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***  Myoglobin  ***

elNémo ID: 21111011185197266

Job options:

ID        	=	 21111011185197266
JOBID     	=	 Myoglobin
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 Myoglobin

HEADER    OXYGEN STORAGE/TRANSPORT                11-NOV-05   2D6C              
TITLE     CRYSTAL STRUCTURE OF MYOGLOBIN RECONSTITUTED WITH IRON                
TITLE    2 PORPHYCENE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOGLOBIN;                                                 
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;                               
SOURCE   3 ORGANISM_COMMON: SPERM WHALE;                                        
SOURCE   4 ORGANISM_TAXID: 9755;                                                
SOURCE   5 TISSUE: SKELETAL MUSCLE                                              
KEYWDS    OXYGEN STORAGE/TRANSPORT, MYOGLOBIN, HEMOPROTEIN,                     
KEYWDS   2 PORPHYCENE, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,         
KEYWDS   3 RSGI, STRUCTURAL GENOMICS                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.HAYASHI,D.MURATA,M.MAKINO,H.SUGIMOTO,T.MATSUO,H.SATO,               
AUTHOR   2 Y.SHIRO,Y.HISAEDA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS               
AUTHOR   3 INITIATIVE (RSGI)                                                    
REVDAT   3   24-FEB-09 2D6C    1       VERSN                                    
REVDAT   2   21-AUG-07 2D6C    1       JRNL   HETATM CONECT LINK                
REVDAT   1   31-OCT-06 2D6C    0                                                
JRNL        AUTH   T.HAYASHI,D.MURATA,M.MAKINO,H.SUGIMOTO,T.MATSUO,             
JRNL        AUTH 2 H.SATO,Y.SHIRO,Y.HISAEDA                                     
JRNL        TITL   CRYSTAL STRUCTURE AND PEROXIDASE ACTIVITY OF                 
JRNL        TITL 2 MYOGLOBIN RECONSTITUTED WITH IRON PORPHYCENE                 
JRNL        REF    INORG.CHEM.                   V.  45 10530 2006              
JRNL        REFN                   ISSN 0020-1669                               
JRNL        PMID   17173408                                                     
JRNL        DOI    10.1021/IC061130X                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 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) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 658343.360                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15728                          
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) : 0.251                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 795                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2307                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 116                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2435                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 225                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.31000                                             
REMARK   3    B22 (A**2) : 4.03000                                              
REMARK   3    B33 (A**2) : 0.29000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -6.93000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.31                            
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) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.51                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.69                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 5.180 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.510 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 7.190 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.790 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 69.66                                                
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  : PPC.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : PPC.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2D6C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JAN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB025041.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 90.0                               
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(III)                            
REMARK 200  OPTICS                         : SI(III) MIRRORS                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200   FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.27500                            
REMARK 200   FOR SHELL         : 2.930                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1A6K                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0M AMMONIUM SULFATE, 0.1M              
REMARK 280  IMIDAZOLE PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE        
REMARK 280  293.0K                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.95100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER.                        
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  20       59.93   -159.79                                   
REMARK 500    LYS A  42       -0.61    -58.08                                   
REMARK 500    PHE A  46       62.20   -119.68                                   
REMARK 500    HIS A  48      -25.59   -142.99                                   
REMARK 500    LYS A  50      -63.64   -104.65                                   
REMARK 500    HIS B  36       77.70   -151.18                                   
REMARK 500    GLU B  38       -6.90    -58.65                                   
REMARK 500    LYS B  47      -28.55    108.76                                   
REMARK 500    LYS B  50      -83.25    -82.77                                   
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                             HME A 154  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 IMD A 155   N1  157.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HME B 154  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  93   NE2                                                    
REMARK 620 2 IMD B 155   N1  165.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HME A 154                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 155                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HME B 154                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 155                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MY_001000022.3   RELATED DB: TARGETDB                    
DBREF  2D6C A    1   153  UNP    P02185   MYG_PHYCA        1    153             
DBREF  2D6C B    1   153  UNP    P02185   MYG_PHYCA        1    153             
SEQRES   1 A  153  VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS VAL          
SEQRES   2 A  153  TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN          
SEQRES   3 A  153  ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU THR          
SEQRES   4 A  153  LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR GLU          
SEQRES   5 A  153  ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY          
SEQRES   6 A  153  VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS LYS          
SEQRES   7 A  153  LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA GLN          
SEQRES   8 A  153  SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR LEU          
SEQRES   9 A  153  GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS SER          
SEQRES  10 A  153  ARG HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA          
SEQRES  11 A  153  MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE ALA          
SEQRES  12 A  153  ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY                      
SEQRES   1 B  153  VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS VAL          
SEQRES   2 B  153  TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN          
SEQRES   3 B  153  ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU THR          
SEQRES   4 B  153  LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR GLU          
SEQRES   5 B  153  ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY          
SEQRES   6 B  153  VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS LYS          
SEQRES   7 B  153  LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA GLN          
SEQRES   8 B  153  SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR LEU          
SEQRES   9 B  153  GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS SER          
SEQRES  10 B  153  ARG HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA          
SEQRES  11 B  153  MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE ALA          
SEQRES  12 B  153  ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY                      
HET    HME  A 154      43                                                       
HET    IMD  A 155       5                                                       
HET    HME  B 154      43                                                       
HET    IMD  B 155       5                                                       
HETNAM     HME PORPHYCENE CONTAINING FE                                         
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   3  HME    2(C34 H36 FE N4 O4 2+)                                       
FORMUL   4  IMD    2(C3 H5 N2 1+)                                               
FORMUL   7  HOH   *225(H2 O)                                                    
HELIX    1   1 SER A    3  GLU A   18  1                                  16    
HELIX    2   2 ASP A   20  HIS A   36  1                                  17    
HELIX    3   3 PRO A   37  LYS A   42  1                                   6    
HELIX    4   4 THR A   51  SER A   58  1                                   8    
HELIX    5   5 SER A   58  LYS A   77  1                                  20    
HELIX    6   6 HIS A   82  THR A   95  1                                  14    
HELIX    7   7 PRO A  100  HIS A  119  1                                  20    
HELIX    8   8 GLY A  124  LEU A  149  1                                  26    
HELIX    9   9 SER B    3  LYS B   16  1                                  14    
HELIX   10  10 VAL B   17  ALA B   19  5                                   3    
HELIX   11  11 ASP B   20  HIS B   36  1                                  17    
HELIX   12  12 PRO B   37  LEU B   40  5                                   4    
HELIX   13  13 THR B   51  SER B   58  1                                   8    
HELIX   14  14 SER B   58  LYS B   79  1                                  22    
HELIX   15  15 HIS B   82  LYS B   96  1                                  15    
HELIX   16  16 PRO B  100  HIS B  119  1                                  20    
HELIX   17  17 GLY B  124  LEU B  149  1                                  26    
LINK        FE   HME A 154                 NE2 HIS A  93     1555   1555  2.28  
LINK        FE   HME B 154                 NE2 HIS B  93     1555   1555  2.35  
LINK        FE   HME A 154                 N1  IMD A 155     1555   1555  2.33  
LINK        FE   HME B 154                 N1  IMD B 155     1555   1555  2.45  
SITE     1 AC1 13 LYS A  42  PHE A  43  ARG A  45  VAL A  68                    
SITE     2 AC1 13 ILE A  75  LEU A  89  HIS A  93  LYS A  96                    
SITE     3 AC1 13 HIS A  97  ILE A  99  ILE A 107  PHE A 138                    
SITE     4 AC1 13 IMD A 155                                                     
SITE     1 AC2  5 PHE A  43  HIS A  64  THR A  67  VAL A  68                    
SITE     2 AC2  5 HME A 154                                                     
SITE     1 AC3 12 LEU B  32  PHE B  43  VAL B  68  LEU B  89                    
SITE     2 AC3 12 HIS B  93  LYS B  96  HIS B  97  TYR B 103                    
SITE     3 AC3 12 ILE B 107  IMD B 155  HOH B 158  HOH B 184                    
SITE     1 AC4  5 PHE B  43  HIS B  64  THR B  67  VAL B  68                    
SITE     2 AC4  5 HME B 154                                                     
CRYST1   42.533   79.902   54.619  90.00 110.88  90.00 P 1 21 1      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      0.023511  0.000000  0.008969        0.00000                         
SCALE2      0.000000  0.012515  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019596        0.00000                         
ATOM      1  N   VAL A   1      24.298   5.864  32.360  1.00 47.08           N  
ATOM      2  CA  VAL A   1      23.153   5.758  33.309  1.00 41.92           C  
ATOM      3  C   VAL A   1      22.240   6.974  33.251  1.00 40.61           C  
ATOM      4  O   VAL A   1      22.581   7.999  32.661  1.00 36.20           O  
ATOM      5  CB  VAL A   1      23.643   5.611  34.769  1.00 38.72           C  
ATOM      6  CG1 VAL A   1      24.232   4.227  34.988  1.00 43.39           C  
ATOM      7  CG2 VAL A   1      24.677   6.685  35.079  1.00 34.59           C  
ATOM      8  N   LEU A   2      21.067   6.841  33.861  1.00 34.60           N  
ATOM      9  CA  LEU A   2      20.104   7.929  33.923  1.00 30.61           C  
ATOM     10  C   LEU A   2      19.956   8.303  35.390  1.00 33.67           C  
ATOM     11  O   LEU A   2      20.162   7.471  36.273  1.00 41.54           O  
ATOM     12  CB  LEU A   2      18.739   7.500  33.376  1.00 35.12           C  
ATOM     13  CG  LEU A   2      18.551   7.236  31.880  1.00 35.48           C  
ATOM     14  CD1 LEU A   2      19.229   5.932  31.490  1.00 30.30           C  
ATOM     15  CD2 LEU A   2      17.060   7.174  31.569  1.00 16.48           C  
ATOM     16  N   SER A   3      19.603   9.556  35.648  1.00 24.04           N  
ATOM     17  CA  SER A   3      19.420  10.026  37.013  1.00 29.47           C  
ATOM     18  C   SER A   3      17.954   9.877  37.394  1.00 26.25           C  
ATOM     19  O   SER A   3      17.118   9.557  36.550  1.00 31.11           O  
ATOM     20  CB  SER A   3      19.840  11.492  37.124  1.00 33.09           C  
ATOM     21  OG  SER A   3      19.119  12.295  36.205  1.00 35.50           O  
ATOM     22  N   GLU A   4      17.646  10.107  38.666  1.00 21.22           N  
ATOM     23  CA  GLU A   4      16.272   9.999  39.140  1.00 22.85           C  
ATOM     24  C   GLU A   4      15.429  11.027  38.396  1.00 25.23           C  
ATOM     25  O   GLU A   4      14.247  10.805  38.127  1.00 22.46           O  
ATOM     26  CB  GLU A   4      16.211  10.260  40.647  1.00 24.86           C  
ATOM     27  CG  GLU A   4      14.889   9.888  41.305  1.00 33.10           C  
ATOM     28  CD  GLU A   4      14.537   8.422  41.124  1.00 39.43           C  
ATOM     29  OE1 GLU A   4      15.433   7.569  41.294  1.00 38.85           O  
ATOM     30  OE2 GLU A   4      13.362   8.123  40.822  1.00 37.27           O  
ATOM     31  N   GLY A   5      16.051  12.155  38.065  1.00 25.00           N  
ATOM     32  CA  GLY A   5      15.354  13.204  37.347  1.00 19.78           C  
ATOM     33  C   GLY A   5      15.040  12.750  35.936  1.00 27.52           C  
ATOM     34  O   GLY A   5      13.913  12.899  35.458  1.00 23.41           O  
ATOM     35  N   GLU A   6      16.045  12.193  35.267  1.00 21.71           N  
ATOM     36  CA  GLU A   6      15.873  11.702  33.907  1.00 28.73           C  
ATOM     37  C   GLU A   6      14.808  10.611  33.883  1.00 25.17           C  
ATOM     38  O   GLU A   6      13.957  10.584  32.992  1.00 29.50           O  
ATOM     39  CB  GLU A   6      17.204  11.169  33.369  1.00 26.35           C  
ATOM     40  CG  GLU A   6      18.245  12.262  33.163  1.00 36.70           C  
ATOM     41  CD  GLU A   6      19.628  11.719  32.859  1.00 41.12           C  
ATOM     42  OE1 GLU A   6      20.196  11.018  33.721  1.00 38.30           O  
ATOM     43  OE2 GLU A   6      20.151  11.998  31.761  1.00 35.73           O  
ATOM     44  N   TRP A   7      14.849   9.719  34.870  1.00 21.45           N  
ATOM     45  CA  TRP A   7      13.869   8.642  34.957  1.00 28.17           C  
ATOM     46  C   TRP A   7      12.478   9.214  35.202  1.00 27.67           C  
ATOM     47  O   TRP A   7      11.480   8.653  34.749  1.00 30.91           O  
ATOM     48  CB  TRP A   7      14.234   7.669  36.080  1.00 26.52           C  
ATOM     49  CG  TRP A   7      15.389   6.774  35.746  1.00 29.41           C  
ATOM     50  CD1 TRP A   7      16.580   6.694  36.405  1.00 41.09           C  
ATOM     51  CD2 TRP A   7      15.462   5.834  34.668  1.00 35.52           C  
ATOM     52  NE1 TRP A   7      17.394   5.762  35.806  1.00 32.80           N  
ATOM     53  CE2 TRP A   7      16.732   5.218  34.737  1.00 35.43           C  
ATOM     54  CE3 TRP A   7      14.577   5.451  33.650  1.00 23.25           C  
ATOM     55  CZ2 TRP A   7      17.141   4.239  33.826  1.00 19.94           C  
ATOM     56  CZ3 TRP A   7      14.986   4.475  32.741  1.00 36.79           C  
ATOM     57  CH2 TRP A   7      16.258   3.881  32.838  1.00 27.26           C  
ATOM     58  N   GLN A   8      12.420  10.331  35.922  1.00 30.37           N  
ATOM     59  CA  GLN A   8      11.151  10.989  36.214  1.00 34.01           C  
ATOM     60  C   GLN A   8      10.555  11.488  34.904  1.00 28.93           C  
ATOM     61  O   GLN A   8       9.354  11.354  34.667  1.00 28.89           O  
ATOM     62  CB  GLN A   8      11.370  12.165  37.171  1.00 42.83           C  
ATOM     63  CG  GLN A   8      10.102  12.921  37.580  1.00 55.78           C  
ATOM     64  CD  GLN A   8       9.448  13.672  36.430  1.00 59.90           C  
ATOM     65  OE1 GLN A   8       8.376  13.294  35.954  1.00 61.37           O  
ATOM     66  NE2 GLN A   8      10.098  14.738  35.974  1.00 51.84           N  
ATOM     67  N   LEU A   9      11.404  12.062  34.056  1.00 27.66           N  
ATOM     68  CA  LEU A   9      10.967  12.578  32.764  1.00 23.51           C  
ATOM     69  C   LEU A   9      10.391  11.474  31.883  1.00 23.98           C  
ATOM     70  O   LEU A   9       9.294  11.611  31.345  1.00 33.54           O  
ATOM     71  CB  LEU A   9      12.136  13.245  32.033  1.00 22.08           C  
ATOM     72  CG  LEU A   9      12.689  14.544  32.620  1.00 30.83           C  
ATOM     73  CD1 LEU A   9      13.866  15.020  31.780  1.00 16.33           C  
ATOM     74  CD2 LEU A   9      11.592  15.599  32.656  1.00 19.72           C  
ATOM     75  N   VAL A  10      11.135  10.382  31.743  1.00 25.12           N  
ATOM     76  CA  VAL A  10      10.710   9.256  30.916  1.00 21.85           C  
ATOM     77  C   VAL A  10       9.404   8.614  31.390  1.00 21.95           C  
ATOM     78  O   VAL A  10       8.531   8.298  30.579  1.00 23.45           O  
ATOM     79  CB  VAL A  10      11.812   8.169  30.856  1.00 23.35           C  
ATOM     80  CG1 VAL A  10      11.363   7.015  29.974  1.00 18.27           C  
ATOM     81  CG2 VAL A  10      13.106   8.770  30.322  1.00 11.82           C  
ATOM     82  N   LEU A  11       9.264   8.421  32.696  1.00 12.78           N  
ATOM     83  CA  LEU A  11       8.056   7.805  33.232  1.00 15.03           C  
ATOM     84  C   LEU A  11       6.855   8.741  33.166  1.00 23.66           C  
ATOM     85  O   LEU A  11       5.714   8.290  33.064  1.00 27.02           O  
ATOM     86  CB  LEU A  11       8.286   7.347  34.673  1.00  9.10           C  
ATOM     87  CG  LEU A  11       9.369   6.277  34.846  1.00 19.60           C  
ATOM     88  CD1 LEU A  11       9.456   5.866  36.302  1.00 27.73           C  
ATOM     89  CD2 LEU A  11       9.049   5.072  33.975  1.00 17.97           C  
ATOM     90  N   HIS A  12       7.115  10.043  33.223  1.00  9.68           N  
ATOM     91  CA  HIS A  12       6.043  11.028  33.158  1.00 23.21           C  
ATOM     92  C   HIS A  12       5.453  11.031  31.753  1.00 23.71           C  
ATOM     93  O   HIS A  12       4.241  11.158  31.573  1.00 23.69           O  
ATOM     94  CB  HIS A  12       6.577  12.422  33.496  1.00 25.07           C  
ATOM     95  CG  HIS A  12       5.530  13.491  33.465  1.00 34.87           C  
ATOM     96  ND1 HIS A  12       4.421  13.470  34.283  1.00 34.66           N  
ATOM     97  CD2 HIS A  12       5.424  14.615  32.717  1.00 40.53           C  
ATOM     98  CE1 HIS A  12       3.677  14.534  34.040  1.00 46.77           C  
ATOM     99  NE2 HIS A  12       4.264  15.246  33.094  1.00 33.69           N  
ATOM    100  N   VAL A  13       6.323  10.890  30.760  1.00 24.68           N  
ATOM    101  CA  VAL A  13       5.903  10.866  29.366  1.00 30.10           C  
ATOM    102  C   VAL A  13       5.112   9.594  29.079  1.00 23.75           C  
ATOM    103  O   VAL A  13       3.994   9.646  28.563  1.00 19.84           O  
ATOM    104  CB  VAL A  13       7.116  10.895  28.410  1.00 33.19           C  
ATOM    105  CG1 VAL A  13       6.639  11.005  26.971  1.00 40.06           C  
ATOM    106  CG2 VAL A  13       8.030  12.054  28.762  1.00 41.85           C  
ATOM    107  N   TRP A  14       5.699   8.453  29.428  1.00 18.39           N  
ATOM    108  CA  TRP A  14       5.066   7.165  29.188  1.00 17.66           C  
ATOM    109  C   TRP A  14       3.681   7.051  29.816  1.00 19.28           C  
ATOM    110  O   TRP A  14       2.806   6.374  29.275  1.00 21.59           O  
ATOM    111  CB  TRP A  14       5.967   6.034  29.689  1.00 23.20           C  
ATOM    112  CG  TRP A  14       5.799   4.792  28.880  1.00 12.97           C  
ATOM    113  CD1 TRP A  14       5.019   3.714  29.177  1.00 19.01           C  
ATOM    114  CD2 TRP A  14       6.355   4.542  27.586  1.00 14.78           C  
ATOM    115  NE1 TRP A  14       5.049   2.806  28.143  1.00 21.86           N  
ATOM    116  CE2 TRP A  14       5.863   3.291  27.153  1.00  7.77           C  
ATOM    117  CE3 TRP A  14       7.219   5.258  26.746  1.00  9.51           C  
ATOM    118  CZ2 TRP A  14       6.206   2.738  25.917  1.00 17.15           C  
ATOM    119  CZ3 TRP A  14       7.560   4.710  25.517  1.00 15.54           C  
ATOM    120  CH2 TRP A  14       7.053   3.460  25.114  1.00 12.66           C  
ATOM    121  N   ALA A  15       3.479   7.710  30.954  1.00 30.80           N  
ATOM    122  CA  ALA A  15       2.183   7.677  31.625  1.00 25.47           C  
ATOM    123  C   ALA A  15       1.107   8.191  30.673  1.00 27.99           C  
ATOM    124  O   ALA A  15      -0.035   7.725  30.695  1.00 15.65           O  
ATOM    125  CB  ALA A  15       2.218   8.533  32.885  1.00 17.25           C  
ATOM    126  N   LYS A  16       1.479   9.158  29.836  1.00 28.07           N  
ATOM    127  CA  LYS A  16       0.549   9.725  28.869  1.00 37.44           C  
ATOM    128  C   LYS A  16       0.334   8.750  27.727  1.00 37.26           C  
ATOM    129  O   LYS A  16      -0.761   8.656  27.172  1.00 35.74           O  
ATOM    130  CB  LYS A  16       1.082  11.046  28.311  1.00 36.65           C  
ATOM    131  CG  LYS A  16       1.105  12.170  29.322  1.00 46.07           C  
ATOM    132  CD  LYS A  16       1.015  13.525  28.647  1.00 38.29           C  
ATOM    133  CE  LYS A  16       0.777  14.600  29.686  1.00 43.55           C  
ATOM    134  NZ  LYS A  16      -0.393  14.232  30.537  1.00 52.80           N  
ATOM    135  N   VAL A  17       1.395   8.031  27.378  1.00 31.17           N  
ATOM    136  CA  VAL A  17       1.338   7.050  26.305  1.00 23.39           C  
ATOM    137  C   VAL A  17       0.370   5.935  26.682  1.00 29.50           C  
ATOM    138  O   VAL A  17      -0.516   5.580  25.905  1.00 15.23           O  
ATOM    139  CB  VAL A  17       2.729   6.433  26.042  1.00 28.55           C  
ATOM    140  CG1 VAL A  17       2.639   5.392  24.937  1.00 28.00           C  
ATOM    141  CG2 VAL A  17       3.716   7.526  25.663  1.00 19.93           C  
ATOM    142  N   GLU A  18       0.538   5.395  27.885  1.00 22.87           N  
ATOM    143  CA  GLU A  18      -0.315   4.316  28.361  1.00 29.97           C  
ATOM    144  C   GLU A  18      -1.751   4.785  28.571  1.00 32.85           C  
ATOM    145  O   GLU A  18      -2.657   3.974  28.756  1.00 37.26           O  
ATOM    146  CB  GLU A  18       0.252   3.730  29.657  1.00 31.74           C  
ATOM    147  CG  GLU A  18       1.744   3.440  29.580  1.00 39.22           C  
ATOM    148  CD  GLU A  18       2.150   2.192  30.338  1.00 35.35           C  
ATOM    149  OE1 GLU A  18       1.791   2.070  31.527  1.00 28.73           O  
ATOM    150  OE2 GLU A  18       2.837   1.333  29.742  1.00 24.30           O  
ATOM    151  N   ALA A  19      -1.954   6.099  28.545  1.00 32.13           N  
ATOM    152  CA  ALA A  19      -3.290   6.662  28.706  1.00 28.93           C  
ATOM    153  C   ALA A  19      -4.049   6.380  27.415  1.00 33.71           C  
ATOM    154  O   ALA A  19      -5.274   6.496  27.355  1.00 34.92           O  
ATOM    155  CB  ALA A  19      -3.205   8.165  28.951  1.00 27.80           C  
ATOM    156  N   ASP A  20      -3.295   6.004  26.386  1.00 28.38           N  
ATOM    157  CA  ASP A  20      -3.842   5.684  25.072  1.00 29.75           C  
ATOM    158  C   ASP A  20      -2.831   4.833  24.302  1.00 26.54           C  
ATOM    159  O   ASP A  20      -2.359   5.215  23.230  1.00 17.50           O  
ATOM    160  CB  ASP A  20      -4.151   6.976  24.307  1.00 35.95           C  
ATOM    161  CG  ASP A  20      -4.560   6.723  22.869  1.00 35.57           C  
ATOM    162  OD1 ASP A  20      -5.418   5.846  22.635  1.00 50.76           O  
ATOM    163  OD2 ASP A  20      -4.023   7.407  21.972  1.00 47.74           O  
ATOM    164  N   VAL A  21      -2.500   3.674  24.864  1.00 22.01           N  
ATOM    165  CA  VAL A  21      -1.539   2.770  24.243  1.00 29.17           C  
ATOM    166  C   VAL A  21      -1.929   2.350  22.833  1.00 15.44           C  
ATOM    167  O   VAL A  21      -1.116   2.427  21.915  1.00 24.24           O  
ATOM    168  CB  VAL A  21      -1.322   1.491  25.093  1.00 22.43           C  
ATOM    169  CG1 VAL A  21      -0.383   1.791  26.241  1.00 18.75           C  
ATOM    170  CG2 VAL A  21      -2.654   0.974  25.617  1.00 12.47           C  
ATOM    171  N   ALA A  22      -3.170   1.906  22.663  1.00 19.02           N  
ATOM    172  CA  ALA A  22      -3.647   1.470  21.354  1.00 24.41           C  
ATOM    173  C   ALA A  22      -3.374   2.524  20.289  1.00 13.94           C  
ATOM    174  O   ALA A  22      -2.895   2.209  19.198  1.00 23.22           O  
ATOM    175  CB  ALA A  22      -5.137   1.164  21.417  1.00 19.55           C  
ATOM    176  N   GLY A  23      -3.683   3.776  20.611  1.00 23.92           N  
ATOM    177  CA  GLY A  23      -3.460   4.857  19.668  1.00  9.34           C  
ATOM    178  C   GLY A  23      -1.983   5.112  19.450  1.00 19.28           C  
ATOM    179  O   GLY A  23      -1.528   5.260  18.311  1.00 13.67           O  
ATOM    180  N   HIS A  24      -1.228   5.166  20.544  1.00 13.00           N  
ATOM    181  CA  HIS A  24       0.208   5.399  20.459  1.00 23.79           C  
ATOM    182  C   HIS A  24       0.885   4.233  19.755  1.00 10.78           C  
ATOM    183  O   HIS A  24       1.887   4.412  19.063  1.00 11.69           O  
ATOM    184  CB  HIS A  24       0.812   5.582  21.855  1.00 22.77           C  
ATOM    185  CG  HIS A  24       0.480   6.896  22.493  1.00 22.23           C  
ATOM    186  ND1 HIS A  24      -0.788   7.216  22.928  1.00 16.20           N  
ATOM    187  CD2 HIS A  24       1.253   7.975  22.762  1.00 26.85           C  
ATOM    188  CE1 HIS A  24      -0.782   8.434  23.439  1.00 12.37           C  
ATOM    189  NE2 HIS A  24       0.444   8.917  23.350  1.00 19.24           N  
ATOM    190  N   GLY A  25       0.324   3.041  19.934  1.00  9.86           N  
ATOM    191  CA  GLY A  25       0.877   1.853  19.311  1.00 18.25           C  
ATOM    192  C   GLY A  25       0.740   1.883  17.800  1.00 20.62           C  
ATOM    193  O   GLY A  25       1.672   1.523  17.078  1.00 20.44           O  
ATOM    194  N   GLN A  26      -0.426   2.305  17.318  1.00 15.96           N  
ATOM    195  CA  GLN A  26      -0.663   2.387  15.879  1.00 25.41           C  
ATOM    196  C   GLN A  26       0.292   3.383  15.234  1.00 18.64           C  
ATOM    197  O   GLN A  26       0.994   3.051  14.280  1.00 18.78           O  
ATOM    198  CB  GLN A  26      -2.106   2.809  15.587  1.00 16.01           C  
ATOM    199  CG  GLN A  26      -3.114   1.678  15.623  1.00 20.19           C  
ATOM    200  CD  GLN A  26      -4.505   2.133  15.216  1.00 36.75           C  
ATOM    201  OE1 GLN A  26      -5.142   2.926  15.914  1.00 36.54           O  
ATOM    202  NE2 GLN A  26      -4.982   1.640  14.077  1.00 18.46           N  
ATOM    203  N   ASP A  27       0.319   4.603  15.762  1.00 23.29           N  
ATOM    204  CA  ASP A  27       1.195   5.638  15.227  1.00 22.54           C  
ATOM    205  C   ASP A  27       2.642   5.166  15.163  1.00 19.66           C  
ATOM    206  O   ASP A  27       3.304   5.311  14.139  1.00 17.52           O  
ATOM    207  CB  ASP A  27       1.124   6.908  16.082  1.00 14.50           C  
ATOM    208  CG  ASP A  27      -0.261   7.517  16.112  1.00 23.01           C  
ATOM    209  OD1 ASP A  27      -1.024   7.315  15.143  1.00 19.28           O  
ATOM    210  OD2 ASP A  27      -0.580   8.212  17.101  1.00 24.94           O  
ATOM    211  N   ILE A  28       3.125   4.595  16.261  1.00 20.96           N  
ATOM    212  CA  ILE A  28       4.501   4.123  16.330  1.00 26.78           C  
ATOM    213  C   ILE A  28       4.804   2.951  15.397  1.00 20.03           C  
ATOM    214  O   ILE A  28       5.835   2.945  14.725  1.00 17.71           O  
ATOM    215  CB  ILE A  28       4.873   3.760  17.784  1.00 21.46           C  
ATOM    216  CG1 ILE A  28       4.780   5.020  18.653  1.00 24.48           C  
ATOM    217  CG2 ILE A  28       6.279   3.176  17.839  1.00 21.17           C  
ATOM    218  CD1 ILE A  28       5.033   4.796  20.128  1.00 17.96           C  
ATOM    219  N   LEU A  29       3.920   1.961  15.342  1.00 27.42           N  
ATOM    220  CA  LEU A  29       4.159   0.830  14.454  1.00 28.67           C  
ATOM    221  C   LEU A  29       4.031   1.269  12.997  1.00 34.30           C  
ATOM    222  O   LEU A  29       4.865   0.919  12.161  1.00 27.95           O  
ATOM    223  CB  LEU A  29       3.185  -0.317  14.750  1.00 33.39           C  
ATOM    224  CG  LEU A  29       3.430  -1.108  16.041  1.00 27.14           C  
ATOM    225  CD1 LEU A  29       2.503  -2.316  16.087  1.00 19.90           C  
ATOM    226  CD2 LEU A  29       4.883  -1.566  16.095  1.00 24.20           C  
ATOM    227  N   ILE A  30       2.991   2.043  12.697  1.00 32.19           N  
ATOM    228  CA  ILE A  30       2.780   2.534  11.338  1.00 26.10           C  
ATOM    229  C   ILE A  30       3.962   3.411  10.942  1.00 21.04           C  
ATOM    230  O   ILE A  30       4.416   3.383   9.799  1.00 25.18           O  
ATOM    231  CB  ILE A  30       1.476   3.361  11.229  1.00 26.11           C  
ATOM    232  CG1 ILE A  30       0.264   2.457  11.474  1.00 20.49           C  
ATOM    233  CG2 ILE A  30       1.382   4.015   9.857  1.00 17.84           C  
ATOM    234  CD1 ILE A  30      -1.063   3.189  11.477  1.00 23.74           C  
ATOM    235  N   ARG A  31       4.456   4.189  11.899  1.00 25.78           N  
ATOM    236  CA  ARG A  31       5.596   5.065  11.665  1.00 19.52           C  
ATOM    237  C   ARG A  31       6.840   4.219  11.407  1.00 26.03           C  
ATOM    238  O   ARG A  31       7.680   4.567  10.576  1.00 23.48           O  
ATOM    239  CB  ARG A  31       5.819   5.970  12.882  1.00 26.84           C  
ATOM    240  CG  ARG A  31       7.153   6.704  12.897  1.00 15.96           C  
ATOM    241  CD  ARG A  31       7.299   7.643  11.716  1.00 28.56           C  
ATOM    242  NE  ARG A  31       8.633   8.233  11.667  1.00 34.85           N  
ATOM    243  CZ  ARG A  31       9.044   9.076  10.726  1.00 33.08           C  
ATOM    244  NH1 ARG A  31       8.219   9.432   9.751  1.00 30.27           N  
ATOM    245  NH2 ARG A  31      10.279   9.562  10.758  1.00 26.14           N  
ATOM    246  N   LEU A  32       6.945   3.106  12.127  1.00 21.83           N  
ATOM    247  CA  LEU A  32       8.076   2.196  11.989  1.00 24.87           C  
ATOM    248  C   LEU A  32       8.068   1.489  10.639  1.00 25.23           C  
ATOM    249  O   LEU A  32       9.101   1.380   9.978  1.00 32.35           O  
ATOM    250  CB  LEU A  32       8.045   1.138  13.097  1.00 23.68           C  
ATOM    251  CG  LEU A  32       9.042  -0.013  12.915  1.00 26.86           C  
ATOM    252  CD1 LEU A  32      10.438   0.456  13.287  1.00 29.30           C  
ATOM    253  CD2 LEU A  32       8.633  -1.196  13.774  1.00 29.75           C  
ATOM    254  N   PHE A  33       6.899   1.004  10.237  1.00 20.70           N  
ATOM    255  CA  PHE A  33       6.769   0.291   8.975  1.00 23.42           C  
ATOM    256  C   PHE A  33       6.971   1.190   7.759  1.00 27.67           C  
ATOM    257  O   PHE A  33       7.576   0.774   6.770  1.00 30.72           O  
ATOM    258  CB  PHE A  33       5.404  -0.401   8.905  1.00  7.68           C  
ATOM    259  CG  PHE A  33       5.162  -1.370  10.030  1.00 11.99           C  
ATOM    260  CD1 PHE A  33       6.187  -2.191  10.490  1.00 19.87           C  
ATOM    261  CD2 PHE A  33       3.906  -1.477  10.617  1.00 14.97           C  
ATOM    262  CE1 PHE A  33       5.966  -3.104  11.519  1.00 18.01           C  
ATOM    263  CE2 PHE A  33       3.675  -2.387  11.646  1.00 15.58           C  
ATOM    264  CZ  PHE A  33       4.708  -3.202  12.098  1.00 14.20           C  
ATOM    265  N   LYS A  34       6.468   2.418   7.831  1.00 26.46           N  
ATOM    266  CA  LYS A  34       6.622   3.357   6.724  1.00 27.84           C  
ATOM    267  C   LYS A  34       8.089   3.719   6.530  1.00 27.75           C  
ATOM    268  O   LYS A  34       8.611   3.665   5.417  1.00 36.77           O  
ATOM    269  CB  LYS A  34       5.821   4.633   6.984  1.00 27.56           C  
ATOM    270  CG  LYS A  34       4.484   4.699   6.270  1.00 42.40           C  
ATOM    271  CD  LYS A  34       3.826   6.052   6.495  1.00 51.55           C  
ATOM    272  CE  LYS A  34       2.593   6.221   5.626  1.00 63.68           C  
ATOM    273  NZ  LYS A  34       2.534   7.590   5.037  1.00 72.45           N  
ATOM    274  N   SER A  35       8.748   4.085   7.624  1.00 32.17           N  
ATOM    275  CA  SER A  35      10.152   4.469   7.584  1.00 34.75           C  
ATOM    276  C   SER A  35      11.076   3.321   7.194  1.00 30.41           C  
ATOM    277  O   SER A  35      12.055   3.524   6.474  1.00 38.87           O  
ATOM    278  CB  SER A  35      10.578   5.031   8.942  1.00 30.64           C  
ATOM    279  OG  SER A  35       9.889   6.233   9.232  1.00 45.60           O  
ATOM    280  N   HIS A  36      10.764   2.119   7.667  1.00 27.42           N  
ATOM    281  CA  HIS A  36      11.581   0.943   7.374  1.00 30.18           C  
ATOM    282  C   HIS A  36      10.701  -0.265   7.054  1.00 23.55           C  
ATOM    283  O   HIS A  36      10.545  -1.166   7.874  1.00 17.21           O  
ATOM    284  CB  HIS A  36      12.466   0.624   8.579  1.00 27.56           C  
ATOM    285  CG  HIS A  36      13.103   1.831   9.191  1.00 21.21           C  
ATOM    286  ND1 HIS A  36      14.260   2.398   8.699  1.00 32.45           N  
ATOM    287  CD2 HIS A  36      12.719   2.604  10.232  1.00 26.46           C  
ATOM    288  CE1 HIS A  36      14.560   3.469   9.412  1.00 23.03           C  
ATOM    289  NE2 HIS A  36      13.640   3.617  10.348  1.00 32.15           N  
ATOM    290  N   PRO A  37      10.118  -0.297   5.847  1.00 31.78           N  
ATOM    291  CA  PRO A  37       9.248  -1.391   5.409  1.00 36.14           C  
ATOM    292  C   PRO A  37       9.759  -2.805   5.691  1.00 34.95           C  
ATOM    293  O   PRO A  37       8.961  -3.719   5.898  1.00 30.18           O  
ATOM    294  CB  PRO A  37       9.093  -1.121   3.917  1.00 31.54           C  
ATOM    295  CG  PRO A  37       9.082   0.371   3.869  1.00 32.42           C  
ATOM    296  CD  PRO A  37      10.226   0.732   4.796  1.00 30.42           C  
ATOM    297  N   GLU A  38      11.077  -2.987   5.703  1.00 38.20           N  
ATOM    298  CA  GLU A  38      11.650  -4.311   5.943  1.00 40.63           C  
ATOM    299  C   GLU A  38      11.164  -4.954   7.242  1.00 30.97           C  
ATOM    300  O   GLU A  38      10.919  -6.159   7.289  1.00 22.11           O  
ATOM    301  CB  GLU A  38      13.185  -4.248   5.959  1.00 25.81           C  
ATOM    302  CG  GLU A  38      13.773  -3.502   7.144  1.00 18.74           C  
ATOM    303  CD  GLU A  38      14.134  -2.070   6.813  1.00 22.42           C  
ATOM    304  OE1 GLU A  38      13.297  -1.364   6.214  1.00 35.30           O  
ATOM    305  OE2 GLU A  38      15.257  -1.648   7.158  1.00 26.49           O  
ATOM    306  N   THR A  39      11.025  -4.150   8.291  1.00 25.26           N  
ATOM    307  CA  THR A  39      10.577  -4.656   9.586  1.00 19.07           C  
ATOM    308  C   THR A  39       9.143  -5.174   9.518  1.00 24.21           C  
ATOM    309  O   THR A  39       8.734  -6.013  10.321  1.00 20.12           O  
ATOM    310  CB  THR A  39      10.661  -3.564  10.672  1.00 24.98           C  
ATOM    311  OG1 THR A  39       9.731  -2.515  10.375  1.00 35.34           O  
ATOM    312  CG2 THR A  39      12.069  -2.983  10.730  1.00 16.80           C  
ATOM    313  N   LEU A  40       8.384  -4.666   8.553  1.00 24.21           N  
ATOM    314  CA  LEU A  40       6.996  -5.072   8.362  1.00 29.97           C  
ATOM    315  C   LEU A  40       6.925  -6.578   8.117  1.00 37.52           C  
ATOM    316  O   LEU A  40       6.043  -7.266   8.633  1.00 38.19           O  
ATOM    317  CB  LEU A  40       6.410  -4.315   7.167  1.00 30.04           C  
ATOM    318  CG  LEU A  40       4.938  -4.501   6.802  1.00 32.60           C  
ATOM    319  CD1 LEU A  40       4.054  -4.203   8.000  1.00 31.81           C  
ATOM    320  CD2 LEU A  40       4.602  -3.572   5.644  1.00 44.63           C  
ATOM    321  N   GLU A  41       7.875  -7.070   7.330  1.00 42.02           N  
ATOM    322  CA  GLU A  41       7.980  -8.480   6.969  1.00 43.29           C  
ATOM    323  C   GLU A  41       7.901  -9.394   8.196  1.00 47.68           C  
ATOM    324  O   GLU A  41       7.265 -10.446   8.160  1.00 46.94           O  
ATOM    325  CB  GLU A  41       9.312  -8.704   6.244  1.00 47.91           C  
ATOM    326  CG  GLU A  41       9.367  -9.904   5.321  1.00 51.75           C  
ATOM    327  CD  GLU A  41      10.740 -10.073   4.697  1.00 58.47           C  
ATOM    328  OE1 GLU A  41      11.310  -9.058   4.243  1.00 56.33           O  
ATOM    329  OE2 GLU A  41      11.244 -11.216   4.656  1.00 61.71           O  
ATOM    330  N   LYS A  42       8.540  -8.971   9.280  1.00 50.98           N  
ATOM    331  CA  LYS A  42       8.589  -9.739  10.523  1.00 54.37           C  
ATOM    332  C   LYS A  42       7.254 -10.106  11.188  1.00 56.32           C  
ATOM    333  O   LYS A  42       7.235 -10.758  12.240  1.00 61.15           O  
ATOM    334  CB  LYS A  42       9.491  -9.012  11.519  1.00 50.40           C  
ATOM    335  CG  LYS A  42      10.958  -9.044  11.121  1.00 45.82           C  
ATOM    336  CD  LYS A  42      11.468 -10.481  11.058  1.00 35.49           C  
ATOM    337  CE  LYS A  42      12.968 -10.524  10.808  1.00 31.81           C  
ATOM    338  NZ  LYS A  42      13.519 -11.907  10.869  1.00 18.00           N  
ATOM    339  N   PHE A  43       6.147  -9.683  10.584  1.00 52.56           N  
ATOM    340  CA  PHE A  43       4.823  -9.998  11.098  1.00 46.75           C  
ATOM    341  C   PHE A  43       4.106 -10.741   9.993  1.00 57.37           C  
ATOM    342  O   PHE A  43       4.006 -10.274   8.854  1.00 63.53           O  
ATOM    343  CB  PHE A  43       4.071  -8.730  11.515  1.00 42.97           C  
ATOM    344  CG  PHE A  43       4.620  -8.096  12.770  1.00 33.77           C  
ATOM    345  CD1 PHE A  43       5.784  -7.331  12.731  1.00 34.14           C  
ATOM    346  CD2 PHE A  43       3.986  -8.279  13.994  1.00 33.32           C  
ATOM    347  CE1 PHE A  43       6.304  -6.760  13.894  1.00 35.90           C  
ATOM    348  CE2 PHE A  43       4.500  -7.712  15.162  1.00 41.03           C  
ATOM    349  CZ  PHE A  43       5.660  -6.953  15.110  1.00 43.30           C  
ATOM    350  N   ASP A  44       3.631 -11.920  10.336  1.00 60.70           N  
ATOM    351  CA  ASP A  44       3.006 -12.767   9.355  1.00 65.46           C  
ATOM    352  C   ASP A  44       1.590 -12.354   9.031  1.00 62.65           C  
ATOM    353  O   ASP A  44       1.107 -12.597   7.923  1.00 62.64           O  
ATOM    354  CB  ASP A  44       3.053 -14.217   9.841  1.00 77.99           C  
ATOM    355  CG  ASP A  44       4.463 -14.665  10.221  1.00 89.92           C  
ATOM    356  OD1 ASP A  44       5.450 -14.038   9.770  1.00 91.06           O  
ATOM    357  OD2 ASP A  44       4.576 -15.658  10.964  1.00 94.09           O  
ATOM    358  N   ARG A  45       0.925 -11.724   9.992  1.00 56.76           N  
ATOM    359  CA  ARG A  45      -0.438 -11.277   9.761  1.00 59.16           C  
ATOM    360  C   ARG A  45      -0.374 -10.097   8.813  1.00 55.75           C  
ATOM    361  O   ARG A  45      -1.408  -9.590   8.385  1.00 56.91           O  
ATOM    362  CB  ARG A  45      -1.127 -10.810  11.048  1.00 68.46           C  
ATOM    363  CG  ARG A  45      -0.860 -11.636  12.284  1.00 73.43           C  
ATOM    364  CD  ARG A  45       0.461 -11.252  12.898  1.00 73.42           C  
ATOM    365  NE  ARG A  45       0.706 -11.977  14.135  1.00 69.12           N  
ATOM    366  CZ  ARG A  45       1.898 -12.439  14.488  1.00 66.33           C  
ATOM    367  NH1 ARG A  45       2.937 -12.247  13.689  1.00 60.02           N  
ATOM    368  NH2 ARG A  45       2.050 -13.096  15.630  1.00 64.84           N  
ATOM    369  N   PHE A  46       0.841  -9.640   8.500  1.00 48.17           N  
ATOM    370  CA  PHE A  46       0.995  -8.501   7.600  1.00 49.17           C  
ATOM    371  C   PHE A  46       1.783  -8.800   6.331  1.00 49.54           C  
ATOM    372  O   PHE A  46       2.847  -8.223   6.109  1.00 44.21           O  
ATOM    373  CB  PHE A  46       1.661  -7.312   8.308  1.00 50.79           C  
ATOM    374  CG  PHE A  46       1.181  -7.075   9.711  1.00 49.01           C  
ATOM    375  CD1 PHE A  46      -0.128  -7.353  10.086  1.00 49.30           C  
ATOM    376  CD2 PHE A  46       2.051  -6.553  10.660  1.00 52.93           C  
ATOM    377  CE1 PHE A  46      -0.561  -7.116  11.390  1.00 52.39           C  
ATOM    378  CE2 PHE A  46       1.630  -6.313  11.960  1.00 54.99           C  
ATOM    379  CZ  PHE A  46       0.323  -6.595  12.328  1.00 51.58           C  
ATOM    380  N   LYS A  47       1.268  -9.709   5.508  1.00 54.75           N  
ATOM    381  CA  LYS A  47       1.896 -10.024   4.228  1.00 62.03           C  
ATOM    382  C   LYS A  47       0.990  -9.365   3.194  1.00 65.61           C  
ATOM    383  O   LYS A  47       1.067  -9.667   2.003  1.00 59.77           O  
ATOM    384  CB  LYS A  47       1.944 -11.541   3.975  1.00 61.70           C  
ATOM    385  CG  LYS A  47       3.263 -12.228   4.319  1.00 66.47           C  
ATOM    386  CD  LYS A  47       3.224 -13.694   3.896  1.00 72.34           C  
ATOM    387  CE  LYS A  47       4.458 -14.467   4.351  1.00 71.34           C  
ATOM    388  NZ  LYS A  47       5.694 -14.063   3.622  1.00 62.76           N  
ATOM    389  N   HIS A  48       0.135  -8.456   3.666  1.00 69.73           N  
ATOM    390  CA  HIS A  48      -0.811  -7.760   2.795  1.00 70.52           C  
ATOM    391  C   HIS A  48      -1.085  -6.283   3.114  1.00 66.29           C  
ATOM    392  O   HIS A  48      -1.468  -5.522   2.224  1.00 67.10           O  
ATOM    393  CB  HIS A  48      -2.135  -8.528   2.763  1.00 74.92           C  
ATOM    394  CG  HIS A  48      -2.740  -8.755   4.116  1.00 83.39           C  
ATOM    395  ND1 HIS A  48      -2.107  -9.474   5.107  1.00 85.88           N  
ATOM    396  CD2 HIS A  48      -3.928  -8.366   4.636  1.00 80.74           C  
ATOM    397  CE1 HIS A  48      -2.880  -9.518   6.177  1.00 84.41           C  
ATOM    398  NE2 HIS A  48      -3.990  -8.853   5.918  1.00 82.15           N  
ATOM    399  N   LEU A  49      -0.905  -5.873   4.367  1.00 61.94           N  
ATOM    400  CA  LEU A  49      -1.132  -4.474   4.733  1.00 56.62           C  
ATOM    401  C   LEU A  49      -0.186  -3.567   3.944  1.00 48.24           C  
ATOM    402  O   LEU A  49       1.010  -3.518   4.228  1.00 45.88           O  
ATOM    403  CB  LEU A  49      -0.912  -4.270   6.236  1.00 55.29           C  
ATOM    404  CG  LEU A  49      -2.162  -4.081   7.100  1.00 57.31           C  
ATOM    405  CD1 LEU A  49      -3.036  -5.325   7.058  1.00 56.01           C  
ATOM    406  CD2 LEU A  49      -1.736  -3.776   8.521  1.00 45.43           C  
ATOM    407  N   LYS A  50      -0.729  -2.850   2.960  1.00 47.99           N  
ATOM    408  CA  LYS A  50       0.066  -1.959   2.111  1.00 50.08           C  
ATOM    409  C   LYS A  50      -0.103  -0.475   2.429  1.00 49.55           C  
ATOM    410  O   LYS A  50       0.851   0.195   2.827  1.00 51.13           O  
ATOM    411  CB  LYS A  50      -0.275  -2.206   0.639  1.00 56.84           C  
ATOM    412  CG  LYS A  50       0.024  -3.624   0.177  1.00 57.84           C  
ATOM    413  CD  LYS A  50      -0.394  -3.847  -1.266  1.00 57.02           C  
ATOM    414  CE  LYS A  50      -1.901  -3.727  -1.422  1.00 60.99           C  
ATOM    415  NZ  LYS A  50      -2.342  -4.014  -2.812  1.00 54.80           N  
ATOM    416  N   THR A  51      -1.313   0.040   2.244  1.00 44.15           N  
ATOM    417  CA  THR A  51      -1.585   1.447   2.511  1.00 39.64           C  
ATOM    418  C   THR A  51      -1.514   1.740   4.005  1.00 40.40           C  
ATOM    419  O   THR A  51      -1.406   0.826   4.823  1.00 42.35           O  
ATOM    420  CB  THR A  51      -2.985   1.853   2.015  1.00 37.23           C  
ATOM    421  OG1 THR A  51      -3.982   1.195   2.807  1.00 34.94           O  
ATOM    422  CG2 THR A  51      -3.166   1.465   0.557  1.00 41.81           C  
ATOM    423  N   GLU A  52      -1.577   3.020   4.353  1.00 37.33           N  
ATOM    424  CA  GLU A  52      -1.538   3.428   5.750  1.00 37.58           C  
ATOM    425  C   GLU A  52      -2.912   3.127   6.336  1.00 33.46           C  
ATOM    426  O   GLU A  52      -3.033   2.661   7.471  1.00 31.25           O  
ATOM    427  CB  GLU A  52      -1.244   4.925   5.860  1.00 40.65           C  
ATOM    428  CG  GLU A  52      -0.697   5.354   7.211  1.00 50.42           C  
ATOM    429  CD  GLU A  52      -0.552   6.858   7.327  1.00 60.51           C  
ATOM    430  OE1 GLU A  52      -0.122   7.491   6.339  1.00 66.19           O  
ATOM    431  OE2 GLU A  52      -0.856   7.405   8.409  1.00 53.27           O  
ATOM    432  N   ALA A  53      -3.944   3.392   5.540  1.00 34.21           N  
ATOM    433  CA  ALA A  53      -5.324   3.153   5.947  1.00 36.10           C  
ATOM    434  C   ALA A  53      -5.514   1.685   6.319  1.00 30.62           C  
ATOM    435  O   ALA A  53      -6.229   1.364   7.270  1.00 28.50           O  
ATOM    436  CB  ALA A  53      -6.275   3.539   4.820  1.00 36.69           C  
ATOM    437  N   GLU A  54      -4.878   0.797   5.563  1.00 30.44           N  
ATOM    438  CA  GLU A  54      -4.969  -0.631   5.843  1.00 26.48           C  
ATOM    439  C   GLU A  54      -4.352  -0.914   7.210  1.00 20.58           C  
ATOM    440  O   GLU A  54      -4.881  -1.708   7.988  1.00 15.62           O  
ATOM    441  CB  GLU A  54      -4.246  -1.434   4.760  1.00 13.40           C  
ATOM    442  CG  GLU A  54      -5.093  -1.720   3.533  1.00 14.87           C  
ATOM    443  CD  GLU A  54      -4.321  -2.441   2.441  1.00 31.90           C  
ATOM    444  OE1 GLU A  54      -3.420  -3.241   2.773  1.00 31.54           O  
ATOM    445  OE2 GLU A  54      -4.624  -2.219   1.251  1.00 29.99           O  
ATOM    446  N   MET A  55      -3.235  -0.254   7.498  1.00 16.10           N  
ATOM    447  CA  MET A  55      -2.557  -0.419   8.779  1.00 26.16           C  
ATOM    448  C   MET A  55      -3.420   0.135   9.903  1.00 22.62           C  
ATOM    449  O   MET A  55      -3.447  -0.407  11.006  1.00 28.00           O  
ATOM    450  CB  MET A  55      -1.206   0.304   8.764  1.00 17.74           C  
ATOM    451  CG  MET A  55      -0.094  -0.489   8.105  1.00 33.04           C  
ATOM    452  SD  MET A  55       1.400   0.480   7.809  1.00 37.99           S  
ATOM    453  CE  MET A  55       2.189  -0.520   6.539  1.00 28.06           C  
ATOM    454  N   LYS A  56      -4.131   1.216   9.605  1.00 26.03           N  
ATOM    455  CA  LYS A  56      -4.999   1.870  10.575  1.00 22.07           C  
ATOM    456  C   LYS A  56      -6.190   0.994  10.955  1.00 27.27           C  
ATOM    457  O   LYS A  56      -6.709   1.088  12.067  1.00 30.05           O  
ATOM    458  CB  LYS A  56      -5.507   3.195   9.998  1.00 29.16           C  
ATOM    459  CG  LYS A  56      -6.251   4.083  10.985  1.00 36.08           C  
ATOM    460  CD  LYS A  56      -5.293   4.768  11.946  1.00 48.02           C  
ATOM    461  CE  LYS A  56      -6.007   5.822  12.779  1.00 48.21           C  
ATOM    462  NZ  LYS A  56      -5.060   6.590  13.635  1.00 51.67           N  
ATOM    463  N   ALA A  57      -6.618   0.143  10.029  1.00 26.31           N  
ATOM    464  CA  ALA A  57      -7.764  -0.730  10.266  1.00 29.83           C  
ATOM    465  C   ALA A  57      -7.389  -2.109  10.793  1.00 26.18           C  
ATOM    466  O   ALA A  57      -8.212  -2.782  11.413  1.00 29.80           O  
ATOM    467  CB  ALA A  57      -8.578  -0.872   8.985  1.00 28.13           C  
ATOM    468  N   SER A  58      -6.155  -2.535  10.545  1.00 25.05           N  
ATOM    469  CA  SER A  58      -5.706  -3.847  10.997  1.00 27.38           C  
ATOM    470  C   SER A  58      -5.854  -4.017  12.503  1.00 34.49           C  
ATOM    471  O   SER A  58      -5.193  -3.331  13.284  1.00 33.83           O  
ATOM    472  CB  SER A  58      -4.246  -4.074  10.600  1.00 37.98           C  
ATOM    473  OG  SER A  58      -3.778  -5.325  11.076  1.00 28.63           O  
ATOM    474  N   GLU A  59      -6.729  -4.934  12.904  1.00 37.06           N  
ATOM    475  CA  GLU A  59      -6.953  -5.202  14.318  1.00 45.35           C  
ATOM    476  C   GLU A  59      -5.648  -5.728  14.911  1.00 46.52           C  
ATOM    477  O   GLU A  59      -5.250  -5.337  16.007  1.00 48.33           O  
ATOM    478  CB  GLU A  59      -8.067  -6.239  14.486  1.00 42.20           C  
ATOM    479  CG  GLU A  59      -8.633  -6.322  15.895  1.00 47.93           C  
ATOM    480  CD  GLU A  59      -9.410  -5.079  16.286  1.00 47.31           C  
ATOM    481  OE1 GLU A  59      -9.490  -4.142  15.462  1.00 54.57           O  
ATOM    482  OE2 GLU A  59      -9.941  -5.040  17.418  1.00 48.06           O  
ATOM    483  N   ASP A  60      -4.986  -6.614  14.170  1.00 42.76           N  
ATOM    484  CA  ASP A  60      -3.714  -7.186  14.604  1.00 47.33           C  
ATOM    485  C   ASP A  60      -2.708  -6.080  14.883  1.00 43.36           C  
ATOM    486  O   ASP A  60      -2.143  -5.995  15.973  1.00 38.90           O  
ATOM    487  CB  ASP A  60      -3.148  -8.114  13.528  1.00 38.00           C  
ATOM    488  CG  ASP A  60      -3.645  -9.534  13.665  1.00 47.47           C  
ATOM    489  OD1 ASP A  60      -4.449  -9.799  14.582  1.00 50.27           O  
ATOM    490  OD2 ASP A  60      -3.233 -10.387  12.856  1.00 53.95           O  
ATOM    491  N   LEU A  61      -2.489  -5.238  13.878  1.00 37.74           N  
ATOM    492  CA  LEU A  61      -1.557  -4.125  13.982  1.00 21.16           C  
ATOM    493  C   LEU A  61      -1.760  -3.417  15.314  1.00 24.67           C  
ATOM    494  O   LEU A  61      -0.796  -3.061  15.991  1.00 19.92           O  
ATOM    495  CB  LEU A  61      -1.796  -3.138  12.838  1.00 15.67           C  
ATOM    496  CG  LEU A  61      -0.694  -2.148  12.438  1.00 29.08           C  
ATOM    497  CD1 LEU A  61      -0.225  -1.342  13.640  1.00 31.68           C  
ATOM    498  CD2 LEU A  61       0.464  -2.914  11.829  1.00 35.79           C  
ATOM    499  N   LYS A  62      -3.024  -3.224  15.695  1.00 11.90           N  
ATOM    500  CA  LYS A  62      -3.333  -2.535  16.940  1.00 24.37           C  
ATOM    501  C   LYS A  62      -2.966  -3.361  18.171  1.00 24.31           C  
ATOM    502  O   LYS A  62      -2.385  -2.834  19.121  1.00 20.77           O  
ATOM    503  CB  LYS A  62      -4.816  -2.145  16.978  1.00 14.72           C  
ATOM    504  CG  LYS A  62      -5.179  -1.215  18.130  1.00 25.54           C  
ATOM    505  CD  LYS A  62      -6.597  -0.672  17.995  1.00 42.10           C  
ATOM    506  CE  LYS A  62      -7.637  -1.783  18.008  1.00 47.30           C  
ATOM    507  NZ  LYS A  62      -9.019  -1.240  18.111  1.00 39.71           N  
ATOM    508  N   LYS A  63      -3.292  -4.648  18.150  1.00 19.19           N  
ATOM    509  CA  LYS A  63      -2.974  -5.528  19.269  1.00 24.50           C  
ATOM    510  C   LYS A  63      -1.465  -5.562  19.500  1.00 21.90           C  
ATOM    511  O   LYS A  63      -0.998  -5.589  20.638  1.00 29.05           O  
ATOM    512  CB  LYS A  63      -3.477  -6.946  18.989  1.00 21.29           C  
ATOM    513  CG  LYS A  63      -4.991  -7.072  18.945  1.00 33.37           C  
ATOM    514  CD  LYS A  63      -5.433  -8.507  18.676  1.00 48.46           C  
ATOM    515  CE  LYS A  63      -5.013  -9.449  19.796  1.00 55.68           C  
ATOM    516  NZ  LYS A  63      -5.463 -10.852  19.550  1.00 63.48           N  
ATOM    517  N   HIS A  64      -0.710  -5.563  18.408  1.00 14.90           N  
ATOM    518  CA  HIS A  64       0.743  -5.592  18.478  1.00 18.84           C  
ATOM    519  C   HIS A  64       1.305  -4.291  19.028  1.00 24.72           C  
ATOM    520  O   HIS A  64       2.332  -4.290  19.703  1.00 13.98           O  
ATOM    521  CB  HIS A  64       1.325  -5.874  17.093  1.00 19.49           C  
ATOM    522  CG  HIS A  64       1.282  -7.320  16.710  1.00 31.01           C  
ATOM    523  ND1 HIS A  64       1.182  -7.745  15.403  1.00 37.01           N  
ATOM    524  CD2 HIS A  64       1.344  -8.441  17.467  1.00 26.05           C  
ATOM    525  CE1 HIS A  64       1.181  -9.066  15.372  1.00 33.64           C  
ATOM    526  NE2 HIS A  64       1.279  -9.513  16.611  1.00 28.19           N  
ATOM    527  N   GLY A  65       0.629  -3.185  18.740  1.00 17.65           N  
ATOM    528  CA  GLY A  65       1.090  -1.902  19.234  1.00 25.36           C  
ATOM    529  C   GLY A  65       0.997  -1.865  20.745  1.00 16.59           C  
ATOM    530  O   GLY A  65       1.834  -1.265  21.418  1.00 24.33           O  
ATOM    531  N   VAL A  66      -0.031  -2.521  21.275  1.00 14.08           N  
ATOM    532  CA  VAL A  66      -0.256  -2.580  22.711  1.00 19.83           C  
ATOM    533  C   VAL A  66       0.776  -3.474  23.389  1.00 26.09           C  
ATOM    534  O   VAL A  66       1.213  -3.190  24.502  1.00 29.14           O  
ATOM    535  CB  VAL A  66      -1.671  -3.116  23.032  1.00 19.68           C  
ATOM    536  CG1 VAL A  66      -1.797  -3.409  24.522  1.00 10.93           C  
ATOM    537  CG2 VAL A  66      -2.717  -2.097  22.607  1.00 16.31           C  
ATOM    538  N   THR A  67       1.165  -4.551  22.716  1.00 17.93           N  
ATOM    539  CA  THR A  67       2.143  -5.474  23.277  1.00 21.51           C  
ATOM    540  C   THR A  67       3.496  -4.802  23.509  1.00 19.66           C  
ATOM    541  O   THR A  67       4.085  -4.939  24.581  1.00 20.18           O  
ATOM    542  CB  THR A  67       2.349  -6.701  22.360  1.00 21.18           C  
ATOM    543  OG1 THR A  67       1.096  -7.364  22.153  1.00 11.31           O  
ATOM    544  CG2 THR A  67       3.322  -7.681  22.996  1.00  7.04           C  
ATOM    545  N   VAL A  68       3.983  -4.072  22.508  1.00 20.81           N  
ATOM    546  CA  VAL A  68       5.273  -3.393  22.619  1.00 23.59           C  
ATOM    547  C   VAL A  68       5.326  -2.359  23.734  1.00 29.30           C  
ATOM    548  O   VAL A  68       6.136  -2.469  24.654  1.00 21.59           O  
ATOM    549  CB  VAL A  68       5.663  -2.670  21.312  1.00 31.18           C  
ATOM    550  CG1 VAL A  68       6.800  -3.400  20.637  1.00 37.65           C  
ATOM    551  CG2 VAL A  68       4.466  -2.566  20.391  1.00 33.01           C  
ATOM    552  N   LEU A  69       4.470  -1.348  23.639  1.00 23.89           N  
ATOM    553  CA  LEU A  69       4.436  -0.285  24.634  1.00 22.68           C  
ATOM    554  C   LEU A  69       4.207  -0.848  26.031  1.00 16.54           C  
ATOM    555  O   LEU A  69       4.857  -0.429  26.987  1.00 12.19           O  
ATOM    556  CB  LEU A  69       3.348   0.730  24.276  1.00 18.01           C  
ATOM    557  CG  LEU A  69       3.437   1.249  22.836  1.00 14.06           C  
ATOM    558  CD1 LEU A  69       2.454   2.387  22.643  1.00 14.77           C  
ATOM    559  CD2 LEU A  69       4.855   1.719  22.538  1.00 14.08           C  
ATOM    560  N   THR A  70       3.285  -1.800  26.141  1.00 19.01           N  
ATOM    561  CA  THR A  70       2.996  -2.431  27.421  1.00 21.49           C  
ATOM    562  C   THR A  70       4.288  -2.974  28.019  1.00 26.62           C  
ATOM    563  O   THR A  70       4.645  -2.658  29.152  1.00 26.78           O  
ATOM    564  CB  THR A  70       1.989  -3.589  27.258  1.00 11.89           C  
ATOM    565  OG1 THR A  70       0.660  -3.096  27.467  1.00 38.72           O  
ATOM    566  CG2 THR A  70       2.279  -4.708  28.252  1.00 27.92           C  
ATOM    567  N   ALA A  71       4.988  -3.788  27.238  1.00 19.16           N  
ATOM    568  CA  ALA A  71       6.234  -4.388  27.683  1.00 18.53           C  
ATOM    569  C   ALA A  71       7.320  -3.339  27.891  1.00 21.12           C  
ATOM    570  O   ALA A  71       8.007  -3.347  28.911  1.00 18.59           O  
ATOM    571  CB  ALA A  71       6.695  -5.433  26.676  1.00  8.56           C  
ATOM    572  N   LEU A  72       7.472  -2.435  26.928  1.00 17.70           N  
ATOM    573  CA  LEU A  72       8.490  -1.397  27.031  1.00 22.16           C  
ATOM    574  C   LEU A  72       8.244  -0.543  28.267  1.00 18.77           C  
ATOM    575  O   LEU A  72       9.170  -0.239  29.016  1.00 13.48           O  
ATOM    576  CB  LEU A  72       8.492  -0.516  25.779  1.00 18.54           C  
ATOM    577  CG  LEU A  72       9.636   0.500  25.704  1.00 25.75           C  
ATOM    578  CD1 LEU A  72      10.971  -0.226  25.823  1.00 16.66           C  
ATOM    579  CD2 LEU A  72       9.561   1.269  24.392  1.00 26.75           C  
ATOM    580  N   GLY A  73       6.989  -0.159  28.475  1.00 22.64           N  
ATOM    581  CA  GLY A  73       6.652   0.641  29.635  1.00 18.91           C  
ATOM    582  C   GLY A  73       7.034  -0.092  30.905  1.00 25.56           C  
ATOM    583  O   GLY A  73       7.507   0.515  31.864  1.00 29.98           O  
ATOM    584  N   ALA A  74       6.832  -1.407  30.910  1.00 29.46           N  
ATOM    585  CA  ALA A  74       7.166  -2.229  32.067  1.00 21.55           C  
ATOM    586  C   ALA A  74       8.670  -2.179  32.318  1.00 23.93           C  
ATOM    587  O   ALA A  74       9.118  -2.082  33.461  1.00 28.23           O  
ATOM    588  CB  ALA A  74       6.720  -3.668  31.832  1.00 19.25           C  
ATOM    589  N   ILE A  75       9.443  -2.239  31.239  1.00 15.95           N  
ATOM    590  CA  ILE A  75      10.897  -2.200  31.325  1.00 19.52           C  
ATOM    591  C   ILE A  75      11.408  -0.838  31.791  1.00 27.21           C  
ATOM    592  O   ILE A  75      12.341  -0.760  32.589  1.00 36.16           O  
ATOM    593  CB  ILE A  75      11.540  -2.541  29.962  1.00 19.54           C  
ATOM    594  CG1 ILE A  75      11.291  -4.013  29.635  1.00 18.91           C  
ATOM    595  CG2 ILE A  75      13.031  -2.235  29.986  1.00 23.05           C  
ATOM    596  CD1 ILE A  75      11.865  -4.444  28.315  1.00 24.99           C  
ATOM    597  N   LEU A  76      10.796   0.232  31.289  1.00 30.19           N  
ATOM    598  CA  LEU A  76      11.199   1.586  31.660  1.00 23.00           C  
ATOM    599  C   LEU A  76      10.909   1.881  33.127  1.00 25.03           C  
ATOM    600  O   LEU A  76      11.671   2.585  33.788  1.00 29.46           O  
ATOM    601  CB  LEU A  76      10.483   2.615  30.781  1.00  9.17           C  
ATOM    602  CG  LEU A  76      10.914   2.692  29.314  1.00 16.80           C  
ATOM    603  CD1 LEU A  76      10.030   3.691  28.574  1.00  6.98           C  
ATOM    604  CD2 LEU A  76      12.380   3.104  29.230  1.00  4.66           C  
ATOM    605  N   LYS A  77       9.806   1.339  33.629  1.00 21.92           N  
ATOM    606  CA  LYS A  77       9.418   1.544  35.017  1.00 18.78           C  
ATOM    607  C   LYS A  77      10.414   0.896  35.979  1.00 23.43           C  
ATOM    608  O   LYS A  77      10.424   1.207  37.169  1.00 20.28           O  
ATOM    609  CB  LYS A  77       8.013   0.985  35.250  1.00 17.61           C  
ATOM    610  CG  LYS A  77       6.922   1.698  34.459  1.00 23.71           C  
ATOM    611  CD  LYS A  77       5.695   0.809  34.297  1.00 34.79           C  
ATOM    612  CE  LYS A  77       4.612   1.465  33.446  1.00 22.02           C  
ATOM    613  NZ  LYS A  77       3.947   2.599  34.147  1.00 29.81           N  
ATOM    614  N   LYS A  78      11.249  -0.003  35.462  1.00 22.54           N  
ATOM    615  CA  LYS A  78      12.247  -0.671  36.291  1.00 25.22           C  
ATOM    616  C   LYS A  78      13.435   0.259  36.489  1.00 23.38           C  
ATOM    617  O   LYS A  78      14.327   0.002  37.297  1.00 23.39           O  
ATOM    618  CB  LYS A  78      12.702  -1.982  35.639  1.00 23.01           C  
ATOM    619  CG  LYS A  78      11.582  -2.994  35.414  1.00  9.17           C  
ATOM    620  CD  LYS A  78      10.713  -3.189  36.659  1.00 15.99           C  
ATOM    621  CE  LYS A  78      11.518  -3.633  37.874  1.00 10.36           C  
ATOM    622  NZ  LYS A  78      12.214  -4.932  37.664  1.00 19.95           N  
ATOM    623  N   LYS A  79      13.436   1.346  35.730  1.00 24.73           N  
ATOM    624  CA  LYS A  79      14.488   2.344  35.820  1.00 21.83           C  
ATOM    625  C   LYS A  79      15.911   1.784  35.803  1.00 28.14           C  
ATOM    626  O   LYS A  79      16.766   2.229  36.567  1.00 33.01           O  
ATOM    627  CB  LYS A  79      14.275   3.181  37.081  1.00 13.09           C  
ATOM    628  CG  LYS A  79      12.940   3.912  37.117  1.00 20.77           C  
ATOM    629  CD  LYS A  79      12.741   4.637  38.443  1.00 27.91           C  
ATOM    630  CE  LYS A  79      13.914   5.558  38.748  1.00 27.72           C  
ATOM    631  NZ  LYS A  79      14.788   4.968  39.805  1.00 57.58           N  
ATOM    632  N   GLY A  80      16.159   0.807  34.937  1.00 27.37           N  
ATOM    633  CA  GLY A  80      17.495   0.247  34.838  1.00 28.23           C  
ATOM    634  C   GLY A  80      17.674  -1.156  35.381  1.00 26.30           C  
ATOM    635  O   GLY A  80      18.531  -1.906  34.922  1.00 32.07           O  
ATOM    636  N   HIS A  81      16.878  -1.503  36.358  1.00 23.54           N  
ATOM    637  CA  HIS A  81      16.961  -2.824  36.949  1.00 28.50           C  
ATOM    638  C   HIS A  81      15.946  -3.710  36.239  1.00 21.07           C  
ATOM    639  O   HIS A  81      14.918  -4.076  36.813  1.00 13.22           O  
ATOM    640  CB  HIS A  81      16.637  -2.707  38.435  1.00 32.49           C  
ATOM    641  CG  HIS A  81      17.421  -1.637  39.124  1.00 35.78           C  
ATOM    642  ND1 HIS A  81      18.744  -1.798  39.473  1.00 35.74           N  
ATOM    643  CD2 HIS A  81      17.092  -0.369  39.467  1.00 29.33           C  
ATOM    644  CE1 HIS A  81      19.197  -0.675  40.001  1.00 35.38           C  
ATOM    645  NE2 HIS A  81      18.214   0.207  40.010  1.00 37.94           N  
ATOM    646  N   HIS A  82      16.262  -4.069  34.996  1.00 16.01           N  
ATOM    647  CA  HIS A  82      15.390  -4.859  34.133  1.00 23.48           C  
ATOM    648  C   HIS A  82      16.048  -6.103  33.521  1.00 23.05           C  
ATOM    649  O   HIS A  82      15.474  -6.742  32.636  1.00 20.15           O  
ATOM    650  CB  HIS A  82      14.936  -3.939  33.010  1.00 21.70           C  
ATOM    651  CG  HIS A  82      16.076  -3.283  32.296  1.00 11.97           C  
ATOM    652  ND1 HIS A  82      15.995  -2.009  31.777  1.00 16.80           N  
ATOM    653  CD2 HIS A  82      17.323  -3.727  32.012  1.00 12.45           C  
ATOM    654  CE1 HIS A  82      17.144  -1.697  31.205  1.00  8.78           C  
ATOM    655  NE2 HIS A  82      17.966  -2.722  31.333  1.00 11.74           N  
ATOM    656  N   GLU A  83      17.252  -6.436  33.974  1.00 17.33           N  
ATOM    657  CA  GLU A  83      17.973  -7.584  33.427  1.00 20.97           C  
ATOM    658  C   GLU A  83      17.129  -8.847  33.291  1.00 19.56           C  
ATOM    659  O   GLU A  83      17.059  -9.443  32.218  1.00 11.94           O  
ATOM    660  CB  GLU A  83      19.214  -7.882  34.268  1.00 18.06           C  
ATOM    661  CG  GLU A  83      20.073  -8.997  33.705  1.00 33.56           C  
ATOM    662  CD  GLU A  83      21.412  -9.107  34.400  1.00 36.44           C  
ATOM    663  OE1 GLU A  83      22.163  -8.110  34.400  1.00 45.23           O  
ATOM    664  OE2 GLU A  83      21.716 -10.188  34.943  1.00 50.76           O  
ATOM    665  N   ALA A  84      16.487  -9.249  34.380  1.00 11.70           N  
ATOM    666  CA  ALA A  84      15.655 -10.444  34.378  1.00 16.00           C  
ATOM    667  C   ALA A  84      14.506 -10.333  33.380  1.00 18.81           C  
ATOM    668  O   ALA A  84      14.094 -11.330  32.789  1.00 24.33           O  
ATOM    669  CB  ALA A  84      15.118 -10.690  35.768  1.00 21.40           C  
ATOM    670  N   GLU A  85      13.990  -9.123  33.189  1.00 16.86           N  
ATOM    671  CA  GLU A  85      12.892  -8.913  32.251  1.00 13.36           C  
ATOM    672  C   GLU A  85      13.343  -9.117  30.812  1.00 22.74           C  
ATOM    673  O   GLU A  85      12.607  -9.666  29.990  1.00 22.16           O  
ATOM    674  CB  GLU A  85      12.314  -7.499  32.390  1.00 12.67           C  
ATOM    675  CG  GLU A  85      11.365  -7.303  33.564  1.00 11.19           C  
ATOM    676  CD  GLU A  85      12.075  -7.169  34.899  1.00 17.95           C  
ATOM    677  OE1 GLU A  85      13.317  -7.288  34.939  1.00 16.26           O  
ATOM    678  OE2 GLU A  85      11.383  -6.942  35.912  1.00 19.90           O  
ATOM    679  N   LEU A  86      14.560  -8.676  30.514  1.00 19.45           N  
ATOM    680  CA  LEU A  86      15.104  -8.781  29.167  1.00 18.15           C  
ATOM    681  C   LEU A  86      15.459 -10.201  28.738  1.00 22.83           C  
ATOM    682  O   LEU A  86      15.493 -10.502  27.542  1.00 19.51           O  
ATOM    683  CB  LEU A  86      16.337  -7.882  29.032  1.00 20.63           C  
ATOM    684  CG  LEU A  86      16.112  -6.403  29.359  1.00 20.41           C  
ATOM    685  CD1 LEU A  86      17.387  -5.618  29.094  1.00 17.05           C  
ATOM    686  CD2 LEU A  86      14.971  -5.859  28.517  1.00 23.50           C  
ATOM    687  N   LYS A  87      15.716 -11.074  29.707  1.00 25.49           N  
ATOM    688  CA  LYS A  87      16.075 -12.452  29.395  1.00 24.99           C  
ATOM    689  C   LYS A  87      15.084 -13.121  28.442  1.00 24.94           C  
ATOM    690  O   LYS A  87      15.463 -13.545  27.347  1.00 11.37           O  
ATOM    691  CB  LYS A  87      16.214 -13.276  30.681  1.00 22.99           C  
ATOM    692  CG  LYS A  87      17.426 -12.898  31.518  1.00 32.88           C  
ATOM    693  CD  LYS A  87      17.618 -13.836  32.697  1.00 34.70           C  
ATOM    694  CE  LYS A  87      18.895 -13.505  33.456  1.00 42.29           C  
ATOM    695  NZ  LYS A  87      19.127 -14.425  34.605  1.00 44.68           N  
ATOM    696  N   PRO A  88      13.802 -13.217  28.838  1.00 15.29           N  
ATOM    697  CA  PRO A  88      12.822 -13.851  27.951  1.00 19.23           C  
ATOM    698  C   PRO A  88      12.664 -13.077  26.646  1.00 27.19           C  
ATOM    699  O   PRO A  88      12.500 -13.660  25.573  1.00  8.47           O  
ATOM    700  CB  PRO A  88      11.549 -13.845  28.791  1.00 28.03           C  
ATOM    701  CG  PRO A  88      11.701 -12.604  29.609  1.00 14.94           C  
ATOM    702  CD  PRO A  88      13.145 -12.678  30.041  1.00 10.67           C  
ATOM    703  N   LEU A  89      12.725 -11.756  26.757  1.00 19.25           N  
ATOM    704  CA  LEU A  89      12.593 -10.868  25.613  1.00 22.31           C  
ATOM    705  C   LEU A  89      13.628 -11.199  24.543  1.00 25.84           C  
ATOM    706  O   LEU A  89      13.282 -11.493  23.397  1.00 17.67           O  
ATOM    707  CB  LEU A  89      12.775  -9.427  26.079  1.00 28.51           C  
ATOM    708  CG  LEU A  89      11.729  -8.382  25.707  1.00 22.48           C  
ATOM    709  CD1 LEU A  89      10.313  -8.909  25.912  1.00 21.37           C  
ATOM    710  CD2 LEU A  89      11.984  -7.168  26.571  1.00 35.16           C  
ATOM    711  N   ALA A  90      14.900 -11.139  24.927  1.00 25.55           N  
ATOM    712  CA  ALA A  90      15.995 -11.433  24.010  1.00 24.94           C  
ATOM    713  C   ALA A  90      15.865 -12.858  23.491  1.00 21.85           C  
ATOM    714  O   ALA A  90      16.173 -13.140  22.335  1.00 21.53           O  
ATOM    715  CB  ALA A  90      17.331 -11.256  24.718  1.00 32.28           C  
ATOM    716  N   GLN A  91      15.390 -13.745  24.358  1.00 17.59           N  
ATOM    717  CA  GLN A  91      15.215 -15.147  24.012  1.00 25.71           C  
ATOM    718  C   GLN A  91      14.290 -15.320  22.812  1.00 21.22           C  
ATOM    719  O   GLN A  91      14.657 -15.960  21.831  1.00 21.09           O  
ATOM    720  CB  GLN A  91      14.645 -15.917  25.207  1.00 24.51           C  
ATOM    721  CG  GLN A  91      14.880 -17.421  25.151  1.00 42.82           C  
ATOM    722  CD  GLN A  91      14.373 -18.057  23.867  1.00 56.55           C  
ATOM    723  OE1 GLN A  91      15.137 -18.680  23.127  1.00 59.49           O  
ATOM    724  NE2 GLN A  91      13.083 -17.903  23.596  1.00 52.24           N  
ATOM    725  N   SER A  92      13.093 -14.742  22.896  1.00 17.90           N  
ATOM    726  CA  SER A  92      12.100 -14.848  21.829  1.00 21.09           C  
ATOM    727  C   SER A  92      12.422 -14.067  20.555  1.00 22.52           C  
ATOM    728  O   SER A  92      12.245 -14.580  19.449  1.00 19.84           O  
ATOM    729  CB  SER A  92      10.725 -14.419  22.352  1.00 19.74           C  
ATOM    730  OG  SER A  92      10.742 -13.080  22.811  1.00 21.45           O  
ATOM    731  N   HIS A  93      12.889 -12.832  20.703  1.00 13.61           N  
ATOM    732  CA  HIS A  93      13.201 -12.000  19.545  1.00 22.80           C  
ATOM    733  C   HIS A  93      14.468 -12.408  18.822  1.00 29.65           C  
ATOM    734  O   HIS A  93      14.577 -12.252  17.604  1.00 23.32           O  
ATOM    735  CB  HIS A  93      13.304 -10.535  19.960  1.00 14.65           C  
ATOM    736  CG  HIS A  93      12.020  -9.978  20.477  1.00 10.74           C  
ATOM    737  ND1 HIS A  93      11.457 -10.393  21.664  1.00 18.32           N  
ATOM    738  CD2 HIS A  93      11.156  -9.085  19.941  1.00  3.31           C  
ATOM    739  CE1 HIS A  93      10.301  -9.781  21.836  1.00 18.96           C  
ATOM    740  NE2 HIS A  93      10.094  -8.983  20.805  1.00 15.84           N  
ATOM    741  N   ALA A  94      15.429 -12.926  19.572  1.00 22.25           N  
ATOM    742  CA  ALA A  94      16.682 -13.346  18.976  1.00 26.97           C  
ATOM    743  C   ALA A  94      16.519 -14.674  18.249  1.00 26.39           C  
ATOM    744  O   ALA A  94      16.779 -14.769  17.051  1.00 28.87           O  
ATOM    745  CB  ALA A  94      17.756 -13.466  20.046  1.00 30.71           C  
ATOM    746  N   THR A  95      16.061 -15.691  18.972  1.00 20.97           N  
ATOM    747  CA  THR A  95      15.905 -17.023  18.398  1.00 21.82           C  
ATOM    748  C   THR A  95      14.622 -17.294  17.612  1.00 24.49           C  
ATOM    749  O   THR A  95      14.677 -17.705  16.453  1.00 19.71           O  
ATOM    750  CB  THR A  95      16.027 -18.106  19.492  1.00 15.18           C  
ATOM    751  OG1 THR A  95      14.955 -17.965  20.431  1.00 28.63           O  
ATOM    752  CG2 THR A  95      17.352 -17.973  20.228  1.00 17.19           C  
ATOM    753  N   LYS A  96      13.473 -17.064  18.238  1.00 22.20           N  
ATOM    754  CA  LYS A  96      12.186 -17.331  17.602  1.00 28.01           C  
ATOM    755  C   LYS A  96      11.774 -16.423  16.441  1.00 39.42           C  
ATOM    756  O   LYS A  96      11.059 -16.863  15.541  1.00 43.92           O  
ATOM    757  CB  LYS A  96      11.083 -17.331  18.666  1.00 21.17           C  
ATOM    758  CG  LYS A  96       9.700 -17.681  18.138  1.00 26.64           C  
ATOM    759  CD  LYS A  96       8.680 -17.715  19.265  1.00 30.50           C  
ATOM    760  CE  LYS A  96       7.272 -17.935  18.738  1.00 26.90           C  
ATOM    761  NZ  LYS A  96       6.265 -17.895  19.837  1.00 29.32           N  
ATOM    762  N   HIS A  97      12.214 -15.169  16.446  1.00 37.17           N  
ATOM    763  CA  HIS A  97      11.838 -14.252  15.372  1.00 27.12           C  
ATOM    764  C   HIS A  97      13.040 -13.649  14.662  1.00 30.23           C  
ATOM    765  O   HIS A  97      12.900 -13.022  13.612  1.00 23.53           O  
ATOM    766  CB  HIS A  97      10.963 -13.134  15.928  1.00 40.72           C  
ATOM    767  CG  HIS A  97       9.791 -13.625  16.713  1.00 34.18           C  
ATOM    768  ND1 HIS A  97       8.827 -14.445  16.169  1.00 36.34           N  
ATOM    769  CD2 HIS A  97       9.440 -13.437  18.007  1.00 35.56           C  
ATOM    770  CE1 HIS A  97       7.933 -14.743  17.095  1.00 31.76           C  
ATOM    771  NE2 HIS A  97       8.282 -14.144  18.219  1.00 36.87           N  
ATOM    772  N   LYS A  98      14.217 -13.833  15.247  1.00 35.05           N  
ATOM    773  CA  LYS A  98      15.452 -13.319  14.662  1.00 34.97           C  
ATOM    774  C   LYS A  98      15.413 -11.833  14.286  1.00 32.67           C  
ATOM    775  O   LYS A  98      15.685 -11.466  13.146  1.00 33.43           O  
ATOM    776  CB  LYS A  98      15.831 -14.140  13.430  1.00 40.59           C  
ATOM    777  CG  LYS A  98      16.134 -15.598  13.722  1.00 45.12           C  
ATOM    778  CD  LYS A  98      16.761 -16.298  12.527  1.00 53.65           C  
ATOM    779  CE  LYS A  98      17.185 -17.709  12.899  1.00 56.67           C  
ATOM    780  NZ  LYS A  98      17.930 -18.379  11.800  1.00 56.23           N  
ATOM    781  N  AILE A  99      15.080 -10.988  15.260  0.50 30.90           N  
ATOM    782  N  BILE A  99      15.082 -10.988  15.255  0.50 31.33           N  
ATOM    783  CA AILE A  99      15.020  -9.541  15.044  0.50 23.52           C  
ATOM    784  CA BILE A  99      15.014  -9.543  15.046  0.50 24.69           C  
ATOM    785  C  AILE A  99      16.383  -8.913  15.333  0.50 27.23           C  
ATOM    786  C  BILE A  99      16.379  -8.913  15.335  0.50 27.81           C  
ATOM    787  O  AILE A  99      16.874  -8.978  16.457  0.50 27.76           O  
ATOM    788  O  BILE A  99      16.867  -8.974  16.462  0.50 28.51           O  
ATOM    789  CB AILE A  99      13.974  -8.864  15.947  0.50 16.91           C  
ATOM    790  CB BILE A  99      13.960  -8.903  15.961  0.50 18.16           C  
ATOM    791  CG1AILE A  99      12.570  -9.349  15.599  0.50 10.62           C  
ATOM    792  CG1BILE A  99      12.564  -9.398  15.583  0.50 10.46           C  
ATOM    793  CG2AILE A  99      14.065  -7.357  15.803  0.50 10.29           C  
ATOM    794  CG2BILE A  99      14.047  -7.389  15.882  0.50 15.49           C  
ATOM    795  CD1AILE A  99      11.995 -10.308  16.612  0.50 22.30           C  
ATOM    796  CD1BILE A  99      12.142  -9.027  14.180  0.50 11.42           C  
ATOM    797  N   PRO A 100      16.997  -8.257  14.338  1.00 27.38           N  
ATOM    798  CA  PRO A 100      18.301  -7.627  14.503  1.00 32.55           C  
ATOM    799  C   PRO A 100      18.191  -6.447  15.450  1.00 32.53           C  
ATOM    800  O   PRO A 100      17.146  -5.797  15.511  1.00 38.40           O  
ATOM    801  CB  PRO A 100      18.664  -7.222  13.076  1.00 36.49           C  
ATOM    802  CG  PRO A 100      17.863  -8.238  12.222  1.00 42.36           C  
ATOM    803  CD  PRO A 100      16.543  -8.058  12.967  1.00 25.43           C  
ATOM    804  N   ILE A 101      19.257  -6.178  16.192  1.00 25.75           N  
ATOM    805  CA  ILE A 101      19.261  -5.059  17.117  1.00 33.32           C  
ATOM    806  C   ILE A 101      18.980  -3.756  16.371  1.00 36.35           C  
ATOM    807  O   ILE A 101      18.449  -2.802  16.944  1.00 42.45           O  
ATOM    808  CB  ILE A 101      20.619  -4.921  17.844  1.00 33.45           C  
ATOM    809  CG1 ILE A 101      20.886  -6.167  18.698  1.00 27.67           C  
ATOM    810  CG2 ILE A 101      20.613  -3.684  18.729  1.00 35.92           C  
ATOM    811  CD1 ILE A 101      19.882  -6.391  19.805  1.00 23.88           C  
ATOM    812  N   LYS A 102      19.334  -3.722  15.090  1.00 35.72           N  
ATOM    813  CA  LYS A 102      19.120  -2.542  14.261  1.00 32.64           C  
ATOM    814  C   LYS A 102      17.644  -2.153  14.249  1.00 35.28           C  
ATOM    815  O   LYS A 102      17.304  -0.971  14.173  1.00 26.59           O  
ATOM    816  CB  LYS A 102      19.596  -2.811  12.831  1.00 39.70           C  
ATOM    817  CG  LYS A 102      19.586  -1.590  11.923  1.00 52.38           C  
ATOM    818  CD  LYS A 102      20.121  -1.938  10.542  1.00 66.88           C  
ATOM    819  CE  LYS A 102      20.240  -0.708   9.657  1.00 74.19           C  
ATOM    820  NZ  LYS A 102      21.200   0.288  10.213  1.00 69.97           N  
ATOM    821  N   TYR A 103      16.775  -3.157  14.319  1.00 18.48           N  
ATOM    822  CA  TYR A 103      15.335  -2.934  14.334  1.00 24.17           C  
ATOM    823  C   TYR A 103      14.936  -2.209  15.613  1.00 22.49           C  
ATOM    824  O   TYR A 103      14.082  -1.323  15.592  1.00 31.91           O  
ATOM    825  CB  TYR A 103      14.597  -4.272  14.226  1.00 27.07           C  
ATOM    826  CG  TYR A 103      14.528  -4.826  12.815  1.00 21.29           C  
ATOM    827  CD1 TYR A 103      15.509  -4.515  11.872  1.00 27.84           C  
ATOM    828  CD2 TYR A 103      13.491  -5.675  12.429  1.00 24.61           C  
ATOM    829  CE1 TYR A 103      15.457  -5.035  10.580  1.00 22.65           C  
ATOM    830  CE2 TYR A 103      13.431  -6.203  11.137  1.00  9.81           C  
ATOM    831  CZ  TYR A 103      14.417  -5.877  10.222  1.00  9.62           C  
ATOM    832  OH  TYR A 103      14.365  -6.391   8.950  1.00 20.47           O  
ATOM    833  N   LEU A 104      15.558  -2.589  16.725  1.00 23.97           N  
ATOM    834  CA  LEU A 104      15.283  -1.956  18.010  1.00 13.38           C  
ATOM    835  C   LEU A 104      15.584  -0.467  17.860  1.00 13.28           C  
ATOM    836  O   LEU A 104      14.863   0.381  18.381  1.00 18.59           O  
ATOM    837  CB  LEU A 104      16.165  -2.566  19.105  1.00  7.77           C  
ATOM    838  CG  LEU A 104      15.838  -3.972  19.628  1.00 24.08           C  
ATOM    839  CD1 LEU A 104      14.716  -3.890  20.639  1.00 28.82           C  
ATOM    840  CD2 LEU A 104      15.468  -4.901  18.480  1.00 20.91           C  
ATOM    841  N   GLU A 105      16.657  -0.160  17.138  1.00 14.57           N  
ATOM    842  CA  GLU A 105      17.037   1.225  16.898  1.00 23.73           C  
ATOM    843  C   GLU A 105      15.933   1.909  16.101  1.00 23.45           C  
ATOM    844  O   GLU A 105      15.509   3.014  16.439  1.00 29.37           O  
ATOM    845  CB  GLU A 105      18.354   1.298  16.119  1.00 19.53           C  
ATOM    846  CG  GLU A 105      19.598   1.111  16.967  1.00 17.49           C  
ATOM    847  CD  GLU A 105      20.878   1.221  16.158  1.00 35.13           C  
ATOM    848  OE1 GLU A 105      21.043   2.231  15.442  1.00 31.86           O  
ATOM    849  OE2 GLU A 105      21.720   0.301  16.243  1.00 20.45           O  
ATOM    850  N   PHE A 106      15.465   1.243  15.048  1.00 23.81           N  
ATOM    851  CA  PHE A 106      14.408   1.798  14.208  1.00 29.16           C  
ATOM    852  C   PHE A 106      13.158   2.146  15.010  1.00 29.96           C  
ATOM    853  O   PHE A 106      12.608   3.240  14.867  1.00 34.23           O  
ATOM    854  CB  PHE A 106      14.019   0.820  13.091  1.00 28.41           C  
ATOM    855  CG  PHE A 106      15.079   0.627  12.040  1.00 25.67           C  
ATOM    856  CD1 PHE A 106      16.021   1.619  11.781  1.00 28.00           C  
ATOM    857  CD2 PHE A 106      15.105  -0.536  11.273  1.00 29.52           C  
ATOM    858  CE1 PHE A 106      16.973   1.456  10.771  1.00 34.41           C  
ATOM    859  CE2 PHE A 106      16.051  -0.709  10.260  1.00 14.90           C  
ATOM    860  CZ  PHE A 106      16.986   0.289  10.009  1.00 18.70           C  
ATOM    861  N   ILE A 107      12.706   1.219  15.850  1.00 23.71           N  
ATOM    862  CA  ILE A 107      11.511   1.462  16.645  1.00 19.47           C  
ATOM    863  C   ILE A 107      11.737   2.582  17.653  1.00 14.11           C  
ATOM    864  O   ILE A 107      10.792   3.258  18.057  1.00 12.87           O  
ATOM    865  CB  ILE A 107      11.045   0.188  17.384  1.00 19.29           C  
ATOM    866  CG1 ILE A 107       9.607   0.379  17.874  1.00 22.76           C  
ATOM    867  CG2 ILE A 107      11.959  -0.102  18.564  1.00 15.90           C  
ATOM    868  CD1 ILE A 107       8.950  -0.893  18.369  1.00 26.74           C  
ATOM    869  N   SER A 108      12.988   2.778  18.057  1.00 19.68           N  
ATOM    870  CA  SER A 108      13.320   3.839  19.001  1.00 20.09           C  
ATOM    871  C   SER A 108      13.165   5.181  18.293  1.00 24.17           C  
ATOM    872  O   SER A 108      12.707   6.159  18.883  1.00 15.42           O  
ATOM    873  CB  SER A 108      14.757   3.686  19.506  1.00 15.86           C  
ATOM    874  OG  SER A 108      14.905   2.512  20.281  1.00 19.71           O  
ATOM    875  N   GLU A 109      13.555   5.214  17.021  1.00 23.02           N  
ATOM    876  CA  GLU A 109      13.455   6.421  16.208  1.00 24.58           C  
ATOM    877  C   GLU A 109      11.976   6.768  16.072  1.00 24.06           C  
ATOM    878  O   GLU A 109      11.580   7.925  16.215  1.00 20.13           O  
ATOM    879  CB  GLU A 109      14.076   6.165  14.831  1.00 27.48           C  
ATOM    880  CG  GLU A 109      14.226   7.386  13.920  1.00 44.04           C  
ATOM    881  CD  GLU A 109      12.926   7.835  13.274  1.00 42.75           C  
ATOM    882  OE1 GLU A 109      11.984   7.018  13.181  1.00 53.69           O  
ATOM    883  OE2 GLU A 109      12.855   9.005  12.841  1.00 33.60           O  
ATOM    884  N   ALA A 110      11.168   5.745  15.811  1.00 16.70           N  
ATOM    885  CA  ALA A 110       9.729   5.911  15.653  1.00 16.36           C  
ATOM    886  C   ALA A 110       9.076   6.360  16.958  1.00 14.89           C  
ATOM    887  O   ALA A 110       8.142   7.160  16.947  1.00 24.92           O  
ATOM    888  CB  ALA A 110       9.106   4.601  15.175  1.00 15.65           C  
ATOM    889  N   ILE A 111       9.568   5.846  18.082  1.00 21.49           N  
ATOM    890  CA  ILE A 111       9.022   6.208  19.386  1.00 18.14           C  
ATOM    891  C   ILE A 111       9.318   7.666  19.723  1.00 19.50           C  
ATOM    892  O   ILE A 111       8.442   8.395  20.187  1.00 28.42           O  
ATOM    893  CB  ILE A 111       9.584   5.296  20.502  1.00 17.20           C  
ATOM    894  CG1 ILE A 111       9.023   3.882  20.339  1.00 13.77           C  
ATOM    895  CG2 ILE A 111       9.213   5.845  21.875  1.00 13.03           C  
ATOM    896  CD1 ILE A 111       9.573   2.886  21.331  1.00 11.67           C  
ATOM    897  N   ILE A 112      10.555   8.091  19.490  1.00 21.03           N  
ATOM    898  CA  ILE A 112      10.937   9.470  19.763  1.00 23.73           C  
ATOM    899  C   ILE A 112      10.113  10.401  18.878  1.00 19.11           C  
ATOM    900  O   ILE A 112       9.507  11.358  19.357  1.00 23.48           O  
ATOM    901  CB  ILE A 112      12.438   9.705  19.478  1.00 27.23           C  
ATOM    902  CG1 ILE A 112      13.289   8.835  20.407  1.00 39.51           C  
ATOM    903  CG2 ILE A 112      12.779  11.174  19.653  1.00 30.19           C  
ATOM    904  CD1 ILE A 112      12.963   8.997  21.880  1.00 29.21           C  
ATOM    905  N   HIS A 113      10.091  10.100  17.584  1.00 25.25           N  
ATOM    906  CA  HIS A 113       9.354  10.889  16.603  1.00 31.01           C  
ATOM    907  C   HIS A 113       7.876  11.050  16.951  1.00 37.73           C  
ATOM    908  O   HIS A 113       7.318  12.141  16.833  1.00 39.43           O  
ATOM    909  CB  HIS A 113       9.472  10.236  15.224  1.00 25.52           C  
ATOM    910  CG  HIS A 113       8.569  10.834  14.192  1.00 24.70           C  
ATOM    911  ND1 HIS A 113       8.931  11.915  13.418  1.00 33.76           N  
ATOM    912  CD2 HIS A 113       7.306  10.513  13.823  1.00 21.64           C  
ATOM    913  CE1 HIS A 113       7.931  12.233  12.615  1.00 32.21           C  
ATOM    914  NE2 HIS A 113       6.933  11.398  12.842  1.00 25.97           N  
ATOM    915  N   VAL A 114       7.243   9.957  17.366  1.00 30.20           N  
ATOM    916  CA  VAL A 114       5.827   9.984  17.712  1.00 23.96           C  
ATOM    917  C   VAL A 114       5.542  10.726  19.016  1.00 22.86           C  
ATOM    918  O   VAL A 114       4.545  11.440  19.120  1.00 16.46           O  
ATOM    919  CB  VAL A 114       5.254   8.546  17.802  1.00 22.58           C  
ATOM    920  CG1 VAL A 114       3.864   8.571  18.422  1.00  9.99           C  
ATOM    921  CG2 VAL A 114       5.189   7.930  16.410  1.00  9.78           C  
ATOM    922  N   LEU A 115       6.407  10.557  20.009  1.00 15.94           N  
ATOM    923  CA  LEU A 115       6.212  11.232  21.288  1.00 28.72           C  
ATOM    924  C   LEU A 115       6.411  12.734  21.133  1.00 24.02           C  
ATOM    925  O   LEU A 115       5.708  13.536  21.756  1.00 21.35           O  
ATOM    926  CB  LEU A 115       7.181  10.676  22.335  1.00 28.34           C  
ATOM    927  CG  LEU A 115       6.728   9.435  23.113  1.00 26.04           C  
ATOM    928  CD1 LEU A 115       6.245   8.351  22.162  1.00 16.09           C  
ATOM    929  CD2 LEU A 115       7.885   8.934  23.965  1.00 16.99           C  
ATOM    930  N   HIS A 116       7.369  13.106  20.293  1.00 17.30           N  
ATOM    931  CA  HIS A 116       7.661  14.510  20.042  1.00 23.25           C  
ATOM    932  C   HIS A 116       6.490  15.212  19.364  1.00 31.42           C  
ATOM    933  O   HIS A 116       6.159  16.348  19.702  1.00 27.24           O  
ATOM    934  CB  HIS A 116       8.910  14.635  19.172  1.00 18.57           C  
ATOM    935  CG  HIS A 116       9.162  16.022  18.671  1.00 29.19           C  
ATOM    936  ND1 HIS A 116       8.825  16.423  17.397  1.00 35.61           N  
ATOM    937  CD2 HIS A 116       9.717  17.102  19.272  1.00 34.63           C  
ATOM    938  CE1 HIS A 116       9.165  17.689  17.233  1.00 38.56           C  
ATOM    939  NE2 HIS A 116       9.708  18.124  18.355  1.00 36.31           N  
ATOM    940  N   SER A 117       5.840  14.512  18.424  1.00 32.38           N  
ATOM    941  CA  SER A 117       4.709  15.079  17.682  1.00 30.32           C  
ATOM    942  C   SER A 117       3.434  15.040  18.500  1.00 26.77           C  
ATOM    943  O   SER A 117       2.499  15.803  18.255  1.00 32.76           O  
ATOM    944  CB  SER A 117       4.506  14.323  16.356  0.53 24.55           C  
ATOM    945  OG  SER A 117       3.212  13.752  16.269  0.53 23.43           O  
ATOM    946  N   ARG A 118       3.421  14.159  19.480  1.00 28.30           N  
ATOM    947  CA  ARG A 118       2.243  13.977  20.304  1.00 28.22           C  
ATOM    948  C   ARG A 118       2.243  14.662  21.664  1.00 32.02           C  
ATOM    949  O   ARG A 118       1.220  15.196  22.094  1.00 19.15           O  
ATOM    950  CB  ARG A 118       1.999  12.475  20.506  1.00 38.38           C  
ATOM    951  CG  ARG A 118       0.619  11.960  20.094  1.00 31.46           C  
ATOM    952  CD  ARG A 118       0.536  10.472  20.366  1.00 28.03           C  
ATOM    953  NE  ARG A 118      -0.801   9.925  20.173  1.00 31.28           N  
ATOM    954  CZ  ARG A 118      -1.887  10.385  20.779  1.00 33.43           C  
ATOM    955  NH1 ARG A 118      -1.797  11.407  21.618  1.00 44.13           N  
ATOM    956  NH2 ARG A 118      -3.063   9.825  20.544  1.00 44.22           N  
ATOM    957  N   HIS A 119       3.385  14.674  22.339  1.00 26.27           N  
ATOM    958  CA  HIS A 119       3.442  15.260  23.688  1.00 33.92           C  
ATOM    959  C   HIS A 119       4.440  16.404  23.802  1.00 36.06           C  
ATOM    960  O   HIS A 119       5.435  16.352  24.510  1.00 31.87           O  
ATOM    961  CB  HIS A 119       3.702  14.109  24.658  1.00 24.92           C  
ATOM    962  CG  HIS A 119       2.653  13.032  24.576  1.00 35.48           C  
ATOM    963  ND1 HIS A 119       1.343  13.231  24.966  1.00 34.04           N  
ATOM    964  CD2 HIS A 119       2.712  11.759  24.114  1.00 34.59           C  
ATOM    965  CE1 HIS A 119       0.645  12.127  24.754  1.00 33.79           C  
ATOM    966  NE2 HIS A 119       1.452  11.219  24.236  1.00 34.31           N  
ATOM    967  N   PRO A 120       4.123  17.487  23.142  1.00 45.99           N  
ATOM    968  CA  PRO A 120       4.939  18.689  23.078  1.00 47.36           C  
ATOM    969  C   PRO A 120       5.591  19.209  24.360  1.00 49.53           C  
ATOM    970  O   PRO A 120       6.830  19.278  24.500  1.00 50.38           O  
ATOM    971  CB  PRO A 120       3.983  19.675  22.433  1.00 46.69           C  
ATOM    972  CG  PRO A 120       3.218  18.821  21.442  1.00 53.25           C  
ATOM    973  CD  PRO A 120       2.924  17.571  22.293  1.00 50.97           C  
ATOM    974  N   GLY A 121       4.719  19.650  25.261  1.00 44.42           N  
ATOM    975  CA  GLY A 121       5.159  20.196  26.528  1.00 48.64           C  
ATOM    976  C   GLY A 121       5.419  19.097  27.537  1.00 44.18           C  
ATOM    977  O   GLY A 121       5.744  19.346  28.701  1.00 41.70           O  
ATOM    978  N   ASP A 122       5.267  17.864  27.072  1.00 42.49           N  
ATOM    979  CA  ASP A 122       5.481  16.703  27.924  1.00 37.15           C  
ATOM    980  C   ASP A 122       6.730  15.954  27.471  1.00 34.49           C  
ATOM    981  O   ASP A 122       7.243  15.095  28.186  1.00 36.16           O  
ATOM    982  CB  ASP A 122       4.269  15.785  27.839  1.00 45.15           C  
ATOM    983  CG  ASP A 122       2.986  16.551  27.586  1.00 48.53           C  
ATOM    984  OD1 ASP A 122       2.600  17.357  28.457  1.00 52.30           O  
ATOM    985  OD2 ASP A 122       2.371  16.346  26.517  1.00 49.47           O  
ATOM    986  N   PHE A 123       7.211  16.302  26.281  1.00 25.33           N  
ATOM    987  CA  PHE A 123       8.387  15.677  25.694  1.00 12.02           C  
ATOM    988  C   PHE A 123       9.315  16.776  25.189  1.00 16.32           C  
ATOM    989  O   PHE A 123       9.541  16.907  23.988  1.00 25.36           O  
ATOM    990  CB  PHE A 123       7.956  14.771  24.534  1.00 17.29           C  
ATOM    991  CG  PHE A 123       9.016  13.810  24.076  1.00 16.44           C  
ATOM    992  CD1 PHE A 123       9.535  12.860  24.950  1.00 21.36           C  
ATOM    993  CD2 PHE A 123       9.484  13.841  22.766  1.00 13.32           C  
ATOM    994  CE1 PHE A 123      10.507  11.955  24.527  1.00 18.62           C  
ATOM    995  CE2 PHE A 123      10.456  12.939  22.331  1.00  3.90           C  
ATOM    996  CZ  PHE A 123      10.968  11.995  23.213  1.00 15.50           C  
ATOM    997  N   GLY A 124       9.836  17.574  26.115  1.00 19.63           N  
ATOM    998  CA  GLY A 124      10.730  18.652  25.739  1.00 13.83           C  
ATOM    999  C   GLY A 124      12.115  18.125  25.427  1.00 19.43           C  
ATOM   1000  O   GLY A 124      12.369  16.926  25.541  1.00 23.70           O  
ATOM   1001  N   ALA A 125      13.013  19.020  25.033  1.00  8.76           N  
ATOM   1002  CA  ALA A 125      14.379  18.638  24.700  1.00 19.45           C  
ATOM   1003  C   ALA A 125      15.023  17.817  25.815  1.00 21.92           C  
ATOM   1004  O   ALA A 125      15.787  16.890  25.553  1.00 13.53           O  
ATOM   1005  CB  ALA A 125      15.209  19.880  24.420  1.00 16.94           C  
ATOM   1006  N   ASP A 126      14.716  18.164  27.060  1.00 26.98           N  
ATOM   1007  CA  ASP A 126      15.270  17.449  28.202  1.00 26.50           C  
ATOM   1008  C   ASP A 126      14.647  16.061  28.287  1.00 31.17           C  
ATOM   1009  O   ASP A 126      15.344  15.065  28.492  1.00 25.38           O  
ATOM   1010  CB  ASP A 126      15.008  18.234  29.492  1.00 32.38           C  
ATOM   1011  CG  ASP A 126      13.529  18.424  29.775  1.00 42.87           C  
ATOM   1012  OD1 ASP A 126      12.769  18.720  28.827  1.00 41.86           O  
ATOM   1013  OD2 ASP A 126      13.131  18.290  30.953  1.00 40.20           O  
ATOM   1014  N   ALA A 127      13.330  16.003  28.117  1.00 20.98           N  
ATOM   1015  CA  ALA A 127      12.603  14.744  28.166  1.00 25.66           C  
ATOM   1016  C   ALA A 127      13.065  13.818  27.047  1.00 22.28           C  
ATOM   1017  O   ALA A 127      13.333  12.640  27.280  1.00 23.80           O  
ATOM   1018  CB  ALA A 127      11.109  15.002  28.050  1.00 10.35           C  
ATOM   1019  N   GLN A 128      13.157  14.352  25.832  1.00 26.26           N  
ATOM   1020  CA  GLN A 128      13.596  13.550  24.696  1.00 23.95           C  
ATOM   1021  C   GLN A 128      15.023  13.089  24.931  1.00 28.54           C  
ATOM   1022  O   GLN A 128      15.441  12.046  24.429  1.00 29.21           O  
ATOM   1023  CB  GLN A 128      13.527  14.351  23.394  1.00 20.90           C  
ATOM   1024  CG  GLN A 128      13.883  13.524  22.164  1.00 17.76           C  
ATOM   1025  CD  GLN A 128      13.623  14.255  20.864  1.00 18.95           C  
ATOM   1026  OE1 GLN A 128      12.660  15.010  20.752  1.00 18.34           O  
ATOM   1027  NE2 GLN A 128      14.474  14.024  19.868  1.00 10.91           N  
ATOM   1028  N   GLY A 129      15.768  13.880  25.696  1.00 25.95           N  
ATOM   1029  CA  GLY A 129      17.142  13.532  25.999  1.00 24.89           C  
ATOM   1030  C   GLY A 129      17.186  12.338  26.932  1.00 21.26           C  
ATOM   1031  O   GLY A 129      18.015  11.443  26.770  1.00 27.37           O  
ATOM   1032  N   ALA A 130      16.280  12.322  27.905  1.00 26.19           N  
ATOM   1033  CA  ALA A 130      16.202  11.240  28.880  1.00 28.46           C  
ATOM   1034  C   ALA A 130      15.669   9.949  28.258  1.00 28.82           C  
ATOM   1035  O   ALA A 130      16.133   8.857  28.595  1.00 20.33           O  
ATOM   1036  CB  ALA A 130      15.323  11.658  30.060  1.00 18.85           C  
ATOM   1037  N   MET A 131      14.690  10.070  27.358  1.00 27.54           N  
ATOM   1038  CA  MET A 131      14.112   8.900  26.691  1.00 22.07           C  
ATOM   1039  C   MET A 131      15.152   8.257  25.778  1.00 20.78           C  
ATOM   1040  O   MET A 131      15.204   7.034  25.644  1.00 20.40           O  
ATOM   1041  CB  MET A 131      12.874   9.302  25.879  1.00 21.24           C  
ATOM   1042  CG  MET A 131      12.226   8.171  25.076  1.00 13.81           C  
ATOM   1043  SD  MET A 131      11.613   6.806  26.074  1.00 15.06           S  
ATOM   1044  CE  MET A 131      10.116   7.520  26.767  1.00 17.21           C  
ATOM   1045  N   ASN A 132      15.980   9.084  25.150  1.00 19.66           N  
ATOM   1046  CA  ASN A 132      17.018   8.573  24.269  1.00 13.17           C  
ATOM   1047  C   ASN A 132      17.966   7.705  25.091  1.00 22.36           C  
ATOM   1048  O   ASN A 132      18.395   6.642  24.642  1.00 29.48           O  
ATOM   1049  CB  ASN A 132      17.782   9.730  23.618  1.00 21.94           C  
ATOM   1050  CG  ASN A 132      18.930   9.257  22.745  1.00 24.10           C  
ATOM   1051  OD1 ASN A 132      18.809   8.267  22.023  1.00 30.81           O  
ATOM   1052  ND2 ASN A 132      20.048   9.975  22.795  1.00 36.60           N  
ATOM   1053  N   LYS A 133      18.281   8.160  26.301  1.00 17.12           N  
ATOM   1054  CA  LYS A 133      19.165   7.418  27.195  1.00 28.01           C  
ATOM   1055  C   LYS A 133      18.519   6.109  27.631  1.00 25.18           C  
ATOM   1056  O   LYS A 133      19.159   5.060  27.635  1.00 19.43           O  
ATOM   1057  CB  LYS A 133      19.496   8.242  28.442  1.00 32.87           C  
ATOM   1058  CG  LYS A 133      20.476   9.382  28.227  1.00 36.86           C  
ATOM   1059  CD  LYS A 133      20.925   9.941  29.570  1.00 33.68           C  
ATOM   1060  CE  LYS A 133      21.964  11.037  29.411  1.00 44.92           C  
ATOM   1061  NZ  LYS A 133      22.486  11.497  30.729  1.00 40.51           N  
ATOM   1062  N   ALA A 134      17.247   6.182  28.007  1.00 24.43           N  
ATOM   1063  CA  ALA A 134      16.514   5.005  28.448  1.00 21.31           C  
ATOM   1064  C   ALA A 134      16.481   3.929  27.362  1.00 21.34           C  
ATOM   1065  O   ALA A 134      16.856   2.783  27.604  1.00 11.58           O  
ATOM   1066  CB  ALA A 134      15.100   5.395  28.848  1.00  7.34           C  
ATOM   1067  N   LEU A 135      16.040   4.300  26.165  1.00 22.02           N  
ATOM   1068  CA  LEU A 135      15.965   3.350  25.059  1.00 24.07           C  
ATOM   1069  C   LEU A 135      17.340   2.828  24.659  1.00 21.57           C  
ATOM   1070  O   LEU A 135      17.471   1.701  24.179  1.00 23.78           O  
ATOM   1071  CB  LEU A 135      15.289   3.995  23.848  1.00 16.61           C  
ATOM   1072  CG  LEU A 135      13.817   4.379  24.019  1.00 16.89           C  
ATOM   1073  CD1 LEU A 135      13.286   4.933  22.703  1.00  9.78           C  
ATOM   1074  CD2 LEU A 135      13.008   3.164  24.444  1.00  7.31           C  
ATOM   1075  N   GLU A 136      18.364   3.649  24.857  1.00 22.82           N  
ATOM   1076  CA  GLU A 136      19.719   3.249  24.512  1.00 27.06           C  
ATOM   1077  C   GLU A 136      20.177   2.168  25.489  1.00 27.52           C  
ATOM   1078  O   GLU A 136      20.667   1.115  25.080  1.00 15.52           O  
ATOM   1079  CB  GLU A 136      20.654   4.459  24.566  1.00 24.77           C  
ATOM   1080  CG  GLU A 136      21.980   4.244  23.860  1.00 38.11           C  
ATOM   1081  CD  GLU A 136      22.848   5.487  23.859  1.00 43.00           C  
ATOM   1082  OE1 GLU A 136      22.406   6.527  23.325  1.00 49.61           O  
ATOM   1083  OE2 GLU A 136      23.974   5.422  24.395  1.00 42.49           O  
ATOM   1084  N   LEU A 137      20.011   2.432  26.781  1.00 20.91           N  
ATOM   1085  CA  LEU A 137      20.385   1.467  27.806  1.00 16.41           C  
ATOM   1086  C   LEU A 137      19.663   0.164  27.482  1.00 22.69           C  
ATOM   1087  O   LEU A 137      20.234  -0.922  27.571  1.00 26.25           O  
ATOM   1088  CB  LEU A 137      19.948   1.964  29.185  1.00 20.92           C  
ATOM   1089  CG  LEU A 137      20.061   0.987  30.359  1.00 22.93           C  
ATOM   1090  CD1 LEU A 137      21.525   0.691  30.651  1.00 22.81           C  
ATOM   1091  CD2 LEU A 137      19.385   1.583  31.584  1.00 18.08           C  
ATOM   1092  N   PHE A 138      18.399   0.297  27.097  1.00 24.86           N  
ATOM   1093  CA  PHE A 138      17.563  -0.843  26.748  1.00 20.10           C  
ATOM   1094  C   PHE A 138      18.196  -1.695  25.659  1.00 20.49           C  
ATOM   1095  O   PHE A 138      18.351  -2.907  25.810  1.00 22.75           O  
ATOM   1096  CB  PHE A 138      16.194  -0.358  26.269  1.00 16.47           C  
ATOM   1097  CG  PHE A 138      15.360  -1.436  25.640  1.00 19.94           C  
ATOM   1098  CD1 PHE A 138      14.903  -2.513  26.394  1.00 14.48           C  
ATOM   1099  CD2 PHE A 138      15.048  -1.387  24.284  1.00 16.55           C  
ATOM   1100  CE1 PHE A 138      14.148  -3.526  25.807  1.00 16.73           C  
ATOM   1101  CE2 PHE A 138      14.296  -2.393  23.688  1.00 22.97           C  
ATOM   1102  CZ  PHE A 138      13.845  -3.463  24.449  1.00 11.78           C  
ATOM   1103  N   ARG A 139      18.556  -1.051  24.555  1.00 20.67           N  
ATOM   1104  CA  ARG A 139      19.151  -1.755  23.432  1.00 20.62           C  
ATOM   1105  C   ARG A 139      20.465  -2.448  23.782  1.00 28.75           C  
ATOM   1106  O   ARG A 139      20.664  -3.615  23.437  1.00 26.47           O  
ATOM   1107  CB  ARG A 139      19.358  -0.792  22.256  1.00  2.15           C  
ATOM   1108  CG  ARG A 139      18.070  -0.120  21.787  1.00 16.85           C  
ATOM   1109  CD  ARG A 139      18.156   0.332  20.334  1.00 11.11           C  
ATOM   1110  NE  ARG A 139      19.171   1.360  20.111  1.00 15.19           N  
ATOM   1111  CZ  ARG A 139      19.054   2.632  20.481  1.00 19.36           C  
ATOM   1112  NH1 ARG A 139      17.959   3.055  21.099  1.00 13.11           N  
ATOM   1113  NH2 ARG A 139      20.035   3.488  20.228  1.00 25.48           N  
ATOM   1114  N   LYS A 140      21.356  -1.745  24.476  1.00 25.50           N  
ATOM   1115  CA  LYS A 140      22.644  -2.326  24.835  1.00 21.65           C  
ATOM   1116  C   LYS A 140      22.502  -3.465  25.838  1.00 20.55           C  
ATOM   1117  O   LYS A 140      23.277  -4.420  25.802  1.00 24.48           O  
ATOM   1118  CB  LYS A 140      23.594  -1.248  25.370  1.00 17.16           C  
ATOM   1119  CG  LYS A 140      23.329  -0.785  26.788  1.00 31.97           C  
ATOM   1120  CD  LYS A 140      24.291  -1.442  27.762  1.00 33.25           C  
ATOM   1121  CE  LYS A 140      24.271  -0.731  29.100  1.00 26.72           C  
ATOM   1122  NZ  LYS A 140      24.647   0.707  28.954  1.00 38.31           N  
ATOM   1123  N   ASP A 141      21.522  -3.373  26.732  1.00 13.33           N  
ATOM   1124  CA  ASP A 141      21.311  -4.444  27.699  1.00 15.79           C  
ATOM   1125  C   ASP A 141      20.712  -5.650  26.988  1.00 11.61           C  
ATOM   1126  O   ASP A 141      20.851  -6.781  27.449  1.00 24.67           O  
ATOM   1127  CB  ASP A 141      20.389  -3.999  28.840  1.00 19.32           C  
ATOM   1128  CG  ASP A 141      21.132  -3.241  29.930  1.00 21.76           C  
ATOM   1129  OD1 ASP A 141      22.376  -3.324  29.973  1.00 15.35           O  
ATOM   1130  OD2 ASP A 141      20.472  -2.572  30.752  1.00 15.79           O  
ATOM   1131  N   ILE A 142      20.047  -5.402  25.862  1.00 20.73           N  
ATOM   1132  CA  ILE A 142      19.448  -6.474  25.071  1.00 28.32           C  
ATOM   1133  C   ILE A 142      20.522  -7.188  24.255  1.00 29.40           C  
ATOM   1134  O   ILE A 142      20.610  -8.415  24.267  1.00 22.37           O  
ATOM   1135  CB  ILE A 142      18.366  -5.935  24.099  1.00 28.51           C  
ATOM   1136  CG1 ILE A 142      16.991  -5.998  24.763  1.00 40.59           C  
ATOM   1137  CG2 ILE A 142      18.368  -6.737  22.801  1.00 29.58           C  
ATOM   1138  CD1 ILE A 142      15.844  -5.773  23.805  1.00 56.22           C  
ATOM   1139  N   ALA A 143      21.327  -6.410  23.536  1.00 30.21           N  
ATOM   1140  CA  ALA A 143      22.397  -6.967  22.718  1.00 24.74           C  
ATOM   1141  C   ALA A 143      23.299  -7.831  23.593  1.00 30.06           C  
ATOM   1142  O   ALA A 143      23.820  -8.853  23.145  1.00 32.15           O  
ATOM   1143  CB  ALA A 143      23.204  -5.846  22.073  1.00 24.20           C  
ATOM   1144  N   ALA A 144      23.480  -7.413  24.843  1.00 25.90           N  
ATOM   1145  CA  ALA A 144      24.302  -8.162  25.784  1.00 27.32           C  
ATOM   1146  C   ALA A 144      23.712  -9.561  25.910  1.00 29.20           C  
ATOM   1147  O   ALA A 144      24.434 -10.557  25.886  1.00 28.42           O  
ATOM   1148  CB  ALA A 144      24.309  -7.470  27.142  1.00 28.68           C  
ATOM   1149  N   LYS A 145      22.390  -9.620  26.040  1.00 28.26           N  
ATOM   1150  CA  LYS A 145      21.677 -10.885  26.159  1.00 26.59           C  
ATOM   1151  C   LYS A 145      21.706 -11.599  24.808  1.00 28.93           C  
ATOM   1152  O   LYS A 145      21.661 -12.827  24.742  1.00 26.44           O  
ATOM   1153  CB  LYS A 145      20.226 -10.638  26.581  1.00 20.95           C  
ATOM   1154  CG  LYS A 145      20.060  -9.757  27.816  1.00 28.87           C  
ATOM   1155  CD  LYS A 145      19.584 -10.550  29.027  1.00 32.99           C  
ATOM   1156  CE  LYS A 145      20.715 -10.827  30.006  1.00 30.75           C  
ATOM   1157  NZ  LYS A 145      21.826 -11.595  29.385  1.00 39.53           N  
ATOM   1158  N   TYR A 146      21.776 -10.823  23.731  1.00 24.79           N  
ATOM   1159  CA  TYR A 146      21.829 -11.392  22.389  1.00 31.18           C  
ATOM   1160  C   TYR A 146      23.085 -12.243  22.232  1.00 32.31           C  
ATOM   1161  O   TYR A 146      23.003 -13.414  21.867  1.00 28.85           O  
ATOM   1162  CB  TYR A 146      21.810 -10.278  21.335  1.00 20.78           C  
ATOM   1163  CG  TYR A 146      20.460 -10.080  20.671  1.00 28.25           C  
ATOM   1164  CD1 TYR A 146      19.278 -10.154  21.409  1.00 31.63           C  
ATOM   1165  CD2 TYR A 146      20.366  -9.820  19.305  1.00 20.96           C  
ATOM   1166  CE1 TYR A 146      18.037  -9.979  20.803  1.00 19.75           C  
ATOM   1167  CE2 TYR A 146      19.128  -9.641  18.687  1.00 23.50           C  
ATOM   1168  CZ  TYR A 146      17.969  -9.724  19.443  1.00 27.38           C  
ATOM   1169  OH  TYR A 146      16.743  -9.552  18.846  1.00 28.87           O  
ATOM   1170  N   LYS A 147      24.244 -11.659  22.518  1.00 36.34           N  
ATOM   1171  CA  LYS A 147      25.499 -12.392  22.404  1.00 43.27           C  
ATOM   1172  C   LYS A 147      25.586 -13.543  23.398  1.00 32.77           C  
ATOM   1173  O   LYS A 147      26.265 -14.534  23.139  1.00 39.35           O  
ATOM   1174  CB  LYS A 147      26.698 -11.463  22.607  1.00 46.97           C  
ATOM   1175  CG  LYS A 147      27.387 -11.036  21.316  1.00 51.11           C  
ATOM   1176  CD  LYS A 147      28.821 -10.608  21.597  1.00 56.16           C  
ATOM   1177  CE  LYS A 147      29.659 -11.791  22.073  1.00 55.60           C  
ATOM   1178  NZ  LYS A 147      30.823 -11.360  22.899  1.00 51.03           N  
ATOM   1179  N   GLU A 148      24.910 -13.411  24.537  1.00 28.66           N  
ATOM   1180  CA  GLU A 148      24.932 -14.472  25.535  1.00 25.71           C  
ATOM   1181  C   GLU A 148      24.302 -15.710  24.918  1.00 29.73           C  
ATOM   1182  O   GLU A 148      24.848 -16.808  25.015  1.00 32.64           O  
ATOM   1183  CB  GLU A 148      24.167 -14.058  26.795  1.00 32.28           C  
ATOM   1184  CG  GLU A 148      24.357 -15.029  27.954  1.00 49.27           C  
ATOM   1185  CD  GLU A 148      23.992 -14.427  29.296  1.00 60.29           C  
ATOM   1186  OE1 GLU A 148      24.528 -13.348  29.627  1.00 60.44           O  
ATOM   1187  OE2 GLU A 148      23.181 -15.035  30.026  1.00 66.73           O  
ATOM   1188  N   LEU A 149      23.151 -15.528  24.281  1.00 31.37           N  
ATOM   1189  CA  LEU A 149      22.477 -16.633  23.613  1.00 41.32           C  
ATOM   1190  C   LEU A 149      23.297 -16.920  22.365  1.00 39.87           C  
ATOM   1191  O   LEU A 149      22.953 -17.783  21.557  1.00 23.23           O  
ATOM   1192  CB  LEU A 149      21.053 -16.244  23.210  1.00 40.19           C  
ATOM   1193  CG  LEU A 149      20.064 -15.902  24.325  1.00 47.31           C  
ATOM   1194  CD1 LEU A 149      18.721 -15.532  23.715  1.00 36.37           C  
ATOM   1195  CD2 LEU A 149      19.916 -17.089  25.262  1.00 45.18           C  
ATOM   1196  N   GLY A 150      24.386 -16.172  22.216  1.00 37.06           N  
ATOM   1197  CA  GLY A 150      25.258 -16.342  21.072  1.00 49.16           C  
ATOM   1198  C   GLY A 150      24.617 -15.855  19.792  1.00 54.16           C  
ATOM   1199  O   GLY A 150      25.011 -16.274  18.699  1.00 56.45           O  
ATOM   1200  N   TYR A 151      23.632 -14.968  19.918  1.00 58.94           N  
ATOM   1201  CA  TYR A 151      22.951 -14.454  18.742  1.00 58.37           C  
ATOM   1202  C   TYR A 151      23.912 -13.717  17.841  1.00 60.39           C  
ATOM   1203  O   TYR A 151      24.321 -12.587  18.124  1.00 52.84           O  
ATOM   1204  CB  TYR A 151      21.806 -13.505  19.098  1.00 59.31           C  
ATOM   1205  CG  TYR A 151      21.022 -13.098  17.868  1.00 66.40           C  
ATOM   1206  CD1 TYR A 151      20.010 -13.913  17.366  1.00 67.06           C  
ATOM   1207  CD2 TYR A 151      21.326 -11.925  17.174  1.00 72.31           C  
ATOM   1208  CE1 TYR A 151      19.321 -13.578  16.208  1.00 69.53           C  
ATOM   1209  CE2 TYR A 151      20.641 -11.580  16.011  1.00 72.43           C  
ATOM   1210  CZ  TYR A 151      19.641 -12.414  15.536  1.00 71.10           C  
ATOM   1211  OH  TYR A 151      18.967 -12.090  14.381  1.00 65.35           O  
ATOM   1212  N   GLN A 152      24.285 -14.384  16.762  1.00 66.27           N  
ATOM   1213  CA  GLN A 152      25.164 -13.790  15.786  1.00 67.06           C  
ATOM   1214  C   GLN A 152      24.590 -13.953  14.393  1.00 69.41           C  
ATOM   1215  O   GLN A 152      24.545 -15.054  13.833  1.00 65.47           O  
ATOM   1216  CB  GLN A 152      26.560 -14.390  15.833  1.00 66.32           C  
ATOM   1217  CG  GLN A 152      27.463 -13.840  14.717  1.00 70.82           C  
ATOM   1218  CD  GLN A 152      27.416 -12.314  14.596  1.00 76.64           C  
ATOM   1219  OE1 GLN A 152      26.365 -11.706  14.771  1.00 84.65           O  
ATOM   1220  NE2 GLN A 152      28.550 -11.689  14.290  1.00 72.59           N  
ATOM   1221  N   GLY A 153      24.146 -12.830  13.848  1.00 70.50           N  
ATOM   1222  CA  GLY A 153      23.579 -12.824  12.518  1.00 69.68           C  
ATOM   1223  C   GLY A 153      24.647 -12.661  11.452  1.00 71.83           C  
ATOM   1224  O   GLY A 153      25.853 -12.714  11.725  1.00 71.57           O  
TER    1225      GLY A 153                                                      
ATOM   1226  N   VAL B   1      37.439  26.884  19.076  1.00 42.30           N  
ATOM   1227  CA  VAL B   1      37.245  27.864  20.138  1.00 51.67           C  
ATOM   1228  C   VAL B   1      37.551  29.261  19.600  1.00 50.18           C  
ATOM   1229  O   VAL B   1      38.000  29.404  18.461  1.00 53.43           O  
ATOM   1230  CB  VAL B   1      38.152  27.550  21.351  1.00 48.64           C  
ATOM   1231  CG1 VAL B   1      37.923  28.568  22.457  1.00 50.94           C  
ATOM   1232  CG2 VAL B   1      37.869  26.142  21.861  1.00 59.65           C  
ATOM   1233  N   LEU B   2      37.298  30.287  20.408  1.00 41.44           N  
ATOM   1234  CA  LEU B   2      37.534  31.660  19.977  1.00 35.29           C  
ATOM   1235  C   LEU B   2      37.977  32.605  21.093  1.00 30.93           C  
ATOM   1236  O   LEU B   2      37.728  32.373  22.281  1.00 34.67           O  
ATOM   1237  CB  LEU B   2      36.267  32.235  19.326  1.00 29.52           C  
ATOM   1238  CG  LEU B   2      35.727  31.645  18.019  1.00 30.38           C  
ATOM   1239  CD1 LEU B   2      35.036  30.318  18.277  1.00 11.46           C  
ATOM   1240  CD2 LEU B   2      34.758  32.635  17.387  1.00 20.48           C  
ATOM   1241  N   SER B   3      38.631  33.684  20.680  1.00 26.65           N  
ATOM   1242  CA  SER B   3      39.109  34.713  21.592  1.00 35.71           C  
ATOM   1243  C   SER B   3      38.026  35.771  21.705  1.00 33.22           C  
ATOM   1244  O   SER B   3      37.050  35.751  20.956  1.00 29.90           O  
ATOM   1245  CB  SER B   3      40.377  35.364  21.039  1.00 33.87           C  
ATOM   1246  OG  SER B   3      40.097  36.074  19.847  1.00 30.90           O  
ATOM   1247  N   GLU B   4      38.202  36.691  22.648  1.00 23.09           N  
ATOM   1248  CA  GLU B   4      37.248  37.777  22.835  1.00 30.43           C  
ATOM   1249  C   GLU B   4      37.296  38.642  21.579  1.00 35.73           C  
ATOM   1250  O   GLU B   4      36.267  39.123  21.107  1.00 29.03           O  
ATOM   1251  CB  GLU B   4      37.619  38.612  24.066  1.00 26.92           C  
ATOM   1252  CG  GLU B   4      36.777  39.876  24.297  1.00 43.92           C  
ATOM   1253  CD  GLU B   4      35.329  39.588  24.669  1.00 58.06           C  
ATOM   1254  OE1 GLU B   4      35.048  38.479  25.166  1.00 65.20           O  
ATOM   1255  OE2 GLU B   4      34.470  40.476  24.476  1.00 58.39           O  
ATOM   1256  N   GLY B   5      38.501  38.820  21.039  1.00 31.46           N  
ATOM   1257  CA  GLY B   5      38.681  39.619  19.837  1.00 37.48           C  
ATOM   1258  C   GLY B   5      37.973  39.037  18.629  1.00 33.24           C  
ATOM   1259  O   GLY B   5      37.272  39.748  17.908  1.00 27.74           O  
ATOM   1260  N   GLU B   6      38.162  37.744  18.394  1.00 33.57           N  
ATOM   1261  CA  GLU B   6      37.510  37.077  17.275  1.00 38.08           C  
ATOM   1262  C   GLU B   6      36.002  37.141  17.501  1.00 44.41           C  
ATOM   1263  O   GLU B   6      35.219  37.180  16.552  1.00 40.53           O  
ATOM   1264  CB  GLU B   6      37.970  35.621  17.191  1.00 35.03           C  
ATOM   1265  CG  GLU B   6      39.461  35.463  16.937  1.00 28.03           C  
ATOM   1266  CD  GLU B   6      39.924  34.026  17.060  1.00 27.04           C  
ATOM   1267  OE1 GLU B   6      39.830  33.466  18.172  1.00 36.03           O  
ATOM   1268  OE2 GLU B   6      40.380  33.458  16.047  1.00 36.79           O  
ATOM   1269  N   TRP B   7      35.609  37.158  18.772  1.00 45.65           N  
ATOM   1270  CA  TRP B   7      34.204  37.231  19.155  1.00 44.97           C  
ATOM   1271  C   TRP B   7      33.665  38.647  19.000  1.00 45.92           C  
ATOM   1272  O   TRP B   7      32.456  38.850  18.891  1.00 48.81           O  
ATOM   1273  CB  TRP B   7      34.020  36.767  20.604  1.00 43.19           C  
ATOM   1274  CG  TRP B   7      33.836  35.285  20.748  1.00 41.61           C  
ATOM   1275  CD1 TRP B   7      34.611  34.427  21.472  1.00 41.63           C  
ATOM   1276  CD2 TRP B   7      32.796  34.492  20.165  1.00 29.98           C  
ATOM   1277  NE1 TRP B   7      34.119  33.148  21.379  1.00 32.73           N  
ATOM   1278  CE2 TRP B   7      33.004  33.159  20.582  1.00 39.83           C  
ATOM   1279  CE3 TRP B   7      31.706  34.778  19.332  1.00 35.18           C  
ATOM   1280  CZ2 TRP B   7      32.162  32.110  20.194  1.00 38.86           C  
ATOM   1281  CZ3 TRP B   7      30.868  33.735  18.945  1.00 41.67           C  
ATOM   1282  CH2 TRP B   7      31.103  32.417  19.378  1.00 37.50           C  
ATOM   1283  N   GLN B   8      34.563  39.627  19.000  1.00 43.47           N  
ATOM   1284  CA  GLN B   8      34.157  41.016  18.841  1.00 45.85           C  
ATOM   1285  C   GLN B   8      33.974  41.321  17.362  1.00 44.55           C  
ATOM   1286  O   GLN B   8      33.073  42.068  16.981  1.00 45.50           O  
ATOM   1287  CB  GLN B   8      35.204  41.960  19.435  1.00 55.73           C  
ATOM   1288  CG  GLN B   8      35.355  41.860  20.942  1.00 55.86           C  
ATOM   1289  CD  GLN B   8      36.336  42.876  21.491  1.00 63.63           C  
ATOM   1290  OE1 GLN B   8      37.486  42.944  21.054  1.00 59.93           O  
ATOM   1291  NE2 GLN B   8      35.886  43.674  22.453  1.00 62.03           N  
ATOM   1292  N   LEU B   9      34.832  40.739  16.531  1.00 41.85           N  
ATOM   1293  CA  LEU B   9      34.744  40.950  15.095  1.00 46.92           C  
ATOM   1294  C   LEU B   9      33.541  40.203  14.530  1.00 51.50           C  
ATOM   1295  O   LEU B   9      32.771  40.761  13.747  1.00 44.57           O  
ATOM   1296  CB  LEU B   9      36.026  40.484  14.401  1.00 41.45           C  
ATOM   1297  CG  LEU B   9      37.312  41.240  14.752  1.00 40.14           C  
ATOM   1298  CD1 LEU B   9      38.370  40.945  13.694  1.00 38.35           C  
ATOM   1299  CD2 LEU B   9      37.044  42.738  14.812  1.00 35.29           C  
ATOM   1300  N   VAL B  10      33.380  38.944  14.932  1.00 46.67           N  
ATOM   1301  CA  VAL B  10      32.257  38.135  14.472  1.00 42.51           C  
ATOM   1302  C   VAL B  10      30.948  38.879  14.714  1.00 41.22           C  
ATOM   1303  O   VAL B  10      30.073  38.917  13.849  1.00 35.19           O  
ATOM   1304  CB  VAL B  10      32.196  36.778  15.212  1.00 42.38           C  
ATOM   1305  CG1 VAL B  10      30.866  36.088  14.930  1.00 37.93           C  
ATOM   1306  CG2 VAL B  10      33.344  35.891  14.764  1.00 37.38           C  
ATOM   1307  N   LEU B  11      30.820  39.473  15.894  1.00 38.99           N  
ATOM   1308  CA  LEU B  11      29.616  40.215  16.239  1.00 45.26           C  
ATOM   1309  C   LEU B  11      29.605  41.569  15.538  1.00 50.53           C  
ATOM   1310  O   LEU B  11      28.543  42.153  15.320  1.00 54.97           O  
ATOM   1311  CB  LEU B  11      29.523  40.402  17.754  1.00 37.76           C  
ATOM   1312  CG  LEU B  11      29.407  39.101  18.552  1.00 30.29           C  
ATOM   1313  CD1 LEU B  11      29.327  39.409  20.036  1.00 34.31           C  
ATOM   1314  CD2 LEU B  11      28.177  38.333  18.100  1.00 26.49           C  
ATOM   1315  N   HIS B  12      30.787  42.064  15.186  1.00 51.18           N  
ATOM   1316  CA  HIS B  12      30.894  43.337  14.492  1.00 51.97           C  
ATOM   1317  C   HIS B  12      30.306  43.165  13.097  1.00 50.33           C  
ATOM   1318  O   HIS B  12      29.493  43.973  12.644  1.00 45.54           O  
ATOM   1319  CB  HIS B  12      32.358  43.771  14.388  1.00 54.80           C  
ATOM   1320  CG  HIS B  12      32.547  45.087  13.695  1.00 61.92           C  
ATOM   1321  ND1 HIS B  12      31.997  46.260  14.165  1.00 60.49           N  
ATOM   1322  CD2 HIS B  12      33.216  45.413  12.563  1.00 62.18           C  
ATOM   1323  CE1 HIS B  12      32.319  47.252  13.354  1.00 63.29           C  
ATOM   1324  NE2 HIS B  12      33.058  46.765  12.374  1.00 57.40           N  
ATOM   1325  N   VAL B  13      30.721  42.099  12.421  1.00 52.59           N  
ATOM   1326  CA  VAL B  13      30.235  41.808  11.079  1.00 53.35           C  
ATOM   1327  C   VAL B  13      28.762  41.432  11.118  1.00 50.79           C  
ATOM   1328  O   VAL B  13      28.018  41.699  10.173  1.00 51.38           O  
ATOM   1329  CB  VAL B  13      31.049  40.658  10.423  1.00 48.75           C  
ATOM   1330  CG1 VAL B  13      31.353  39.582  11.447  1.00 57.23           C  
ATOM   1331  CG2 VAL B  13      30.276  40.063   9.254  1.00 47.66           C  
ATOM   1332  N   TRP B  14      28.342  40.818  12.218  1.00 45.56           N  
ATOM   1333  CA  TRP B  14      26.953  40.417  12.353  1.00 41.81           C  
ATOM   1334  C   TRP B  14      26.069  41.604  12.699  1.00 38.46           C  
ATOM   1335  O   TRP B  14      24.851  41.546  12.541  1.00 40.03           O  
ATOM   1336  CB  TRP B  14      26.801  39.328  13.416  1.00 33.83           C  
ATOM   1337  CG  TRP B  14      25.465  38.666  13.340  1.00 24.66           C  
ATOM   1338  CD1 TRP B  14      24.341  38.990  14.045  1.00 13.83           C  
ATOM   1339  CD2 TRP B  14      25.087  37.617  12.443  1.00 18.51           C  
ATOM   1340  NE1 TRP B  14      23.286  38.209  13.640  1.00 18.32           N  
ATOM   1341  CE2 TRP B  14      23.716  37.357  12.656  1.00 19.42           C  
ATOM   1342  CE3 TRP B  14      25.774  36.873  11.475  1.00 22.05           C  
ATOM   1343  CZ2 TRP B  14      23.016  36.381  11.936  1.00 27.01           C  
ATOM   1344  CZ3 TRP B  14      25.079  35.903  10.758  1.00 19.55           C  
ATOM   1345  CH2 TRP B  14      23.713  35.666  10.994  1.00 18.91           C  
ATOM   1346  N   ALA B  15      26.690  42.680  13.173  1.00 35.05           N  
ATOM   1347  CA  ALA B  15      25.957  43.890  13.526  1.00 42.13           C  
ATOM   1348  C   ALA B  15      25.419  44.519  12.245  1.00 46.19           C  
ATOM   1349  O   ALA B  15      24.305  45.043  12.213  1.00 45.81           O  
ATOM   1350  CB  ALA B  15      26.876  44.871  14.244  1.00 52.27           C  
ATOM   1351  N   LYS B  16      26.224  44.457  11.189  1.00 46.02           N  
ATOM   1352  CA  LYS B  16      25.840  45.007   9.895  1.00 53.64           C  
ATOM   1353  C   LYS B  16      24.791  44.129   9.224  1.00 51.91           C  
ATOM   1354  O   LYS B  16      24.105  44.561   8.297  1.00 52.29           O  
ATOM   1355  CB  LYS B  16      27.073  45.142   9.000  1.00 54.36           C  
ATOM   1356  CG  LYS B  16      27.997  46.271   9.419  1.00 51.32           C  
ATOM   1357  CD  LYS B  16      29.444  45.824   9.473  1.00 57.89           C  
ATOM   1358  CE  LYS B  16      30.355  46.977   9.864  1.00 62.55           C  
ATOM   1359  NZ  LYS B  16      29.959  47.581  11.167  1.00 59.03           N  
ATOM   1360  N   VAL B  17      24.671  42.892   9.696  1.00 44.02           N  
ATOM   1361  CA  VAL B  17      23.688  41.964   9.156  1.00 37.90           C  
ATOM   1362  C   VAL B  17      22.318  42.364   9.683  1.00 37.58           C  
ATOM   1363  O   VAL B  17      21.317  42.291   8.971  1.00 29.56           O  
ATOM   1364  CB  VAL B  17      23.983  40.515   9.599  1.00 40.35           C  
ATOM   1365  CG1 VAL B  17      22.871  39.589   9.128  1.00 41.55           C  
ATOM   1366  CG2 VAL B  17      25.320  40.062   9.038  1.00 40.79           C  
ATOM   1367  N   GLU B  18      22.289  42.794  10.940  1.00 40.49           N  
ATOM   1368  CA  GLU B  18      21.052  43.205  11.586  1.00 45.14           C  
ATOM   1369  C   GLU B  18      20.705  44.652  11.263  1.00 46.28           C  
ATOM   1370  O   GLU B  18      19.844  45.258  11.903  1.00 52.73           O  
ATOM   1371  CB  GLU B  18      21.166  43.002  13.097  1.00 51.63           C  
ATOM   1372  CG  GLU B  18      21.472  41.560  13.477  1.00 42.70           C  
ATOM   1373  CD  GLU B  18      21.674  41.374  14.967  1.00 47.43           C  
ATOM   1374  OE1 GLU B  18      22.543  42.067  15.540  1.00 32.09           O  
ATOM   1375  OE2 GLU B  18      20.968  40.530  15.561  1.00 30.85           O  
ATOM   1376  N   ALA B  19      21.395  45.204  10.271  1.00 47.71           N  
ATOM   1377  CA  ALA B  19      21.137  46.565   9.820  1.00 43.84           C  
ATOM   1378  C   ALA B  19      20.106  46.371   8.719  1.00 41.39           C  
ATOM   1379  O   ALA B  19      19.225  47.204   8.502  1.00 37.81           O  
ATOM   1380  CB  ALA B  19      22.406  47.188   9.258  1.00 37.96           C  
ATOM   1381  N   ASP B  20      20.239  45.239   8.035  1.00 38.07           N  
ATOM   1382  CA  ASP B  20      19.343  44.846   6.960  1.00 37.42           C  
ATOM   1383  C   ASP B  20      19.215  43.330   7.026  1.00 34.31           C  
ATOM   1384  O   ASP B  20      19.796  42.609   6.216  1.00 26.47           O  
ATOM   1385  CB  ASP B  20      19.909  45.266   5.600  1.00 53.59           C  
ATOM   1386  CG  ASP B  20      18.955  44.969   4.457  1.00 59.17           C  
ATOM   1387  OD1 ASP B  20      17.791  45.418   4.527  1.00 52.38           O  
ATOM   1388  OD2 ASP B  20      19.368  44.291   3.490  1.00 47.99           O  
ATOM   1389  N   VAL B  21      18.463  42.853   8.014  1.00 32.50           N  
ATOM   1390  CA  VAL B  21      18.257  41.424   8.199  1.00 26.75           C  
ATOM   1391  C   VAL B  21      17.538  40.806   7.009  1.00 23.50           C  
ATOM   1392  O   VAL B  21      18.041  39.869   6.390  1.00 21.05           O  
ATOM   1393  CB  VAL B  21      17.445  41.137   9.483  1.00 29.39           C  
ATOM   1394  CG1 VAL B  21      18.366  41.142  10.690  1.00 21.55           C  
ATOM   1395  CG2 VAL B  21      16.352  42.185   9.654  1.00 25.57           C  
ATOM   1396  N   ALA B  22      16.363  41.336   6.692  1.00 28.08           N  
ATOM   1397  CA  ALA B  22      15.578  40.840   5.569  1.00 29.61           C  
ATOM   1398  C   ALA B  22      16.460  40.650   4.335  1.00 28.51           C  
ATOM   1399  O   ALA B  22      16.556  39.547   3.793  1.00 18.49           O  
ATOM   1400  CB  ALA B  22      14.445  41.810   5.263  1.00 23.84           C  
ATOM   1401  N   GLY B  23      17.104  41.731   3.900  1.00 24.77           N  
ATOM   1402  CA  GLY B  23      17.972  41.663   2.736  1.00 27.41           C  
ATOM   1403  C   GLY B  23      19.009  40.559   2.834  1.00 33.81           C  
ATOM   1404  O   GLY B  23      19.223  39.809   1.878  1.00 30.16           O  
ATOM   1405  N   HIS B  24      19.659  40.459   3.989  1.00 31.13           N  
ATOM   1406  CA  HIS B  24      20.673  39.434   4.206  1.00 17.80           C  
ATOM   1407  C   HIS B  24      20.051  38.047   4.278  1.00 16.49           C  
ATOM   1408  O   HIS B  24      20.630  37.075   3.797  1.00 16.64           O  
ATOM   1409  CB  HIS B  24      21.447  39.706   5.498  1.00 25.77           C  
ATOM   1410  CG  HIS B  24      22.466  40.794   5.376  1.00 31.17           C  
ATOM   1411  ND1 HIS B  24      22.128  42.118   5.198  1.00 23.51           N  
ATOM   1412  CD2 HIS B  24      23.819  40.752   5.401  1.00 28.93           C  
ATOM   1413  CE1 HIS B  24      23.228  42.845   5.119  1.00 26.35           C  
ATOM   1414  NE2 HIS B  24      24.268  42.040   5.239  1.00 28.61           N  
ATOM   1415  N   GLY B  25      18.873  37.958   4.889  1.00 19.19           N  
ATOM   1416  CA  GLY B  25      18.200  36.678   5.005  1.00 26.42           C  
ATOM   1417  C   GLY B  25      17.867  36.108   3.641  1.00 25.41           C  
ATOM   1418  O   GLY B  25      18.129  34.936   3.361  1.00 24.67           O  
ATOM   1419  N   GLN B  26      17.289  36.944   2.787  1.00 22.48           N  
ATOM   1420  CA  GLN B  26      16.919  36.530   1.441  1.00 29.05           C  
ATOM   1421  C   GLN B  26      18.132  35.980   0.698  1.00 33.55           C  
ATOM   1422  O   GLN B  26      18.129  34.833   0.246  1.00 32.81           O  
ATOM   1423  CB  GLN B  26      16.338  37.718   0.673  1.00 20.83           C  
ATOM   1424  CG  GLN B  26      15.082  38.304   1.298  1.00 18.93           C  
ATOM   1425  CD  GLN B  26      14.637  39.584   0.618  1.00 33.84           C  
ATOM   1426  OE1 GLN B  26      15.351  40.586   0.633  1.00 36.52           O  
ATOM   1427  NE2 GLN B  26      13.451  39.558   0.018  1.00 29.10           N  
ATOM   1428  N   ASP B  27      19.167  36.807   0.585  1.00 33.18           N  
ATOM   1429  CA  ASP B  27      20.394  36.429  -0.107  1.00 27.28           C  
ATOM   1430  C   ASP B  27      20.930  35.076   0.344  1.00 32.65           C  
ATOM   1431  O   ASP B  27      21.274  34.229  -0.482  1.00 26.43           O  
ATOM   1432  CB  ASP B  27      21.473  37.496   0.102  1.00 21.46           C  
ATOM   1433  CG  ASP B  27      21.034  38.869  -0.367  1.00 35.12           C  
ATOM   1434  OD1 ASP B  27      20.026  38.955  -1.099  1.00 35.65           O  
ATOM   1435  OD2 ASP B  27      21.704  39.862  -0.012  1.00 36.18           O  
ATOM   1436  N   ILE B  28      21.001  34.878   1.657  1.00 30.03           N  
ATOM   1437  CA  ILE B  28      21.503  33.628   2.214  1.00 23.93           C  
ATOM   1438  C   ILE B  28      20.666  32.431   1.778  1.00 26.40           C  
ATOM   1439  O   ILE B  28      21.198  31.456   1.250  1.00 25.03           O  
ATOM   1440  CB  ILE B  28      21.540  33.691   3.754  1.00 22.66           C  
ATOM   1441  CG1 ILE B  28      22.497  34.802   4.189  1.00 21.76           C  
ATOM   1442  CG2 ILE B  28      21.973  32.344   4.332  1.00 11.76           C  
ATOM   1443  CD1 ILE B  28      22.526  35.044   5.671  1.00 29.47           C  
ATOM   1444  N   LEU B  29      19.357  32.508   1.993  1.00 27.96           N  
ATOM   1445  CA  LEU B  29      18.470  31.416   1.611  1.00 27.21           C  
ATOM   1446  C   LEU B  29      18.494  31.169   0.107  1.00 26.71           C  
ATOM   1447  O   LEU B  29      18.532  30.022  -0.338  1.00 41.03           O  
ATOM   1448  CB  LEU B  29      17.041  31.706   2.076  1.00 21.99           C  
ATOM   1449  CG  LEU B  29      16.833  31.655   3.593  1.00 26.60           C  
ATOM   1450  CD1 LEU B  29      15.418  32.085   3.944  1.00 31.56           C  
ATOM   1451  CD2 LEU B  29      17.103  30.243   4.090  1.00 40.41           C  
ATOM   1452  N   ILE B  30      18.476  32.243  -0.676  1.00 28.64           N  
ATOM   1453  CA  ILE B  30      18.506  32.115  -2.128  1.00 33.14           C  
ATOM   1454  C   ILE B  30      19.764  31.369  -2.566  1.00 30.72           C  
ATOM   1455  O   ILE B  30      19.717  30.534  -3.470  1.00 32.86           O  
ATOM   1456  CB  ILE B  30      18.461  33.502  -2.809  1.00 33.64           C  
ATOM   1457  CG1 ILE B  30      17.080  34.130  -2.596  1.00 30.01           C  
ATOM   1458  CG2 ILE B  30      18.785  33.371  -4.295  1.00 23.58           C  
ATOM   1459  CD1 ILE B  30      16.949  35.545  -3.125  1.00 19.00           C  
ATOM   1460  N   ARG B  31      20.883  31.670  -1.917  1.00 33.82           N  
ATOM   1461  CA  ARG B  31      22.148  31.017  -2.230  1.00 29.08           C  
ATOM   1462  C   ARG B  31      22.061  29.539  -1.869  1.00 36.16           C  
ATOM   1463  O   ARG B  31      22.516  28.675  -2.617  1.00 47.42           O  
ATOM   1464  CB  ARG B  31      23.288  31.671  -1.445  1.00 33.09           C  
ATOM   1465  CG  ARG B  31      24.613  30.922  -1.521  1.00 35.98           C  
ATOM   1466  CD  ARG B  31      25.161  30.881  -2.939  1.00 35.40           C  
ATOM   1467  NE  ARG B  31      26.412  30.132  -3.011  1.00 44.51           N  
ATOM   1468  CZ  ARG B  31      27.170  30.038  -4.098  1.00 48.20           C  
ATOM   1469  NH1 ARG B  31      26.807  30.650  -5.217  1.00 46.34           N  
ATOM   1470  NH2 ARG B  31      28.291  29.329  -4.066  1.00 44.96           N  
ATOM   1471  N   LEU B  32      21.470  29.261  -0.712  1.00 33.68           N  
ATOM   1472  CA  LEU B  32      21.310  27.897  -0.225  1.00 28.23           C  
ATOM   1473  C   LEU B  32      20.530  27.032  -1.204  1.00 36.98           C  
ATOM   1474  O   LEU B  32      20.967  25.941  -1.573  1.00 36.34           O  
ATOM   1475  CB  LEU B  32      20.585  27.909   1.120  1.00 25.80           C  
ATOM   1476  CG  LEU B  32      20.061  26.565   1.634  1.00 30.59           C  
ATOM   1477  CD1 LEU B  32      21.230  25.646   1.956  1.00 34.68           C  
ATOM   1478  CD2 LEU B  32      19.200  26.788   2.867  1.00 29.54           C  
ATOM   1479  N   PHE B  33      19.367  27.524  -1.616  1.00 33.60           N  
ATOM   1480  CA  PHE B  33      18.510  26.792  -2.538  1.00 42.10           C  
ATOM   1481  C   PHE B  33      19.132  26.644  -3.924  1.00 37.11           C  
ATOM   1482  O   PHE B  33      18.957  25.618  -4.586  1.00 27.39           O  
ATOM   1483  CB  PHE B  33      17.151  27.487  -2.644  1.00 43.90           C  
ATOM   1484  CG  PHE B  33      16.481  27.710  -1.315  1.00 46.65           C  
ATOM   1485  CD1 PHE B  33      16.454  26.698  -0.359  1.00 39.19           C  
ATOM   1486  CD2 PHE B  33      15.857  28.920  -1.027  1.00 41.18           C  
ATOM   1487  CE1 PHE B  33      15.814  26.887   0.864  1.00 48.85           C  
ATOM   1488  CE2 PHE B  33      15.214  29.120   0.194  1.00 24.89           C  
ATOM   1489  CZ  PHE B  33      15.192  28.102   1.141  1.00 40.67           C  
ATOM   1490  N   LYS B  34      19.858  27.670  -4.356  1.00 32.56           N  
ATOM   1491  CA  LYS B  34      20.516  27.655  -5.656  1.00 39.02           C  
ATOM   1492  C   LYS B  34      21.696  26.695  -5.648  1.00 41.22           C  
ATOM   1493  O   LYS B  34      21.912  25.945  -6.600  1.00 40.84           O  
ATOM   1494  CB  LYS B  34      21.002  29.061  -6.015  1.00 36.24           C  
ATOM   1495  CG  LYS B  34      22.121  29.086  -7.043  1.00 40.94           C  
ATOM   1496  CD  LYS B  34      21.705  29.792  -8.319  1.00 53.18           C  
ATOM   1497  CE  LYS B  34      22.816  29.723  -9.359  1.00 62.78           C  
ATOM   1498  NZ  LYS B  34      22.417  30.333 -10.659  1.00 74.57           N  
ATOM   1499  N   SER B  35      22.461  26.729  -4.564  1.00 34.51           N  
ATOM   1500  CA  SER B  35      23.625  25.871  -4.427  1.00 40.93           C  
ATOM   1501  C   SER B  35      23.234  24.482  -3.939  1.00 45.02           C  
ATOM   1502  O   SER B  35      24.015  23.537  -4.052  1.00 36.86           O  
ATOM   1503  CB  SER B  35      24.625  26.493  -3.450  1.00 40.02           C  
ATOM   1504  OG  SER B  35      25.041  27.771  -3.895  1.00 33.76           O  
ATOM   1505  N   HIS B  36      22.025  24.362  -3.400  1.00 43.80           N  
ATOM   1506  CA  HIS B  36      21.535  23.087  -2.884  1.00 51.50           C  
ATOM   1507  C   HIS B  36      20.011  23.018  -2.993  1.00 56.49           C  
ATOM   1508  O   HIS B  36      19.301  23.200  -2.005  1.00 50.64           O  
ATOM   1509  CB  HIS B  36      21.962  22.925  -1.421  1.00 55.18           C  
ATOM   1510  CG  HIS B  36      23.431  23.117  -1.200  1.00 57.20           C  
ATOM   1511  ND1 HIS B  36      24.377  22.242  -1.686  1.00 61.42           N  
ATOM   1512  CD2 HIS B  36      24.117  24.111  -0.587  1.00 63.88           C  
ATOM   1513  CE1 HIS B  36      25.584  22.688  -1.385  1.00 63.98           C  
ATOM   1514  NE2 HIS B  36      25.454  23.821  -0.718  1.00 67.22           N  
ATOM   1515  N   PRO B  37      19.491  22.755  -4.203  1.00 55.74           N  
ATOM   1516  CA  PRO B  37      18.049  22.660  -4.455  1.00 57.54           C  
ATOM   1517  C   PRO B  37      17.346  21.711  -3.490  1.00 55.05           C  
ATOM   1518  O   PRO B  37      16.185  21.914  -3.132  1.00 49.94           O  
ATOM   1519  CB  PRO B  37      17.987  22.162  -5.896  1.00 56.11           C  
ATOM   1520  CG  PRO B  37      19.205  22.769  -6.506  1.00 55.16           C  
ATOM   1521  CD  PRO B  37      20.251  22.526  -5.444  1.00 58.33           C  
ATOM   1522  N   GLU B  38      18.065  20.674  -3.075  1.00 49.10           N  
ATOM   1523  CA  GLU B  38      17.533  19.675  -2.160  1.00 51.47           C  
ATOM   1524  C   GLU B  38      17.070  20.270  -0.831  1.00 56.37           C  
ATOM   1525  O   GLU B  38      16.481  19.569  -0.005  1.00 57.82           O  
ATOM   1526  CB  GLU B  38      18.592  18.604  -1.903  1.00 45.10           C  
ATOM   1527  CG  GLU B  38      19.909  19.159  -1.383  1.00 52.42           C  
ATOM   1528  CD  GLU B  38      20.912  18.068  -1.064  1.00 51.47           C  
ATOM   1529  OE1 GLU B  38      20.478  16.986  -0.616  1.00 53.89           O  
ATOM   1530  OE2 GLU B  38      22.129  18.290  -1.249  1.00 55.05           O  
ATOM   1531  N   THR B  39      17.335  21.557  -0.625  1.00 51.66           N  
ATOM   1532  CA  THR B  39      16.935  22.221   0.611  1.00 45.43           C  
ATOM   1533  C   THR B  39      15.561  22.878   0.516  1.00 47.32           C  
ATOM   1534  O   THR B  39      14.953  23.198   1.537  1.00 46.98           O  
ATOM   1535  CB  THR B  39      17.962  23.285   1.046  1.00 40.62           C  
ATOM   1536  OG1 THR B  39      18.211  24.185  -0.038  1.00 30.65           O  
ATOM   1537  CG2 THR B  39      19.267  22.625   1.472  1.00 41.59           C  
ATOM   1538  N   LEU B  40      15.076  23.094  -0.702  1.00 48.68           N  
ATOM   1539  CA  LEU B  40      13.755  23.684  -0.883  1.00 52.84           C  
ATOM   1540  C   LEU B  40      12.722  22.579  -0.775  1.00 54.02           C  
ATOM   1541  O   LEU B  40      11.518  22.819  -0.869  1.00 55.29           O  
ATOM   1542  CB  LEU B  40      13.646  24.372  -2.242  1.00 54.33           C  
ATOM   1543  CG  LEU B  40      14.034  25.852  -2.220  1.00 57.22           C  
ATOM   1544  CD1 LEU B  40      14.091  26.420  -3.639  1.00 58.85           C  
ATOM   1545  CD2 LEU B  40      13.017  26.615  -1.378  1.00 67.88           C  
ATOM   1546  N   GLU B  41      13.210  21.362  -0.571  1.00 55.68           N  
ATOM   1547  CA  GLU B  41      12.349  20.201  -0.432  1.00 62.33           C  
ATOM   1548  C   GLU B  41      11.769  20.231   0.967  1.00 64.82           C  
ATOM   1549  O   GLU B  41      10.805  19.536   1.282  1.00 63.28           O  
ATOM   1550  CB  GLU B  41      13.166  18.923  -0.664  1.00 70.41           C  
ATOM   1551  CG  GLU B  41      12.389  17.634  -0.464  1.00 76.48           C  
ATOM   1552  CD  GLU B  41      13.238  16.402  -0.709  1.00 80.44           C  
ATOM   1553  OE1 GLU B  41      13.779  16.267  -1.829  1.00 76.32           O  
ATOM   1554  OE2 GLU B  41      13.366  15.573   0.218  1.00 84.69           O  
ATOM   1555  N   LYS B  42      12.378  21.064   1.797  1.00 67.83           N  
ATOM   1556  CA  LYS B  42      11.940  21.233   3.169  1.00 66.50           C  
ATOM   1557  C   LYS B  42      10.886  22.345   3.237  1.00 65.53           C  
ATOM   1558  O   LYS B  42       9.961  22.280   4.049  1.00 61.56           O  
ATOM   1559  CB  LYS B  42      13.132  21.573   4.064  1.00 65.66           C  
ATOM   1560  CG  LYS B  42      14.221  20.515   4.042  1.00 63.44           C  
ATOM   1561  CD  LYS B  42      13.645  19.153   4.356  1.00 68.12           C  
ATOM   1562  CE  LYS B  42      14.699  18.078   4.212  1.00 66.33           C  
ATOM   1563  NZ  LYS B  42      14.135  16.739   4.514  1.00 69.09           N  
ATOM   1564  N   PHE B  43      11.019  23.352   2.371  1.00 65.25           N  
ATOM   1565  CA  PHE B  43      10.083  24.472   2.314  1.00 64.57           C  
ATOM   1566  C   PHE B  43       9.090  24.185   1.208  1.00 69.77           C  
ATOM   1567  O   PHE B  43       9.442  23.706   0.132  1.00 68.87           O  
ATOM   1568  CB  PHE B  43      10.868  25.766   2.130  1.00 48.64           C  
ATOM   1569  CG  PHE B  43      11.746  26.061   3.311  1.00 56.57           C  
ATOM   1570  CD1 PHE B  43      11.177  26.444   4.521  1.00 60.50           C  
ATOM   1571  CD2 PHE B  43      13.122  25.868   3.254  1.00 57.08           C  
ATOM   1572  CE1 PHE B  43      11.953  26.626   5.650  1.00 50.35           C  
ATOM   1573  CE2 PHE B  43      13.914  26.049   4.393  1.00 59.66           C  
ATOM   1574  CZ  PHE B  43      13.322  26.429   5.589  1.00 59.76           C  
ATOM   1575  N   ASP B  44       7.830  24.425   1.526  1.00 72.01           N  
ATOM   1576  CA  ASP B  44       6.721  24.124   0.641  1.00 69.19           C  
ATOM   1577  C   ASP B  44       6.046  25.318   0.008  1.00 65.94           C  
ATOM   1578  O   ASP B  44       5.498  25.222  -1.096  1.00 61.61           O  
ATOM   1579  CB  ASP B  44       5.690  23.320   1.433  1.00 76.14           C  
ATOM   1580  CG  ASP B  44       5.333  23.981   2.766  1.00 78.03           C  
ATOM   1581  OD1 ASP B  44       6.229  24.573   3.402  1.00 80.40           O  
ATOM   1582  OD2 ASP B  44       4.161  23.911   3.191  1.00 82.39           O  
ATOM   1583  N   ARG B  45       6.050  26.443   0.703  1.00 66.41           N  
ATOM   1584  CA  ARG B  45       5.410  27.604   0.127  1.00 70.65           C  
ATOM   1585  C   ARG B  45       6.352  28.154  -0.912  1.00 71.10           C  
ATOM   1586  O   ARG B  45       6.052  29.128  -1.603  1.00 73.12           O  
ATOM   1587  CB  ARG B  45       5.033  28.621   1.206  1.00 78.57           C  
ATOM   1588  CG  ARG B  45       3.852  28.117   2.047  1.00 85.68           C  
ATOM   1589  CD  ARG B  45       3.407  29.059   3.163  1.00 88.04           C  
ATOM   1590  NE  ARG B  45       2.260  28.489   3.869  1.00 89.35           N  
ATOM   1591  CZ  ARG B  45       1.157  29.158   4.193  1.00 94.75           C  
ATOM   1592  NH1 ARG B  45       1.036  30.443   3.887  1.00 95.48           N  
ATOM   1593  NH2 ARG B  45       0.153  28.527   4.788  1.00 98.56           N  
ATOM   1594  N   PHE B  46       7.516  27.526  -1.007  1.00 70.46           N  
ATOM   1595  CA  PHE B  46       8.428  27.909  -2.048  1.00 73.91           C  
ATOM   1596  C   PHE B  46       8.788  26.695  -2.866  1.00 75.19           C  
ATOM   1597  O   PHE B  46       8.510  25.538  -2.533  1.00 79.86           O  
ATOM   1598  CB  PHE B  46       9.771  28.502  -1.590  1.00 70.07           C  
ATOM   1599  CG  PHE B  46       9.835  28.965  -0.173  1.00 67.84           C  
ATOM   1600  CD1 PHE B  46       8.858  29.779   0.377  1.00 64.92           C  
ATOM   1601  CD2 PHE B  46      10.965  28.672   0.583  1.00 68.24           C  
ATOM   1602  CE1 PHE B  46       9.019  30.300   1.660  1.00 68.33           C  
ATOM   1603  CE2 PHE B  46      11.133  29.187   1.861  1.00 60.49           C  
ATOM   1604  CZ  PHE B  46      10.160  30.004   2.401  1.00 57.52           C  
ATOM   1605  N   LYS B  47       9.461  27.053  -3.940  1.00 76.72           N  
ATOM   1606  CA  LYS B  47      10.018  26.229  -4.988  1.00 76.84           C  
ATOM   1607  C   LYS B  47       9.210  26.425  -6.239  1.00 75.22           C  
ATOM   1608  O   LYS B  47       9.732  26.292  -7.345  1.00 74.04           O  
ATOM   1609  CB  LYS B  47      10.206  24.763  -4.621  1.00 73.49           C  
ATOM   1610  CG  LYS B  47      11.219  24.234  -5.618  1.00 77.72           C  
ATOM   1611  CD  LYS B  47      11.691  22.817  -5.459  1.00 83.61           C  
ATOM   1612  CE  LYS B  47      12.890  22.627  -6.402  1.00 86.86           C  
ATOM   1613  NZ  LYS B  47      13.461  21.255  -6.518  1.00 85.28           N  
ATOM   1614  N   HIS B  48       7.944  26.748  -6.096  1.00 72.51           N  
ATOM   1615  CA  HIS B  48       7.292  27.098  -7.313  1.00 71.72           C  
ATOM   1616  C   HIS B  48       7.675  28.564  -7.434  1.00 69.19           C  
ATOM   1617  O   HIS B  48       6.966  29.388  -8.018  1.00 71.19           O  
ATOM   1618  CB  HIS B  48       5.798  26.931  -7.257  1.00 82.18           C  
ATOM   1619  CG  HIS B  48       5.267  26.575  -8.594  1.00 84.76           C  
ATOM   1620  ND1 HIS B  48       4.983  25.279  -8.961  1.00 83.43           N  
ATOM   1621  CD2 HIS B  48       5.124  27.325  -9.710  1.00 82.80           C  
ATOM   1622  CE1 HIS B  48       4.681  25.248 -10.247  1.00 77.62           C  
ATOM   1623  NE2 HIS B  48       4.762  26.476 -10.725  1.00 82.26           N  
ATOM   1624  N   LEU B  49       8.816  28.854  -6.811  1.00 65.74           N  
ATOM   1625  CA  LEU B  49       9.440  30.170  -6.772  1.00 63.53           C  
ATOM   1626  C   LEU B  49      10.610  30.013  -7.735  1.00 65.57           C  
ATOM   1627  O   LEU B  49      11.583  29.317  -7.447  1.00 65.49           O  
ATOM   1628  CB  LEU B  49       9.916  30.485  -5.352  1.00 62.57           C  
ATOM   1629  CG  LEU B  49       8.993  31.445  -4.607  1.00 62.53           C  
ATOM   1630  CD1 LEU B  49       9.653  31.846  -3.304  1.00 56.11           C  
ATOM   1631  CD2 LEU B  49       8.718  32.669  -5.476  1.00 59.56           C  
ATOM   1632  N   LYS B  50      10.480  30.663  -8.887  1.00 67.23           N  
ATOM   1633  CA  LYS B  50      11.434  30.587  -9.994  1.00 57.43           C  
ATOM   1634  C   LYS B  50      12.686  31.464  -9.977  1.00 56.72           C  
ATOM   1635  O   LYS B  50      13.769  31.018  -9.598  1.00 60.25           O  
ATOM   1636  CB  LYS B  50      10.659  30.846 -11.289  1.00 61.48           C  
ATOM   1637  CG  LYS B  50       9.348  30.089 -11.353  1.00 62.95           C  
ATOM   1638  CD  LYS B  50       9.616  28.600 -11.285  1.00 70.21           C  
ATOM   1639  CE  LYS B  50       8.449  27.844 -10.686  1.00 65.87           C  
ATOM   1640  NZ  LYS B  50       8.797  26.406 -10.542  1.00 59.61           N  
ATOM   1641  N   THR B  51      12.522  32.707 -10.418  1.00 54.31           N  
ATOM   1642  CA  THR B  51      13.618  33.667 -10.511  1.00 49.72           C  
ATOM   1643  C   THR B  51      14.083  34.242  -9.181  1.00 49.40           C  
ATOM   1644  O   THR B  51      13.481  34.006  -8.132  1.00 44.33           O  
ATOM   1645  CB  THR B  51      13.222  34.850 -11.415  1.00 47.60           C  
ATOM   1646  OG1 THR B  51      12.202  35.625 -10.771  1.00 41.15           O  
ATOM   1647  CG2 THR B  51      12.694  34.346 -12.746  1.00 49.23           C  
ATOM   1648  N   GLU B  52      15.174  34.996  -9.241  1.00 45.66           N  
ATOM   1649  CA  GLU B  52      15.707  35.649  -8.059  1.00 43.07           C  
ATOM   1650  C   GLU B  52      14.730  36.772  -7.756  1.00 39.11           C  
ATOM   1651  O   GLU B  52      14.604  37.214  -6.617  1.00 37.46           O  
ATOM   1652  CB  GLU B  52      17.105  36.214  -8.334  1.00 54.06           C  
ATOM   1653  CG  GLU B  52      18.196  35.153  -8.408  1.00 64.83           C  
ATOM   1654  CD  GLU B  52      19.577  35.740  -8.643  1.00 68.45           C  
ATOM   1655  OE1 GLU B  52      19.817  36.280  -9.745  1.00 68.03           O  
ATOM   1656  OE2 GLU B  52      20.421  35.661  -7.724  1.00 67.48           O  
ATOM   1657  N   ALA B  53      14.031  37.221  -8.793  1.00 37.73           N  
ATOM   1658  CA  ALA B  53      13.042  38.278  -8.648  1.00 36.87           C  
ATOM   1659  C   ALA B  53      11.893  37.735  -7.812  1.00 35.73           C  
ATOM   1660  O   ALA B  53      11.406  38.401  -6.900  1.00 36.68           O  
ATOM   1661  CB  ALA B  53      12.532  38.715 -10.019  1.00 46.51           C  
ATOM   1662  N   GLU B  54      11.469  36.515  -8.128  1.00 25.26           N  
ATOM   1663  CA  GLU B  54      10.377  35.873  -7.408  1.00 23.99           C  
ATOM   1664  C   GLU B  54      10.769  35.510  -5.979  1.00 11.36           C  
ATOM   1665  O   GLU B  54       9.967  35.650  -5.055  1.00 16.37           O  
ATOM   1666  CB  GLU B  54       9.908  34.622  -8.156  1.00 19.23           C  
ATOM   1667  CG  GLU B  54       9.009  34.915  -9.351  1.00 28.47           C  
ATOM   1668  CD  GLU B  54       8.558  33.656 -10.074  1.00 31.36           C  
ATOM   1669  OE1 GLU B  54       8.214  32.669  -9.390  1.00 25.71           O  
ATOM   1670  OE2 GLU B  54       8.535  33.656 -11.323  1.00 31.73           O  
ATOM   1671  N   MET B  55      12.001  35.048  -5.791  1.00 16.36           N  
ATOM   1672  CA  MET B  55      12.461  34.687  -4.457  1.00 25.94           C  
ATOM   1673  C   MET B  55      12.675  35.925  -3.590  1.00 31.28           C  
ATOM   1674  O   MET B  55      12.422  35.901  -2.385  1.00 25.35           O  
ATOM   1675  CB  MET B  55      13.756  33.876  -4.533  1.00 13.11           C  
ATOM   1676  CG  MET B  55      13.624  32.573  -5.299  1.00 23.63           C  
ATOM   1677  SD  MET B  55      15.034  31.470  -5.067  1.00 40.24           S  
ATOM   1678  CE  MET B  55      14.196  29.943  -4.606  1.00 22.54           C  
ATOM   1679  N   LYS B  56      13.137  37.009  -4.205  1.00 28.77           N  
ATOM   1680  CA  LYS B  56      13.372  38.253  -3.476  1.00 39.09           C  
ATOM   1681  C   LYS B  56      12.063  38.950  -3.163  1.00 39.14           C  
ATOM   1682  O   LYS B  56      11.964  39.787  -2.274  1.00 43.67           O  
ATOM   1683  CB  LYS B  56      14.295  39.173  -4.296  1.00 28.22           C  
ATOM   1684  CG  LYS B  56      15.714  38.635  -4.464  1.00 43.86           C  
ATOM   1685  CD  LYS B  56      16.510  39.428  -5.497  1.00 45.27           C  
ATOM   1686  CE  LYS B  56      17.892  38.841  -5.758  1.00 43.89           C  
ATOM   1687  NZ  LYS B  56      18.646  39.597  -6.802  1.00 55.32           N  
ATOM   1688  N   ALA B  57      11.052  38.571  -3.895  1.00 35.87           N  
ATOM   1689  CA  ALA B  57       9.753  39.174  -3.720  1.00 38.18           C  
ATOM   1690  C   ALA B  57       8.937  38.484  -2.628  1.00 32.94           C  
ATOM   1691  O   ALA B  57       8.118  39.116  -1.962  1.00 21.68           O  
ATOM   1692  CB  ALA B  57       8.994  39.125  -5.036  1.00 41.62           C  
ATOM   1693  N   SER B  58       9.120  37.178  -2.490  1.00 22.29           N  
ATOM   1694  CA  SER B  58       8.400  36.391  -1.490  1.00 35.49           C  
ATOM   1695  C   SER B  58       8.464  36.986  -0.088  1.00 27.52           C  
ATOM   1696  O   SER B  58       9.524  37.029   0.541  1.00 20.75           O  
ATOM   1697  CB  SER B  58       8.953  34.965  -1.453  1.00 33.20           C  
ATOM   1698  OG  SER B  58       8.296  34.192  -0.467  1.00 24.96           O  
ATOM   1699  N   GLU B  59       7.318  37.452   0.392  1.00 34.92           N  
ATOM   1700  CA  GLU B  59       7.230  38.025   1.727  1.00 37.75           C  
ATOM   1701  C   GLU B  59       7.417  36.846   2.675  1.00 45.06           C  
ATOM   1702  O   GLU B  59       7.931  36.979   3.791  1.00 35.40           O  
ATOM   1703  CB  GLU B  59       5.851  38.647   1.937  1.00 35.56           C  
ATOM   1704  CG  GLU B  59       5.811  39.687   3.030  1.00 34.43           C  
ATOM   1705  CD  GLU B  59       6.792  40.805   2.774  1.00 37.93           C  
ATOM   1706  OE1 GLU B  59       6.729  41.411   1.682  1.00 42.06           O  
ATOM   1707  OE2 GLU B  59       7.626  41.077   3.661  1.00 49.86           O  
ATOM   1708  N   ASP B  60       6.988  35.685   2.193  1.00 40.58           N  
ATOM   1709  CA  ASP B  60       7.072  34.431   2.921  1.00 32.76           C  
ATOM   1710  C   ASP B  60       8.538  34.044   3.111  1.00 36.51           C  
ATOM   1711  O   ASP B  60       8.974  33.753   4.225  1.00 26.00           O  
ATOM   1712  CB  ASP B  60       6.328  33.349   2.133  1.00 42.70           C  
ATOM   1713  CG  ASP B  60       6.116  32.082   2.931  1.00 54.72           C  
ATOM   1714  OD1 ASP B  60       7.110  31.401   3.253  1.00 68.95           O  
ATOM   1715  OD2 ASP B  60       4.949  31.765   3.242  1.00 70.17           O  
ATOM   1716  N   LEU B  61       9.292  34.048   2.016  1.00 32.35           N  
ATOM   1717  CA  LEU B  61      10.709  33.702   2.046  1.00 22.94           C  
ATOM   1718  C   LEU B  61      11.475  34.720   2.875  1.00 23.96           C  
ATOM   1719  O   LEU B  61      12.447  34.386   3.554  1.00 22.58           O  
ATOM   1720  CB  LEU B  61      11.268  33.659   0.619  1.00 13.83           C  
ATOM   1721  CG  LEU B  61      12.749  33.311   0.414  1.00 18.43           C  
ATOM   1722  CD1 LEU B  61      12.981  32.900  -1.029  1.00 22.38           C  
ATOM   1723  CD2 LEU B  61      13.625  34.501   0.776  1.00 23.67           C  
ATOM   1724  N   LYS B  62      11.030  35.969   2.808  1.00 24.00           N  
ATOM   1725  CA  LYS B  62      11.654  37.053   3.550  1.00 17.74           C  
ATOM   1726  C   LYS B  62      11.538  36.758   5.037  1.00 25.64           C  
ATOM   1727  O   LYS B  62      12.483  36.962   5.799  1.00 24.89           O  
ATOM   1728  CB  LYS B  62      10.958  38.375   3.211  1.00 23.91           C  
ATOM   1729  CG  LYS B  62      11.490  39.611   3.925  1.00 24.77           C  
ATOM   1730  CD  LYS B  62      10.869  40.864   3.308  1.00 25.99           C  
ATOM   1731  CE  LYS B  62      11.325  42.148   3.990  1.00 41.99           C  
ATOM   1732  NZ  LYS B  62      10.677  42.345   5.318  1.00 59.42           N  
ATOM   1733  N   LYS B  63      10.370  36.264   5.440  1.00 22.02           N  
ATOM   1734  CA  LYS B  63      10.117  35.932   6.834  1.00 19.10           C  
ATOM   1735  C   LYS B  63      11.071  34.847   7.334  1.00 21.04           C  
ATOM   1736  O   LYS B  63      11.577  34.931   8.452  1.00 16.45           O  
ATOM   1737  CB  LYS B  63       8.669  35.469   7.018  1.00 25.60           C  
ATOM   1738  CG  LYS B  63       7.892  36.288   8.039  1.00 23.69           C  
ATOM   1739  CD  LYS B  63       7.481  37.644   7.485  1.00 25.71           C  
ATOM   1740  CE  LYS B  63       6.150  37.545   6.752  1.00 40.36           C  
ATOM   1741  NZ  LYS B  63       5.090  37.014   7.665  1.00 38.47           N  
ATOM   1742  N   HIS B  64      11.317  33.832   6.509  1.00 17.40           N  
ATOM   1743  CA  HIS B  64      12.222  32.755   6.900  1.00 15.42           C  
ATOM   1744  C   HIS B  64      13.662  33.234   7.001  1.00 20.07           C  
ATOM   1745  O   HIS B  64      14.455  32.685   7.767  1.00 25.46           O  
ATOM   1746  CB  HIS B  64      12.132  31.578   5.922  1.00 12.48           C  
ATOM   1747  CG  HIS B  64      10.964  30.678   6.174  1.00 23.47           C  
ATOM   1748  ND1 HIS B  64       9.720  30.899   5.625  1.00 30.98           N  
ATOM   1749  CD2 HIS B  64      10.838  29.585   6.963  1.00 11.04           C  
ATOM   1750  CE1 HIS B  64       8.878  29.981   6.065  1.00 27.46           C  
ATOM   1751  NE2 HIS B  64       9.531  29.172   6.880  1.00 30.10           N  
ATOM   1752  N   GLY B  65      13.996  34.260   6.225  1.00 25.11           N  
ATOM   1753  CA  GLY B  65      15.340  34.801   6.267  1.00 18.55           C  
ATOM   1754  C   GLY B  65      15.561  35.505   7.591  1.00 28.70           C  
ATOM   1755  O   GLY B  65      16.616  35.378   8.211  1.00 28.33           O  
ATOM   1756  N   VAL B  66      14.555  36.253   8.030  1.00 20.47           N  
ATOM   1757  CA  VAL B  66      14.644  36.971   9.291  1.00 19.65           C  
ATOM   1758  C   VAL B  66      14.718  35.994  10.455  1.00 13.17           C  
ATOM   1759  O   VAL B  66      15.375  36.266  11.456  1.00  9.07           O  
ATOM   1760  CB  VAL B  66      13.435  37.901   9.489  1.00 16.62           C  
ATOM   1761  CG1 VAL B  66      13.480  38.533  10.877  1.00  5.64           C  
ATOM   1762  CG2 VAL B  66      13.438  38.976   8.415  1.00 18.13           C  
ATOM   1763  N   THR B  67      14.046  34.853  10.317  1.00 20.60           N  
ATOM   1764  CA  THR B  67      14.045  33.839  11.365  1.00 15.31           C  
ATOM   1765  C   THR B  67      15.422  33.193  11.536  1.00 19.75           C  
ATOM   1766  O   THR B  67      15.886  33.013  12.661  1.00 22.99           O  
ATOM   1767  CB  THR B  67      12.997  32.735  11.079  1.00 21.68           C  
ATOM   1768  OG1 THR B  67      11.680  33.298  11.142  1.00 18.15           O  
ATOM   1769  CG2 THR B  67      13.108  31.613  12.103  1.00 27.34           C  
ATOM   1770  N   VAL B  68      16.076  32.848  10.427  1.00 14.22           N  
ATOM   1771  CA  VAL B  68      17.401  32.230  10.495  1.00 17.69           C  
ATOM   1772  C   VAL B  68      18.428  33.159  11.123  1.00 22.27           C  
ATOM   1773  O   VAL B  68      19.075  32.805  12.109  1.00 19.26           O  
ATOM   1774  CB  VAL B  68      17.935  31.815   9.101  1.00 20.07           C  
ATOM   1775  CG1 VAL B  68      17.471  30.418   8.758  1.00 33.13           C  
ATOM   1776  CG2 VAL B  68      17.470  32.796   8.048  1.00 31.21           C  
ATOM   1777  N   LEU B  69      18.579  34.346  10.544  1.00 22.58           N  
ATOM   1778  CA  LEU B  69      19.534  35.320  11.053  1.00 21.88           C  
ATOM   1779  C   LEU B  69      19.243  35.647  12.515  1.00 14.83           C  
ATOM   1780  O   LEU B  69      20.161  35.787  13.322  1.00 10.35           O  
ATOM   1781  CB  LEU B  69      19.487  36.600  10.211  1.00 17.46           C  
ATOM   1782  CG  LEU B  69      19.781  36.433   8.717  1.00 17.33           C  
ATOM   1783  CD1 LEU B  69      19.813  37.796   8.047  1.00 25.77           C  
ATOM   1784  CD2 LEU B  69      21.108  35.724   8.530  1.00 23.32           C  
ATOM   1785  N   THR B  70      17.961  35.754  12.847  1.00 16.24           N  
ATOM   1786  CA  THR B  70      17.535  36.064  14.208  1.00 25.67           C  
ATOM   1787  C   THR B  70      18.063  35.062  15.227  1.00 21.67           C  
ATOM   1788  O   THR B  70      18.750  35.435  16.178  1.00 23.34           O  
ATOM   1789  CB  THR B  70      15.992  36.112  14.309  1.00 26.01           C  
ATOM   1790  OG1 THR B  70      15.514  37.335  13.735  1.00 25.25           O  
ATOM   1791  CG2 THR B  70      15.541  36.021  15.758  1.00 27.79           C  
ATOM   1792  N   ALA B  71      17.732  33.791  15.028  1.00 24.39           N  
ATOM   1793  CA  ALA B  71      18.168  32.735  15.930  1.00 14.86           C  
ATOM   1794  C   ALA B  71      19.690  32.632  15.971  1.00 16.14           C  
ATOM   1795  O   ALA B  71      20.284  32.535  17.044  1.00 18.80           O  
ATOM   1796  CB  ALA B  71      17.565  31.400  15.500  1.00 24.54           C  
ATOM   1797  N   LEU B  72      20.319  32.653  14.801  1.00 16.05           N  
ATOM   1798  CA  LEU B  72      21.771  32.556  14.724  1.00 17.31           C  
ATOM   1799  C   LEU B  72      22.441  33.749  15.401  1.00 20.58           C  
ATOM   1800  O   LEU B  72      23.423  33.593  16.127  1.00 25.63           O  
ATOM   1801  CB  LEU B  72      22.220  32.462  13.263  1.00 11.32           C  
ATOM   1802  CG  LEU B  72      23.711  32.200  13.033  1.00 12.58           C  
ATOM   1803  CD1 LEU B  72      24.165  31.020  13.882  1.00 10.96           C  
ATOM   1804  CD2 LEU B  72      23.960  31.928  11.558  1.00 19.90           C  
ATOM   1805  N   GLY B  73      21.909  34.942  15.155  1.00 21.66           N  
ATOM   1806  CA  GLY B  73      22.469  36.129  15.770  1.00 19.20           C  
ATOM   1807  C   GLY B  73      22.449  35.952  17.273  1.00 16.96           C  
ATOM   1808  O   GLY B  73      23.362  36.382  17.976  1.00 21.90           O  
ATOM   1809  N   ALA B  74      21.396  35.304  17.759  1.00 15.48           N  
ATOM   1810  CA  ALA B  74      21.237  35.044  19.183  1.00 13.35           C  
ATOM   1811  C   ALA B  74      22.321  34.088  19.675  1.00 11.12           C  
ATOM   1812  O   ALA B  74      22.936  34.318  20.716  1.00 25.95           O  
ATOM   1813  CB  ALA B  74      19.860  34.452  19.450  1.00  8.02           C  
ATOM   1814  N   ILE B  75      22.553  33.016  18.924  1.00 18.68           N  
ATOM   1815  CA  ILE B  75      23.564  32.035  19.297  1.00 24.60           C  
ATOM   1816  C   ILE B  75      24.966  32.630  19.286  1.00 14.59           C  
ATOM   1817  O   ILE B  75      25.743  32.423  20.218  1.00 26.08           O  
ATOM   1818  CB  ILE B  75      23.532  30.809  18.357  1.00 19.60           C  
ATOM   1819  CG1 ILE B  75      22.246  30.012  18.598  1.00 21.57           C  
ATOM   1820  CG2 ILE B  75      24.766  29.942  18.581  1.00 18.37           C  
ATOM   1821  CD1 ILE B  75      22.280  28.597  18.046  1.00 34.63           C  
ATOM   1822  N   LEU B  76      25.287  33.368  18.230  1.00 27.53           N  
ATOM   1823  CA  LEU B  76      26.599  33.989  18.111  1.00 17.76           C  
ATOM   1824  C   LEU B  76      26.866  34.942  19.272  1.00 20.63           C  
ATOM   1825  O   LEU B  76      27.959  34.947  19.838  1.00 24.02           O  
ATOM   1826  CB  LEU B  76      26.708  34.746  16.785  1.00 23.88           C  
ATOM   1827  CG  LEU B  76      26.621  33.912  15.505  1.00 19.49           C  
ATOM   1828  CD1 LEU B  76      26.729  34.828  14.296  1.00 17.73           C  
ATOM   1829  CD2 LEU B  76      27.735  32.874  15.485  1.00 25.86           C  
ATOM   1830  N   LYS B  77      25.865  35.742  19.629  1.00 18.84           N  
ATOM   1831  CA  LYS B  77      26.013  36.695  20.722  1.00 20.20           C  
ATOM   1832  C   LYS B  77      26.268  36.000  22.054  1.00 20.10           C  
ATOM   1833  O   LYS B  77      26.734  36.626  23.005  1.00 17.45           O  
ATOM   1834  CB  LYS B  77      24.771  37.583  20.835  1.00 16.44           C  
ATOM   1835  CG  LYS B  77      24.525  38.469  19.624  1.00 18.65           C  
ATOM   1836  CD  LYS B  77      23.251  39.282  19.794  1.00 22.97           C  
ATOM   1837  CE  LYS B  77      22.754  39.830  18.462  1.00 33.75           C  
ATOM   1838  NZ  LYS B  77      23.701  40.801  17.850  1.00 48.58           N  
ATOM   1839  N   LYS B  78      25.962  34.708  22.124  1.00 27.19           N  
ATOM   1840  CA  LYS B  78      26.182  33.954  23.352  1.00 29.35           C  
ATOM   1841  C   LYS B  78      27.669  33.659  23.512  1.00 20.62           C  
ATOM   1842  O   LYS B  78      28.145  33.400  24.617  1.00 20.36           O  
ATOM   1843  CB  LYS B  78      25.384  32.645  23.339  1.00 22.83           C  
ATOM   1844  CG  LYS B  78      23.870  32.831  23.391  1.00 23.69           C  
ATOM   1845  CD  LYS B  78      23.444  33.771  24.521  1.00 28.03           C  
ATOM   1846  CE  LYS B  78      23.950  33.312  25.887  1.00 38.03           C  
ATOM   1847  NZ  LYS B  78      23.401  31.993  26.315  1.00 19.86           N  
ATOM   1848  N   LYS B  79      28.394  33.699  22.398  1.00 23.62           N  
ATOM   1849  CA  LYS B  79      29.833  33.464  22.402  1.00 30.39           C  
ATOM   1850  C   LYS B  79      30.240  32.093  22.932  1.00 31.55           C  
ATOM   1851  O   LYS B  79      31.058  31.992  23.844  1.00 27.27           O  
ATOM   1852  CB  LYS B  79      30.526  34.553  23.223  1.00 26.63           C  
ATOM   1853  CG  LYS B  79      30.375  35.948  22.643  1.00 39.12           C  
ATOM   1854  CD  LYS B  79      30.670  37.013  23.685  1.00 41.19           C  
ATOM   1855  CE  LYS B  79      30.795  38.384  23.047  1.00 41.33           C  
ATOM   1856  NZ  LYS B  79      31.975  38.444  22.141  1.00 53.37           N  
ATOM   1857  N   GLY B  80      29.675  31.039  22.356  1.00 32.40           N  
ATOM   1858  CA  GLY B  80      30.019  29.699  22.792  1.00 25.68           C  
ATOM   1859  C   GLY B  80      29.130  29.162  23.895  1.00 23.42           C  
ATOM   1860  O   GLY B  80      28.899  27.956  23.973  1.00 22.04           O  
ATOM   1861  N   HIS B  81      28.634  30.048  24.753  1.00 17.65           N  
ATOM   1862  CA  HIS B  81      27.764  29.634  25.846  1.00 17.69           C  
ATOM   1863  C   HIS B  81      26.329  29.554  25.336  1.00 19.44           C  
ATOM   1864  O   HIS B  81      25.422  30.207  25.852  1.00 13.52           O  
ATOM   1865  CB  HIS B  81      27.875  30.623  27.006  1.00  5.69           C  
ATOM   1866  CG  HIS B  81      29.260  30.738  27.564  1.00 21.51           C  
ATOM   1867  ND1 HIS B  81      30.112  31.773  27.242  1.00 29.00           N  
ATOM   1868  CD2 HIS B  81      29.950  29.930  28.403  1.00 28.02           C  
ATOM   1869  CE1 HIS B  81      31.267  31.598  27.859  1.00 31.80           C  
ATOM   1870  NE2 HIS B  81      31.195  30.487  28.570  1.00 31.29           N  
ATOM   1871  N   HIS B  82      26.147  28.721  24.319  1.00 17.50           N  
ATOM   1872  CA  HIS B  82      24.862  28.530  23.658  1.00 27.01           C  
ATOM   1873  C   HIS B  82      24.229  27.169  23.936  1.00 25.00           C  
ATOM   1874  O   HIS B  82      23.175  26.849  23.387  1.00 25.35           O  
ATOM   1875  CB  HIS B  82      25.071  28.694  22.156  1.00 23.63           C  
ATOM   1876  CG  HIS B  82      26.209  27.877  21.623  1.00 23.68           C  
ATOM   1877  ND1 HIS B  82      27.051  28.327  20.628  1.00 24.04           N  
ATOM   1878  CD2 HIS B  82      26.648  26.640  21.954  1.00 16.52           C  
ATOM   1879  CE1 HIS B  82      27.959  27.403  20.371  1.00 21.15           C  
ATOM   1880  NE2 HIS B  82      27.737  26.370  21.162  1.00 22.54           N  
ATOM   1881  N   GLU B  83      24.877  26.374  24.781  1.00 30.05           N  
ATOM   1882  CA  GLU B  83      24.399  25.035  25.126  1.00 25.19           C  
ATOM   1883  C   GLU B  83      22.877  24.961  25.204  1.00 23.89           C  
ATOM   1884  O   GLU B  83      22.231  24.214  24.466  1.00 22.47           O  
ATOM   1885  CB  GLU B  83      24.983  24.594  26.474  1.00 18.43           C  
ATOM   1886  CG  GLU B  83      26.370  25.146  26.783  1.00 40.27           C  
ATOM   1887  CD  GLU B  83      26.339  26.604  27.217  1.00 45.49           C  
ATOM   1888  OE1 GLU B  83      25.237  27.190  27.274  1.00 48.24           O  
ATOM   1889  OE2 GLU B  83      27.418  27.163  27.505  1.00 46.60           O  
ATOM   1890  N   ALA B  84      22.320  25.753  26.111  1.00 22.54           N  
ATOM   1891  CA  ALA B  84      20.887  25.803  26.350  1.00 20.74           C  
ATOM   1892  C   ALA B  84      20.032  26.140  25.129  1.00 23.70           C  
ATOM   1893  O   ALA B  84      18.931  25.610  24.978  1.00 22.74           O  
ATOM   1894  CB  ALA B  84      20.611  26.788  27.454  1.00 23.72           C  
ATOM   1895  N   GLU B  85      20.529  27.015  24.261  1.00 18.86           N  
ATOM   1896  CA  GLU B  85      19.769  27.408  23.078  1.00 14.78           C  
ATOM   1897  C   GLU B  85      19.765  26.377  21.954  1.00 13.30           C  
ATOM   1898  O   GLU B  85      18.845  26.350  21.137  1.00 14.70           O  
ATOM   1899  CB  GLU B  85      20.272  28.752  22.542  1.00  6.97           C  
ATOM   1900  CG  GLU B  85      20.050  29.909  23.503  1.00 22.94           C  
ATOM   1901  CD  GLU B  85      21.251  30.195  24.388  1.00 20.35           C  
ATOM   1902  OE1 GLU B  85      21.999  29.251  24.724  1.00 20.46           O  
ATOM   1903  OE2 GLU B  85      21.436  31.373  24.757  1.00 19.82           O  
ATOM   1904  N   LEU B  86      20.785  25.528  21.912  1.00 19.46           N  
ATOM   1905  CA  LEU B  86      20.869  24.511  20.873  1.00 24.60           C  
ATOM   1906  C   LEU B  86      19.894  23.360  21.093  1.00 26.09           C  
ATOM   1907  O   LEU B  86      19.488  22.697  20.139  1.00 27.57           O  
ATOM   1908  CB  LEU B  86      22.294  23.959  20.777  1.00 20.97           C  
ATOM   1909  CG  LEU B  86      23.383  24.933  20.328  1.00 16.87           C  
ATOM   1910  CD1 LEU B  86      24.670  24.156  20.074  1.00 14.36           C  
ATOM   1911  CD2 LEU B  86      22.944  25.659  19.060  1.00  8.62           C  
ATOM   1912  N   LYS B  87      19.514  23.125  22.346  1.00 21.97           N  
ATOM   1913  CA  LYS B  87      18.591  22.039  22.662  1.00 29.56           C  
ATOM   1914  C   LYS B  87      17.273  22.118  21.890  1.00 32.52           C  
ATOM   1915  O   LYS B  87      16.978  21.243  21.076  1.00 23.71           O  
ATOM   1916  CB  LYS B  87      18.305  21.993  24.168  1.00 34.58           C  
ATOM   1917  CG  LYS B  87      19.467  21.498  25.013  1.00 32.64           C  
ATOM   1918  CD  LYS B  87      19.064  21.374  26.475  1.00 28.04           C  
ATOM   1919  CE  LYS B  87      20.208  20.842  27.322  1.00 24.31           C  
ATOM   1920  NZ  LYS B  87      19.836  20.769  28.761  1.00 30.43           N  
ATOM   1921  N   PRO B  88      16.464  23.165  22.131  1.00 28.49           N  
ATOM   1922  CA  PRO B  88      15.194  23.260  21.404  1.00 25.11           C  
ATOM   1923  C   PRO B  88      15.387  23.344  19.895  1.00 20.47           C  
ATOM   1924  O   PRO B  88      14.648  22.725  19.130  1.00 14.04           O  
ATOM   1925  CB  PRO B  88      14.554  24.518  21.989  1.00 28.35           C  
ATOM   1926  CG  PRO B  88      15.736  25.361  22.344  1.00 33.40           C  
ATOM   1927  CD  PRO B  88      16.675  24.356  22.973  1.00 35.10           C  
ATOM   1928  N   LEU B  89      16.387  24.111  19.474  1.00 22.17           N  
ATOM   1929  CA  LEU B  89      16.681  24.274  18.055  1.00 20.28           C  
ATOM   1930  C   LEU B  89      16.984  22.930  17.402  1.00 23.74           C  
ATOM   1931  O   LEU B  89      16.429  22.593  16.356  1.00 21.84           O  
ATOM   1932  CB  LEU B  89      17.878  25.205  17.867  1.00 27.13           C  
ATOM   1933  CG  LEU B  89      18.304  25.430  16.416  1.00 24.86           C  
ATOM   1934  CD1 LEU B  89      17.264  26.284  15.706  1.00 21.54           C  
ATOM   1935  CD2 LEU B  89      19.663  26.101  16.387  1.00 19.65           C  
ATOM   1936  N   ALA B  90      17.875  22.169  18.026  1.00 21.47           N  
ATOM   1937  CA  ALA B  90      18.258  20.863  17.513  1.00 17.52           C  
ATOM   1938  C   ALA B  90      17.098  19.872  17.570  1.00 20.90           C  
ATOM   1939  O   ALA B  90      16.969  19.020  16.692  1.00 31.32           O  
ATOM   1940  CB  ALA B  90      19.446  20.322  18.300  1.00 21.64           C  
ATOM   1941  N   GLN B  91      16.254  19.983  18.593  1.00 20.86           N  
ATOM   1942  CA  GLN B  91      15.127  19.065  18.723  1.00 23.26           C  
ATOM   1943  C   GLN B  91      14.105  19.207  17.601  1.00 27.46           C  
ATOM   1944  O   GLN B  91      13.623  18.207  17.075  1.00 23.88           O  
ATOM   1945  CB  GLN B  91      14.407  19.247  20.065  1.00 24.58           C  
ATOM   1946  CG  GLN B  91      13.212  18.300  20.221  1.00 13.82           C  
ATOM   1947  CD  GLN B  91      12.379  18.573  21.459  1.00 28.44           C  
ATOM   1948  OE1 GLN B  91      12.125  19.726  21.803  1.00 24.44           O  
ATOM   1949  NE2 GLN B  91      11.940  17.509  22.129  1.00 25.46           N  
ATOM   1950  N   SER B  92      13.773  20.442  17.236  1.00 17.26           N  
ATOM   1951  CA  SER B  92      12.790  20.671  16.180  1.00 25.93           C  
ATOM   1952  C   SER B  92      13.322  20.362  14.782  1.00 22.75           C  
ATOM   1953  O   SER B  92      12.600  19.819  13.948  1.00 21.01           O  
ATOM   1954  CB  SER B  92      12.282  22.118  16.225  1.00 18.53           C  
ATOM   1955  OG  SER B  92      13.314  23.040  15.919  1.00 28.89           O  
ATOM   1956  N   HIS B  93      14.581  20.703  14.528  1.00 17.95           N  
ATOM   1957  CA  HIS B  93      15.180  20.462  13.219  1.00 15.87           C  
ATOM   1958  C   HIS B  93      15.544  19.008  12.954  1.00 14.68           C  
ATOM   1959  O   HIS B  93      15.452  18.537  11.823  1.00 17.65           O  
ATOM   1960  CB  HIS B  93      16.426  21.328  13.039  1.00 20.23           C  
ATOM   1961  CG  HIS B  93      16.125  22.784  12.878  1.00 23.71           C  
ATOM   1962  ND1 HIS B  93      15.508  23.528  13.859  1.00 24.63           N  
ATOM   1963  CD2 HIS B  93      16.333  23.627  11.839  1.00 18.83           C  
ATOM   1964  CE1 HIS B  93      15.348  24.766  13.432  1.00 17.22           C  
ATOM   1965  NE2 HIS B  93      15.839  24.853  12.209  1.00 24.23           N  
ATOM   1966  N   ALA B  94      15.961  18.299  13.994  1.00 15.57           N  
ATOM   1967  CA  ALA B  94      16.341  16.903  13.838  1.00 25.58           C  
ATOM   1968  C   ALA B  94      15.141  15.967  13.900  1.00 26.92           C  
ATOM   1969  O   ALA B  94      14.960  15.117  13.028  1.00 11.88           O  
ATOM   1970  CB  ALA B  94      17.351  16.519  14.911  1.00 33.34           C  
ATOM   1971  N   THR B  95      14.314  16.147  14.926  1.00 25.09           N  
ATOM   1972  CA  THR B  95      13.151  15.296  15.143  1.00 22.11           C  
ATOM   1973  C   THR B  95      11.915  15.577  14.297  1.00 26.94           C  
ATOM   1974  O   THR B  95      11.270  14.647  13.817  1.00 21.50           O  
ATOM   1975  CB  THR B  95      12.726  15.335  16.619  1.00 22.77           C  
ATOM   1976  OG1 THR B  95      13.879  15.168  17.451  1.00 21.80           O  
ATOM   1977  CG2 THR B  95      11.729  14.220  16.914  1.00 19.81           C  
ATOM   1978  N   LYS B  96      11.578  16.850  14.120  1.00 24.35           N  
ATOM   1979  CA  LYS B  96      10.392  17.215  13.353  1.00 21.84           C  
ATOM   1980  C   LYS B  96      10.626  17.434  11.863  1.00 27.43           C  
ATOM   1981  O   LYS B  96       9.920  16.869  11.029  1.00 26.96           O  
ATOM   1982  CB  LYS B  96       9.756  18.472  13.950  1.00 28.94           C  
ATOM   1983  CG  LYS B  96       8.525  18.974  13.211  1.00 25.24           C  
ATOM   1984  CD  LYS B  96       8.017  20.267  13.836  1.00 36.59           C  
ATOM   1985  CE  LYS B  96       6.811  20.821  13.093  1.00 46.23           C  
ATOM   1986  NZ  LYS B  96       6.363  22.123  13.663  1.00 42.44           N  
ATOM   1987  N   HIS B  97      11.619  18.251  11.533  1.00 27.97           N  
ATOM   1988  CA  HIS B  97      11.909  18.569  10.142  1.00 25.34           C  
ATOM   1989  C   HIS B  97      12.969  17.697   9.482  1.00 27.86           C  
ATOM   1990  O   HIS B  97      13.313  17.900   8.319  1.00 17.64           O  
ATOM   1991  CB  HIS B  97      12.275  20.049  10.049  1.00 27.61           C  
ATOM   1992  CG  HIS B  97      11.223  20.945  10.623  1.00 31.64           C  
ATOM   1993  ND1 HIS B  97       9.946  21.007  10.108  1.00 25.60           N  
ATOM   1994  CD2 HIS B  97      11.226  21.740  11.719  1.00 33.11           C  
ATOM   1995  CE1 HIS B  97       9.207  21.797  10.864  1.00 25.36           C  
ATOM   1996  NE2 HIS B  97       9.959  22.255  11.849  1.00 25.00           N  
ATOM   1997  N   LYS B  98      13.472  16.719  10.230  1.00 26.53           N  
ATOM   1998  CA  LYS B  98      14.475  15.791   9.722  1.00 29.33           C  
ATOM   1999  C   LYS B  98      15.538  16.487   8.872  1.00 29.12           C  
ATOM   2000  O   LYS B  98      15.818  16.065   7.750  1.00 37.42           O  
ATOM   2001  CB  LYS B  98      13.793  14.703   8.888  1.00 25.15           C  
ATOM   2002  CG  LYS B  98      12.521  14.138   9.508  1.00 19.58           C  
ATOM   2003  CD  LYS B  98      12.785  13.488  10.855  1.00 26.99           C  
ATOM   2004  CE  LYS B  98      11.521  12.857  11.416  1.00 34.94           C  
ATOM   2005  NZ  LYS B  98      11.768  12.172  12.718  1.00 41.69           N  
ATOM   2006  N   ILE B  99      16.127  17.550   9.408  1.00 28.17           N  
ATOM   2007  CA  ILE B  99      17.156  18.296   8.690  1.00 26.62           C  
ATOM   2008  C   ILE B  99      18.554  17.771   9.009  1.00 36.53           C  
ATOM   2009  O   ILE B  99      18.961  17.730  10.167  1.00 34.64           O  
ATOM   2010  CB  ILE B  99      17.100  19.796   9.040  1.00 25.53           C  
ATOM   2011  CG1 ILE B  99      15.741  20.369   8.633  1.00 21.71           C  
ATOM   2012  CG2 ILE B  99      18.233  20.543   8.344  1.00 23.46           C  
ATOM   2013  CD1 ILE B  99      15.441  20.243   7.153  1.00 33.15           C  
ATOM   2014  N   PRO B 100      19.305  17.355   7.977  1.00 45.39           N  
ATOM   2015  CA  PRO B 100      20.663  16.831   8.157  1.00 47.42           C  
ATOM   2016  C   PRO B 100      21.672  17.911   8.528  1.00 48.54           C  
ATOM   2017  O   PRO B 100      21.551  19.056   8.096  1.00 51.32           O  
ATOM   2018  CB  PRO B 100      20.977  16.214   6.795  1.00 54.93           C  
ATOM   2019  CG  PRO B 100      19.631  15.842   6.269  1.00 50.30           C  
ATOM   2020  CD  PRO B 100      18.823  17.060   6.618  1.00 47.59           C  
ATOM   2021  N   ILE B 101      22.669  17.536   9.325  1.00 47.61           N  
ATOM   2022  CA  ILE B 101      23.720  18.466   9.736  1.00 47.09           C  
ATOM   2023  C   ILE B 101      24.481  18.906   8.489  1.00 41.33           C  
ATOM   2024  O   ILE B 101      25.302  19.823   8.523  1.00 42.55           O  
ATOM   2025  CB  ILE B 101      24.706  17.790  10.716  1.00 47.88           C  
ATOM   2026  CG1 ILE B 101      23.973  17.346  11.985  1.00 46.34           C  
ATOM   2027  CG2 ILE B 101      25.832  18.742  11.075  1.00 51.93           C  
ATOM   2028  CD1 ILE B 101      23.354  18.482  12.775  1.00 48.54           C  
ATOM   2029  N   LYS B 102      24.173  18.233   7.390  1.00 39.95           N  
ATOM   2030  CA  LYS B 102      24.780  18.475   6.091  1.00 48.30           C  
ATOM   2031  C   LYS B 102      24.320  19.807   5.508  1.00 42.57           C  
ATOM   2032  O   LYS B 102      25.031  20.423   4.714  1.00 44.49           O  
ATOM   2033  CB  LYS B 102      24.413  17.319   5.161  1.00 58.93           C  
ATOM   2034  CG  LYS B 102      25.181  17.239   3.858  1.00 65.46           C  
ATOM   2035  CD  LYS B 102      24.823  15.939   3.158  1.00 71.50           C  
ATOM   2036  CE  LYS B 102      25.468  15.795   1.799  1.00 84.28           C  
ATOM   2037  NZ  LYS B 102      25.079  14.485   1.208  1.00 88.35           N  
ATOM   2038  N   TYR B 103      23.127  20.243   5.905  1.00 41.30           N  
ATOM   2039  CA  TYR B 103      22.581  21.515   5.437  1.00 29.61           C  
ATOM   2040  C   TYR B 103      23.153  22.629   6.301  1.00 30.58           C  
ATOM   2041  O   TYR B 103      23.308  23.764   5.847  1.00 33.63           O  
ATOM   2042  CB  TYR B 103      21.055  21.538   5.538  1.00 27.24           C  
ATOM   2043  CG  TYR B 103      20.338  20.518   4.680  1.00 39.50           C  
ATOM   2044  CD1 TYR B 103      21.040  19.658   3.833  1.00 38.55           C  
ATOM   2045  CD2 TYR B 103      18.948  20.414   4.718  1.00 46.23           C  
ATOM   2046  CE1 TYR B 103      20.372  18.720   3.048  1.00 44.57           C  
ATOM   2047  CE2 TYR B 103      18.271  19.482   3.939  1.00 40.48           C  
ATOM   2048  CZ  TYR B 103      18.986  18.640   3.107  1.00 44.50           C  
ATOM   2049  OH  TYR B 103      18.315  17.722   2.333  1.00 28.49           O  
ATOM   2050  N   LEU B 104      23.452  22.299   7.555  1.00 32.94           N  
ATOM   2051  CA  LEU B 104      24.027  23.262   8.486  1.00 33.41           C  
ATOM   2052  C   LEU B 104      25.355  23.720   7.906  1.00 39.52           C  
ATOM   2053  O   LEU B 104      25.789  24.852   8.126  1.00 34.46           O  
ATOM   2054  CB  LEU B 104      24.248  22.614   9.856  1.00 36.09           C  
ATOM   2055  CG  LEU B 104      23.026  22.421  10.759  1.00 40.82           C  
ATOM   2056  CD1 LEU B 104      22.526  23.782  11.204  1.00 37.84           C  
ATOM   2057  CD2 LEU B 104      21.931  21.652  10.030  1.00 33.42           C  
ATOM   2058  N   GLU B 105      25.994  22.822   7.164  1.00 41.27           N  
ATOM   2059  CA  GLU B 105      27.261  23.123   6.519  1.00 31.30           C  
ATOM   2060  C   GLU B 105      26.957  23.906   5.250  1.00 29.13           C  
ATOM   2061  O   GLU B 105      27.629  24.887   4.936  1.00 30.39           O  
ATOM   2062  CB  GLU B 105      28.007  21.833   6.167  1.00 30.96           C  
ATOM   2063  CG  GLU B 105      28.295  20.936   7.358  1.00 40.96           C  
ATOM   2064  CD  GLU B 105      29.269  19.822   7.028  1.00 56.41           C  
ATOM   2065  OE1 GLU B 105      29.720  19.748   5.865  1.00 59.67           O  
ATOM   2066  OE2 GLU B 105      29.585  19.019   7.933  1.00 53.96           O  
ATOM   2067  N   PHE B 106      25.928  23.468   4.528  1.00 31.07           N  
ATOM   2068  CA  PHE B 106      25.522  24.129   3.294  1.00 32.70           C  
ATOM   2069  C   PHE B 106      25.183  25.598   3.516  1.00 27.21           C  
ATOM   2070  O   PHE B 106      25.592  26.460   2.739  1.00 28.82           O  
ATOM   2071  CB  PHE B 106      24.292  23.447   2.683  1.00 36.36           C  
ATOM   2072  CG  PHE B 106      24.552  22.076   2.129  1.00 36.48           C  
ATOM   2073  CD1 PHE B 106      25.831  21.686   1.745  1.00 37.23           C  
ATOM   2074  CD2 PHE B 106      23.497  21.189   1.938  1.00 42.91           C  
ATOM   2075  CE1 PHE B 106      26.055  20.434   1.177  1.00 30.12           C  
ATOM   2076  CE2 PHE B 106      23.709  19.934   1.370  1.00 39.06           C  
ATOM   2077  CZ  PHE B 106      24.991  19.557   0.988  1.00 39.26           C  
ATOM   2078  N  AILE B 107      24.433  25.880   4.576  0.50 20.83           N  
ATOM   2079  N  BILE B 107      24.433  25.880   4.576  0.50 21.89           N  
ATOM   2080  CA AILE B 107      24.032  27.249   4.875  0.50 22.48           C  
ATOM   2081  CA BILE B 107      24.037  27.250   4.868  0.50 24.69           C  
ATOM   2082  C  AILE B 107      25.195  28.088   5.398  0.50 24.31           C  
ATOM   2083  C  BILE B 107      25.198  28.088   5.394  0.50 25.28           C  
ATOM   2084  O  AILE B 107      25.216  29.308   5.224  0.50 16.73           O  
ATOM   2085  O  BILE B 107      25.218  29.307   5.220  0.50 17.34           O  
ATOM   2086  CB AILE B 107      22.873  27.280   5.900  0.50 18.82           C  
ATOM   2087  CB BILE B 107      22.872  27.294   5.885  0.50 23.84           C  
ATOM   2088  CG1AILE B 107      22.277  28.687   5.963  0.50 17.41           C  
ATOM   2089  CG1BILE B 107      22.074  28.583   5.684  0.50 27.32           C  
ATOM   2090  CG2AILE B 107      23.373  26.852   7.275  0.50 23.49           C  
ATOM   2091  CG2BILE B 107      23.404  27.217   7.313  0.50 30.47           C  
ATOM   2092  CD1AILE B 107      20.943  28.759   6.678  0.50  7.16           C  
ATOM   2093  CD1BILE B 107      21.573  28.766   4.260  0.50 19.12           C  
ATOM   2094  N   SER B 108      26.162  27.435   6.036  1.00 23.42           N  
ATOM   2095  CA  SER B 108      27.323  28.141   6.565  1.00 31.06           C  
ATOM   2096  C   SER B 108      28.124  28.695   5.393  1.00 32.79           C  
ATOM   2097  O   SER B 108      28.574  29.842   5.421  1.00 25.03           O  
ATOM   2098  CB  SER B 108      28.201  27.205   7.399  1.00 26.61           C  
ATOM   2099  OG  SER B 108      27.579  26.888   8.633  1.00 29.90           O  
ATOM   2100  N   GLU B 109      28.294  27.876   4.359  1.00 33.06           N  
ATOM   2101  CA  GLU B 109      29.032  28.304   3.178  1.00 40.21           C  
ATOM   2102  C   GLU B 109      28.228  29.403   2.495  1.00 36.52           C  
ATOM   2103  O   GLU B 109      28.790  30.338   1.929  1.00 33.95           O  
ATOM   2104  CB  GLU B 109      29.260  27.124   2.219  1.00 37.32           C  
ATOM   2105  CG  GLU B 109      28.078  26.730   1.331  1.00 56.71           C  
ATOM   2106  CD  GLU B 109      27.869  27.679   0.160  1.00 65.74           C  
ATOM   2107  OE1 GLU B 109      28.817  28.413  -0.190  1.00 70.14           O  
ATOM   2108  OE2 GLU B 109      26.762  27.681  -0.419  1.00 71.30           O  
ATOM   2109  N   ALA B 110      26.906  29.284   2.563  1.00 39.61           N  
ATOM   2110  CA  ALA B 110      26.017  30.270   1.963  1.00 39.08           C  
ATOM   2111  C   ALA B 110      26.182  31.611   2.672  1.00 32.37           C  
ATOM   2112  O   ALA B 110      26.191  32.661   2.032  1.00 29.41           O  
ATOM   2113  CB  ALA B 110      24.568  29.798   2.061  1.00 32.38           C  
ATOM   2114  N   ILE B 111      26.317  31.570   3.994  1.00 31.45           N  
ATOM   2115  CA  ILE B 111      26.480  32.790   4.780  1.00 34.87           C  
ATOM   2116  C   ILE B 111      27.826  33.464   4.530  1.00 35.88           C  
ATOM   2117  O   ILE B 111      27.889  34.683   4.371  1.00 43.19           O  
ATOM   2118  CB  ILE B 111      26.321  32.510   6.292  1.00 44.59           C  
ATOM   2119  CG1 ILE B 111      24.886  32.055   6.582  1.00 30.82           C  
ATOM   2120  CG2 ILE B 111      26.650  33.765   7.098  1.00 30.86           C  
ATOM   2121  CD1 ILE B 111      24.611  31.750   8.037  1.00 36.15           C  
ATOM   2122  N   ILE B 112      28.901  32.681   4.501  1.00 31.77           N  
ATOM   2123  CA  ILE B 112      30.225  33.242   4.250  1.00 38.88           C  
ATOM   2124  C   ILE B 112      30.291  33.740   2.809  1.00 35.94           C  
ATOM   2125  O   ILE B 112      30.968  34.724   2.508  1.00 38.31           O  
ATOM   2126  CB  ILE B 112      31.340  32.196   4.496  1.00 42.49           C  
ATOM   2127  CG1 ILE B 112      31.537  32.004   6.004  1.00 48.36           C  
ATOM   2128  CG2 ILE B 112      32.639  32.637   3.827  1.00 28.29           C  
ATOM   2129  CD1 ILE B 112      32.631  31.021   6.372  1.00 55.68           C  
ATOM   2130  N   HIS B 113      29.574  33.053   1.927  1.00 26.24           N  
ATOM   2131  CA  HIS B 113      29.517  33.422   0.517  1.00 27.01           C  
ATOM   2132  C   HIS B 113      28.775  34.748   0.368  1.00 30.05           C  
ATOM   2133  O   HIS B 113      29.132  35.581  -0.464  1.00 25.05           O  
ATOM   2134  CB  HIS B 113      28.782  32.341  -0.279  1.00 30.69           C  
ATOM   2135  CG  HIS B 113      28.411  32.759  -1.668  1.00 49.22           C  
ATOM   2136  ND1 HIS B 113      29.300  32.728  -2.721  1.00 47.34           N  
ATOM   2137  CD2 HIS B 113      27.248  33.238  -2.172  1.00 41.77           C  
ATOM   2138  CE1 HIS B 113      28.701  33.168  -3.813  1.00 42.57           C  
ATOM   2139  NE2 HIS B 113      27.455  33.484  -3.507  1.00 42.87           N  
ATOM   2140  N   VAL B 114      27.739  34.930   1.182  1.00 30.83           N  
ATOM   2141  CA  VAL B 114      26.931  36.144   1.149  1.00 30.81           C  
ATOM   2142  C   VAL B 114      27.626  37.341   1.792  1.00 28.31           C  
ATOM   2143  O   VAL B 114      27.582  38.448   1.259  1.00 31.23           O  
ATOM   2144  CB  VAL B 114      25.571  35.922   1.850  1.00 32.21           C  
ATOM   2145  CG1 VAL B 114      24.845  37.252   2.020  1.00 19.91           C  
ATOM   2146  CG2 VAL B 114      24.718  34.965   1.029  1.00 38.15           C  
ATOM   2147  N   LEU B 115      28.258  37.123   2.939  1.00 27.08           N  
ATOM   2148  CA  LEU B 115      28.954  38.204   3.628  1.00 40.07           C  
ATOM   2149  C   LEU B 115      30.184  38.649   2.847  1.00 35.85           C  
ATOM   2150  O   LEU B 115      30.573  39.816   2.892  1.00 24.86           O  
ATOM   2151  CB  LEU B 115      29.367  37.758   5.033  1.00 38.92           C  
ATOM   2152  CG  LEU B 115      28.254  37.689   6.083  1.00 44.42           C  
ATOM   2153  CD1 LEU B 115      28.760  36.985   7.331  1.00 50.28           C  
ATOM   2154  CD2 LEU B 115      27.779  39.099   6.413  1.00 35.95           C  
ATOM   2155  N   HIS B 116      30.787  37.712   2.121  1.00 36.57           N  
ATOM   2156  CA  HIS B 116      31.982  37.999   1.338  1.00 48.22           C  
ATOM   2157  C   HIS B 116      31.677  38.815   0.081  1.00 47.65           C  
ATOM   2158  O   HIS B 116      32.455  39.689  -0.304  1.00 39.78           O  
ATOM   2159  CB  HIS B 116      32.671  36.686   0.953  1.00 48.44           C  
ATOM   2160  CG  HIS B 116      34.104  36.849   0.549  1.00 53.48           C  
ATOM   2161  ND1 HIS B 116      34.490  37.584  -0.551  1.00 52.91           N  
ATOM   2162  CD2 HIS B 116      35.244  36.370   1.101  1.00 48.45           C  
ATOM   2163  CE1 HIS B 116      35.806  37.551  -0.660  1.00 55.67           C  
ATOM   2164  NE2 HIS B 116      36.288  36.820   0.330  1.00 55.24           N  
ATOM   2165  N   SER B 117      30.542  38.535  -0.556  1.00 46.78           N  
ATOM   2166  CA  SER B 117      30.159  39.250  -1.771  1.00 45.57           C  
ATOM   2167  C   SER B 117      29.364  40.510  -1.451  1.00 47.41           C  
ATOM   2168  O   SER B 117      29.342  41.457  -2.237  1.00 46.62           O  
ATOM   2169  CB  SER B 117      29.309  38.356  -2.676  0.53 39.61           C  
ATOM   2170  OG  SER B 117      27.950  38.385  -2.280  0.53 23.89           O  
ATOM   2171  N   ARG B 118      28.709  40.510  -0.295  1.00 51.30           N  
ATOM   2172  CA  ARG B 118      27.895  41.642   0.129  1.00 54.65           C  
ATOM   2173  C   ARG B 118      28.692  42.588   1.023  1.00 51.50           C  
ATOM   2174  O   ARG B 118      28.275  43.721   1.263  1.00 47.57           O  
ATOM   2175  CB  ARG B 118      26.662  41.130   0.880  1.00 52.08           C  
ATOM   2176  CG  ARG B 118      25.395  41.956   0.711  1.00 53.05           C  
ATOM   2177  CD  ARG B 118      24.216  41.208   1.321  1.00 45.80           C  
ATOM   2178  NE  ARG B 118      22.931  41.869   1.109  1.00 49.41           N  
ATOM   2179  CZ  ARG B 118      22.609  43.064   1.592  1.00 45.49           C  
ATOM   2180  NH1 ARG B 118      23.481  43.747   2.319  1.00 51.64           N  
ATOM   2181  NH2 ARG B 118      21.406  43.572   1.356  1.00 51.83           N  
ATOM   2182  N   HIS B 119      29.840  42.124   1.510  1.00 51.58           N  
ATOM   2183  CA  HIS B 119      30.670  42.947   2.384  1.00 55.71           C  
ATOM   2184  C   HIS B 119      32.169  42.732   2.202  1.00 52.46           C  
ATOM   2185  O   HIS B 119      32.827  42.154   3.062  1.00 52.63           O  
ATOM   2186  CB  HIS B 119      30.298  42.693   3.846  1.00 41.41           C  
ATOM   2187  CG  HIS B 119      28.883  43.044   4.175  1.00 56.24           C  
ATOM   2188  ND1 HIS B 119      28.349  44.289   3.920  1.00 58.86           N  
ATOM   2189  CD2 HIS B 119      27.886  42.313   4.727  1.00 61.82           C  
ATOM   2190  CE1 HIS B 119      27.084  44.310   4.299  1.00 67.36           C  
ATOM   2191  NE2 HIS B 119      26.779  43.123   4.793  1.00 64.95           N  
ATOM   2192  N   PRO B 120      32.731  43.201   1.079  1.00 56.77           N  
ATOM   2193  CA  PRO B 120      34.169  43.032   0.842  1.00 61.04           C  
ATOM   2194  C   PRO B 120      35.009  43.848   1.825  1.00 63.49           C  
ATOM   2195  O   PRO B 120      35.956  43.344   2.429  1.00 59.28           O  
ATOM   2196  CB  PRO B 120      34.340  43.521  -0.595  1.00 59.71           C  
ATOM   2197  CG  PRO B 120      33.005  43.225  -1.218  1.00 48.24           C  
ATOM   2198  CD  PRO B 120      32.053  43.674  -0.140  1.00 58.16           C  
ATOM   2199  N   GLY B 121      34.640  45.114   1.977  1.00 64.58           N  
ATOM   2200  CA  GLY B 121      35.357  46.008   2.865  1.00 63.31           C  
ATOM   2201  C   GLY B 121      35.494  45.614   4.325  1.00 63.45           C  
ATOM   2202  O   GLY B 121      36.525  45.904   4.930  1.00 68.91           O  
ATOM   2203  N   ASP B 122      34.477  44.967   4.901  1.00 62.24           N  
ATOM   2204  CA  ASP B 122      34.521  44.581   6.313  1.00 52.88           C  
ATOM   2205  C   ASP B 122      34.394  43.077   6.595  1.00 45.03           C  
ATOM   2206  O   ASP B 122      34.069  42.652   7.712  1.00 35.34           O  
ATOM   2207  CB  ASP B 122      33.472  45.375   7.088  1.00 55.50           C  
ATOM   2208  CG  ASP B 122      32.086  45.182   6.540  1.00 64.85           C  
ATOM   2209  OD1 ASP B 122      31.957  44.636   5.427  1.00 68.67           O  
ATOM   2210  OD2 ASP B 122      31.122  45.587   7.213  1.00 66.65           O  
ATOM   2211  N   PHE B 123      34.650  42.290   5.552  1.00 48.45           N  
ATOM   2212  CA  PHE B 123      34.676  40.834   5.640  1.00 45.68           C  
ATOM   2213  C   PHE B 123      36.041  40.471   5.056  1.00 43.39           C  
ATOM   2214  O   PHE B 123      36.841  41.356   4.753  1.00 39.96           O  
ATOM   2215  CB  PHE B 123      33.535  40.172   4.858  1.00 39.76           C  
ATOM   2216  CG  PHE B 123      33.196  38.783   5.342  1.00 39.36           C  
ATOM   2217  CD1 PHE B 123      32.518  38.587   6.546  1.00 51.14           C  
ATOM   2218  CD2 PHE B 123      33.535  37.672   4.581  1.00 51.70           C  
ATOM   2219  CE1 PHE B 123      32.180  37.300   6.975  1.00 50.87           C  
ATOM   2220  CE2 PHE B 123      33.202  36.388   5.003  1.00 48.94           C  
ATOM   2221  CZ  PHE B 123      32.525  36.201   6.196  1.00 54.11           C  
ATOM   2222  N   GLY B 124      36.329  39.192   4.890  1.00 44.56           N  
ATOM   2223  CA  GLY B 124      37.636  38.853   4.380  1.00 42.93           C  
ATOM   2224  C   GLY B 124      38.405  38.188   5.494  1.00 41.08           C  
ATOM   2225  O   GLY B 124      37.822  37.803   6.503  1.00 39.57           O  
ATOM   2226  N   ALA B 125      39.712  38.071   5.318  1.00 42.45           N  
ATOM   2227  CA  ALA B 125      40.567  37.410   6.285  1.00 48.31           C  
ATOM   2228  C   ALA B 125      40.253  37.733   7.746  1.00 48.69           C  
ATOM   2229  O   ALA B 125      39.891  36.837   8.510  1.00 48.95           O  
ATOM   2230  CB  ALA B 125      42.030  37.721   5.970  1.00 51.94           C  
ATOM   2231  N   ASP B 126      40.378  39.002   8.129  1.00 53.30           N  
ATOM   2232  CA  ASP B 126      40.132  39.430   9.509  1.00 55.68           C  
ATOM   2233  C   ASP B 126      38.773  39.032  10.092  1.00 51.91           C  
ATOM   2234  O   ASP B 126      38.542  39.185  11.292  1.00 44.34           O  
ATOM   2235  CB  ASP B 126      40.296  40.949   9.622  1.00 57.66           C  
ATOM   2236  CG  ASP B 126      39.190  41.711   8.915  1.00 52.21           C  
ATOM   2237  OD1 ASP B 126      38.960  41.441   7.717  1.00 24.47           O  
ATOM   2238  OD2 ASP B 126      38.557  42.582   9.555  1.00 46.34           O  
ATOM   2239  N   ALA B 127      37.876  38.534   9.248  1.00 48.82           N  
ATOM   2240  CA  ALA B 127      36.552  38.127   9.704  1.00 47.91           C  
ATOM   2241  C   ALA B 127      36.169  36.766   9.131  1.00 48.44           C  
ATOM   2242  O   ALA B 127      35.415  36.015   9.745  1.00 57.83           O  
ATOM   2243  CB  ALA B 127      35.521  39.174   9.307  1.00 55.52           C  
ATOM   2244  N   GLN B 128      36.696  36.458   7.951  1.00 42.18           N  
ATOM   2245  CA  GLN B 128      36.430  35.189   7.280  1.00 43.01           C  
ATOM   2246  C   GLN B 128      36.772  34.036   8.213  1.00 45.58           C  
ATOM   2247  O   GLN B 128      35.925  33.197   8.521  1.00 43.49           O  
ATOM   2248  CB  GLN B 128      37.277  35.080   6.009  1.00 35.45           C  
ATOM   2249  CG  GLN B 128      37.157  33.753   5.273  1.00 48.12           C  
ATOM   2250  CD  GLN B 128      36.002  33.720   4.291  1.00 54.03           C  
ATOM   2251  OE1 GLN B 128      35.713  32.685   3.691  1.00 56.79           O  
ATOM   2252  NE2 GLN B 128      35.343  34.857   4.114  1.00 59.06           N  
ATOM   2253  N   GLY B 129      38.024  34.005   8.658  1.00 42.74           N  
ATOM   2254  CA  GLY B 129      38.473  32.953   9.550  1.00 41.09           C  
ATOM   2255  C   GLY B 129      37.754  32.961  10.884  1.00 34.18           C  
ATOM   2256  O   GLY B 129      37.491  31.905  11.457  1.00 43.32           O  
ATOM   2257  N   ALA B 130      37.439  34.153  11.382  1.00 30.62           N  
ATOM   2258  CA  ALA B 130      36.745  34.294  12.656  1.00 29.32           C  
ATOM   2259  C   ALA B 130      35.321  33.767  12.541  1.00 32.50           C  
ATOM   2260  O   ALA B 130      34.896  32.922  13.330  1.00 34.44           O  
ATOM   2261  CB  ALA B 130      36.730  35.754  13.083  1.00 25.41           C  
ATOM   2262  N   MET B 131      34.584  34.273  11.555  1.00 30.82           N  
ATOM   2263  CA  MET B 131      33.210  33.844  11.328  1.00 24.24           C  
ATOM   2264  C   MET B 131      33.214  32.372  10.936  1.00 31.40           C  
ATOM   2265  O   MET B 131      32.236  31.655  11.150  1.00 34.94           O  
ATOM   2266  CB  MET B 131      32.568  34.672  10.215  1.00 17.92           C  
ATOM   2267  CG  MET B 131      31.104  34.344   9.973  1.00 23.16           C  
ATOM   2268  SD  MET B 131      30.117  34.492  11.476  1.00 32.09           S  
ATOM   2269  CE  MET B 131      29.762  36.251  11.481  1.00 11.64           C  
ATOM   2270  N   ASN B 132      34.327  31.932  10.358  1.00 27.43           N  
ATOM   2271  CA  ASN B 132      34.482  30.546   9.945  1.00 33.79           C  
ATOM   2272  C   ASN B 132      34.630  29.715  11.217  1.00 34.92           C  
ATOM   2273  O   ASN B 132      34.299  28.531  11.245  1.00 31.55           O  
ATOM   2274  CB  ASN B 132      35.729  30.401   9.068  1.00 45.94           C  
ATOM   2275  CG  ASN B 132      35.696  29.159   8.199  1.00 46.21           C  
ATOM   2276  OD1 ASN B 132      34.771  28.966   7.408  1.00 33.86           O  
ATOM   2277  ND2 ASN B 132      36.711  28.311   8.335  1.00 44.15           N  
ATOM   2278  N   LYS B 133      35.125  30.361  12.271  1.00 32.27           N  
ATOM   2279  CA  LYS B 133      35.327  29.717  13.565  1.00 35.26           C  
ATOM   2280  C   LYS B 133      34.023  29.503  14.332  1.00 27.66           C  
ATOM   2281  O   LYS B 133      33.707  28.384  14.733  1.00 24.77           O  
ATOM   2282  CB  LYS B 133      36.277  30.552  14.430  1.00 41.25           C  
ATOM   2283  CG  LYS B 133      37.758  30.295  14.205  1.00 32.11           C  
ATOM   2284  CD  LYS B 133      38.592  31.130  15.169  1.00 36.78           C  
ATOM   2285  CE  LYS B 133      39.991  30.561  15.357  1.00 29.50           C  
ATOM   2286  NZ  LYS B 133      40.769  30.506  14.093  1.00 34.25           N  
ATOM   2287  N   ALA B 134      33.278  30.585  14.539  1.00 23.87           N  
ATOM   2288  CA  ALA B 134      32.015  30.528  15.272  1.00 33.36           C  
ATOM   2289  C   ALA B 134      30.993  29.582  14.645  1.00 32.44           C  
ATOM   2290  O   ALA B 134      30.308  28.845  15.354  1.00 34.19           O  
ATOM   2291  CB  ALA B 134      31.420  31.926  15.393  1.00 26.90           C  
ATOM   2292  N   LEU B 135      30.885  29.604  13.321  1.00 22.85           N  
ATOM   2293  CA  LEU B 135      29.934  28.738  12.638  1.00 23.11           C  
ATOM   2294  C   LEU B 135      30.350  27.282  12.764  1.00 27.20           C  
ATOM   2295  O   LEU B 135      29.508  26.393  12.904  1.00 22.55           O  
ATOM   2296  CB  LEU B 135      29.822  29.125  11.162  1.00 20.83           C  
ATOM   2297  CG  LEU B 135      29.275  30.530  10.897  1.00 17.69           C  
ATOM   2298  CD1 LEU B 135      29.052  30.721   9.405  1.00 29.73           C  
ATOM   2299  CD2 LEU B 135      27.968  30.724  11.655  1.00 24.92           C  
ATOM   2300  N   GLU B 136      31.656  27.045  12.716  1.00 24.06           N  
ATOM   2301  CA  GLU B 136      32.193  25.698  12.831  1.00 23.20           C  
ATOM   2302  C   GLU B 136      31.839  25.147  14.205  1.00 24.29           C  
ATOM   2303  O   GLU B 136      31.454  23.987  14.343  1.00 29.11           O  
ATOM   2304  CB  GLU B 136      33.711  25.725  12.650  1.00 23.01           C  
ATOM   2305  CG  GLU B 136      34.332  24.362  12.416  1.00 22.49           C  
ATOM   2306  CD  GLU B 136      35.785  24.458  11.996  1.00 51.54           C  
ATOM   2307  OE1 GLU B 136      36.177  25.517  11.459  1.00 40.77           O  
ATOM   2308  OE2 GLU B 136      36.532  23.475  12.192  1.00 54.84           O  
ATOM   2309  N   LEU B 137      31.975  25.992  15.222  1.00 14.08           N  
ATOM   2310  CA  LEU B 137      31.656  25.602  16.587  1.00 24.67           C  
ATOM   2311  C   LEU B 137      30.158  25.346  16.682  1.00 24.02           C  
ATOM   2312  O   LEU B 137      29.711  24.436  17.382  1.00 29.08           O  
ATOM   2313  CB  LEU B 137      32.044  26.717  17.559  1.00 19.66           C  
ATOM   2314  CG  LEU B 137      31.710  26.467  19.030  1.00 18.83           C  
ATOM   2315  CD1 LEU B 137      32.614  25.375  19.576  1.00 24.96           C  
ATOM   2316  CD2 LEU B 137      31.890  27.749  19.823  1.00 19.34           C  
ATOM   2317  N   PHE B 138      29.389  26.162  15.969  1.00 26.77           N  
ATOM   2318  CA  PHE B 138      27.938  26.040  15.952  1.00 20.10           C  
ATOM   2319  C   PHE B 138      27.522  24.661  15.457  1.00 22.61           C  
ATOM   2320  O   PHE B 138      26.796  23.939  16.141  1.00 24.37           O  
ATOM   2321  CB  PHE B 138      27.327  27.114  15.048  1.00 21.64           C  
ATOM   2322  CG  PHE B 138      25.868  26.908  14.770  1.00 19.59           C  
ATOM   2323  CD1 PHE B 138      24.926  27.043  15.786  1.00 16.76           C  
ATOM   2324  CD2 PHE B 138      25.437  26.541  13.500  1.00 16.23           C  
ATOM   2325  CE1 PHE B 138      23.574  26.811  15.539  1.00 16.48           C  
ATOM   2326  CE2 PHE B 138      24.087  26.305  13.243  1.00 12.05           C  
ATOM   2327  CZ  PHE B 138      23.154  26.440  14.264  1.00 17.01           C  
ATOM   2328  N   ARG B 139      27.987  24.300  14.266  1.00 20.99           N  
ATOM   2329  CA  ARG B 139      27.656  23.009  13.678  1.00 24.68           C  
ATOM   2330  C   ARG B 139      28.128  21.859  14.561  1.00 28.64           C  
ATOM   2331  O   ARG B 139      27.432  20.856  14.714  1.00 34.76           O  
ATOM   2332  CB  ARG B 139      28.281  22.881  12.286  1.00 17.49           C  
ATOM   2333  CG  ARG B 139      27.850  23.964  11.305  1.00 28.85           C  
ATOM   2334  CD  ARG B 139      28.050  23.518   9.859  1.00 22.60           C  
ATOM   2335  NE  ARG B 139      29.443  23.209   9.552  1.00 29.87           N  
ATOM   2336  CZ  ARG B 139      30.399  24.120   9.405  1.00 30.52           C  
ATOM   2337  NH1 ARG B 139      30.119  25.410   9.534  1.00 40.70           N  
ATOM   2338  NH2 ARG B 139      31.640  23.741   9.134  1.00 33.89           N  
ATOM   2339  N   LYS B 140      29.311  22.013  15.146  1.00 31.61           N  
ATOM   2340  CA  LYS B 140      29.878  20.987  16.012  1.00 30.77           C  
ATOM   2341  C   LYS B 140      28.982  20.685  17.211  1.00 25.88           C  
ATOM   2342  O   LYS B 140      28.604  19.535  17.439  1.00 24.72           O  
ATOM   2343  CB  LYS B 140      31.260  21.421  16.506  1.00 34.10           C  
ATOM   2344  CG  LYS B 140      31.875  20.479  17.530  1.00 30.37           C  
ATOM   2345  CD  LYS B 140      33.136  21.073  18.133  1.00 50.43           C  
ATOM   2346  CE  LYS B 140      33.683  20.202  19.252  1.00 56.98           C  
ATOM   2347  NZ  LYS B 140      34.874  20.819  19.901  1.00 52.81           N  
ATOM   2348  N   ASP B 141      28.650  21.718  17.979  1.00 19.01           N  
ATOM   2349  CA  ASP B 141      27.809  21.539  19.154  1.00 27.60           C  
ATOM   2350  C   ASP B 141      26.387  21.117  18.800  1.00 23.74           C  
ATOM   2351  O   ASP B 141      25.730  20.432  19.581  1.00 30.67           O  
ATOM   2352  CB  ASP B 141      27.782  22.818  19.997  1.00 25.29           C  
ATOM   2353  CG  ASP B 141      29.143  23.162  20.573  1.00 32.18           C  
ATOM   2354  OD1 ASP B 141      29.878  22.228  20.958  1.00 31.28           O  
ATOM   2355  OD2 ASP B 141      29.475  24.364  20.651  1.00 26.91           O  
ATOM   2356  N   ILE B 142      25.913  21.524  17.627  1.00 26.42           N  
ATOM   2357  CA  ILE B 142      24.572  21.151  17.191  1.00 28.31           C  
ATOM   2358  C   ILE B 142      24.528  19.650  16.937  1.00 27.16           C  
ATOM   2359  O   ILE B 142      23.605  18.962  17.373  1.00 23.52           O  
ATOM   2360  CB  ILE B 142      24.164  21.907  15.901  1.00 24.63           C  
ATOM   2361  CG1 ILE B 142      23.414  23.186  16.271  1.00 34.84           C  
ATOM   2362  CG2 ILE B 142      23.294  21.022  15.013  1.00 39.22           C  
ATOM   2363  CD1 ILE B 142      22.106  22.938  17.002  1.00 34.21           C  
ATOM   2364  N   ALA B 143      25.535  19.149  16.228  1.00 20.83           N  
ATOM   2365  CA  ALA B 143      25.621  17.729  15.921  1.00 23.83           C  
ATOM   2366  C   ALA B 143      25.605  16.920  17.216  1.00 25.62           C  
ATOM   2367  O   ALA B 143      24.947  15.882  17.303  1.00 22.26           O  
ATOM   2368  CB  ALA B 143      26.894  17.445  15.140  1.00 30.03           C  
ATOM   2369  N   ALA B 144      26.333  17.406  18.219  1.00 24.56           N  
ATOM   2370  CA  ALA B 144      26.409  16.741  19.516  1.00 27.62           C  
ATOM   2371  C   ALA B 144      25.018  16.582  20.122  1.00 30.45           C  
ATOM   2372  O   ALA B 144      24.642  15.493  20.552  1.00 34.55           O  
ATOM   2373  CB  ALA B 144      27.306  17.535  20.458  1.00 24.32           C  
ATOM   2374  N   LYS B 145      24.263  17.678  20.154  1.00 31.68           N  
ATOM   2375  CA  LYS B 145      22.903  17.669  20.692  1.00 29.95           C  
ATOM   2376  C   LYS B 145      22.036  16.725  19.871  1.00 26.50           C  
ATOM   2377  O   LYS B 145      21.275  15.928  20.415  1.00 22.50           O  
ATOM   2378  CB  LYS B 145      22.311  19.081  20.664  1.00 19.51           C  
ATOM   2379  CG  LYS B 145      22.863  20.004  21.731  1.00 26.10           C  
ATOM   2380  CD  LYS B 145      22.237  19.714  23.085  1.00 25.25           C  
ATOM   2381  CE  LYS B 145      22.972  20.434  24.203  1.00 23.43           C  
ATOM   2382  NZ  LYS B 145      24.286  19.796  24.487  1.00 20.80           N  
ATOM   2383  N   TYR B 146      22.152  16.836  18.553  1.00 26.11           N  
ATOM   2384  CA  TYR B 146      21.415  15.985  17.627  1.00 22.55           C  
ATOM   2385  C   TYR B 146      21.497  14.547  18.113  1.00 27.84           C  
ATOM   2386  O   TYR B 146      20.490  13.907  18.427  1.00 21.27           O  
ATOM   2387  CB  TYR B 146      22.046  16.075  16.236  1.00 26.73           C  
ATOM   2388  CG  TYR B 146      21.213  16.806  15.211  1.00 26.37           C  
ATOM   2389  CD1 TYR B 146      20.585  18.011  15.520  1.00 25.44           C  
ATOM   2390  CD2 TYR B 146      21.077  16.307  13.918  1.00 33.48           C  
ATOM   2391  CE1 TYR B 146      19.843  18.701  14.562  1.00 29.72           C  
ATOM   2392  CE2 TYR B 146      20.339  16.990  12.952  1.00 28.20           C  
ATOM   2393  CZ  TYR B 146      19.727  18.187  13.283  1.00 28.51           C  
ATOM   2394  OH  TYR B 146      19.013  18.888  12.342  1.00 22.48           O  
ATOM   2395  N   LYS B 147      22.727  14.053  18.160  1.00 27.37           N  
ATOM   2396  CA  LYS B 147      23.009  12.702  18.611  1.00 32.78           C  
ATOM   2397  C   LYS B 147      22.494  12.525  20.034  1.00 32.78           C  
ATOM   2398  O   LYS B 147      22.008  11.458  20.410  1.00 31.73           O  
ATOM   2399  CB  LYS B 147      24.518  12.461  18.552  1.00 36.51           C  
ATOM   2400  CG  LYS B 147      25.010  11.252  19.315  1.00 48.82           C  
ATOM   2401  CD  LYS B 147      26.528  11.187  19.266  1.00 41.94           C  
ATOM   2402  CE  LYS B 147      27.063  10.221  20.300  1.00 56.72           C  
ATOM   2403  NZ  LYS B 147      26.654  10.639  21.669  1.00 57.72           N  
ATOM   2404  N   GLU B 148      22.601  13.594  20.814  1.00 38.68           N  
ATOM   2405  CA  GLU B 148      22.164  13.606  22.203  1.00 37.83           C  
ATOM   2406  C   GLU B 148      20.661  13.359  22.327  1.00 38.43           C  
ATOM   2407  O   GLU B 148      20.178  12.919  23.370  1.00 38.95           O  
ATOM   2408  CB  GLU B 148      22.513  14.957  22.829  1.00 46.30           C  
ATOM   2409  CG  GLU B 148      23.419  14.893  24.043  1.00 58.39           C  
ATOM   2410  CD  GLU B 148      23.774  16.273  24.558  1.00 56.86           C  
ATOM   2411  OE1 GLU B 148      24.383  17.051  23.794  1.00 59.35           O  
ATOM   2412  OE2 GLU B 148      23.438  16.582  25.721  1.00 69.02           O  
ATOM   2413  N   LEU B 149      19.927  13.637  21.255  1.00 35.12           N  
ATOM   2414  CA  LEU B 149      18.482  13.465  21.257  1.00 36.34           C  
ATOM   2415  C   LEU B 149      17.995  12.235  20.492  1.00 34.32           C  
ATOM   2416  O   LEU B 149      16.790  12.024  20.357  1.00 29.44           O  
ATOM   2417  CB  LEU B 149      17.820  14.728  20.706  1.00 41.17           C  
ATOM   2418  CG  LEU B 149      18.035  15.984  21.558  1.00 46.10           C  
ATOM   2419  CD1 LEU B 149      17.501  17.199  20.818  1.00 43.97           C  
ATOM   2420  CD2 LEU B 149      17.343  15.824  22.907  1.00 34.49           C  
ATOM   2421  N   GLY B 150      18.926  11.430  19.987  1.00 43.52           N  
ATOM   2422  CA  GLY B 150      18.542  10.224  19.270  1.00 40.31           C  
ATOM   2423  C   GLY B 150      18.772  10.225  17.769  1.00 41.33           C  
ATOM   2424  O   GLY B 150      18.120   9.473  17.043  1.00 42.02           O  
ATOM   2425  N   TYR B 151      19.690  11.057  17.293  1.00 43.24           N  
ATOM   2426  CA  TYR B 151      19.978  11.115  15.864  1.00 47.68           C  
ATOM   2427  C   TYR B 151      21.466  10.976  15.580  1.00 56.34           C  
ATOM   2428  O   TYR B 151      21.928   9.909  15.172  1.00 64.25           O  
ATOM   2429  CB  TYR B 151      19.453  12.423  15.264  1.00 54.62           C  
ATOM   2430  CG  TYR B 151      17.944  12.504  15.245  1.00 62.31           C  
ATOM   2431  CD1 TYR B 151      17.220  12.636  16.428  1.00 61.96           C  
ATOM   2432  CD2 TYR B 151      17.237  12.406  14.048  1.00 64.72           C  
ATOM   2433  CE1 TYR B 151      15.829  12.668  16.423  1.00 58.70           C  
ATOM   2434  CE2 TYR B 151      15.845  12.429  14.032  1.00 63.67           C  
ATOM   2435  CZ  TYR B 151      15.149  12.560  15.224  1.00 58.60           C  
ATOM   2436  OH  TYR B 151      13.774  12.568  15.218  1.00 59.47           O  
TER    2437      TYR B 151                                                      
HETATM 2438 FE   HME A 154       8.373  -7.904  19.778  1.00 17.92          FE  
HETATM 2439  NC  HME A 154       9.519  -6.605  18.517  1.00 22.29           N  
HETATM 2440  NB  HME A 154       9.102  -6.293  20.991  1.00 23.25           N  
HETATM 2441  NA  HME A 154       7.214  -9.154  21.164  1.00 15.97           N  
HETATM 2442  ND  HME A 154       7.609  -9.466  18.645  1.00 16.08           N  
HETATM 2443  C4C HME A 154       9.763  -6.743  17.188  1.00 22.54           C  
HETATM 2444  C3C HME A 154      10.616  -5.606  16.769  1.00 26.05           C  
HETATM 2445  C2C HME A 154      10.846  -4.821  17.880  1.00 26.84           C  
HETATM 2446  C1C HME A 154      10.135  -5.480  18.983  1.00 27.46           C  
HETATM 2447  C4B HME A 154       9.894  -5.279  20.410  1.00 15.78           C  
HETATM 2448  C3B HME A 154      10.230  -4.325  21.449  1.00 24.67           C  
HETATM 2449  C2B HME A 154       9.627  -4.788  22.618  1.00 24.85           C  
HETATM 2450  C1B HME A 154       8.923  -6.033  22.317  1.00 28.66           C  
HETATM 2451  CHB HME A 154       8.197  -6.797  23.285  1.00 15.59           C  
HETATM 2452  CHA HME A 154       7.424  -8.000  23.363  1.00 18.60           C  
HETATM 2453  C4A HME A 154       6.986  -9.025  22.499  1.00 22.37           C  
HETATM 2454  C3A HME A 154       6.163 -10.173  22.936  1.00 13.12           C  
HETATM 2455  C2A HME A 154       5.919 -10.959  21.836  1.00 10.75           C  
HETATM 2456  C1A HME A 154       6.603 -10.278  20.679  1.00 21.23           C  
HETATM 2457  C4D HME A 154       6.811 -10.462  19.222  1.00 16.87           C  
HETATM 2458  C3D HME A 154       6.435 -11.366  18.154  1.00 24.91           C  
HETATM 2459  C2D HME A 154       7.035 -10.883  16.988  1.00 19.83           C  
HETATM 2460  C1D HME A 154       7.775  -9.676  17.333  1.00 19.07           C  
HETATM 2461  CHD HME A 154       8.511  -8.919  16.380  1.00 22.96           C  
HETATM 2462  CHC HME A 154       9.309  -7.750  16.324  1.00 20.34           C  
HETATM 2463  CAC HME A 154      11.140  -5.354  15.351  1.00 24.71           C  
HETATM 2464  CBC HME A 154      10.239  -4.733  14.368  1.00 31.61           C  
HETATM 2465  CMC HME A 154      11.666  -3.564  17.883  1.00 26.84           C  
HETATM 2466  CMB HME A 154      11.049  -3.073  21.344  1.00 27.27           C  
HETATM 2467  CAB HME A 154       9.667  -4.130  24.009  1.00 19.00           C  
HETATM 2468  CBB HME A 154      10.702  -4.632  24.907  1.00 27.24           C  
HETATM 2469  CMA HME A 154       5.676 -10.426  24.356  1.00  3.97           C  
HETATM 2470  CAA HME A 154       5.081 -12.243  21.958  1.00 20.48           C  
HETATM 2471  CBA HME A 154       6.380 -13.201  21.689  1.00 16.22           C  
HETATM 2472  CGA HME A 154       6.401 -14.637  21.629  1.00 23.75           C  
HETATM 2473  O1A HME A 154       5.987 -15.428  22.554  1.00 20.49           O  
HETATM 2474  O2A HME A 154       6.853 -15.023  20.586  1.00 21.34           O  
HETATM 2475  CAD HME A 154       5.578 -12.579  18.251  1.00 19.78           C  
HETATM 2476  CBD HME A 154       4.040 -12.093  18.366  1.00 27.43           C  
HETATM 2477  CGD HME A 154       2.957 -12.960  19.099  1.00 23.84           C  
HETATM 2478  O1D HME A 154       1.794 -12.498  19.143  1.00 27.11           O  
HETATM 2479  O2D HME A 154       3.291 -14.085  19.620  1.00 26.07           O  
HETATM 2480  CMD HME A 154       6.954 -11.472  15.598  1.00 10.65           C  
HETATM 2481  N1  IMD A 155       6.285  -6.880  19.595  1.00 24.86           N  
HETATM 2482  C2  IMD A 155       5.031  -6.831  20.028  1.00 36.96           C  
HETATM 2483  N3  IMD A 155       4.366  -6.010  19.232  1.00 43.85           N  
HETATM 2484  C4  IMD A 155       5.204  -5.544  18.299  1.00 40.40           C  
HETATM 2485  C5  IMD A 155       6.439  -6.103  18.530  1.00 30.97           C  
HETATM 2486 FE   HME B 154      15.133  26.362  10.558  1.00 19.29          FE  
HETATM 2487  NC  HME B 154      16.571  25.570   9.147  1.00 20.08           N  
HETATM 2488  NB  HME B 154      17.025  27.158  11.065  1.00 27.06           N  
HETATM 2489  NA  HME B 154      13.726  27.069  12.078  1.00 11.75           N  
HETATM 2490  ND  HME B 154      13.275  25.482  10.118  1.00 22.62           N  
HETATM 2491  C4C HME B 154      16.364  24.719   8.108  1.00 17.48           C  
HETATM 2492  C3C HME B 154      17.661  24.516   7.425  1.00 21.61           C  
HETATM 2493  C2C HME B 154      18.606  25.272   8.088  1.00 33.02           C  
HETATM 2494  C1C HME B 154      17.885  25.935   9.184  1.00 33.92           C  
HETATM 2495  C4B HME B 154      18.163  26.861  10.282  1.00 28.69           C  
HETATM 2496  C3B HME B 154      19.288  27.592  10.834  1.00 24.33           C  
HETATM 2497  C2B HME B 154      18.791  28.306  11.929  1.00 18.18           C  
HETATM 2498  C1B HME B 154      17.364  28.019  12.064  1.00 28.37           C  
HETATM 2499  CHB HME B 154      16.524  28.569  13.084  1.00 21.71           C  
HETATM 2500  CHA HME B 154      15.151  28.522  13.515  1.00 22.79           C  
HETATM 2501  C4A HME B 154      13.941  27.905  13.124  1.00 11.92           C  
HETATM 2502  C3A HME B 154      12.653  28.090  13.832  1.00 12.26           C  
HETATM 2503  C2A HME B 154      11.697  27.351  13.169  1.00 13.61           C  
HETATM 2504  C1A HME B 154      12.416  26.692  12.020  1.00 21.74           C  
HETATM 2505  C4D HME B 154      12.135  25.792  10.878  1.00 25.73           C  
HETATM 2506  C3D HME B 154      11.025  25.101  10.268  1.00 24.81           C  
HETATM 2507  C2D HME B 154      11.536  24.402   9.177  1.00 22.71           C  
HETATM 2508  C1D HME B 154      12.969  24.661   9.109  1.00 19.21           C  
HETATM 2509  CHD HME B 154      13.806  24.101   8.106  1.00 28.07           C  
HETATM 2510  CHC HME B 154      15.164  24.117   7.710  1.00 15.34           C  
HETATM 2511  CAC HME B 154      17.901  23.630   6.198  1.00 23.18           C  
HETATM 2512  CBC HME B 154      17.600  24.178   4.868  1.00 42.27           C  
HETATM 2513  CMC HME B 154      20.055  25.347   7.705  1.00 43.14           C  
HETATM 2514  CMB HME B 154      20.713  27.615  10.364  1.00 26.15           C  
HETATM 2515  CAB HME B 154      19.576  29.247  12.861  1.00 30.05           C  
HETATM 2516  CBB HME B 154      20.139  28.607  14.056  1.00 40.16           C  
HETATM 2517  CMA HME B 154      12.440  28.949  15.066  1.00  4.87           C  
HETATM 2518  CAA HME B 154      10.231  27.327  13.655  1.00 25.65           C  
HETATM 2519  CBA HME B 154      10.363  25.770  14.146  1.00 25.22           C  
HETATM 2520  CGA HME B 154       9.353  24.938  14.742  1.00 36.31           C  
HETATM 2521  O1A HME B 154       8.657  25.230  15.784  1.00 35.70           O  
HETATM 2522  O2A HME B 154       9.227  23.909  14.135  1.00 33.56           O  
HETATM 2523  CAD HME B 154       9.602  25.131  10.695  1.00 22.55           C  
HETATM 2524  CBD HME B 154       8.994  26.538  10.174  1.00 34.62           C  
HETATM 2525  CGD HME B 154       7.735  27.204  10.830  1.00 27.30           C  
HETATM 2526  O1D HME B 154       7.360  28.296  10.346  1.00 39.73           O  
HETATM 2527  O2D HME B 154       7.147  26.629  11.816  1.00 39.83           O  
HETATM 2528  CMD HME B 154      10.780  23.526   8.211  1.00 21.03           C  
HETATM 2529  N1  IMD B 155      13.911  28.025   9.239  1.00 53.55           N  
HETATM 2530  C2  IMD B 155      13.281  29.184   9.402  1.00 58.27           C  
HETATM 2531  N3  IMD B 155      13.652  29.977   8.409  1.00 54.95           N  
HETATM 2532  C4  IMD B 155      14.511  29.316   7.627  1.00 58.39           C  
HETATM 2533  C5  IMD B 155      14.682  28.060   8.159  1.00 55.89           C  
HETATM 2534  O   HOH A 156      -2.258  12.694  23.720  1.00 21.77           O  
HETATM 2535  O   HOH A 157      -6.630  -3.781   7.982  1.00  9.00           O  
HETATM 2536  O   HOH A 158      -2.448  -7.137  22.312  1.00 13.36           O  
HETATM 2537  O   HOH A 159       9.963  -9.636  29.804  1.00 19.90           O  
HETATM 2538  O   HOH A 160      16.902   5.513  21.302  1.00 33.38           O  
HETATM 2539  O   HOH A 161      20.836   6.213  20.362  1.00 27.91           O  
HETATM 2540  O   HOH A 162      16.747  -8.674  37.623  1.00 30.62           O  
HETATM 2541  O   HOH A 163      -4.066  -0.784  13.529  1.00 16.11           O  
HETATM 2542  O   HOH A 164      -1.494  -0.142  19.051  1.00 24.29           O  
HETATM 2543  O   HOH A 165      -5.181   8.435  19.733  1.00 30.08           O  
HETATM 2544  O   HOH A 166      22.001   0.515  19.120  1.00 24.68           O  
HETATM 2545  O   HOH A 167      23.551  -2.092  32.300  1.00 20.13           O  
HETATM 2546  O   HOH A 168      -7.704   7.426  22.133  1.00 28.73           O  
HETATM 2547  O   HOH A 169      18.978  -3.922   8.817  1.00 30.81           O  
HETATM 2548  O   HOH A 170       8.993   3.215  38.751  1.00 34.96           O  
HETATM 2549  O   HOH A 171      16.889   3.092  39.315  1.00 18.40           O  
HETATM 2550  O   HOH A 172       3.124  -1.096  30.853  1.00 20.04           O  
HETATM 2551  O   HOH A 173      -0.172  -9.196  -0.826  1.00 53.22           O  
HETATM 2552  O   HOH A 174      23.948  -9.749  17.558  1.00 52.28           O  
HETATM 2553  O   HOH A 175      12.304  -8.175   8.294  1.00 22.99           O  
HETATM 2554  O   HOH A 176      20.177  -3.317  37.154  1.00 28.44           O  
HETATM 2555  O   HOH A 177      -3.686   6.570  16.278  1.00 36.45           O  
HETATM 2556  O   HOH A 178      21.939 -13.139  35.015  1.00 30.14           O  
HETATM 2557  O   HOH A 179      25.988   6.622  25.585  1.00 29.92           O  
HETATM 2558  O   HOH A 180       5.637   1.304   4.513  1.00 32.50           O  
HETATM 2559  O   HOH A 181      12.634  15.628  37.469  1.00 28.45           O  
HETATM 2560  O   HOH A 182     -11.724  -7.545  16.168  1.00 42.16           O  
HETATM 2561  O   HOH A 183       7.944  14.450  15.538  1.00 44.64           O  
HETATM 2562  O   HOH A 184      -5.756  -7.769  11.643  1.00 41.64           O  
HETATM 2563  O   HOH A 185       7.239  10.634  36.498  1.00 34.36           O  
HETATM 2564  O   HOH A 186      -3.477   1.603  29.627  1.00 24.88           O  
HETATM 2565  O   HOH A 187      19.811   2.116  37.127  1.00 32.23           O  
HETATM 2566  O   HOH A 188      20.631   4.087  34.147  1.00 29.90           O  
HETATM 2567  O   HOH A 189      11.891 -16.578  12.930  1.00 32.38           O  
HETATM 2568  O   HOH A 190      24.728   2.963  31.176  1.00 31.65           O  
HETATM 2569  O   HOH A 191      -2.513  10.764  16.922  1.00 27.28           O  
HETATM 2570  O   HOH A 192       5.221   5.119  33.254  1.00 30.43           O  
HETATM 2571  O   HOH A 193      17.522   6.360  39.098  1.00 42.46           O  
HETATM 2572  O   HOH A 194      10.268  18.862  29.248  1.00 39.58           O  
HETATM 2573  O   HOH A 195      -0.340 -14.439  13.107  1.00 28.58           O  
HETATM 2574  O   HOH A 196      -4.455   9.330  15.185  1.00 55.04           O  
HETATM 2575  O   HOH A 197      12.785  -1.832  13.311  1.00 36.90           O  
HETATM 2576  O   HOH A 198       2.663   7.043  12.570  1.00 23.65           O  
HETATM 2577  O   HOH A 199      -6.970  -4.895  18.335  1.00 40.50           O  
HETATM 2578  O   HOH A 200      21.813 -13.759  32.027  1.00 46.87           O  
HETATM 2579  O   HOH A 201      -9.599   0.620  12.955  1.00 43.62           O  
HETATM 2580  O   HOH A 202      14.055  21.099  27.623  1.00 37.12           O  
HETATM 2581  O   HOH A 203      18.315  -5.625  37.232  1.00 26.98           O  
HETATM 2582  O   HOH A 204      10.482  20.867  18.706  1.00 21.98           O  
HETATM 2583  O   HOH A 205      26.342  -9.791  13.509  1.00 28.86           O  
HETATM 2584  O   HOH A 206      22.590   8.714  21.617  1.00 33.57           O  
HETATM 2585  O   HOH A 207      -1.815   7.500  32.968  1.00 46.88           O  
HETATM 2586  O   HOH A 208      -2.871 -13.358  13.408  1.00 44.13           O  
HETATM 2587  O   HOH A 209      18.005 -11.373  12.091  1.00 36.90           O  
HETATM 2588  O   HOH A 210      24.883 -19.080  18.461  1.00 26.04           O  
HETATM 2589  O   HOH A 211      -2.036   8.580   3.747  1.00 38.17           O  
HETATM 2590  O   HOH A 212      21.903   3.804  38.475  1.00 35.33           O  
HETATM 2591  O   HOH A 213       3.675   7.491  10.266  1.00 38.90           O  
HETATM 2592  O   HOH A 214     -10.737  -2.379  12.144  1.00 38.29           O  
HETATM 2593  O   HOH A 215       4.841   9.555  35.985  1.00 42.46           O  
HETATM 2594  O   HOH A 216      -9.298  -5.349  20.331  1.00 36.75           O  
HETATM 2595  O   HOH A 217       1.980 -10.408  21.686  1.00 29.64           O  
HETATM 2596  O   HOH A 218       8.922   9.005  38.273  1.00 36.23           O  
HETATM 2597  O   HOH A 219      10.748 -15.993  25.703  1.00 26.62           O  
HETATM 2598  O   HOH A 220      22.869 -12.156  37.352  1.00 46.08           O  
HETATM 2599  O   HOH A 221      31.312  -8.381  21.149  1.00 37.53           O  
HETATM 2600  O   HOH A 222      16.705  13.398  40.842  1.00 50.88           O  
HETATM 2601  O   HOH A 223       5.437  15.004  13.499  1.00 45.59           O  
HETATM 2602  O   HOH A 224      20.182   2.660   9.362  1.00 39.72           O  
HETATM 2603  O   HOH A 225      20.534  -1.543  33.215  1.00 19.48           O  
HETATM 2604  O   HOH A 226      15.294  -6.276  39.152  1.00 29.86           O  
HETATM 2605  O   HOH A 227       7.502  -6.641  29.597  1.00 17.80           O  
HETATM 2606  O   HOH A 228      -1.553  -9.766  21.436  1.00 33.53           O  
HETATM 2607  O   HOH A 229      24.808   8.298  30.236  1.00 45.65           O  
HETATM 2608  O   HOH A 230      11.420   4.540  12.112  1.00 49.53           O  
HETATM 2609  O   HOH A 231       8.863  20.367  24.011  1.00 66.76           O  
HETATM 2610  O   HOH A 232      20.728  -5.263  32.384  1.00 38.66           O  
HETATM 2611  O   HOH A 233      22.664 -19.080  12.975  1.00 39.00           O  
HETATM 2612  O   HOH A 234      26.538   6.256  30.766  1.00 38.55           O  
HETATM 2613  O   HOH A 235      24.859  -8.960  20.364  1.00 50.03           O  
HETATM 2614  O   HOH A 236      18.646  14.053  29.639  1.00 40.62           O  
HETATM 2615  O   HOH A 237       4.357  11.878  37.937  1.00 59.85           O  
HETATM 2616  O   HOH A 238      16.202   0.976  29.880  1.00 38.18           O  
HETATM 2617  O   HOH A 239      -5.456   2.261  24.508  1.00 18.41           O  
HETATM 2618  O   HOH A 240      17.878   8.785  43.404  1.00 47.65           O  
HETATM 2619  O   HOH A 241      -0.369   7.294  11.912  1.00 27.79           O  
HETATM 2620  O   HOH A 242      20.055 -21.123  12.555  1.00 36.50           O  
HETATM 2621  O   HOH A 243       9.610  -5.316  32.273  1.00 54.82           O  
HETATM 2622  O   HOH A 244      19.146  16.021  37.954  1.00 44.35           O  
HETATM 2623  O   HOH A 245      25.728 -19.245  23.595  1.00 48.03           O  
HETATM 2624  O   HOH A 246      -3.624 -13.848  16.718  1.00 43.23           O  
HETATM 2625  O   HOH A 247      19.045  -5.164  40.060  1.00 42.33           O  
HETATM 2626  O   HOH A 248       5.228  12.385  10.198  1.00 45.14           O  
HETATM 2627  O   HOH A 249      16.523  11.239  44.733  1.00 40.63           O  
HETATM 2628  O   HOH A 250      21.367 -15.354  13.336  1.00 38.87           O  
HETATM 2629  O   HOH A 251      20.126  16.091  33.613  1.00 64.35           O  
HETATM 2630  O   HOH A 252       8.701 -13.302  13.261  1.00 37.59           O  
HETATM 2631  O   HOH A 253      17.619  -6.776   7.851  1.00 31.02           O  
HETATM 2632  O   HOH A 254       8.550   7.241  42.184  1.00 55.20           O  
HETATM 2633  O   HOH A 255      -8.159   1.975  15.799  1.00 26.87           O  
HETATM 2634  O   HOH A 256      -6.121  -0.571  25.071  1.00 42.70           O  
HETATM 2635  O   HOH A 257      -4.259   5.546  32.344  1.00 55.36           O  
HETATM 2636  O   HOH A 258      15.365  17.010  38.846  1.00 42.58           O  
HETATM 2637  O   HOH A 259       6.673   9.336  40.507  1.00 33.40           O  
HETATM 2638  O   HOH A 260       3.303  10.385  13.573  1.00 48.57           O  
HETATM 2639  O   HOH A 261       0.891  11.812  12.481  1.00 38.92           O  
HETATM 2640  O   HOH A 262       0.177  13.064  16.510  1.00 46.36           O  
HETATM 2641  O   HOH A 263       1.929  11.896   3.199  1.00 37.05           O  
HETATM 2642  O   HOH A 264       4.891   8.763   3.448  1.00 33.39           O  
HETATM 2643  O   HOH A 265      -0.158   5.230   2.282  1.00 30.39           O  
HETATM 2644  O   HOH A 266       1.127  10.760   7.695  1.00 44.84           O  
HETATM 2645  O   HOH A 267      22.066  -7.139  14.496  1.00 53.42           O  
HETATM 2646  O   HOH A 268      22.894  13.118  34.041  1.00 31.22           O  
HETATM 2647  O   HOH A 269      19.164  11.698  41.940  1.00 46.57           O  
HETATM 2648  O   HOH A 270      18.764   3.071  42.181  1.00 49.03           O  
HETATM 2649  O   HOH A 271      21.723  14.883  36.058  1.00 44.35           O  
HETATM 2650  O   HOH A 272      -0.697 -14.620  17.351  1.00 50.12           O  
HETATM 2651  O   HOH A 273      -1.231  11.002   5.601  1.00 47.40           O  
HETATM 2652  O   HOH A 274      -1.495 -12.343   5.716  1.00 50.65           O  
HETATM 2653  O   HOH A 275      -9.946  -8.373  17.914  1.00 33.50           O  
HETATM 2654  O   HOH A 276      24.696   0.425  20.759  1.00 36.84           O  
HETATM 2655  O   HOH A 277      23.214  14.771  31.843  1.00 33.25           O  
HETATM 2656  O   HOH A 278      -9.438   4.582  15.576  1.00 44.69           O  
HETATM 2657  O   HOH A 279      22.400   3.913  29.638  1.00 53.02           O  
HETATM 2658  O   HOH A 280       4.591  11.823   4.741  1.00 44.72           O  
HETATM 2659  O   HOH A 281       5.278  12.531  40.391  1.00 36.79           O  
HETATM 2660  O   HOH A 282      -3.899 -15.627  13.154  1.00 42.04           O  
HETATM 2661  O   HOH A 283      10.693   2.557  41.515  1.00 31.16           O  
HETATM 2662  O   HOH B 156      10.062  35.793  10.282  1.00 11.86           O  
HETATM 2663  O   HOH B 157      30.347  29.318  -1.925  1.00 37.63           O  
HETATM 2664  O   HOH B 158      10.222  26.461  17.547  1.00 18.06           O  
HETATM 2665  O   HOH B 159      32.569  22.445  21.696  1.00 24.65           O  
HETATM 2666  O   HOH B 160      26.331  41.437  16.938  1.00 23.54           O  
HETATM 2667  O   HOH B 161      18.453  31.859  18.901  1.00 31.47           O  
HETATM 2668  O   HOH B 162      23.556  26.380  29.250  1.00 30.14           O  
HETATM 2669  O   HOH B 163      38.362  42.127  23.290  1.00 31.46           O  
HETATM 2670  O   HOH B 164      26.083  20.585  22.445  1.00 20.76           O  
HETATM 2671  O   HOH B 165       7.224  35.880  -4.432  1.00 38.97           O  
HETATM 2672  O   HOH B 166      13.556  10.049  15.250  1.00 27.31           O  
HETATM 2673  O   HOH B 167      17.069  28.393  20.768  1.00 26.52           O  
HETATM 2674  O   HOH B 168      35.790  27.005  15.816  1.00 31.80           O  
HETATM 2675  O   HOH B 169      17.077  20.171  29.455  1.00 35.07           O  
HETATM 2676  O   HOH B 170      11.973  22.468  20.284  1.00 29.75           O  
HETATM 2677  O   HOH B 171      20.236  33.336 -10.952  1.00 31.62           O  
HETATM 2678  O   HOH B 172      21.995  17.961  27.745  1.00 40.65           O  
HETATM 2679  O   HOH B 173      17.479  44.986   9.475  1.00 34.20           O  
HETATM 2680  O   HOH B 174      28.197  42.532  -4.598  1.00 33.65           O  
HETATM 2681  O   HOH B 175      21.814  35.043  -3.226  1.00 25.07           O  
HETATM 2682  O   HOH B 176      36.551  40.722   1.927  1.00 45.87           O  
HETATM 2683  O   HOH B 177      28.160  31.287  20.310  1.00 17.74           O  
HETATM 2684  O   HOH B 178      15.417  44.002   7.409  1.00 29.88           O  
HETATM 2685  O   HOH B 179      14.648  26.512  19.429  1.00 24.48           O  
HETATM 2686  O   HOH B 180      18.874  44.349   0.326  1.00 34.30           O  
HETATM 2687  O   HOH B 181       6.365  32.926  -1.604  1.00 26.87           O  
HETATM 2688  O   HOH B 182      12.762  25.349  17.836  1.00 16.56           O  
HETATM 2689  O   HOH B 183      33.747  49.238  10.564  1.00 40.24           O  
HETATM 2690  O   HOH B 184       7.890  22.886  17.661  1.00 39.84           O  
HETATM 2691  O   HOH B 185      25.562  11.310  24.193  1.00 34.67           O  
HETATM 2692  O   HOH B 186      10.273  16.447   8.018  1.00 70.96           O  
HETATM 2693  O   HOH B 187      21.992  19.206  30.099  1.00 35.24           O  
HETATM 2694  O   HOH B 188      30.120  17.221  17.701  1.00 59.97           O  
HETATM 2695  O   HOH B 189      30.739  35.393  -2.461  1.00 29.16           O  
HETATM 2696  O   HOH B 190      39.039  29.422   7.165  1.00 45.87           O  
HETATM 2697  O   HOH B 191       6.068  22.557   8.041  1.00 40.44           O  
HETATM 2698  O   HOH B 192      11.890  37.376  -0.043  1.00 22.50           O  
HETATM 2699  O   HOH B 193      17.226  29.606  18.535  1.00 23.52           O  
HETATM 2700  O   HOH B 194      23.095  29.355  27.319  1.00 23.03           O  
HETATM 2701  O   HOH B 195      11.892  41.020  -6.365  1.00 24.30           O  
HETATM 2702  O   HOH B 196       7.512  19.831  -1.552  1.00 45.50           O  
HETATM 2703  O   HOH B 197      17.147  18.566  31.932  1.00 26.51           O  
HETATM 2704  O   HOH B 198       8.772  22.770  -2.505  1.00 55.85           O  
HETATM 2705  O   HOH B 199      23.539  20.576  -5.421  1.00 46.53           O  
HETATM 2706  O   HOH B 200      38.302  48.053   6.047  1.00 37.02           O  
HETATM 2707  O   HOH B 201      31.441  30.328   0.300  1.00 30.76           O  
HETATM 2708  O   HOH B 202       4.393  34.272  -0.014  1.00 38.46           O  
HETATM 2709  O   HOH B 203      10.033  20.471   7.390  1.00 37.99           O  
HETATM 2710  O   HOH B 204      15.523  32.937  18.202  1.00 27.87           O  
HETATM 2711  O   HOH B 205       9.802  30.282  11.810  1.00 25.09           O  
HETATM 2712  O   HOH B 206       7.868  21.195   2.573  1.00 45.73           O  
HETATM 2713  O   HOH B 207      31.981  42.411  24.018  1.00 45.86           O  
HETATM 2714  O   HOH B 208      24.257  18.652  31.405  1.00 38.97           O  
HETATM 2715  O   HOH B 209      32.482  47.018   2.970  1.00 47.48           O  
HETATM 2716  O   HOH B 210      22.058  19.825  32.704  1.00 37.95           O  
HETATM 2717  O   HOH B 211      29.841  23.797   2.652  1.00 51.67           O  
HETATM 2718  O   HOH B 212      16.400  13.589  11.304  1.00 38.89           O  
HETATM 2719  O   HOH B 213      29.466  29.139  17.918  1.00 34.03           O  
HETATM 2720  O   HOH B 214      27.954  46.776   2.629  1.00 47.82           O  
HETATM 2721  O   HOH B 215      17.372   8.745  12.846  1.00 28.85           O  
HETATM 2722  O   HOH B 216      12.719  43.029  -1.373  1.00 46.78           O  
HETATM 2723  O   HOH B 217      33.138  33.620  25.560  1.00 24.75           O  
HETATM 2724  O   HOH B 218      29.940  46.322   5.047  1.00 49.08           O  
HETATM 2725  O   HOH B 219      28.108  45.572  -4.687  1.00 42.64           O  
HETATM 2726  O   HOH B 220      31.595  27.328   5.823  1.00 35.64           O  
HETATM 2727  O   HOH B 221       5.946  32.277   5.759  1.00 47.36           O  
HETATM 2728  O   HOH B 222      32.314  21.150  13.221  1.00 36.18           O  
HETATM 2729  O   HOH B 223      31.938  41.851  20.533  1.00 45.63           O  
HETATM 2730  O   HOH B 224       8.298  22.529   6.308  1.00 49.76           O  
HETATM 2731  O   HOH B 225       6.896  18.053   7.183  1.00 53.79           O  
HETATM 2732  O   HOH B 226       9.750  42.751  -6.304  1.00 36.02           O  
HETATM 2733  O   HOH B 227      29.091  42.971  21.226  1.00 41.95           O  
HETATM 2734  O   HOH B 228      36.710  30.492   2.528  1.00 46.52           O  
HETATM 2735  O   HOH B 229      42.121  45.895   3.661  1.00 46.05           O  
HETATM 2736  O   HOH B 230      19.353  20.503  33.221  1.00 56.15           O  
HETATM 2737  O   HOH B 231      14.348  30.235  18.364  1.00 45.43           O  
HETATM 2738  O   HOH B 232      33.014  24.659   6.505  1.00 46.49           O  
HETATM 2739  O   HOH B 233      23.504  10.918  13.373  1.00 48.94           O  
HETATM 2740  O   HOH B 234      22.523  22.271  30.285  1.00 55.89           O  
HETATM 2741  O   HOH B 235      18.759  44.002  -2.677  1.00 59.10           O  
HETATM 2742  O   HOH B 236      17.943  40.777  -1.419  1.00 60.91           O  
HETATM 2743  O   HOH B 237       3.068  31.148   6.168  1.00 51.66           O  
HETATM 2744  O   HOH B 238       9.814  32.300   9.003  1.00 48.92           O  
HETATM 2745  O   HOH B 239      40.778  48.964   7.831  1.00 32.02           O  
HETATM 2746  O   HOH B 240       9.467  43.636   7.269  1.00 45.82           O  
HETATM 2747  O   HOH B 241      20.083  10.204  11.292  1.00 48.59           O  
HETATM 2748  O   HOH B 242      43.509  28.468   8.519  1.00 50.72           O  
HETATM 2749  O   HOH B 243      45.039  29.427  10.908  1.00 43.07           O  
HETATM 2750  O   HOH B 244      41.635  30.786   8.917  1.00 38.12           O  
HETATM 2751  O   HOH B 245      44.283  25.955   8.851  1.00 49.51           O  
HETATM 2752  O   HOH B 246       5.425  28.323   5.258  1.00 52.22           O  
HETATM 2753  O   HOH B 247      39.077  29.544  11.518  1.00 40.99           O  
HETATM 2754  O   HOH B 248      39.201  36.517   0.209  1.00 45.34           O  
HETATM 2755  O   HOH B 249       4.081  18.527   6.428  1.00 43.60           O  
HETATM 2756  O   HOH B 250      21.521   9.475   8.900  1.00 43.64           O  
HETATM 2757  O   HOH B 251      42.812  47.329   6.695  1.00 39.80           O  
HETATM 2758  O   HOH B 252       7.965  18.835   3.970  1.00 36.03           O  
CONECT  740 2438                                                                
CONECT 1965 2486                                                                
CONECT 2438  740 2439 2440 2441                                                 
CONECT 2438 2442 2481                                                           
CONECT 2439 2438 2443 2446                                                      
CONECT 2440 2438 2447 2450                                                      
CONECT 2441 2438 2453 2456                                                      
CONECT 2442 2438 2457 2460                                                      
CONECT 2443 2439 2444 2462                                                      
CONECT 2444 2443 2445 2463                                                      
CONECT 2445 2444 2446 2465                                                      
CONECT 2446 2439 2445 2447                                                      
CONECT 2447 2440 2446 2448                                                      
CONECT 2448 2447 2449 2466                                                      
CONECT 2449 2448 2450 2467                                                      
CONECT 2450 2440 2449 2451                                                      
CONECT 2451 2450 2452                                                           
CONECT 2452 2451 2453                                                           
CONECT 2453 2441 2452 2454                                                      
CONECT 2454 2453 2455 2469                                                      
CONECT 2455 2454 2456 2470                                                      
CONECT 2456 2441 2455 2457                                                      
CONECT 2457 2442 2456 2458                                                      
CONECT 2458 2457 2459 2475                                                      
CONECT 2459 2458 2460 2480                                                      
CONECT 2460 2442 2459 2461                                                      
CONECT 2461 2460 2462                                                           
CONECT 2462 2443 2461                                                           
CONECT 2463 2444 2464                                                           
CONECT 2464 2463                                                                
CONECT 2465 2445                                                                
CONECT 2466 2448                                                                
CONECT 2467 2449 2468                                                           
CONECT 2468 2467                                                                
CONECT 2469 2454                                                                
CONECT 2470 2455 2471                                                           
CONECT 2471 2470 2472                                                           
CONECT 2472 2471 2473 2474                                                      
CONECT 2473 2472                                                                
CONECT 2474 2472                                                                
CONECT 2475 2458 2476                                                           
CONECT 2476 2475 2477                                                           
CONECT 2477 2476 2478 2479                                                      
CONECT 2478 2477                                                                
CONECT 2479 2477                                                                
CONECT 2480 2459                                                                
CONECT 2481 2438 2482 2485                                                      
CONECT 2482 2481 2483                                                           
CONECT 2483 2482 2484                                                           
CONECT 2484 2483 2485                                                           
CONECT 2485 2481 2484                                                           
CONECT 2486 1965 2487 2488 2489                                                 
CONECT 2486 2490 2529                                                           
CONECT 2487 2486 2491 2494                                                      
CONECT 2488 2486 2495 2498                                                      
CONECT 2489 2486 2501 2504                                                      
CONECT 2490 2486 2505 2508                                                      
CONECT 2491 2487 2492 2510                                                      
CONECT 2492 2491 2493 2511                                                      
CONECT 2493 2492 2494 2513                                                      
CONECT 2494 2487 2493 2495                                                      
CONECT 2495 2488 2494 2496                                                      
CONECT 2496 2495 2497 2514                                                      
CONECT 2497 2496 2498 2515                                                      
CONECT 2498 2488 2497 2499                                                      
CONECT 2499 2498 2500                                                           
CONECT 2500 2499 2501                                                           
CONECT 2501 2489 2500 2502                                                      
CONECT 2502 2501 2503 2517                                                      
CONECT 2503 2502 2504 2518                                                      
CONECT 2504 2489 2503 2505                                                      
CONECT 2505 2490 2504 2506                                                      
CONECT 2506 2505 2507 2523                                                      
CONECT 2507 2506 2508 2528                                                      
CONECT 2508 2490 2507 2509                                                      
CONECT 2509 2508 2510                                                           
CONECT 2510 2491 2509                                                           
CONECT 2511 2492 2512                                                           
CONECT 2512 2511                                                                
CONECT 2513 2493                                                                
CONECT 2514 2496                                                                
CONECT 2515 2497 2516                                                           
CONECT 2516 2515                                                                
CONECT 2517 2502                                                                
CONECT 2518 2503 2519                                                           
CONECT 2519 2518 2520                                                           
CONECT 2520 2519 2521 2522                                                      
CONECT 2521 2520                                                                
CONECT 2522 2520                                                                
CONECT 2523 2506 2524                                                           
CONECT 2524 2523 2525                                                           
CONECT 2525 2524 2526 2527                                                      
CONECT 2526 2525                                                                
CONECT 2527 2525                                                                
CONECT 2528 2507                                                                
CONECT 2529 2486 2530 2533                                                      
CONECT 2530 2529 2531                                                           
CONECT 2531 2530 2532                                                           
CONECT 2532 2531 2533                                                           
CONECT 2533 2529 2532                                                           
MASTER      288    0    4   17    0    0   11    6 2756    2  100   24          
END                                                                             



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