL A 127      71.015  86.846   0.935  1.00 43.74           N  
ATOM    731  CA  VAL A 127      70.607  86.545  -0.422  1.00 43.89           C  
ATOM    732  C   VAL A 127      71.648  85.714  -1.160  1.00 42.40           C  
ATOM    733  O   VAL A 127      72.816  86.089  -1.230  1.00 43.83           O  
ATOM    734  CB  VAL A 127      70.385  87.865  -1.179  1.00 44.05           C  
ATOM    735  CG1 VAL A 127      69.977  87.589  -2.614  1.00 44.43           C  
ATOM    736  CG2 VAL A 127      69.339  88.694  -0.452  1.00 44.23           C  
ATOM    737  N   ILE A 128      71.232  84.592  -1.721  1.00 43.24           N  
ATOM    738  CA  ILE A 128      72.142  83.754  -2.488  1.00 42.97           C  
ATOM    739  C   ILE A 128      71.620  83.533  -3.898  1.00 42.33           C  
ATOM    740  O   ILE A 128      70.487  83.096  -4.085  1.00 44.34           O  
ATOM    741  CB  ILE A 128      72.367  82.391  -1.811  1.00 43.12           C  
ATOM    742  CG1 ILE A 128      72.944  82.599  -0.391  1.00 43.17           C  
ATOM    743  CG2 ILE A 128      73.308  81.546  -2.680  1.00 42.83           C  
ATOM    744  CD1 ILE A 128      73.035  81.333   0.449  1.00 43.93           C  
ATOM    745  N   LYS A 129      72.447  83.821  -4.890  1.00 42.34           N  
ATOM    746  CA  LYS A 129      72.068  83.629  -6.286  1.00 42.81           C  
ATOM    747  C   LYS A 129      73.212  83.023  -7.090  1.00 41.73           C  
ATOM    748  O   LYS A 129      74.370  83.246  -6.765  1.00 43.72           O  
ATOM    749  CB  LYS A 129      71.651  84.966  -6.880  1.00 42.75           C  
ATOM    750  CG  LYS A 129      70.411  85.578  -6.238  1.00 43.60           C  
ATOM    751  CD  LYS A 129      70.022  86.896  -6.888  1.00 45.44           C  
ATOM    752  CE  LYS A 129      68.767  87.475  -6.250  1.00 45.20           C  
ATOM    753  NZ  LYS A 129      68.383  88.782  -6.850  1.00 46.13           N  
ATOM    754  N   VAL A 130      72.911  82.279  -8.149  1.00 42.43           N  
ATOM    755  CA  VAL A 130      73.994  81.741  -9.005  1.00 42.66           C  
ATOM    756  C   VAL A 130      73.874  82.101 -10.488  1.00 42.81           C  
ATOM    757  O   VAL A 130      74.202  81.282 -11.347  1.00 43.30           O  
ATOM    758  CB  VAL A 130      74.054  80.225  -8.916  1.00 42.47           C  
ATOM    759  CG1 VAL A 130      74.392  79.803  -7.522  1.00 42.28           C  
ATOM    760  CG2 VAL A 130      72.774  79.667  -9.364  1.00 42.77           C  
ATOM    761  N   CYS A 131      73.378  83.308 -10.766  1.00 43.20           N  
ATOM    762  CA  CYS A 131      73.102  83.817 -12.107  1.00 43.52           C  
ATOM    763  C   CYS A 131      74.403  84.184 -12.846  1.00 44.24           C  
ATOM    764  O   CYS A 131      75.468  84.302 -12.254  1.00 44.20           O  
ATOM    765  CB  CYS A 131      72.221  85.085 -12.009  1.00 44.33           C  
ATOM    766  SG  CYS A 131      70.653  84.843 -11.142  1.00 44.57           S  
ATOM    767  N   GLU A 132      74.283  84.374 -14.177  1.00 44.38           N  
ATOM    768  CA  GLU A 132      75.394  84.862 -14.995  1.00 44.88           C  
ATOM    769  C   GLU A 132      75.385  86.378 -14.883  1.00 44.79           C  
ATOM    770  O   GLU A 132      74.984  87.098 -15.798  1.00 44.27           O  
ATOM    771  CB  GLU A 132      75.245  84.421 -16.447  1.00 45.54           C  
ATOM    772  CG  GLU A 132      75.298  82.926 -16.663  1.00 45.83           C  
ATOM    773  CD  GLU A 132      75.217  82.562 -18.105  1.00 46.56           C  
ATOM    774  OE1 GLU A 132      75.054  83.437 -18.924  1.00 47.66           O  
ATOM    775  OE2 GLU A 132      75.317  81.396 -18.397  1.00 47.53           O  
ATOM    776  N   PHE A 133      75.780  86.832 -13.705  1.00 43.99           N  
ATOM    777  CA  PHE A 133      75.682  88.226 -13.314  1.00 43.99           C  
ATOM    778  C   PHE A 133      76.633  89.119 -14.041  1.00 44.80           C  
ATOM    779  O   PHE A 133      77.802  88.782 -14.231  1.00 45.17           O  
ATOM    780  CB  PHE A 133      76.006  88.396 -11.840  1.00 43.92           C  
ATOM    781  CG  PHE A 133      74.971  87.997 -10.911  1.00 43.22           C  
ATOM    782  CD1 PHE A 133      73.871  88.802 -10.736  1.00 42.47           C  
ATOM    783  CD2 PHE A 133      75.084  86.836 -10.175  1.00 43.00           C  
ATOM    784  CE1 PHE A 133      72.895  88.458  -9.854  1.00 43.81           C  
ATOM    785  CE2 PHE A 133      74.108  86.491  -9.289  1.00 43.45           C  
ATOM    786  CZ  PHE A 133      73.009  87.306  -9.133  1.00 43.35           C  
ATOM    787  N   GLN A 134      76.160  90.307 -14.367  1.00 45.00           N  
ATOM    788  CA  GLN A 134      77.058  91.301 -14.895  1.00 45.50           C  
ATOM    789  C   GLN A 134      77.570  92.124 -13.749  1.00 45.69           C  
ATOM    790  O   GLN A 134      76.854  92.942 -13.170  1.00 45.80           O  
ATOM    791  CB  GLN A 134      76.389  92.202 -15.934  1.00 46.27           C  
ATOM    792  CG  GLN A 134      77.314  93.291 -16.467  1.00 47.11           C  
ATOM    793  CD  GLN A 134      78.460  92.746 -17.316  1.00 46.85           C  
ATOM    794  OE1 GLN A 134      78.237  92.246 -18.426  1.00 46.55           O  
ATOM    795  NE2 GLN A 134      79.698  92.830 -16.793  1.00 46.65           N  
ATOM    796  N   PHE A 135      78.815  91.885 -13.414  1.00 45.11           N  
ATOM    797  CA  PHE A 135      79.452  92.559 -12.323  1.00 45.13           C  
ATOM    798  C   PHE A 135      80.141  93.797 -12.844  1.00 44.86           C  
ATOM    799  O   PHE A 135      80.498  93.878 -14.026  1.00 45.36           O  
ATOM    800  CB  PHE A 135      80.433  91.644 -11.605  1.00 44.54           C  
ATOM    801  CG  PHE A 135      79.777  90.560 -10.800  1.00 43.96           C  
ATOM    802  CD1 PHE A 135      79.881  89.234 -11.172  1.00 44.31           C  
ATOM    803  CD2 PHE A 135      79.043  90.877  -9.665  1.00 44.07           C  
ATOM    804  CE1 PHE A 135      79.279  88.248 -10.422  1.00 44.45           C  
ATOM    805  CE2 PHE A 135      78.436  89.897  -8.921  1.00 43.58           C  
ATOM    806  CZ  PHE A 135      78.555  88.582  -9.295  1.00 43.33           C  
ATOM    807  N   CYS A 136      80.308  94.760 -11.963  1.00 44.01           N  
ATOM    808  CA  CYS A 136      80.973  96.005 -12.295  1.00 43.57           C  
ATOM    809  C   CYS A 136      82.453  95.767 -12.544  1.00 44.39           C  
ATOM    810  O   CYS A 136      82.998  94.730 -12.171  1.00 44.43           O  
ATOM    811  CB  CYS A 136      80.818  96.995 -11.149  1.00 43.34           C  
ATOM    812  SG  CYS A 136      79.110  97.401 -10.760  1.00 41.33           S  
ATOM    813  N   ASN A 137      83.117  96.755 -13.140  1.00 44.56           N  
ATOM    814  CA  ASN A 137      84.555  96.656 -13.358  1.00 44.61           C  
ATOM    815  C   ASN A 137      85.255  96.500 -12.014  1.00 44.05           C  
ATOM    816  O   ASN A 137      86.262  95.804 -11.889  1.00 44.34           O  
ATOM    817  CB  ASN A 137      85.064  97.890 -14.077  1.00 45.54           C  
ATOM    818  CG  ASN A 137      84.628  97.958 -15.517  1.00 46.01           C  
ATOM    819  OD1 ASN A 137      84.231  96.954 -16.120  1.00 45.27           O  
ATOM    820  ND2 ASN A 137      84.693  99.135 -16.080  1.00 44.30           N  
ATOM    821  N   ASP A 138      84.681  97.139 -11.002  1.00 43.84           N  
ATOM    822  CA  ASP A 138      85.142  97.068  -9.628  1.00 43.56           C  
ATOM    823  C   ASP A 138      83.905  96.989  -8.733  1.00 43.47           C  
ATOM    824  O   ASP A 138      83.347  98.025  -8.381  1.00 42.97           O  
ATOM    825  CB  ASP A 138      85.969  98.306  -9.273  1.00 44.55           C  
ATOM    826  CG  ASP A 138      86.557  98.223  -7.891  1.00 44.11           C  
ATOM    827  OD1 ASP A 138      86.320  97.232  -7.247  1.00 43.39           O  
ATOM    828  OD2 ASP A 138      87.238  99.136  -7.485  1.00 45.00           O  
ATOM    829  N   PRO A 139      83.391  95.782  -8.449  1.00 43.03           N  
ATOM    830  CA  PRO A 139      82.180  95.519  -7.693  1.00 42.46           C  
ATOM    831  C   PRO A 139      82.244  96.039  -6.271  1.00 42.52           C  
ATOM    832  O   PRO A 139      83.219  95.812  -5.561  1.00 42.19           O  
ATOM    833  CB  PRO A 139      82.124  93.985  -7.690  1.00 42.46           C  
ATOM    834  CG  PRO A 139      82.934  93.569  -8.877  1.00 43.07           C  
ATOM    835  CD  PRO A 139      84.047  94.576  -8.953  1.00 42.87           C  
ATOM    836  N   PHE A 140      81.180  96.689  -5.846  1.00 42.66           N  
ATOM    837  CA  PHE A 140      81.058  97.148  -4.477  1.00 42.56           C  
ATOM    838  C   PHE A 140      79.605  97.442  -4.201  1.00 42.93           C  
ATOM    839  O   PHE A 140      78.798  97.550  -5.125  1.00 42.69           O  
ATOM    840  CB  PHE A 140      81.911  98.383  -4.191  1.00 42.58           C  
ATOM    841  CG  PHE A 140      81.510  99.609  -4.931  1.00 42.59           C  
ATOM    842  CD1 PHE A 140      80.581 100.492  -4.394  1.00 43.01           C  
ATOM    843  CD2 PHE A 140      82.067  99.896  -6.148  1.00 42.92           C  
ATOM    844  CE1 PHE A 140      80.223 101.629  -5.079  1.00 43.69           C  
ATOM    845  CE2 PHE A 140      81.714 101.028  -6.839  1.00 43.46           C  
ATOM    846  CZ  PHE A 140      80.790 101.900  -6.305  1.00 42.97           C  
ATOM    847  N   LEU A 141      79.273  97.582  -2.936  1.00 42.73           N  
ATOM    848  CA  LEU A 141      77.938  97.973  -2.544  1.00 42.18           C  
ATOM    849  C   LEU A 141      78.012  99.317  -1.845  1.00 42.07           C  
ATOM    850  O   LEU A 141      78.871  99.516  -0.991  1.00 42.50           O  
ATOM    851  CB  LEU A 141      77.348  96.905  -1.616  1.00 42.20           C  
ATOM    852  CG  LEU A 141      75.945  97.154  -1.073  1.00 41.78           C  
ATOM    853  CD1 LEU A 141      74.921  97.084  -2.210  1.00 40.48           C  
ATOM    854  CD2 LEU A 141      75.665  96.125  -0.006  1.00 41.24           C  
ATOM    855  N   GLY A 142      77.159 100.254  -2.214  1.00 42.74           N  
ATOM    856  CA  GLY A 142      77.186 101.530  -1.518  1.00 42.73           C  
ATOM    857  C   GLY A 142      76.301 101.469  -0.277  1.00 42.64           C  
ATOM    858  O   GLY A 142      75.363 100.670  -0.228  1.00 42.43           O  
ATOM    859  N   VAL A 143      76.565 102.353   0.693  1.00 42.56           N  
ATOM    860  CA  VAL A 143      75.743 102.509   1.896  1.00 42.70           C  
ATOM    861  C   VAL A 143      74.682 103.583   1.623  1.00 44.49           C  
ATOM    862  O   VAL A 143      74.991 104.700   1.193  1.00 42.79           O  
ATOM    863  CB  VAL A 143      76.622 102.871   3.156  1.00 42.33           C  
ATOM    864  CG1 VAL A 143      75.731 103.134   4.436  1.00 41.26           C  
ATOM    865  CG2 VAL A 143      77.636 101.701   3.467  1.00 42.05           C  
ATOM    866  N   ASN A 165      69.803  83.291 -17.121  1.00 45.28           N  
ATOM    867  CA  ASN A 165      70.294  81.910 -17.025  1.00 45.27           C  
ATOM    868  C   ASN A 165      70.661  81.565 -15.571  1.00 45.65           C  
ATOM    869  O   ASN A 165      71.748  81.045 -15.295  1.00 45.53           O  
ATOM    870  CB  ASN A 165      71.481  81.705 -17.970  1.00 47.37           C  
ATOM    871  CG  ASN A 165      71.080  81.564 -19.461  1.00 46.71           C  
ATOM    872  OD1 ASN A 165      70.017  82.055 -19.889  1.00 48.18           O  
ATOM    873  ND2 ASN A 165      71.940  80.901 -20.218  1.00 47.72           N  
ATOM    874  N   CYS A 166      69.719  81.826 -14.636  1.00 44.92           N  
ATOM    875  CA  CYS A 166      69.864  81.554 -13.201  1.00 45.42           C  
ATOM    876  C   CYS A 166      69.399  80.119 -12.907  1.00 45.25           C  
ATOM    877  O   CYS A 166      68.367  79.686 -13.435  1.00 44.85           O  
ATOM    878  CB  CYS A 166      69.006  82.534 -12.360  1.00 45.75           C  
ATOM    879  SG  CYS A 166      69.367  84.302 -12.620  1.00 48.43           S  
ATOM    880  N   THR A 167      70.137  79.395 -12.043  1.00 45.20           N  
ATOM    881  CA  THR A 167      69.797  78.024 -11.641  1.00 45.56           C  
ATOM    882  C   THR A 167      69.460  77.912 -10.154  1.00 44.96           C  
ATOM    883  O   THR A 167      69.147  76.824  -9.673  1.00 45.68           O  
ATOM    884  CB  THR A 167      70.938  77.054 -11.983  1.00 46.37           C  
ATOM    885  OG1 THR A 167      72.108  77.417 -11.264  1.00 45.71           O  
ATOM    886  CG2 THR A 167      71.237  77.131 -13.470  1.00 46.02           C  
ATOM    887  N   PHE A 168      69.571  79.015  -9.417  1.00 45.22           N  
ATOM    888  CA  PHE A 168      69.300  78.994  -7.979  1.00 44.50           C  
ATOM    889  C   PHE A 168      69.114  80.380  -7.391  1.00 43.56           C  
ATOM    890  O   PHE A 168      69.849  81.315  -7.726  1.00 44.22           O  
ATOM    891  CB  PHE A 168      70.403  78.268  -7.192  1.00 44.23           C  
ATOM    892  CG  PHE A 168      70.191  78.289  -5.712  1.00 44.43           C  
ATOM    893  CD1 PHE A 168      69.458  77.306  -5.088  1.00 44.62           C  
ATOM    894  CD2 PHE A 168      70.720  79.313  -4.934  1.00 43.55           C  
ATOM    895  CE1 PHE A 168      69.259  77.336  -3.722  1.00 44.61           C  
ATOM    896  CE2 PHE A 168      70.516  79.338  -3.576  1.00 43.48           C  
ATOM    897  CZ  PHE A 168      69.789  78.351  -2.971  1.00 44.03           C  
ATOM    898  N   GLU A 169      68.150  80.496  -6.483  1.00 43.67           N  
ATOM    899  CA  GLU A 169      67.952  81.702  -5.690  1.00 43.59           C  
ATOM    900  C   GLU A 169      67.409  81.381  -4.305  1.00 43.68           C  
ATOM    901  O   GLU A 169      66.485  80.580  -4.158  1.00 43.31           O  
ATOM    902  CB  GLU A 169      66.997  82.670  -6.387  1.00 43.05           C  
ATOM    903  CG  GLU A 169      66.696  83.946  -5.578  1.00 43.85           C  
ATOM    904  CD  GLU A 169      65.837  84.928  -6.312  1.00 44.90           C  
ATOM    905  OE1 GLU A 169      65.434  84.637  -7.410  1.00 44.66           O  
ATOM    906  OE2 GLU A 169      65.591  85.982  -5.776  1.00 44.71           O  
ATOM    907  N   TYR A 170      67.948  82.053  -3.298  1.00 43.52           N  
ATOM    908  CA  TYR A 170      67.462  81.951  -1.927  1.00 43.94           C  
ATOM    909  C   TYR A 170      67.507  83.277  -1.192  1.00 43.94           C  
ATOM    910  O   TYR A 170      68.488  84.011  -1.277  1.00 44.95           O  
ATOM    911  CB  TYR A 170      68.278  80.930  -1.148  1.00 44.05           C  
ATOM    912  CG  TYR A 170      68.041  81.004   0.321  1.00 44.36           C  
ATOM    913  CD1 TYR A 170      66.966  80.363   0.888  1.00 44.44           C  
ATOM    914  CD2 TYR A 170      68.904  81.742   1.108  1.00 44.00           C  
ATOM    915  CE1 TYR A 170      66.755  80.454   2.245  1.00 44.68           C  
ATOM    916  CE2 TYR A 170      68.695  81.832   2.456  1.00 44.22           C  
ATOM    917  CZ  TYR A 170      67.624  81.191   3.027  1.00 44.59           C  
ATOM    918  OH  TYR A 170      67.413  81.277   4.375  1.00 44.12           O  
ATOM    919  N   VAL A 171      66.457  83.583  -0.443  1.00 43.94           N  
ATOM    920  CA  VAL A 171      66.462  84.771   0.401  1.00 44.32           C  
ATOM    921  C   VAL A 171      65.978  84.456   1.821  1.00 44.11           C  
ATOM    922  O   VAL A 171      64.901  83.882   1.985  1.00 44.02           O  
ATOM    923  CB  VAL A 171      65.573  85.874  -0.205  1.00 44.17           C  
ATOM    924  CG1 VAL A 171      65.574  87.118   0.701  1.00 43.96           C  
ATOM    925  CG2 VAL A 171      66.085  86.223  -1.594  1.00 44.54           C  
ATOM    926  N   SER A 172      66.741  84.889   2.840  1.00 43.82           N  
ATOM    927  CA  SER A 172      66.359  84.754   4.244  1.00 43.97           C  
ATOM    928  C   SER A 172      65.371  85.863   4.611  1.00 44.05           C  
ATOM    929  O   SER A 172      64.759  85.841   5.683  1.00 44.87           O  
ATOM    930  CB  SER A 172      67.578  84.819   5.167  1.00 43.76           C  
ATOM    931  OG  SER A 172      68.435  83.741   4.959  1.00 43.95           O  
ATOM    932  N   PHE A 186      88.367  95.684  16.508  1.00 38.35           N  
ATOM    933  CA  PHE A 186      87.134  95.155  15.968  1.00 38.56           C  
ATOM    934  C   PHE A 186      86.387  94.385  17.065  1.00 38.72           C  
ATOM    935  O   PHE A 186      86.979  93.992  18.081  1.00 38.72           O  
ATOM    936  CB  PHE A 186      87.424  94.249  14.747  1.00 37.97           C  
ATOM    937  CG  PHE A 186      88.008  94.985  13.507  1.00 38.21           C  
ATOM    938  CD1 PHE A 186      89.400  94.815  13.128  1.00 37.96           C  
ATOM    939  CD2 PHE A 186      87.187  95.865  12.700  1.00 38.10           C  
ATOM    940  CE1 PHE A 186      89.939  95.492  11.985  1.00 37.56           C  
ATOM    941  CE2 PHE A 186      87.727  96.543  11.563  1.00 38.03           C  
ATOM    942  CZ  PHE A 186      89.103  96.354  11.204  1.00 37.20           C  
ATOM    943  N   LYS A 187      85.066  94.202  16.868  1.00 38.14           N  
ATOM    944  CA  LYS A 187      84.165  93.566  17.839  1.00 38.98           C  
ATOM    945  C   LYS A 187      83.674  92.188  17.408  1.00 38.43           C  
ATOM    946  O   LYS A 187      83.255  91.388  18.245  1.00 37.73           O  
ATOM    947  CB  LYS A 187      82.964  94.474  18.103  1.00 38.96           C  
ATOM    948  CG  LYS A 187      83.312  95.860  18.667  1.00 39.19           C  
ATOM    949  CD  LYS A 187      83.978  95.766  20.046  1.00 39.22           C  
ATOM    950  CE  LYS A 187      84.197  97.139  20.654  1.00 39.55           C  
ATOM    951  NZ  LYS A 187      84.888  97.057  21.970  1.00 40.30           N  
ATOM    952  N   ASN A 188      83.680  91.919  16.107  1.00 38.50           N  
ATOM    953  CA  ASN A 188      83.131  90.662  15.607  1.00 37.76           C  
ATOM    954  C   ASN A 188      84.023  89.949  14.595  1.00 37.81           C  
ATOM    955  O   ASN A 188      84.404  90.509  13.567  1.00 37.39           O  
ATOM    956  CB  ASN A 188      81.759  90.906  15.011  1.00 38.32           C  
ATOM    957  CG  ASN A 188      80.747  91.315  16.046  1.00 38.57           C  
ATOM    958  OD1 ASN A 188      80.286  90.490  16.844  1.00 38.72           O  
ATOM    959  ND2 ASN A 188      80.385  92.572  16.049  1.00 38.58           N  
ATOM    960  N   LEU A 189      84.361  88.701  14.894  1.00 37.24           N  
ATOM    961  CA  LEU A 189      85.141  87.866  13.989  1.00 36.58           C  
ATOM    962  C   LEU A 189      84.243  86.854  13.307  1.00 35.50           C  
ATOM    963  O   LEU A 189      83.522  86.100  13.962  1.00 37.08           O  
ATOM    964  CB  LEU A 189      86.261  87.155  14.751  1.00 36.45           C  
ATOM    965  CG  LEU A 189      87.065  86.070  14.010  1.00 35.81           C  
ATOM    966  CD1 LEU A 189      87.844  86.671  12.849  1.00 36.01           C  
ATOM    967  CD2 LEU A 189      88.025  85.408  15.003  1.00 36.64           C  
ATOM    968  N   ARG A 190      84.261  86.858  11.988  1.00 35.96           N  
ATOM    969  CA  ARG A 190      83.421  85.951  11.228  1.00 34.67           C  
ATOM    970  C   ARG A 190      84.255  85.079  10.312  1.00 34.32           C  
ATOM    971  O   ARG A 190      84.797  85.552   9.312  1.00 35.27           O  
ATOM    972  CB  ARG A 190      82.397  86.731  10.425  1.00 35.47           C  
ATOM    973  CG  ARG A 190      81.432  87.547  11.271  1.00 35.82           C  
ATOM    974  CD  ARG A 190      80.364  88.157  10.454  1.00 36.57           C  
ATOM    975  NE  ARG A 190      80.876  89.190   9.569  1.00 37.19           N  
ATOM    976  CZ  ARG A 190      80.191  89.720   8.532  1.00 38.46           C  
ATOM    977  NH1 ARG A 190      78.971  89.295   8.269  1.00 37.68           N  
ATOM    978  NH2 ARG A 190      80.741  90.666   7.777  1.00 38.58           N  
ATOM    979  N   GLU A 191      84.401  83.815  10.682  1.00 34.64           N  
ATOM    980  CA  GLU A 191      85.253  82.900   9.939  1.00 34.23           C  
ATOM    981  C   GLU A 191      84.417  82.014   9.045  1.00 33.65           C  
ATOM    982  O   GLU A 191      83.326  81.598   9.424  1.00 36.03           O  
ATOM    983  CB  GLU A 191      86.092  82.078  10.907  1.00 34.28           C  
ATOM    984  CG  GLU A 191      87.021  82.933  11.754  1.00 34.56           C  
ATOM    985  CD  GLU A 191      87.915  82.157  12.671  1.00 34.58           C  
ATOM    986  OE1 GLU A 191      87.510  81.129  13.145  1.00 34.39           O  
ATOM    987  OE2 GLU A 191      89.023  82.590  12.882  1.00 35.00           O  
ATOM    988  N   PHE A 192      84.924  81.734   7.858  1.00 34.06           N  
ATOM    989  CA  PHE A 192      84.231  80.918   6.880  1.00 34.23           C  
ATOM    990  C   PHE A 192      85.149  79.922   6.203  1.00 33.99           C  
ATOM    991  O   PHE A 192      86.338  80.174   6.035  1.00 35.81           O  
ATOM    992  CB  PHE A 192      83.633  81.802   5.793  1.00 34.80           C  
ATOM    993  CG  PHE A 192      82.662  82.803   6.277  1.00 34.24           C  
ATOM    994  CD1 PHE A 192      83.099  83.997   6.808  1.00 34.45           C  
ATOM    995  CD2 PHE A 192      81.312  82.570   6.193  1.00 34.52           C  
ATOM    996  CE1 PHE A 192      82.211  84.931   7.259  1.00 34.44           C  
ATOM    997  CE2 PHE A 192      80.411  83.505   6.646  1.00 34.79           C  
ATOM    998  CZ  PHE A 192      80.862  84.688   7.183  1.00 35.34           C  
ATOM    999  N   VAL A 193      84.585  78.827   5.743  1.00 35.23           N  
ATOM   1000  CA  VAL A 193      85.311  77.917   4.874  1.00 35.74           C  
ATOM   1001  C   VAL A 193      84.493  77.676   3.631  1.00 35.47           C  
ATOM   1002  O   VAL A 193      83.309  77.361   3.718  1.00 36.91           O  
ATOM   1003  CB  VAL A 193      85.620  76.582   5.564  1.00 35.42           C  
ATOM   1004  CG1 VAL A 193      86.339  75.652   4.623  1.00 35.66           C  
ATOM   1005  CG2 VAL A 193      86.456  76.834   6.772  1.00 35.44           C  
ATOM   1006  N   PHE A 194      85.114  77.842   2.477  1.00 36.15           N  
ATOM   1007  CA  PHE A 194      84.439  77.631   1.213  1.00 36.74           C  
ATOM   1008  C   PHE A 194      85.167  76.572   0.395  1.00 37.18           C  
ATOM   1009  O   PHE A 194      86.315  76.771   0.002  1.00 37.34           O  
ATOM   1010  CB  PHE A 194      84.403  78.939   0.415  1.00 36.58           C  
ATOM   1011  CG  PHE A 194      83.718  80.095   1.118  1.00 36.31           C  
ATOM   1012  CD1 PHE A 194      84.447  81.110   1.712  1.00 35.89           C  
ATOM   1013  CD2 PHE A 194      82.357  80.162   1.186  1.00 36.63           C  
ATOM   1014  CE1 PHE A 194      83.809  82.162   2.343  1.00 35.52           C  
ATOM   1015  CE2 PHE A 194      81.717  81.207   1.818  1.00 36.23           C  
ATOM   1016  CZ  PHE A 194      82.447  82.210   2.394  1.00 35.34           C  
ATOM   1017  N   LYS A 195      84.528  75.446   0.123  1.00 37.73           N  
ATOM   1018  CA  LYS A 195      85.210  74.437  -0.691  1.00 38.46           C  
ATOM   1019  C   LYS A 195      84.279  73.801  -1.715  1.00 39.34           C  
ATOM   1020  O   LYS A 195      83.071  73.729  -1.508  1.00 39.37           O  
ATOM   1021  CB  LYS A 195      85.886  73.370   0.184  1.00 37.96           C  
ATOM   1022  CG  LYS A 195      84.969  72.486   1.012  1.00 37.76           C  
ATOM   1023  CD  LYS A 195      85.791  71.479   1.844  1.00 36.04           C  
ATOM   1024  CE  LYS A 195      84.897  70.463   2.542  1.00 35.86           C  
ATOM   1025  NZ  LYS A 195      85.678  69.456   3.341  1.00 33.93           N  
ATOM   1026  N   ASN A 196      84.848  73.330  -2.825  1.00 40.23           N  
ATOM   1027  CA  ASN A 196      84.056  72.700  -3.880  1.00 41.21           C  
ATOM   1028  C   ASN A 196      84.423  71.258  -4.147  1.00 41.76           C  
ATOM   1029  O   ASN A 196      85.509  70.961  -4.647  1.00 41.85           O  
ATOM   1030  CB  ASN A 196      84.154  73.470  -5.178  1.00 41.25           C  
ATOM   1031  CG  ASN A 196      83.373  74.708  -5.160  1.00 40.79           C  
ATOM   1032  OD1 ASN A 196      82.144  74.663  -5.287  1.00 41.46           O  
ATOM   1033  ND2 ASN A 196      84.034  75.817  -5.008  1.00 40.28           N  
ATOM   1034  N   ILE A 197      83.506  70.364  -3.812  1.00 42.45           N  
ATOM   1035  CA  ILE A 197      83.720  68.943  -4.032  1.00 43.13           C  
ATOM   1036  C   ILE A 197      82.662  68.380  -4.960  1.00 44.30           C  
ATOM   1037  O   ILE A 197      81.482  68.357  -4.626  1.00 44.21           O  
ATOM   1038  CB  ILE A 197      83.720  68.171  -2.704  1.00 42.43           C  
ATOM   1039  CG1 ILE A 197      84.855  68.712  -1.811  1.00 40.78           C  
ATOM   1040  CG2 ILE A 197      83.869  66.665  -2.969  1.00 43.32           C  
ATOM   1041  CD1 ILE A 197      84.853  68.178  -0.406  1.00 38.41           C  
ATOM   1042  N   ASP A 198      83.088  67.933  -6.131  1.00 44.52           N  
ATOM   1043  CA  ASP A 198      82.199  67.342  -7.126  1.00 45.19           C  
ATOM   1044  C   ASP A 198      80.978  68.210  -7.444  1.00 44.99           C  
ATOM   1045  O   ASP A 198      79.876  67.698  -7.634  1.00 45.69           O  
ATOM   1046  CB  ASP A 198      81.751  65.955  -6.666  1.00 45.84           C  
ATOM   1047  CG  ASP A 198      82.928  64.998  -6.502  1.00 46.27           C  
ATOM   1048  OD1 ASP A 198      83.906  65.161  -7.199  1.00 45.93           O  
ATOM   1049  OD2 ASP A 198      82.839  64.115  -5.684  1.00 46.48           O  
ATOM   1050  N   GLY A 199      81.179  69.520  -7.531  1.00 44.60           N  
ATOM   1051  CA  GLY A 199      80.098  70.435  -7.879  1.00 44.60           C  
ATOM   1052  C   GLY A 199      79.332  70.986  -6.676  1.00 44.39           C  
ATOM   1053  O   GLY A 199      78.433  71.817  -6.844  1.00 44.62           O  
ATOM   1054  N   TYR A 200      79.668  70.534  -5.474  1.00 43.88           N  
ATOM   1055  CA  TYR A 200      78.975  71.006  -4.283  1.00 44.12           C  
ATOM   1056  C   TYR A 200      79.782  72.059  -3.546  1.00 42.38           C  
ATOM   1057  O   TYR A 200      80.920  71.816  -3.135  1.00 42.08           O  
ATOM   1058  CB  TYR A 200      78.672  69.831  -3.367  1.00 44.06           C  
ATOM   1059  CG  TYR A 200      77.702  68.868  -3.967  1.00 45.43           C  
ATOM   1060  CD1 TYR A 200      78.158  67.891  -4.832  1.00 45.95           C  
ATOM   1061  CD2 TYR A 200      76.361  68.948  -3.661  1.00 46.00           C  
ATOM   1062  CE1 TYR A 200      77.285  67.006  -5.395  1.00 47.41           C  
ATOM   1063  CE2 TYR A 200      75.482  68.050  -4.225  1.00 48.03           C  
ATOM   1064  CZ  TYR A 200      75.944  67.085  -5.092  1.00 49.04           C  
ATOM   1065  OH  TYR A 200      75.072  66.197  -5.651  1.00 50.85           O  
ATOM   1066  N   PHE A 201      79.182  73.232  -3.380  1.00 41.61           N  
ATOM   1067  CA  PHE A 201      79.822  74.349  -2.706  1.00 40.68           C  
ATOM   1068  C   PHE A 201      79.457  74.311  -1.235  1.00 40.42           C  
ATOM   1069  O   PHE A 201      78.316  74.584  -0.852  1.00 40.32           O  
ATOM   1070  CB  PHE A 201      79.368  75.662  -3.338  1.00 40.89           C  
ATOM   1071  CG  PHE A 201      80.097  76.864  -2.875  1.00 39.55           C  
ATOM   1072  CD1 PHE A 201      81.257  77.247  -3.502  1.00 39.78           C  
ATOM   1073  CD2 PHE A 201      79.634  77.619  -1.828  1.00 38.78           C  
ATOM   1074  CE1 PHE A 201      81.945  78.345  -3.101  1.00 39.09           C  
ATOM   1075  CE2 PHE A 201      80.325  78.729  -1.427  1.00 38.25           C  
ATOM   1076  CZ  PHE A 201      81.476  79.085  -2.063  1.00 38.13           C  
ATOM   1077  N   LYS A 202      80.419  73.923  -0.418  1.00 39.42           N  
ATOM   1078  CA  LYS A 202      80.187  73.690   0.994  1.00 39.09           C  
ATOM   1079  C   LYS A 202      80.648  74.867   1.832  1.00 37.65           C  
ATOM   1080  O   LYS A 202      81.789  75.318   1.715  1.00 37.96           O  
ATOM   1081  CB  LYS A 202      80.896  72.401   1.394  1.00 39.00           C  
ATOM   1082  CG  LYS A 202      80.341  71.166   0.666  1.00 40.18           C  
ATOM   1083  CD  LYS A 202      81.135  69.913   0.971  1.00 40.20           C  
ATOM   1084  CE  LYS A 202      80.686  68.726   0.097  1.00 41.27           C  
ATOM   1085  NZ  LYS A 202      79.356  68.158   0.517  1.00 42.23           N  
ATOM   1086  N   ILE A 203      79.750  75.378   2.663  1.00 37.54           N  
ATOM   1087  CA  ILE A 203      80.033  76.541   3.487  1.00 36.97           C  
ATOM   1088  C   ILE A 203      79.980  76.226   4.968  1.00 36.25           C  
ATOM   1089  O   ILE A 203      78.947  75.781   5.482  1.00 37.22           O  
ATOM   1090  CB  ILE A 203      79.017  77.662   3.224  1.00 36.99           C  
ATOM   1091  CG1 ILE A 203      79.041  78.047   1.744  1.00 37.24           C  
ATOM   1092  CG2 ILE A 203      79.329  78.880   4.128  1.00 37.31           C  
ATOM   1093  CD1 ILE A 203      77.915  78.979   1.313  1.00 38.13           C  
ATOM   1094  N   TYR A 204      81.067  76.541   5.658  1.00 35.99           N  
ATOM   1095  CA  TYR A 204      81.162  76.385   7.104  1.00 35.39           C  
ATOM   1096  C   TYR A 204      81.400  77.758   7.663  1.00 34.64           C  
ATOM   1097  O   TYR A 204      81.995  78.591   6.983  1.00 36.19           O  
ATOM   1098  CB  TYR A 204      82.331  75.485   7.495  1.00 35.09           C  
ATOM   1099  CG  TYR A 204      82.345  74.147   6.833  1.00 35.06           C  
ATOM   1100  CD1 TYR A 204      82.711  74.038   5.502  1.00 35.79           C  
ATOM   1101  CD2 TYR A 204      82.029  73.031   7.539  1.00 34.96           C  
ATOM   1102  CE1 TYR A 204      82.742  72.827   4.893  1.00 35.93           C  
ATOM   1103  CE2 TYR A 204      82.063  71.803   6.925  1.00 34.92           C  
ATOM   1104  CZ  TYR A 204      82.417  71.702   5.605  1.00 35.60           C  
ATOM   1105  OH  TYR A 204      82.449  70.475   4.993  1.00 36.49           O  
ATOM   1106  N   SER A 205      80.957  78.024   8.875  1.00 34.44           N  
ATOM   1107  CA  SER A 205      81.263  79.327   9.442  1.00 34.47           C  
ATOM   1108  C   SER A 205      81.123  79.380  10.938  1.00 33.87           C  
ATOM   1109  O   SER A 205      80.452  78.550  11.540  1.00 34.36           O  
ATOM   1110  CB  SER A 205      80.379  80.383   8.833  1.00 34.53           C  
ATOM   1111  OG  SER A 205      79.067  80.195   9.218  1.00 34.66           O  
ATOM   1112  N   LYS A 206      81.729  80.396  11.531  1.00 34.36           N  
ATOM   1113  CA  LYS A 206      81.596  80.651  12.954  1.00 34.49           C  
ATOM   1114  C   LYS A 206      81.688  82.127  13.281  1.00 34.75           C  
ATOM   1115  O   LYS A 206      82.627  82.812  12.874  1.00 34.94           O  
ATOM   1116  CB  LYS A 206      82.668  79.892  13.735  1.00 34.22           C  
ATOM   1117  CG  LYS A 206      82.706  80.169  15.238  1.00 34.37           C  
ATOM   1118  CD  LYS A 206      81.516  79.557  15.951  1.00 34.84           C  
ATOM   1119  CE  LYS A 206      81.584  79.800  17.445  1.00 35.65           C  
ATOM   1120  NZ  LYS A 206      80.371  79.297  18.136  1.00 34.53           N  
ATOM   1121  N   HIS A 207      80.743  82.618  14.064  1.00 35.23           N  
ATOM   1122  CA  HIS A 207      80.792  84.005  14.497  1.00 35.76           C  
ATOM   1123  C   HIS A 207      81.146  84.051  15.970  1.00 35.80           C  
ATOM   1124  O   HIS A 207      80.564  83.321  16.776  1.00 35.50           O  
ATOM   1125  CB  HIS A 207      79.446  84.709  14.291  1.00 35.63           C  
ATOM   1126  CG  HIS A 207      78.961  84.789  12.866  1.00 35.54           C  
ATOM   1127  ND1 HIS A 207      77.783  85.419  12.530  1.00 35.87           N  
ATOM   1128  CD2 HIS A 207      79.478  84.321  11.698  1.00 35.61           C  
ATOM   1129  CE1 HIS A 207      77.595  85.333  11.227  1.00 35.90           C  
ATOM   1130  NE2 HIS A 207      78.606  84.674  10.702  1.00 36.51           N  
ATOM   1131  N   THR A 208      82.087  84.910  16.327  1.00 36.40           N  
ATOM   1132  CA  THR A 208      82.480  85.053  17.721  1.00 37.16           C  
ATOM   1133  C   THR A 208      82.834  86.504  18.029  1.00 37.37           C  
ATOM   1134  O   THR A 208      83.364  87.199  17.164  1.00 37.58           O  
ATOM   1135  CB  THR A 208      83.681  84.129  18.028  1.00 37.10           C  
ATOM   1136  OG1 THR A 208      84.026  84.205  19.418  1.00 37.87           O  
ATOM   1137  CG2 THR A 208      84.883  84.504  17.203  1.00 36.98           C  
ATOM   1138  N   PRO A 209      82.535  87.002  19.235  1.00 37.96           N  
ATOM   1139  CA  PRO A 209      82.925  88.313  19.708  1.00 38.03           C  
ATOM   1140  C   PRO A 209      84.426  88.377  19.916  1.00 38.01           C  
ATOM   1141  O   PRO A 209      85.029  87.412  20.390  1.00 38.24           O  
ATOM   1142  CB  PRO A 209      82.154  88.441  21.028  1.00 38.18           C  
ATOM   1143  CG  PRO A 209      81.909  87.013  21.473  1.00 38.16           C  
ATOM   1144  CD  PRO A 209      81.736  86.221  20.192  1.00 37.72           C  
ATOM   1145  N   ILE A 210      85.011  89.510  19.565  1.00 38.18           N  
ATOM   1146  CA  ILE A 210      86.431  89.763  19.753  1.00 38.57           C  
ATOM   1147  C   ILE A 210      86.690  91.151  20.324  1.00 38.86           C  
ATOM   1148  O   ILE A 210      85.815  92.012  20.298  1.00 38.64           O  
ATOM   1149  CB  ILE A 210      87.213  89.587  18.441  1.00 38.25           C  
ATOM   1150  CG1 ILE A 210      86.704  90.574  17.388  1.00 37.89           C  
ATOM   1151  CG2 ILE A 210      87.056  88.160  17.958  1.00 37.53           C  
ATOM   1152  CD1 ILE A 210      87.582  90.712  16.155  1.00 37.93           C  
ATOM   1153  N   ASN A 211      87.907  91.364  20.811  1.00 38.64           N  
ATOM   1154  CA  ASN A 211      88.360  92.678  21.251  1.00 38.96           C  
ATOM   1155  C   ASN A 211      89.776  92.923  20.749  1.00 38.70           C  
ATOM   1156  O   ASN A 211      90.739  92.834  21.512  1.00 39.16           O  
ATOM   1157  CB  ASN A 211      88.301  92.796  22.765  1.00 39.21           C  
ATOM   1158  CG  ASN A 211      86.899  92.718  23.306  1.00 39.15           C  
ATOM   1159  OD1 ASN A 211      86.155  93.709  23.274  1.00 39.38           O  
ATOM   1160  ND2 ASN A 211      86.526  91.568  23.804  1.00 38.55           N  
ATOM   1161  N   LEU A 212      89.903  93.144  19.446  1.00 38.76           N  
ATOM   1162  CA  LEU A 212      91.217  93.262  18.811  1.00 38.69           C  
ATOM   1163  C   LEU A 212      91.107  93.906  17.438  1.00 38.77           C  
ATOM   1164  O   LEU A 212      90.308  93.480  16.609  1.00 38.26           O  
ATOM   1165  CB  LEU A 212      91.891  91.881  18.704  1.00 38.63           C  
ATOM   1166  CG  LEU A 212      93.301  91.831  18.022  1.00 37.84           C  
ATOM   1167  CD1 LEU A 212      94.325  92.613  18.856  1.00 38.42           C  
ATOM   1168  CD2 LEU A 212      93.736  90.369  17.890  1.00 36.96           C  
ATOM   1169  N   VAL A 213      91.891  94.948  17.194  1.00 38.38           N  
ATOM   1170  CA  VAL A 213      91.815  95.633  15.907  1.00 38.70           C  
ATOM   1171  C   VAL A 213      92.941  95.271  14.943  1.00 38.08           C  
ATOM   1172  O   VAL A 213      92.751  95.261  13.730  1.00 37.91           O  
ATOM   1173  CB  VAL A 213      91.752  97.161  16.122  1.00 38.76           C  
ATOM   1174  CG1 VAL A 213      93.101  97.724  16.584  1.00 39.31           C  
ATOM   1175  CG2 VAL A 213      91.303  97.827  14.822  1.00 38.73           C  
ATOM   1176  N   ARG A 214      94.130  95.048  15.472  1.00 37.93           N  
ATOM   1177  CA  ARG A 214      95.309  94.894  14.634  1.00 37.28           C  
ATOM   1178  C   ARG A 214      95.332  93.671  13.726  1.00 36.67           C  
ATOM   1179  O   ARG A 214      95.800  93.768  12.597  1.00 36.32           O  
ATOM   1180  CB  ARG A 214      96.555  94.851  15.496  1.00 37.27           C  
ATOM   1181  CG  ARG A 214      97.864  94.819  14.721  1.00 36.85           C  
ATOM   1182  CD  ARG A 214      99.041  94.869  15.618  1.00 36.82           C  
ATOM   1183  NE  ARG A 214      99.118  93.688  16.481  1.00 36.38           N  
ATOM   1184  CZ  ARG A 214      98.880  93.661  17.815  1.00 37.47           C  
ATOM   1185  NH1 ARG A 214      98.549  94.758  18.466  1.00 38.09           N  
ATOM   1186  NH2 ARG A 214      98.982  92.518  18.470  1.00 37.55           N  
ATOM   1187  N   ASP A 215      94.919  92.514  14.228  1.00 36.81           N  
ATOM   1188  CA  ASP A 215      95.112  91.274  13.480  1.00 36.28           C  
ATOM   1189  C   ASP A 215      94.131  90.181  13.912  1.00 36.00           C  
ATOM   1190  O   ASP A 215      93.264  90.424  14.749  1.00 36.55           O  
ATOM   1191  CB  ASP A 215      96.560  90.811  13.672  1.00 35.89           C  
ATOM   1192  CG  ASP A 215      97.112  90.051  12.496  1.00 35.62           C  
ATOM   1193  OD1 ASP A 215      96.324  89.573  11.715  1.00 35.39           O  
ATOM   1194  OD2 ASP A 215      98.312  89.957  12.375  1.00 35.67           O  
ATOM   1195  N   LEU A 216      94.237  88.993  13.309  1.00 35.99           N  
ATOM   1196  CA  LEU A 216      93.421  87.855  13.736  1.00 36.02           C  
ATOM   1197  C   LEU A 216      93.774  87.487  15.170  1.00 35.79           C  
ATOM   1198  O   LEU A 216      94.956  87.366  15.490  1.00 35.48           O  
ATOM   1199  CB  LEU A 216      93.682  86.597  12.882  1.00 36.10           C  
ATOM   1200  CG  LEU A 216      93.152  86.573  11.447  1.00 35.59           C  
ATOM   1201  CD1 LEU A 216      93.690  85.330  10.733  1.00 35.26           C  
ATOM   1202  CD2 LEU A 216      91.614  86.550  11.461  1.00 36.39           C  
ATOM   1203  N   PRO A 217      92.794  87.297  16.056  1.00 35.81           N  
ATOM   1204  CA  PRO A 217      92.986  86.809  17.400  1.00 35.43           C  
ATOM   1205  C   PRO A 217      93.552  85.404  17.360  1.00 35.06           C  
ATOM   1206  O   PRO A 217      93.168  84.603  16.504  1.00 34.91           O  
ATOM   1207  CB  PRO A 217      91.565  86.815  17.976  1.00 35.58           C  
ATOM   1208  CG  PRO A 217      90.801  87.795  17.124  1.00 36.18           C  
ATOM   1209  CD  PRO A 217      91.420  87.694  15.743  1.00 35.97           C  
ATOM   1210  N   GLN A 218      94.416  85.095  18.313  1.00 34.64           N  
ATOM   1211  CA  GLN A 218      94.961  83.755  18.451  1.00 34.53           C  
ATOM   1212  C   GLN A 218      94.051  82.929  19.337  1.00 34.87           C  
ATOM   1213  O   GLN A 218      93.553  83.420  20.348  1.00 34.64           O  
ATOM   1214  CB  GLN A 218      96.374  83.798  19.025  1.00 34.19           C  
ATOM   1215  CG  GLN A 218      97.030  82.442  19.155  1.00 34.24           C  
ATOM   1216  CD  GLN A 218      98.464  82.549  19.585  1.00 33.99           C  
ATOM   1217  OE1 GLN A 218      98.972  83.648  19.827  1.00 33.73           O  
ATOM   1218  NE2 GLN A 218      99.136  81.411  19.691  1.00 33.31           N  
ATOM   1219  N   GLY A 219      93.826  81.681  18.960  1.00 34.96           N  
ATOM   1220  CA  GLY A 219      92.977  80.798  19.742  1.00 35.05           C  
ATOM   1221  C   GLY A 219      92.387  79.725  18.852  1.00 34.53           C  
ATOM   1222  O   GLY A 219      92.730  79.632  17.674  1.00 33.67           O  
ATOM   1223  N   PHE A 220      91.509  78.904  19.411  1.00 34.33           N  
ATOM   1224  CA  PHE A 220      90.918  77.827  18.637  1.00 33.12           C  
ATOM   1225  C   PHE A 220      89.405  77.836  18.730  1.00 32.77           C  
ATOM   1226  O   PHE A 220      88.835  77.959  19.814  1.00 33.24           O  
ATOM   1227  CB  PHE A 220      91.425  76.469  19.114  1.00 33.10           C  
ATOM   1228  CG  PHE A 220      90.880  75.356  18.303  1.00 32.06           C  
ATOM   1229  CD1 PHE A 220      91.506  74.964  17.146  1.00 31.79           C  
ATOM   1230  CD2 PHE A 220      89.729  74.714  18.679  1.00 31.54           C  
ATOM   1231  CE1 PHE A 220      90.995  73.951  16.391  1.00 30.76           C  
ATOM   1232  CE2 PHE A 220      89.215  73.707  17.921  1.00 31.25           C  
ATOM   1233  CZ  PHE A 220      89.848  73.321  16.775  1.00 30.99           C  
ATOM   1234  N   SER A 221      88.763  77.693  17.583  1.00 32.57           N  
ATOM   1235  CA  SER A 221      87.318  77.588  17.508  1.00 32.60           C  
ATOM   1236  C   SER A 221      86.958  76.818  16.254  1.00 32.23           C  
ATOM   1237  O   SER A 221      87.436  77.148  15.170  1.00 32.18           O  
ATOM   1238  CB  SER A 221      86.690  78.965  17.491  1.00 32.14           C  
ATOM   1239  OG  SER A 221      85.299  78.881  17.441  1.00 32.85           O  
ATOM   1240  N   ALA A 222      86.148  75.776  16.395  1.00 32.38           N  
ATOM   1241  CA  ALA A 222      85.777  74.970  15.239  1.00 32.48           C  
ATOM   1242  C   ALA A 222      84.542  75.530  14.555  1.00 33.09           C  
ATOM   1243  O   ALA A 222      83.632  76.042  15.209  1.00 33.37           O  
ATOM   1244  CB  ALA A 222      85.556  73.530  15.645  1.00 31.86           C  
ATOM   1245  N   LEU A 223      84.514  75.399  13.235  1.00 33.03           N  
ATOM   1246  CA  LEU A 223      83.415  75.892  12.411  1.00 33.31           C  
ATOM   1247  C   LEU A 223      82.430  74.810  11.978  1.00 33.73           C  
ATOM   1248  O   LEU A 223      82.807  73.819  11.346  1.00 33.99           O  
ATOM   1249  CB  LEU A 223      83.994  76.522  11.138  1.00 33.87           C  
ATOM   1250  CG  LEU A 223      84.525  77.972  11.211  1.00 33.95           C  
ATOM   1251  CD1 LEU A 223      85.596  78.118  12.281  1.00 34.05           C  
ATOM   1252  CD2 LEU A 223      85.095  78.329   9.862  1.00 34.20           C  
ATOM   1253  N   GLU A 224      81.152  75.016  12.286  1.00 33.75           N  
ATOM   1254  CA  GLU A 224      80.111  74.097  11.844  1.00 33.60           C  
ATOM   1255  C   GLU A 224      79.692  74.404  10.409  1.00 34.26           C  
ATOM   1256  O   GLU A 224      79.802  75.554   9.985  1.00 34.91           O  
ATOM   1257  CB  GLU A 224      78.891  74.188  12.767  1.00 33.86           C  
ATOM   1258  CG  GLU A 224      78.093  75.489  12.715  1.00 33.55           C  
ATOM   1259  CD  GLU A 224      78.647  76.547  13.618  1.00 32.57           C  
ATOM   1260  OE1 GLU A 224      79.733  76.352  14.103  1.00 33.38           O  
ATOM   1261  OE2 GLU A 224      77.981  77.534  13.851  1.00 31.51           O  
ATOM   1262  N   PRO A 225      79.224  73.411   9.642  1.00 34.61           N  
ATOM   1263  CA  PRO A 225      78.633  73.564   8.328  1.00 35.23           C  
ATOM   1264  C   PRO A 225      77.288  74.235   8.428  1.00 35.21           C  
ATOM   1265  O   PRO A 225      76.530  73.961   9.357  1.00 35.04           O  
ATOM   1266  CB  PRO A 225      78.500  72.121   7.840  1.00 35.69           C  
ATOM   1267  CG  PRO A 225      78.445  71.298   9.098  1.00 34.78           C  
ATOM   1268  CD  PRO A 225      79.318  72.030  10.096  1.00 34.43           C  
ATOM   1269  N   LEU A 226      76.958  75.062   7.449  1.00 35.57           N  
ATOM   1270  CA  LEU A 226      75.632  75.655   7.400  1.00 35.74           C  
ATOM   1271  C   LEU A 226      74.924  75.388   6.083  1.00 36.14           C  
ATOM   1272  O   LEU A 226      73.713  75.163   6.055  1.00 36.74           O  
ATOM   1273  CB  LEU A 226      75.695  77.169   7.614  1.00 35.99           C  
ATOM   1274  CG  LEU A 226      76.268  77.669   8.949  1.00 35.43           C  
ATOM   1275  CD1 LEU A 226      76.273  79.179   8.918  1.00 35.12           C  
ATOM   1276  CD2 LEU A 226      75.440  77.163  10.122  1.00 34.46           C  
ATOM   1277  N   VAL A 227      75.661  75.490   4.987  1.00 36.72           N  
ATOM   1278  CA  VAL A 227      75.050  75.437   3.666  1.00 37.46           C  
ATOM   1279  C   VAL A 227      75.806  74.522   2.714  1.00 38.17           C  
ATOM   1280  O   VAL A 227      77.031  74.424   2.774  1.00 38.10           O  
ATOM   1281  CB  VAL A 227      74.954  76.862   3.077  1.00 36.82           C  
ATOM   1282  CG1 VAL A 227      74.358  76.835   1.689  1.00 38.73           C  
ATOM   1283  CG2 VAL A 227      74.113  77.743   3.982  1.00 37.05           C  
ATOM   1284  N   ASP A 228      75.077  73.849   1.832  1.00 39.60           N  
ATOM   1285  CA  ASP A 228      75.686  73.031   0.791  1.00 40.52           C  
ATOM   1286  C   ASP A 228      74.913  73.226  -0.514  1.00 41.46           C  
ATOM   1287  O   ASP A 228      73.776  72.773  -0.643  1.00 41.94           O  
ATOM   1288  CB  ASP A 228      75.714  71.563   1.214  1.00 40.93           C  
ATOM   1289  CG  ASP A 228      76.451  70.662   0.240  1.00 41.61           C  
ATOM   1290  OD1 ASP A 228      76.554  71.013  -0.902  1.00 42.50           O  
ATOM   1291  OD2 ASP A 228      76.941  69.631   0.665  1.00 42.73           O  
ATOM   1292  N   LEU A 229      75.500  73.986  -1.441  1.00 41.98           N  
ATOM   1293  CA  LEU A 229      74.808  74.358  -2.671  1.00 43.26           C  
ATOM   1294  C   LEU A 229      75.275  73.530  -3.878  1.00 43.85           C  
ATOM   1295  O   LEU A 229      76.434  73.635  -4.291  1.00 43.90           O  
ATOM   1296  CB  LEU A 229      75.049  75.841  -2.992  1.00 43.11           C  
ATOM   1297  CG  LEU A 229      74.743  76.858  -1.906  1.00 41.88           C  
ATOM   1298  CD1 LEU A 229      75.176  78.233  -2.393  1.00 42.41           C  
ATOM   1299  CD2 LEU A 229      73.249  76.849  -1.579  1.00 42.38           C  
ATOM   1300  N   PRO A 230      74.396  72.742  -4.508  1.00 44.95           N  
ATOM   1301  CA  PRO A 230      74.674  71.890  -5.651  1.00 45.65           C  
ATOM   1302  C   PRO A 230      74.688  72.720  -6.919  1.00 45.16           C  
ATOM   1303  O   PRO A 230      73.823  72.559  -7.780  1.00 45.08           O  
ATOM   1304  CB  PRO A 230      73.492  70.929  -5.625  1.00 48.11           C  
ATOM   1305  CG  PRO A 230      72.355  71.769  -5.082  1.00 47.81           C  
ATOM   1306  CD  PRO A 230      72.999  72.694  -4.058  1.00 45.71           C  
ATOM   1307  N   ILE A 231      75.635  73.640  -6.994  1.00 44.97           N  
ATOM   1308  CA  ILE A 231      75.685  74.608  -8.081  1.00 45.10           C  
ATOM   1309  C   ILE A 231      76.315  74.051  -9.353  1.00 45.05           C  
ATOM   1310  O   ILE A 231      75.927  74.442 -10.455  1.00 44.77           O  
ATOM   1311  CB  ILE A 231      76.354  75.916  -7.591  1.00 44.90           C  
ATOM   1312  CG1 ILE A 231      77.836  75.692  -7.177  1.00 44.67           C  
ATOM   1313  CG2 ILE A 231      75.560  76.436  -6.428  1.00 44.19           C  
ATOM   1314  CD1 ILE A 231      78.592  76.959  -6.762  1.00 43.84           C  
ATOM   1315  N   GLY A 232      77.292  73.161  -9.226  1.00 44.83           N  
ATOM   1316  CA  GLY A 232      77.902  72.568 -10.407  1.00 44.56           C  
ATOM   1317  C   GLY A 232      78.755  73.574 -11.169  1.00 44.31           C  
ATOM   1318  O   GLY A 232      78.936  73.450 -12.380  1.00 43.98           O  
ATOM   1319  N   ILE A 233      79.258  74.572 -10.460  1.00 44.72           N  
ATOM   1320  CA  ILE A 233      80.046  75.632 -11.071  1.00 44.89           C  
ATOM   1321  C   ILE A 233      81.537  75.388 -10.865  1.00 44.61           C  
ATOM   1322  O   ILE A 233      81.969  75.074  -9.754  1.00 44.66           O  
ATOM   1323  CB  ILE A 233      79.655  77.033 -10.526  1.00 45.26           C  
ATOM   1324  CG1 ILE A 233      78.184  77.335 -10.900  1.00 45.15           C  
ATOM   1325  CG2 ILE A 233      80.590  78.115 -11.087  1.00 45.12           C  
ATOM   1326  CD1 ILE A 233      77.606  78.620 -10.292  1.00 44.31           C  
ATOM   1327  N   ASN A 234      82.314  75.534 -11.938  1.00 45.19           N  
ATOM   1328  CA  ASN A 234      83.772  75.416 -11.908  1.00 45.24           C  
ATOM   1329  C   ASN A 234      84.350  76.739 -11.398  1.00 44.64           C  
ATOM   1330  O   ASN A 234      84.331  77.746 -12.117  1.00 44.63           O  
ATOM   1331  CB  ASN A 234      84.301  75.045 -13.290  1.00 46.28           C  
ATOM   1332  CG  ASN A 234      85.836  75.005 -13.392  1.00 47.63           C  
ATOM   1333  OD1 ASN A 234      86.533  74.647 -12.423  1.00 47.13           O  
ATOM   1334  ND2 ASN A 234      86.340  75.370 -14.561  1.00 48.72           N  
ATOM   1335  N   ILE A 235      84.806  76.756 -10.144  1.00 44.62           N  
ATOM   1336  CA  ILE A 235      85.307  77.949  -9.458  1.00 44.57           C  
ATOM   1337  C   ILE A 235      86.816  77.921  -9.340  1.00 43.65           C  
ATOM   1338  O   ILE A 235      87.387  76.978  -8.797  1.00 43.53           O  
ATOM   1339  CB  ILE A 235      84.648  78.081  -8.070  1.00 42.94           C  
ATOM   1340  CG1 ILE A 235      83.137  78.275  -8.262  1.00 43.48           C  
ATOM   1341  CG2 ILE A 235      85.272  79.237  -7.299  1.00 42.43           C  
ATOM   1342  CD1 ILE A 235      82.296  78.098  -7.031  1.00 42.47           C  
ATOM   1343  N   THR A 236      87.453  78.951  -9.887  1.00 43.43           N  
ATOM   1344  CA  THR A 236      88.901  79.046  -9.899  1.00 43.08           C  
ATOM   1345  C   THR A 236      89.351  80.349  -9.268  1.00 42.11           C  
ATOM   1346  O   THR A 236      90.505  80.478  -8.855  1.00 41.43           O  
ATOM   1347  CB  THR A 236      89.449  78.937 -11.332  1.00 44.34           C  
ATOM   1348  OG1 THR A 236      88.977  80.037 -12.113  1.00 44.14           O  
ATOM   1349  CG2 THR A 236      88.970  77.646 -11.960  1.00 45.71           C  
ATOM   1350  N   ARG A 237      88.438  81.317  -9.208  1.00 41.72           N  
ATOM   1351  CA  ARG A 237      88.710  82.645  -8.680  1.00 40.86           C  
ATOM   1352  C   ARG A 237      87.547  83.140  -7.841  1.00 40.35           C  
ATOM   1353  O   ARG A 237      86.402  82.755  -8.073  1.00 42.75           O  
ATOM   1354  CB  ARG A 237      88.934  83.634  -9.809  1.00 42.03           C  
ATOM   1355  CG  ARG A 237      90.143  83.359 -10.687  1.00 42.21           C  
ATOM   1356  CD  ARG A 237      90.339  84.421 -11.709  1.00 43.60           C  
ATOM   1357  NE  ARG A 237      91.520  84.178 -12.516  1.00 44.00           N  
ATOM   1358  CZ  ARG A 237      91.548  83.480 -13.673  1.00 44.88           C  
ATOM   1359  NH1 ARG A 237      90.444  82.967 -14.184  1.00 44.35           N  
ATOM   1360  NH2 ARG A 237      92.701  83.314 -14.306  1.00 44.46           N  
ATOM   1361  N   PHE A 238      87.816  84.060  -6.928  1.00 40.02           N  
ATOM   1362  CA  PHE A 238      86.727  84.666  -6.192  1.00 39.62           C  
ATOM   1363  C   PHE A 238      87.051  86.105  -5.819  1.00 39.41           C  
ATOM   1364  O   PHE A 238      88.202  86.534  -5.862  1.00 40.49           O  
ATOM   1365  CB  PHE A 238      86.410  83.859  -4.942  1.00 39.89           C  
ATOM   1366  CG  PHE A 238      87.376  84.005  -3.850  1.00 39.37           C  
ATOM   1367  CD1 PHE A 238      87.083  84.867  -2.808  1.00 39.53           C  
ATOM   1368  CD2 PHE A 238      88.571  83.321  -3.841  1.00 39.24           C  
ATOM   1369  CE1 PHE A 238      87.959  85.038  -1.779  1.00 39.59           C  
ATOM   1370  CE2 PHE A 238      89.447  83.497  -2.811  1.00 38.91           C  
ATOM   1371  CZ  PHE A 238      89.137  84.356  -1.781  1.00 39.41           C  
ATOM   1372  N   GLN A 239      86.030  86.853  -5.445  1.00 39.32           N  
ATOM   1373  CA  GLN A 239      86.199  88.246  -5.060  1.00 39.67           C  
ATOM   1374  C   GLN A 239      85.270  88.597  -3.910  1.00 39.11           C  
ATOM   1375  O   GLN A 239      84.216  87.987  -3.763  1.00 39.97           O  
ATOM   1376  CB  GLN A 239      85.935  89.120  -6.279  1.00 40.08           C  
ATOM   1377  CG  GLN A 239      86.237  90.573  -6.123  1.00 39.94           C  
ATOM   1378  CD  GLN A 239      86.193  91.258  -7.454  1.00 40.86           C  
ATOM   1379  OE1 GLN A 239      85.423  90.870  -8.338  1.00 43.29           O  
ATOM   1380  NE2 GLN A 239      87.021  92.270  -7.627  1.00 40.31           N  
ATOM   1381  N   THR A 240      85.633  89.562  -3.075  1.00 39.51           N  
ATOM   1382  CA  THR A 240      84.717  89.944  -2.005  1.00 39.88           C  
ATOM   1383  C   THR A 240      83.939  91.205  -2.357  1.00 40.34           C  
ATOM   1384  O   THR A 240      84.266  91.899  -3.320  1.00 40.43           O  
ATOM   1385  CB  THR A 240      85.460  90.176  -0.678  1.00 39.48           C  
ATOM   1386  OG1 THR A 240      84.515  90.279   0.386  1.00 39.48           O  
ATOM   1387  CG2 THR A 240      86.256  91.465  -0.734  1.00 38.92           C  
ATOM   1388  N   LEU A 241      82.932  91.508  -1.540  1.00 40.23           N  
ATOM   1389  CA  LEU A 241      82.085  92.687  -1.691  1.00 40.72           C  
ATOM   1390  C   LEU A 241      82.035  93.529  -0.420  1.00 40.65           C  
ATOM   1391  O   LEU A 241      81.604  93.060   0.642  1.00 40.38           O  
ATOM   1392  CB  LEU A 241      80.664  92.246  -2.070  1.00 40.99           C  
ATOM   1393  CG  LEU A 241      80.512  91.569  -3.443  1.00 41.22           C  
ATOM   1394  CD1 LEU A 241      79.185  90.854  -3.519  1.00 41.27           C  
ATOM   1395  CD2 LEU A 241      80.575  92.640  -4.519  1.00 42.30           C  
ATOM   1396  N   LEU A 242      82.463  94.782  -0.552  1.00 41.01           N  
ATOM   1397  CA  LEU A 242      82.540  95.717   0.566  1.00 40.75           C  
ATOM   1398  C   LEU A 242      81.477  96.810   0.478  1.00 41.46           C  
ATOM   1399  O   LEU A 242      81.157  97.277  -0.619  1.00 41.44           O  
ATOM   1400  CB  LEU A 242      83.931  96.371   0.569  1.00 40.85           C  
ATOM   1401  CG  LEU A 242      85.148  95.400   0.555  1.00 40.02           C  
ATOM   1402  CD1 LEU A 242      86.443  96.196   0.479  1.00 39.21           C  
ATOM   1403  CD2 LEU A 242      85.129  94.547   1.785  1.00 39.77           C  
ATOM   1404  N   ALA A 243      80.973  97.238   1.643  1.00 41.01           N  
ATOM   1405  CA  ALA A 243      80.018  98.333   1.782  1.00 41.43           C  
ATOM   1406  C   ALA A 243      80.735  99.662   1.982  1.00 41.07           C  
ATOM   1407  O   ALA A 243      81.426  99.863   2.982  1.00 40.77           O  
ATOM   1408  CB  ALA A 243      79.090  98.073   2.945  1.00 40.79           C  
ATOM   1409  N   LEU A 244      80.585 100.571   1.031  1.00 41.53           N  
ATOM   1410  CA  LEU A 244      81.324 101.823   1.079  1.00 42.17           C  
ATOM   1411  C   LEU A 244      80.431 103.028   1.384  1.00 42.22           C  
ATOM   1412  O   LEU A 244      79.370 103.194   0.774  1.00 41.95           O  
ATOM   1413  CB  LEU A 244      81.997 102.048  -0.275  1.00 41.57           C  
ATOM   1414  CG  LEU A 244      82.790 100.858  -0.839  1.00 41.71           C  
ATOM   1415  CD1 LEU A 244      83.374 101.266  -2.176  1.00 42.27           C  
ATOM   1416  CD2 LEU A 244      83.884 100.418   0.142  1.00 41.74           C  
ATOM   1417  N   HIS A 245      80.893 103.909   2.286  1.00 42.25           N  
ATOM   1418  CA  HIS A 245      80.174 105.131   2.661  1.00 42.36           C  
ATOM   1419  C   HIS A 245      80.413 106.233   1.625  1.00 43.18           C  
ATOM   1420  O   HIS A 245      79.658 107.205   1.543  1.00 44.06           O  
ATOM   1421  CB  HIS A 245      80.602 105.620   4.069  1.00 42.38           C  
ATOM   1422  CG  HIS A 245      80.157 104.724   5.233  1.00 42.05           C  
ATOM   1423  ND1 HIS A 245      78.875 104.753   5.739  1.00 42.09           N  
ATOM   1424  CD2 HIS A 245      80.831 103.800   5.969  1.00 41.70           C  
ATOM   1425  CE1 HIS A 245      78.780 103.888   6.738  1.00 41.40           C  
ATOM   1426  NE2 HIS A 245      79.952 103.299   6.897  1.00 40.66           N  
ATOM   1427  N   ALA A 263      87.694  97.290   8.070  1.00 36.69           N  
ATOM   1428  CA  ALA A 263      87.237  95.905   8.018  1.00 36.87           C  
ATOM   1429  C   ALA A 263      88.185  95.070   7.153  1.00 36.84           C  
ATOM   1430  O   ALA A 263      87.922  94.807   5.972  1.00 36.99           O  
ATOM   1431  CB  ALA A 263      85.802  95.825   7.498  1.00 37.87           C  
ATOM   1432  N   ALA A 264      89.280  94.627   7.775  1.00 36.39           N  
ATOM   1433  CA  ALA A 264      90.284  93.760   7.176  1.00 36.27           C  
ATOM   1434  C   ALA A 264      89.750  92.348   7.012  1.00 35.70           C  
ATOM   1435  O   ALA A 264      88.869  91.910   7.756  1.00 36.60           O  
ATOM   1436  CB  ALA A 264      91.527  93.736   8.040  1.00 36.35           C  
ATOM   1437  N   TYR A 265      90.303  91.636   6.055  1.00 35.76           N  
ATOM   1438  CA  TYR A 265      89.935  90.247   5.867  1.00 34.82           C  
ATOM   1439  C   TYR A 265      91.127  89.436   5.441  1.00 38.39           C  
ATOM   1440  O   TYR A 265      92.139  89.976   5.000  1.00 34.31           O  
ATOM   1441  CB  TYR A 265      88.773  90.094   4.898  1.00 35.68           C  
ATOM   1442  CG  TYR A 265      89.038  90.463   3.493  1.00 36.00           C  
ATOM   1443  CD1 TYR A 265      89.455  89.504   2.599  1.00 35.96           C  
ATOM   1444  CD2 TYR A 265      88.845  91.758   3.084  1.00 36.53           C  
ATOM   1445  CE1 TYR A 265      89.677  89.840   1.293  1.00 36.76           C  
ATOM   1446  CE2 TYR A 265      89.072  92.094   1.778  1.00 36.86           C  
ATOM   1447  CZ  TYR A 265      89.485  91.139   0.888  1.00 37.07           C  
ATOM   1448  OH  TYR A 265      89.720  91.481  -0.405  1.00 37.16           O  
ATOM   1449  N   TYR A 266      91.026  88.136   5.614  1.00 35.18           N  
ATOM   1450  CA  TYR A 266      92.137  87.257   5.364  1.00 34.77           C  
ATOM   1451  C   TYR A 266      91.760  86.135   4.433  1.00 34.00           C  
ATOM   1452  O   TYR A 266      90.674  85.573   4.532  1.00 36.00           O  
ATOM   1453  CB  TYR A 266      92.596  86.699   6.704  1.00 34.67           C  
ATOM   1454  CG  TYR A 266      92.884  87.789   7.695  1.00 34.62           C  
ATOM   1455  CD1 TYR A 266      91.844  88.339   8.427  1.00 35.15           C  
ATOM   1456  CD2 TYR A 266      94.155  88.249   7.874  1.00 35.10           C  
ATOM   1457  CE1 TYR A 266      92.079  89.343   9.321  1.00 35.36           C  
ATOM   1458  CE2 TYR A 266      94.391  89.253   8.779  1.00 35.01           C  
ATOM   1459  CZ  TYR A 266      93.357  89.800   9.494  1.00 35.44           C  
ATOM   1460  OH  TYR A 266      93.605  90.802  10.386  1.00 35.86           O  
ATOM   1461  N   VAL A 267      92.670  85.778   3.553  1.00 34.50           N  
ATOM   1462  CA  VAL A 267      92.442  84.655   2.662  1.00 34.43           C  
ATOM   1463  C   VAL A 267      93.532  83.608   2.772  1.00 33.85           C  
ATOM   1464  O   VAL A 267      94.705  83.885   2.510  1.00 33.90           O  
ATOM   1465  CB  VAL A 267      92.360  85.137   1.205  1.00 35.39           C  
ATOM   1466  CG1 VAL A 267      92.191  83.956   0.259  1.00 35.97           C  
ATOM   1467  CG2 VAL A 267      91.186  86.107   1.063  1.00 35.94           C  
ATOM   1468  N   GLY A 268      93.141  82.397   3.123  1.00 34.04           N  
ATOM   1469  CA  GLY A 268      94.081  81.300   3.221  1.00 33.82           C  
ATOM   1470  C   GLY A 268      93.657  80.205   2.281  1.00 33.98           C  
ATOM   1471  O   GLY A 268      92.594  80.285   1.677  1.00 35.26           O  
ATOM   1472  N   TYR A 269      94.459  79.167   2.167  1.00 34.24           N  
ATOM   1473  CA  TYR A 269      94.082  78.079   1.287  1.00 34.30           C  
ATOM   1474  C   TYR A 269      94.165  76.752   1.987  1.00 33.72           C  
ATOM   1475  O   TYR A 269      95.045  76.527   2.819  1.00 33.05           O  
ATOM   1476  CB  TYR A 269      94.916  78.114   0.022  1.00 34.16           C  
ATOM   1477  CG  TYR A 269      94.650  79.364  -0.735  1.00 34.71           C  
ATOM   1478  CD1 TYR A 269      95.437  80.478  -0.544  1.00 34.37           C  
ATOM   1479  CD2 TYR A 269      93.590  79.410  -1.595  1.00 35.94           C  
ATOM   1480  CE1 TYR A 269      95.158  81.637  -1.225  1.00 34.65           C  
ATOM   1481  CE2 TYR A 269      93.314  80.555  -2.271  1.00 36.45           C  
ATOM   1482  CZ  TYR A 269      94.089  81.673  -2.090  1.00 35.85           C  
ATOM   1483  OH  TYR A 269      93.807  82.830  -2.769  1.00 36.85           O  
ATOM   1484  N   LEU A 270      93.252  75.874   1.629  1.00 34.30           N  
ATOM   1485  CA  LEU A 270      93.135  74.588   2.274  1.00 33.52           C  
ATOM   1486  C   LEU A 270      94.002  73.543   1.597  1.00 33.22           C  
ATOM   1487  O   LEU A 270      94.235  73.601   0.389  1.00 33.39           O  
ATOM   1488  CB  LEU A 270      91.681  74.151   2.220  1.00 34.11           C  
ATOM   1489  CG  LEU A 270      90.640  75.164   2.734  1.00 34.61           C  
ATOM   1490  CD1 LEU A 270      89.270  74.585   2.507  1.00 35.23           C  
ATOM   1491  CD2 LEU A 270      90.858  75.480   4.198  1.00 34.44           C  
ATOM   1492  N   GLN A 271      94.472  72.581   2.380  1.00 32.98           N  
ATOM   1493  CA  GLN A 271      95.271  71.472   1.880  1.00 32.47           C  
ATOM   1494  C   GLN A 271      94.755  70.167   2.467  1.00 31.99           C  
ATOM   1495  O   GLN A 271      94.231  70.171   3.581  1.00 31.98           O  
ATOM   1496  CB  GLN A 271      96.743  71.672   2.253  1.00 31.73           C  
ATOM   1497  CG  GLN A 271      97.406  72.850   1.588  1.00 32.61           C  
ATOM   1498  CD  GLN A 271      98.876  72.953   1.943  1.00 31.59           C  
ATOM   1499  OE1 GLN A 271      99.453  72.057   2.581  1.00 30.74           O  
ATOM   1500  NE2 GLN A 271      99.495  74.050   1.534  1.00 31.17           N  
ATOM   1501  N   PRO A 272      94.942  69.028   1.787  1.00 31.92           N  
ATOM   1502  CA  PRO A 272      94.526  67.697   2.210  1.00 31.34           C  
ATOM   1503  C   PRO A 272      95.413  67.135   3.312  1.00 31.04           C  
ATOM   1504  O   PRO A 272      96.064  66.099   3.153  1.00 31.27           O  
ATOM   1505  CB  PRO A 272      94.644  66.903   0.908  1.00 31.46           C  
ATOM   1506  CG  PRO A 272      95.768  67.580   0.162  1.00 31.35           C  
ATOM   1507  CD  PRO A 272      95.590  69.060   0.464  1.00 31.65           C  
ATOM   1508  N   ARG A 273      95.413  67.828   4.437  1.00 30.94           N  
ATOM   1509  CA  ARG A 273      96.173  67.457   5.608  1.00 30.59           C  
ATOM   1510  C   ARG A 273      95.390  66.513   6.488  1.00 30.24           C  
ATOM   1511  O   ARG A 273      94.156  66.527   6.499  1.00 30.62           O  
ATOM   1512  CB  ARG A 273      96.521  68.678   6.435  1.00 30.27           C  
ATOM   1513  CG  ARG A 273      97.345  69.732   5.758  1.00 30.68           C  
ATOM   1514  CD  ARG A 273      98.689  69.242   5.431  1.00 30.11           C  
ATOM   1515  NE  ARG A 273      99.528  70.286   4.906  1.00 30.07           N  
ATOM   1516  CZ  ARG A 273     100.395  71.037   5.618  1.00 29.28           C  
ATOM   1517  NH1 ARG A 273     100.560  70.885   6.928  1.00 28.33           N  
ATOM   1518  NH2 ARG A 273     101.091  71.953   4.973  1.00 29.82           N  
ATOM   1519  N   THR A 274      96.105  65.715   7.259  1.00 29.74           N  
ATOM   1520  CA  THR A 274      95.459  64.877   8.243  1.00 29.66           C  
ATOM   1521  C   THR A 274      95.489  65.584   9.574  1.00 29.32           C  
ATOM   1522  O   THR A 274      96.533  66.085   9.996  1.00 29.32           O  
ATOM   1523  CB  THR A 274      96.127  63.500   8.358  1.00 29.84           C  
ATOM   1524  OG1 THR A 274      96.050  62.829   7.098  1.00 29.79           O  
ATOM   1525  CG2 THR A 274      95.407  62.664   9.408  1.00 29.47           C  
ATOM   1526  N   PHE A 275      94.338  65.657  10.209  1.00 29.38           N  
ATOM   1527  CA  PHE A 275      94.217  66.253  11.521  1.00 29.14           C  
ATOM   1528  C   PHE A 275      93.702  65.298  12.565  1.00 29.07           C  
ATOM   1529  O   PHE A 275      92.807  64.489  12.312  1.00 29.47           O  
ATOM   1530  CB  PHE A 275      93.301  67.474  11.489  1.00 29.62           C  
ATOM   1531  CG  PHE A 275      93.946  68.724  11.024  1.00 29.72           C  
ATOM   1532  CD1 PHE A 275      94.278  68.961   9.710  1.00 29.95           C  
ATOM   1533  CD2 PHE A 275      94.208  69.700  11.946  1.00 29.71           C  
ATOM   1534  CE1 PHE A 275      94.872  70.160   9.359  1.00 29.93           C  
ATOM   1535  CE2 PHE A 275      94.783  70.871  11.595  1.00 30.00           C  
ATOM   1536  CZ  PHE A 275      95.117  71.109  10.301  1.00 30.03           C  
ATOM   1537  N   LEU A 276      94.229  65.440  13.768  1.00 28.74           N  
ATOM   1538  CA  LEU A 276      93.690  64.723  14.909  1.00 28.56           C  
ATOM   1539  C   LEU A 276      92.797  65.703  15.646  1.00 28.57           C  
ATOM   1540  O   LEU A 276      93.268  66.729  16.132  1.00 28.89           O  
ATOM   1541  CB  LEU A 276      94.818  64.217  15.819  1.00 28.27           C  
ATOM   1542  CG  LEU A 276      94.413  63.401  17.062  1.00 28.29           C  
ATOM   1543  CD1 LEU A 276      93.804  62.062  16.638  1.00 27.80           C  
ATOM   1544  CD2 LEU A 276      95.644  63.196  17.944  1.00 26.67           C  
ATOM   1545  N   LEU A 277      91.506  65.429  15.688  1.00 28.86           N  
ATOM   1546  CA  LEU A 277      90.558  66.359  16.282  1.00 29.13           C  
ATOM   1547  C   LEU A 277      90.100  65.897  17.650  1.00 28.82           C  
ATOM   1548  O   LEU A 277      89.684  64.752  17.822  1.00 29.16           O  
ATOM   1549  CB  LEU A 277      89.349  66.514  15.358  1.00 29.87           C  
ATOM   1550  CG  LEU A 277      89.654  66.937  13.901  1.00 30.18           C  
ATOM   1551  CD1 LEU A 277      88.366  66.947  13.111  1.00 31.77           C  
ATOM   1552  CD2 LEU A 277      90.300  68.310  13.880  1.00 30.01           C  
ATOM   1553  N   LYS A 278      90.181  66.792  18.624  1.00 29.13           N  
ATOM   1554  CA  LYS A 278      89.783  66.471  19.984  1.00 28.96           C  
ATOM   1555  C   LYS A 278      88.392  66.956  20.318  1.00 29.81           C  
ATOM   1556  O   LYS A 278      88.159  68.165  20.414  1.00 30.65           O  
ATOM   1557  CB  LYS A 278      90.769  67.074  20.977  1.00 29.17           C  
ATOM   1558  CG  LYS A 278      90.433  66.830  22.437  1.00 29.24           C  
ATOM   1559  CD  LYS A 278      91.511  67.379  23.347  1.00 29.19           C  
ATOM   1560  CE  LYS A 278      91.158  67.158  24.807  1.00 29.48           C  
ATOM   1561  NZ  LYS A 278      92.201  67.701  25.720  1.00 29.37           N  
ATOM   1562  N   TYR A 279      87.483  66.005  20.537  1.00 29.52           N  
ATOM   1563  CA  TYR A 279      86.100  66.293  20.896  1.00 29.51           C  
ATOM   1564  C   TYR A 279      85.935  66.180  22.401  1.00 29.76           C  
ATOM   1565  O   TYR A 279      86.281  65.153  22.990  1.00 29.70           O  
ATOM   1566  CB  TYR A 279      85.150  65.307  20.227  1.00 30.15           C  
ATOM   1567  CG  TYR A 279      85.048  65.419  18.743  1.00 30.42           C  
ATOM   1568  CD1 TYR A 279      85.973  64.797  17.940  1.00 30.13           C  
ATOM   1569  CD2 TYR A 279      84.010  66.120  18.180  1.00 31.44           C  
ATOM   1570  CE1 TYR A 279      85.863  64.880  16.578  1.00 30.56           C  
ATOM   1571  CE2 TYR A 279      83.899  66.200  16.815  1.00 31.52           C  
ATOM   1572  CZ  TYR A 279      84.825  65.579  16.016  1.00 31.67           C  
ATOM   1573  OH  TYR A 279      84.721  65.651  14.650  1.00 32.07           O  
ATOM   1574  N   ASN A 280      85.365  67.201  23.024  1.00 30.25           N  
ATOM   1575  CA  ASN A 280      85.160  67.181  24.468  1.00 30.57           C  
ATOM   1576  C   ASN A 280      83.880  66.437  24.809  1.00 30.96           C  
ATOM   1577  O   ASN A 280      83.276  65.790  23.950  1.00 31.20           O  
ATOM   1578  CB  ASN A 280      85.144  68.579  25.061  1.00 30.84           C  
ATOM   1579  CG  ASN A 280      83.934  69.377  24.696  1.00 31.09           C  
ATOM   1580  OD1 ASN A 280      82.996  68.864  24.069  1.00 31.82           O  
ATOM   1581  ND2 ASN A 280      83.915  70.618  25.106  1.00 31.50           N  
ATOM   1582  N   GLU A 281      83.480  66.500  26.070  1.00 30.89           N  
ATOM   1583  CA  GLU A 281      82.303  65.779  26.553  1.00 30.95           C  
ATOM   1584  C   GLU A 281      80.965  66.218  25.922  1.00 31.09           C  
ATOM   1585  O   GLU A 281      79.993  65.462  25.982  1.00 30.92           O  
ATOM   1586  CB  GLU A 281      82.216  65.905  28.074  1.00 31.27           C  
ATOM   1587  CG  GLU A 281      83.385  65.256  28.822  1.00 31.83           C  
ATOM   1588  CD  GLU A 281      84.607  66.139  28.902  1.00 32.07           C  
ATOM   1589  OE1 GLU A 281      84.534  67.256  28.453  1.00 31.46           O  
ATOM   1590  OE2 GLU A 281      85.608  65.696  29.405  1.00 32.24           O  
ATOM   1591  N   ASN A 282      80.907  67.436  25.343  1.00 31.06           N  
ATOM   1592  CA  ASN A 282      79.709  67.990  24.704  1.00 31.26           C  
ATOM   1593  C   ASN A 282      79.750  67.817  23.175  1.00 31.60           C  
ATOM   1594  O   ASN A 282      78.876  68.329  22.470  1.00 32.24           O  
ATOM   1595  CB  ASN A 282      79.549  69.474  25.061  1.00 31.85           C  
ATOM   1596  CG  ASN A 282      79.217  69.741  26.537  1.00 31.90           C  
ATOM   1597  OD1 ASN A 282      79.296  68.845  27.393  1.00 31.60           O  
ATOM   1598  ND2 ASN A 282      78.848  70.985  26.831  1.00 32.57           N  
ATOM   1599  N   GLY A 283      80.775  67.119  22.651  1.00 31.77           N  
ATOM   1600  CA  GLY A 283      80.962  66.887  21.225  1.00 31.78           C  
ATOM   1601  C   GLY A 283      81.504  68.106  20.496  1.00 31.58           C  
ATOM   1602  O   GLY A 283      81.331  68.246  19.284  1.00 31.75           O  
ATOM   1603  N   THR A 284      82.153  68.993  21.231  1.00 31.31           N  
ATOM   1604  CA  THR A 284      82.710  70.191  20.647  1.00 31.38           C  
ATOM   1605  C   THR A 284      84.171  69.970  20.373  1.00 31.93           C  
ATOM   1606  O   THR A 284      84.894  69.466  21.231  1.00 30.90           O  
ATOM   1607  CB  THR A 284      82.518  71.396  21.582  1.00 31.85           C  
ATOM   1608  OG1 THR A 284      81.120  71.641  21.756  1.00 32.14           O  
ATOM   1609  CG2 THR A 284      83.185  72.632  21.025  1.00 32.10           C  
ATOM   1610  N   ILE A 285      84.632  70.340  19.185  1.00 31.20           N  
ATOM   1611  CA  ILE A 285      86.049  70.197  18.929  1.00 30.68           C  
ATOM   1612  C   ILE A 285      86.718  71.327  19.678  1.00 30.50           C  
ATOM   1613  O   ILE A 285      86.394  72.493  19.454  1.00 30.85           O  
ATOM   1614  CB  ILE A 285      86.384  70.288  17.433  1.00 30.69           C  
ATOM   1615  CG1 ILE A 285      85.690  69.182  16.667  1.00 31.02           C  
ATOM   1616  CG2 ILE A 285      87.894  70.170  17.246  1.00 30.20           C  
ATOM   1617  CD1 ILE A 285      85.713  69.356  15.155  1.00 31.32           C  
ATOM   1618  N   THR A 286      87.615  70.990  20.590  1.00 30.35           N  
ATOM   1619  CA  THR A 286      88.259  72.004  21.407  1.00 30.58           C  
ATOM   1620  C   THR A 286      89.715  72.171  21.049  1.00 30.30           C  
ATOM   1621  O   THR A 286      90.312  73.202  21.356  1.00 30.42           O  
ATOM   1622  CB  THR A 286      88.127  71.687  22.901  1.00 31.13           C  
ATOM   1623  OG1 THR A 286      88.743  70.426  23.182  1.00 30.62           O  
ATOM   1624  CG2 THR A 286      86.668  71.633  23.284  1.00 31.01           C  
ATOM   1625  N   ASP A 287      90.286  71.177  20.382  1.00 30.25           N  
ATOM   1626  CA  ASP A 287      91.674  71.303  19.953  1.00 29.62           C  
ATOM   1627  C   ASP A 287      91.923  70.482  18.697  1.00 29.26           C  
ATOM   1628  O   ASP A 287      91.033  69.759  18.240  1.00 29.73           O  
ATOM   1629  CB  ASP A 287      92.596  70.855  21.094  1.00 29.56           C  
ATOM   1630  CG  ASP A 287      93.984  71.481  21.074  1.00 29.10           C  
ATOM   1631  OD1 ASP A 287      94.377  71.992  20.053  1.00 29.32           O  
ATOM   1632  OD2 ASP A 287      94.644  71.431  22.083  1.00 28.89           O  
ATOM   1633  N   ALA A 288      93.126  70.574  18.148  1.00 29.08           N  
ATOM   1634  CA  ALA A 288      93.469  69.801  16.964  1.00 28.81           C  
ATOM   1635  C   ALA A 288      94.979  69.726  16.742  1.00 28.42           C  
ATOM   1636  O   ALA A 288      95.712  70.654  17.080  1.00 28.34           O  
ATOM   1637  CB  ALA A 288      92.794  70.401  15.747  1.00 29.65           C  
ATOM   1638  N   VAL A 289      95.428  68.654  16.095  1.00 28.17           N  
ATOM   1639  CA  VAL A 289      96.827  68.531  15.701  1.00 28.04           C  
ATOM   1640  C   VAL A 289      96.984  68.414  14.201  1.00 28.25           C  
ATOM   1641  O   VAL A 289      96.429  67.514  13.578  1.00 28.72           O  
ATOM   1642  CB  VAL A 289      97.480  67.284  16.336  1.00 27.85           C  
ATOM   1643  CG1 VAL A 289      98.927  67.148  15.899  1.00 26.61           C  
ATOM   1644  CG2 VAL A 289      97.395  67.374  17.812  1.00 27.58           C  
ATOM   1645  N   ASP A 290      97.790  69.297  13.631  1.00 28.12           N  
ATOM   1646  CA  ASP A 290      98.124  69.234  12.216  1.00 27.97           C  
ATOM   1647  C   ASP A 290      99.294  68.278  12.075  1.00 27.14           C  
ATOM   1648  O   ASP A 290     100.409  68.606  12.493  1.00 26.82           O  
ATOM   1649  CB  ASP A 290      98.477  70.616  11.685  1.00 28.40           C  
ATOM   1650  CG  ASP A 290      98.843  70.645  10.192  1.00 28.49           C  
ATOM   1651  OD1 ASP A 290      99.307  69.646   9.647  1.00 27.68           O  
ATOM   1652  OD2 ASP A 290      98.646  71.684   9.602  1.00 29.44           O  
ATOM   1653  N   CYS A 291      99.041  67.081  11.542  1.00 27.46           N  
ATOM   1654  CA  CYS A 291      99.979  65.967  11.533  1.00 26.96           C  
ATOM   1655  C   CYS A 291     101.246  66.211  10.698  1.00 26.59           C  
ATOM   1656  O   CYS A 291     102.178  65.417  10.762  1.00 25.71           O  
ATOM   1657  CB  CYS A 291      99.293  64.688  11.031  1.00 28.12           C  
ATOM   1658  SG  CYS A 291      97.878  64.139  12.040  1.00 29.14           S  
ATOM   1659  N   ALA A 292     101.285  67.289   9.875  1.00 26.34           N  
ATOM   1660  CA  ALA A 292     102.461  67.610   9.044  1.00 26.22           C  
ATOM   1661  C   ALA A 292     103.086  68.944   9.439  1.00 26.40           C  
ATOM   1662  O   ALA A 292     103.913  69.482   8.705  1.00 25.96           O  
ATOM   1663  CB  ALA A 292     102.067  67.632   7.581  1.00 27.80           C  
ATOM   1664  N   LEU A 293     102.706  69.470  10.594  1.00 26.23           N  
ATOM   1665  CA  LEU A 293     103.240  70.739  11.076  1.00 25.87           C  
ATOM   1666  C   LEU A 293     104.705  70.665  11.485  1.00 25.30           C  
ATOM   1667  O   LEU A 293     105.479  71.587  11.225  1.00 26.44           O  
ATOM   1668  CB  LEU A 293     102.415  71.217  12.268  1.00 26.38           C  
ATOM   1669  CG  LEU A 293     102.833  72.536  12.934  1.00 26.39           C  
ATOM   1670  CD1 LEU A 293     102.792  73.669  11.939  1.00 27.37           C  
ATOM   1671  CD2 LEU A 293     101.896  72.804  14.094  1.00 27.00           C  
ATOM   1672  N   ASP A 294     105.076  69.577  12.146  1.00 25.11           N  
ATOM   1673  CA  ASP A 294     106.409  69.391  12.699  1.00 24.71           C  
ATOM   1674  C   ASP A 294     106.503  67.967  13.277  1.00 24.21           C  
ATOM   1675  O   ASP A 294     105.474  67.309  13.427  1.00 24.07           O  
ATOM   1676  CB  ASP A 294     106.679  70.487  13.755  1.00 24.83           C  
ATOM   1677  CG  ASP A 294     105.674  70.516  14.888  1.00 24.62           C  
ATOM   1678  OD1 ASP A 294     105.157  69.475  15.219  1.00 24.46           O  
ATOM   1679  OD2 ASP A 294     105.434  71.573  15.425  1.00 25.72           O  
ATOM   1680  N   PRO A 295     107.709  67.439  13.556  1.00 23.47           N  
ATOM   1681  CA  PRO A 295     107.951  66.119  14.114  1.00 23.15           C  
ATOM   1682  C   PRO A 295     107.190  65.827  15.403  1.00 23.31           C  
ATOM   1683  O   PRO A 295     106.755  64.697  15.624  1.00 23.34           O  
ATOM   1684  CB  PRO A 295     109.453  66.151  14.352  1.00 22.15           C  
ATOM   1685  CG  PRO A 295     109.973  67.112  13.333  1.00 22.62           C  
ATOM   1686  CD  PRO A 295     108.941  68.185  13.261  1.00 23.51           C  
ATOM   1687  N   LEU A 296     106.972  66.833  16.236  1.00 23.13           N  
ATOM   1688  CA  LEU A 296     106.236  66.570  17.460  1.00 23.09           C  
ATOM   1689  C   LEU A 296     104.782  66.282  17.154  1.00 24.05           C  
ATOM   1690  O   LEU A 296     104.180  65.394  17.758  1.00 24.23           O  
ATOM   1691  CB  LEU A 296     106.341  67.733  18.435  1.00 23.07           C  
ATOM   1692  CG  LEU A 296     105.585  67.556  19.775  1.00 23.61           C  
ATOM   1693  CD1 LEU A 296     106.070  66.304  20.525  1.00 24.12           C  
ATOM   1694  CD2 LEU A 296     105.805  68.787  20.617  1.00 23.79           C  
ATOM   1695  N   SER A 297     104.214  67.028  16.218  1.00 24.12           N  
ATOM   1696  CA  SER A 297     102.832  66.828  15.831  1.00 23.56           C  
ATOM   1697  C   SER A 297     102.680  65.471  15.162  1.00 24.38           C  
ATOM   1698  O   SER A 297     101.688  64.774  15.379  1.00 24.57           O  
ATOM   1699  CB  SER A 297     102.389  67.930  14.910  1.00 24.99           C  
ATOM   1700  OG  SER A 297     102.398  69.164  15.577  1.00 24.78           O  
ATOM   1701  N   GLU A 298     103.686  65.063  14.392  1.00 23.62           N  
ATOM   1702  CA  GLU A 298     103.646  63.756  13.752  1.00 23.65           C  
ATOM   1703  C   GLU A 298     103.583  62.672  14.821  1.00 23.63           C  
ATOM   1704  O   GLU A 298     102.828  61.705  14.691  1.00 23.64           O  
ATOM   1705  CB  GLU A 298     104.888  63.532  12.884  1.00 23.64           C  
ATOM   1706  CG  GLU A 298     104.968  64.383  11.623  1.00 23.65           C  
ATOM   1707  CD  GLU A 298     106.304  64.277  10.921  1.00 23.68           C  
ATOM   1708  OE1 GLU A 298     107.160  63.590  11.421  1.00 23.25           O  
ATOM   1709  OE2 GLU A 298     106.468  64.890   9.891  1.00 23.39           O  
ATOM   1710  N   THR A 299     104.343  62.865  15.902  1.00 23.65           N  
ATOM   1711  CA  THR A 299     104.360  61.929  17.015  1.00 23.39           C  
ATOM   1712  C   THR A 299     102.998  61.878  17.692  1.00 23.70           C  
ATOM   1713  O   THR A 299     102.477  60.795  17.962  1.00 23.99           O  
ATOM   1714  CB  THR A 299     105.428  62.315  18.054  1.00 23.82           C  
ATOM   1715  OG1 THR A 299     106.713  62.332  17.441  1.00 23.10           O  
ATOM   1716  CG2 THR A 299     105.450  61.300  19.166  1.00 23.77           C  
ATOM   1717  N   LYS A 300     102.412  63.045  17.949  1.00 23.67           N  
ATOM   1718  CA  LYS A 300     101.096  63.106  18.580  1.00 23.49           C  
ATOM   1719  C   LYS A 300     100.023  62.378  17.767  1.00 24.16           C  
ATOM   1720  O   LYS A 300      99.214  61.636  18.333  1.00 24.60           O  
ATOM   1721  CB  LYS A 300     100.680  64.561  18.805  1.00 24.13           C  
ATOM   1722  CG  LYS A 300     101.419  65.266  19.916  1.00 23.82           C  
ATOM   1723  CD  LYS A 300     100.983  66.703  20.046  1.00 23.89           C  
ATOM   1724  CE  LYS A 300     101.688  67.396  21.192  1.00 24.96           C  
ATOM   1725  NZ  LYS A 300     101.255  68.809  21.325  1.00 23.84           N  
ATOM   1726  N   CYS A 301     100.031  62.549  16.431  1.00 24.05           N  
ATOM   1727  CA  CYS A 301      99.089  61.865  15.541  1.00 24.67           C  
ATOM   1728  C   CYS A 301      99.310  60.342  15.526  1.00 23.93           C  
ATOM   1729  O   CYS A 301      98.344  59.577  15.590  1.00 24.08           O  
ATOM   1730  CB  CYS A 301      99.172  62.437  14.116  1.00 25.38           C  
ATOM   1731  SG  CYS A 301      98.503  64.115  13.960  1.00 27.00           S  
ATOM   1732  N   THR A 302     100.581  59.901  15.510  1.00 23.84           N  
ATOM   1733  CA  THR A 302     100.971  58.486  15.502  1.00 23.65           C  
ATOM   1734  C   THR A 302     100.458  57.755  16.734  1.00 23.74           C  
ATOM   1735  O   THR A 302      99.965  56.632  16.647  1.00 23.82           O  
ATOM   1736  CB  THR A 302     102.501  58.353  15.441  1.00 23.35           C  
ATOM   1737  OG1 THR A 302     102.976  58.924  14.222  1.00 22.96           O  
ATOM   1738  CG2 THR A 302     102.926  56.899  15.515  1.00 23.03           C  
ATOM   1739  N   LEU A 303     100.565  58.414  17.876  1.00 23.90           N  
ATOM   1740  CA  LEU A 303     100.157  57.848  19.148  1.00 23.83           C  
ATOM   1741  C   LEU A 303      98.697  58.135  19.472  1.00 24.17           C  
ATOM   1742  O   LEU A 303      98.211  57.746  20.534  1.00 24.45           O  
ATOM   1743  CB  LEU A 303     101.024  58.435  20.260  1.00 23.73           C  
ATOM   1744  CG  LEU A 303     102.532  58.200  20.140  1.00 23.31           C  
ATOM   1745  CD1 LEU A 303     103.221  58.955  21.245  1.00 23.07           C  
ATOM   1746  CD2 LEU A 303     102.845  56.725  20.216  1.00 23.11           C  
ATOM   1747  N   LYS A 304      98.013  58.857  18.589  1.00 24.53           N  
ATOM   1748  CA  LYS A 304      96.628  59.244  18.800  1.00 24.64           C  
ATOM   1749  C   LYS A 304      96.431  59.908  20.150  1.00 25.10           C  
ATOM   1750  O   LYS A 304      95.512  59.558  20.890  1.00 25.40           O  
ATOM   1751  CB  LYS A 304      95.698  58.040  18.663  1.00 24.88           C  
ATOM   1752  CG  LYS A 304      95.799  57.306  17.326  1.00 24.50           C  
ATOM   1753  CD  LYS A 304      95.245  58.148  16.180  1.00 25.42           C  
ATOM   1754  CE  LYS A 304      95.174  57.360  14.876  1.00 24.98           C  
ATOM   1755  NZ  LYS A 304      96.518  56.966  14.392  1.00 24.43           N  
ATOM   1756  N   SER A 305      97.291  60.865  20.476  1.00 25.24           N  
ATOM   1757  CA  SER A 305      97.179  61.577  21.738  1.00 25.54           C  
ATOM   1758  C   SER A 305      97.756  62.972  21.650  1.00 25.29           C  
ATOM   1759  O   SER A 305      98.641  63.236  20.849  1.00 25.31           O  
ATOM   1760  CB  SER A 305      97.861  60.830  22.852  1.00 25.07           C  
ATOM   1761  OG  SER A 305      97.670  61.506  24.068  1.00 25.72           O  
ATOM   1762  N   PHE A 306      97.270  63.870  22.492  1.00 25.80           N  
ATOM   1763  CA  PHE A 306      97.791  65.232  22.522  1.00 25.60           C  
ATOM   1764  C   PHE A 306      98.907  65.366  23.537  1.00 25.08           C  
ATOM   1765  O   PHE A 306      99.470  66.448  23.721  1.00 24.62           O  
ATOM   1766  CB  PHE A 306      96.677  66.235  22.823  1.00 26.22           C  
ATOM   1767  CG  PHE A 306      95.770  66.505  21.654  1.00 27.09           C  
ATOM   1768  CD1 PHE A 306      95.055  65.497  21.041  1.00 27.29           C  
ATOM   1769  CD2 PHE A 306      95.632  67.785  21.165  1.00 27.98           C  
ATOM   1770  CE1 PHE A 306      94.244  65.763  19.976  1.00 27.89           C  
ATOM   1771  CE2 PHE A 306      94.813  68.043  20.104  1.00 28.10           C  
ATOM   1772  CZ  PHE A 306      94.119  67.025  19.508  1.00 28.51           C  
ATOM   1773  N   THR A 307      99.217  64.259  24.194  1.00 24.90           N  
ATOM   1774  CA  THR A 307     100.295  64.200  25.160  1.00 24.49           C  
ATOM   1775  C   THR A 307     101.276  63.122  24.734  1.00 24.16           C  
ATOM   1776  O   THR A 307     100.870  62.013  24.388  1.00 24.26           O  
ATOM   1777  CB  THR A 307      99.768  63.901  26.576  1.00 24.42           C  
ATOM   1778  OG1 THR A 307      98.858  64.936  26.979  1.00 24.53           O  
ATOM   1779  CG2 THR A 307     100.905  63.811  27.580  1.00 24.35           C  
ATOM   1780  N   VAL A 308     102.561  63.442  24.741  1.00 23.99           N  
ATOM   1781  CA  VAL A 308     103.569  62.457  24.383  1.00 23.65           C  
ATOM   1782  C   VAL A 308     104.488  62.177  25.549  1.00 23.22           C  
ATOM   1783  O   VAL A 308     105.144  63.081  26.077  1.00 23.08           O  
ATOM   1784  CB  VAL A 308     104.381  62.917  23.156  1.00 23.74           C  
ATOM   1785  CG1 VAL A 308     105.463  61.922  22.855  1.00 23.08           C  
ATOM   1786  CG2 VAL A 308     103.453  63.075  21.977  1.00 23.72           C  
ATOM   1787  N   GLU A 309     104.556  60.916  25.935  1.00 23.02           N  
ATOM   1788  CA  GLU A 309     105.416  60.503  27.023  1.00 22.80           C  
ATOM   1789  C   GLU A 309     106.858  60.565  26.599  1.00 22.21           C  
ATOM   1790  O   GLU A 309     107.186  60.525  25.416  1.00 22.18           O  
ATOM   1791  CB  GLU A 309     105.058  59.099  27.504  1.00 22.48           C  
ATOM   1792  CG  GLU A 309     103.683  58.990  28.101  1.00 22.46           C  
ATOM   1793  CD  GLU A 309     102.618  58.770  27.071  1.00 23.68           C  
ATOM   1794  OE1 GLU A 309     102.914  58.786  25.887  1.00 23.32           O  
ATOM   1795  OE2 GLU A 309     101.497  58.582  27.473  1.00 23.16           O  
ATOM   1796  N   LYS A 310     107.713  60.698  27.570  1.00 22.05           N  
ATOM   1797  CA  LYS A 310     109.129  60.747  27.346  1.00 21.74           C  
ATOM   1798  C   LYS A 310     109.628  59.483  26.666  1.00 21.49           C  
ATOM   1799  O   LYS A 310     109.330  58.372  27.113  1.00 21.91           O  
ATOM   1800  CB  LYS A 310     109.775  60.956  28.689  1.00 21.57           C  
ATOM   1801  CG  LYS A 310     111.218  61.101  28.720  1.00 21.18           C  
ATOM   1802  CD  LYS A 310     111.577  61.745  30.042  1.00 20.68           C  
ATOM   1803  CE  LYS A 310     113.039  61.746  30.287  1.00 19.90           C  
ATOM   1804  NZ  LYS A 310     113.488  60.465  30.847  1.00 19.82           N  
ATOM   1805  N   GLY A 311     110.410  59.635  25.606  1.00 21.00           N  
ATOM   1806  CA  GLY A 311     110.937  58.471  24.895  1.00 20.72           C  
ATOM   1807  C   GLY A 311     111.215  58.735  23.427  1.00 20.23           C  
ATOM   1808  O   GLY A 311     111.210  59.880  22.965  1.00 20.41           O  
ATOM   1809  N   ILE A 312     111.506  57.671  22.692  1.00 20.14           N  
ATOM   1810  CA  ILE A 312     111.778  57.769  21.270  1.00 20.07           C  
ATOM   1811  C   ILE A 312     110.698  57.009  20.534  1.00 20.33           C  
ATOM   1812  O   ILE A 312     110.408  55.858  20.857  1.00 20.63           O  
ATOM   1813  CB  ILE A 312     113.184  57.232  20.916  1.00 19.48           C  
ATOM   1814  CG1 ILE A 312     113.444  57.414  19.423  1.00 19.80           C  
ATOM   1815  CG2 ILE A 312     113.354  55.781  21.339  1.00 19.59           C  
ATOM   1816  CD1 ILE A 312     114.895  57.171  18.990  1.00 18.61           C  
ATOM   1817  N   TYR A 313     110.088  57.655  19.556  1.00 20.46           N  
ATOM   1818  CA  TYR A 313     109.000  57.032  18.824  1.00 20.77           C  
ATOM   1819  C   TYR A 313     109.282  56.987  17.347  1.00 20.66           C  
ATOM   1820  O   TYR A 313     109.849  57.921  16.801  1.00 20.93           O  
ATOM   1821  CB  TYR A 313     107.719  57.816  19.063  1.00 21.30           C  
ATOM   1822  CG  TYR A 313     107.342  57.859  20.490  1.00 21.43           C  
ATOM   1823  CD1 TYR A 313     107.805  58.873  21.298  1.00 21.22           C  
ATOM   1824  CD2 TYR A 313     106.546  56.887  20.999  1.00 21.90           C  
ATOM   1825  CE1 TYR A 313     107.461  58.894  22.620  1.00 21.63           C  
ATOM   1826  CE2 TYR A 313     106.198  56.907  22.312  1.00 21.86           C  
ATOM   1827  CZ  TYR A 313     106.648  57.899  23.123  1.00 21.79           C  
ATOM   1828  OH  TYR A 313     106.292  57.896  24.441  1.00 22.03           O  
ATOM   1829  N   GLN A 314     108.852  55.928  16.683  1.00 20.78           N  
ATOM   1830  CA  GLN A 314     108.974  55.861  15.237  1.00 20.58           C  
ATOM   1831  C   GLN A 314     107.675  56.347  14.645  1.00 20.87           C  
ATOM   1832  O   GLN A 314     106.622  55.767  14.904  1.00 20.99           O  
ATOM   1833  CB  GLN A 314     109.303  54.455  14.779  1.00 19.90           C  
ATOM   1834  CG  GLN A 314     109.503  54.338  13.304  1.00 19.92           C  
ATOM   1835  CD  GLN A 314     110.018  52.993  12.929  1.00 19.41           C  
ATOM   1836  OE1 GLN A 314     111.174  52.651  13.202  1.00 18.47           O  
ATOM   1837  NE2 GLN A 314     109.167  52.199  12.296  1.00 18.70           N  
ATOM   1838  N   THR A 315     107.736  57.448  13.913  1.00 20.87           N  
ATOM   1839  CA  THR A 315     106.512  58.098  13.475  1.00 21.14           C  
ATOM   1840  C   THR A 315     106.287  58.091  11.978  1.00 20.91           C  
ATOM   1841  O   THR A 315     105.151  58.191  11.512  1.00 21.27           O  
ATOM   1842  CB  THR A 315     106.528  59.555  13.930  1.00 21.84           C  
ATOM   1843  OG1 THR A 315     107.613  60.238  13.290  1.00 21.75           O  
ATOM   1844  CG2 THR A 315     106.715  59.641  15.420  1.00 22.01           C  
ATOM   1845  N   SER A 316     107.350  57.996  11.210  1.00 20.76           N  
ATOM   1846  CA  SER A 316     107.178  58.103   9.774  1.00 20.71           C  
ATOM   1847  C   SER A 316     108.316  57.461   9.025  1.00 20.56           C  
ATOM   1848  O   SER A 316     109.104  56.702   9.593  1.00 20.60           O  
ATOM   1849  CB  SER A 316     107.057  59.559   9.368  1.00 20.49           C  
ATOM   1850  OG  SER A 316     106.583  59.671   8.054  1.00 20.86           O  
ATOM   1851  N   ASN A 317     108.369  57.747   7.735  1.00 20.89           N  
ATOM   1852  CA  ASN A 317     109.395  57.233   6.854  1.00 21.09           C  
ATOM   1853  C   ASN A 317     109.855  58.320   5.912  1.00 21.47           C  
ATOM   1854  O   ASN A 317     109.051  58.977   5.252  1.00 21.49           O  
ATOM   1855  CB  ASN A 317     108.911  56.027   6.091  1.00 21.07           C  
ATOM   1856  CG  ASN A 317     108.690  54.840   6.968  1.00 19.48           C  
ATOM   1857  OD1 ASN A 317     109.648  54.208   7.428  1.00 19.56           O  
ATOM   1858  ND2 ASN A 317     107.448  54.516   7.209  1.00 18.99           N  
ATOM   1859  N   PHE A 318     111.153  58.512   5.875  1.00 21.98           N  
ATOM   1860  CA  PHE A 318     111.794  59.469   5.013  1.00 22.99           C  
ATOM   1861  C   PHE A 318     111.954  58.849   3.660  1.00 23.22           C  
ATOM   1862  O   PHE A 318     112.403  57.710   3.555  1.00 23.45           O  
ATOM   1863  CB  PHE A 318     113.159  59.842   5.581  1.00 23.16           C  
ATOM   1864  CG  PHE A 318     113.987  60.710   4.719  1.00 23.85           C  
ATOM   1865  CD1 PHE A 318     113.672  62.037   4.532  1.00 24.79           C  
ATOM   1866  CD2 PHE A 318     115.112  60.200   4.099  1.00 24.02           C  
ATOM   1867  CE1 PHE A 318     114.460  62.839   3.735  1.00 24.47           C  
ATOM   1868  CE2 PHE A 318     115.899  60.997   3.305  1.00 24.31           C  
ATOM   1869  CZ  PHE A 318     115.571  62.318   3.123  1.00 24.51           C  
ATOM   1870  N   ARG A 319     111.571  59.574   2.626  1.00 23.64           N  
ATOM   1871  CA  ARG A 319     111.775  59.103   1.272  1.00 24.30           C  
ATOM   1872  C   ARG A 319     112.151  60.254   0.369  1.00 25.64           C  
ATOM   1873  O   ARG A 319     111.412  61.234   0.255  1.00 26.07           O  
ATOM   1874  CB  ARG A 319     110.529  58.424   0.725  1.00 24.28           C  
ATOM   1875  CG  ARG A 319     110.147  57.123   1.408  1.00 23.09           C  
ATOM   1876  CD  ARG A 319     109.015  56.441   0.725  1.00 23.19           C  
ATOM   1877  NE  ARG A 319     107.785  57.217   0.804  1.00 23.51           N  
ATOM   1878  CZ  ARG A 319     106.930  57.212   1.852  1.00 23.30           C  
ATOM   1879  NH1 ARG A 319     107.179  56.467   2.907  1.00 21.80           N  
ATOM   1880  NH2 ARG A 319     105.840  57.961   1.813  1.00 23.43           N  
ATOM   1881  N   VAL A 320     113.268  60.106  -0.316  1.00 26.15           N  
ATOM   1882  CA  VAL A 320     113.695  61.097  -1.280  1.00 27.53           C  
ATOM   1883  C   VAL A 320     112.814  61.008  -2.507  1.00 28.22           C  
ATOM   1884  O   VAL A 320     112.557  59.922  -3.022  1.00 28.17           O  
ATOM   1885  CB  VAL A 320     115.170  60.886  -1.644  1.00 27.14           C  
ATOM   1886  CG1 VAL A 320     115.585  61.812  -2.774  1.00 28.62           C  
ATOM   1887  CG2 VAL A 320     116.018  61.155  -0.421  1.00 25.86           C  
ATOM   1888  N   GLN A 321     112.321  62.148  -2.955  1.00 28.87           N  
ATOM   1889  CA  GLN A 321     111.433  62.174  -4.099  1.00 29.47           C  
ATOM   1890  C   GLN A 321     112.226  62.407  -5.375  1.00 30.40           C  
ATOM   1891  O   GLN A 321     113.284  63.034  -5.322  1.00 30.57           O  
ATOM   1892  CB  GLN A 321     110.393  63.278  -3.905  1.00 29.68           C  
ATOM   1893  CG  GLN A 321     109.577  63.104  -2.655  1.00 29.13           C  
ATOM   1894  CD  GLN A 321     108.826  61.816  -2.664  1.00 28.97           C  
ATOM   1895  OE1 GLN A 321     108.029  61.557  -3.569  1.00 29.04           O  
ATOM   1896  NE2 GLN A 321     109.075  60.983  -1.665  1.00 27.76           N  
ATOM   1897  N   PRO A 322     111.744  61.914  -6.520  1.00 31.24           N  
ATOM   1898  CA  PRO A 322     112.295  62.139  -7.833  1.00 32.45           C  
ATOM   1899  C   PRO A 322     112.071  63.577  -8.238  1.00 32.67           C  
ATOM   1900  O   PRO A 322     111.098  64.197  -7.812  1.00 32.42           O  
ATOM   1901  CB  PRO A 322     111.515  61.154  -8.699  1.00 32.35           C  
ATOM   1902  CG  PRO A 322     110.214  60.946  -7.968  1.00 31.48           C  
ATOM   1903  CD  PRO A 322     110.567  61.041  -6.503  1.00 31.02           C  
ATOM   1904  N   THR A 323     112.950  64.093  -9.082  1.00 33.42           N  
ATOM   1905  CA  THR A 323     112.825  65.474  -9.538  1.00 34.13           C  
ATOM   1906  C   THR A 323     112.195  65.586 -10.921  1.00 34.42           C  
ATOM   1907  O   THR A 323     111.478  66.544 -11.212  1.00 34.86           O  
ATOM   1908  CB  THR A 323     114.205  66.158  -9.554  1.00 34.50           C  
ATOM   1909  OG1 THR A 323     114.741  66.174  -8.229  1.00 34.93           O  
ATOM   1910  CG2 THR A 323     114.095  67.585 -10.064  1.00 34.76           C  
ATOM   1911  N   GLU A 324     112.482  64.620 -11.774  1.00 34.45           N  
ATOM   1912  CA  GLU A 324     112.009  64.626 -13.150  1.00 35.01           C  
ATOM   1913  C   GLU A 324     111.838  63.205 -13.636  1.00 34.82           C  
ATOM   1914  O   GLU A 324     112.425  62.285 -13.060  1.00 34.73           O  
ATOM   1915  CB  GLU A 324     112.978  65.378 -14.058  1.00 35.08           C  
ATOM   1916  CG  GLU A 324     114.367  64.768 -14.164  1.00 35.30           C  
ATOM   1917  CD  GLU A 324     115.268  65.569 -15.072  1.00 35.57           C  
ATOM   1918  OE1 GLU A 324     114.908  65.761 -16.206  1.00 35.87           O  
ATOM   1919  OE2 GLU A 324     116.307  66.009 -14.626  1.00 35.81           O  
ATOM   1920  N   SER A 325     111.046  63.018 -14.686  1.00 35.16           N  
ATOM   1921  CA  SER A 325     110.900  61.686 -15.247  1.00 35.53           C  
ATOM   1922  C   SER A 325     111.850  61.454 -16.413  1.00 35.92           C  
ATOM   1923  O   SER A 325     112.223  62.389 -17.123  1.00 36.35           O  
ATOM   1924  CB  SER A 325     109.475  61.446 -15.705  1.00 35.83           C  
ATOM   1925  OG  SER A 325     109.133  62.288 -16.772  1.00 36.40           O  
ATOM   1926  N   ILE A 326     112.214  60.193 -16.610  1.00 36.50           N  
ATOM   1927  CA  ILE A 326     113.065  59.765 -17.710  1.00 37.36           C  
ATOM   1928  C   ILE A 326     112.341  58.748 -18.564  1.00 37.09           C  
ATOM   1929  O   ILE A 326     112.033  57.654 -18.095  1.00 36.55           O  
ATOM   1930  CB  ILE A 326     114.361  59.127 -17.169  1.00 36.94           C  
ATOM   1931  CG1 ILE A 326     115.070  60.098 -16.200  1.00 36.74           C  
ATOM   1932  CG2 ILE A 326     115.271  58.688 -18.304  1.00 37.83           C  
ATOM   1933  CD1 ILE A 326     115.550  61.409 -16.781  1.00 36.81           C  
ATOM   1934  N   VAL A 327     112.114  59.070 -19.824  1.00 38.19           N  
ATOM   1935  CA  VAL A 327     111.406  58.147 -20.698  1.00 37.89           C  
ATOM   1936  C   VAL A 327     112.283  57.658 -21.834  1.00 38.20           C  
ATOM   1937  O   VAL A 327     112.778  58.442 -22.641  1.00 39.60           O  
ATOM   1938  CB  VAL A 327     110.153  58.815 -21.265  1.00 38.66           C  
ATOM   1939  CG1 VAL A 327     109.442  57.871 -22.187  1.00 39.10           C  
ATOM   1940  CG2 VAL A 327     109.248  59.241 -20.116  1.00 38.79           C  
ATOM   1941  N   ARG A 328     112.479  56.351 -21.907  1.00 38.21           N  
ATOM   1942  CA  ARG A 328     113.338  55.789 -22.930  1.00 38.68           C  
ATOM   1943  C   ARG A 328     112.653  54.715 -23.776  1.00 39.27           C  
ATOM   1944  O   ARG A 328     112.116  53.734 -23.255  1.00 39.55           O  
ATOM   1945  CB  ARG A 328     114.553  55.186 -22.262  1.00 38.49           C  
ATOM   1946  CG  ARG A 328     115.428  56.154 -21.469  1.00 38.17           C  
ATOM   1947  CD  ARG A 328     116.674  56.519 -22.184  1.00 38.73           C  
ATOM   1948  NE  ARG A 328     116.592  57.765 -22.905  1.00 38.95           N  
ATOM   1949  CZ  ARG A 328     117.578  58.220 -23.708  1.00 39.08           C  
ATOM   1950  NH1 ARG A 328     118.675  57.515 -23.853  1.00 39.54           N  
ATOM   1951  NH2 ARG A 328     117.453  59.365 -24.345  1.00 39.48           N  
ATOM   1952  N   PHE A 329     112.744  54.889 -25.088  1.00 39.63           N  
ATOM   1953  CA  PHE A 329     112.261  53.934 -26.082  1.00 40.66           C  
ATOM   1954  C   PHE A 329     113.260  53.912 -27.233  1.00 40.94           C  
ATOM   1955  O   PHE A 329     113.929  54.917 -27.453  1.00 41.20           O  
ATOM   1956  CB  PHE A 329     110.882  54.318 -26.620  1.00 41.31           C  
ATOM   1957  CG  PHE A 329     109.759  54.276 -25.639  1.00 40.90           C  
ATOM   1958  CD1 PHE A 329     109.323  55.408 -25.009  1.00 40.23           C  
ATOM   1959  CD2 PHE A 329     109.120  53.085 -25.369  1.00 41.01           C  
ATOM   1960  CE1 PHE A 329     108.268  55.350 -24.133  1.00 40.32           C  
ATOM   1961  CE2 PHE A 329     108.066  53.029 -24.492  1.00 41.13           C  
ATOM   1962  CZ  PHE A 329     107.641  54.163 -23.875  1.00 40.30           C  
ATOM   1963  N   PRO A 330     113.374  52.829 -28.008  1.00 41.11           N  
ATOM   1964  CA  PRO A 330     114.219  52.757 -29.186  1.00 42.09           C  
ATOM   1965  C   PRO A 330     113.835  53.914 -30.100  1.00 43.39           C  
ATOM   1966  O   PRO A 330     112.642  54.138 -30.304  1.00 43.39           O  
ATOM   1967  CB  PRO A 330     113.813  51.410 -29.789  1.00 42.44           C  
ATOM   1968  CG  PRO A 330     113.345  50.597 -28.603  1.00 41.90           C  
ATOM   1969  CD  PRO A 330     112.636  51.597 -27.709  1.00 41.98           C  
ATOM   1970  N   ASN A 331     114.831  54.624 -30.690  1.00 43.14           N  
ATOM   1971  CA  ASN A 331     114.519  55.804 -31.499  1.00 43.81           C  
ATOM   1972  C   ASN A 331     114.178  55.432 -32.961  1.00 45.15           C  
ATOM   1973  O   ASN A 331     114.807  55.841 -33.906  1.00 45.20           O  
ATOM   1974  CB  ASN A 331     115.683  56.829 -31.427  1.00 43.65           C  
ATOM   1975  CG  ASN A 331     117.092  56.339 -31.892  1.00 43.57           C  
ATOM   1976  OD1 ASN A 331     117.376  56.323 -33.099  1.00 43.98           O  
ATOM   1977  ND2 ASN A 331     117.959  55.983 -30.946  1.00 43.08           N  
ATOM   1978  N   ILE A 332     113.022  54.731 -33.084  1.00 46.37           N  
ATOM   1979  CA  ILE A 332     112.477  54.239 -34.351  1.00 47.45           C  
ATOM   1980  C   ILE A 332     111.281  55.074 -34.794  1.00 48.53           C  
ATOM   1981  O   ILE A 332     110.428  55.426 -33.981  1.00 48.14           O  
ATOM   1982  CB  ILE A 332     112.083  52.758 -34.222  1.00 47.38           C  
ATOM   1983  CG1 ILE A 332     111.642  52.235 -35.588  1.00 48.79           C  
ATOM   1984  CG2 ILE A 332     110.970  52.579 -33.166  1.00 47.94           C  
ATOM   1985  CD1 ILE A 332     111.605  50.745 -35.688  1.00 49.54           C  
ATOM   1986  N   THR A 333     111.249  55.429 -36.081  1.00 49.05           N  
ATOM   1987  CA  THR A 333     110.188  56.272 -36.629  1.00 49.43           C  
ATOM   1988  C   THR A 333     109.245  55.559 -37.600  1.00 49.64           C  
ATOM   1989  O   THR A 333     108.350  56.183 -38.169  1.00 50.14           O  
ATOM   1990  CB  THR A 333     110.799  57.484 -37.344  1.00 50.24           C  
ATOM   1991  OG1 THR A 333     111.630  57.027 -38.425  1.00 50.52           O  
ATOM   1992  CG2 THR A 333     111.647  58.287 -36.365  1.00 49.96           C  
ATOM   1993  N   ASN A 334     109.451  54.269 -37.816  1.00 49.68           N  
ATOM   1994  CA  ASN A 334     108.592  53.515 -38.722  1.00 50.22           C  
ATOM   1995  C   ASN A 334     107.222  53.381 -38.093  1.00 50.78           C  
ATOM   1996  O   ASN A 334     107.128  53.203 -36.887  1.00 51.32           O  
ATOM   1997  CB  ASN A 334     109.157  52.135 -38.986  1.00 50.49           C  
ATOM   1998  CG  ASN A 334     110.462  52.162 -39.675  1.00 49.97           C  
ATOM   1999  OD1 ASN A 334     110.831  53.151 -40.316  1.00 50.48           O  
ATOM   2000  ND2 ASN A 334     111.186  51.079 -39.569  1.00 49.70           N  
ATOM   2001  N   LEU A 335     106.160  53.449 -38.881  1.00 50.61           N  
ATOM   2002  CA  LEU A 335     104.830  53.268 -38.302  1.00 52.00           C  
ATOM   2003  C   LEU A 335     104.342  51.851 -38.582  1.00 52.00           C  
ATOM   2004  O   LEU A 335     104.640  51.302 -39.641  1.00 52.30           O  
ATOM   2005  CB  LEU A 335     103.857  54.294 -38.882  1.00 51.82           C  
ATOM   2006  CG  LEU A 335     104.275  55.778 -38.732  1.00 51.22           C  
ATOM   2007  CD1 LEU A 335     103.204  56.655 -39.362  1.00 51.87           C  
ATOM   2008  CD2 LEU A 335     104.481  56.123 -37.258  1.00 50.95           C  
ATOM   2009  N   CYS A 336     103.595  51.274 -37.611  1.00 52.65           N  
ATOM   2010  CA  CYS A 336     103.098  49.889 -37.736  1.00 54.09           C  
ATOM   2011  C   CYS A 336     101.929  49.816 -38.744  1.00 54.98           C  
ATOM   2012  O   CYS A 336     101.008  50.591 -38.695  1.00 55.49           O  
ATOM   2013  CB  CYS A 336     102.593  49.395 -36.359  1.00 53.97           C  
ATOM   2014  SG  CYS A 336     103.898  49.183 -35.124  1.00 50.06           S  
ATOM   2015  N   PRO A 337     101.953  48.783 -39.671  1.00 55.91           N  
ATOM   2016  CA  PRO A 337     101.009  48.600 -40.769  1.00 57.49           C  
ATOM   2017  C   PRO A 337      99.670  48.032 -40.323  1.00 58.37           C  
ATOM   2018  O   PRO A 337      99.279  46.944 -40.740  1.00 59.15           O  
ATOM   2019  CB  PRO A 337     101.752  47.596 -41.656  1.00 57.61           C  
ATOM   2020  CG  PRO A 337     102.526  46.737 -40.695  1.00 57.45           C  
ATOM   2021  CD  PRO A 337     102.984  47.683 -39.620  1.00 55.61           C  
ATOM   2022  N   PHE A 338      98.957  48.779 -39.493  1.00 58.17           N  
ATOM   2023  CA  PHE A 338      97.644  48.330 -39.057  1.00 58.68           C  
ATOM   2024  C   PHE A 338      96.646  48.487 -40.189  1.00 60.51           C  
ATOM   2025  O   PHE A 338      95.703  47.711 -40.316  1.00 61.41           O  
ATOM   2026  CB  PHE A 338      97.169  49.098 -37.828  1.00 58.32           C  
ATOM   2027  CG  PHE A 338      97.882  48.713 -36.572  1.00 57.13           C  
ATOM   2028  CD1 PHE A 338      98.781  49.573 -35.978  1.00 55.93           C  
ATOM   2029  CD2 PHE A 338      97.662  47.480 -35.987  1.00 57.24           C  
ATOM   2030  CE1 PHE A 338      99.437  49.211 -34.828  1.00 54.73           C  
ATOM   2031  CE2 PHE A 338      98.321  47.118 -34.837  1.00 55.53           C  
ATOM   2032  CZ  PHE A 338      99.211  47.987 -34.259  1.00 54.70           C  
ATOM   2033  N   GLY A 339      96.850  49.485 -41.038  1.00 60.32           N  
ATOM   2034  CA  GLY A 339      95.934  49.712 -42.149  1.00 61.33           C  
ATOM   2035  C   GLY A 339      95.892  48.500 -43.069  1.00 61.42           C  
ATOM   2036  O   GLY A 339      94.847  48.154 -43.617  1.00 62.58           O  
ATOM   2037  N   GLU A 340      97.016  47.808 -43.184  1.00 60.43           N  
ATOM   2038  CA  GLU A 340      97.138  46.644 -44.053  1.00 60.96           C  
ATOM   2039  C   GLU A 340      96.420  45.422 -43.486  1.00 61.71           C  
ATOM   2040  O   GLU A 340      96.309  44.392 -44.153  1.00 61.92           O  
ATOM   2041  CB  GLU A 340      98.613  46.323 -44.276  1.00 60.63           C  
ATOM   2042  CG  GLU A 340      99.380  47.377 -45.053  1.00 60.12           C  
ATOM   2043  CD  GLU A 340     100.859  47.070 -45.199  1.00 60.13           C  
ATOM   2044  OE1 GLU A 340     101.329  46.110 -44.616  1.00 59.92           O  
ATOM   2045  OE2 GLU A 340     101.520  47.806 -45.889  1.00 60.38           O  
ATOM   2046  N   VAL A 341      95.965  45.525 -42.245  1.00 61.41           N  
ATOM   2047  CA  VAL A 341      95.241  44.452 -41.591  1.00 62.39           C  
ATOM   2048  C   VAL A 341      93.758  44.776 -41.538  1.00 63.20           C  
ATOM   2049  O   VAL A 341      92.916  43.954 -41.891  1.00 64.01           O  
ATOM   2050  CB  VAL A 341      95.757  44.259 -40.156  1.00 61.36           C  
ATOM   2051  CG1 VAL A 341      94.939  43.200 -39.443  1.00 62.19           C  
ATOM   2052  CG2 VAL A 341      97.219  43.877 -40.192  1.00 60.56           C  
ATOM   2053  N   PHE A 342      93.450  45.975 -41.066  1.00 62.37           N  
ATOM   2054  CA  PHE A 342      92.074  46.408 -40.859  1.00 63.18           C  
ATOM   2055  C   PHE A 342      91.324  46.832 -42.137  1.00 64.32           C  
ATOM   2056  O   PHE A 342      90.113  46.635 -42.224  1.00 64.67           O  
ATOM   2057  CB  PHE A 342      92.067  47.531 -39.828  1.00 63.13           C  
ATOM   2058  CG  PHE A 342      92.320  47.027 -38.433  1.00 62.62           C  
ATOM   2059  CD1 PHE A 342      93.600  46.938 -37.914  1.00 61.61           C  
ATOM   2060  CD2 PHE A 342      91.274  46.632 -37.646  1.00 63.00           C  
ATOM   2061  CE1 PHE A 342      93.810  46.459 -36.645  1.00 60.72           C  
ATOM   2062  CE2 PHE A 342      91.478  46.153 -36.378  1.00 62.31           C  
ATOM   2063  CZ  PHE A 342      92.749  46.065 -35.878  1.00 60.81           C  
ATOM   2064  N   ASN A 343      92.050  47.403 -43.115  1.00 64.24           N  
ATOM   2065  CA  ASN A 343      91.483  47.881 -44.401  1.00 64.62           C  
ATOM   2066  C   ASN A 343      91.883  46.953 -45.549  1.00 65.36           C  
ATOM   2067  O   ASN A 343      91.928  47.396 -46.723  1.00 66.20           O  
ATOM   2068  CB  ASN A 343      91.910  49.330 -44.652  1.00 65.12           C  
ATOM   2069  CG  ASN A 343      91.097  50.368 -43.856  1.00 65.16           C  
ATOM   2070  OD1 ASN A 343      89.862  50.272 -43.779  1.00 65.18           O  
ATOM   2071  ND2 ASN A 343      91.779  51.351 -43.283  1.00 64.91           N  
ATOM   2072  N   ALA A 344      92.156  45.669 -45.278  1.00 65.81           N  
ATOM   2073  CA  ALA A 344      92.537  44.654 -46.261  1.00 66.54           C  
ATOM   2074  C   ALA A 344      91.425  44.415 -47.273  1.00 67.76           C  
ATOM   2075  O   ALA A 344      90.242  44.466 -46.936  1.00 67.73           O  
ATOM   2076  CB  ALA A 344      92.870  43.350 -45.566  1.00 66.08           C  
ATOM   2077  N   THR A 345      91.800  44.130 -48.513  1.00 68.23           N  
ATOM   2078  CA  THR A 345      90.804  43.890 -49.541  1.00 69.00           C  
ATOM   2079  C   THR A 345      89.936  42.691 -49.170  1.00 69.23           C  
ATOM   2080  O   THR A 345      88.709  42.750 -49.274  1.00 69.90           O  
ATOM   2081  CB  THR A 345      91.481  43.668 -50.907  1.00 69.53           C  
ATOM   2082  OG1 THR A 345      92.266  44.821 -51.234  1.00 69.30           O  
ATOM   2083  CG2 THR A 345      90.450  43.455 -52.005  1.00 69.79           C  
ATOM   2084  N   ARG A 346      90.572  41.612 -48.713  1.00 68.73           N  
ATOM   2085  CA  ARG A 346      89.848  40.410 -48.311  1.00 69.27           C  
ATOM   2086  C   ARG A 346      90.405  39.793 -47.042  1.00 68.91           C  
ATOM   2087  O   ARG A 346      91.615  39.620 -46.893  1.00 68.76           O  
ATOM   2088  CB  ARG A 346      89.885  39.337 -49.395  1.00 69.66           C  
ATOM   2089  CG  ARG A 346      89.177  39.663 -50.699  1.00 69.99           C  
ATOM   2090  CD  ARG A 346      87.696  39.695 -50.555  1.00 70.47           C  
ATOM   2091  NE  ARG A 346      87.037  39.911 -51.842  1.00 71.15           N  
ATOM   2092  CZ  ARG A 346      86.794  41.117 -52.410  1.00 71.21           C  
ATOM   2093  NH1 ARG A 346      87.150  42.236 -51.811  1.00 70.73           N  
ATOM   2094  NH2 ARG A 346      86.190  41.173 -53.587  1.00 70.86           N  
ATOM   2095  N   PHE A 347      89.504  39.410 -46.154  1.00 69.15           N  
ATOM   2096  CA  PHE A 347      89.858  38.644 -44.975  1.00 68.55           C  
ATOM   2097  C   PHE A 347      89.844  37.157 -45.267  1.00 69.08           C  
ATOM   2098  O   PHE A 347      89.082  36.689 -46.113  1.00 69.17           O  
ATOM   2099  CB  PHE A 347      88.943  38.957 -43.796  1.00 67.94           C  
ATOM   2100  CG  PHE A 347      89.337  40.140 -42.980  1.00 68.40           C  
ATOM   2101  CD1 PHE A 347      89.873  41.286 -43.535  1.00 67.86           C  
ATOM   2102  CD2 PHE A 347      89.190  40.079 -41.606  1.00 66.04           C  
ATOM   2103  CE1 PHE A 347      90.251  42.329 -42.731  1.00 67.15           C  
ATOM   2104  CE2 PHE A 347      89.570  41.115 -40.811  1.00 66.37           C  
ATOM   2105  CZ  PHE A 347      90.103  42.244 -41.377  1.00 65.84           C  
ATOM   2106  N   ALA A 348      90.681  36.420 -44.553  1.00 67.89           N  
ATOM   2107  CA  ALA A 348      90.747  34.969 -44.647  1.00 68.40           C  
ATOM   2108  C   ALA A 348      89.570  34.312 -43.935  1.00 68.75           C  
ATOM   2109  O   ALA A 348      88.908  34.928 -43.101  1.00 68.12           O  
ATOM   2110  CB  ALA A 348      92.047  34.463 -44.055  1.00 66.88           C  
ATOM   2111  N   SER A 349      89.319  33.058 -44.278  1.00 68.95           N  
ATOM   2112  CA  SER A 349      88.313  32.260 -43.598  1.00 69.62           C  
ATOM   2113  C   SER A 349      88.791  31.861 -42.219  1.00 69.40           C  
ATOM   2114  O   SER A 349      89.994  31.780 -41.973  1.00 68.36           O  
ATOM   2115  CB  SER A 349      87.997  31.030 -44.396  1.00 70.93           C  
ATOM   2116  OG  SER A 349      87.380  31.344 -45.599  1.00 71.88           O  
ATOM   2117  N   VAL A 350      87.860  31.592 -41.316  1.00 69.52           N  
ATOM   2118  CA  VAL A 350      88.223  31.220 -39.957  1.00 69.24           C  
ATOM   2119  C   VAL A 350      88.888  29.845 -39.866  1.00 68.51           C  
ATOM   2120  O   VAL A 350      89.666  29.607 -38.950  1.00 68.41           O  
ATOM   2121  CB  VAL A 350      87.013  31.332 -39.017  1.00 68.97           C  
ATOM   2122  CG1 VAL A 350      86.039  30.246 -39.273  1.00 70.05           C  
ATOM   2123  CG2 VAL A 350      87.504  31.279 -37.595  1.00 68.54           C  
ATOM   2124  N   TYR A 351      88.613  28.934 -40.799  1.00 70.52           N  
ATOM   2125  CA  TYR A 351      89.306  27.647 -40.766  1.00 70.15           C  
ATOM   2126  C   TYR A 351      90.785  27.813 -41.123  1.00 69.43           C  
ATOM   2127  O   TYR A 351      91.603  26.941 -40.843  1.00 68.99           O  
ATOM   2128  CB  TYR A 351      88.668  26.632 -41.713  1.00 71.10           C  
ATOM   2129  CG  TYR A 351      89.227  26.659 -43.111  1.00 71.04           C  
ATOM   2130  CD1 TYR A 351      90.228  25.769 -43.475  1.00 70.20           C  
ATOM   2131  CD2 TYR A 351      88.760  27.570 -44.025  1.00 71.68           C  
ATOM   2132  CE1 TYR A 351      90.735  25.800 -44.757  1.00 70.07           C  
ATOM   2133  CE2 TYR A 351      89.264  27.605 -45.298  1.00 71.14           C  
ATOM   2134  CZ  TYR A 351      90.246  26.728 -45.671  1.00 70.09           C  
ATOM   2135  OH  TYR A 351      90.754  26.767 -46.941  1.00 69.59           O  
ATOM   2136  N   ALA A 352      91.117  28.913 -41.798  1.00 68.07           N  
ATOM   2137  CA  ALA A 352      92.465  29.172 -42.267  1.00 68.88           C  
ATOM   2138  C   ALA A 352      92.800  30.627 -42.033  1.00 67.81           C  
ATOM   2139  O   ALA A 352      93.008  31.385 -42.980  1.00 67.95           O  
ATOM   2140  CB  ALA A 352      92.596  28.838 -43.741  1.00 69.35           C  
ATOM   2141  N   TRP A 353      92.801  31.018 -40.770  1.00 67.48           N  
ATOM   2142  CA  TRP A 353      92.973  32.407 -40.392  1.00 66.10           C  
ATOM   2143  C   TRP A 353      94.405  32.862 -40.598  1.00 65.28           C  
ATOM   2144  O   TRP A 353      95.341  32.067 -40.487  1.00 65.62           O  
ATOM   2145  CB  TRP A 353      92.526  32.594 -38.947  1.00 65.87           C  
ATOM   2146  CG  TRP A 353      93.056  31.579 -37.994  1.00 65.32           C  
ATOM   2147  CD1 TRP A 353      92.519  30.366 -37.702  1.00 66.14           C  
ATOM   2148  CD2 TRP A 353      94.212  31.695 -37.181  1.00 64.35           C  
ATOM   2149  NE1 TRP A 353      93.276  29.734 -36.773  1.00 65.37           N  
ATOM   2150  CE2 TRP A 353      94.298  30.527 -36.435  1.00 64.79           C  
ATOM   2151  CE3 TRP A 353      95.165  32.677 -37.006  1.00 64.08           C  
ATOM   2152  CZ2 TRP A 353      95.285  30.319 -35.559  1.00 63.90           C  
ATOM   2153  CZ3 TRP A 353      96.166  32.448 -36.099  1.00 62.33           C  
ATOM   2154  CH2 TRP A 353      96.223  31.301 -35.398  1.00 62.66           C  
ATOM   2155  N   ASN A 354      94.582  34.140 -40.928  1.00 64.47           N  
ATOM   2156  CA  ASN A 354      95.924  34.658 -41.149  1.00 63.73           C  
ATOM   2157  C   ASN A 354      96.526  35.155 -39.861  1.00 62.25           C  
ATOM   2158  O   ASN A 354      95.808  35.628 -38.988  1.00 62.49           O  
ATOM   2159  CB  ASN A 354      95.924  35.773 -42.172  1.00 63.50           C  
ATOM   2160  CG  ASN A 354      95.648  35.303 -43.554  1.00 64.41           C  
ATOM   2161  OD1 ASN A 354      95.894  34.146 -43.910  1.00 64.85           O  
ATOM   2162  ND2 ASN A 354      95.156  36.196 -44.365  1.00 64.67           N  
ATOM   2163  N   ARG A 355      97.849  35.087 -39.763  1.00 60.84           N  
ATOM   2164  CA  ARG A 355      98.560  35.618 -38.609  1.00 59.35           C  
ATOM   2165  C   ARG A 355      99.690  36.532 -39.044  1.00 58.13           C  
ATOM   2166  O   ARG A 355     100.750  36.059 -39.454  1.00 58.02           O  
ATOM   2167  CB  ARG A 355      99.119  34.489 -37.773  1.00 59.27           C  
ATOM   2168  CG  ARG A 355      99.806  34.908 -36.496  1.00 57.39           C  
ATOM   2169  CD  ARG A 355     100.099  33.725 -35.665  1.00 57.24           C  
ATOM   2170  NE  ARG A 355     100.758  34.047 -34.409  1.00 55.31           N  
ATOM   2171  CZ  ARG A 355     100.121  34.469 -33.294  1.00 55.72           C  
ATOM   2172  NH1 ARG A 355      98.822  34.678 -33.303  1.00 57.97           N  
ATOM   2173  NH2 ARG A 355     100.800  34.681 -32.179  1.00 54.44           N  
ATOM   2174  N   LYS A 356      99.463  37.836 -38.989  1.00 57.72           N  
ATOM   2175  CA  LYS A 356     100.475  38.777 -39.443  1.00 57.42           C  
ATOM   2176  C   LYS A 356     101.348  39.263 -38.306  1.00 55.84           C  
ATOM   2177  O   LYS A 356     100.853  39.645 -37.246  1.00 55.54           O  
ATOM   2178  CB  LYS A 356      99.851  39.980 -40.131  1.00 57.44           C  
ATOM   2179  CG  LYS A 356     100.879  40.929 -40.737  1.00 57.90           C  
ATOM   2180  CD  LYS A 356     100.211  42.055 -41.450  1.00 59.40           C  
ATOM   2181  CE  LYS A 356     101.196  42.937 -42.189  1.00 58.57           C  
ATOM   2182  NZ  LYS A 356     100.482  44.000 -42.908  1.00 59.58           N  
ATOM   2183  N   ARG A 357     102.653  39.272 -38.529  1.00 55.48           N  
ATOM   2184  CA  ARG A 357     103.572  39.766 -37.521  1.00 54.08           C  
ATOM   2185  C   ARG A 357     103.810  41.258 -37.651  1.00 53.79           C  
ATOM   2186  O   ARG A 357     104.170  41.753 -38.719  1.00 54.80           O  
ATOM   2187  CB  ARG A 357     104.919  39.074 -37.617  1.00 53.65           C  
ATOM   2188  CG  ARG A 357     105.915  39.518 -36.558  1.00 52.37           C  
ATOM   2189  CD  ARG A 357     107.220  38.891 -36.737  1.00 52.11           C  
ATOM   2190  NE  ARG A 357     108.137  39.281 -35.683  1.00 51.40           N  
ATOM   2191  CZ  ARG A 357     109.476  39.245 -35.760  1.00 51.47           C  
ATOM   2192  NH1 ARG A 357     110.079  38.845 -36.860  1.00 51.44           N  
ATOM   2193  NH2 ARG A 357     110.181  39.622 -34.711  1.00 50.79           N  
ATOM   2194  N   ILE A 358     103.650  41.959 -36.540  1.00 53.10           N  
ATOM   2195  CA  ILE A 358     103.916  43.379 -36.449  1.00 52.56           C  
ATOM   2196  C   ILE A 358     105.168  43.592 -35.602  1.00 51.66           C  
ATOM   2197  O   ILE A 358     105.228  43.176 -34.440  1.00 51.79           O  
ATOM   2198  CB  ILE A 358     102.697  44.095 -35.843  1.00 52.87           C  
ATOM   2199  CG1 ILE A 358     101.477  43.846 -36.762  1.00 54.04           C  
ATOM   2200  CG2 ILE A 358     102.973  45.587 -35.636  1.00 53.06           C  
ATOM   2201  CD1 ILE A 358     100.153  44.254 -36.177  1.00 54.53           C  
ATOM   2202  N   SER A 359     106.182  44.209 -36.197  1.00 51.77           N  
ATOM   2203  CA  SER A 359     107.455  44.406 -35.512  1.00 50.26           C  
ATOM   2204  C   SER A 359     108.230  45.585 -36.069  1.00 50.13           C  
ATOM   2205  O   SER A 359     107.952  46.059 -37.170  1.00 50.17           O  
ATOM   2206  CB  SER A 359     108.309  43.161 -35.621  1.00 50.42           C  
ATOM   2207  OG  SER A 359     108.711  42.944 -36.949  1.00 50.51           O  
ATOM   2208  N   ASN A 360     109.235  46.022 -35.314  1.00 49.55           N  
ATOM   2209  CA  ASN A 360     110.142  47.092 -35.728  1.00 49.88           C  
ATOM   2210  C   ASN A 360     109.400  48.342 -36.193  1.00 50.17           C  
ATOM   2211  O   ASN A 360     109.612  48.807 -37.318  1.00 50.05           O  
ATOM   2212  CB  ASN A 360     111.077  46.594 -36.803  1.00 49.99           C  
ATOM   2213  CG  ASN A 360     111.931  45.477 -36.308  1.00 49.78           C  
ATOM   2214  OD1 ASN A 360     112.441  45.516 -35.181  1.00 49.52           O  
ATOM   2215  ND2 ASN A 360     112.100  44.470 -37.123  1.00 49.78           N  
ATOM   2216  N   CYS A 361     108.494  48.853 -35.342  1.00 50.02           N  
ATOM   2217  CA  CYS A 361     107.629  49.976 -35.689  1.00 49.53           C  
ATOM   2218  C   CYS A 361     107.030  50.674 -34.454  1.00 49.54           C  
ATOM   2219  O   CYS A 361     107.148  50.181 -33.323  1.00 49.58           O  
ATOM   2220  CB  CYS A 361     106.521  49.479 -36.653  1.00 51.14           C  
ATOM   2221  SG  CYS A 361     105.418  48.167 -35.987  1.00 51.06           S  
ATOM   2222  N   VAL A 362     106.376  51.827 -34.700  1.00 50.73           N  
ATOM   2223  CA  VAL A 362     105.637  52.608 -33.717  1.00 50.35           C  
ATOM   2224  C   VAL A 362     104.151  52.329 -33.851  1.00 50.29           C  
ATOM   2225  O   VAL A 362     103.554  52.534 -34.915  1.00 51.17           O  
ATOM   2226  CB  VAL A 362     105.896  54.109 -33.904  1.00 49.27           C  
ATOM   2227  CG1 VAL A 362     105.089  54.917 -32.885  1.00 48.94           C  
ATOM   2228  CG2 VAL A 362     107.377  54.373 -33.749  1.00 49.47           C  
ATOM   2229  N   ALA A 363     103.563  51.831 -32.783  1.00 50.17           N  
ATOM   2230  CA  ALA A 363     102.176  51.424 -32.817  1.00 50.62           C  
ATOM   2231  C   ALA A 363     101.277  52.420 -32.131  1.00 50.52           C  
ATOM   2232  O   ALA A 363     101.248  52.502 -30.906  1.00 49.75           O  
ATOM   2233  CB  ALA A 363     102.019  50.076 -32.165  1.00 50.91           C  
ATOM   2234  N   ASP A 364     100.542  53.178 -32.923  1.00 51.09           N  
ATOM   2235  CA  ASP A 364      99.629  54.164 -32.378  1.00 51.56           C  
ATOM   2236  C   ASP A 364      98.253  53.544 -32.249  1.00 52.22           C  
ATOM   2237  O   ASP A 364      97.564  53.333 -33.246  1.00 53.01           O  
ATOM   2238  CB  ASP A 364      99.581  55.413 -33.251  1.00 51.90           C  
ATOM   2239  CG  ASP A 364      98.713  56.508 -32.656  1.00 52.42           C  
ATOM   2240  OD1 ASP A 364      97.931  56.216 -31.767  1.00 53.03           O  
ATOM   2241  OD2 ASP A 364      98.839  57.632 -33.081  1.00 53.60           O  
ATOM   2242  N   TYR A 365      97.855  53.222 -31.028  1.00 52.14           N  
ATOM   2243  CA  TYR A 365      96.612  52.502 -30.817  1.00 52.54           C  
ATOM   2244  C   TYR A 365      95.465  53.448 -30.558  1.00 54.42           C  
ATOM   2245  O   TYR A 365      94.336  53.011 -30.327  1.00 55.24           O  
ATOM   2246  CB  TYR A 365      96.754  51.527 -29.656  1.00 51.02           C  
ATOM   2247  CG  TYR A 365      97.707  50.416 -29.940  1.00 50.43           C  
ATOM   2248  CD1 TYR A 365      98.990  50.484 -29.460  1.00 50.20           C  
ATOM   2249  CD2 TYR A 365      97.301  49.329 -30.682  1.00 51.84           C  
ATOM   2250  CE1 TYR A 365      99.866  49.479 -29.719  1.00 50.33           C  
ATOM   2251  CE2 TYR A 365      98.185  48.319 -30.946  1.00 52.12           C  
ATOM   2252  CZ  TYR A 365      99.466  48.395 -30.466  1.00 51.40           C  
ATOM   2253  OH  TYR A 365     100.364  47.395 -30.735  1.00 51.38           O  
ATOM   2254  N   SER A 366      95.744  54.748 -30.613  1.00 53.91           N  
ATOM   2255  CA  SER A 366      94.700  55.734 -30.395  1.00 54.82           C  
ATOM   2256  C   SER A 366      93.814  55.776 -31.615  1.00 56.40           C  
ATOM   2257  O   SER A 366      92.618  56.034 -31.518  1.00 57.37           O  
ATOM   2258  CB  SER A 366      95.285  57.105 -30.135  1.00 54.54           C  
ATOM   2259  OG  SER A 366      95.985  57.128 -28.925  1.00 53.99           O  
ATOM   2260  N   VAL A 367      94.393  55.478 -32.768  1.00 55.77           N  
ATOM   2261  CA  VAL A 367      93.635  55.490 -33.997  1.00 56.97           C  
ATOM   2262  C   VAL A 367      92.591  54.391 -33.978  1.00 57.92           C  
ATOM   2263  O   VAL A 367      91.416  54.630 -34.262  1.00 58.70           O  
ATOM   2264  CB  VAL A 367      94.579  55.288 -35.195  1.00 56.80           C  
ATOM   2265  CG1 VAL A 367      93.773  55.109 -36.491  1.00 60.24           C  
ATOM   2266  CG2 VAL A 367      95.512  56.485 -35.292  1.00 55.80           C  
ATOM   2267  N   LEU A 368      93.012  53.188 -33.615  1.00 57.40           N  
ATOM   2268  CA  LEU A 368      92.101  52.065 -33.588  1.00 58.40           C  
ATOM   2269  C   LEU A 368      91.052  52.211 -32.494  1.00 58.58           C  
ATOM   2270  O   LEU A 368      89.893  51.854 -32.687  1.00 59.64           O  
ATOM   2271  CB  LEU A 368      92.886  50.764 -33.371  1.00 58.08           C  
ATOM   2272  CG  LEU A 368      93.814  50.311 -34.504  1.00 58.45           C  
ATOM   2273  CD1 LEU A 368      94.669  49.149 -34.009  1.00 57.64           C  
ATOM   2274  CD2 LEU A 368      92.988  49.868 -35.692  1.00 60.23           C  
ATOM   2275  N   TYR A 369      91.457  52.729 -31.340  1.00 58.02           N  
ATOM   2276  CA  TYR A 369      90.540  52.879 -30.223  1.00 58.39           C  
ATOM   2277  C   TYR A 369      89.512  53.985 -30.440  1.00 58.92           C  
ATOM   2278  O   TYR A 369      88.334  53.808 -30.132  1.00 59.57           O  
ATOM   2279  CB  TYR A 369      91.313  53.107 -28.930  1.00 57.50           C  
ATOM   2280  CG  TYR A 369      90.425  53.191 -27.734  1.00 57.73           C  
ATOM   2281  CD1 TYR A 369      89.765  52.057 -27.293  1.00 57.51           C  
ATOM   2282  CD2 TYR A 369      90.266  54.391 -27.071  1.00 57.81           C  
ATOM   2283  CE1 TYR A 369      88.945  52.128 -26.193  1.00 57.61           C  
ATOM   2284  CE2 TYR A 369      89.446  54.462 -25.970  1.00 57.15           C  
ATOM   2285  CZ  TYR A 369      88.787  53.336 -25.531  1.00 57.99           C  
ATOM   2286  OH  TYR A 369      87.969  53.406 -24.434  1.00 59.70           O  
ATOM   2287  N   ASN A 370      89.958  55.135 -30.940  1.00 58.85           N  
ATOM   2288  CA  ASN A 370      89.074  56.274 -31.142  1.00 59.53           C  
ATOM   2289  C   ASN A 370      88.150  56.100 -32.347  1.00 61.01           C  
ATOM   2290  O   ASN A 370      87.051  56.665 -32.380  1.00 61.54           O  
ATOM   2291  CB  ASN A 370      89.882  57.548 -31.259  1.00 59.90           C  
ATOM   2292  CG  ASN A 370      90.486  57.941 -29.942  1.00 59.33           C  
ATOM   2293  OD1 ASN A 370      89.965  57.583 -28.880  1.00 60.77           O  
ATOM   2294  ND2 ASN A 370      91.567  58.668 -29.984  1.00 58.69           N  
ATOM   2295  N   SER A 371      88.578  55.320 -33.341  1.00 60.28           N  
ATOM   2296  CA  SER A 371      87.756  55.079 -34.516  1.00 61.53           C  
ATOM   2297  C   SER A 371      86.379  54.545 -34.152  1.00 62.30           C  
ATOM   2298  O   SER A 371      86.242  53.589 -33.392  1.00 62.33           O  
ATOM   2299  CB  SER A 371      88.447  54.097 -35.432  1.00 61.49           C  
ATOM   2300  OG  SER A 371      87.561  53.621 -36.405  1.00 62.49           O  
ATOM   2301  N   ALA A 372      85.348  55.145 -34.743  1.00 63.28           N  
ATOM   2302  CA  ALA A 372      83.962  54.768 -34.471  1.00 63.18           C  
ATOM   2303  C   ALA A 372      83.476  53.634 -35.364  1.00 63.09           C  
ATOM   2304  O   ALA A 372      82.333  53.195 -35.249  1.00 63.51           O  
ATOM   2305  CB  ALA A 372      83.054  55.971 -34.658  1.00 63.12           C  
ATOM   2306  N   SER A 373      84.331  53.180 -36.270  1.00 63.71           N  
ATOM   2307  CA  SER A 373      83.956  52.145 -37.229  1.00 63.75           C  
ATOM   2308  C   SER A 373      83.825  50.753 -36.614  1.00 63.48           C  
ATOM   2309  O   SER A 373      83.266  49.849 -37.237  1.00 64.29           O  
ATOM   2310  CB  SER A 373      84.966  52.083 -38.360  1.00 64.30           C  
ATOM   2311  OG  SER A 373      86.203  51.592 -37.917  1.00 63.47           O  
ATOM   2312  N   PHE A 374      84.356  50.564 -35.413  1.00 63.81           N  
ATOM   2313  CA  PHE A 374      84.350  49.242 -34.805  1.00 64.19           C  
ATOM   2314  C   PHE A 374      83.076  48.965 -34.029  1.00 64.29           C  
ATOM   2315  O   PHE A 374      82.576  49.825 -33.304  1.00 64.38           O  
ATOM   2316  CB  PHE A 374      85.565  49.084 -33.900  1.00 63.27           C  
ATOM   2317  CG  PHE A 374      86.841  49.151 -34.675  1.00 63.26           C  
ATOM   2318  CD1 PHE A 374      87.777  50.132 -34.421  1.00 62.16           C  
ATOM   2319  CD2 PHE A 374      87.089  48.258 -35.693  1.00 63.67           C  
ATOM   2320  CE1 PHE A 374      88.935  50.197 -35.161  1.00 61.67           C  
ATOM   2321  CE2 PHE A 374      88.244  48.331 -36.431  1.00 63.38           C  
ATOM   2322  CZ  PHE A 374      89.169  49.299 -36.161  1.00 62.44           C  
ATOM   2323  N   SER A 375      82.565  47.740 -34.154  1.00 64.52           N  
ATOM   2324  CA  SER A 375      81.376  47.347 -33.414  1.00 64.53           C  
ATOM   2325  C   SER A 375      81.773  47.024 -31.992  1.00 64.20           C  
ATOM   2326  O   SER A 375      81.023  47.263 -31.043  1.00 64.50           O  
ATOM   2327  CB  SER A 375      80.715  46.139 -34.052  1.00 65.46           C  
ATOM   2328  OG  SER A 375      80.222  46.444 -35.332  1.00 66.69           O  
ATOM   2329  N   THR A 376      82.979  46.498 -31.849  1.00 64.07           N  
ATOM   2330  CA  THR A 376      83.500  46.174 -30.538  1.00 63.17           C  
ATOM   2331  C   THR A 376      85.012  46.323 -30.496  1.00 62.04           C  
ATOM   2332  O   THR A 376      85.705  46.124 -31.498  1.00 62.36           O  
ATOM   2333  CB  THR A 376      83.103  44.748 -30.118  1.00 63.23           C  
ATOM   2334  OG1 THR A 376      83.476  44.541 -28.758  1.00 61.92           O  
ATOM   2335  CG2 THR A 376      83.801  43.722 -30.993  1.00 63.66           C  
ATOM   2336  N   PHE A 377      85.514  46.659 -29.318  1.00 60.90           N  
ATOM   2337  CA  PHE A 377      86.937  46.765 -29.044  1.00 59.98           C  
ATOM   2338  C   PHE A 377      87.125  46.323 -27.610  1.00 58.69           C  
ATOM   2339  O   PHE A 377      87.135  47.147 -26.695  1.00 58.10           O  
ATOM   2340  CB  PHE A 377      87.406  48.215 -29.216  1.00 59.12           C  
ATOM   2341  CG  PHE A 377      88.897  48.425 -29.305  1.00 59.02           C  
ATOM   2342  CD1 PHE A 377      89.429  49.008 -30.435  1.00 59.31           C  
ATOM   2343  CD2 PHE A 377      89.770  48.064 -28.283  1.00 58.44           C  
ATOM   2344  CE1 PHE A 377      90.769  49.223 -30.544  1.00 58.79           C  
ATOM   2345  CE2 PHE A 377      91.121  48.285 -28.407  1.00 57.60           C  
ATOM   2346  CZ  PHE A 377      91.616  48.866 -29.537  1.00 58.11           C  
ATOM   2347  N   LYS A 378      87.197  45.020 -27.400  1.00 58.33           N  
ATOM   2348  CA  LYS A 378      87.243  44.504 -26.043  1.00 57.51           C  
ATOM   2349  C   LYS A 378      88.620  43.964 -25.696  1.00 56.76           C  
ATOM   2350  O   LYS A 378      89.126  43.063 -26.372  1.00 56.28           O  
ATOM   2351  CB  LYS A 378      86.185  43.418 -25.841  1.00 57.11           C  
ATOM   2352  CG  LYS A 378      86.257  42.694 -24.491  1.00 56.28           C  
ATOM   2353  CD  LYS A 378      85.928  43.596 -23.310  1.00 56.41           C  
ATOM   2354  CE  LYS A 378      85.978  42.811 -22.001  1.00 57.15           C  
ATOM   2355  NZ  LYS A 378      85.720  43.679 -20.812  1.00 54.58           N  
ATOM   2356  N   CYS A 379      89.222  44.509 -24.633  1.00 56.13           N  
ATOM   2357  CA  CYS A 379      90.539  44.096 -24.167  1.00 55.30           C  
ATOM   2358  C   CYS A 379      90.423  43.183 -22.953  1.00 54.81           C  
ATOM   2359  O   CYS A 379      89.690  43.483 -22.003  1.00 54.61           O  
ATOM   2360  CB  CYS A 379      91.409  45.311 -23.838  1.00 52.30           C  
ATOM   2361  SG  CYS A 379      91.765  46.380 -25.262  1.00 52.09           S  
ATOM   2362  N   TYR A 380      91.168  42.074 -22.997  1.00 54.21           N  
ATOM   2363  CA  TYR A 380      91.245  41.065 -21.946  1.00 54.42           C  
ATOM   2364  C   TYR A 380      92.599  41.128 -21.260  1.00 53.38           C  
ATOM   2365  O   TYR A 380      92.744  40.721 -20.108  1.00 52.03           O  
ATOM   2366  CB  TYR A 380      91.005  39.684 -22.544  1.00 54.66           C  
ATOM   2367  CG  TYR A 380      89.663  39.574 -23.203  1.00 55.32           C  
ATOM   2368  CD1 TYR A 380      89.563  39.603 -24.582  1.00 56.13           C  
ATOM   2369  CD2 TYR A 380      88.526  39.459 -22.429  1.00 55.59           C  
ATOM   2370  CE1 TYR A 380      88.326  39.516 -25.180  1.00 56.67           C  
ATOM   2371  CE2 TYR A 380      87.293  39.371 -23.025  1.00 56.25           C  
ATOM   2372  CZ  TYR A 380      87.189  39.399 -24.395  1.00 56.89           C  
ATOM   2373  OH  TYR A 380      85.953  39.315 -24.991  1.00 57.47           O  
ATOM   2374  N   GLY A 381      93.585  41.650 -21.978  1.00 52.58           N  
ATOM   2375  CA  GLY A 381      94.941  41.757 -21.470  1.00 50.80           C  
ATOM   2376  C   GLY A 381      95.153  43.037 -20.687  1.00 48.11           C  
ATOM   2377  O   GLY A 381      95.282  43.016 -19.464  1.00 45.89           O  
ATOM   2378  N   VAL A 382      95.242  44.148 -21.404  1.00 46.31           N  
ATOM   2379  CA  VAL A 382      95.523  45.425 -20.784  1.00 43.76           C  
ATOM   2380  C   VAL A 382      94.460  46.420 -21.196  1.00 43.53           C  
ATOM   2381  O   VAL A 382      93.785  46.208 -22.193  1.00 46.55           O  
ATOM   2382  CB  VAL A 382      96.900  45.914 -21.236  1.00 43.20           C  
ATOM   2383  CG1 VAL A 382      97.922  44.854 -20.916  1.00 42.24           C  
ATOM   2384  CG2 VAL A 382      96.902  46.233 -22.713  1.00 44.81           C  
ATOM   2385  N   SER A 383      94.314  47.503 -20.459  1.00 44.05           N  
ATOM   2386  CA  SER A 383      93.340  48.513 -20.826  1.00 45.22           C  
ATOM   2387  C   SER A 383      93.796  49.217 -22.105  1.00 47.46           C  
ATOM   2388  O   SER A 383      94.983  49.504 -22.252  1.00 48.12           O  
ATOM   2389  CB  SER A 383      93.158  49.478 -19.679  1.00 43.03           C  
ATOM   2390  OG  SER A 383      92.575  48.821 -18.578  1.00 37.36           O  
ATOM   2391  N   PRO A 384      92.876  49.545 -23.024  1.00 44.13           N  
ATOM   2392  CA  PRO A 384      93.131  50.099 -24.343  1.00 46.45           C  
ATOM   2393  C   PRO A 384      93.786  51.470 -24.347  1.00 46.59           C  
ATOM   2394  O   PRO A 384      94.367  51.875 -25.349  1.00 47.68           O  
ATOM   2395  CB  PRO A 384      91.730  50.173 -24.945  1.00 51.12           C  
ATOM   2396  CG  PRO A 384      90.796  50.227 -23.765  1.00 50.41           C  
ATOM   2397  CD  PRO A 384      91.453  49.380 -22.710  1.00 46.50           C  
ATOM   2398  N   THR A 385      93.704  52.191 -23.239  1.00 45.32           N  
ATOM   2399  CA  THR A 385      94.273  53.528 -23.187  1.00 45.81           C  
ATOM   2400  C   THR A 385      95.701  53.502 -22.661  1.00 44.93           C  
ATOM   2401  O   THR A 385      96.407  54.510 -22.693  1.00 45.63           O  
ATOM   2402  CB  THR A 385      93.406  54.444 -22.318  1.00 45.32           C  
ATOM   2403  OG1 THR A 385      93.398  53.958 -20.978  1.00 44.06           O  
ATOM   2404  CG2 THR A 385      91.977  54.446 -22.853  1.00 48.08           C  
ATOM   2405  N   LYS A 386      96.136  52.337 -22.189  1.00 43.83           N  
ATOM   2406  CA  LYS A 386      97.479  52.168 -21.655  1.00 42.62           C  
ATOM   2407  C   LYS A 386      98.432  51.715 -22.749  1.00 44.73           C  
ATOM   2408  O   LYS A 386      99.653  51.735 -22.572  1.00 43.79           O  
ATOM   2409  CB  LYS A 386      97.488  51.136 -20.533  1.00 43.03           C  
ATOM   2410  CG  LYS A 386      96.657  51.476 -19.305  1.00 39.31           C  
ATOM   2411  CD  LYS A 386      97.281  52.573 -18.474  1.00 40.06           C  
ATOM   2412  CE  LYS A 386      96.599  52.644 -17.114  1.00 39.16           C  
ATOM   2413  NZ  LYS A 386      97.118  53.753 -16.270  1.00 36.69           N  
ATOM   2414  N   LEU A 387      97.860  51.322 -23.886  1.00 44.87           N  
ATOM   2415  CA  LEU A 387      98.606  50.755 -25.001  1.00 45.46           C  
ATOM   2416  C   LEU A 387      99.562  51.759 -25.613  1.00 46.41           C  
ATOM   2417  O   LEU A 387     100.510  51.383 -26.295  1.00 46.40           O  
ATOM   2418  CB  LEU A 387      97.646  50.256 -26.087  1.00 47.22           C  
ATOM   2419  CG  LEU A 387      96.786  49.017 -25.770  1.00 46.88           C  
ATOM   2420  CD1 LEU A 387      95.753  48.833 -26.873  1.00 49.26           C  
ATOM   2421  CD2 LEU A 387      97.669  47.788 -25.701  1.00 47.37           C  
ATOM   2422  N   ASN A 388      99.309  53.036 -25.382  1.00 46.25           N  
ATOM   2423  CA  ASN A 388     100.162  54.081 -25.909  1.00 46.73           C  
ATOM   2424  C   ASN A 388     101.488  54.196 -25.156  1.00 45.77           C  
ATOM   2425  O   ASN A 388     102.473  54.670 -25.716  1.00 45.56           O  
ATOM   2426  CB  ASN A 388      99.430  55.399 -25.876  1.00 47.06           C  
ATOM   2427  CG  ASN A 388      98.337  55.467 -26.886  1.00 48.58           C  
ATOM   2428  OD1 ASN A 388      98.443  54.923 -27.994  1.00 49.81           O  
ATOM   2429  ND2 ASN A 388      97.271  56.123 -26.519  1.00 49.89           N  
ATOM   2430  N   ASP A 389     101.510  53.812 -23.877  1.00 45.13           N  
ATOM   2431  CA  ASP A 389     102.725  53.922 -23.068  1.00 44.42           C  
ATOM   2432  C   ASP A 389     103.486  52.606 -23.061  1.00 43.86           C  
ATOM   2433  O   ASP A 389     104.710  52.564 -23.180  1.00 43.10           O  
ATOM   2434  CB  ASP A 389     102.379  54.285 -21.628  1.00 44.29           C  
ATOM   2435  CG  ASP A 389     103.600  54.671 -20.810  1.00 43.35           C  
ATOM   2436  OD1 ASP A 389     104.017  55.807 -20.918  1.00 43.00           O  
ATOM   2437  OD2 ASP A 389     104.114  53.841 -20.094  1.00 42.40           O  
ATOM   2438  N   LEU A 390     102.723  51.541 -22.906  1.00 44.32           N  
ATOM   2439  CA  LEU A 390     103.184  50.170 -22.805  1.00 44.06           C  
ATOM   2440  C   LEU A 390     103.732  49.712 -24.146  1.00 44.23           C  
ATOM   2441  O   LEU A 390     103.210  50.150 -25.172  1.00 45.46           O  
ATOM   2442  CB  LEU A 390     101.969  49.315 -22.436  1.00 43.86           C  
ATOM   2443  CG  LEU A 390     102.191  47.899 -22.020  1.00 42.72           C  
ATOM   2444  CD1 LEU A 390     102.859  47.869 -20.646  1.00 40.03           C  
ATOM   2445  CD2 LEU A 390     100.847  47.197 -22.022  1.00 41.80           C  
ATOM   2446  N   CYS A 391     104.758  48.830 -24.171  1.00 44.55           N  
ATOM   2447  CA  CYS A 391     105.188  48.276 -25.459  1.00 45.52           C  
ATOM   2448  C   CYS A 391     105.625  46.820 -25.365  1.00 45.48           C  
ATOM   2449  O   CYS A 391     105.770  46.263 -24.271  1.00 45.15           O  
ATOM   2450  CB  CYS A 391     106.261  49.145 -26.114  1.00 45.88           C  
ATOM   2451  SG  CYS A 391     107.852  49.285 -25.372  1.00 43.84           S  
ATOM   2452  N   PHE A 392     105.718  46.190 -26.556  1.00 46.19           N  
ATOM   2453  CA  PHE A 392     105.742  44.742 -26.731  1.00 46.43           C  
ATOM   2454  C   PHE A 392     106.953  44.215 -27.473  1.00 47.75           C  
ATOM   2455  O   PHE A 392     107.572  44.923 -28.279  1.00 47.25           O  
ATOM   2456  CB  PHE A 392     104.503  44.396 -27.539  1.00 47.04           C  
ATOM   2457  CG  PHE A 392     103.338  45.165 -27.045  1.00 46.97           C  
ATOM   2458  CD1 PHE A 392     102.968  46.331 -27.698  1.00 47.57           C  
ATOM   2459  CD2 PHE A 392     102.642  44.791 -25.938  1.00 46.95           C  
ATOM   2460  CE1 PHE A 392     101.925  47.090 -27.244  1.00 47.41           C  
ATOM   2461  CE2 PHE A 392     101.586  45.556 -25.482  1.00 46.59           C  
ATOM   2462  CZ  PHE A 392     101.238  46.704 -26.137  1.00 47.20           C  
ATOM   2463  N   THR A 393     107.253  42.941 -27.232  1.00 46.63           N  
ATOM   2464  CA  THR A 393     108.333  42.264 -27.939  1.00 46.70           C  
ATOM   2465  C   THR A 393     107.881  41.974 -29.356  1.00 47.78           C  
ATOM   2466  O   THR A 393     108.657  42.066 -30.302  1.00 47.70           O  
ATOM   2467  CB  THR A 393     108.694  40.938 -27.259  1.00 46.53           C  
ATOM   2468  OG1 THR A 393     107.596  40.040 -27.368  1.00 47.21           O  
ATOM   2469  CG2 THR A 393     108.996  41.150 -25.788  1.00 44.71           C  
ATOM   2470  N   ASN A 394     106.606  41.626 -29.486  1.00 48.17           N  
ATOM   2471  CA  ASN A 394     105.949  41.367 -30.758  1.00 48.95           C  
ATOM   2472  C   ASN A 394     104.450  41.582 -30.631  1.00 49.61           C  
ATOM   2473  O   ASN A 394     103.881  41.389 -29.551  1.00 49.68           O  
ATOM   2474  CB  ASN A 394     106.207  39.959 -31.248  1.00 49.84           C  
ATOM   2475  CG  ASN A 394     107.593  39.729 -31.745  1.00 49.32           C  
ATOM   2476  OD1 ASN A 394     107.947  40.159 -32.854  1.00 50.39           O  
ATOM   2477  ND2 ASN A 394     108.390  39.049 -30.958  1.00 49.59           N  
ATOM   2478  N   VAL A 395     103.806  41.928 -31.738  1.00 50.63           N  
ATOM   2479  CA  VAL A 395     102.351  41.960 -31.786  1.00 51.31           C  
ATOM   2480  C   VAL A 395     101.880  41.164 -32.995  1.00 52.30           C  
ATOM   2481  O   VAL A 395     102.430  41.302 -34.083  1.00 52.62           O  
ATOM   2482  CB  VAL A 395     101.825  43.408 -31.836  1.00 51.35           C  
ATOM   2483  CG1 VAL A 395     100.285  43.421 -31.901  1.00 52.13           C  
ATOM   2484  CG2 VAL A 395     102.311  44.153 -30.607  1.00 49.84           C  
ATOM   2485  N   TYR A 396     100.886  40.307 -32.810  1.00 52.35           N  
ATOM   2486  CA  TYR A 396     100.382  39.537 -33.942  1.00 53.44           C  
ATOM   2487  C   TYR A 396      98.919  39.814 -34.191  1.00 54.25           C  
ATOM   2488  O   TYR A 396      98.121  39.906 -33.260  1.00 55.12           O  
ATOM   2489  CB  TYR A 396     100.605  38.044 -33.723  1.00 53.78           C  
ATOM   2490  CG  TYR A 396     102.048  37.678 -33.687  1.00 53.31           C  
ATOM   2491  CD1 TYR A 396     102.741  37.781 -32.504  1.00 51.92           C  
ATOM   2492  CD2 TYR A 396     102.689  37.247 -34.834  1.00 53.26           C  
ATOM   2493  CE1 TYR A 396     104.065  37.466 -32.458  1.00 51.10           C  
ATOM   2494  CE2 TYR A 396     104.025  36.925 -34.784  1.00 51.83           C  
ATOM   2495  CZ  TYR A 396     104.710  37.039 -33.598  1.00 50.95           C  
ATOM   2496  OH  TYR A 396     106.039  36.735 -33.532  1.00 49.60           O  
ATOM   2497  N   ALA A 397      98.564  39.942 -35.460  1.00 55.56           N  
ATOM   2498  CA  ALA A 397      97.189  40.216 -35.832  1.00 57.20           C  
ATOM   2499  C   ALA A 397      96.553  39.022 -36.518  1.00 58.66           C  
ATOM   2500  O   ALA A 397      96.912  38.675 -37.647  1.00 58.95           O  
ATOM   2501  CB  ALA A 397      97.137  41.430 -36.736  1.00 57.32           C  
ATOM   2502  N   ASP A 398      95.600  38.401 -35.834  1.00 59.26           N  
ATOM   2503  CA  ASP A 398      94.916  37.233 -36.362  1.00 60.38           C  
ATOM   2504  C   ASP A 398      93.661  37.700 -37.089  1.00 61.24           C  
ATOM   2505  O   ASP A 398      92.753  38.251 -36.470  1.00 62.03           O  
ATOM   2506  CB  ASP A 398      94.570  36.263 -35.242  1.00 60.74           C  
ATOM   2507  CG  ASP A 398      95.809  35.715 -34.524  1.00 60.02           C  
ATOM   2508  OD1 ASP A 398      96.740  35.303 -35.184  1.00 59.45           O  
ATOM   2509  OD2 ASP A 398      95.834  35.756 -33.315  1.00 60.12           O  
ATOM   2510  N   SER A 399      93.636  37.535 -38.406  1.00 62.48           N  
ATOM   2511  CA  SER A 399      92.586  38.122 -39.247  1.00 63.69           C  
ATOM   2512  C   SER A 399      91.718  37.117 -39.997  1.00 65.03           C  
ATOM   2513  O   SER A 399      92.214  36.306 -40.788  1.00 66.17           O  
ATOM   2514  CB  SER A 399      93.229  39.066 -40.237  1.00 64.16           C  
ATOM   2515  OG  SER A 399      92.304  39.517 -41.171  1.00 65.22           O  
ATOM   2516  N   PHE A 400      90.411  37.167 -39.726  1.00 65.50           N  
ATOM   2517  CA  PHE A 400      89.457  36.253 -40.355  1.00 68.32           C  
ATOM   2518  C   PHE A 400      87.988  36.702 -40.283  1.00 67.22           C  
ATOM   2519  O   PHE A 400      87.636  37.616 -39.536  1.00 67.34           O  
ATOM   2520  CB  PHE A 400      89.613  34.872 -39.752  1.00 66.61           C  
ATOM   2521  CG  PHE A 400      89.508  34.868 -38.287  1.00 66.60           C  
ATOM   2522  CD1 PHE A 400      88.310  34.669 -37.686  1.00 67.27           C  
ATOM   2523  CD2 PHE A 400      90.622  35.079 -37.499  1.00 65.35           C  
ATOM   2524  CE1 PHE A 400      88.210  34.666 -36.321  1.00 66.50           C  
ATOM   2525  CE2 PHE A 400      90.529  35.083 -36.146  1.00 64.85           C  
ATOM   2526  CZ  PHE A 400      89.320  34.874 -35.553  1.00 65.42           C  
ATOM   2527  N   VAL A 401      87.128  36.044 -41.073  1.00 69.08           N  
ATOM   2528  CA  VAL A 401      85.681  36.316 -41.057  1.00 69.06           C  
ATOM   2529  C   VAL A 401      84.840  35.259 -40.343  1.00 69.40           C  
ATOM   2530  O   VAL A 401      84.965  34.060 -40.593  1.00 69.68           O  
ATOM   2531  CB  VAL A 401      85.137  36.467 -42.489  1.00 70.33           C  
ATOM   2532  CG1 VAL A 401      83.613  36.691 -42.487  1.00 71.07           C  
ATOM   2533  CG2 VAL A 401      85.816  37.611 -43.146  1.00 69.62           C  
ATOM   2534  N   ILE A 402      83.952  35.743 -39.476  1.00 69.38           N  
ATOM   2535  CA  ILE A 402      82.993  34.930 -38.724  1.00 70.23           C  
ATOM   2536  C   ILE A 402      81.573  35.471 -38.847  1.00 72.23           C  
ATOM   2537  O   ILE A 402      81.364  36.577 -39.343  1.00 69.57           O  
ATOM   2538  CB  ILE A 402      83.356  34.857 -37.234  1.00 69.67           C  
ATOM   2539  CG1 ILE A 402      83.359  36.276 -36.644  1.00 69.57           C  
ATOM   2540  CG2 ILE A 402      84.690  34.170 -37.053  1.00 69.63           C  
ATOM   2541  CD1 ILE A 402      83.470  36.325 -35.161  1.00 69.12           C  
ATOM   2542  N   ARG A 403      80.595  34.699 -38.387  1.00 71.31           N  
ATOM   2543  CA  ARG A 403      79.223  35.189 -38.311  1.00 72.85           C  
ATOM   2544  C   ARG A 403      79.064  36.063 -37.059  1.00 72.26           C  
ATOM   2545  O   ARG A 403      79.652  35.772 -36.024  1.00 69.98           O  
ATOM   2546  CB  ARG A 403      78.241  34.027 -38.299  1.00 73.27           C  
ATOM   2547  CG  ARG A 403      76.783  34.421 -38.321  1.00 72.29           C  
ATOM   2548  CD  ARG A 403      75.875  33.262 -38.573  1.00 73.03           C  
ATOM   2549  NE  ARG A 403      75.862  32.317 -37.470  1.00 73.27           N  
ATOM   2550  CZ  ARG A 403      75.144  31.170 -37.447  1.00 73.94           C  
ATOM   2551  NH1 ARG A 403      74.390  30.836 -38.474  1.00 74.03           N  
ATOM   2552  NH2 ARG A 403      75.196  30.378 -36.390  1.00 72.82           N  
ATOM   2553  N   GLY A 404      78.256  37.115 -37.153  1.00 72.56           N  
ATOM   2554  CA  GLY A 404      78.057  38.084 -36.071  1.00 71.34           C  
ATOM   2555  C   GLY A 404      77.771  37.533 -34.682  1.00 70.50           C  
ATOM   2556  O   GLY A 404      78.384  37.968 -33.707  1.00 69.93           O  
ATOM   2557  N   ASP A 405      76.878  36.566 -34.563  1.00 70.77           N  
ATOM   2558  CA  ASP A 405      76.567  36.038 -33.234  1.00 71.20           C  
ATOM   2559  C   ASP A 405      77.729  35.276 -32.599  1.00 70.45           C  
ATOM   2560  O   ASP A 405      77.685  34.945 -31.412  1.00 69.87           O  
ATOM   2561  CB  ASP A 405      75.325  35.144 -33.264  1.00 71.78           C  
ATOM   2562  CG  ASP A 405      74.013  35.928 -33.361  1.00 72.45           C  
ATOM   2563  OD1 ASP A 405      74.022  37.116 -33.125  1.00 72.11           O  
ATOM   2564  OD2 ASP A 405      73.009  35.327 -33.665  1.00 73.01           O  
ATOM   2565  N   GLU A 406      78.759  34.971 -33.384  1.00 70.12           N  
ATOM   2566  CA  GLU A 406      79.912  34.225 -32.896  1.00 69.47           C  
ATOM   2567  C   GLU A 406      81.024  35.130 -32.380  1.00 70.24           C  
ATOM   2568  O   GLU A 406      82.030  34.645 -31.866  1.00 67.90           O  
ATOM   2569  CB  GLU A 406      80.443  33.310 -33.997  1.00 69.67           C  
ATOM   2570  CG  GLU A 406      79.473  32.226 -34.374  1.00 70.52           C  
ATOM   2571  CD  GLU A 406      79.876  31.456 -35.564  1.00 70.84           C  
ATOM   2572  OE1 GLU A 406      80.809  31.844 -36.240  1.00 71.23           O  
ATOM   2573  OE2 GLU A 406      79.255  30.447 -35.794  1.00 71.95           O  
ATOM   2574  N   VAL A 407      80.840  36.445 -32.470  1.00 68.48           N  
ATOM   2575  CA  VAL A 407      81.865  37.381 -32.004  1.00 68.48           C  
ATOM   2576  C   VAL A 407      82.137  37.152 -30.525  1.00 67.46           C  
ATOM   2577  O   VAL A 407      83.272  37.253 -30.063  1.00 66.55           O  
ATOM   2578  CB  VAL A 407      81.442  38.853 -32.238  1.00 69.10           C  
ATOM   2579  CG1 VAL A 407      82.421  39.805 -31.531  1.00 68.71           C  
ATOM   2580  CG2 VAL A 407      81.433  39.171 -33.740  1.00 69.44           C  
ATOM   2581  N   ARG A 408      81.082  36.860 -29.778  1.00 67.65           N  
ATOM   2582  CA  ARG A 408      81.162  36.629 -28.343  1.00 67.68           C  
ATOM   2583  C   ARG A 408      82.064  35.450 -27.969  1.00 66.34           C  
ATOM   2584  O   ARG A 408      82.544  35.373 -26.839  1.00 65.38           O  
ATOM   2585  CB  ARG A 408      79.773  36.390 -27.780  1.00 67.15           C  
ATOM   2586  CG  ARG A 408      79.712  36.204 -26.271  1.00 66.87           C  
ATOM   2587  CD  ARG A 408      78.317  36.023 -25.794  1.00 67.98           C  
ATOM   2588  NE  ARG A 408      77.716  34.803 -26.327  1.00 68.01           N  
ATOM   2589  CZ  ARG A 408      77.924  33.554 -25.847  1.00 67.65           C  
ATOM   2590  NH1 ARG A 408      78.723  33.350 -24.817  1.00 65.93           N  
ATOM   2591  NH2 ARG A 408      77.321  32.528 -26.423  1.00 67.84           N  
ATOM   2592  N   GLN A 409      82.271  34.510 -28.894  1.00 66.22           N  
ATOM   2593  CA  GLN A 409      83.073  33.335 -28.590  1.00 65.48           C  
ATOM   2594  C   GLN A 409      84.570  33.595 -28.682  1.00 64.71           C  
ATOM   2595  O   GLN A 409      85.367  32.786 -28.200  1.00 63.88           O  
ATOM   2596  CB  GLN A 409      82.712  32.156 -29.503  1.00 66.23           C  
ATOM   2597  CG  GLN A 409      81.343  31.544 -29.256  1.00 66.34           C  
ATOM   2598  CD  GLN A 409      81.119  30.296 -30.115  1.00 66.98           C  
ATOM   2599  OE1 GLN A 409      82.011  29.435 -30.247  1.00 66.09           O  
ATOM   2600  NE2 GLN A 409      79.916  30.195 -30.706  1.00 67.38           N  
ATOM   2601  N   ILE A 410      84.988  34.701 -29.286  1.00 64.88           N  
ATOM   2602  CA  ILE A 410      86.423  34.911 -29.371  1.00 63.71           C  
ATOM   2603  C   ILE A 410      86.897  35.664 -28.147  1.00 62.68           C  
ATOM   2604  O   ILE A 410      87.013  36.889 -28.144  1.00 61.80           O  
ATOM   2605  CB  ILE A 410      86.824  35.635 -30.663  1.00 63.94           C  
ATOM   2606  CG1 ILE A 410      86.358  34.796 -31.859  1.00 65.14           C  
ATOM   2607  CG2 ILE A 410      88.347  35.862 -30.699  1.00 62.59           C  
ATOM   2608  CD1 ILE A 410      86.513  35.476 -33.175  1.00 66.56           C  
ATOM   2609  N   ALA A 411      87.157  34.897 -27.102  1.00 61.75           N  
ATOM   2610  CA  ALA A 411      87.575  35.423 -25.819  1.00 60.46           C  
ATOM   2611  C   ALA A 411      88.152  34.282 -24.983  1.00 60.02           C  
ATOM   2612  O   ALA A 411      87.750  33.129 -25.159  1.00 59.85           O  
ATOM   2613  CB  ALA A 411      86.391  36.075 -25.122  1.00 60.66           C  
ATOM   2614  N   PRO A 412      89.078  34.568 -24.066  1.00 59.29           N  
ATOM   2615  CA  PRO A 412      89.624  33.618 -23.126  1.00 58.67           C  
ATOM   2616  C   PRO A 412      88.508  33.151 -22.215  1.00 58.91           C  
ATOM   2617  O   PRO A 412      87.679  33.956 -21.792  1.00 58.97           O  
ATOM   2618  CB  PRO A 412      90.676  34.447 -22.382  1.00 58.39           C  
ATOM   2619  CG  PRO A 412      90.258  35.890 -22.583  1.00 57.98           C  
ATOM   2620  CD  PRO A 412      89.610  35.928 -23.945  1.00 57.98           C  
ATOM   2621  N   GLY A 413      88.482  31.861 -21.900  1.00 57.08           N  
ATOM   2622  CA  GLY A 413      87.464  31.336 -21.002  1.00 56.01           C  
ATOM   2623  C   GLY A 413      86.170  30.918 -21.707  1.00 56.43           C  
ATOM   2624  O   GLY A 413      85.273  30.361 -21.077  1.00 56.25           O  
ATOM   2625  N   GLN A 414      86.056  31.192 -23.011  1.00 59.39           N  
ATOM   2626  CA  GLN A 414      84.832  30.831 -23.714  1.00 60.19           C  
ATOM   2627  C   GLN A 414      84.929  29.491 -24.404  1.00 60.38           C  
ATOM   2628  O   GLN A 414      86.008  29.049 -24.802  1.00 60.54           O  
ATOM   2629  CB  GLN A 414      84.454  31.906 -24.728  1.00 60.85           C  
ATOM   2630  CG  GLN A 414      84.144  33.237 -24.103  1.00 60.98           C  
ATOM   2631  CD  GLN A 414      82.954  33.167 -23.202  1.00 60.64           C  
ATOM   2632  OE1 GLN A 414      81.851  32.827 -23.643  1.00 61.87           O  
ATOM   2633  NE2 GLN A 414      83.152  33.467 -21.926  1.00 60.33           N  
ATOM   2634  N   THR A 415      83.783  28.849 -24.551  1.00 61.27           N  
ATOM   2635  CA  THR A 415      83.680  27.586 -25.251  1.00 62.07           C  
ATOM   2636  C   THR A 415      82.525  27.674 -26.227  1.00 62.39           C  
ATOM   2637  O   THR A 415      81.690  28.578 -26.128  1.00 62.40           O  
ATOM   2638  CB  THR A 415      83.478  26.407 -24.273  1.00 61.48           C  
ATOM   2639  OG1 THR A 415      82.213  26.539 -23.613  1.00 59.22           O  
ATOM   2640  CG2 THR A 415      84.587  26.361 -23.215  1.00 59.94           C  
ATOM   2641  N   GLY A 416      82.471  26.750 -27.168  1.00 62.94           N  
ATOM   2642  CA  GLY A 416      81.409  26.742 -28.155  1.00 63.68           C  
ATOM   2643  C   GLY A 416      81.925  26.144 -29.442  1.00 66.07           C  
ATOM   2644  O   GLY A 416      83.091  25.761 -29.526  1.00 65.80           O  
ATOM   2645  N   LYS A 417      81.074  26.091 -30.453  1.00 66.35           N  
ATOM   2646  CA  LYS A 417      81.453  25.486 -31.720  1.00 67.20           C  
ATOM   2647  C   LYS A 417      82.539  26.256 -32.484  1.00 68.11           C  
ATOM   2648  O   LYS A 417      83.224  25.681 -33.319  1.00 67.17           O  
ATOM   2649  CB  LYS A 417      80.205  25.222 -32.575  1.00 66.05           C  
ATOM   2650  CG  LYS A 417      79.288  26.419 -32.834  1.00 66.76           C  
ATOM   2651  CD  LYS A 417      78.119  26.052 -33.790  1.00 65.88           C  
ATOM   2652  CE  LYS A 417      77.157  25.018 -33.171  1.00 63.74           C  
ATOM   2653  NZ  LYS A 417      77.451  23.619 -33.603  1.00 63.50           N  
ATOM   2654  N   ILE A 418      82.732  27.544 -32.200  1.00 67.42           N  
ATOM   2655  CA  ILE A 418      83.826  28.272 -32.848  1.00 68.66           C  
ATOM   2656  C   ILE A 418      85.039  28.281 -31.935  1.00 61.27           C  
ATOM   2657  O   ILE A 418      86.151  27.937 -32.351  1.00 74.12           O  
ATOM   2658  CB  ILE A 418      83.412  29.714 -33.243  1.00 68.31           C  
ATOM   2659  CG1 ILE A 418      82.857  29.724 -34.677  1.00 68.79           C  
ATOM   2660  CG2 ILE A 418      84.582  30.721 -33.112  1.00 67.94           C  
ATOM   2661  CD1 ILE A 418      81.713  28.756 -34.931  1.00 69.37           C  
ATOM   2662  N   ALA A 419      84.809  28.628 -30.672  1.00 68.13           N  
ATOM   2663  CA  ALA A 419      85.880  28.707 -29.684  1.00 66.17           C  
ATOM   2664  C   ALA A 419      86.603  27.377 -29.537  1.00 66.51           C  
ATOM   2665  O   ALA A 419      87.801  27.348 -29.258  1.00 65.81           O  
ATOM   2666  CB  ALA A 419      85.311  29.130 -28.342  1.00 64.62           C  
ATOM   2667  N   ASP A 420      85.882  26.267 -29.663  1.00 66.37           N  
ATOM   2668  CA  ASP A 420      86.501  24.968 -29.504  1.00 66.60           C  
ATOM   2669  C   ASP A 420      86.949  24.335 -30.823  1.00 67.54           C  
ATOM   2670  O   ASP A 420      87.911  23.565 -30.839  1.00 66.74           O  
ATOM   2671  CB  ASP A 420      85.533  24.021 -28.781  1.00 67.12           C  
ATOM   2672  CG  ASP A 420      86.208  22.779 -28.205  1.00 67.29           C  
ATOM   2673  OD1 ASP A 420      87.045  22.934 -27.341  1.00 67.05           O  
ATOM   2674  OD2 ASP A 420      85.870  21.692 -28.609  1.00 66.86           O  
ATOM   2675  N   TYR A 421      86.249  24.610 -31.930  1.00 66.49           N  
ATOM   2676  CA  TYR A 421      86.542  23.849 -33.146  1.00 68.72           C  
ATOM   2677  C   TYR A 421      87.422  24.549 -34.179  1.00 68.62           C  
ATOM   2678  O   TYR A 421      88.177  23.876 -34.882  1.00 68.32           O  
ATOM   2679  CB  TYR A 421      85.252  23.429 -33.856  1.00 67.34           C  
ATOM   2680  CG  TYR A 421      84.222  22.678 -33.009  1.00 67.37           C  
ATOM   2681  CD1 TYR A 421      82.921  22.642 -33.461  1.00 67.05           C  
ATOM   2682  CD2 TYR A 421      84.548  22.056 -31.803  1.00 67.25           C  
ATOM   2683  CE1 TYR A 421      81.949  22.002 -32.736  1.00 66.35           C  
ATOM   2684  CE2 TYR A 421      83.563  21.419 -31.075  1.00 66.87           C  
ATOM   2685  CZ  TYR A 421      82.270  21.395 -31.541  1.00 65.90           C  
ATOM   2686  OH  TYR A 421      81.282  20.772 -30.829  1.00 63.67           O  
ATOM   2687  N   ASN A 422      87.296  25.866 -34.348  1.00 68.44           N  
ATOM   2688  CA  ASN A 422      88.068  26.503 -35.414  1.00 68.54           C  
ATOM   2689  C   ASN A 422      89.003  27.625 -34.973  1.00 67.47           C  
ATOM   2690  O   ASN A 422      90.011  27.862 -35.633  1.00 68.07           O  
ATOM   2691  CB  ASN A 422      87.155  26.935 -36.549  1.00 68.27           C  
ATOM   2692  CG  ASN A 422      86.035  27.787 -36.111  1.00 70.29           C  
ATOM   2693  OD1 ASN A 422      84.904  27.304 -36.012  1.00 68.74           O  
ATOM   2694  ND2 ASN A 422      86.302  29.018 -35.836  1.00 68.40           N  
ATOM   2695  N   TYR A 423      88.703  28.308 -33.872  1.00 67.31           N  
ATOM   2696  CA  TYR A 423      89.597  29.379 -33.439  1.00 66.48           C  
ATOM   2697  C   TYR A 423      89.656  29.514 -31.932  1.00 66.08           C  
ATOM   2698  O   TYR A 423      88.767  30.091 -31.302  1.00 65.78           O  
ATOM   2699  CB  TYR A 423      89.219  30.726 -34.041  1.00 65.89           C  
ATOM   2700  CG  TYR A 423      90.248  31.760 -33.725  1.00 65.57           C  
ATOM   2701  CD1 TYR A 423      91.462  31.731 -34.395  1.00 65.06           C  
ATOM   2702  CD2 TYR A 423      90.003  32.723 -32.768  1.00 64.73           C  
ATOM   2703  CE1 TYR A 423      92.420  32.661 -34.112  1.00 64.04           C  
ATOM   2704  CE2 TYR A 423      90.967  33.651 -32.492  1.00 64.43           C  
ATOM   2705  CZ  TYR A 423      92.164  33.615 -33.162  1.00 63.82           C  
ATOM   2706  OH  TYR A 423      93.119  34.539 -32.898  1.00 62.13           O  
ATOM   2707  N   LYS A 424      90.726  28.989 -31.361  1.00 64.59           N  
ATOM   2708  CA  LYS A 424      90.909  28.949 -29.920  1.00 63.48           C  
ATOM   2709  C   LYS A 424      91.933  29.965 -29.413  1.00 62.76           C  
ATOM   2710  O   LYS A 424      93.055  30.042 -29.920  1.00 62.49           O  
ATOM   2711  CB  LYS A 424      91.343  27.530 -29.524  1.00 64.07           C  
ATOM   2712  CG  LYS A 424      91.725  27.313 -28.062  1.00 62.96           C  
ATOM   2713  CD  LYS A 424      90.522  27.365 -27.141  1.00 63.37           C  
ATOM   2714  CE  LYS A 424      90.904  26.938 -25.735  1.00 62.66           C  
ATOM   2715  NZ  LYS A 424      89.754  26.985 -24.809  1.00 59.39           N  
ATOM   2716  N   LEU A 425      91.562  30.707 -28.371  1.00 62.24           N  
ATOM   2717  CA  LEU A 425      92.505  31.584 -27.686  1.00 60.72           C  
ATOM   2718  C   LEU A 425      92.958  30.929 -26.393  1.00 60.83           C  
ATOM   2719  O   LEU A 425      92.208  30.143 -25.819  1.00 60.25           O  
ATOM   2720  CB  LEU A 425      91.888  32.949 -27.346  1.00 60.29           C  
ATOM   2721  CG  LEU A 425      91.468  33.837 -28.502  1.00 60.31           C  
ATOM   2722  CD1 LEU A 425      90.844  35.100 -27.937  1.00 59.80           C  
ATOM   2723  CD2 LEU A 425      92.688  34.174 -29.356  1.00 60.00           C  
ATOM   2724  N   PRO A 426      94.162  31.246 -25.905  1.00 59.59           N  
ATOM   2725  CA  PRO A 426      94.650  30.871 -24.598  1.00 59.55           C  
ATOM   2726  C   PRO A 426      93.732  31.486 -23.559  1.00 58.27           C  
ATOM   2727  O   PRO A 426      93.220  32.581 -23.759  1.00 58.22           O  
ATOM   2728  CB  PRO A 426      96.034  31.528 -24.546  1.00 58.90           C  
ATOM   2729  CG  PRO A 426      96.431  31.743 -25.982  1.00 59.52           C  
ATOM   2730  CD  PRO A 426      95.136  31.992 -26.726  1.00 59.39           C  
ATOM   2731  N   ASP A 427      93.567  30.827 -22.422  1.00 58.66           N  
ATOM   2732  CA  ASP A 427      92.681  31.387 -21.405  1.00 58.21           C  
ATOM   2733  C   ASP A 427      93.417  32.452 -20.604  1.00 58.47           C  
ATOM   2734  O   ASP A 427      92.822  33.172 -19.802  1.00 58.52           O  
ATOM   2735  CB  ASP A 427      92.151  30.288 -20.495  1.00 57.71           C  
ATOM   2736  CG  ASP A 427      91.242  29.300 -21.236  1.00 56.04           C  
ATOM   2737  OD1 ASP A 427      90.441  29.716 -22.062  1.00 56.96           O  
ATOM   2738  OD2 ASP A 427      91.372  28.128 -20.978  1.00 53.48           O  
ATOM   2739  N   ASP A 428      94.714  32.558 -20.860  1.00 58.53           N  
ATOM   2740  CA  ASP A 428      95.582  33.566 -20.286  1.00 58.25           C  
ATOM   2741  C   ASP A 428      95.956  34.588 -21.361  1.00 57.60           C  
ATOM   2742  O   ASP A 428      96.945  35.313 -21.237  1.00 57.73           O  
ATOM   2743  CB  ASP A 428      96.823  32.910 -19.682  1.00 59.23           C  
ATOM   2744  CG  ASP A 428      97.595  32.076 -20.692  1.00 59.09           C  
ATOM   2745  OD1 ASP A 428      98.753  31.816 -20.466  1.00 58.67           O  
ATOM   2746  OD2 ASP A 428      96.992  31.647 -21.656  1.00 58.76           O  
ATOM   2747  N   PHE A 429      95.141  34.642 -22.414  1.00 57.94           N  
ATOM   2748  CA  PHE A 429      95.355  35.539 -23.534  1.00 56.94           C  
ATOM   2749  C   PHE A 429      95.511  36.981 -23.128  1.00 55.69           C  
ATOM   2750  O   PHE A 429      94.715  37.525 -22.363  1.00 55.22           O  
ATOM   2751  CB  PHE A 429      94.174  35.435 -24.498  1.00 57.27           C  
ATOM   2752  CG  PHE A 429      94.161  36.458 -25.587  1.00 56.29           C  
ATOM   2753  CD1 PHE A 429      94.977  36.351 -26.692  1.00 56.31           C  
ATOM   2754  CD2 PHE A 429      93.305  37.546 -25.492  1.00 55.53           C  
ATOM   2755  CE1 PHE A 429      94.940  37.312 -27.676  1.00 55.78           C  
ATOM   2756  CE2 PHE A 429      93.267  38.500 -26.470  1.00 55.53           C  
ATOM   2757  CZ  PHE A 429      94.086  38.386 -27.564  1.00 55.90           C  
ATOM   2758  N   THR A 430      96.536  37.609 -23.679  1.00 55.25           N  
ATOM   2759  CA  THR A 430      96.784  39.009 -23.439  1.00 54.55           C  
ATOM   2760  C   THR A 430      96.583  39.774 -24.723  1.00 54.52           C  
ATOM   2761  O   THR A 430      97.273  39.537 -25.718  1.00 54.18           O  
ATOM   2762  CB  THR A 430      98.214  39.242 -22.918  1.00 54.19           C  
ATOM   2763  OG1 THR A 430      98.385  38.560 -21.671  1.00 55.35           O  
ATOM   2764  CG2 THR A 430      98.491  40.724 -22.726  1.00 51.88           C  
ATOM   2765  N   GLY A 431      95.638  40.695 -24.703  1.00 54.15           N  
ATOM   2766  CA  GLY A 431      95.372  41.482 -25.885  1.00 54.39           C  
ATOM   2767  C   GLY A 431      93.938  41.942 -26.009  1.00 55.09           C  
ATOM   2768  O   GLY A 431      93.212  42.010 -25.007  1.00 54.95           O  
ATOM   2769  N   CYS A 432      93.573  42.341 -27.242  1.00 55.25           N  
ATOM   2770  CA  CYS A 432      92.280  42.947 -27.562  1.00 56.57           C  
ATOM   2771  C   CYS A 432      91.678  42.313 -28.823  1.00 56.72           C  
ATOM   2772  O   CYS A 432      92.388  42.053 -29.800  1.00 56.91           O  
ATOM   2773  CB  CYS A 432      92.432  44.484 -27.761  1.00 56.86           C  
ATOM   2774  SG  CYS A 432      93.215  45.406 -26.334  1.00 56.17           S  
ATOM   2775  N   VAL A 433      90.354  42.092 -28.797  1.00 57.62           N  
ATOM   2776  CA  VAL A 433      89.581  41.561 -29.919  1.00 58.68           C  
ATOM   2777  C   VAL A 433      88.754  42.674 -30.540  1.00 59.28           C  
ATOM   2778  O   VAL A 433      87.871  43.253 -29.901  1.00 59.37           O  
ATOM   2779  CB  VAL A 433      88.674  40.416 -29.441  1.00 58.56           C  
ATOM   2780  CG1 VAL A 433      87.842  39.870 -30.596  1.00 59.86           C  
ATOM   2781  CG2 VAL A 433      89.545  39.316 -28.838  1.00 58.58           C  
ATOM   2782  N   ILE A 434      89.060  42.987 -31.789  1.00 60.54           N  
ATOM   2783  CA  ILE A 434      88.423  44.096 -32.470  1.00 61.18           C  
ATOM   2784  C   ILE A 434      87.598  43.587 -33.638  1.00 62.91           C  
ATOM   2785  O   ILE A 434      88.091  42.818 -34.461  1.00 62.80           O  
ATOM   2786  CB  ILE A 434      89.490  45.082 -32.968  1.00 61.41           C  
ATOM   2787  CG1 ILE A 434      90.331  45.578 -31.778  1.00 59.92           C  
ATOM   2788  CG2 ILE A 434      88.808  46.254 -33.656  1.00 61.64           C  
ATOM   2789  CD1 ILE A 434      91.601  46.300 -32.177  1.00 59.25           C  
ATOM   2790  N   ALA A 435      86.340  43.997 -33.722  1.00 62.83           N  
ATOM   2791  CA  ALA A 435      85.515  43.505 -34.821  1.00 64.35           C  
ATOM   2792  C   ALA A 435      84.507  44.538 -35.299  1.00 65.46           C  
ATOM   2793  O   ALA A 435      84.062  45.413 -34.547  1.00 64.60           O  
ATOM   2794  CB  ALA A 435      84.795  42.225 -34.416  1.00 64.85           C  
ATOM   2795  N   TRP A 436      84.147  44.412 -36.572  1.00 65.58           N  
ATOM   2796  CA  TRP A 436      83.155  45.266 -37.205  1.00 67.32           C  
ATOM   2797  C   TRP A 436      82.426  44.485 -38.277  1.00 66.70           C  
ATOM   2798  O   TRP A 436      82.967  43.515 -38.811  1.00 72.63           O  
ATOM   2799  CB  TRP A 436      83.850  46.491 -37.790  1.00 65.67           C  
ATOM   2800  CG  TRP A 436      84.843  46.199 -38.875  1.00 66.25           C  
ATOM   2801  CD1 TRP A 436      84.647  46.349 -40.209  1.00 66.38           C  
ATOM   2802  CD2 TRP A 436      86.191  45.687 -38.727  1.00 65.90           C  
ATOM   2803  NE1 TRP A 436      85.777  45.990 -40.896  1.00 66.59           N  
ATOM   2804  CE2 TRP A 436      86.726  45.578 -40.003  1.00 66.25           C  
ATOM   2805  CE3 TRP A 436      86.973  45.319 -37.631  1.00 64.78           C  
ATOM   2806  CZ2 TRP A 436      88.006  45.119 -40.216  1.00 65.96           C  
ATOM   2807  CZ3 TRP A 436      88.243  44.850 -37.847  1.00 65.17           C  
ATOM   2808  CH2 TRP A 436      88.745  44.756 -39.102  1.00 65.02           C  
ATOM   2809  N   ASN A 437      81.206  44.885 -38.612  1.00 68.30           N  
ATOM   2810  CA  ASN A 437      80.504  44.122 -39.634  1.00 69.20           C  
ATOM   2811  C   ASN A 437      81.035  44.480 -41.006  1.00 68.94           C  
ATOM   2812  O   ASN A 437      81.506  45.595 -41.234  1.00 70.41           O  
ATOM   2813  CB  ASN A 437      79.001  44.315 -39.578  1.00 70.13           C  
ATOM   2814  CG  ASN A 437      78.553  45.603 -40.107  1.00 71.52           C  
ATOM   2815  OD1 ASN A 437      78.510  45.791 -41.336  1.00 72.71           O  
ATOM   2816  ND2 ASN A 437      78.213  46.512 -39.228  1.00 71.16           N  
ATOM   2817  N   SER A 438      80.869  43.557 -41.935  1.00 70.13           N  
ATOM   2818  CA  SER A 438      81.225  43.763 -43.329  1.00 71.64           C  
ATOM   2819  C   SER A 438      80.013  43.510 -44.210  1.00 62.82           C  
ATOM   2820  O   SER A 438      80.118  42.964 -45.320  1.00102.42           O  
ATOM   2821  CB  SER A 438      82.339  42.835 -43.714  1.00 71.33           C  
ATOM   2822  OG  SER A 438      81.965  41.514 -43.482  1.00 71.35           O  
ATOM   2823  N   ASN A 439      78.848  43.909 -43.710  1.00 76.82           N  
ATOM   2824  CA  ASN A 439      77.599  43.669 -44.412  1.00 70.59           C  
ATOM   2825  C   ASN A 439      77.535  44.460 -45.708  1.00 74.48           C  
ATOM   2826  O   ASN A 439      76.811  44.103 -46.633  1.00 74.34           O  
ATOM   2827  CB  ASN A 439      76.424  44.004 -43.524  1.00 74.29           C  
ATOM   2828  CG  ASN A 439      75.170  43.406 -44.030  1.00 75.36           C  
ATOM   2829  OD1 ASN A 439      75.129  42.190 -44.233  1.00 75.39           O  
ATOM   2830  ND2 ASN A 439      74.153  44.208 -44.236  1.00 75.25           N  
ATOM   2831  N   ASN A 440      78.294  45.543 -45.769  1.00 73.61           N  
ATOM   2832  CA  ASN A 440      78.336  46.392 -46.939  1.00 74.22           C  
ATOM   2833  C   ASN A 440      79.603  46.164 -47.747  1.00 74.31           C  
ATOM   2834  O   ASN A 440      79.986  47.012 -48.552  1.00 75.20           O  
ATOM   2835  CB  ASN A 440      78.231  47.839 -46.521  1.00 74.70           C  
ATOM   2836  CG  ASN A 440      79.390  48.244 -45.680  1.00 75.07           C  
ATOM   2837  OD1 ASN A 440      79.988  47.401 -44.994  1.00 73.87           O  
ATOM   2838  ND2 ASN A 440      79.724  49.507 -45.706  1.00 75.30           N  
ATOM   2839  N   LEU A 441      80.260  45.026 -47.536  1.00 73.22           N  
ATOM   2840  CA  LEU A 441      81.481  44.751 -48.276  1.00 74.21           C  
ATOM   2841  C   LEU A 441      81.611  43.276 -48.667  1.00 74.64           C  
ATOM   2842  O   LEU A 441      81.828  42.967 -49.839  1.00 73.89           O  
ATOM   2843  CB  LEU A 441      82.687  45.216 -47.454  1.00 74.23           C  
ATOM   2844  CG  LEU A 441      84.050  45.213 -48.162  1.00 73.74           C  
ATOM   2845  CD1 LEU A 441      84.916  46.315 -47.571  1.00 73.32           C  
ATOM   2846  CD2 LEU A 441      84.731  43.878 -47.959  1.00 72.74           C  
ATOM   2847  N   ASP A 442      81.522  42.366 -47.695  1.00 72.87           N  
ATOM   2848  CA  ASP A 442      81.704  40.947 -48.004  1.00 74.42           C  
ATOM   2849  C   ASP A 442      80.402  40.281 -48.420  1.00 74.75           C  
ATOM   2850  O   ASP A 442      80.402  39.348 -49.218  1.00 75.61           O  
ATOM   2851  CB  ASP A 442      82.301  40.177 -46.820  1.00 74.51           C  
ATOM   2852  CG  ASP A 442      83.746  40.570 -46.490  1.00 72.23           C  
ATOM   2853  OD1 ASP A 442      84.570  40.555 -47.370  1.00 73.09           O  
ATOM   2854  OD2 ASP A 442      84.010  40.859 -45.357  1.00 72.18           O  
ATOM   2855  N   SER A 443      79.286  40.747 -47.878  1.00 74.74           N  
ATOM   2856  CA  SER A 443      77.997  40.144 -48.220  1.00 73.42           C  
ATOM   2857  C   SER A 443      77.649  40.438 -49.683  1.00 76.59           C  
ATOM   2858  O   SER A 443      78.021  41.492 -50.203  1.00 76.30           O  
ATOM   2859  CB  SER A 443      76.912  40.662 -47.308  1.00 76.30           C  
ATOM   2860  OG  SER A 443      77.136  40.262 -45.995  1.00 73.48           O  
ATOM   2861  N   LYS A 444      76.921  39.510 -50.340  1.00 75.42           N  
ATOM   2862  CA  LYS A 444      76.498  39.660 -51.742  1.00 76.81           C  
ATOM   2863  C   LYS A 444      75.028  39.301 -51.920  1.00 76.50           C  
ATOM   2864  O   LYS A 444      74.448  38.557 -51.130  1.00 76.71           O  
ATOM   2865  CB  LYS A 444      77.362  38.795 -52.693  1.00 77.09           C  
ATOM   2866  CG  LYS A 444      78.877  39.204 -52.803  1.00 76.55           C  
ATOM   2867  CD  LYS A 444      79.643  38.331 -53.860  1.00 76.95           C  
ATOM   2868  CE  LYS A 444      81.147  38.731 -53.991  1.00 77.10           C  
ATOM   2869  NZ  LYS A 444      81.846  37.949 -55.075  1.00 76.42           N  
ATOM   2870  N   GLY A 447      74.875  35.303 -52.874  1.00 76.48           N  
ATOM   2871  CA  GLY A 447      75.473  35.298 -51.547  1.00 77.17           C  
ATOM   2872  C   GLY A 447      76.975  35.034 -51.643  1.00 77.10           C  
ATOM   2873  O   GLY A 447      77.446  34.443 -52.621  1.00 76.80           O  
ATOM   2874  N   ASN A 448      77.730  35.463 -50.617  1.00 76.80           N  
ATOM   2875  CA  ASN A 448      79.178  35.246 -50.518  1.00 77.55           C  
ATOM   2876  C   ASN A 448      79.463  33.930 -49.812  1.00 77.00           C  
ATOM   2877  O   ASN A 448      79.252  33.806 -48.604  1.00 75.35           O  
ATOM   2878  CB  ASN A 448      79.871  36.398 -49.818  1.00 76.87           C  
ATOM   2879  CG  ASN A 448      81.397  36.256 -49.818  1.00 75.47           C  
ATOM   2880  OD1 ASN A 448      81.939  35.145 -49.711  1.00 75.34           O  
ATOM   2881  ND2 ASN A 448      82.089  37.361 -49.949  1.00 75.62           N  
ATOM   2882  N   TYR A 449      79.916  32.948 -50.580  1.00 76.51           N  
ATOM   2883  CA  TYR A 449      80.154  31.599 -50.083  1.00 74.94           C  
ATOM   2884  C   TYR A 449      81.634  31.272 -49.992  1.00 76.31           C  
ATOM   2885  O   TYR A 449      82.022  30.103 -50.020  1.00 74.91           O  
ATOM   2886  CB  TYR A 449      79.457  30.574 -50.974  1.00 77.27           C  
ATOM   2887  CG  TYR A 449      77.962  30.593 -50.877  1.00 76.92           C  
ATOM   2888  CD1 TYR A 449      77.321  29.794 -49.945  1.00 76.31           C  
ATOM   2889  CD2 TYR A 449      77.229  31.409 -51.711  1.00 77.13           C  
ATOM   2890  CE1 TYR A 449      75.950  29.811 -49.858  1.00 76.83           C  
ATOM   2891  CE2 TYR A 449      75.857  31.434 -51.622  1.00 77.68           C  
ATOM   2892  CZ  TYR A 449      75.216  30.638 -50.702  1.00 77.52           C  
ATOM   2893  OH  TYR A 449      73.847  30.659 -50.614  1.00 78.59           O  
ATOM   2894  N   ASN A 450      82.468  32.296 -49.897  1.00 74.41           N  
ATOM   2895  CA  ASN A 450      83.908  32.081 -49.848  1.00 75.19           C  
ATOM   2896  C   ASN A 450      84.429  31.919 -48.422  1.00 74.36           C  
ATOM   2897  O   ASN A 450      85.635  31.779 -48.212  1.00 73.16           O  
ATOM   2898  CB  ASN A 450      84.632  33.225 -50.529  1.00 75.46           C  
ATOM   2899  CG  ASN A 450      84.396  33.275 -52.016  1.00 75.25           C  
ATOM   2900  OD1 ASN A 450      84.196  32.250 -52.681  1.00 75.00           O  
ATOM   2901  ND2 ASN A 450      84.420  34.467 -52.554  1.00 75.34           N  
ATOM   2902  N   TYR A 451      83.533  31.946 -47.442  1.00 74.03           N  
ATOM   2903  CA  TYR A 451      83.948  31.837 -46.052  1.00 73.63           C  
ATOM   2904  C   TYR A 451      83.564  30.519 -45.405  1.00 74.61           C  
ATOM   2905  O   TYR A 451      82.386  30.217 -45.190  1.00 73.53           O  
ATOM   2906  CB  TYR A 451      83.445  33.049 -45.276  1.00 73.72           C  
ATOM   2907  CG  TYR A 451      84.185  34.248 -45.759  1.00 73.31           C  
ATOM   2908  CD1 TYR A 451      83.605  35.214 -46.572  1.00 73.24           C  
ATOM   2909  CD2 TYR A 451      85.502  34.333 -45.429  1.00 71.71           C  
ATOM   2910  CE1 TYR A 451      84.396  36.269 -47.028  1.00 72.98           C  
ATOM   2911  CE2 TYR A 451      86.270  35.343 -45.870  1.00 71.38           C  
ATOM   2912  CZ  TYR A 451      85.745  36.314 -46.669  1.00 72.11           C  
ATOM   2913  OH  TYR A 451      86.562  37.324 -47.120  1.00 71.55           O  
ATOM   2914  N   LEU A 452      84.599  29.736 -45.104  1.00 73.02           N  
ATOM   2915  CA  LEU A 452      84.457  28.391 -44.559  1.00 73.06           C  
ATOM   2916  C   LEU A 452      84.983  28.315 -43.125  1.00 71.45           C  
ATOM   2917  O   LEU A 452      85.960  28.976 -42.765  1.00 71.01           O  
ATOM   2918  CB  LEU A 452      85.168  27.383 -45.488  1.00 72.53           C  
ATOM   2919  CG  LEU A 452      85.002  25.872 -45.161  1.00 73.03           C  
ATOM   2920  CD1 LEU A 452      84.912  25.098 -46.467  1.00 73.78           C  
ATOM   2921  CD2 LEU A 452      86.185  25.361 -44.344  1.00 72.83           C  
ATOM   2922  N   TYR A 453      84.313  27.513 -42.315  1.00 71.62           N  
ATOM   2923  CA  TYR A 453      84.682  27.283 -40.931  1.00 71.94           C  
ATOM   2924  C   TYR A 453      84.657  25.781 -40.637  1.00 73.09           C  
ATOM   2925  O   TYR A 453      84.017  25.017 -41.365  1.00 75.02           O  
ATOM   2926  CB  TYR A 453      83.742  28.069 -40.016  1.00 72.26           C  
ATOM   2927  CG  TYR A 453      82.328  27.616 -40.023  1.00 73.04           C  
ATOM   2928  CD1 TYR A 453      81.884  26.736 -39.068  1.00 73.09           C  
ATOM   2929  CD2 TYR A 453      81.468  28.090 -40.991  1.00 72.51           C  
ATOM   2930  CE1 TYR A 453      80.572  26.330 -39.073  1.00 73.07           C  
ATOM   2931  CE2 TYR A 453      80.160  27.684 -41.001  1.00 74.20           C  
ATOM   2932  CZ  TYR A 453      79.710  26.812 -40.047  1.00 73.78           C  
ATOM   2933  OH  TYR A 453      78.397  26.412 -40.052  1.00 75.04           O  
ATOM   2934  N   ARG A 454      85.376  25.350 -39.584  1.00 72.21           N  
ATOM   2935  CA  ARG A 454      85.452  23.932 -39.204  1.00 72.43           C  
ATOM   2936  C   ARG A 454      85.346  23.781 -37.686  1.00 70.91           C  
ATOM   2937  O   ARG A 454      84.588  22.953 -37.177  1.00 71.29           O  
ATOM   2938  CB  ARG A 454      86.771  23.328 -39.730  1.00 72.55           C  
ATOM   2939  CG  ARG A 454      86.951  21.762 -39.590  1.00 72.94           C  
ATOM   2940  CD  ARG A 454      88.363  21.290 -39.973  1.00 72.08           C  
ATOM   2941  NE  ARG A 454      88.705  21.572 -41.414  1.00 71.38           N  
ATOM   2942  CZ  ARG A 454      89.908  21.285 -42.044  1.00 70.45           C  
ATOM   2943  NH1 ARG A 454      90.899  20.681 -41.409  1.00 70.33           N  
ATOM   2944  NH2 ARG A 454      90.080  21.621 -43.313  1.00 71.11           N  
ATOM   2945  N   LYS A 462      94.043  23.229 -29.919  1.00 62.22           N  
ATOM   2946  CA  LYS A 462      94.994  23.999 -29.134  1.00 62.34           C  
ATOM   2947  C   LYS A 462      94.900  25.498 -29.499  1.00 61.90           C  
ATOM   2948  O   LYS A 462      94.408  25.826 -30.587  1.00 62.67           O  
ATOM   2949  CB  LYS A 462      96.445  23.484 -29.354  1.00 61.52           C  
ATOM   2950  CG  LYS A 462      96.726  22.026 -28.857  1.00 60.94           C  
ATOM   2951  CD  LYS A 462      98.250  21.656 -28.932  1.00 60.05           C  
ATOM   2952  CE  LYS A 462      98.520  20.189 -28.481  1.00 60.39           C  
ATOM   2953  NZ  LYS A 462      99.985  19.880 -28.403  1.00 59.57           N  
ATOM   2954  N   PRO A 463      95.350  26.443 -28.612  1.00 62.22           N  
ATOM   2955  CA  PRO A 463      95.408  27.876 -28.862  1.00 61.96           C  
ATOM   2956  C   PRO A 463      96.235  28.193 -30.093  1.00 62.05           C  
ATOM   2957  O   PRO A 463      97.326  27.651 -30.274  1.00 62.49           O  
ATOM   2958  CB  PRO A 463      96.084  28.410 -27.601  1.00 61.28           C  
ATOM   2959  CG  PRO A 463      95.766  27.414 -26.528  1.00 61.75           C  
ATOM   2960  CD  PRO A 463      95.801  26.083 -27.221  1.00 61.94           C  
ATOM   2961  N   PHE A 464      95.704  29.070 -30.926  1.00 61.93           N  
ATOM   2962  CA  PHE A 464      96.351  29.492 -32.156  1.00 62.37           C  
ATOM   2963  C   PHE A 464      96.629  28.349 -33.134  1.00 62.54           C  
ATOM   2964  O   PHE A 464      97.523  28.453 -33.975  1.00 62.53           O  
ATOM   2965  CB  PHE A 464      97.638  30.263 -31.855  1.00 61.60           C  
ATOM   2966  CG  PHE A 464      97.398  31.479 -31.006  1.00 60.95           C  
ATOM   2967  CD1 PHE A 464      97.991  31.607 -29.767  1.00 60.58           C  
ATOM   2968  CD2 PHE A 464      96.560  32.495 -31.445  1.00 60.69           C  
ATOM   2969  CE1 PHE A 464      97.767  32.721 -28.991  1.00 60.28           C  
ATOM   2970  CE2 PHE A 464      96.328  33.605 -30.668  1.00 59.66           C  
ATOM   2971  CZ  PHE A 464      96.935  33.719 -29.439  1.00 59.03           C  
ATOM   2972  N   GLU A 465      95.831  27.283 -33.067  1.00 62.78           N  
ATOM   2973  CA  GLU A 465      95.927  26.203 -34.042  1.00 63.43           C  
ATOM   2974  C   GLU A 465      95.218  26.577 -35.350  1.00 64.29           C  
ATOM   2975  O   GLU A 465      94.105  27.112 -35.332  1.00 64.82           O  
ATOM   2976  CB  GLU A 465      95.319  24.919 -33.470  1.00 62.64           C  
ATOM   2977  CG  GLU A 465      95.478  23.690 -34.345  1.00 62.71           C  
ATOM   2978  CD  GLU A 465      94.865  22.467 -33.743  1.00 60.76           C  
ATOM   2979  OE1 GLU A 465      94.957  21.434 -34.349  1.00 60.52           O  
ATOM   2980  OE2 GLU A 465      94.292  22.559 -32.679  1.00 61.27           O  
ATOM   2981  N   ARG A 466      95.852  26.267 -36.482  1.00 64.91           N  
ATOM   2982  CA  ARG A 466      95.247  26.488 -37.796  1.00 65.95           C  
ATOM   2983  C   ARG A 466      94.932  25.146 -38.439  1.00 67.17           C  
ATOM   2984  O   ARG A 466      95.810  24.504 -39.023  1.00 66.86           O  
ATOM   2985  CB  ARG A 466      96.186  27.263 -38.723  1.00 65.86           C  
ATOM   2986  CG  ARG A 466      96.552  28.664 -38.279  1.00 65.48           C  
ATOM   2987  CD  ARG A 466      97.620  29.276 -39.121  1.00 65.56           C  
ATOM   2988  NE  ARG A 466      97.139  29.750 -40.435  1.00 66.78           N  
ATOM   2989  CZ  ARG A 466      97.855  29.715 -41.592  1.00 68.14           C  
ATOM   2990  NH1 ARG A 466      99.065  29.195 -41.619  1.00 66.90           N  
ATOM   2991  NH2 ARG A 466      97.341  30.213 -42.710  1.00 68.57           N  
ATOM   2992  N   ASP A 467      93.688  24.697 -38.323  1.00 67.57           N  
ATOM   2993  CA  ASP A 467      93.345  23.365 -38.818  1.00 68.55           C  
ATOM   2994  C   ASP A 467      93.024  23.399 -40.316  1.00 69.50           C  
ATOM   2995  O   ASP A 467      91.857  23.485 -40.703  1.00 69.64           O  
ATOM   2996  CB  ASP A 467      92.163  22.768 -38.047  1.00 69.23           C  
ATOM   2997  CG  ASP A 467      91.924  21.296 -38.404  1.00 70.42           C  
ATOM   2998  OD1 ASP A 467      92.738  20.741 -39.111  1.00 70.26           O  
ATOM   2999  OD2 ASP A 467      90.931  20.745 -37.984  1.00 70.86           O  
ATOM   3000  N   ILE A 468      94.082  23.360 -41.143  1.00 69.50           N  
ATOM   3001  CA  ILE A 468      94.002  23.478 -42.603  1.00 69.72           C  
ATOM   3002  C   ILE A 468      93.580  22.125 -43.186  1.00 69.40           C  
ATOM   3003  O   ILE A 468      92.820  22.045 -44.160  1.00 69.22           O  
ATOM   3004  CB  ILE A 468      95.388  23.935 -43.211  1.00 69.28           C  
ATOM   3005  CG1 ILE A 468      95.902  25.333 -42.547  1.00 68.76           C  
ATOM   3006  CG2 ILE A 468      95.313  24.082 -44.788  1.00 70.32           C  
ATOM   3007  CD1 ILE A 468      94.956  26.547 -42.699  1.00 69.05           C  
ATOM   3008  N   TYR A 489      80.657  12.292 -44.375  1.00 81.97           N  
ATOM   3009  CA  TYR A 489      80.179  13.331 -43.473  1.00 81.67           C  
ATOM   3010  C   TYR A 489      81.383  14.188 -43.051  1.00 81.26           C  
ATOM   3011  O   TYR A 489      82.227  13.741 -42.265  1.00 80.96           O  
ATOM   3012  CB  TYR A 489      79.452  12.707 -42.242  1.00 82.28           C  
ATOM   3013  CG  TYR A 489      78.651  13.735 -41.367  1.00 82.14           C  
ATOM   3014  CD1 TYR A 489      77.213  13.886 -41.561  1.00 82.37           C  
ATOM   3015  CD2 TYR A 489      79.329  14.554 -40.367  1.00 82.24           C  
ATOM   3016  CE1 TYR A 489      76.472  14.830 -40.777  1.00 82.95           C  
ATOM   3017  CE2 TYR A 489      78.581  15.500 -39.588  1.00 82.30           C  
ATOM   3018  CZ  TYR A 489      77.154  15.642 -39.789  1.00 82.75           C  
ATOM   3019  OH  TYR A 489      76.431  16.560 -39.042  1.00 82.32           O  
ATOM   3020  N   PHE A 490      81.474  15.416 -43.589  1.00 80.97           N  
ATOM   3021  CA  PHE A 490      82.599  16.322 -43.335  1.00 78.83           C  
ATOM   3022  C   PHE A 490      82.356  17.254 -42.144  1.00 79.05           C  
ATOM   3023  O   PHE A 490      81.221  17.664 -41.911  1.00 78.87           O  
ATOM   3024  CB  PHE A 490      82.874  17.184 -44.564  1.00 79.36           C  
ATOM   3025  CG  PHE A 490      83.470  16.448 -45.702  1.00 80.56           C  
ATOM   3026  CD1 PHE A 490      82.665  15.834 -46.646  1.00 80.74           C  
ATOM   3027  CD2 PHE A 490      84.846  16.375 -45.844  1.00 80.56           C  
ATOM   3028  CE1 PHE A 490      83.222  15.163 -47.711  1.00 81.21           C  
ATOM   3029  CE2 PHE A 490      85.408  15.708 -46.906  1.00 80.81           C  
ATOM   3030  CZ  PHE A 490      84.592  15.101 -47.845  1.00 80.98           C  
ATOM   3031  N   PRO A 491      83.410  17.597 -41.385  1.00 77.73           N  
ATOM   3032  CA  PRO A 491      83.478  18.661 -40.389  1.00 76.73           C  
ATOM   3033  C   PRO A 491      83.453  20.071 -40.999  1.00 82.65           C  
ATOM   3034  O   PRO A 491      83.384  21.055 -40.267  1.00 72.91           O  
ATOM   3035  CB  PRO A 491      84.833  18.409 -39.710  1.00 76.87           C  
ATOM   3036  CG  PRO A 491      85.182  16.986 -40.023  1.00 78.38           C  
ATOM   3037  CD  PRO A 491      84.599  16.720 -41.384  1.00 78.96           C  
ATOM   3038  N   LEU A 492      83.563  20.170 -42.323  1.00 74.80           N  
ATOM   3039  CA  LEU A 492      83.671  21.463 -42.997  1.00 75.57           C  
ATOM   3040  C   LEU A 492      82.315  22.035 -43.397  1.00 75.22           C  
ATOM   3041  O   LEU A 492      81.536  21.390 -44.098  1.00 75.97           O  
ATOM   3042  CB  LEU A 492      84.515  21.327 -44.276  1.00 76.30           C  
ATOM   3043  CG  LEU A 492      86.042  21.257 -44.109  1.00 74.55           C  
ATOM   3044  CD1 LEU A 492      86.457  19.888 -43.543  1.00 75.51           C  
ATOM   3045  CD2 LEU A 492      86.696  21.499 -45.466  1.00 74.93           C  
ATOM   3046  N   GLN A 493      82.052  23.264 -42.956  1.00 74.60           N  
ATOM   3047  CA  GLN A 493      80.815  23.980 -43.256  1.00 73.41           C  
ATOM   3048  C   GLN A 493      81.109  25.411 -43.685  1.00 78.76           C  
ATOM   3049  O   GLN A 493      82.146  25.958 -43.332  1.00 77.13           O  
ATOM   3050  CB  GLN A 493      79.870  23.970 -42.058  1.00 75.12           C  
ATOM   3051  CG  GLN A 493      79.245  22.619 -41.750  1.00 75.81           C  
ATOM   3052  CD  GLN A 493      80.051  21.775 -40.783  1.00 75.52           C  
ATOM   3053  OE1 GLN A 493      80.539  22.287 -39.772  1.00 76.26           O  
ATOM   3054  NE2 GLN A 493      80.179  20.482 -41.072  1.00 76.90           N  
ATOM   3055  N   SER A 494      80.196  26.036 -44.426  1.00 73.19           N  
ATOM   3056  CA  SER A 494      80.423  27.412 -44.861  1.00 73.61           C  
ATOM   3057  C   SER A 494      79.166  28.264 -44.791  1.00 74.05           C  
ATOM   3058  O   SER A 494      78.057  27.743 -44.644  1.00 74.21           O  
ATOM   3059  CB  SER A 494      80.950  27.411 -46.277  1.00 74.08           C  
ATOM   3060  OG  SER A 494      80.000  26.892 -47.156  1.00 73.68           O  
ATOM   3061  N   TYR A 495      79.353  29.579 -44.877  1.00 73.86           N  
ATOM   3062  CA  TYR A 495      78.236  30.518 -44.836  1.00 75.34           C  
ATOM   3063  C   TYR A 495      77.969  31.157 -46.179  1.00 75.81           C  
ATOM   3064  O   TYR A 495      78.900  31.424 -46.935  1.00 76.68           O  
ATOM   3065  CB  TYR A 495      78.509  31.662 -43.861  1.00 75.15           C  
ATOM   3066  CG  TYR A 495      78.596  31.275 -42.424  1.00 74.37           C  
ATOM   3067  CD1 TYR A 495      77.451  30.873 -41.766  1.00 74.89           C  
ATOM   3068  CD2 TYR A 495      79.802  31.356 -41.744  1.00 74.73           C  
ATOM   3069  CE1 TYR A 495      77.511  30.537 -40.434  1.00 74.54           C  
ATOM   3070  CE2 TYR A 495      79.860  31.028 -40.406  1.00 73.88           C  
ATOM   3071  CZ  TYR A 495      78.716  30.616 -39.759  1.00 73.78           C  
ATOM   3072  OH  TYR A 495      78.734  30.280 -38.443  1.00 73.27           O  
ATOM   3073  N   GLY A 496      76.698  31.460 -46.438  1.00 75.79           N  
ATOM   3074  CA  GLY A 496      76.300  32.268 -47.587  1.00 76.89           C  
ATOM   3075  C   GLY A 496      75.880  33.627 -47.077  1.00 76.98           C  
ATOM   3076  O   GLY A 496      74.739  33.815 -46.648  1.00 76.26           O  
ATOM   3077  N   PHE A 497      76.802  34.574 -47.073  1.00 73.96           N  
ATOM   3078  CA  PHE A 497      76.488  35.864 -46.485  1.00 75.81           C  
ATOM   3079  C   PHE A 497      75.776  36.790 -47.463  1.00 71.61           C  
ATOM   3080  O   PHE A 497      76.251  37.039 -48.579  1.00 80.34           O  
ATOM   3081  CB  PHE A 497      77.743  36.532 -45.932  1.00 76.29           C  
ATOM   3082  CG  PHE A 497      78.320  35.872 -44.679  1.00 75.34           C  
ATOM   3083  CD1 PHE A 497      79.593  35.308 -44.692  1.00 75.41           C  
ATOM   3084  CD2 PHE A 497      77.591  35.819 -43.486  1.00 76.00           C  
ATOM   3085  CE1 PHE A 497      80.119  34.732 -43.546  1.00 74.84           C  
ATOM   3086  CE2 PHE A 497      78.117  35.239 -42.353  1.00 75.17           C  
ATOM   3087  CZ  PHE A 497      79.380  34.703 -42.381  1.00 73.87           C  
ATOM   3088  N   GLN A 498      74.622  37.290 -47.029  1.00 78.85           N  
ATOM   3089  CA  GLN A 498      73.780  38.172 -47.824  1.00 77.81           C  
ATOM   3090  C   GLN A 498      73.473  39.429 -47.012  1.00 74.95           C  
ATOM   3091  O   GLN A 498      73.323  39.343 -45.794  1.00 75.62           O  
ATOM   3092  CB  GLN A 498      72.490  37.435 -48.221  1.00 76.32           C  
ATOM   3093  CG  GLN A 498      72.725  36.242 -49.139  1.00 77.06           C  
ATOM   3094  CD  GLN A 498      71.451  35.511 -49.513  1.00 77.31           C  
ATOM   3095  OE1 GLN A 498      71.043  34.561 -48.841  1.00 76.14           O  
ATOM   3096  NE2 GLN A 498      70.815  35.952 -50.591  1.00 77.41           N  
ATOM   3097  N   PRO A 499      73.331  40.597 -47.658  1.00 80.66           N  
ATOM   3098  CA  PRO A 499      73.107  41.899 -47.047  1.00 75.63           C  
ATOM   3099  C   PRO A 499      71.782  41.980 -46.304  1.00 76.23           C  
ATOM   3100  O   PRO A 499      71.588  42.861 -45.464  1.00 75.99           O  
ATOM   3101  CB  PRO A 499      73.153  42.848 -48.253  1.00 76.12           C  
ATOM   3102  CG  PRO A 499      72.809  41.983 -49.444  1.00 76.65           C  
ATOM   3103  CD  PRO A 499      73.396  40.632 -49.125  1.00 76.15           C  
ATOM   3104  N   THR A 500      70.884  41.050 -46.607  1.00 76.57           N  
ATOM   3105  CA  THR A 500      69.566  41.003 -45.990  1.00 76.82           C  
ATOM   3106  C   THR A 500      69.457  40.057 -44.777  1.00 76.22           C  
ATOM   3107  O   THR A 500      68.367  39.921 -44.212  1.00 76.42           O  
ATOM   3108  CB  THR A 500      68.518  40.592 -47.038  1.00 76.85           C  
ATOM   3109  OG1 THR A 500      68.822  39.278 -47.532  1.00 76.47           O  
ATOM   3110  CG2 THR A 500      68.543  41.577 -48.192  1.00 76.78           C  
ATOM   3111  N   ASN A 501      70.565  39.391 -44.381  1.00 76.13           N  
ATOM   3112  CA  ASN A 501      70.591  38.465 -43.245  1.00 75.88           C  
ATOM   3113  C   ASN A 501      70.623  39.223 -41.913  1.00 75.37           C  
ATOM   3114  O   ASN A 501      71.039  40.383 -41.834  1.00 75.44           O  
ATOM   3115  CB  ASN A 501      71.776  37.486 -43.345  1.00 75.91           C  
ATOM   3116  CG  ASN A 501      71.661  36.430 -44.486  1.00 74.77           C  
ATOM   3117  OD1 ASN A 501      70.581  36.192 -45.052  1.00 76.47           O  
ATOM   3118  ND2 ASN A 501      72.783  35.777 -44.793  1.00 76.28           N  
ATOM   3119  N   VAL A 503      71.304  40.896 -38.494  1.00 74.85           N  
ATOM   3120  CA  VAL A 503      72.469  41.449 -37.806  1.00 74.69           C  
ATOM   3121  C   VAL A 503      73.372  40.300 -37.315  1.00 74.28           C  
ATOM   3122  O   VAL A 503      74.566  40.253 -37.626  1.00 73.99           O  
ATOM   3123  CB  VAL A 503      72.017  42.408 -36.631  1.00 75.18           C  
ATOM   3124  CG1 VAL A 503      73.258  42.949 -35.810  1.00 75.15           C  
ATOM   3125  CG2 VAL A 503      71.190  43.640 -37.216  1.00 75.18           C  
ATOM   3126  N   GLY A 504      72.797  39.352 -36.552  1.00 74.11           N  
ATOM   3127  CA  GLY A 504      73.530  38.206 -35.986  1.00 73.19           C  
ATOM   3128  C   GLY A 504      73.956  37.218 -37.066  1.00 77.85           C  
ATOM   3129  O   GLY A 504      74.810  36.357 -36.845  1.00 73.14           O  
ATOM   3130  N   TYR A 505      73.365  37.365 -38.248  1.00 73.27           N  
ATOM   3131  CA  TYR A 505      73.658  36.486 -39.363  1.00 74.39           C  
ATOM   3132  C   TYR A 505      74.487  37.176 -40.441  1.00 79.04           C  
ATOM   3133  O   TYR A 505      74.701  36.625 -41.520  1.00 74.17           O  
ATOM   3134  CB  TYR A 505      72.354  35.941 -39.918  1.00 75.04           C  
ATOM   3135  CG  TYR A 505      71.615  35.117 -38.904  1.00 74.99           C  
ATOM   3136  CD1 TYR A 505      70.658  35.718 -38.102  1.00 76.06           C  
ATOM   3137  CD2 TYR A 505      71.887  33.769 -38.766  1.00 75.09           C  
ATOM   3138  CE1 TYR A 505      69.983  34.972 -37.162  1.00 75.79           C  
ATOM   3139  CE2 TYR A 505      71.211  33.022 -37.828  1.00 75.62           C  
ATOM   3140  CZ  TYR A 505      70.260  33.620 -37.028  1.00 76.38           C  
ATOM   3141  OH  TYR A 505      69.583  32.876 -36.088  1.00 76.29           O  
ATOM   3142  N   GLN A 506      74.965  38.375 -40.137  1.00 72.91           N  
ATOM   3143  CA  GLN A 506      75.807  39.120 -41.054  1.00 72.35           C  
ATOM   3144  C   GLN A 506      77.247  38.729 -40.776  1.00 78.40           C  
ATOM   3145  O   GLN A 506      77.544  38.262 -39.676  1.00 65.73           O  
ATOM   3146  CB  GLN A 506      75.566  40.617 -40.863  1.00 74.28           C  
ATOM   3147  CG  GLN A 506      74.176  41.018 -41.263  1.00 75.31           C  
ATOM   3148  CD  GLN A 506      73.893  42.480 -41.095  1.00 74.55           C  
ATOM   3149  OE1 GLN A 506      74.770  43.282 -40.765  1.00 74.59           O  
ATOM   3150  NE2 GLN A 506      72.642  42.836 -41.327  1.00 75.15           N  
ATOM   3151  N   PRO A 507      78.151  38.848 -41.753  1.00 71.83           N  
ATOM   3152  CA  PRO A 507      79.564  38.602 -41.600  1.00 71.34           C  
ATOM   3153  C   PRO A 507      80.216  39.697 -40.795  1.00 69.88           C  
ATOM   3154  O   PRO A 507      79.874  40.874 -40.953  1.00 80.98           O  
ATOM   3155  CB  PRO A 507      80.073  38.617 -43.038  1.00 72.03           C  
ATOM   3156  CG  PRO A 507      79.098  39.497 -43.782  1.00 72.79           C  
ATOM   3157  CD  PRO A 507      77.749  39.275 -43.097  1.00 74.51           C  
ATOM   3158  N   TYR A 508      81.195  39.309 -39.998  1.00 70.75           N  
ATOM   3159  CA  TYR A 508      82.041  40.232 -39.270  1.00 73.11           C  
ATOM   3160  C   TYR A 508      83.506  39.982 -39.520  1.00 68.21           C  
ATOM   3161  O   TYR A 508      83.984  38.843 -39.539  1.00 67.37           O  
ATOM   3162  CB  TYR A 508      81.745  40.189 -37.774  1.00 68.56           C  
ATOM   3163  CG  TYR A 508      80.525  40.957 -37.356  1.00 70.68           C  
ATOM   3164  CD1 TYR A 508      79.267  40.560 -37.729  1.00 69.79           C  
ATOM   3165  CD2 TYR A 508      80.685  42.070 -36.555  1.00 68.66           C  
ATOM   3166  CE1 TYR A 508      78.166  41.264 -37.311  1.00 70.79           C  
ATOM   3167  CE2 TYR A 508      79.588  42.776 -36.132  1.00 69.27           C  
ATOM   3168  CZ  TYR A 508      78.330  42.372 -36.507  1.00 70.53           C  
ATOM   3169  OH  TYR A 508      77.226  43.064 -36.078  1.00 71.22           O  
ATOM   3170  N   ARG A 509      84.227  41.073 -39.656  1.00 67.71           N  
ATOM   3171  CA  ARG A 509      85.659  41.029 -39.799  1.00 67.56           C  
ATOM   3172  C   ARG A 509      86.280  41.209 -38.446  1.00 69.40           C  
ATOM   3173  O   ARG A 509      86.061  42.216 -37.771  1.00 63.20           O  
ATOM   3174  CB  ARG A 509      86.138  42.084 -40.769  1.00 66.25           C  
ATOM   3175  CG  ARG A 509      85.875  41.747 -42.210  1.00 68.63           C  
ATOM   3176  CD  ARG A 509      86.445  42.754 -43.121  1.00 68.08           C  
ATOM   3177  NE  ARG A 509      86.402  42.294 -44.507  1.00 69.44           N  
ATOM   3178  CZ  ARG A 509      87.210  42.733 -45.493  1.00 69.47           C  
ATOM   3179  NH1 ARG A 509      88.115  43.660 -45.241  1.00 68.77           N  
ATOM   3180  NH2 ARG A 509      87.084  42.220 -46.710  1.00 69.56           N  
ATOM   3181  N   VAL A 510      87.006  40.198 -38.009  1.00 65.54           N  
ATOM   3182  CA  VAL A 510      87.593  40.248 -36.691  1.00 64.32           C  
ATOM   3183  C   VAL A 510      89.095  40.137 -36.754  1.00 62.90           C  
ATOM   3184  O   VAL A 510      89.655  39.296 -37.461  1.00 68.88           O  
ATOM   3185  CB  VAL A 510      86.987  39.155 -35.779  1.00 65.65           C  
ATOM   3186  CG1 VAL A 510      87.135  37.793 -36.406  1.00 66.30           C  
ATOM   3187  CG2 VAL A 510      87.678  39.182 -34.408  1.00 63.63           C  
ATOM   3188  N   VAL A 511      89.739  41.023 -36.020  1.00 62.82           N  
ATOM   3189  CA  VAL A 511      91.173  41.022 -35.888  1.00 61.82           C  
ATOM   3190  C   VAL A 511      91.525  40.876 -34.424  1.00 60.85           C  
ATOM   3191  O   VAL A 511      91.120  41.692 -33.595  1.00 60.67           O  
ATOM   3192  CB  VAL A 511      91.776  42.320 -36.444  1.00 61.98           C  
ATOM   3193  CG1 VAL A 511      93.286  42.318 -36.265  1.00 60.24           C  
ATOM   3194  CG2 VAL A 511      91.416  42.450 -37.907  1.00 62.81           C  
ATOM   3195  N   VAL A 512      92.278  39.847 -34.096  1.00 59.80           N  
ATOM   3196  CA  VAL A 512      92.676  39.672 -32.715  1.00 58.90           C  
ATOM   3197  C   VAL A 512      94.111  40.115 -32.562  1.00 57.69           C  
ATOM   3198  O   VAL A 512      94.994  39.620 -33.259  1.00 58.00           O  
ATOM   3199  CB  VAL A 512      92.525  38.209 -32.269  1.00 59.69           C  
ATOM   3200  CG1 VAL A 512      92.971  38.058 -30.832  1.00 57.78           C  
ATOM   3201  CG2 VAL A 512      91.081  37.773 -32.449  1.00 60.26           C  
ATOM   3202  N   LEU A 513      94.350  41.059 -31.669  1.00 56.31           N  
ATOM   3203  CA  LEU A 513      95.705  41.522 -31.460  1.00 55.05           C  
ATOM   3204  C   LEU A 513      96.291  40.868 -30.229  1.00 54.63           C  
ATOM   3205  O   LEU A 513      95.881  41.137 -29.098  1.00 54.77           O  
ATOM   3206  CB  LEU A 513      95.771  43.050 -31.327  1.00 54.64           C  
ATOM   3207  CG  LEU A 513      95.292  43.882 -32.535  1.00 55.57           C  
ATOM   3208  CD1 LEU A 513      95.396  45.353 -32.184  1.00 55.10           C  
ATOM   3209  CD2 LEU A 513      96.148  43.573 -33.762  1.00 55.88           C  
ATOM   3210  N   SER A 514      97.247  39.990 -30.480  1.00 53.84           N  
ATOM   3211  CA  SER A 514      97.943  39.238 -29.453  1.00 53.40           C  
ATOM   3212  C   SER A 514      99.226  39.952 -29.093  1.00 52.01           C  
ATOM   3213  O   SER A 514     100.060  40.223 -29.961  1.00 52.44           O  
ATOM   3214  CB  SER A 514      98.245  37.840 -29.941  1.00 54.51           C  
ATOM   3215  OG  SER A 514      99.097  37.177 -29.050  1.00 54.19           O  
ATOM   3216  N   PHE A 515      99.377  40.299 -27.828  1.00 51.80           N  
ATOM   3217  CA  PHE A 515     100.533  41.076 -27.406  1.00 50.59           C  
ATOM   3218  C   PHE A 515     101.453  40.294 -26.491  1.00 49.58           C  
ATOM   3219  O   PHE A 515     101.013  39.765 -25.470  1.00 49.60           O  
ATOM   3220  CB  PHE A 515     100.066  42.300 -26.644  1.00 50.42           C  
ATOM   3221  CG  PHE A 515      99.252  43.267 -27.423  1.00 50.92           C  
ATOM   3222  CD1 PHE A 515      97.934  43.077 -27.547  1.00 52.52           C  
ATOM   3223  CD2 PHE A 515      99.790  44.363 -27.985  1.00 50.47           C  
ATOM   3224  CE1 PHE A 515      97.133  43.966 -28.210  1.00 53.12           C  
ATOM   3225  CE2 PHE A 515      99.020  45.264 -28.650  1.00 50.34           C  
ATOM   3226  CZ  PHE A 515      97.679  45.072 -28.762  1.00 51.54           C  
ATOM   3227  N   GLU A 516     102.736  40.257 -26.818  1.00 48.34           N  
ATOM   3228  CA  GLU A 516     103.689  39.586 -25.946  1.00 47.30           C  
ATOM   3229  C   GLU A 516     104.449  40.602 -25.093  1.00 46.34           C  
ATOM   3230  O   GLU A 516     105.303  41.347 -25.584  1.00 46.65           O  
ATOM   3231  CB  GLU A 516     104.644  38.719 -26.765  1.00 47.40           C  
ATOM   3232  CG  GLU A 516     105.667  37.942 -25.939  1.00 46.70           C  
ATOM   3233  CD  GLU A 516     106.525  37.033 -26.785  1.00 46.92           C  
ATOM   3234  OE1 GLU A 516     106.178  36.809 -27.924  1.00 48.44           O  
ATOM   3235  OE2 GLU A 516     107.531  36.571 -26.297  1.00 46.39           O  
ATOM   3236  N   LEU A 517     104.130  40.614 -23.803  1.00 45.54           N  
ATOM   3237  CA  LEU A 517     104.692  41.545 -22.823  1.00 44.98           C  
ATOM   3238  C   LEU A 517     105.825  40.979 -21.989  1.00 44.04           C  
ATOM   3239  O   LEU A 517     106.212  41.570 -20.982  1.00 42.79           O  
ATOM   3240  CB  LEU A 517     103.607  42.042 -21.884  1.00 44.03           C  
ATOM   3241  CG  LEU A 517     102.593  42.980 -22.468  1.00 44.12           C  
ATOM   3242  CD1 LEU A 517     101.488  43.146 -21.498  1.00 40.63           C  
ATOM   3243  CD2 LEU A 517     103.260  44.338 -22.686  1.00 44.11           C  
ATOM   3244  N   LEU A 518     106.351  39.836 -22.382  1.00 44.61           N  
ATOM   3245  CA  LEU A 518     107.438  39.254 -21.623  1.00 43.65           C  
ATOM   3246  C   LEU A 518     108.610  40.220 -21.629  1.00 42.46           C  
ATOM   3247  O   LEU A 518     108.894  40.853 -22.646  1.00 42.43           O  
ATOM   3248  CB  LEU A 518     107.844  37.905 -22.227  1.00 44.90           C  
ATOM   3249  CG  LEU A 518     106.811  36.761 -22.106  1.00 45.84           C  
ATOM   3250  CD1 LEU A 518     107.293  35.584 -22.928  1.00 45.85           C  
ATOM   3251  CD2 LEU A 518     106.645  36.349 -20.639  1.00 45.96           C  
ATOM   3252  N   HIS A 519     109.292  40.338 -20.499  1.00 41.08           N  
ATOM   3253  CA  HIS A 519     110.410  41.261 -20.417  1.00 40.12           C  
ATOM   3254  C   HIS A 519     111.587  40.791 -21.244  1.00 39.97           C  
ATOM   3255  O   HIS A 519     112.322  39.872 -20.879  1.00 38.77           O  
ATOM   3256  CB  HIS A 519     110.816  41.485 -18.969  1.00 38.09           C  
ATOM   3257  CG  HIS A 519     109.809  42.281 -18.216  1.00 37.40           C  
ATOM   3258  ND1 HIS A 519     108.779  41.696 -17.497  1.00 36.46           N  
ATOM   3259  CD2 HIS A 519     109.657  43.629 -18.070  1.00 36.92           C  
ATOM   3260  CE1 HIS A 519     108.033  42.655 -16.944  1.00 34.57           C  
ATOM   3261  NE2 HIS A 519     108.549  43.821 -17.277  1.00 34.81           N  
ATOM   3262  N   ALA A 520     111.723  41.436 -22.382  1.00 40.39           N  
ATOM   3263  CA  ALA A 520     112.690  41.139 -23.416  1.00 39.97           C  
ATOM   3264  C   ALA A 520     112.765  42.403 -24.258  1.00 40.98           C  
ATOM   3265  O   ALA A 520     111.962  43.305 -24.035  1.00 40.78           O  
ATOM   3266  CB  ALA A 520     112.246  39.914 -24.191  1.00 40.07           C  
ATOM   3267  N   PRO A 521     113.715  42.554 -25.180  1.00 40.97           N  
ATOM   3268  CA  PRO A 521     113.811  43.718 -26.032  1.00 41.65           C  
ATOM   3269  C   PRO A 521     112.482  43.955 -26.736  1.00 43.11           C  
ATOM   3270  O   PRO A 521     111.884  43.025 -27.270  1.00 43.63           O  
ATOM   3271  CB  PRO A 521     114.904  43.300 -27.016  1.00 41.07           C  
ATOM   3272  CG  PRO A 521     115.755  42.328 -26.223  1.00 39.73           C  
ATOM   3273  CD  PRO A 521     114.762  41.547 -25.398  1.00 39.80           C  
ATOM   3274  N   ALA A 522     112.034  45.208 -26.726  1.00 43.71           N  
ATOM   3275  CA  ALA A 522     110.769  45.567 -27.355  1.00 45.22           C  
ATOM   3276  C   ALA A 522     111.010  45.982 -28.787  1.00 46.18           C  
ATOM   3277  O   ALA A 522     112.043  46.580 -29.095  1.00 45.82           O  
ATOM   3278  CB  ALA A 522     110.090  46.690 -26.590  1.00 44.87           C  
ATOM   3279  N   THR A 523     110.060  45.677 -29.670  1.00 46.41           N  
ATOM   3280  CA  THR A 523     110.186  46.117 -31.049  1.00 47.68           C  
ATOM   3281  C   THR A 523     108.979  46.926 -31.503  1.00 48.08           C  
ATOM   3282  O   THR A 523     109.060  47.650 -32.496  1.00 48.62           O  
ATOM   3283  CB  THR A 523     110.365  44.941 -32.015  1.00 48.01           C  
ATOM   3284  OG1 THR A 523     109.170  44.178 -32.058  1.00 48.07           O  
ATOM   3285  CG2 THR A 523     111.500  44.047 -31.547  1.00 47.30           C  
ATOM   3286  N   VAL A 524     107.857  46.798 -30.792  1.00 47.48           N  
ATOM   3287  CA  VAL A 524     106.647  47.530 -31.145  1.00 48.24           C  
ATOM   3288  C   VAL A 524     106.271  48.456 -30.002  1.00 47.24           C  
ATOM   3289  O   VAL A 524     105.670  47.984 -29.036  1.00 47.53           O  
ATOM   3290  CB  VAL A 524     105.459  46.568 -31.375  1.00 48.40           C  
ATOM   3291  CG1 VAL A 524     104.226  47.348 -31.747  1.00 49.40           C  
ATOM   3292  CG2 VAL A 524     105.783  45.595 -32.452  1.00 49.21           C  
ATOM   3293  N   CYS A 525     106.611  49.761 -30.101  1.00 48.15           N  
ATOM   3294  CA  CYS A 525     106.365  50.723 -29.008  1.00 47.54           C  
ATOM   3295  C   CYS A 525     105.464  51.867 -29.449  1.00 47.90           C  
ATOM   3296  O   CYS A 525     105.367  52.163 -30.633  1.00 48.71           O  
ATOM   3297  CB  CYS A 525     107.697  51.235 -28.353  1.00 46.38           C  
ATOM   3298  SG  CYS A 525     108.785  49.916 -27.447  1.00 44.23           S  
ATOM   3299  N   GLY A 526     104.754  52.477 -28.483  1.00 47.30           N  
ATOM   3300  CA  GLY A 526     103.757  53.511 -28.752  1.00 47.39           C  
ATOM   3301  C   GLY A 526     104.360  54.853 -29.151  1.00 47.32           C  
ATOM   3302  O   GLY A 526     105.576  55.049 -29.090  1.00 46.94           O  
ATOM   3303  N   PRO A 527     103.507  55.812 -29.510  1.00 47.50           N  
ATOM   3304  CA  PRO A 527     103.824  57.133 -30.002  1.00 46.95           C  
ATOM   3305  C   PRO A 527     104.196  58.057 -28.867  1.00 46.28           C  
ATOM   3306  O   PRO A 527     103.510  59.046 -28.613  1.00 46.86           O  
ATOM   3307  CB  PRO A 527     102.508  57.553 -30.650  1.00 48.68           C  
ATOM   3308  CG  PRO A 527     101.460  56.888 -29.784  1.00 48.60           C  
ATOM   3309  CD  PRO A 527     102.071  55.558 -29.385  1.00 48.20           C  
ATOM   3310  N   LYS A 528     105.266  57.725 -28.170  1.00 45.65           N  
ATOM   3311  CA  LYS A 528     105.678  58.522 -27.035  1.00 44.53           C  
ATOM   3312  C   LYS A 528     107.122  58.938 -27.200  1.00 43.74           C  
ATOM   3313  O   LYS A 528     107.990  58.114 -27.489  1.00 43.31           O  
ATOM   3314  CB  LYS A 528     105.453  57.754 -25.735  1.00 43.70           C  
ATOM   3315  CG  LYS A 528     105.750  58.553 -24.485  1.00 42.64           C  
ATOM   3316  CD  LYS A 528     105.272  57.825 -23.238  1.00 42.28           C  
ATOM   3317  CE  LYS A 528     105.447  58.685 -21.995  1.00 41.69           C  
ATOM   3318  NZ  LYS A 528     104.938  58.008 -20.783  1.00 41.73           N  
ATOM   3319  N   LYS A 529     107.368  60.230 -27.065  1.00 43.69           N  
ATOM   3320  CA  LYS A 529     108.702  60.761 -27.246  1.00 43.00           C  
ATOM   3321  C   LYS A 529     109.572  60.435 -26.057  1.00 42.31           C  
ATOM   3322  O   LYS A 529     109.108  60.443 -24.917  1.00 41.63           O  
ATOM   3323  CB  LYS A 529     108.657  62.269 -27.468  1.00 43.16           C  
ATOM   3324  CG  LYS A 529     108.007  62.693 -28.779  1.00 44.67           C  
ATOM   3325  CD  LYS A 529     108.045  64.208 -28.946  1.00 45.18           C  
ATOM   3326  CE  LYS A 529     107.403  64.645 -30.258  1.00 45.76           C  
ATOM   3327  NZ  LYS A 529     107.422  66.129 -30.424  1.00 47.69           N  
ATOM   3328  N   SER A 530     110.836  60.166 -26.328  1.00 41.52           N  
ATOM   3329  CA  SER A 530     111.796  59.923 -25.278  1.00 40.74           C  
ATOM   3330  C   SER A 530     112.333  61.231 -24.736  1.00 40.14           C  
ATOM   3331  O   SER A 530     112.188  62.287 -25.354  1.00 40.09           O  
ATOM   3332  CB  SER A 530     112.941  59.087 -25.799  1.00 40.39           C  
ATOM   3333  OG  SER A 530     113.725  59.819 -26.704  1.00 41.19           O  
ATOM   3334  N   THR A 531     112.999  61.139 -23.603  1.00 39.55           N  
ATOM   3335  CA  THR A 531     113.656  62.266 -22.970  1.00 39.12           C  
ATOM   3336  C   THR A 531     115.118  61.922 -22.808  1.00 38.89           C  
ATOM   3337  O   THR A 531     115.523  60.795 -23.085  1.00 38.89           O  
ATOM   3338  CB  THR A 531     113.057  62.578 -21.589  1.00 38.68           C  
ATOM   3339  OG1 THR A 531     113.390  61.525 -20.681  1.00 38.00           O  
ATOM   3340  CG2 THR A 531     111.547  62.691 -21.687  1.00 39.48           C  
ATOM   3341  N   ASN A 532     115.916  62.881 -22.364  1.00 38.47           N  
ATOM   3342  CA  ASN A 532     117.319  62.613 -22.099  1.00 38.53           C  
ATOM   3343  C   ASN A 532     117.431  61.846 -20.797  1.00 38.25           C  
ATOM   3344  O   ASN A 532     116.527  61.904 -19.964  1.00 38.10           O  
ATOM   3345  CB  ASN A 532     118.126  63.893 -22.050  1.00 37.92           C  
ATOM   3346  CG  ASN A 532     119.606  63.642 -22.163  1.00 38.67           C  
ATOM   3347  OD1 ASN A 532     120.040  62.496 -22.354  1.00 38.60           O  
ATOM   3348  ND2 ASN A 532     120.388  64.685 -22.046  1.00 38.84           N  
ATOM   3349  N   LEU A 533     118.522  61.118 -20.620  1.00 38.37           N  
ATOM   3350  CA  LEU A 533     118.705  60.361 -19.393  1.00 37.94           C  
ATOM   3351  C   LEU A 533     119.667  61.055 -18.447  1.00 37.49           C  
ATOM   3352  O   LEU A 533     120.746  61.497 -18.841  1.00 37.66           O  
ATOM   3353  CB  LEU A 533     119.168  58.937 -19.707  1.00 38.24           C  
ATOM   3354  CG  LEU A 533     119.262  57.977 -18.503  1.00 37.64           C  
ATOM   3355  CD1 LEU A 533     118.839  56.606 -18.948  1.00 38.12           C  
ATOM   3356  CD2 LEU A 533     120.691  57.923 -17.977  1.00 36.79           C  
ATOM   3357  N   VAL A 534     119.270  61.130 -17.184  1.00 37.38           N  
ATOM   3358  CA  VAL A 534     120.064  61.787 -16.164  1.00 36.92           C  
ATOM   3359  C   VAL A 534     120.597  60.796 -15.146  1.00 36.49           C  
ATOM   3360  O   VAL A 534     119.831  60.073 -14.518  1.00 35.89           O  
ATOM   3361  CB  VAL A 534     119.206  62.844 -15.456  1.00 36.69           C  
ATOM   3362  CG1 VAL A 534     120.010  63.532 -14.379  1.00 36.30           C  
ATOM   3363  CG2 VAL A 534     118.697  63.844 -16.486  1.00 37.13           C  
ATOM   3364  N   LYS A 535     121.912  60.762 -14.991  1.00 36.00           N  
ATOM   3365  CA  LYS A 535     122.535  59.807 -14.085  1.00 35.58           C  
ATOM   3366  C   LYS A 535     122.835  60.389 -12.716  1.00 35.19           C  
ATOM   3367  O   LYS A 535     123.058  61.590 -12.563  1.00 35.04           O  
ATOM   3368  CB  LYS A 535     123.814  59.254 -14.704  1.00 35.32           C  
ATOM   3369  CG  LYS A 535     123.556  58.462 -15.958  1.00 36.07           C  
ATOM   3370  CD  LYS A 535     124.815  57.935 -16.597  1.00 36.17           C  
ATOM   3371  CE  LYS A 535     124.468  57.220 -17.895  1.00 36.85           C  
ATOM   3372  NZ  LYS A 535     125.662  56.742 -18.628  1.00 37.16           N  
ATOM   3373  N   ASN A 536     122.891  59.490 -11.740  1.00 34.67           N  
ATOM   3374  CA  ASN A 536     123.248  59.764 -10.352  1.00 34.65           C  
ATOM   3375  C   ASN A 536     122.297  60.736  -9.662  1.00 34.46           C  
ATOM   3376  O   ASN A 536     122.694  61.459  -8.749  1.00 34.65           O  
ATOM   3377  CB  ASN A 536     124.662  60.293 -10.279  1.00 34.82           C  
ATOM   3378  CG  ASN A 536     125.650  59.369 -10.914  1.00 35.09           C  
ATOM   3379  OD1 ASN A 536     125.607  58.145 -10.745  1.00 35.02           O  
ATOM   3380  ND2 ASN A 536     126.557  59.940 -11.661  1.00 34.94           N  
ATOM   3381  N   LYS A 537     121.038  60.731 -10.073  1.00 34.52           N  
ATOM   3382  CA  LYS A 537     120.022  61.559  -9.450  1.00 34.48           C  
ATOM   3383  C   LYS A 537     118.753  60.722  -9.313  1.00 33.81           C  
ATOM   3384  O   LYS A 537     118.527  59.835 -10.133  1.00 33.94           O  
ATOM   3385  CB  LYS A 537     119.769  62.819 -10.284  1.00 34.70           C  
ATOM   3386  CG  LYS A 537     118.825  63.836  -9.627  1.00 34.70           C  
ATOM   3387  CD  LYS A 537     118.819  65.157 -10.369  1.00 34.93           C  
ATOM   3388  CE  LYS A 537     117.856  65.137 -11.530  1.00 35.23           C  
ATOM   3389  NZ  LYS A 537     117.896  66.403 -12.292  1.00 35.54           N  
ATOM   3390  N   CYS A 538     117.925  61.013  -8.288  1.00 33.96           N  
ATOM   3391  CA  CYS A 538     116.645  60.309  -8.115  1.00 33.67           C  
ATOM   3392  C   CYS A 538     115.651  60.768  -9.184  1.00 33.19           C  
ATOM   3393  O   CYS A 538     115.288  61.938  -9.258  1.00 33.86           O  
ATOM   3394  CB  CYS A 538     116.074  60.603  -6.710  1.00 33.61           C  
ATOM   3395  SG  CYS A 538     114.511  59.756  -6.339  1.00 31.18           S  
ATOM   3396  N   VAL A 539     115.224  59.804 -10.034  1.00 33.46           N  
ATOM   3397  CA  VAL A 539     114.306  60.055 -11.146  1.00 33.43           C  
ATOM   3398  C   VAL A 539     113.176  59.040 -11.221  1.00 33.61           C  
ATOM   3399  O   VAL A 539     113.275  57.920 -10.715  1.00 33.91           O  
ATOM   3400  CB  VAL A 539     115.065  60.045 -12.483  1.00 33.95           C  
ATOM   3401  CG1 VAL A 539     116.126  61.153 -12.523  1.00 34.22           C  
ATOM   3402  CG2 VAL A 539     115.722  58.684 -12.683  1.00 34.05           C  
ATOM   3403  N   ASN A 540     112.111  59.434 -11.902  1.00 33.72           N  
ATOM   3404  CA  ASN A 540     110.981  58.557 -12.178  1.00 33.35           C  
ATOM   3405  C   ASN A 540     111.160  58.008 -13.585  1.00 34.69           C  
ATOM   3406  O   ASN A 540     110.994  58.738 -14.555  1.00 35.66           O  
ATOM   3407  CB  ASN A 540     109.677  59.324 -12.020  1.00 33.99           C  
ATOM   3408  CG  ASN A 540     108.444  58.488 -12.198  1.00 34.21           C  
ATOM   3409  OD1 ASN A 540     108.453  57.434 -12.841  1.00 34.44           O  
ATOM   3410  ND2 ASN A 540     107.358  58.951 -11.629  1.00 32.93           N  
ATOM   3411  N   PHE A 541     111.571  56.758 -13.711  1.00 34.44           N  
ATOM   3412  CA  PHE A 541     111.942  56.257 -15.027  1.00 34.76           C  
ATOM   3413  C   PHE A 541     110.896  55.375 -15.680  1.00 34.87           C  
ATOM   3414  O   PHE A 541     110.063  54.754 -15.018  1.00 35.31           O  
ATOM   3415  CB  PHE A 541     113.261  55.496 -14.971  1.00 35.34           C  
ATOM   3416  CG  PHE A 541     113.283  54.390 -13.986  1.00 34.89           C  
ATOM   3417  CD1 PHE A 541     112.741  53.158 -14.290  1.00 34.89           C  
ATOM   3418  CD2 PHE A 541     113.864  54.566 -12.754  1.00 34.14           C  
ATOM   3419  CE1 PHE A 541     112.767  52.137 -13.379  1.00 34.39           C  
ATOM   3420  CE2 PHE A 541     113.895  53.544 -11.848  1.00 33.56           C  
ATOM   3421  CZ  PHE A 541     113.342  52.331 -12.158  1.00 33.68           C  
ATOM   3422  N   ASN A 542     110.989  55.305 -17.004  1.00 36.00           N  
ATOM   3423  CA  ASN A 542     110.172  54.446 -17.845  1.00 35.75           C  
ATOM   3424  C   ASN A 542     110.999  53.860 -18.982  1.00 36.35           C  
ATOM   3425  O   ASN A 542     111.327  54.559 -19.940  1.00 37.70           O  
ATOM   3426  CB  ASN A 542     108.995  55.216 -18.401  1.00 36.24           C  
ATOM   3427  CG  ASN A 542     108.058  54.365 -19.210  1.00 36.99           C  
ATOM   3428  OD1 ASN A 542     108.492  53.505 -19.994  1.00 37.30           O  
ATOM   3429  ND2 ASN A 542     106.780  54.599 -19.023  1.00 37.76           N  
ATOM   3430  N   PHE A 543     111.355  52.588 -18.875  1.00 36.40           N  
ATOM   3431  CA  PHE A 543     112.144  51.944 -19.915  1.00 36.50           C  
ATOM   3432  C   PHE A 543     111.290  50.937 -20.656  1.00 37.53           C  
ATOM   3433  O   PHE A 543     110.931  49.897 -20.110  1.00 37.37           O  
ATOM   3434  CB  PHE A 543     113.369  51.237 -19.340  1.00 37.05           C  
ATOM   3435  CG  PHE A 543     114.419  52.142 -18.787  1.00 36.93           C  
ATOM   3436  CD1 PHE A 543     114.416  52.509 -17.466  1.00 36.53           C  
ATOM   3437  CD2 PHE A 543     115.424  52.614 -19.598  1.00 37.44           C  
ATOM   3438  CE1 PHE A 543     115.400  53.327 -16.966  1.00 36.57           C  
ATOM   3439  CE2 PHE A 543     116.406  53.429 -19.107  1.00 37.86           C  
ATOM   3440  CZ  PHE A 543     116.391  53.785 -17.790  1.00 37.48           C  
ATOM   3441  N   ASN A 544     110.922  51.255 -21.883  1.00 38.35           N  
ATOM   3442  CA  ASN A 544     110.073  50.379 -22.680  1.00 39.51           C  
ATOM   3443  C   ASN A 544     108.774  50.005 -21.968  1.00 39.44           C  
ATOM   3444  O   ASN A 544     108.311  48.870 -22.081  1.00 39.95           O  
ATOM   3445  CB  ASN A 544     110.816  49.104 -23.037  1.00 39.74           C  
ATOM   3446  CG  ASN A 544     112.053  49.341 -23.801  1.00 39.82           C  
ATOM   3447  OD1 ASN A 544     112.134  50.251 -24.627  1.00 40.11           O  
ATOM   3448  ND2 ASN A 544     113.045  48.529 -23.550  1.00 39.34           N  
ATOM   3449  N   GLY A 545     108.179  50.931 -21.228  1.00 38.31           N  
ATOM   3450  CA  GLY A 545     106.928  50.644 -20.543  1.00 38.88           C  
ATOM   3451  C   GLY A 545     107.128  50.167 -19.103  1.00 36.92           C  
ATOM   3452  O   GLY A 545     106.161  50.085 -18.347  1.00 36.40           O  
ATOM   3453  N   LEU A 546     108.371  49.868 -18.717  1.00 36.63           N  
ATOM   3454  CA  LEU A 546     108.674  49.428 -17.356  1.00 35.81           C  
ATOM   3455  C   LEU A 546     109.000  50.611 -16.482  1.00 35.45           C  
ATOM   3456  O   LEU A 546     109.970  51.328 -16.729  1.00 35.70           O  
ATOM   3457  CB  LEU A 546     109.871  48.476 -17.343  1.00 35.91           C  
ATOM   3458  CG  LEU A 546     110.392  48.066 -15.949  1.00 34.45           C  
ATOM   3459  CD1 LEU A 546     109.329  47.256 -15.200  1.00 33.47           C  
ATOM   3460  CD2 LEU A 546     111.654  47.264 -16.126  1.00 34.91           C  
ATOM   3461  N   THR A 547     108.204  50.824 -15.450  1.00 34.71           N  
ATOM   3462  CA  THR A 547     108.393  52.009 -14.646  1.00 34.22           C  
ATOM   3463  C   THR A 547     108.829  51.720 -13.231  1.00 33.34           C  
ATOM   3464  O   THR A 547     108.662  50.608 -12.722  1.00 32.75           O  
ATOM   3465  CB  THR A 547     107.096  52.825 -14.599  1.00 34.59           C  
ATOM   3466  OG1 THR A 547     106.081  52.075 -13.919  1.00 32.13           O  
ATOM   3467  CG2 THR A 547     106.635  53.115 -16.001  1.00 35.18           C  
ATOM   3468  N   GLY A 548     109.355  52.757 -12.597  1.00 33.81           N  
ATOM   3469  CA  GLY A 548     109.761  52.716 -11.205  1.00 33.07           C  
ATOM   3470  C   GLY A 548     110.518  53.980 -10.842  1.00 33.00           C  
ATOM   3471  O   GLY A 548     110.709  54.857 -11.681  1.00 34.10           O  
ATOM   3472  N   THR A 549     110.919  54.084  -9.588  1.00 32.78           N  
ATOM   3473  CA  THR A 549     111.650  55.250  -9.123  1.00 32.72           C  
ATOM   3474  C   THR A 549     112.975  54.813  -8.547  1.00 32.31           C  
ATOM   3475  O   THR A 549     113.043  53.838  -7.798  1.00 30.76           O  
ATOM   3476  CB  THR A 549     110.845  56.040  -8.077  1.00 31.06           C  
ATOM   3477  OG1 THR A 549     109.615  56.479  -8.659  1.00 32.47           O  
ATOM   3478  CG2 THR A 549     111.633  57.257  -7.603  1.00 32.04           C  
ATOM   3479  N   GLY A 550     114.031  55.515  -8.906  1.00 32.45           N  
ATOM   3480  CA  GLY A 550     115.345  55.165  -8.398  1.00 31.81           C  
ATOM   3481  C   GLY A 550     116.438  55.968  -9.056  1.00 32.19           C  
ATOM   3482  O   GLY A 550     116.190  56.755  -9.970  1.00 33.03           O  
ATOM   3483  N   VAL A 551     117.648  55.755  -8.586  1.00 32.13           N  
ATOM   3484  CA  VAL A 551     118.815  56.418  -9.112  1.00 32.79           C  
ATOM   3485  C   VAL A 551     119.475  55.540 -10.158  1.00 32.16           C  
ATOM   3486  O   VAL A 551     119.769  54.371  -9.900  1.00 33.11           O  
ATOM   3487  CB  VAL A 551     119.797  56.711  -7.971  1.00 32.48           C  
ATOM   3488  CG1 VAL A 551     121.036  57.379  -8.510  1.00 32.95           C  
ATOM   3489  CG2 VAL A 551     119.113  57.582  -6.940  1.00 32.35           C  
ATOM   3490  N   LEU A 552     119.694  56.096 -11.339  1.00 33.19           N  
ATOM   3491  CA  LEU A 552     120.296  55.368 -12.446  1.00 33.48           C  
ATOM   3492  C   LEU A 552     121.786  55.648 -12.492  1.00 33.29           C  
ATOM   3493  O   LEU A 552     122.187  56.806 -12.611  1.00 34.82           O  
ATOM   3494  CB  LEU A 552     119.664  55.822 -13.768  1.00 33.84           C  
ATOM   3495  CG  LEU A 552     118.130  55.748 -13.860  1.00 34.17           C  
ATOM   3496  CD1 LEU A 552     117.690  56.350 -15.176  1.00 35.81           C  
ATOM   3497  CD2 LEU A 552     117.679  54.315 -13.747  1.00 33.88           C  
ATOM   3498  N   THR A 553     122.605  54.613 -12.378  1.00 33.84           N  
ATOM   3499  CA  THR A 553     124.049  54.818 -12.366  1.00 33.91           C  
ATOM   3500  C   THR A 553     124.738  53.935 -13.388  1.00 33.83           C  
ATOM   3501  O   THR A 553     124.154  52.977 -13.888  1.00 34.56           O  
ATOM   3502  CB  THR A 553     124.647  54.518 -10.979  1.00 33.98           C  
ATOM   3503  OG1 THR A 553     124.584  53.114 -10.723  1.00 33.75           O  
ATOM   3504  CG2 THR A 553     123.852  55.238  -9.908  1.00 33.94           C  
ATOM   3505  N   GLU A 554     126.005  54.216 -13.657  1.00 34.38           N  
ATOM   3506  CA  GLU A 554     126.779  53.361 -14.544  1.00 34.61           C  
ATOM   3507  C   GLU A 554     127.021  52.049 -13.832  1.00 34.38           C  
ATOM   3508  O   GLU A 554     127.076  52.020 -12.600  1.00 34.15           O  
ATOM   3509  CB  GLU A 554     128.107  54.014 -14.914  1.00 34.60           C  
ATOM   3510  CG  GLU A 554     127.987  55.261 -15.768  1.00 35.53           C  
ATOM   3511  CD  GLU A 554     129.329  55.848 -16.114  1.00 36.65           C  
ATOM   3512  OE1 GLU A 554     130.305  55.389 -15.573  1.00 34.99           O  
ATOM   3513  OE2 GLU A 554     129.381  56.744 -16.925  1.00 36.06           O  
ATOM   3514  N   SER A 555     127.173  50.967 -14.587  1.00 34.53           N  
ATOM   3515  CA  SER A 555     127.353  49.669 -13.954  1.00 34.60           C  
ATOM   3516  C   SER A 555     128.395  48.830 -14.648  1.00 34.67           C  
ATOM   3517  O   SER A 555     128.790  49.096 -15.783  1.00 34.68           O  
ATOM   3518  CB  SER A 555     126.072  48.883 -13.992  1.00 34.43           C  
ATOM   3519  OG  SER A 555     125.834  48.406 -15.277  1.00 34.80           O  
ATOM   3520  N   ASN A 556     128.802  47.778 -13.961  1.00 34.63           N  
ATOM   3521  CA  ASN A 556     129.733  46.802 -14.484  1.00 34.65           C  
ATOM   3522  C   ASN A 556     129.054  45.446 -14.634  1.00 34.50           C  
ATOM   3523  O   ASN A 556     129.706  44.404 -14.569  1.00 34.28           O  
ATOM   3524  CB  ASN A 556     130.942  46.725 -13.583  1.00 34.57           C  
ATOM   3525  CG  ASN A 556     130.570  46.313 -12.197  1.00 35.06           C  
ATOM   3526  OD1 ASN A 556     129.411  46.473 -11.787  1.00 34.81           O  
ATOM   3527  ND2 ASN A 556     131.518  45.796 -11.458  1.00 35.55           N  
ATOM   3528  N   LYS A 557     127.737  45.463 -14.823  1.00 34.45           N  
ATOM   3529  CA  LYS A 557     126.996  44.227 -14.975  1.00 34.13           C  
ATOM   3530  C   LYS A 557     126.956  43.823 -16.429  1.00 34.77           C  
ATOM   3531  O   LYS A 557     126.377  44.501 -17.279  1.00 34.53           O  
ATOM   3532  CB  LYS A 557     125.597  44.361 -14.383  1.00 34.02           C  
ATOM   3533  CG  LYS A 557     125.646  44.551 -12.883  1.00 33.40           C  
ATOM   3534  CD  LYS A 557     124.288  44.623 -12.232  1.00 33.12           C  
ATOM   3535  CE  LYS A 557     124.464  44.898 -10.742  1.00 31.27           C  
ATOM   3536  NZ  LYS A 557     123.182  44.952 -10.010  1.00 31.10           N  
ATOM   3537  N   LYS A 558     127.597  42.709 -16.718  1.00 34.26           N  
ATOM   3538  CA  LYS A 558     127.738  42.274 -18.087  1.00 34.46           C  
ATOM   3539  C   LYS A 558     126.522  41.522 -18.556  1.00 34.34           C  
ATOM   3540  O   LYS A 558     126.462  40.300 -18.456  1.00 34.84           O  
ATOM   3541  CB  LYS A 558     128.968  41.386 -18.243  1.00 34.61           C  
ATOM   3542  CG  LYS A 558     129.278  40.988 -19.680  1.00 35.47           C  
ATOM   3543  CD  LYS A 558     130.542  40.137 -19.755  1.00 36.26           C  
ATOM   3544  CE  LYS A 558     130.888  39.783 -21.204  1.00 37.12           C  
ATOM   3545  NZ  LYS A 558     132.131  38.947 -21.284  1.00 39.63           N  
ATOM   3546  N   PHE A 559     125.565  42.256 -19.084  1.00 34.91           N  
ATOM   3547  CA  PHE A 559     124.385  41.617 -19.623  1.00 33.73           C  
ATOM   3548  C   PHE A 559     124.788  40.915 -20.887  1.00 34.76           C  
ATOM   3549  O   PHE A 559     125.616  41.427 -21.647  1.00 34.60           O  
ATOM   3550  CB  PHE A 559     123.280  42.613 -19.959  1.00 34.16           C  
ATOM   3551  CG  PHE A 559     122.430  43.084 -18.816  1.00 33.89           C  
ATOM   3552  CD1 PHE A 559     122.903  43.163 -17.518  1.00 33.34           C  
ATOM   3553  CD2 PHE A 559     121.118  43.448 -19.063  1.00 34.06           C  
ATOM   3554  CE1 PHE A 559     122.082  43.590 -16.513  1.00 32.79           C  
ATOM   3555  CE2 PHE A 559     120.309  43.874 -18.058  1.00 34.16           C  
ATOM   3556  CZ  PHE A 559     120.787  43.942 -16.783  1.00 33.96           C  
ATOM   3557  N   LEU A 560     124.199  39.764 -21.137  1.00 35.03           N  
ATOM   3558  CA  LEU A 560     124.461  39.082 -22.378  1.00 35.20           C  
ATOM   3559  C   LEU A 560     123.621  39.798 -23.424  1.00 35.73           C  
ATOM   3560  O   LEU A 560     122.608  40.395 -23.071  1.00 35.48           O  
ATOM   3561  CB  LEU A 560     124.126  37.593 -22.236  1.00 35.55           C  
ATOM   3562  CG  LEU A 560     124.939  36.843 -21.131  1.00 35.26           C  
ATOM   3563  CD1 LEU A 560     124.440  35.410 -21.009  1.00 33.40           C  
ATOM   3564  CD2 LEU A 560     126.437  36.865 -21.466  1.00 34.18           C  
ATOM   3565  N   PRO A 561     123.994  39.775 -24.704  1.00 34.97           N  
ATOM   3566  CA  PRO A 561     123.339  40.468 -25.805  1.00 35.30           C  
ATOM   3567  C   PRO A 561     121.831  40.238 -25.914  1.00 35.38           C  
ATOM   3568  O   PRO A 561     121.120  41.069 -26.474  1.00 35.36           O  
ATOM   3569  CB  PRO A 561     124.071  39.890 -27.020  1.00 35.66           C  
ATOM   3570  CG  PRO A 561     125.444  39.535 -26.501  1.00 35.24           C  
ATOM   3571  CD  PRO A 561     125.213  39.034 -25.102  1.00 35.05           C  
ATOM   3572  N   PHE A 562     121.339  39.120 -25.394  1.00 34.99           N  
ATOM   3573  CA  PHE A 562     119.915  38.827 -25.495  1.00 34.92           C  
ATOM   3574  C   PHE A 562     119.124  39.323 -24.285  1.00 35.47           C  
ATOM   3575  O   PHE A 562     117.892  39.277 -24.288  1.00 36.48           O  
ATOM   3576  CB  PHE A 562     119.709  37.319 -25.651  1.00 34.63           C  
ATOM   3577  CG  PHE A 562     120.195  36.500 -24.492  1.00 34.14           C  
ATOM   3578  CD1 PHE A 562     119.366  36.224 -23.429  1.00 36.52           C  
ATOM   3579  CD2 PHE A 562     121.473  36.012 -24.463  1.00 34.32           C  
ATOM   3580  CE1 PHE A 562     119.800  35.467 -22.371  1.00 36.64           C  
ATOM   3581  CE2 PHE A 562     121.907  35.264 -23.402  1.00 35.23           C  
ATOM   3582  CZ  PHE A 562     121.070  34.990 -22.359  1.00 34.77           C  
ATOM   3583  N   GLN A 563     119.836  39.772 -23.250  1.00 35.23           N  
ATOM   3584  CA  GLN A 563     119.219  40.182 -21.998  1.00 36.83           C  
ATOM   3585  C   GLN A 563     118.920  41.662 -21.989  1.00 35.31           C  
ATOM   3586  O   GLN A 563     119.753  42.483 -22.368  1.00 35.12           O  
ATOM   3587  CB  GLN A 563     120.125  39.813 -20.828  1.00 38.27           C  
ATOM   3588  CG  GLN A 563     120.284  38.339 -20.696  1.00 29.00           C  
ATOM   3589  CD  GLN A 563     121.192  37.908 -19.598  1.00 31.25           C  
ATOM   3590  OE1 GLN A 563     122.285  38.457 -19.421  1.00 32.15           O  
ATOM   3591  NE2 GLN A 563     120.763  36.906 -18.839  1.00 28.94           N  
ATOM   3592  N   GLN A 564     117.719  42.000 -21.568  1.00 36.85           N  
ATOM   3593  CA  GLN A 564     117.290  43.394 -21.560  1.00 36.19           C  
ATOM   3594  C   GLN A 564     117.103  43.955 -20.164  1.00 36.40           C  
ATOM   3595  O   GLN A 564     117.328  45.145 -19.922  1.00 36.27           O  
ATOM   3596  CB  GLN A 564     116.016  43.540 -22.386  1.00 36.89           C  
ATOM   3597  CG  GLN A 564     115.446  44.937 -22.462  1.00 37.41           C  
ATOM   3598  CD  GLN A 564     116.362  45.960 -23.060  1.00 37.25           C  
ATOM   3599  OE1 GLN A 564     117.154  45.729 -23.991  1.00 37.62           O  
ATOM   3600  NE2 GLN A 564     116.261  47.148 -22.487  1.00 37.42           N  
ATOM   3601  N   PHE A 565     116.667  43.108 -19.249  1.00 35.60           N  
ATOM   3602  CA  PHE A 565     116.383  43.523 -17.890  1.00 34.41           C  
ATOM   3603  C   PHE A 565     117.085  42.582 -16.936  1.00 36.84           C  
ATOM   3604  O   PHE A 565     117.225  41.402 -17.244  1.00 25.68           O  
ATOM   3605  CB  PHE A 565     114.880  43.460 -17.622  1.00 35.55           C  
ATOM   3606  CG  PHE A 565     114.053  44.309 -18.548  1.00 36.43           C  
ATOM   3607  CD1 PHE A 565     113.505  43.774 -19.706  1.00 36.74           C  
ATOM   3608  CD2 PHE A 565     113.819  45.635 -18.274  1.00 36.19           C  
ATOM   3609  CE1 PHE A 565     112.731  44.551 -20.557  1.00 37.57           C  
ATOM   3610  CE2 PHE A 565     113.055  46.420 -19.128  1.00 36.77           C  
ATOM   3611  CZ  PHE A 565     112.509  45.875 -20.264  1.00 37.34           C  
ATOM   3612  N   GLY A 566     117.490  43.083 -15.780  1.00 32.84           N  
ATOM   3613  CA  GLY A 566     118.005  42.230 -14.717  1.00 31.74           C  
ATOM   3614  C   GLY A 566     117.030  42.244 -13.555  1.00 32.47           C  
ATOM   3615  O   GLY A 566     116.249  43.186 -13.416  1.00 33.09           O  
ATOM   3616  N   ARG A 567     117.084  41.229 -12.699  1.00 31.19           N  
ATOM   3617  CA  ARG A 567     116.185  41.196 -11.547  1.00 30.65           C  
ATOM   3618  C   ARG A 567     116.851  40.802 -10.242  1.00 29.57           C  
ATOM   3619  O   ARG A 567     117.838  40.065 -10.213  1.00 30.51           O  
ATOM   3620  CB  ARG A 567     115.010  40.266 -11.781  1.00 29.81           C  
ATOM   3621  CG  ARG A 567     114.030  40.716 -12.838  1.00 30.13           C  
ATOM   3622  CD  ARG A 567     112.916  39.760 -12.966  1.00 29.47           C  
ATOM   3623  NE  ARG A 567     112.085  40.051 -14.112  1.00 29.60           N  
ATOM   3624  CZ  ARG A 567     110.987  40.827 -14.112  1.00 30.08           C  
ATOM   3625  NH1 ARG A 567     110.545  41.420 -13.017  1.00 27.61           N  
ATOM   3626  NH2 ARG A 567     110.337  40.999 -15.240  1.00 32.62           N  
ATOM   3627  N   ASP A 568     116.265  41.296  -9.159  1.00 27.27           N  
ATOM   3628  CA  ASP A 568     116.677  41.013  -7.795  1.00 26.43           C  
ATOM   3629  C   ASP A 568     115.865  39.850  -7.216  1.00 24.71           C  
ATOM   3630  O   ASP A 568     114.987  39.299  -7.876  1.00 24.64           O  
ATOM   3631  CB  ASP A 568     116.524  42.284  -6.950  1.00 26.59           C  
ATOM   3632  CG  ASP A 568     117.532  42.391  -5.795  1.00 25.29           C  
ATOM   3633  OD1 ASP A 568     117.891  41.381  -5.243  1.00 24.80           O  
ATOM   3634  OD2 ASP A 568     117.945  43.486  -5.492  1.00 26.08           O  
ATOM   3635  N   ILE A 569     116.137  39.495  -5.970  1.00 23.93           N  
ATOM   3636  CA  ILE A 569     115.478  38.380  -5.294  1.00 23.15           C  
ATOM   3637  C   ILE A 569     113.974  38.600  -5.195  1.00 21.54           C  
ATOM   3638  O   ILE A 569     113.188  37.661  -5.297  1.00 20.23           O  
ATOM   3639  CB  ILE A 569     116.062  38.179  -3.882  1.00 22.18           C  
ATOM   3640  CG1 ILE A 569     117.579  37.823  -3.965  1.00 22.87           C  
ATOM   3641  CG2 ILE A 569     115.279  37.097  -3.121  1.00 18.93           C  
ATOM   3642  CD1 ILE A 569     117.931  36.564  -4.753  1.00 23.94           C  
ATOM   3643  N   ALA A 570     113.577  39.847  -4.988  1.00 21.62           N  
ATOM   3644  CA  ALA A 570     112.175  40.230  -4.844  1.00 20.33           C  
ATOM   3645  C   ALA A 570     111.465  40.336  -6.196  1.00 21.59           C  
ATOM   3646  O   ALA A 570     110.305  40.742  -6.257  1.00 20.86           O  
ATOM   3647  CB  ALA A 570     112.079  41.559  -4.126  1.00 19.90           C  
ATOM   3648  N   ASP A 571     112.171  40.019  -7.282  1.00 23.34           N  
ATOM   3649  CA  ASP A 571     111.654  40.097  -8.649  1.00 23.46           C  
ATOM   3650  C   ASP A 571     111.537  41.539  -9.124  1.00 24.35           C  
ATOM   3651  O   ASP A 571     110.975  41.817 -10.184  1.00 24.80           O  
ATOM   3652  CB  ASP A 571     110.281  39.410  -8.747  1.00 22.54           C  
ATOM   3653  CG  ASP A 571     109.991  38.759 -10.123  1.00 23.19           C  
ATOM   3654  OD1 ASP A 571     110.900  38.222 -10.716  1.00 24.83           O  
ATOM   3655  OD2 ASP A 571     108.857  38.759 -10.536  1.00 22.72           O  
ATOM   3656  N   THR A 572     112.119  42.454  -8.364  1.00 24.49           N  
ATOM   3657  CA  THR A 572     112.144  43.848  -8.756  1.00 25.82           C  
ATOM   3658  C   THR A 572     113.276  44.052  -9.737  1.00 27.60           C  
ATOM   3659  O   THR A 572     114.204  43.245  -9.805  1.00 27.83           O  
ATOM   3660  CB  THR A 572     112.328  44.756  -7.532  1.00 25.02           C  
ATOM   3661  OG1 THR A 572     113.594  44.479  -6.919  1.00 25.45           O  
ATOM   3662  CG2 THR A 572     111.226  44.485  -6.537  1.00 23.63           C  
ATOM   3663  N   THR A 573     113.238  45.147 -10.473  1.00 28.14           N  
ATOM   3664  CA  THR A 573     114.282  45.394 -11.449  1.00 29.56           C  
ATOM   3665  C   THR A 573     115.579  45.787 -10.764  1.00 29.90           C  
ATOM   3666  O   THR A 573     115.599  46.659  -9.900  1.00 29.89           O  
ATOM   3667  CB  THR A 573     113.839  46.482 -12.427  1.00 30.83           C  
ATOM   3668  OG1 THR A 573     112.603  46.084 -13.026  1.00 30.96           O  
ATOM   3669  CG2 THR A 573     114.865  46.689 -13.513  1.00 31.90           C  
ATOM   3670  N   ASP A 574     116.662  45.124 -11.147  1.00 30.57           N  
ATOM   3671  CA  ASP A 574     117.982  45.378 -10.581  1.00 30.84           C  
ATOM   3672  C   ASP A 574     118.784  46.340 -11.449  1.00 32.08           C  
ATOM   3673  O   ASP A 574     119.513  47.200 -10.949  1.00 32.25           O  
ATOM   3674  CB  ASP A 574     118.717  44.044 -10.418  1.00 30.51           C  
ATOM   3675  CG  ASP A 574     120.082  44.138  -9.782  1.00 30.78           C  
ATOM   3676  OD1 ASP A 574     120.203  44.676  -8.709  1.00 30.21           O  
ATOM   3677  OD2 ASP A 574     121.010  43.644 -10.383  1.00 31.82           O  
ATOM   3678  N   ALA A 575     118.669  46.151 -12.756  1.00 32.04           N  
ATOM   3679  CA  ALA A 575     119.390  46.933 -13.743  1.00 32.59           C  
ATOM   3680  C   ALA A 575     118.659  46.854 -15.067  1.00 32.98           C  
ATOM   3681  O   ALA A 575     117.899  45.914 -15.307  1.00 33.65           O  
ATOM   3682  CB  ALA A 575     120.818  46.437 -13.879  1.00 33.58           C  
ATOM   3683  N   VAL A 576     118.882  47.835 -15.928  1.00 34.58           N  
ATOM   3684  CA  VAL A 576     118.289  47.823 -17.259  1.00 35.08           C  
ATOM   3685  C   VAL A 576     119.281  48.158 -18.350  1.00 34.91           C  
ATOM   3686  O   VAL A 576     120.252  48.878 -18.123  1.00 35.93           O  
ATOM   3687  CB  VAL A 576     117.141  48.838 -17.348  1.00 35.52           C  
ATOM   3688  CG1 VAL A 576     116.032  48.459 -16.420  1.00 35.15           C  
ATOM   3689  CG2 VAL A 576     117.669  50.220 -16.986  1.00 35.30           C  
ATOM   3690  N   ARG A 577     118.992  47.702 -19.558  1.00 35.76           N  
ATOM   3691  CA  ARG A 577     119.766  48.126 -20.706  1.00 36.30           C  
ATOM   3692  C   ARG A 577     119.060  49.275 -21.407  1.00 36.76           C  
ATOM   3693  O   ARG A 577     117.909  49.158 -21.825  1.00 37.11           O  
ATOM   3694  CB  ARG A 577     119.984  46.980 -21.666  1.00 36.34           C  
ATOM   3695  CG  ARG A 577     120.872  47.303 -22.843  1.00 37.28           C  
ATOM   3696  CD  ARG A 577     121.238  46.086 -23.559  1.00 37.53           C  
ATOM   3697  NE  ARG A 577     120.079  45.435 -24.099  1.00 37.46           N  
ATOM   3698  CZ  ARG A 577     120.091  44.285 -24.787  1.00 37.00           C  
ATOM   3699  NH1 ARG A 577     121.216  43.659 -25.039  1.00 36.38           N  
ATOM   3700  NH2 ARG A 577     118.948  43.790 -25.207  1.00 37.04           N  
ATOM   3701  N   ASP A 578     119.736  50.399 -21.537  1.00 37.20           N  
ATOM   3702  CA  ASP A 578     119.114  51.542 -22.186  1.00 37.23           C  
ATOM   3703  C   ASP A 578     118.791  51.180 -23.644  1.00 38.10           C  
ATOM   3704  O   ASP A 578     119.673  50.736 -24.374  1.00 38.23           O  
ATOM   3705  CB  ASP A 578     120.000  52.785 -22.076  1.00 37.42           C  
ATOM   3706  CG  ASP A 578     119.405  54.015 -22.758  1.00 38.45           C  
ATOM   3707  OD1 ASP A 578     119.113  53.929 -23.937  1.00 39.13           O  
ATOM   3708  OD2 ASP A 578     119.235  55.021 -22.117  1.00 38.04           O  
ATOM   3709  N   PRO A 579     117.523  51.291 -24.072  1.00 38.39           N  
ATOM   3710  CA  PRO A 579     117.010  50.876 -25.365  1.00 38.80           C  
ATOM   3711  C   PRO A 579     117.548  51.668 -26.549  1.00 39.86           C  
ATOM   3712  O   PRO A 579     117.408  51.226 -27.686  1.00 39.60           O  
ATOM   3713  CB  PRO A 579     115.505  51.091 -25.209  1.00 39.32           C  
ATOM   3714  CG  PRO A 579     115.371  52.146 -24.168  1.00 38.87           C  
ATOM   3715  CD  PRO A 579     116.517  51.907 -23.213  1.00 37.98           C  
ATOM   3716  N   GLN A 580     118.129  52.843 -26.308  1.00 39.25           N  
ATOM   3717  CA  GLN A 580     118.654  53.647 -27.406  1.00 39.43           C  
ATOM   3718  C   GLN A 580     120.149  53.447 -27.544  1.00 39.88           C  
ATOM   3719  O   GLN A 580     120.676  53.338 -28.653  1.00 40.72           O  
ATOM   3720  CB  GLN A 580     118.355  55.125 -27.194  1.00 40.83           C  
ATOM   3721  CG  GLN A 580     116.899  55.457 -27.255  1.00 40.78           C  
ATOM   3722  CD  GLN A 580     116.628  56.935 -27.098  1.00 41.05           C  
ATOM   3723  OE1 GLN A 580     117.541  57.738 -26.880  1.00 41.06           O  
ATOM   3724  NE2 GLN A 580     115.363  57.297 -27.211  1.00 41.18           N  
ATOM   3725  N   THR A 581     120.826  53.396 -26.406  1.00 39.13           N  
ATOM   3726  CA  THR A 581     122.266  53.179 -26.357  1.00 38.91           C  
ATOM   3727  C   THR A 581     122.514  51.972 -25.479  1.00 38.34           C  
ATOM   3728  O   THR A 581     122.151  51.964 -24.310  1.00 38.55           O  
ATOM   3729  CB  THR A 581     123.020  54.422 -25.852  1.00 39.18           C  
ATOM   3730  OG1 THR A 581     124.408  54.104 -25.727  1.00 38.60           O  
ATOM   3731  CG2 THR A 581     122.472  54.911 -24.508  1.00 38.84           C  
ATOM   3732  N   LEU A 582     123.106  50.931 -26.028  1.00 38.29           N  
ATOM   3733  CA  LEU A 582     123.132  49.677 -25.294  1.00 37.97           C  
ATOM   3734  C   LEU A 582     124.179  49.597 -24.189  1.00 37.56           C  
ATOM   3735  O   LEU A 582     125.164  48.869 -24.293  1.00 37.75           O  
ATOM   3736  CB  LEU A 582     123.328  48.519 -26.276  1.00 37.90           C  
ATOM   3737  CG  LEU A 582     122.269  48.412 -27.421  1.00 38.25           C  
ATOM   3738  CD1 LEU A 582     122.608  47.209 -28.288  1.00 38.60           C  
ATOM   3739  CD2 LEU A 582     120.845  48.299 -26.845  1.00 38.23           C  
ATOM   3740  N   GLU A 583     123.913  50.320 -23.109  1.00 37.52           N  
ATOM   3741  CA  GLU A 583     124.738  50.318 -21.910  1.00 36.97           C  
ATOM   3742  C   GLU A 583     123.875  49.894 -20.737  1.00 36.28           C  
ATOM   3743  O   GLU A 583     122.648  50.032 -20.782  1.00 36.28           O  
ATOM   3744  CB  GLU A 583     125.351  51.690 -21.633  1.00 36.91           C  
ATOM   3745  CG  GLU A 583     124.355  52.789 -21.283  1.00 36.75           C  
ATOM   3746  CD  GLU A 583     125.050  54.083 -20.953  1.00 36.48           C  
ATOM   3747  OE1 GLU A 583     126.253  54.111 -21.014  1.00 36.04           O  
ATOM   3748  OE2 GLU A 583     124.394  55.042 -20.623  1.00 35.91           O  
ATOM   3749  N   ILE A 584     124.500  49.367 -19.692  1.00 36.09           N  
ATOM   3750  CA  ILE A 584     123.739  48.898 -18.544  1.00 35.71           C  
ATOM   3751  C   ILE A 584     123.748  49.877 -17.389  1.00 34.90           C  
ATOM   3752  O   ILE A 584     124.796  50.341 -16.944  1.00 34.73           O  
ATOM   3753  CB  ILE A 584     124.253  47.531 -18.063  1.00 35.69           C  
ATOM   3754  CG1 ILE A 584     124.283  46.527 -19.237  1.00 35.53           C  
ATOM   3755  CG2 ILE A 584     123.385  47.005 -16.914  1.00 34.88           C  
ATOM   3756  CD1 ILE A 584     122.969  46.362 -19.968  1.00 35.71           C  
ATOM   3757  N   LEU A 585     122.555  50.178 -16.907  1.00 35.00           N  
ATOM   3758  CA  LEU A 585     122.366  51.098 -15.807  1.00 34.05           C  
ATOM   3759  C   LEU A 585     121.856  50.378 -14.580  1.00 33.96           C  
ATOM   3760  O   LEU A 585     120.871  49.640 -14.650  1.00 34.61           O  
ATOM   3761  CB  LEU A 585     121.342  52.152 -16.195  1.00 34.36           C  
ATOM   3762  CG  LEU A 585     121.603  52.876 -17.485  1.00 35.04           C  
ATOM   3763  CD1 LEU A 585     120.429  53.750 -17.779  1.00 35.38           C  
ATOM   3764  CD2 LEU A 585     122.875  53.690 -17.377  1.00 34.83           C  
ATOM   3765  N   ASP A 586     122.513  50.593 -13.455  1.00 33.58           N  
ATOM   3766  CA  ASP A 586     122.056  50.006 -12.202  1.00 33.45           C  
ATOM   3767  C   ASP A 586     120.945  50.846 -11.639  1.00 32.69           C  
ATOM   3768  O   ASP A 586     120.983  52.072 -11.747  1.00 33.52           O  
ATOM   3769  CB  ASP A 586     123.172  49.906 -11.165  1.00 33.50           C  
ATOM   3770  CG  ASP A 586     124.124  48.778 -11.396  1.00 33.22           C  
ATOM   3771  OD1 ASP A 586     123.786  47.869 -12.107  1.00 33.23           O  
ATOM   3772  OD2 ASP A 586     125.193  48.811 -10.850  1.00 33.97           O  
ATOM   3773  N   ILE A 587     119.965  50.216 -11.010  1.00 32.35           N  
ATOM   3774  CA  ILE A 587     118.917  50.991 -10.382  1.00 31.91           C  
ATOM   3775  C   ILE A 587     118.952  50.851  -8.876  1.00 31.10           C  
ATOM   3776  O   ILE A 587     118.643  49.793  -8.329  1.00 30.60           O  
ATOM   3777  CB  ILE A 587     117.542  50.571 -10.905  1.00 32.29           C  
ATOM   3778  CG1 ILE A 587     117.507  50.782 -12.423  1.00 32.80           C  
ATOM   3779  CG2 ILE A 587     116.454  51.384 -10.202  1.00 31.98           C  
ATOM   3780  CD1 ILE A 587     116.315  50.209 -13.106  1.00 33.26           C  
ATOM   3781  N   THR A 588     119.292  51.931  -8.199  1.00 30.75           N  
ATOM   3782  CA  THR A 588     119.320  51.918  -6.748  1.00 29.99           C  
ATOM   3783  C   THR A 588     118.180  52.782  -6.233  1.00 29.91           C  
ATOM   3784  O   THR A 588     118.183  53.987  -6.462  1.00 30.43           O  
ATOM   3785  CB  THR A 588     120.657  52.433  -6.187  1.00 29.91           C  
ATOM   3786  OG1 THR A 588     121.722  51.590  -6.633  1.00 30.68           O  
ATOM   3787  CG2 THR A 588     120.616  52.419  -4.666  1.00 28.63           C  
ATOM   3788  N   PRO A 589     117.196  52.222  -5.531  1.00 28.65           N  
ATOM   3789  CA  PRO A 589     116.051  52.928  -5.012  1.00 28.77           C  
ATOM   3790  C   PRO A 589     116.539  54.137  -4.236  1.00 28.60           C  
ATOM   3791  O   PRO A 589     117.583  54.073  -3.588  1.00 27.81           O  
ATOM   3792  CB  PRO A 589     115.395  51.871  -4.125  1.00 27.00           C  
ATOM   3793  CG  PRO A 589     115.771  50.577  -4.791  1.00 26.50           C  
ATOM   3794  CD  PRO A 589     117.183  50.788  -5.275  1.00 27.26           C  
ATOM   3795  N   CYS A 590     115.786  55.242  -4.327  1.00 29.00           N  
ATOM   3796  CA  CYS A 590     116.137  56.528  -3.727  1.00 28.23           C  
ATOM   3797  C   CYS A 590     116.160  56.383  -2.203  1.00 26.29           C  
ATOM   3798  O   CYS A 590     115.371  55.617  -1.641  1.00 25.60           O  
ATOM   3799  CB  CYS A 590     115.132  57.611  -4.179  1.00 29.35           C  
ATOM   3800  SG  CYS A 590     115.090  57.854  -5.988  1.00 30.53           S  
ATOM   3801  N   SER A 591     117.082  57.105  -1.534  1.00 26.12           N  
ATOM   3802  CA  SER A 591     117.305  56.982  -0.087  1.00 24.84           C  
ATOM   3803  C   SER A 591     116.041  57.104   0.742  1.00 24.16           C  
ATOM   3804  O   SER A 591     115.192  57.966   0.506  1.00 24.81           O  
ATOM   3805  CB  SER A 591     118.302  58.013   0.392  1.00 24.93           C  
ATOM   3806  OG  SER A 591     118.445  57.944   1.786  1.00 24.56           O  
ATOM   3807  N   PHE A 592     115.921  56.212   1.705  1.00 23.51           N  
ATOM   3808  CA  PHE A 592     114.775  56.180   2.576  1.00 22.79           C  
ATOM   3809  C   PHE A 592     115.176  55.603   3.911  1.00 22.35           C  
ATOM   3810  O   PHE A 592     116.252  55.021   4.039  1.00 22.05           O  
ATOM   3811  CB  PHE A 592     113.658  55.323   1.984  1.00 22.88           C  
ATOM   3812  CG  PHE A 592     113.988  53.877   1.955  1.00 22.10           C  
ATOM   3813  CD1 PHE A 592     113.599  53.054   3.004  1.00 21.81           C  
ATOM   3814  CD2 PHE A 592     114.692  53.328   0.908  1.00 22.46           C  
ATOM   3815  CE1 PHE A 592     113.913  51.722   3.007  1.00 20.90           C  
ATOM   3816  CE2 PHE A 592     115.006  51.992   0.905  1.00 21.91           C  
ATOM   3817  CZ  PHE A 592     114.616  51.187   1.962  1.00 21.02           C  
ATOM   3818  N   GLY A 593     114.308  55.750   4.895  1.00 22.06           N  
ATOM   3819  CA  GLY A 593     114.536  55.142   6.198  1.00 21.63           C  
ATOM   3820  C   GLY A 593     113.485  55.582   7.193  1.00 21.24           C  
ATOM   3821  O   GLY A 593     112.748  56.531   6.951  1.00 21.37           O  
ATOM   3822  N   GLY A 594     113.413  54.905   8.322  1.00 20.81           N  
ATOM   3823  CA  GLY A 594     112.424  55.274   9.318  1.00 20.69           C  
ATOM   3824  C   GLY A 594     112.794  56.597   9.950  1.00 20.46           C  
ATOM   3825  O   GLY A 594     113.967  56.960  10.002  1.00 20.48           O  
ATOM   3826  N   VAL A 595     111.802  57.322  10.429  1.00 20.72           N  
ATOM   3827  CA  VAL A 595     112.074  58.566  11.120  1.00 20.95           C  
ATOM   3828  C   VAL A 595     111.535  58.500  12.527  1.00 20.58           C  
ATOM   3829  O   VAL A 595     110.334  58.283  12.741  1.00 21.08           O  
ATOM   3830  CB  VAL A 595     111.463  59.754  10.380  1.00 21.13           C  
ATOM   3831  CG1 VAL A 595     111.756  61.036  11.117  1.00 21.18           C  
ATOM   3832  CG2 VAL A 595     112.026  59.803   9.018  1.00 21.01           C  
ATOM   3833  N   SER A 596     112.428  58.696  13.482  1.00 20.78           N  
ATOM   3834  CA  SER A 596     112.063  58.646  14.875  1.00 20.69           C  
ATOM   3835  C   SER A 596     112.204  59.991  15.538  1.00 20.51           C  
ATOM   3836  O   SER A 596     113.115  60.759  15.241  1.00 20.57           O  
ATOM   3837  CB  SER A 596     112.894  57.620  15.604  1.00 20.55           C  
ATOM   3838  OG  SER A 596     112.604  56.331  15.158  1.00 20.27           O  
ATOM   3839  N   VAL A 597     111.312  60.266  16.460  1.00 20.59           N  
ATOM   3840  CA  VAL A 597     111.336  61.513  17.178  1.00 20.46           C  
ATOM   3841  C   VAL A 597     111.704  61.278  18.621  1.00 19.91           C  
ATOM   3842  O   VAL A 597     111.076  60.492  19.328  1.00 20.55           O  
ATOM   3843  CB  VAL A 597     109.980  62.211  17.064  1.00 21.02           C  
ATOM   3844  CG1 VAL A 597     109.991  63.518  17.824  1.00 20.89           C  
ATOM   3845  CG2 VAL A 597     109.685  62.450  15.607  1.00 21.44           C  
ATOM   3846  N   ILE A 598     112.750  61.957  19.035  1.00 19.86           N  
ATOM   3847  CA  ILE A 598     113.303  61.856  20.362  1.00 19.91           C  
ATOM   3848  C   ILE A 598     112.809  63.002  21.182  1.00 19.91           C  
ATOM   3849  O   ILE A 598     113.093  64.162  20.885  1.00 20.32           O  
ATOM   3850  CB  ILE A 598     114.819  61.910  20.266  1.00 19.43           C  
ATOM   3851  CG1 ILE A 598     115.273  60.741  19.455  1.00 19.28           C  
ATOM   3852  CG2 ILE A 598     115.448  61.930  21.645  1.00 20.05           C  
ATOM   3853  CD1 ILE A 598     116.626  60.881  18.913  1.00 19.49           C  
ATOM   3854  N   THR A 599     112.050  62.707  22.212  1.00 20.27           N  
ATOM   3855  CA  THR A 599     111.449  63.796  22.931  1.00 20.54           C  
ATOM   3856  C   THR A 599     111.374  63.550  24.430  1.00 21.09           C  
ATOM   3857  O   THR A 599     111.124  62.425  24.864  1.00 21.40           O  
ATOM   3858  CB  THR A 599     110.042  64.024  22.347  1.00 21.03           C  
ATOM   3859  OG1 THR A 599     109.421  65.148  22.961  1.00 21.42           O  
ATOM   3860  CG2 THR A 599     109.167  62.808  22.557  1.00 21.11           C  
ATOM   3861  N   PRO A 600     111.588  64.579  25.250  1.00 21.39           N  
ATOM   3862  CA  PRO A 600     111.299  64.593  26.652  1.00 21.75           C  
ATOM   3863  C   PRO A 600     109.799  64.646  26.703  1.00 21.91           C  
ATOM   3864  O   PRO A 600     109.179  65.054  25.730  1.00 21.74           O  
ATOM   3865  CB  PRO A 600     111.989  65.859  27.138  1.00 21.61           C  
ATOM   3866  CG  PRO A 600     112.007  66.751  25.931  1.00 21.48           C  
ATOM   3867  CD  PRO A 600     112.156  65.827  24.750  1.00 21.26           C  
ATOM   3868  N   GLY A 601     109.189  64.269  27.792  1.00 22.09           N  
ATOM   3869  CA  GLY A 601     107.740  64.291  27.759  1.00 22.41           C  
ATOM   3870  C   GLY A 601     107.247  65.708  27.527  1.00 22.82           C  
ATOM   3871  O   GLY A 601     107.885  66.672  27.964  1.00 23.31           O  
ATOM   3872  N   THR A 602     106.072  65.830  26.914  1.00 23.31           N  
ATOM   3873  CA  THR A 602     105.474  67.144  26.635  1.00 23.36           C  
ATOM   3874  C   THR A 602     105.069  67.928  27.893  1.00 23.57           C  
ATOM   3875  O   THR A 602     104.763  69.117  27.810  1.00 23.15           O  
ATOM   3876  CB  THR A 602     104.270  67.008  25.693  1.00 23.59           C  
ATOM   3877  OG1 THR A 602     103.310  66.099  26.253  1.00 23.58           O  
ATOM   3878  CG2 THR A 602     104.739  66.496  24.378  1.00 23.67           C  
ATOM   3879  N   ASN A 603     105.126  67.268  29.064  1.00 23.81           N  
ATOM   3880  CA  ASN A 603     104.918  67.886  30.371  1.00 24.17           C  
ATOM   3881  C   ASN A 603     106.184  68.639  30.848  1.00 24.14           C  
ATOM   3882  O   ASN A 603     106.160  69.312  31.872  1.00 24.46           O  
ATOM   3883  CB  ASN A 603     104.496  66.820  31.400  1.00 25.01           C  
ATOM   3884  CG  ASN A 603     103.233  67.194  32.183  1.00 25.57           C  
ATOM   3885  OD1 ASN A 603     102.114  66.947  31.711  1.00 26.06           O  
ATOM   3886  ND2 ASN A 603     103.415  67.772  33.356  1.00 26.18           N  
ATOM   3887  N   THR A 604     107.291  68.530  30.073  1.00 23.65           N  
ATOM   3888  CA  THR A 604     108.580  69.173  30.316  1.00 23.49           C  
ATOM   3889  C   THR A 604     108.898  70.159  29.203  1.00 23.03           C  
ATOM   3890  O   THR A 604     109.225  71.318  29.463  1.00 23.41           O  
ATOM   3891  CB  THR A 604     109.711  68.127  30.390  1.00 23.01           C  
ATOM   3892  OG1 THR A 604     109.462  67.226  31.471  1.00 23.43           O  
ATOM   3893  CG2 THR A 604     111.058  68.804  30.587  1.00 22.50           C  
ATOM   3894  N   SER A 605     108.836  69.687  27.961  1.00 23.04           N  
ATOM   3895  CA  SER A 605     109.200  70.517  26.819  1.00 22.72           C  
ATOM   3896  C   SER A 605     108.609  70.047  25.502  1.00 22.23           C  
ATOM   3897  O   SER A 605     108.406  68.856  25.285  1.00 22.39           O  
ATOM   3898  CB  SER A 605     110.700  70.580  26.679  1.00 21.97           C  
ATOM   3899  OG  SER A 605     111.059  71.349  25.562  1.00 21.76           O  
ATOM   3900  N   ASN A 606     108.373  70.991  24.599  1.00 21.85           N  
ATOM   3901  CA  ASN A 606     107.900  70.657  23.263  1.00 21.97           C  
ATOM   3902  C   ASN A 606     109.032  70.659  22.241  1.00 21.75           C  
ATOM   3903  O   ASN A 606     108.787  70.675  21.036  1.00 21.58           O  
ATOM   3904  CB  ASN A 606     106.796  71.595  22.836  1.00 21.99           C  
ATOM   3905  CG  ASN A 606     105.547  71.386  23.619  1.00 22.41           C  
ATOM   3906  OD1 ASN A 606     105.205  70.258  23.991  1.00 22.77           O  
ATOM   3907  ND2 ASN A 606     104.845  72.458  23.882  1.00 21.71           N  
ATOM   3908  N   GLN A 607     110.268  70.665  22.722  1.00 21.47           N  
ATOM   3909  CA  GLN A 607     111.425  70.587  21.844  1.00 21.06           C  
ATOM   3910  C   GLN A 607     111.704  69.137  21.509  1.00 20.80           C  
ATOM   3911  O   GLN A 607     111.665  68.281  22.388  1.00 21.01           O  
ATOM   3912  CB  GLN A 607     112.655  71.207  22.493  1.00 20.89           C  
ATOM   3913  CG  GLN A 607     113.861  71.242  21.589  1.00 20.70           C  
ATOM   3914  CD  GLN A 607     115.009  71.943  22.214  1.00 20.61           C  
ATOM   3915  OE1 GLN A 607     115.217  71.853  23.418  1.00 20.87           O  
ATOM   3916  NE2 GLN A 607     115.776  72.657  21.407  1.00 19.93           N  
ATOM   3917  N   VAL A 608     111.983  68.846  20.246  1.00 20.65           N  
ATOM   3918  CA  VAL A 608     112.297  67.476  19.875  1.00 20.65           C  
ATOM   3919  C   VAL A 608     113.539  67.390  19.010  1.00 20.30           C  
ATOM   3920  O   VAL A 608     113.914  68.362  18.358  1.00 20.53           O  
ATOM   3921  CB  VAL A 608     111.119  66.841  19.129  1.00 20.67           C  
ATOM   3922  CG1 VAL A 608     109.900  66.879  19.986  1.00 21.33           C  
ATOM   3923  CG2 VAL A 608     110.858  67.555  17.838  1.00 20.84           C  
ATOM   3924  N   ALA A 609     114.135  66.207  18.958  1.00 20.02           N  
ATOM   3925  CA  ALA A 609     115.231  65.922  18.039  1.00 20.03           C  
ATOM   3926  C   ALA A 609     114.777  64.834  17.088  1.00 19.73           C  
ATOM   3927  O   ALA A 609     113.993  63.967  17.465  1.00 20.26           O  
ATOM   3928  CB  ALA A 609     116.484  65.508  18.787  1.00 19.73           C  
ATOM   3929  N   VAL A 610     115.252  64.861  15.858  1.00 19.83           N  
ATOM   3930  CA  VAL A 610     114.804  63.865  14.900  1.00 20.08           C  
ATOM   3931  C   VAL A 610     115.911  62.984  14.390  1.00 19.81           C  
ATOM   3932  O   VAL A 610     116.948  63.455  13.931  1.00 19.87           O  
ATOM   3933  CB  VAL A 610     114.110  64.539  13.715  1.00 20.16           C  
ATOM   3934  CG1 VAL A 610     113.677  63.503  12.696  1.00 20.16           C  
ATOM   3935  CG2 VAL A 610     112.921  65.291  14.218  1.00 21.04           C  
ATOM   3936  N   LEU A 611     115.682  61.693  14.474  1.00 20.08           N  
ATOM   3937  CA  LEU A 611     116.621  60.713  13.989  1.00 19.88           C  
ATOM   3938  C   LEU A 611     116.171  60.121  12.675  1.00 20.16           C  
ATOM   3939  O   LEU A 611     115.114  59.492  12.593  1.00 20.55           O  
ATOM   3940  CB  LEU A 611     116.752  59.581  14.997  1.00 20.10           C  
ATOM   3941  CG  LEU A 611     117.645  58.410  14.597  1.00 19.80           C  
ATOM   3942  CD1 LEU A 611     119.103  58.849  14.566  1.00 19.70           C  
ATOM   3943  CD2 LEU A 611     117.405  57.301  15.551  1.00 19.56           C  
ATOM   3944  N   TYR A 612     116.989  60.265  11.657  1.00 20.04           N  
ATOM   3945  CA  TYR A 612     116.694  59.645  10.387  1.00 20.06           C  
ATOM   3946  C   TYR A 612     117.458  58.349  10.371  1.00 20.21           C  
ATOM   3947  O   TYR A 612     118.690  58.349  10.339  1.00 20.56           O  
ATOM   3948  CB  TYR A 612     117.083  60.560   9.244  1.00 20.44           C  
ATOM   3949  CG  TYR A 612     116.251  61.777   9.188  1.00 20.40           C  
ATOM   3950  CD1 TYR A 612     116.571  62.870   9.944  1.00 20.20           C  
ATOM   3951  CD2 TYR A 612     115.154  61.795   8.383  1.00 21.12           C  
ATOM   3952  CE1 TYR A 612     115.779  63.982   9.892  1.00 19.94           C  
ATOM   3953  CE2 TYR A 612     114.363  62.903   8.325  1.00 21.17           C  
ATOM   3954  CZ  TYR A 612     114.672  63.994   9.076  1.00 20.18           C  
ATOM   3955  OH  TYR A 612     113.878  65.109   9.020  1.00 19.56           O  
ATOM   3956  N   GLN A 613     116.740  57.248  10.460  1.00 20.32           N  
ATOM   3957  CA  GLN A 613     117.369  55.964  10.674  1.00 20.08           C  
ATOM   3958  C   GLN A 613     118.114  55.465   9.465  1.00 20.56           C  
ATOM   3959  O   GLN A 613     117.587  55.441   8.359  1.00 21.00           O  
ATOM   3960  CB  GLN A 613     116.323  54.917  11.036  1.00 20.01           C  
ATOM   3961  CG  GLN A 613     115.606  55.117  12.347  1.00 19.78           C  
ATOM   3962  CD  GLN A 613     114.488  54.103  12.487  1.00 19.35           C  
ATOM   3963  OE1 GLN A 613     114.412  53.155  11.698  1.00 18.43           O  
ATOM   3964  NE2 GLN A 613     113.607  54.286  13.452  1.00 19.37           N  
ATOM   3965  N   ASP A 614     119.322  54.993   9.704  1.00 20.74           N  
ATOM   3966  CA  ASP A 614     120.143  54.369   8.675  1.00 21.05           C  
ATOM   3967  C   ASP A 614     120.349  55.226   7.427  1.00 21.44           C  
ATOM   3968  O   ASP A 614     120.329  54.713   6.310  1.00 21.77           O  
ATOM   3969  CB  ASP A 614     119.527  53.025   8.267  1.00 20.83           C  
ATOM   3970  CG  ASP A 614     120.521  52.076   7.586  1.00 21.81           C  
ATOM   3971  OD1 ASP A 614     121.699  52.205   7.841  1.00 20.83           O  
ATOM   3972  OD2 ASP A 614     120.093  51.218   6.838  1.00 21.29           O  
ATOM   3973  N   VAL A 615     120.575  56.520   7.603  1.00 21.40           N  
ATOM   3974  CA  VAL A 615     120.892  57.384   6.475  1.00 21.58           C  
ATOM   3975  C   VAL A 615     122.122  58.201   6.822  1.00 21.43           C  
ATOM   3976  O   VAL A 615     122.458  58.335   8.007  1.00 21.28           O  
ATOM   3977  CB  VAL A 615     119.737  58.350   6.113  1.00 21.90           C  
ATOM   3978  CG1 VAL A 615     118.470  57.585   5.768  1.00 21.93           C  
ATOM   3979  CG2 VAL A 615     119.505  59.285   7.237  1.00 21.32           C  
ATOM   3980  N   ASN A 616     122.773  58.778   5.815  1.00 21.68           N  
ATOM   3981  CA  ASN A 616     123.865  59.706   5.943  1.00 21.94           C  
ATOM   3982  C   ASN A 616     123.315  61.133   6.067  1.00 21.77           C  
ATOM   3983  O   ASN A 616     122.241  61.417   5.516  1.00 22.28           O  
ATOM   3984  CB  ASN A 616     124.849  59.587   4.785  1.00 22.06           C  
ATOM   3985  CG  ASN A 616     126.267  60.086   5.085  1.00 22.05           C  
ATOM   3986  OD1 ASN A 616     126.481  60.876   6.026  1.00 22.22           O  
ATOM   3987  ND2 ASN A 616     127.228  59.623   4.298  1.00 22.29           N  
ATOM   3988  N   CYS A 617     124.063  62.042   6.687  1.00 21.97           N  
ATOM   3989  CA  CYS A 617     123.681  63.448   6.810  1.00 22.52           C  
ATOM   3990  C   CYS A 617     124.002  64.214   5.522  1.00 22.40           C  
ATOM   3991  O   CYS A 617     124.762  65.190   5.516  1.00 23.48           O  
ATOM   3992  CB  CYS A 617     124.390  64.099   8.018  1.00 22.89           C  
ATOM   3993  SG  CYS A 617     123.926  63.402   9.635  1.00 21.26           S  
ATOM   3994  N   THR A 618     123.384  63.750   4.423  1.00 22.63           N  
ATOM   3995  CA  THR A 618     123.524  64.223   3.052  1.00 22.99           C  
ATOM   3996  C   THR A 618     122.147  64.425   2.436  1.00 23.09           C  
ATOM   3997  O   THR A 618     121.680  65.554   2.309  1.00 22.91           O  
ATOM   3998  CB  THR A 618     124.347  63.223   2.226  1.00 22.41           C  
ATOM   3999  OG1 THR A 618     123.743  61.930   2.313  1.00 22.72           O  
ATOM   4000  CG2 THR A 618     125.759  63.133   2.780  1.00 21.79           C  
ATOM   4001  N   GLU A 619     121.481  63.323   2.080  1.00 23.23           N  
ATOM   4002  CA  GLU A 619     120.142  63.411   1.467  1.00 23.26           C  
ATOM   4003  C   GLU A 619     119.062  64.092   2.319  1.00 23.27           C  
ATOM   4004  O   GLU A 619     118.109  64.642   1.763  1.00 23.61           O  
ATOM   4005  CB  GLU A 619     119.617  62.030   1.051  1.00 24.13           C  
ATOM   4006  CG  GLU A 619     120.230  61.454  -0.225  1.00 24.67           C  
ATOM   4007  CD  GLU A 619     121.464  60.694   0.003  1.00 24.30           C  
ATOM   4008  OE1 GLU A 619     121.814  60.508   1.137  1.00 23.66           O  
ATOM   4009  OE2 GLU A 619     122.078  60.291  -0.953  1.00 23.81           O  
ATOM   4010  N   VAL A 620     119.191  64.052   3.660  1.00 23.21           N  
ATOM   4011  CA  VAL A 620     118.232  64.640   4.591  1.00 22.97           C  
ATOM   4012  C   VAL A 620     118.240  66.167   4.432  1.00 22.11           C  
ATOM   4013  O   VAL A 620     117.223  66.837   4.637  1.00 22.09           O  
ATOM   4014  CB  VAL A 620     118.588  64.220   6.068  1.00 22.03           C  
ATOM   4015  CG1 VAL A 620     117.643  64.904   7.113  1.00 21.01           C  
ATOM   4016  CG2 VAL A 620     118.491  62.657   6.227  1.00 22.00           C  
ATOM   4017  N   ASN A 641     123.817  71.811  13.968  1.00 20.37           N  
ATOM   4018  CA  ASN A 641     123.457  70.978  15.113  1.00 20.18           C  
ATOM   4019  C   ASN A 641     123.050  69.570  14.623  1.00 20.48           C  
ATOM   4020  O   ASN A 641     121.955  69.076  14.927  1.00 20.27           O  
ATOM   4021  CB  ASN A 641     122.356  71.682  15.941  1.00 20.62           C  
ATOM   4022  CG  ASN A 641     122.154  71.131  17.393  1.00 20.47           C  
ATOM   4023  OD1 ASN A 641     123.074  70.567  18.004  1.00 20.30           O  
ATOM   4024  ND2 ASN A 641     120.950  71.326  17.941  1.00 20.50           N  
ATOM   4025  N   VAL A 642     123.945  68.950  13.827  1.00 20.44           N  
ATOM   4026  CA  VAL A 642     123.753  67.637  13.203  1.00 20.35           C  
ATOM   4027  C   VAL A 642     124.835  66.655  13.628  1.00 20.34           C  
ATOM   4028  O   VAL A 642     126.026  66.914  13.462  1.00 21.46           O  
ATOM   4029  CB  VAL A 642     123.768  67.781  11.677  1.00 20.32           C  
ATOM   4030  CG1 VAL A 642     123.584  66.444  11.043  1.00 20.74           C  
ATOM   4031  CG2 VAL A 642     122.676  68.744  11.251  1.00 20.72           C  
ATOM   4032  N   PHE A 643     124.410  65.525  14.168  1.00 20.03           N  
ATOM   4033  CA  PHE A 643     125.313  64.503  14.668  1.00 19.96           C  
ATOM   4034  C   PHE A 643     125.134  63.176  13.943  1.00 19.80           C  
ATOM   4035  O   PHE A 643     124.071  62.557  13.997  1.00 20.23           O  
ATOM   4036  CB  PHE A 643     125.079  64.344  16.172  1.00 19.66           C  
ATOM   4037  CG  PHE A 643     125.902  63.310  16.887  1.00 19.50           C  
ATOM   4038  CD1 PHE A 643     127.156  62.925  16.457  1.00 19.02           C  
ATOM   4039  CD2 PHE A 643     125.399  62.729  18.028  1.00 19.12           C  
ATOM   4040  CE1 PHE A 643     127.871  61.978  17.149  1.00 19.12           C  
ATOM   4041  CE2 PHE A 643     126.111  61.790  18.719  1.00 18.50           C  
ATOM   4042  CZ  PHE A 643     127.348  61.411  18.277  1.00 18.71           C  
ATOM   4043  N   GLN A 644     126.171  62.734  13.247  1.00 19.98           N  
ATOM   4044  CA  GLN A 644     126.087  61.470  12.531  1.00 19.86           C  
ATOM   4045  C   GLN A 644     126.439  60.328  13.468  1.00 19.55           C  
ATOM   4046  O   GLN A 644     127.528  60.305  14.038  1.00 19.31           O  
ATOM   4047  CB  GLN A 644     127.055  61.441  11.348  1.00 19.99           C  
ATOM   4048  CG  GLN A 644     127.007  60.155  10.501  1.00 20.48           C  
ATOM   4049  CD  GLN A 644     125.793  60.077   9.591  1.00 20.95           C  
ATOM   4050  OE1 GLN A 644     125.682  60.924   8.700  1.00 21.47           O  
ATOM   4051  NE2 GLN A 644     124.913  59.092   9.790  1.00 20.62           N  
ATOM   4052  N   THR A 645     125.534  59.371  13.604  1.00 19.34           N  
ATOM   4053  CA  THR A 645     125.754  58.214  14.456  1.00 19.13           C  
ATOM   4054  C   THR A 645     125.541  56.974  13.611  1.00 18.87           C  
ATOM   4055  O   THR A 645     125.042  57.063  12.491  1.00 19.03           O  
ATOM   4056  CB  THR A 645     124.770  58.170  15.636  1.00 18.82           C  
ATOM   4057  OG1 THR A 645     123.479  57.816  15.154  1.00 18.80           O  
ATOM   4058  CG2 THR A 645     124.685  59.516  16.324  1.00 18.76           C  
ATOM   4059  N   ARG A 646     125.842  55.799  14.144  1.00 18.52           N  
ATOM   4060  CA  ARG A 646     125.607  54.596  13.356  1.00 18.68           C  
ATOM   4061  C   ARG A 646     124.143  54.200  13.354  1.00 18.47           C  
ATOM   4062  O   ARG A 646     123.750  53.249  12.684  1.00 17.81           O  
ATOM   4063  CB  ARG A 646     126.455  53.437  13.828  1.00 18.19           C  
ATOM   4064  CG  ARG A 646     127.923  53.595  13.525  1.00 19.61           C  
ATOM   4065  CD  ARG A 646     128.686  52.378  13.839  1.00 19.73           C  
ATOM   4066  NE  ARG A 646     130.074  52.505  13.426  1.00 19.82           N  
ATOM   4067  CZ  ARG A 646     130.963  51.490  13.383  1.00 21.23           C  
ATOM   4068  NH1 ARG A 646     130.599  50.270  13.732  1.00 20.53           N  
ATOM   4069  NH2 ARG A 646     132.204  51.723  12.985  1.00 20.78           N  
ATOM   4070  N   ALA A 647     123.335  54.923  14.115  1.00 18.51           N  
ATOM   4071  CA  ALA A 647     121.912  54.670  14.164  1.00 18.33           C  
ATOM   4072  C   ALA A 647     121.204  55.467  13.085  1.00 19.05           C  
ATOM   4073  O   ALA A 647     120.021  55.252  12.819  1.00 19.20           O  
ATOM   4074  CB  ALA A 647     121.362  55.026  15.533  1.00 17.45           C  
ATOM   4075  N   GLY A 648     121.911  56.411  12.473  1.00 19.28           N  
ATOM   4076  CA  GLY A 648     121.283  57.326  11.537  1.00 19.76           C  
ATOM   4077  C   GLY A 648     121.771  58.752  11.769  1.00 19.66           C  
ATOM   4078  O   GLY A 648     122.699  58.971  12.554  1.00 19.97           O  
ATOM   4079  N   CYS A 649     121.146  59.714  11.080  1.00 20.46           N  
ATOM   4080  CA  CYS A 649     121.509  61.129  11.158  1.00 20.71           C  
ATOM   4081  C   CYS A 649     120.594  61.810  12.182  1.00 20.05           C  
ATOM   4082  O   CYS A 649     119.375  61.867  11.990  1.00 20.56           O  
ATOM   4083  CB  CYS A 649     121.378  61.803   9.775  1.00 21.26           C  
ATOM   4084  SG  CYS A 649     121.896  63.534   9.729  1.00 21.68           S  
ATOM   4085  N   LEU A 650     121.179  62.290  13.290  1.00 20.09           N  
ATOM   4086  CA  LEU A 650     120.447  62.895  14.401  1.00 19.98           C  
ATOM   4087  C   LEU A 650     120.502  64.407  14.330  1.00 19.79           C  
ATOM   4088  O   LEU A 650     121.570  65.010  14.419  1.00 20.06           O  
ATOM   4089  CB  LEU A 650     121.042  62.406  15.722  1.00 19.64           C  
ATOM   4090  CG  LEU A 650     120.449  62.964  16.997  1.00 19.74           C  
ATOM   4091  CD1 LEU A 650     119.015  62.534  17.132  1.00 19.96           C  
ATOM   4092  CD2 LEU A 650     121.263  62.463  18.150  1.00 20.00           C  
ATOM   4093  N   ILE A 651     119.348  65.026  14.161  1.00 19.76           N  
ATOM   4094  CA  ILE A 651     119.299  66.463  13.997  1.00 19.88           C  
ATOM   4095  C   ILE A 651     118.535  67.152  15.115  1.00 19.99           C  
ATOM   4096  O   ILE A 651     117.396  66.806  15.419  1.00 19.80           O  
ATOM   4097  CB  ILE A 651     118.679  66.814  12.640  1.00 19.77           C  
ATOM   4098  CG1 ILE A 651     119.530  66.169  11.539  1.00 19.99           C  
ATOM   4099  CG2 ILE A 651     118.602  68.327  12.472  1.00 20.82           C  
ATOM   4100  CD1 ILE A 651     118.979  66.283  10.163  1.00 19.84           C  
ATOM   4101  N   GLY A 652     119.161  68.153  15.719  1.00 20.05           N  
ATOM   4102  CA  GLY A 652     118.526  68.922  16.783  1.00 20.30           C  
ATOM   4103  C   GLY A 652     119.094  68.623  18.162  1.00 20.28           C  
ATOM   4104  O   GLY A 652     118.885  69.392  19.100  1.00 20.71           O  
ATOM   4105  N   ALA A 653     119.823  67.527  18.287  1.00 19.78           N  
ATOM   4106  CA  ALA A 653     120.454  67.186  19.552  1.00 19.82           C  
ATOM   4107  C   ALA A 653     121.898  67.652  19.547  1.00 19.75           C  
ATOM   4108  O   ALA A 653     122.624  67.424  18.580  1.00 19.41           O  
ATOM   4109  CB  ALA A 653     120.396  65.696  19.800  1.00 19.52           C  
ATOM   4110  N   GLU A 654     122.323  68.283  20.630  1.00 19.67           N  
ATOM   4111  CA  GLU A 654     123.697  68.748  20.742  1.00 19.50           C  
ATOM   4112  C   GLU A 654     124.612  67.608  21.118  1.00 19.25           C  
ATOM   4113  O   GLU A 654     124.323  66.866  22.047  1.00 19.46           O  
ATOM   4114  CB  GLU A 654     123.803  69.853  21.787  1.00 19.44           C  
ATOM   4115  CG  GLU A 654     125.190  70.456  21.935  1.00 19.61           C  
ATOM   4116  CD  GLU A 654     125.241  71.554  22.954  1.00 19.71           C  
ATOM   4117  OE1 GLU A 654     124.235  71.825  23.556  1.00 19.19           O  
ATOM   4118  OE2 GLU A 654     126.289  72.124  23.130  1.00 19.48           O  
ATOM   4119  N   HIS A 655     125.740  67.479  20.439  1.00 19.14           N  
ATOM   4120  CA  HIS A 655     126.667  66.415  20.795  1.00 18.91           C  
ATOM   4121  C   HIS A 655     127.527  66.854  21.968  1.00 18.83           C  
ATOM   4122  O   HIS A 655     128.207  67.877  21.913  1.00 18.86           O  
ATOM   4123  CB  HIS A 655     127.546  66.015  19.610  1.00 18.88           C  
ATOM   4124  CG  HIS A 655     128.434  64.841  19.894  1.00 18.88           C  
ATOM   4125  ND1 HIS A 655     129.608  64.623  19.214  1.00 19.09           N  
ATOM   4126  CD2 HIS A 655     128.322  63.827  20.781  1.00 18.89           C  
ATOM   4127  CE1 HIS A 655     130.179  63.528  19.674  1.00 18.78           C  
ATOM   4128  NE2 HIS A 655     129.419  63.030  20.624  1.00 18.75           N  
ATOM   4129  N   VAL A 656     127.453  66.092  23.045  1.00 18.84           N  
ATOM   4130  CA  VAL A 656     128.149  66.391  24.283  1.00 19.02           C  
ATOM   4131  C   VAL A 656     129.212  65.329  24.576  1.00 18.66           C  
ATOM   4132  O   VAL A 656     128.929  64.137  24.495  1.00 18.33           O  
ATOM   4133  CB  VAL A 656     127.111  66.480  25.423  1.00 19.03           C  
ATOM   4134  CG1 VAL A 656     127.770  66.693  26.758  1.00 18.18           C  
ATOM   4135  CG2 VAL A 656     126.179  67.628  25.138  1.00 19.06           C  
ATOM   4136  N   ASN A 657     130.438  65.787  24.913  1.00 18.72           N  
ATOM   4137  CA  ASN A 657     131.585  64.901  25.214  1.00 18.93           C  
ATOM   4138  C   ASN A 657     131.400  64.131  26.521  1.00 18.44           C  
ATOM   4139  O   ASN A 657     131.923  63.003  26.648  1.00 18.36           O  
ATOM   4140  CB  ASN A 657     132.882  65.734  25.279  1.00 19.31           C  
ATOM   4141  CG  ASN A 657     133.691  65.753  23.964  1.00 19.44           C  
ATOM   4142  OD1 ASN A 657     133.483  64.930  23.057  1.00 19.71           O  
ATOM   4143  ND2 ASN A 657     134.619  66.700  23.881  1.00 19.75           N  
ATOM   4144  N   ASN A 658     130.679  64.685  27.498  1.00 18.37           N  
ATOM   4145  CA  ASN A 658     130.446  64.067  28.800  1.00 17.83           C  
ATOM   4146  C   ASN A 658     129.466  62.915  28.699  1.00 17.34           C  
ATOM   4147  O   ASN A 658     128.411  63.039  28.083  1.00 17.62           O  
ATOM   4148  CB  ASN A 658     129.926  65.094  29.774  1.00 17.82           C  
ATOM   4149  CG  ASN A 658     130.910  66.162  30.032  1.00 17.57           C  
ATOM   4150  OD1 ASN A 658     132.119  65.922  30.096  1.00 17.51           O  
ATOM   4151  ND2 ASN A 658     130.423  67.363  30.176  1.00 17.22           N  
ATOM   4152  N   SER A 659     129.812  61.796  29.313  1.00 17.13           N  
ATOM   4153  CA  SER A 659     128.915  60.656  29.334  1.00 16.74           C  
ATOM   4154  C   SER A 659     127.980  60.778  30.518  1.00 16.54           C  
ATOM   4155  O   SER A 659     128.314  61.414  31.516  1.00 16.61           O  
ATOM   4156  CB  SER A 659     129.706  59.369  29.413  1.00 15.78           C  
ATOM   4157  OG  SER A 659     130.411  59.279  30.624  1.00 15.79           O  
ATOM   4158  N   TYR A 660     126.829  60.140  30.425  1.00 16.36           N  
ATOM   4159  CA  TYR A 660     125.862  60.133  31.508  1.00 16.54           C  
ATOM   4160  C   TYR A 660     125.156  58.799  31.507  1.00 16.37           C  
ATOM   4161  O   TYR A 660     125.393  57.971  30.629  1.00 15.98           O  
ATOM   4162  CB  TYR A 660     124.820  61.246  31.332  1.00 16.80           C  
ATOM   4163  CG  TYR A 660     125.370  62.654  31.205  1.00 16.94           C  
ATOM   4164  CD1 TYR A 660     125.733  63.138  29.970  1.00 17.34           C  
ATOM   4165  CD2 TYR A 660     125.497  63.458  32.312  1.00 17.24           C  
ATOM   4166  CE1 TYR A 660     126.222  64.405  29.832  1.00 17.41           C  
ATOM   4167  CE2 TYR A 660     125.988  64.740  32.176  1.00 17.40           C  
ATOM   4168  CZ  TYR A 660     126.352  65.210  30.937  1.00 17.51           C  
ATOM   4169  OH  TYR A 660     126.843  66.492  30.793  1.00 17.12           O  
ATOM   4170  N   GLU A 661     124.281  58.577  32.465  1.00 16.54           N  
ATOM   4171  CA  GLU A 661     123.491  57.358  32.440  1.00 16.77           C  
ATOM   4172  C   GLU A 661     122.504  57.471  31.288  1.00 16.92           C  
ATOM   4173  O   GLU A 661     122.005  58.565  31.020  1.00 16.73           O  
ATOM   4174  CB  GLU A 661     122.746  57.159  33.761  1.00 17.23           C  
ATOM   4175  CG  GLU A 661     123.635  56.838  34.950  1.00 17.84           C  
ATOM   4176  CD  GLU A 661     122.850  56.546  36.193  1.00 17.61           C  
ATOM   4177  OE1 GLU A 661     121.647  56.548  36.125  1.00 17.58           O  
ATOM   4178  OE2 GLU A 661     123.454  56.325  37.213  1.00 17.63           O  
ATOM   4179  N   CYS A 662     122.216  56.349  30.602  1.00 16.97           N  
ATOM   4180  CA  CYS A 662     121.296  56.331  29.468  1.00 16.87           C  
ATOM   4181  C   CYS A 662     119.872  56.699  29.903  1.00 17.08           C  
ATOM   4182  O   CYS A 662     119.381  56.214  30.923  1.00 16.83           O  
ATOM   4183  CB  CYS A 662     121.272  54.959  28.787  1.00 16.23           C  
ATOM   4184  SG  CYS A 662     120.310  54.915  27.230  1.00 16.22           S  
ATOM   4185  N   ASP A 663     119.229  57.564  29.114  1.00 17.09           N  
ATOM   4186  CA  ASP A 663     117.883  58.087  29.339  1.00 17.52           C  
ATOM   4187  C   ASP A 663     116.959  57.668  28.184  1.00 17.57           C  
ATOM   4188  O   ASP A 663     116.230  56.677  28.312  1.00 17.50           O  
ATOM   4189  CB  ASP A 663     118.009  59.603  29.486  1.00 17.90           C  
ATOM   4190  CG  ASP A 663     116.759  60.303  29.864  1.00 17.97           C  
ATOM   4191  OD1 ASP A 663     116.803  61.507  30.005  1.00 18.64           O  
ATOM   4192  OD2 ASP A 663     115.734  59.674  30.012  1.00 18.32           O  
ATOM   4193  N   ILE A 664     116.999  58.374  27.057  1.00 17.74           N  
ATOM   4194  CA  ILE A 664     116.237  57.946  25.889  1.00 17.60           C  
ATOM   4195  C   ILE A 664     117.219  57.354  24.896  1.00 17.15           C  
ATOM   4196  O   ILE A 664     117.976  58.098  24.285  1.00 17.44           O  
ATOM   4197  CB  ILE A 664     115.508  59.111  25.199  1.00 18.24           C  
ATOM   4198  CG1 ILE A 664     114.532  59.776  26.165  1.00 18.64           C  
ATOM   4199  CG2 ILE A 664     114.790  58.592  23.949  1.00 18.40           C  
ATOM   4200  CD1 ILE A 664     113.960  61.096  25.657  1.00 19.78           C  
ATOM   4201  N   PRO A 665     117.245  56.042  24.706  1.00 17.29           N  
ATOM   4202  CA  PRO A 665     118.230  55.362  23.908  1.00 16.55           C  
ATOM   4203  C   PRO A 665     118.028  55.650  22.446  1.00 16.57           C  
ATOM   4204  O   PRO A 665     116.900  55.642  21.964  1.00 16.88           O  
ATOM   4205  CB  PRO A 665     117.949  53.907  24.230  1.00 15.96           C  
ATOM   4206  CG  PRO A 665     116.493  53.874  24.588  1.00 16.31           C  
ATOM   4207  CD  PRO A 665     116.216  55.195  25.252  1.00 17.30           C  
ATOM   4208  N   ILE A 666     119.123  55.835  21.730  1.00 16.24           N  
ATOM   4209  CA  ILE A 666     119.083  55.993  20.295  1.00 15.95           C  
ATOM   4210  C   ILE A 666     119.600  54.745  19.616  1.00 15.49           C  
ATOM   4211  O   ILE A 666     118.965  54.207  18.711  1.00 16.22           O  
ATOM   4212  CB  ILE A 666     119.867  57.234  19.866  1.00 16.35           C  
ATOM   4213  CG1 ILE A 666     119.135  58.452  20.393  1.00 16.80           C  
ATOM   4214  CG2 ILE A 666     120.058  57.260  18.388  1.00 16.62           C  
ATOM   4215  CD1 ILE A 666     119.858  59.723  20.203  1.00 17.34           C  
ATOM   4216  N   GLY A 667     120.746  54.274  20.069  1.00 15.13           N  
ATOM   4217  CA  GLY A 667     121.344  53.084  19.499  1.00 14.32           C  
ATOM   4218  C   GLY A 667     122.826  53.274  19.265  1.00 14.72           C  
ATOM   4219  O   GLY A 667     123.313  54.398  19.192  1.00 14.56           O  
ATOM   4220  N   ALA A 668     123.546  52.172  19.138  1.00 14.44           N  
ATOM   4221  CA  ALA A 668     124.971  52.189  18.868  1.00 14.12           C  
ATOM   4222  C   ALA A 668     125.750  52.955  19.924  1.00 14.26           C  
ATOM   4223  O   ALA A 668     126.712  53.651  19.609  1.00 15.15           O  
ATOM   4224  CB  ALA A 668     125.235  52.792  17.499  1.00 14.76           C  
ATOM   4225  N   GLY A 669     125.343  52.823  21.181  1.00 14.95           N  
ATOM   4226  CA  GLY A 669     126.048  53.440  22.289  1.00 14.45           C  
ATOM   4227  C   GLY A 669     125.607  54.864  22.581  1.00 15.05           C  
ATOM   4228  O   GLY A 669     126.063  55.458  23.557  1.00 14.97           O  
ATOM   4229  N   ILE A 670     124.735  55.415  21.746  1.00 15.17           N  
ATOM   4230  CA  ILE A 670     124.279  56.787  21.911  1.00 15.49           C  
ATOM   4231  C   ILE A 670     122.890  56.847  22.552  1.00 15.55           C  
ATOM   4232  O   ILE A 670     121.976  56.116  22.149  1.00 16.03           O  
ATOM   4233  CB  ILE A 670     124.259  57.526  20.551  1.00 15.97           C  
ATOM   4234  CG1 ILE A 670     125.642  57.468  19.873  1.00 15.64           C  
ATOM   4235  CG2 ILE A 670     123.811  58.974  20.720  1.00 16.73           C  
ATOM   4236  CD1 ILE A 670     126.779  58.086  20.664  1.00 15.90           C  
ATOM   4237  N   CYS A 671     122.753  57.711  23.564  1.00 16.20           N  
ATOM   4238  CA  CYS A 671     121.506  58.010  24.265  1.00 16.75           C  
ATOM   4239  C   CYS A 671     121.328  59.528  24.243  1.00 17.11           C  
ATOM   4240  O   CYS A 671     122.311  60.263  24.078  1.00 17.90           O  
ATOM   4241  CB  CYS A 671     121.502  57.457  25.714  1.00 16.70           C  
ATOM   4242  SG  CYS A 671     121.634  55.629  25.826  1.00 15.94           S  
ATOM   4243  N   ALA A 672     120.083  60.005  24.412  1.00 17.63           N  
ATOM   4244  CA  ALA A 672     119.770  61.434  24.466  1.00 18.37           C  
ATOM   4245  C   ALA A 672     118.964  61.785  25.697  1.00 18.24           C  
ATOM   4246  O   ALA A 672     118.274  60.946  26.278  1.00 18.31           O  
ATOM   4247  CB  ALA A 672     119.014  61.857  23.234  1.00 18.84           C  
ATOM   4248  N   SER A 673     119.073  63.037  26.111  1.00 18.84           N  
ATOM   4249  CA  SER A 673     118.351  63.522  27.280  1.00 19.00           C  
ATOM   4250  C   SER A 673     118.140  65.021  27.205  1.00 19.29           C  
ATOM   4251  O   SER A 673     118.749  65.698  26.381  1.00 19.54           O  
ATOM   4252  CB  SER A 673     119.107  63.191  28.537  1.00 18.82           C  
ATOM   4253  OG  SER A 673     120.281  63.930  28.598  1.00 18.66           O  
ATOM   4254  N   TYR A 674     117.282  65.549  28.071  1.00 19.64           N  
ATOM   4255  CA  TYR A 674     117.029  66.988  28.120  1.00 20.00           C  
ATOM   4256  C   TYR A 674     117.708  67.619  29.339  1.00 20.02           C  
ATOM   4257  O   TYR A 674     117.307  67.373  30.477  1.00 19.80           O  
ATOM   4258  CB  TYR A 674     115.516  67.202  28.128  1.00 20.28           C  
ATOM   4259  CG  TYR A 674     115.033  68.615  28.002  1.00 20.65           C  
ATOM   4260  CD1 TYR A 674     115.192  69.290  26.819  1.00 20.83           C  
ATOM   4261  CD2 TYR A 674     114.393  69.219  29.057  1.00 20.96           C  
ATOM   4262  CE1 TYR A 674     114.724  70.570  26.689  1.00 20.98           C  
ATOM   4263  CE2 TYR A 674     113.921  70.500  28.928  1.00 21.26           C  
ATOM   4264  CZ  TYR A 674     114.085  71.174  27.750  1.00 21.35           C  
ATOM   4265  OH  TYR A 674     113.615  72.460  27.622  1.00 21.91           O  
ATOM   4266  N   GLN A 675     118.762  68.400  29.093  1.00 20.00           N  
ATOM   4267  CA  GLN A 675     119.583  68.963  30.168  1.00 20.44           C  
ATOM   4268  C   GLN A 675     120.180  70.321  29.774  1.00 20.58           C  
ATOM   4269  O   GLN A 675     120.027  70.750  28.634  1.00 20.61           O  
ATOM   4270  CB  GLN A 675     120.725  67.981  30.529  1.00 19.84           C  
ATOM   4271  CG  GLN A 675     120.292  66.651  31.128  1.00 19.42           C  
ATOM   4272  CD  GLN A 675     121.484  65.813  31.595  1.00 18.85           C  
ATOM   4273  OE1 GLN A 675     121.865  64.820  30.969  1.00 18.27           O  
ATOM   4274  NE2 GLN A 675     122.079  66.221  32.712  1.00 17.83           N  
ATOM   4275  N   THR A 676     120.898  70.978  30.709  1.00 20.57           N  
ATOM   4276  CA  THR A 676     121.542  72.280  30.486  1.00 20.82           C  
ATOM   4277  C   THR A 676     122.998  72.074  30.071  1.00 21.91           C  
ATOM   4278  O   THR A 676     123.681  73.014  29.660  1.00 21.39           O  
ATOM   4279  CB  THR A 676     121.480  73.182  31.761  1.00 21.24           C  
ATOM   4280  OG1 THR A 676     122.113  72.506  32.863  1.00 21.83           O  
ATOM   4281  CG2 THR A 676     120.023  73.523  32.156  1.00 21.07           C  
ATOM   4282  N   SER A 689     117.634  77.477  28.915  1.00 21.81           N  
ATOM   4283  CA  SER A 689     118.965  76.913  29.138  1.00 21.19           C  
ATOM   4284  C   SER A 689     119.054  75.408  28.819  1.00 21.28           C  
ATOM   4285  O   SER A 689     120.147  74.918  28.512  1.00 21.07           O  
ATOM   4286  CB  SER A 689     119.416  77.179  30.578  1.00 21.82           C  
ATOM   4287  OG  SER A 689     118.592  76.523  31.508  1.00 21.88           O  
ATOM   4288  N   GLN A 690     117.922  74.686  28.896  1.00 21.17           N  
ATOM   4289  CA  GLN A 690     117.851  73.247  28.622  1.00 21.15           C  
ATOM   4290  C   GLN A 690     117.662  72.966  27.143  1.00 20.92           C  
ATOM   4291  O   GLN A 690     116.997  73.722  26.433  1.00 21.11           O  
ATOM   4292  CB  GLN A 690     116.714  72.599  29.403  1.00 21.13           C  
ATOM   4293  CG  GLN A 690     116.899  72.582  30.883  1.00 21.15           C  
ATOM   4294  CD  GLN A 690     115.731  71.965  31.587  1.00 21.24           C  
ATOM   4295  OE1 GLN A 690     114.598  72.435  31.457  1.00 20.73           O  
ATOM   4296  NE2 GLN A 690     115.981  70.901  32.337  1.00 20.83           N  
ATOM   4297  N   SER A 691     118.233  71.862  26.695  1.00 20.88           N  
ATOM   4298  CA  SER A 691     118.093  71.409  25.328  1.00 20.62           C  
ATOM   4299  C   SER A 691     118.348  69.920  25.247  1.00 20.21           C  
ATOM   4300  O   SER A 691     118.840  69.307  26.196  1.00 20.52           O  
ATOM   4301  CB  SER A 691     119.054  72.141  24.420  1.00 20.80           C  
ATOM   4302  OG  SER A 691     120.376  71.776  24.688  1.00 20.80           O  
ATOM   4303  N   ILE A 692     118.017  69.328  24.118  1.00 20.07           N  
ATOM   4304  CA  ILE A 692     118.277  67.920  23.941  1.00 19.92           C  
ATOM   4305  C   ILE A 692     119.724  67.709  23.572  1.00 19.58           C  
ATOM   4306  O   ILE A 692     120.245  68.373  22.676  1.00 19.86           O  
ATOM   4307  CB  ILE A 692     117.359  67.310  22.882  1.00 19.86           C  
ATOM   4308  CG1 ILE A 692     115.924  67.434  23.356  1.00 20.02           C  
ATOM   4309  CG2 ILE A 692     117.738  65.846  22.655  1.00 19.88           C  
ATOM   4310  CD1 ILE A 692     114.910  67.142  22.314  1.00 20.08           C  
ATOM   4311  N   ILE A 693     120.363  66.789  24.274  1.00 19.46           N  
ATOM   4312  CA  ILE A 693     121.751  66.463  24.039  1.00 19.28           C  
ATOM   4313  C   ILE A 693     121.887  64.999  23.705  1.00 19.07           C  
ATOM   4314  O   ILE A 693     121.042  64.191  24.080  1.00 19.24           O  
ATOM   4315  CB  ILE A 693     122.617  66.777  25.270  1.00 19.30           C  
ATOM   4316  CG1 ILE A 693     122.165  65.919  26.477  1.00 19.30           C  
ATOM   4317  CG2 ILE A 693     122.523  68.257  25.591  1.00 19.37           C  
ATOM   4318  CD1 ILE A 693     123.099  65.963  27.666  1.00 19.09           C  
ATOM   4319  N   ALA A 694     122.972  64.660  23.040  1.00 18.89           N  
ATOM   4320  CA  ALA A 694     123.290  63.290  22.706  1.00 18.75           C  
ATOM   4321  C   ALA A 694     124.699  62.989  23.149  1.00 18.18           C  
ATOM   4322  O   ALA A 694     125.590  63.828  23.031  1.00 18.83           O  
ATOM   4323  CB  ALA A 694     123.139  63.058  21.223  1.00 19.00           C  
ATOM   4324  N   TYR A 695     124.901  61.792  23.654  1.00 17.75           N  
ATOM   4325  CA  TYR A 695     126.191  61.404  24.190  1.00 17.21           C  
ATOM   4326  C   TYR A 695     126.381  59.910  24.184  1.00 16.53           C  
ATOM   4327  O   TYR A 695     125.415  59.153  24.091  1.00 17.10           O  
ATOM   4328  CB  TYR A 695     126.305  61.918  25.618  1.00 17.44           C  
ATOM   4329  CG  TYR A 695     125.123  61.506  26.447  1.00 17.10           C  
ATOM   4330  CD1 TYR A 695     125.095  60.303  27.106  1.00 17.09           C  
ATOM   4331  CD2 TYR A 695     124.054  62.339  26.529  1.00 17.73           C  
ATOM   4332  CE1 TYR A 695     123.991  59.943  27.833  1.00 16.95           C  
ATOM   4333  CE2 TYR A 695     122.962  61.985  27.252  1.00 17.97           C  
ATOM   4334  CZ  TYR A 695     122.924  60.795  27.894  1.00 17.30           C  
ATOM   4335  OH  TYR A 695     121.818  60.457  28.611  1.00 17.64           O  
ATOM   4336  N   THR A 696     127.624  59.476  24.326  1.00 16.51           N  
ATOM   4337  CA  THR A 696     127.875  58.065  24.507  1.00 15.84           C  
ATOM   4338  C   THR A 696     127.562  57.745  25.948  1.00 15.41           C  
ATOM   4339  O   THR A 696     128.028  58.434  26.851  1.00 15.65           O  
ATOM   4340  CB  THR A 696     129.320  57.694  24.171  1.00 14.86           C  
ATOM   4341  OG1 THR A 696     129.589  58.035  22.810  1.00 14.85           O  
ATOM   4342  CG2 THR A 696     129.544  56.218  24.365  1.00 14.90           C  
ATOM   4343  N   MET A 697     126.747  56.731  26.172  1.00 15.09           N  
ATOM   4344  CA  MET A 697     126.321  56.440  27.529  1.00 14.81           C  
ATOM   4345  C   MET A 697     127.439  55.873  28.378  1.00 14.13           C  
ATOM   4346  O   MET A 697     128.300  55.143  27.888  1.00 13.77           O  
ATOM   4347  CB  MET A 697     125.131  55.492  27.539  1.00 14.97           C  
ATOM   4348  CG  MET A 697     125.397  54.120  26.977  1.00 14.17           C  
ATOM   4349  SD  MET A 697     123.965  53.063  27.076  1.00 14.94           S  
ATOM   4350  CE  MET A 697     124.575  51.553  26.419  1.00 13.37           C  
ATOM   4351  N   SER A 698     127.397  56.205  29.659  1.00 14.30           N  
ATOM   4352  CA  SER A 698     128.301  55.667  30.656  1.00 13.47           C  
ATOM   4353  C   SER A 698     127.853  54.280  31.054  1.00 12.55           C  
ATOM   4354  O   SER A 698     126.656  54.013  31.147  1.00 12.67           O  
ATOM   4355  CB  SER A 698     128.331  56.536  31.887  1.00 13.81           C  
ATOM   4356  OG  SER A 698     129.149  55.960  32.868  1.00 12.44           O  
ATOM   4357  N   LEU A 699     128.798  53.395  31.320  1.00 11.90           N  
ATOM   4358  CA  LEU A 699     128.433  52.064  31.770  1.00 11.24           C  
ATOM   4359  C   LEU A 699     128.528  51.951  33.278  1.00 10.98           C  
ATOM   4360  O   LEU A 699     128.318  50.877  33.838  1.00 10.35           O  
ATOM   4361  CB  LEU A 699     129.330  51.015  31.134  1.00 10.88           C  
ATOM   4362  CG  LEU A 699     129.361  50.975  29.624  1.00 11.22           C  
ATOM   4363  CD1 LEU A 699     130.257  49.855  29.226  1.00 10.11           C  
ATOM   4364  CD2 LEU A 699     127.966  50.806  29.049  1.00 11.44           C  
ATOM   4365  N   GLY A 700     128.859  53.055  33.930  1.00 10.87           N  
ATOM   4366  CA  GLY A 700     129.044  53.074  35.371  1.00 10.63           C  
ATOM   4367  C   GLY A 700     130.373  53.720  35.718  1.00 10.20           C  
ATOM   4368  O   GLY A 700     131.208  53.953  34.843  1.00 10.36           O  
ATOM   4369  N   ALA A 701     130.559  54.037  36.993  1.00  9.71           N  
ATOM   4370  CA  ALA A 701     131.793  54.661  37.447  1.00  9.62           C  
ATOM   4371  C   ALA A 701     132.936  53.679  37.357  1.00 10.40           C  
ATOM   4372  O   ALA A 701     132.740  52.483  37.562  1.00  5.55           O  
ATOM   4373  CB  ALA A 701     131.653  55.150  38.873  1.00  9.39           C  
ATOM   4374  N   GLU A 702     134.126  54.177  37.075  1.00  9.86           N  
ATOM   4375  CA  GLU A 702     135.309  53.333  37.054  1.00  9.52           C  
ATOM   4376  C   GLU A 702     135.855  53.196  38.467  1.00  9.18           C  
ATOM   4377  O   GLU A 702     135.999  54.191  39.176  1.00  9.76           O  
ATOM   4378  CB  GLU A 702     136.347  53.929  36.113  1.00  9.55           C  
ATOM   4379  CG  GLU A 702     137.584  53.097  35.899  1.00  9.46           C  
ATOM   4380  CD  GLU A 702     138.498  53.737  34.897  1.00  9.57           C  
ATOM   4381  OE1 GLU A 702     138.123  54.744  34.351  1.00  9.31           O  
ATOM   4382  OE2 GLU A 702     139.574  53.233  34.678  1.00  9.24           O  
ATOM   4383  N   ASN A 703     136.133  51.969  38.884  1.00  9.62           N  
ATOM   4384  CA  ASN A 703     136.607  51.716  40.239  1.00  9.13           C  
ATOM   4385  C   ASN A 703     137.578  50.560  40.321  1.00  8.90           C  
ATOM   4386  O   ASN A 703     137.157  49.410  40.305  1.00  9.07           O  
ATOM   4387  CB  ASN A 703     135.440  51.432  41.160  1.00  9.26           C  
ATOM   4388  CG  ASN A 703     135.874  51.279  42.579  1.00  8.46           C  
ATOM   4389  OD1 ASN A 703     137.014  51.606  42.914  1.00  8.73           O  
ATOM   4390  ND2 ASN A 703     135.006  50.794  43.426  1.00  8.28           N  
ATOM   4391  N   SER A 704     138.870  50.836  40.411  1.00  8.83           N  
ATOM   4392  CA  SER A 704     139.827  49.743  40.507  1.00  8.50           C  
ATOM   4393  C   SER A 704     139.761  49.113  41.888  1.00  8.30           C  
ATOM   4394  O   SER A 704     139.464  49.786  42.873  1.00  8.40           O  
ATOM   4395  CB  SER A 704     141.226  50.248  40.252  1.00  8.41           C  
ATOM   4396  OG  SER A 704     141.607  51.166  41.236  1.00  8.32           O  
ATOM   4397  N   VAL A 705     140.108  47.841  41.978  1.00  8.21           N  
ATOM   4398  CA  VAL A 705     140.152  47.164  43.263  1.00  8.26           C  
ATOM   4399  C   VAL A 705     141.589  47.116  43.735  1.00  8.18           C  
ATOM   4400  O   VAL A 705     142.484  46.773  42.964  1.00  8.24           O  
ATOM   4401  CB  VAL A 705     139.552  45.749  43.155  1.00  8.15           C  
ATOM   4402  CG1 VAL A 705     139.640  45.018  44.495  1.00  7.70           C  
ATOM   4403  CG2 VAL A 705     138.105  45.859  42.704  1.00  8.51           C  
ATOM   4404  N   ALA A 706     141.826  47.460  44.994  1.00  8.08           N  
ATOM   4405  CA  ALA A 706     143.186  47.505  45.520  1.00  8.02           C  
ATOM   4406  C   ALA A 706     143.702  46.119  45.842  1.00  8.20           C  
ATOM   4407  O   ALA A 706     143.973  45.794  46.994  1.00  8.16           O  
ATOM   4408  CB  ALA A 706     143.231  48.359  46.764  1.00  8.04           C  
ATOM   4409  N   TYR A 707     143.850  45.317  44.809  1.00  8.18           N  
ATOM   4410  CA  TYR A 707     144.285  43.948  44.929  1.00  8.42           C  
ATOM   4411  C   TYR A 707     145.762  43.847  45.211  1.00  8.35           C  
ATOM   4412  O   TYR A 707     146.570  44.556  44.615  1.00  8.74           O  
ATOM   4413  CB  TYR A 707     143.969  43.182  43.655  1.00  8.37           C  
ATOM   4414  CG  TYR A 707     144.406  41.752  43.699  1.00  8.21           C  
ATOM   4415  CD1 TYR A 707     143.594  40.800  44.238  1.00  7.77           C  
ATOM   4416  CD2 TYR A 707     145.639  41.395  43.224  1.00  8.41           C  
ATOM   4417  CE1 TYR A 707     144.017  39.500  44.299  1.00  7.70           C  
ATOM   4418  CE2 TYR A 707     146.053  40.101  43.294  1.00  8.84           C  
ATOM   4419  CZ  TYR A 707     145.257  39.160  43.830  1.00 11.69           C  
ATOM   4420  OH  TYR A 707     145.695  37.863  43.908  1.00  7.31           O  
ATOM   4421  N   SER A 708     146.105  42.936  46.100  1.00  8.30           N  
ATOM   4422  CA  SER A 708     147.476  42.559  46.384  1.00  8.44           C  
ATOM   4423  C   SER A 708     147.408  41.144  46.923  1.00  8.79           C  
ATOM   4424  O   SER A 708     146.324  40.689  47.290  1.00  8.18           O  
ATOM   4425  CB  SER A 708     148.118  43.507  47.366  1.00  8.48           C  
ATOM   4426  OG  SER A 708     147.515  43.397  48.595  1.00  8.58           O  
ATOM   4427  N   ASN A 709     148.550  40.458  46.999  1.00  8.68           N  
ATOM   4428  CA  ASN A 709     148.599  39.044  47.415  1.00  8.52           C  
ATOM   4429  C   ASN A 709     148.475  38.840  48.927  1.00  8.55           C  
ATOM   4430  O   ASN A 709     148.354  37.689  49.376  1.00  8.56           O  
ATOM   4431  CB  ASN A 709     149.873  38.393  46.878  1.00  8.52           C  
ATOM   4432  CG  ASN A 709     151.177  39.116  47.264  1.00  8.70           C  
ATOM   4433  OD1 ASN A 709     151.172  40.305  47.624  1.00  8.54           O  
ATOM   4434  ND2 ASN A 709     152.279  38.401  47.179  1.00  8.64           N  
ATOM   4435  N   ASN A 710     148.496  39.911  49.738  1.00  8.48           N  
ATOM   4436  CA  ASN A 710     148.389  39.826  51.192  1.00  8.56           C  
ATOM   4437  C   ASN A 710     147.472  40.871  51.801  1.00  8.25           C  
ATOM   4438  O   ASN A 710     147.706  41.291  52.930  1.00  8.29           O  
ATOM   4439  CB  ASN A 710     149.753  39.909  51.826  1.00  8.56           C  
ATOM   4440  CG  ASN A 710     150.408  41.198  51.570  1.00  8.58           C  
ATOM   4441  OD1 ASN A 710     149.941  42.002  50.756  1.00  8.72           O  
ATOM   4442  ND2 ASN A 710     151.498  41.434  52.244  1.00  8.41           N  
ATOM   4443  N   SER A 711     146.423  41.285  51.102  1.00  8.26           N  
ATOM   4444  CA  SER A 711     145.520  42.284  51.670  1.00  8.07           C  
ATOM   4445  C   SER A 711     144.078  41.898  51.472  1.00  8.70           C  
ATOM   4446  O   SER A 711     143.655  41.571  50.366  1.00  8.14           O  
ATOM   4447  CB  SER A 711     145.737  43.640  51.048  1.00  8.28           C  
ATOM   4448  OG  SER A 711     144.871  44.598  51.604  1.00  8.36           O  
ATOM   4449  N   ILE A 712     143.323  41.926  52.555  1.00  8.05           N  
ATOM   4450  CA  ILE A 712     141.922  41.563  52.514  1.00  7.84           C  
ATOM   4451  C   ILE A 712     141.072  42.673  53.098  1.00  7.62           C  
ATOM   4452  O   ILE A 712     141.422  43.256  54.121  1.00  7.92           O  
ATOM   4453  CB  ILE A 712     141.690  40.250  53.287  1.00  7.85           C  
ATOM   4454  CG1 ILE A 712     140.261  39.760  53.098  1.00  7.54           C  
ATOM   4455  CG2 ILE A 712     141.974  40.459  54.766  1.00  8.06           C  
ATOM   4456  CD1 ILE A 712     140.046  38.324  53.517  1.00  7.30           C  
ATOM   4457  N   ALA A 713     139.949  42.970  52.472  1.00  7.97           N  
ATOM   4458  CA  ALA A 713     139.049  43.952  53.052  1.00  7.57           C  
ATOM   4459  C   ALA A 713     137.902  43.239  53.724  1.00  7.55           C  
ATOM   4460  O   ALA A 713     137.206  42.432  53.111  1.00  7.54           O  
ATOM   4461  CB  ALA A 713     138.550  44.928  52.018  1.00  8.13           C  
ATOM   4462  N   ILE A 714     137.730  43.507  55.003  1.00  7.63           N  
ATOM   4463  CA  ILE A 714     136.696  42.852  55.787  1.00  7.68           C  
ATOM   4464  C   ILE A 714     135.770  43.900  56.346  1.00  7.40           C  
ATOM   4465  O   ILE A 714     136.244  44.836  56.990  1.00  7.50           O  
ATOM   4466  CB  ILE A 714     137.314  42.031  56.926  1.00  7.57           C  
ATOM   4467  CG1 ILE A 714     138.203  40.984  56.321  1.00  7.64           C  
ATOM   4468  CG2 ILE A 714     136.239  41.403  57.821  1.00  7.44           C  
ATOM   4469  CD1 ILE A 714     139.065  40.310  57.279  1.00  7.61           C  
ATOM   4470  N   PRO A 715     134.463  43.794  56.125  1.00  7.59           N  
ATOM   4471  CA  PRO A 715     133.502  44.744  56.569  1.00  7.52           C  
ATOM   4472  C   PRO A 715     133.470  44.769  58.066  1.00  7.29           C  
ATOM   4473  O   PRO A 715     133.498  43.721  58.697  1.00  7.60           O  
ATOM   4474  CB  PRO A 715     132.211  44.238  55.958  1.00  7.30           C  
ATOM   4475  CG  PRO A 715     132.437  42.788  55.735  1.00  7.42           C  
ATOM   4476  CD  PRO A 715     133.900  42.646  55.442  1.00  7.51           C  
ATOM   4477  N   THR A 716     133.384  45.959  58.614  1.00  7.43           N  
ATOM   4478  CA  THR A 716     133.318  46.207  60.048  1.00  7.54           C  
ATOM   4479  C   THR A 716     131.914  46.573  60.542  1.00  7.62           C  
ATOM   4480  O   THR A 716     131.625  46.461  61.732  1.00  7.82           O  
ATOM   4481  CB  THR A 716     134.283  47.335  60.420  1.00  7.53           C  
ATOM   4482  OG1 THR A 716     133.877  48.540  59.767  1.00  7.53           O  
ATOM   4483  CG2 THR A 716     135.690  47.002  59.991  1.00  7.41           C  
ATOM   4484  N   ASN A 717     131.043  46.985  59.614  1.00  7.40           N  
ATOM   4485  CA  ASN A 717     129.660  47.375  59.884  1.00  7.61           C  
ATOM   4486  C   ASN A 717     128.801  46.894  58.723  1.00  7.20           C  
ATOM   4487  O   ASN A 717     129.322  46.531  57.672  1.00  7.43           O  
ATOM   4488  CB  ASN A 717     129.558  48.892  60.072  1.00  7.77           C  
ATOM   4489  CG  ASN A 717     128.321  49.344  60.847  1.00  8.17           C  
ATOM   4490  OD1 ASN A 717     127.400  48.553  61.103  1.00  7.92           O  
ATOM   4491  ND2 ASN A 717     128.304  50.613  61.207  1.00  8.44           N  
ATOM   4492  N   PHE A 718     127.478  46.936  58.909  1.00  7.28           N  
ATOM   4493  CA  PHE A 718     126.498  46.491  57.922  1.00  7.06           C  
ATOM   4494  C   PHE A 718     125.246  47.321  57.969  1.00  7.17           C  
ATOM   4495  O   PHE A 718     124.968  48.008  58.956  1.00  7.42           O  
ATOM   4496  CB  PHE A 718     126.102  45.051  58.173  1.00  6.98           C  
ATOM   4497  CG  PHE A 718     125.434  44.913  59.462  1.00  7.03           C  
ATOM   4498  CD1 PHE A 718     124.095  45.101  59.565  1.00  7.11           C  
ATOM   4499  CD2 PHE A 718     126.148  44.613  60.587  1.00  7.04           C  
ATOM   4500  CE1 PHE A 718     123.487  45.018  60.751  1.00  7.23           C  
ATOM   4501  CE2 PHE A 718     125.539  44.515  61.792  1.00  7.07           C  
ATOM   4502  CZ  PHE A 718     124.204  44.725  61.878  1.00  7.16           C  
ATOM   4503  N   THR A 719     124.479  47.225  56.904  1.00  7.16           N  
ATOM   4504  CA  THR A 719     123.190  47.857  56.828  1.00  7.19           C  
ATOM   4505  C   THR A 719     122.154  46.869  56.341  1.00  7.09           C  
ATOM   4506  O   THR A 719     122.424  46.052  55.462  1.00  7.15           O  
ATOM   4507  CB  THR A 719     123.235  49.087  55.903  1.00  7.04           C  
ATOM   4508  OG1 THR A 719     121.952  49.707  55.872  1.00  7.18           O  
ATOM   4509  CG2 THR A 719     123.629  48.687  54.495  1.00  6.93           C  
ATOM   4510  N   ILE A 720     120.966  46.944  56.904  1.00  7.29           N  
ATOM   4511  CA  ILE A 720     119.873  46.138  56.413  1.00  7.25           C  
ATOM   4512  C   ILE A 720     119.059  46.971  55.460  1.00  7.26           C  
ATOM   4513  O   ILE A 720     118.555  48.031  55.825  1.00  7.62           O  
ATOM   4514  CB  ILE A 720     118.974  45.645  57.547  1.00  7.57           C  
ATOM   4515  CG1 ILE A 720     119.798  44.909  58.602  1.00  7.51           C  
ATOM   4516  CG2 ILE A 720     117.865  44.767  56.996  1.00  7.57           C  
ATOM   4517  CD1 ILE A 720     120.601  43.721  58.121  1.00  7.29           C  
ATOM   4518  N   SER A 721     118.945  46.503  54.234  1.00  7.17           N  
ATOM   4519  CA  SER A 721     118.207  47.236  53.232  1.00  7.29           C  
ATOM   4520  C   SER A 721     117.015  46.440  52.782  1.00  7.41           C  
ATOM   4521  O   SER A 721     117.014  45.211  52.845  1.00  7.26           O  
ATOM   4522  CB  SER A 721     119.089  47.550  52.046  1.00  6.96           C  
ATOM   4523  OG  SER A 721     119.501  46.383  51.407  1.00  6.85           O  
ATOM   4524  N   VAL A 722     115.995  47.133  52.320  1.00  7.58           N  
ATOM   4525  CA  VAL A 722     114.826  46.469  51.794  1.00  7.66           C  
ATOM   4526  C   VAL A 722     114.586  46.950  50.386  1.00  7.78           C  
ATOM   4527  O   VAL A 722     114.528  48.152  50.141  1.00  7.83           O  
ATOM   4528  CB  VAL A 722     113.596  46.731  52.675  1.00  8.14           C  
ATOM   4529  CG1 VAL A 722     112.380  46.025  52.097  1.00  8.06           C  
ATOM   4530  CG2 VAL A 722     113.881  46.239  54.069  1.00  8.20           C  
ATOM   4531  N   THR A 723     114.465  46.018  49.460  1.00  7.73           N  
ATOM   4532  CA  THR A 723     114.231  46.387  48.079  1.00  7.79           C  
ATOM   4533  C   THR A 723     112.902  45.849  47.627  1.00  7.93           C  
ATOM   4534  O   THR A 723     112.387  44.888  48.191  1.00  8.05           O  
ATOM   4535  CB  THR A 723     115.335  45.850  47.159  1.00  7.55           C  
ATOM   4536  OG1 THR A 723     115.292  44.423  47.136  1.00  7.60           O  
ATOM   4537  CG2 THR A 723     116.687  46.285  47.673  1.00  7.13           C  
ATOM   4538  N   THR A 724     112.351  46.433  46.578  1.00  8.09           N  
ATOM   4539  CA  THR A 724     111.063  45.976  46.100  1.00  8.19           C  
ATOM   4540  C   THR A 724     111.148  45.385  44.711  1.00  8.24           C  
ATOM   4541  O   THR A 724     111.583  46.043  43.771  1.00  8.40           O  
ATOM   4542  CB  THR A 724     110.061  47.136  46.094  1.00  8.37           C  
ATOM   4543  OG1 THR A 724     109.932  47.646  47.405  1.00  8.70           O  
ATOM   4544  CG2 THR A 724     108.742  46.656  45.656  1.00  8.79           C  
ATOM   4545  N   GLU A 725     110.700  44.145  44.578  1.00  8.29           N  
ATOM   4546  CA  GLU A 725     110.675  43.496  43.284  1.00  8.22           C  
ATOM   4547  C   GLU A 725     109.252  43.233  42.859  1.00  8.56           C  
ATOM   4548  O   GLU A 725     108.476  42.617  43.581  1.00  8.80           O  
ATOM   4549  CB  GLU A 725     111.455  42.201  43.278  1.00  7.95           C  
ATOM   4550  CG  GLU A 725     111.509  41.580  41.912  1.00  7.81           C  
ATOM   4551  CD  GLU A 725     112.424  40.451  41.826  1.00  7.38           C  
ATOM   4552  OE1 GLU A 725     112.811  39.928  42.849  1.00  7.16           O  
ATOM   4553  OE2 GLU A 725     112.765  40.092  40.722  1.00  6.74           O  
ATOM   4554  N   ILE A 726     108.901  43.734  41.698  1.00  8.73           N  
ATOM   4555  CA  ILE A 726     107.537  43.656  41.222  1.00  8.88           C  
ATOM   4556  C   ILE A 726     107.391  42.740  40.023  1.00  8.92           C  
ATOM   4557  O   ILE A 726     108.072  42.918  39.017  1.00  9.11           O  
ATOM   4558  CB  ILE A 726     107.084  45.075  40.881  1.00  9.27           C  
ATOM   4559  CG1 ILE A 726     107.179  45.933  42.143  1.00  9.29           C  
ATOM   4560  CG2 ILE A 726     105.698  45.043  40.335  1.00  9.77           C  
ATOM   4561  CD1 ILE A 726     107.096  47.397  41.925  1.00 10.59           C  
ATOM   4562  N   LEU A 727     106.498  41.757  40.141  1.00  8.84           N  
ATOM   4563  CA  LEU A 727     106.274  40.799  39.065  1.00  8.84           C  
ATOM   4564  C   LEU A 727     104.794  40.693  38.706  1.00  8.97           C  
ATOM   4565  O   LEU A 727     103.951  40.624  39.601  1.00  9.25           O  
ATOM   4566  CB  LEU A 727     106.732  39.408  39.500  1.00  8.49           C  
ATOM   4567  CG  LEU A 727     108.188  39.255  39.909  1.00  8.13           C  
ATOM   4568  CD1 LEU A 727     108.379  37.896  40.483  1.00  7.73           C  
ATOM   4569  CD2 LEU A 727     109.094  39.438  38.724  1.00  7.87           C  
ATOM   4570  N   PRO A 728     104.437  40.685  37.418  1.00  8.93           N  
ATOM   4571  CA  PRO A 728     103.131  40.342  36.907  1.00  9.08           C  
ATOM   4572  C   PRO A 728     102.809  38.906  37.236  1.00  9.03           C  
ATOM   4573  O   PRO A 728     103.680  38.042  37.169  1.00  8.51           O  
ATOM   4574  CB  PRO A 728     103.292  40.523  35.406  1.00  8.94           C  
ATOM   4575  CG  PRO A 728     104.440  41.475  35.256  1.00  9.15           C  
ATOM   4576  CD  PRO A 728     105.359  41.173  36.408  1.00  9.08           C  
ATOM   4577  N   VAL A 729     101.559  38.640  37.556  1.00  9.23           N  
ATOM   4578  CA  VAL A 729     101.113  37.276  37.787  1.00  9.19           C  
ATOM   4579  C   VAL A 729     100.005  36.902  36.827  1.00  9.16           C  
ATOM   4580  O   VAL A 729      99.927  35.766  36.373  1.00  8.99           O  
ATOM   4581  CB  VAL A 729     100.675  37.070  39.241  1.00  9.05           C  
ATOM   4582  CG1 VAL A 729     100.076  35.693  39.429  1.00  8.85           C  
ATOM   4583  CG2 VAL A 729     101.891  37.211  40.127  1.00  9.09           C  
ATOM   4584  N   SER A 730      99.124  37.847  36.556  1.00  9.37           N  
ATOM   4585  CA  SER A 730      97.956  37.572  35.743  1.00  9.71           C  
ATOM   4586  C   SER A 730      97.675  38.692  34.770  1.00  9.76           C  
ATOM   4587  O   SER A 730      98.247  39.776  34.855  1.00  9.65           O  
ATOM   4588  CB  SER A 730      96.754  37.351  36.631  1.00  9.62           C  
ATOM   4589  OG  SER A 730      96.453  38.503  37.381  1.00  9.73           O  
ATOM   4590  N   MET A 731      96.775  38.417  33.849  1.00  9.79           N  
ATOM   4591  CA  MET A 731      96.300  39.390  32.885  1.00 10.11           C  
ATOM   4592  C   MET A 731      94.794  39.306  32.803  1.00 10.26           C  
ATOM   4593  O   MET A 731      94.200  38.293  33.169  1.00 10.16           O  
ATOM   4594  CB  MET A 731      96.968  39.184  31.525  1.00  9.95           C  
ATOM   4595  CG  MET A 731      96.751  37.830  30.899  1.00  9.92           C  
ATOM   4596  SD  MET A 731      97.574  37.619  29.307  1.00  9.66           S  
ATOM   4597  CE  MET A 731      96.453  38.307  28.126  1.00  9.85           C  
ATOM   4598  N   THR A 732      94.167  40.370  32.341  1.00 10.35           N  
ATOM   4599  CA  THR A 732      92.719  40.407  32.276  1.00 10.71           C  
ATOM   4600  C   THR A 732      92.151  39.239  31.492  1.00 11.15           C  
ATOM   4601  O   THR A 732      92.556  38.962  30.360  1.00 11.15           O  
ATOM   4602  CB  THR A 732      92.243  41.734  31.672  1.00 10.71           C  
ATOM   4603  OG1 THR A 732      92.685  42.818  32.496  1.00 10.50           O  
ATOM   4604  CG2 THR A 732      90.754  41.763  31.589  1.00 11.54           C  
ATOM   4605  N   LYS A 733      91.173  38.571  32.093  1.00 11.48           N  
ATOM   4606  CA  LYS A 733      90.541  37.411  31.498  1.00 11.81           C  
ATOM   4607  C   LYS A 733      89.501  37.812  30.486  1.00 12.12           C  
ATOM   4608  O   LYS A 733      88.303  37.777  30.768  1.00 12.70           O  
ATOM   4609  CB  LYS A 733      89.859  36.573  32.568  1.00 11.77           C  
ATOM   4610  CG  LYS A 733      90.779  35.885  33.527  1.00 11.41           C  
ATOM   4611  CD  LYS A 733      90.014  35.343  34.724  1.00 11.86           C  
ATOM   4612  CE  LYS A 733      89.036  34.238  34.340  1.00 11.87           C  
ATOM   4613  NZ  LYS A 733      88.365  33.659  35.518  1.00 12.01           N  
ATOM   4614  N   THR A 734      89.942  38.213  29.313  1.00 11.93           N  
ATOM   4615  CA  THR A 734      88.977  38.659  28.332  1.00 12.47           C  
ATOM   4616  C   THR A 734      88.325  37.461  27.690  1.00 12.82           C  
ATOM   4617  O   THR A 734      88.894  36.369  27.646  1.00 12.50           O  
ATOM   4618  CB  THR A 734      89.629  39.491  27.222  1.00 12.04           C  
ATOM   4619  OG1 THR A 734      90.532  38.659  26.490  1.00 11.83           O  
ATOM   4620  CG2 THR A 734      90.389  40.663  27.808  1.00 11.95           C  
ATOM   4621  N   SER A 735      87.171  37.690  27.103  1.00 13.11           N  
ATOM   4622  CA  SER A 735      86.469  36.675  26.348  1.00 13.49           C  
ATOM   4623  C   SER A 735      85.751  37.317  25.189  1.00 13.73           C  
ATOM   4624  O   SER A 735      85.058  38.320  25.354  1.00 14.04           O  
ATOM   4625  CB  SER A 735      85.483  35.947  27.223  1.00 13.64           C  
ATOM   4626  OG  SER A 735      84.747  35.023  26.477  1.00 15.01           O  
ATOM   4627  N   VAL A 736      85.928  36.765  24.008  1.00 13.66           N  
ATOM   4628  CA  VAL A 736      85.302  37.347  22.844  1.00 14.20           C  
ATOM   4629  C   VAL A 736      84.382  36.372  22.164  1.00 14.06           C  
ATOM   4630  O   VAL A 736      84.780  35.262  21.828  1.00 13.42           O  
ATOM   4631  CB  VAL A 736      86.363  37.837  21.846  1.00 14.14           C  
ATOM   4632  CG1 VAL A 736      85.694  38.409  20.618  1.00 14.39           C  
ATOM   4633  CG2 VAL A 736      87.232  38.887  22.518  1.00 13.84           C  
ATOM   4634  N   ASP A 737      83.163  36.815  21.929  1.00 14.22           N  
ATOM   4635  CA  ASP A 737      82.177  36.057  21.190  1.00 14.36           C  
ATOM   4636  C   ASP A 737      82.450  36.254  19.712  1.00 14.42           C  
ATOM   4637  O   ASP A 737      82.097  37.300  19.160  1.00 15.19           O  
ATOM   4638  CB  ASP A 737      80.774  36.556  21.554  1.00 15.78           C  
ATOM   4639  CG  ASP A 737      79.660  35.913  20.771  1.00 16.04           C  
ATOM   4640  OD1 ASP A 737      79.943  35.322  19.754  1.00 15.50           O  
ATOM   4641  OD2 ASP A 737      78.527  36.050  21.151  1.00 17.55           O  
ATOM   4642  N   CYS A 738      83.122  35.284  19.065  1.00 14.05           N  
ATOM   4643  CA  CYS A 738      83.571  35.426  17.687  1.00 14.14           C  
ATOM   4644  C   CYS A 738      82.425  35.662  16.689  1.00 14.26           C  
ATOM   4645  O   CYS A 738      82.587  36.381  15.717  1.00 14.84           O  
ATOM   4646  CB  CYS A 738      84.398  34.212  17.252  1.00 13.38           C  
ATOM   4647  SG  CYS A 738      83.491  32.629  17.275  1.00 13.53           S  
ATOM   4648  N   THR A 739      81.230  35.085  16.970  1.00 14.32           N  
ATOM   4649  CA  THR A 739      80.073  35.236  16.095  1.00 14.49           C  
ATOM   4650  C   THR A 739      79.494  36.623  16.216  1.00 14.97           C  
ATOM   4651  O   THR A 739      79.211  37.272  15.213  1.00 15.52           O  
ATOM   4652  CB  THR A 739      78.980  34.210  16.413  1.00 14.24           C  
ATOM   4653  OG1 THR A 739      79.507  32.890  16.253  1.00 13.87           O  
ATOM   4654  CG2 THR A 739      77.795  34.397  15.481  1.00 15.24           C  
ATOM   4655  N   MET A 740      79.327  37.094  17.443  1.00 15.06           N  
ATOM   4656  CA  MET A 740      78.765  38.421  17.640  1.00 15.24           C  
ATOM   4657  C   MET A 740      79.702  39.509  17.150  1.00 15.32           C  
ATOM   4658  O   MET A 740      79.257  40.539  16.650  1.00 15.66           O  
ATOM   4659  CB  MET A 740      78.410  38.655  19.091  1.00 16.31           C  
ATOM   4660  CG  MET A 740      77.725  39.969  19.331  1.00 17.20           C  
ATOM   4661  SD  MET A 740      77.171  40.156  21.007  1.00 19.19           S  
ATOM   4662  CE  MET A 740      76.591  41.835  20.940  1.00 20.18           C  
ATOM   4663  N   TYR A 741      81.000  39.290  17.305  1.00 15.36           N  
ATOM   4664  CA  TYR A 741      81.990  40.248  16.849  1.00 15.24           C  
ATOM   4665  C   TYR A 741      81.924  40.417  15.339  1.00 15.23           C  
ATOM   4666  O   TYR A 741      81.876  41.535  14.833  1.00 15.68           O  
ATOM   4667  CB  TYR A 741      83.393  39.821  17.269  1.00 15.28           C  
ATOM   4668  CG  TYR A 741      84.479  40.703  16.722  1.00 15.54           C  
ATOM   4669  CD1 TYR A 741      84.799  41.891  17.326  1.00 15.75           C  
ATOM   4670  CD2 TYR A 741      85.147  40.316  15.600  1.00 15.01           C  
ATOM   4671  CE1 TYR A 741      85.787  42.676  16.789  1.00 15.40           C  
ATOM   4672  CE2 TYR A 741      86.119  41.092  15.072  1.00 15.13           C  
ATOM   4673  CZ  TYR A 741      86.442  42.258  15.650  1.00 15.16           C  
ATOM   4674  OH  TYR A 741      87.417  43.023  15.094  1.00 14.85           O  
ATOM   4675  N   ILE A 742      81.938  39.298  14.616  1.00 15.48           N  
ATOM   4676  CA  ILE A 742      81.957  39.340  13.158  1.00 15.48           C  
ATOM   4677  C   ILE A 742      80.594  39.689  12.539  1.00 15.98           C  
ATOM   4678  O   ILE A 742      80.524  40.530  11.638  1.00 16.34           O  
ATOM   4679  CB  ILE A 742      82.413  37.987  12.575  1.00 15.34           C  
ATOM   4680  CG1 ILE A 742      83.829  37.680  12.995  1.00 14.86           C  
ATOM   4681  CG2 ILE A 742      82.336  38.047  11.056  1.00 15.36           C  
ATOM   4682  CD1 ILE A 742      84.258  36.270  12.716  1.00 14.19           C  
ATOM   4683  N   CYS A 743      79.529  39.013  13.009  1.00 15.97           N  
ATOM   4684  CA  CYS A 743      78.166  39.099  12.475  1.00 17.00           C  
ATOM   4685  C   CYS A 743      77.171  39.490  13.566  1.00 16.95           C  
ATOM   4686  O   CYS A 743      76.260  38.715  13.904  1.00 16.42           O  
ATOM   4687  CB  CYS A 743      77.762  37.742  11.871  1.00 16.90           C  
ATOM   4688  SG  CYS A 743      78.768  37.199  10.474  1.00 16.60           S  
ATOM   4689  N   GLY A 744      77.325  40.688  14.143  1.00 17.07           N  
ATOM   4690  CA  GLY A 744      76.484  41.123  15.258  1.00 17.33           C  
ATOM   4691  C   GLY A 744      75.028  41.260  14.840  1.00 18.27           C  
ATOM   4692  O   GLY A 744      74.687  42.085  13.992  1.00 18.82           O  
ATOM   4693  N   ASP A 745      74.183  40.430  15.441  1.00 18.50           N  
ATOM   4694  CA  ASP A 745      72.747  40.404  15.199  1.00 18.63           C  
ATOM   4695  C   ASP A 745      72.362  40.278  13.728  1.00 18.52           C  
ATOM   4696  O   ASP A 745      71.379  40.877  13.288  1.00 19.43           O  
ATOM   4697  CB  ASP A 745      72.100  41.648  15.803  1.00 18.56           C  
ATOM   4698  CG  ASP A 745      72.278  41.706  17.313  1.00 19.40           C  
ATOM   4699  OD1 ASP A 745      72.367  40.661  17.923  1.00 19.96           O  
ATOM   4700  OD2 ASP A 745      72.326  42.788  17.847  1.00 20.98           O  
ATOM   4701  N   SER A 746      73.090  39.462  12.973  1.00 18.05           N  
ATOM   4702  CA  SER A 746      72.753  39.269  11.568  1.00 18.16           C  
ATOM   4703  C   SER A 746      72.712  37.812  11.159  1.00 17.65           C  
ATOM   4704  O   SER A 746      73.731  37.120  11.173  1.00 17.65           O  
ATOM   4705  CB  SER A 746      73.736  39.988  10.685  1.00 18.59           C  
ATOM   4706  OG  SER A 746      73.491  39.677   9.337  1.00 19.06           O  
ATOM   4707  N   THR A 747      71.524  37.355  10.787  1.00 17.66           N  
ATOM   4708  CA  THR A 747      71.311  35.979  10.372  1.00 17.72           C  
ATOM   4709  C   THR A 747      71.986  35.702   9.044  1.00 17.50           C  
ATOM   4710  O   THR A 747      72.538  34.623   8.827  1.00 17.56           O  
ATOM   4711  CB  THR A 747      69.817  35.655  10.265  1.00 17.92           C  
ATOM   4712  OG1 THR A 747      69.204  35.824  11.548  1.00 17.91           O  
ATOM   4713  CG2 THR A 747      69.630  34.218   9.802  1.00 17.56           C  
ATOM   4714  N   GLU A 748      71.917  36.668   8.141  1.00 17.89           N  
ATOM   4715  CA  GLU A 748      72.482  36.487   6.811  1.00 17.89           C  
ATOM   4716  C   GLU A 748      74.001  36.317   6.872  1.00 17.63           C  
ATOM   4717  O   GLU A 748      74.556  35.431   6.213  1.00 17.50           O  
ATOM   4718  CB  GLU A 748      72.124  37.690   5.937  1.00 18.99           C  
ATOM   4719  CG  GLU A 748      70.630  37.848   5.669  1.00 19.31           C  
ATOM   4720  CD  GLU A 748      69.895  38.492   6.825  1.00 19.14           C  
ATOM   4721  OE1 GLU A 748      70.546  38.920   7.752  1.00 18.85           O  
ATOM   4722  OE2 GLU A 748      68.693  38.547   6.788  1.00 18.39           O  
ATOM   4723  N   CYS A 749      74.666  37.144   7.696  1.00 17.78           N  
ATOM   4724  CA  CYS A 749      76.105  37.086   7.917  1.00 17.57           C  
ATOM   4725  C   CYS A 749      76.502  35.798   8.648  1.00 17.24           C  
ATOM   4726  O   CYS A 749      77.502  35.172   8.283  1.00 17.37           O  
ATOM   4727  CB  CYS A 749      76.565  38.336   8.674  1.00 18.62           C  
ATOM   4728  SG  CYS A 749      78.349  38.496   8.963  1.00 18.61           S  
ATOM   4729  N   SER A 750      75.731  35.398   9.684  1.00 17.15           N  
ATOM   4730  CA  SER A 750      76.015  34.204  10.479  1.00 16.88           C  
ATOM   4731  C   SER A 750      76.004  32.956   9.612  1.00 16.62           C  
ATOM   4732  O   SER A 750      76.902  32.120   9.709  1.00 16.80           O  
ATOM   4733  CB  SER A 750      75.010  34.063  11.595  1.00 16.79           C  
ATOM   4734  OG  SER A 750      75.277  32.923  12.360  1.00 16.85           O  
ATOM   4735  N   ASN A 751      75.035  32.857   8.713  1.00 16.81           N  
ATOM   4736  CA  ASN A 751      74.989  31.700   7.842  1.00 16.58           C  
ATOM   4737  C   ASN A 751      76.215  31.632   6.934  1.00 16.57           C  
ATOM   4738  O   ASN A 751      76.713  30.543   6.650  1.00 16.54           O  
ATOM   4739  CB  ASN A 751      73.711  31.695   7.046  1.00 16.81           C  
ATOM   4740  CG  ASN A 751      72.539  31.337   7.893  1.00 16.83           C  
ATOM   4741  OD1 ASN A 751      72.687  30.786   8.988  1.00 16.81           O  
ATOM   4742  ND2 ASN A 751      71.366  31.636   7.412  1.00 16.38           N  
ATOM   4743  N   LEU A 752      76.727  32.785   6.505  1.00 17.14           N  
ATOM   4744  CA  LEU A 752      77.952  32.804   5.710  1.00 16.78           C  
ATOM   4745  C   LEU A 752      79.150  32.437   6.569  1.00 16.44           C  
ATOM   4746  O   LEU A 752      80.059  31.739   6.132  1.00 16.28           O  
ATOM   4747  CB  LEU A 752      78.189  34.191   5.109  1.00 17.55           C  
ATOM   4748  CG  LEU A 752      77.223  34.655   4.032  1.00 18.56           C  
ATOM   4749  CD1 LEU A 752      77.469  36.127   3.773  1.00 19.67           C  
ATOM   4750  CD2 LEU A 752      77.438  33.850   2.754  1.00 19.77           C  
ATOM   4751  N   LEU A 753      79.141  32.881   7.816  1.00 16.52           N  
ATOM   4752  CA  LEU A 753      80.233  32.601   8.732  1.00 16.10           C  
ATOM   4753  C   LEU A 753      80.376  31.106   8.971  1.00 15.62           C  
ATOM   4754  O   LEU A 753      81.486  30.602   9.117  1.00 15.40           O  
ATOM   4755  CB  LEU A 753      80.026  33.342  10.055  1.00 16.53           C  
ATOM   4756  CG  LEU A 753      81.144  33.228  11.114  1.00 15.42           C  
ATOM   4757  CD1 LEU A 753      82.463  33.739  10.555  1.00 15.27           C  
ATOM   4758  CD2 LEU A 753      80.739  34.049  12.325  1.00 14.86           C  
ATOM   4759  N   LEU A 754      79.264  30.381   8.965  1.00 16.07           N  
ATOM   4760  CA  LEU A 754      79.283  28.939   9.191  1.00 15.94           C  
ATOM   4761  C   LEU A 754      80.051  28.185   8.114  1.00 16.19           C  
ATOM   4762  O   LEU A 754      80.450  27.040   8.319  1.00 15.99           O  
ATOM   4763  CB  LEU A 754      77.860  28.373   9.238  1.00 15.89           C  
ATOM   4764  CG  LEU A 754      76.979  28.783  10.424  1.00 15.99           C  
ATOM   4765  CD1 LEU A 754      75.573  28.249  10.193  1.00 15.92           C  
ATOM   4766  CD2 LEU A 754      77.551  28.236  11.719  1.00 15.21           C  
ATOM   4767  N   GLN A 755      80.289  28.815   6.974  1.00 16.43           N  
ATOM   4768  CA  GLN A 755      80.984  28.156   5.882  1.00 16.33           C  
ATOM   4769  C   GLN A 755      82.470  28.070   6.164  1.00 18.12           C  
ATOM   4770  O   GLN A 755      83.215  27.439   5.415  1.00 13.61           O  
ATOM   4771  CB  GLN A 755      80.747  28.883   4.566  1.00 16.62           C  
ATOM   4772  CG  GLN A 755      79.317  28.835   4.085  1.00 16.22           C  
ATOM   4773  CD  GLN A 755      79.145  29.561   2.784  1.00 16.47           C  
ATOM   4774  OE1 GLN A 755      80.003  30.354   2.397  1.00 16.76           O  
ATOM   4775  NE2 GLN A 755      78.044  29.301   2.091  1.00 16.27           N  
ATOM   4776  N   TYR A 756      82.902  28.692   7.255  1.00 16.13           N  
ATOM   4777  CA  TYR A 756      84.293  28.685   7.660  1.00 15.24           C  
ATOM   4778  C   TYR A 756      84.543  27.629   8.727  1.00 15.05           C  
ATOM   4779  O   TYR A 756      85.643  27.524   9.275  1.00 14.32           O  
ATOM   4780  CB  TYR A 756      84.684  30.067   8.152  1.00 15.28           C  
ATOM   4781  CG  TYR A 756      84.757  31.066   7.058  1.00 15.38           C  
ATOM   4782  CD1 TYR A 756      83.628  31.735   6.662  1.00 15.81           C  
ATOM   4783  CD2 TYR A 756      85.955  31.316   6.446  1.00 15.33           C  
ATOM   4784  CE1 TYR A 756      83.692  32.648   5.654  1.00 15.84           C  
ATOM   4785  CE2 TYR A 756      86.024  32.232   5.437  1.00 15.76           C  
ATOM   4786  CZ  TYR A 756      84.896  32.895   5.040  1.00 15.95           C  
ATOM   4787  OH  TYR A 756      84.962  33.815   4.027  1.00 16.00           O  
ATOM   4788  N   GLY A 757      83.529  26.818   8.993  1.00 15.23           N  
ATOM   4789  CA  GLY A 757      83.665  25.702   9.910  1.00 14.79           C  
ATOM   4790  C   GLY A 757      83.979  26.098  11.338  1.00 14.08           C  
ATOM   4791  O   GLY A 757      83.266  26.888  11.957  1.00 14.34           O  
ATOM   4792  N   SER A 758      85.052  25.525  11.866  1.00 13.85           N  
ATOM   4793  CA  SER A 758      85.471  25.739  13.245  1.00 13.58           C  
ATOM   4794  C   SER A 758      86.364  26.950  13.415  1.00 13.31           C  
ATOM   4795  O   SER A 758      86.844  27.221  14.514  1.00 13.35           O  
ATOM   4796  CB  SER A 758      86.182  24.523  13.786  1.00 13.64           C  
ATOM   4797  OG  SER A 758      87.409  24.344  13.152  1.00 13.66           O  
ATOM   4798  N   PHE A 759      86.606  27.705  12.347  1.00 13.27           N  
ATOM   4799  CA  PHE A 759      87.466  28.878  12.509  1.00 13.12           C  
ATOM   4800  C   PHE A 759      87.014  29.805  13.628  1.00 12.86           C  
ATOM   4801  O   PHE A 759      87.859  30.410  14.279  1.00 12.81           O  
ATOM   4802  CB  PHE A 759      87.577  29.709  11.235  1.00 13.50           C  
ATOM   4803  CG  PHE A 759      88.726  29.375  10.344  1.00 13.51           C  
ATOM   4804  CD1 PHE A 759      88.547  29.214   8.992  1.00 13.86           C  
ATOM   4805  CD2 PHE A 759      90.009  29.254  10.854  1.00 13.44           C  
ATOM   4806  CE1 PHE A 759      89.599  28.941   8.171  1.00 13.21           C  
ATOM   4807  CE2 PHE A 759      91.059  28.977  10.026  1.00 12.92           C  
ATOM   4808  CZ  PHE A 759      90.841  28.823   8.681  1.00 12.35           C  
ATOM   4809  N   CYS A 760      85.698  29.948  13.829  1.00 13.14           N  
ATOM   4810  CA  CYS A 760      85.132  30.821  14.849  1.00 12.89           C  
ATOM   4811  C   CYS A 760      85.311  30.184  16.253  1.00 12.41           C  
ATOM   4812  O   CYS A 760      85.973  30.767  17.121  1.00 12.83           O  
ATOM   4813  CB  CYS A 760      83.638  31.078  14.506  1.00 12.69           C  
ATOM   4814  SG  CYS A 760      82.781  32.418  15.390  1.00 14.54           S  
ATOM   4815  N   THR A 761      84.778  28.966  16.463  1.00 12.83           N  
ATOM   4816  CA  THR A 761      84.774  28.316  17.779  1.00 12.70           C  
ATOM   4817  C   THR A 761      86.147  27.914  18.302  1.00 12.32           C  
ATOM   4818  O   THR A 761      86.330  27.825  19.515  1.00 12.10           O  
ATOM   4819  CB  THR A 761      83.864  27.086  17.777  1.00 12.54           C  
ATOM   4820  OG1 THR A 761      84.294  26.171  16.772  1.00 13.07           O  
ATOM   4821  CG2 THR A 761      82.443  27.511  17.495  1.00 12.69           C  
ATOM   4822  N   GLN A 762      87.127  27.706  17.429  1.00 12.68           N  
ATOM   4823  CA  GLN A 762      88.449