CNRS Nantes University UFIP UFIP
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***  3zyc_chainA  ***

elNémo ID: 190813194351122834

Job options:

ID        	=	 190813194351122834
JOBID     	=	 3zyc_chainA
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 3zyc_chainA

HEADER    HYDROLASE                               22-AUG-11   3ZYC              
TITLE     DYNAMIN 1 GTPASE GED FUSION DIMER COMPLEXED WITH GMPPCP               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DYNAMIN-1;                                                 
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: GTPASE DOMAIN, RESIDUES 6-320, GTPASE EFFECTOR DOMAIN,     
COMPND   5 RESIDUES 726-750;                                                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    HYDROLASE, MEMBRANE FISSION, NUCLEOTIDE-BINDING, ENDOCYTOSIS, MOTOR   
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.CHAPPIE,J.A.MEARS,S.FANG,M.LEONARD,S.L.SCHMID,R.A.MILLIGAN,       
AUTHOR   2 J.E.HINSHAW,F.DYDA                                                   
REVDAT   4   15-MAY-19 3ZYC    1       REMARK                                   
REVDAT   3   08-MAY-19 3ZYC    1       REMARK                                   
REVDAT   2   28-JUN-17 3ZYC    1       REMARK                                   
REVDAT   1   12-OCT-11 3ZYC    0                                                
JRNL        AUTH   J.S.CHAPPIE,J.A.MEARS,S.FANG,M.LEONARD,S.L.SCHMID,           
JRNL        AUTH 2 R.A.MILLIGAN,J.E.HINSHAW,F.DYDA                              
JRNL        TITL   A PSEUDOATOMIC MODEL OF THE DYNAMIN POLYMER IDENTIFIES A     
JRNL        TITL 2 HYDROLYSIS-DEPENDENT POWERSTROKE.                            
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 147   209 2011              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   21962517                                                     
JRNL        DOI    10.1016/J.CELL.2011.09.003                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.3                                              
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 34188                          
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) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 941                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5240                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 413                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.16700                                             
REMARK   3    B22 (A**2) : 2.89700                                              
REMARK   3    B33 (A**2) : 0.27000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 6.70000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.140                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 18.51                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : GMPPCP.PARAM                                   
REMARK   3  PARAMETER FILE  3  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : GMPPCP.TOP                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH19_MOD.SOL                                 
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ZYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290049416.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MULTILAYER MIRROR                  
REMARK 200  OPTICS                         : CONFOCAL                           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU-MSC SATURN 200              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34206                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.270                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.2300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.57                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.950                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2X2E                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: GGGMPPCP WAS CRYSTALLIZED BY SITTING     
REMARK 280  DROP VAPOR DIFFUSION IN 0.1M HEPES PH 7.0, 200 MM MGCL2, AND 24-    
REMARK 280  30% PEG 2000 MME USING A DROP SIZE OF 3 MICROL AND RESERVOIR        
REMARK 280  VOLUME OF 65 MICROL. CRYSTALS GREW IN 3-5 DAYS AT 20C. THE          
REMARK 280  ADDITION OF 200 MM LICL, NACL, KCL, OR NH4CL TO THE RESERVOIR       
REMARK 280  SOLUTION DRAMATICALLY IMPROVED THE CRYSTALS. CRYSTALS GROWN IN      
REMARK 280  THE PRESENCE OF KCL SHOWED THE BEST DIFFRACTION., VAPOR             
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
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       41.31750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     GLU A   313                                                      
REMARK 465     TYR A   314                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     ASN A   316                                                      
REMARK 465     PHE A   317                                                      
REMARK 465     ARG A   318                                                      
REMARK 465     PRO A   319                                                      
REMARK 465     ASP A   320                                                      
REMARK 465     LYS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     GLY A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     ASP A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     ARG A   327                                                      
REMARK 465     VAL A   328                                                      
REMARK 465     THR A   749                                                      
REMARK 465     VAL A   750                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     PHE D     4                                                      
REMARK 465     ASP D   320                                                      
REMARK 465     LYS D   321                                                      
REMARK 465     HIS D   322                                                      
REMARK 465     GLY D   323                                                      
REMARK 465     THR D   324                                                      
REMARK 465     ASP D   325                                                      
REMARK 465     SER D   326                                                      
REMARK 465     THR D   749                                                      
REMARK 465     VAL D   750                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  56       -7.81   -147.13                                   
REMARK 500    VAL A  64      -68.11   -109.45                                   
REMARK 500    ASN A 112       50.33   -115.47                                   
REMARK 500    SER A 126      148.27   -170.53                                   
REMARK 500    ASN A 168       -5.71     75.39                                   
REMARK 500    ASN A 178       21.07    -75.93                                   
REMARK 500    ASP D  28     -133.68     55.26                                   
REMARK 500    ASP D  30       74.27    -62.95                                   
REMARK 500    SER D  41       17.22     81.17                                   
REMARK 500    PHE D  56       -2.50   -157.21                                   
REMARK 500    GLU D  79       90.30     49.68                                   
REMARK 500    TYR D  80     -169.55   -160.29                                   
REMARK 500    CYS D  86       66.90   -111.56                                   
REMARK 500    LYS D 113       -1.84     68.35                                   
REMARK 500    ASN D 131       86.45    -66.88                                   
REMARK 500    ASN D 168       43.81   -100.79                                   
REMARK 500    ASN D 178       23.50    -77.09                                   
REMARK 500    ASP D 726        3.00    -64.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2007        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH D2003        DISTANCE =  6.10 ANGSTROMS                       
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                              MG A1750  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GCP A1749   O2G                                                    
REMARK 620 2 GCP A1749   O1B 104.1                                              
REMARK 620 3 SER A  45   OG  169.0  83.5                                        
REMARK 620 4 THR A  65   OG1  85.7 161.4  84.9                                  
REMARK 620 5 HOH A1752   O    97.9  92.5  89.7 101.9                            
REMARK 620 6 HOH A1751   O    96.2  77.8  77.4  85.6 164.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1750  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GCP D1749   O1B                                                    
REMARK 620 2 GCP D1749   O2G  95.6                                              
REMARK 620 3 HOH D1752   O    93.8  87.2                                        
REMARK 620 4 SER D  45   OG   87.8 170.1  83.3                                  
REMARK 620 5 THR D  65   OG1 172.7  80.3  92.0  97.2                            
REMARK 620 6 HOH D1751   O    89.3 101.4 170.5  87.9  85.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCP A 1749                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1750                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCP D 1749                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1750                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2X2F   RELATED DB: PDB                                   
REMARK 900 DYNAMIN 1 GTPASE DIMER, SHORT AXIS FORM                              
REMARK 900 RELATED ID: 2DYN   RELATED DB: PDB                                   
REMARK 900 DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)                         
REMARK 900 RELATED ID: 2X2E   RELATED DB: PDB                                   
REMARK 900 DYNAMIN GTPASE DIMER, LONG AXIS FORM                                 
REMARK 900 RELATED ID: 1DYN   RELATED DB: PDB                                   
REMARK 900 DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)                         
DBREF  3ZYC A    6   320  UNP    Q05193   DYN1_HUMAN       6    320             
DBREF  3ZYC A  726   750  UNP    Q05193   DYN1_HUMAN     726    750             
DBREF  3ZYC D    6   320  UNP    Q05193   DYN1_HUMAN       6    320             
DBREF  3ZYC D  726   750  UNP    Q05193   DYN1_HUMAN     726    750             
SEQADV 3ZYC GLY A    1  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC PRO A    2  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC GLU A    3  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC PHE A    4  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC SER A    5  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC LYS A  321  UNP  Q05193              LINKER                         
SEQADV 3ZYC HIS A  322  UNP  Q05193              LINKER                         
SEQADV 3ZYC GLY A  323  UNP  Q05193              LINKER                         
SEQADV 3ZYC THR A  324  UNP  Q05193              LINKER                         
SEQADV 3ZYC ASP A  325  UNP  Q05193              LINKER                         
SEQADV 3ZYC SER A  326  UNP  Q05193              LINKER                         
SEQADV 3ZYC ARG A  327  UNP  Q05193              LINKER                         
SEQADV 3ZYC VAL A  328  UNP  Q05193              LINKER                         
SEQADV 3ZYC ASN A  744  UNP  Q05193    ASP   744 VARIANT                        
SEQADV 3ZYC GLY D    1  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC PRO D    2  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC GLU D    3  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC PHE D    4  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC SER D    5  UNP  Q05193              CLONING ARTIFACT               
SEQADV 3ZYC LYS D  321  UNP  Q05193              LINKER                         
SEQADV 3ZYC HIS D  322  UNP  Q05193              LINKER                         
SEQADV 3ZYC GLY D  323  UNP  Q05193              LINKER                         
SEQADV 3ZYC THR D  324  UNP  Q05193              LINKER                         
SEQADV 3ZYC ASP D  325  UNP  Q05193              LINKER                         
SEQADV 3ZYC SER D  326  UNP  Q05193              LINKER                         
SEQADV 3ZYC ARG D  327  UNP  Q05193              LINKER                         
SEQADV 3ZYC VAL D  328  UNP  Q05193              LINKER                         
SEQADV 3ZYC ASN D  744  UNP  Q05193    ASP   744 VARIANT                        
SEQRES   1 A  353  GLY PRO GLU PHE SER MET GLU ASP LEU ILE PRO LEU VAL          
SEQRES   2 A  353  ASN ARG LEU GLN ASP ALA PHE SER ALA ILE GLY GLN ASN          
SEQRES   3 A  353  ALA ASP LEU ASP LEU PRO GLN ILE ALA VAL VAL GLY GLY          
SEQRES   4 A  353  GLN SER ALA GLY LYS SER SER VAL LEU GLU ASN PHE VAL          
SEQRES   5 A  353  GLY ARG ASP PHE LEU PRO ARG GLY SER GLY ILE VAL THR          
SEQRES   6 A  353  ARG ARG PRO LEU VAL LEU GLN LEU VAL ASN ALA THR THR          
SEQRES   7 A  353  GLU TYR ALA GLU PHE LEU HIS CYS LYS GLY LYS LYS PHE          
SEQRES   8 A  353  THR ASP PHE GLU GLU VAL ARG LEU GLU ILE GLU ALA GLU          
SEQRES   9 A  353  THR ASP ARG VAL THR GLY THR ASN LYS GLY ILE SER PRO          
SEQRES  10 A  353  VAL PRO ILE ASN LEU ARG VAL TYR SER PRO HIS VAL LEU          
SEQRES  11 A  353  ASN LEU THR LEU VAL ASP LEU PRO GLY MET THR LYS VAL          
SEQRES  12 A  353  PRO VAL GLY ASP GLN PRO PRO ASP ILE GLU PHE GLN ILE          
SEQRES  13 A  353  ARG ASP MET LEU MET GLN PHE VAL THR LYS GLU ASN CYS          
SEQRES  14 A  353  LEU ILE LEU ALA VAL SER PRO ALA ASN SER ASP LEU ALA          
SEQRES  15 A  353  ASN SER ASP ALA LEU LYS VAL ALA LYS GLU VAL ASP PRO          
SEQRES  16 A  353  GLN GLY GLN ARG THR ILE GLY VAL ILE THR LYS LEU ASP          
SEQRES  17 A  353  LEU MET ASP GLU GLY THR ASP ALA ARG ASP VAL LEU GLU          
SEQRES  18 A  353  ASN LYS LEU LEU PRO LEU ARG ARG GLY TYR ILE GLY VAL          
SEQRES  19 A  353  VAL ASN ARG SER GLN LYS ASP ILE ASP GLY LYS LYS ASP          
SEQRES  20 A  353  ILE THR ALA ALA LEU ALA ALA GLU ARG LYS PHE PHE LEU          
SEQRES  21 A  353  SER HIS PRO SER TYR ARG HIS LEU ALA ASP ARG MET GLY          
SEQRES  22 A  353  THR PRO TYR LEU GLN LYS VAL LEU ASN GLN GLN LEU THR          
SEQRES  23 A  353  ASN HIS ILE ARG ASP THR LEU PRO GLY LEU ARG ASN LYS          
SEQRES  24 A  353  LEU GLN SER GLN LEU LEU SER ILE GLU LYS GLU VAL GLU          
SEQRES  25 A  353  GLU TYR LYS ASN PHE ARG PRO ASP LYS HIS GLY THR ASP          
SEQRES  26 A  353  SER ARG VAL ASP GLU MET LEU ARG MET TYR HIS ALA LEU          
SEQRES  27 A  353  LYS GLU ALA LEU SER ILE ILE GLY ASN ILE ASN THR THR          
SEQRES  28 A  353  THR VAL                                                      
SEQRES   1 D  353  GLY PRO GLU PHE SER MET GLU ASP LEU ILE PRO LEU VAL          
SEQRES   2 D  353  ASN ARG LEU GLN ASP ALA PHE SER ALA ILE GLY GLN ASN          
SEQRES   3 D  353  ALA ASP LEU ASP LEU PRO GLN ILE ALA VAL VAL GLY GLY          
SEQRES   4 D  353  GLN SER ALA GLY LYS SER SER VAL LEU GLU ASN PHE VAL          
SEQRES   5 D  353  GLY ARG ASP PHE LEU PRO ARG GLY SER GLY ILE VAL THR          
SEQRES   6 D  353  ARG ARG PRO LEU VAL LEU GLN LEU VAL ASN ALA THR THR          
SEQRES   7 D  353  GLU TYR ALA GLU PHE LEU HIS CYS LYS GLY LYS LYS PHE          
SEQRES   8 D  353  THR ASP PHE GLU GLU VAL ARG LEU GLU ILE GLU ALA GLU          
SEQRES   9 D  353  THR ASP ARG VAL THR GLY THR ASN LYS GLY ILE SER PRO          
SEQRES  10 D  353  VAL PRO ILE ASN LEU ARG VAL TYR SER PRO HIS VAL LEU          
SEQRES  11 D  353  ASN LEU THR LEU VAL ASP LEU PRO GLY MET THR LYS VAL          
SEQRES  12 D  353  PRO VAL GLY ASP GLN PRO PRO ASP ILE GLU PHE GLN ILE          
SEQRES  13 D  353  ARG ASP MET LEU MET GLN PHE VAL THR LYS GLU ASN CYS          
SEQRES  14 D  353  LEU ILE LEU ALA VAL SER PRO ALA ASN SER ASP LEU ALA          
SEQRES  15 D  353  ASN SER ASP ALA LEU LYS VAL ALA LYS GLU VAL ASP PRO          
SEQRES  16 D  353  GLN GLY GLN ARG THR ILE GLY VAL ILE THR LYS LEU ASP          
SEQRES  17 D  353  LEU MET ASP GLU GLY THR ASP ALA ARG ASP VAL LEU GLU          
SEQRES  18 D  353  ASN LYS LEU LEU PRO LEU ARG ARG GLY TYR ILE GLY VAL          
SEQRES  19 D  353  VAL ASN ARG SER GLN LYS ASP ILE ASP GLY LYS LYS ASP          
SEQRES  20 D  353  ILE THR ALA ALA LEU ALA ALA GLU ARG LYS PHE PHE LEU          
SEQRES  21 D  353  SER HIS PRO SER TYR ARG HIS LEU ALA ASP ARG MET GLY          
SEQRES  22 D  353  THR PRO TYR LEU GLN LYS VAL LEU ASN GLN GLN LEU THR          
SEQRES  23 D  353  ASN HIS ILE ARG ASP THR LEU PRO GLY LEU ARG ASN LYS          
SEQRES  24 D  353  LEU GLN SER GLN LEU LEU SER ILE GLU LYS GLU VAL GLU          
SEQRES  25 D  353  GLU TYR LYS ASN PHE ARG PRO ASP LYS HIS GLY THR ASP          
SEQRES  26 D  353  SER ARG VAL ASP GLU MET LEU ARG MET TYR HIS ALA LEU          
SEQRES  27 D  353  LYS GLU ALA LEU SER ILE ILE GLY ASN ILE ASN THR THR          
SEQRES  28 D  353  THR VAL                                                      
HET    GCP  A1749      32                                                       
HET     MG  A1750       1                                                       
HET    GCP  D1749      32                                                       
HET     MG  D1750       1                                                       
HETNAM     GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER                     
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  GCP    2(C11 H18 N5 O13 P3)                                         
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *413(H2 O)                                                    
HELIX    1   1 SER A    5  GLY A   24  1                                  20
HELIX    2   2 GLY A   43  GLY A   53  1                                  11
HELIX    3   3 ASP A   93  GLY A  110  1                                  18
HELIX    4   4 ASP A  151  THR A  165  1                                  15
HELIX    5   5 ASP A  180  ASP A  194  1                                  15
HELIX    6   6 LYS A  206  MET A  210  1                                   5
HELIX    7   7 ALA A  216  GLU A  221  1                                   6
HELIX    8   8 SER A  238  GLY A  244  1                                   7
HELIX    9   9 ASP A  247  HIS A  262  1                                  16
HELIX   10  10 TYR A  265  VAL A  311  1                                  47
HELIX   11  11 LEU A  729  THR A  748  1                                  20
SHEET    1   1 1 ILE A  34  VAL A  37  0
SHEET    2   2 1 LEU A  69  ASN A  75  0
SHEET    3   3 1 TYR A  80  PHE A  83  0
SHEET    4   4 1 ILE A 120  SER A 126  0
SHEET    5   5 1 THR A 133  ASP A 136  0
SHEET    6   6 1 LEU A 170  PRO A 176  0
SHEET    7   7 1 THR A 200  THR A 205  0
SHEET    8   8 1 TYR A 231  GLY A 233  0
LINK         O2G GCP A1749                MG    MG A1750     1555   1555  2.00  
LINK         O1B GCP A1749                MG    MG A1750     1555   1555  2.18  
LINK        MG    MG A1750                 OG  SER A  45     1555   1555  2.23  
LINK        MG    MG A1750                 OG1 THR A  65     1555   1555  2.15  
LINK        MG    MG A1750                 O   HOH A1752     1555   1555  2.07  
LINK        MG    MG A1750                 O   HOH A1751     1555   1555  2.08  
LINK         O1B GCP D1749                MG    MG D1750     1555   1555  2.17  
LINK         O2G GCP D1749                MG    MG D1750     1555   1555  2.19  
LINK        MG    MG D1750                 O   HOH D1752     1555   1555  2.05  
LINK        MG    MG D1750                 OG  SER D  45     1555   1555  2.05  
LINK        MG    MG D1750                 OG1 THR D  65     1555   1555  2.07  
LINK        MG    MG D1750                 O   HOH D1751     1555   1555  2.08  
SITE     1 AC1 28 GLN A  40  SER A  41  ALA A  42  GLY A  43                    
SITE     2 AC1 28 LYS A  44  SER A  45  SER A  46  ARG A  59                    
SITE     3 AC1 28 GLY A  60  SER A  61  GLY A  62  VAL A  64                    
SITE     4 AC1 28 THR A  65  GLY A 139  LYS A 206  ASP A 208                    
SITE     5 AC1 28 LEU A 209  ASN A 236  ARG A 237  SER A 238                    
SITE     6 AC1 28 GLN A 239  ILE A 242   MG A1750  HOH A1751                    
SITE     7 AC1 28 HOH A1752  HOH A2036  HOH A2227  ASP D 211                    
SITE     1 AC2  5 SER A  45  THR A  65  GCP A1749  HOH A1751                    
SITE     2 AC2  5 HOH A1752                                                     
SITE     1 AC3 30 ASP A 211  HOH A2158  GLN D  40  SER D  41                    
SITE     2 AC3 30 ALA D  42  GLY D  43  LYS D  44  SER D  45                    
SITE     3 AC3 30 SER D  46  ARG D  59  GLY D  60  SER D  61                    
SITE     4 AC3 30 GLY D  62  VAL D  64  THR D  65  GLY D 139                    
SITE     5 AC3 30 LYS D 206  ASP D 208  LEU D 209  VAL D 235                    
SITE     6 AC3 30 ASN D 236  ARG D 237  SER D 238  GLN D 239                    
SITE     7 AC3 30 ILE D 242   MG D1750  HOH D1751  HOH D1752                    
SITE     8 AC3 30 HOH D2023  HOH D2043                                          
SITE     1 AC4  5 SER D  45  THR D  65  GCP D1749  HOH D1751                    
SITE     2 AC4  5 HOH D1752                                                     
CRYST1   44.151   82.635   95.014  90.00  96.68  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      0.022650  0.000000  0.002653        0.00000                         
SCALE2      0.000000  0.012101  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010597        0.00000                         
MTRIX1   1 -1.000000  0.000300 -0.004200       31.36050    1                    
MTRIX2   1  0.000200  1.000000  0.009200       -0.30530    1                    
MTRIX3   1  0.004200  0.009200 -0.999900       12.56100    1                    
ATOM      1  N   SER A   5      33.151  21.503 -26.413  1.00 50.15           N
ATOM      2  CA  SER A   5      33.680  20.217 -26.851  1.00 52.33           C
ATOM      3  C   SER A   5      32.578  19.169 -26.980  1.00 50.19           C
ATOM      4  O   SER A   5      32.507  18.450 -27.981  1.00 50.23           O
ATOM      5  CB  SER A   5      34.755  19.723 -25.879  1.00 58.92           C
ATOM      6  OG  SER A   5      35.864  20.605 -25.851  1.00 60.81           O
ATOM      7  N   MET A   6      31.699  19.112 -25.983  1.00 47.66           N
ATOM      8  CA  MET A   6      30.601  18.152 -25.977  1.00 46.49           C
ATOM      9  C   MET A   6      29.739  18.306 -27.228  1.00 45.56           C
ATOM     10  O   MET A   6      29.283  17.317 -27.802  1.00 47.66           O
ATOM     11  CB  MET A   6      29.741  18.331 -24.723  1.00 45.91           C
ATOM     12  CG  MET A   6      28.913  17.107 -24.364  1.00 45.29           C
ATOM     13  SD  MET A   6      29.958  15.676 -24.009  1.00 45.01           S
ATOM     14  CE  MET A   6      29.029  14.356 -24.770  1.00 44.52           C
ATOM     15  N   GLU A   7      29.558  19.549 -27.666  1.00 41.91           N
ATOM     16  CA  GLU A   7      28.764  19.843 -28.855  1.00 40.82           C
ATOM     17  C   GLU A   7      29.361  19.255 -30.124  1.00 39.80           C
ATOM     18  O   GLU A   7      28.673  19.135 -31.130  1.00 39.77           O
ATOM     19  CB  GLU A   7      28.630  21.349 -29.058  1.00 41.21           C
ATOM     20  CG  GLU A   7      27.750  22.062 -28.061  1.00 47.84           C
ATOM     21  CD  GLU A   7      27.464  23.487 -28.488  1.00 60.74           C
ATOM     22  OE1 GLU A   7      28.429  24.234 -28.762  1.00 47.58           O
ATOM     23  OE2 GLU A   7      26.271  23.854 -28.569  1.00 76.25           O
ATOM     24  N   ASP A   8      30.651  18.942 -30.090  1.00 39.70           N
ATOM     25  CA  ASP A   8      31.335  18.381 -31.251  1.00 39.86           C
ATOM     26  C   ASP A   8      31.286  16.860 -31.237  1.00 40.88           C
ATOM     27  O   ASP A   8      31.138  16.223 -32.283  1.00 43.76           O
ATOM     28  CB  ASP A   8      32.788  18.855 -31.283  1.00 41.36           C
ATOM     29  CG  ASP A   8      32.914  20.357 -31.095  1.00 43.96           C
ATOM     30  OD1 ASP A   8      32.481  21.112 -31.992  1.00 37.28           O
ATOM     31  OD2 ASP A   8      33.438  20.781 -30.043  1.00 49.63           O
ATOM     32  N   LEU A   9      31.393  16.282 -30.045  1.00 37.48           N
ATOM     33  CA  LEU A   9      31.367  14.834 -29.882  1.00 35.33           C
ATOM     34  C   LEU A   9      29.976  14.257 -30.150  1.00 32.75           C
ATOM     35  O   LEU A   9      29.839  13.285 -30.898  1.00 32.47           O
ATOM     36  CB  LEU A   9      31.851  14.466 -28.472  1.00 36.76           C
ATOM     37  CG  LEU A   9      32.028  13.008 -28.034  1.00 38.68           C
ATOM     38  CD1 LEU A   9      30.710  12.423 -27.569  1.00 41.30           C
ATOM     39  CD2 LEU A   9      32.649  12.177 -29.151  1.00 41.42           C
ATOM     40  N   ILE A  10      28.950  14.877 -29.568  1.00 28.89           N
ATOM     41  CA  ILE A  10      27.570  14.416 -29.732  1.00 26.64           C
ATOM     42  C   ILE A  10      27.172  14.106 -31.180  1.00 26.15           C
ATOM     43  O   ILE A  10      26.782  12.975 -31.483  1.00 24.27           O
ATOM     44  CB  ILE A  10      26.555  15.395 -29.082  1.00 24.97           C
ATOM     45  CG1 ILE A  10      26.697  15.360 -27.560  1.00 25.37           C
ATOM     46  CG2 ILE A  10      25.128  15.037 -29.473  1.00 23.46           C
ATOM     47  CD1 ILE A  10      25.782  16.316 -26.830  1.00 23.95           C
ATOM     48  N   PRO A  11      27.303  15.083 -32.100  1.00 26.53           N
ATOM     49  CA  PRO A  11      26.934  14.828 -33.497  1.00 27.59           C
ATOM     50  C   PRO A  11      27.767  13.739 -34.171  1.00 28.57           C
ATOM     51  O   PRO A  11      27.275  13.061 -35.077  1.00 29.48           O
ATOM     52  CB  PRO A  11      27.117  16.197 -34.158  1.00 27.14           C
ATOM     53  CG  PRO A  11      28.164  16.838 -33.335  1.00 26.23           C
ATOM     54  CD  PRO A  11      27.753  16.474 -31.936  1.00 25.46           C
ATOM     55  N   LEU A  12      29.018  13.571 -33.741  1.00 26.63           N
ATOM     56  CA  LEU A  12      29.870  12.529 -34.311  1.00 25.53           C
ATOM     57  C   LEU A  12      29.380  11.157 -33.870  1.00 21.84           C
ATOM     58  O   LEU A  12      29.334  10.226 -34.666  1.00 19.60           O
ATOM     59  CB  LEU A  12      31.333  12.713 -33.899  1.00 25.90           C
ATOM     60  CG  LEU A  12      32.190  13.640 -34.762  1.00 29.76           C
ATOM     61  CD1 LEU A  12      33.628  13.632 -34.254  1.00 25.96           C
ATOM     62  CD2 LEU A  12      32.146  13.179 -36.211  1.00 34.45           C
ATOM     63  N   VAL A  13      28.980  11.049 -32.607  1.00 23.05           N
ATOM     64  CA  VAL A  13      28.484   9.792 -32.052  1.00 24.21           C
ATOM     65  C   VAL A  13      27.200   9.335 -32.739  1.00 24.18           C
ATOM     66  O   VAL A  13      27.021   8.144 -32.995  1.00 24.34           O
ATOM     67  CB  VAL A  13      28.262   9.901 -30.526  1.00 23.90           C
ATOM     68  CG1 VAL A  13      27.616   8.634 -29.976  1.00 22.75           C
ATOM     69  CG2 VAL A  13      29.592  10.129 -29.845  1.00 24.78           C
ATOM     70  N   ASN A  14      26.316  10.277 -33.052  1.00 26.21           N
ATOM     71  CA  ASN A  14      25.072   9.928 -33.730  1.00 31.54           C
ATOM     72  C   ASN A  14      25.398   9.384 -35.119  1.00 31.66           C
ATOM     73  O   ASN A  14      24.777   8.430 -35.589  1.00 31.93           O
ATOM     74  CB  ASN A  14      24.142  11.138 -33.846  1.00 37.29           C
ATOM     75  CG  ASN A  14      22.822  10.792 -34.519  1.00 52.22           C
ATOM     76  OD1 ASN A  14      22.060   9.954 -34.030  1.00 52.11           O
ATOM     77  ND2 ASN A  14      22.553  11.426 -35.651  1.00 58.19           N
ATOM     78  N   ARG A  15      26.399   9.982 -35.756  1.00 32.33           N
ATOM     79  CA  ARG A  15      26.833   9.564 -37.086  1.00 32.35           C
ATOM     80  C   ARG A  15      27.392   8.148 -37.032  1.00 29.87           C
ATOM     81  O   ARG A  15      27.137   7.336 -37.921  1.00 30.19           O
ATOM     82  CB  ARG A  15      27.912  10.511 -37.612  1.00 35.56           C
ATOM     83  CG  ARG A  15      27.426  11.911 -37.951  1.00 40.44           C
ATOM     84  CD  ARG A  15      27.051  12.039 -39.423  1.00 65.27           C
ATOM     85  NE  ARG A  15      28.141  11.671 -40.333  1.00 72.17           N
ATOM     86  CZ  ARG A  15      29.368  12.191 -40.311  1.00 64.16           C
ATOM     87  NH1 ARG A  15      29.701  13.117 -39.419  1.00 57.83           N
ATOM     88  NH2 ARG A  15      30.268  11.791 -41.201  1.00 55.11           N
ATOM     89  N   LEU A  16      28.167   7.862 -35.991  1.00 28.64           N
ATOM     90  CA  LEU A  16      28.764   6.546 -35.821  1.00 27.06           C
ATOM     91  C   LEU A  16      27.690   5.490 -35.599  1.00 28.51           C
ATOM     92  O   LEU A  16      27.746   4.404 -36.179  1.00 30.24           O
ATOM     93  CB  LEU A  16      29.749   6.551 -34.656  1.00 24.71           C
ATOM     94  CG  LEU A  16      30.522   5.249 -34.454  1.00 17.82           C
ATOM     95  CD1 LEU A  16      31.272   4.883 -35.723  1.00 11.99           C
ATOM     96  CD2 LEU A  16      31.479   5.409 -33.294  1.00 13.36           C
ATOM     97  N   GLN A  17      26.699   5.811 -34.774  1.00 28.33           N
ATOM     98  CA  GLN A  17      25.622   4.870 -34.519  1.00 28.06           C
ATOM     99  C   GLN A  17      24.851   4.594 -35.809  1.00 28.48           C
ATOM    100  O   GLN A  17      24.442   3.462 -36.061  1.00 29.66           O
ATOM    101  CB  GLN A  17      24.713   5.373 -33.396  1.00 18.21           C
ATOM    102  CG  GLN A  17      25.413   5.365 -32.039  1.00 32.36           C
ATOM    103  CD  GLN A  17      24.490   5.680 -30.881  1.00 45.31           C
ATOM    104  OE1 GLN A  17      24.413   6.819 -30.423  1.00 42.85           O
ATOM    105  NE2 GLN A  17      23.794   4.664 -30.389  1.00 58.60           N
ATOM    106  N   ASP A  18      24.691   5.615 -36.648  1.00 28.84           N
ATOM    107  CA  ASP A  18      24.003   5.431 -37.922  1.00 30.54           C
ATOM    108  C   ASP A  18      24.887   4.599 -38.844  1.00 30.78           C
ATOM    109  O   ASP A  18      24.409   3.681 -39.513  1.00 31.45           O
ATOM    110  CB  ASP A  18      23.678   6.775 -38.582  1.00 35.39           C
ATOM    111  CG  ASP A  18      22.520   7.500 -37.908  1.00 40.78           C
ATOM    112  OD1 ASP A  18      21.796   6.880 -37.094  1.00 41.96           O
ATOM    113  OD2 ASP A  18      22.330   8.697 -38.205  1.00 31.79           O
ATOM    114  N   ALA A  19      26.185   4.894 -38.836  1.00 29.54           N
ATOM    115  CA  ALA A  19      27.150   4.175 -39.661  1.00 28.63           C
ATOM    116  C   ALA A  19      27.094   2.684 -39.349  1.00 29.10           C
ATOM    117  O   ALA A  19      27.076   1.855 -40.262  1.00 28.65           O
ATOM    118  CB  ALA A  19      28.551   4.712 -39.419  1.00 28.65           C
ATOM    119  N   PHE A  20      27.053   2.353 -38.059  1.00 30.22           N
ATOM    120  CA  PHE A  20      26.975   0.964 -37.607  1.00 30.78           C
ATOM    121  C   PHE A  20      25.719   0.305 -38.165  1.00 33.19           C
ATOM    122  O   PHE A  20      25.743  -0.867 -38.556  1.00 34.55           O
ATOM    123  CB  PHE A  20      26.944   0.890 -36.077  1.00 30.20           C
ATOM    124  CG  PHE A  20      28.292   1.029 -35.429  1.00 29.89           C
ATOM    125  CD1 PHE A  20      29.450   0.664 -36.106  1.00 29.59           C
ATOM    126  CD2 PHE A  20      28.399   1.499 -34.123  1.00 30.40           C
ATOM    127  CE1 PHE A  20      30.699   0.764 -35.492  1.00 30.38           C
ATOM    128  CE2 PHE A  20      29.643   1.603 -33.499  1.00 30.28           C
ATOM    129  CZ  PHE A  20      30.794   1.232 -34.186  1.00 30.22           C
ATOM    130  N   SER A  21      24.632   1.075 -38.212  1.00 33.31           N
ATOM    131  CA  SER A  21      23.359   0.596 -38.735  1.00 34.31           C
ATOM    132  C   SER A  21      23.518   0.235 -40.210  1.00 34.07           C
ATOM    133  O   SER A  21      23.048  -0.811 -40.660  1.00 33.89           O
ATOM    134  CB  SER A  21      22.280   1.672 -38.574  1.00 41.08           C
ATOM    135  OG  SER A  21      22.107   2.040 -37.213  1.00 47.29           O
ATOM    136  N   ALA A  22      24.214   1.087 -40.955  1.00 36.60           N
ATOM    137  CA  ALA A  22      24.434   0.843 -42.376  1.00 39.82           C
ATOM    138  C   ALA A  22      25.212  -0.455 -42.584  1.00 42.41           C
ATOM    139  O   ALA A  22      24.998  -1.163 -43.568  1.00 41.99           O
ATOM    140  CB  ALA A  22      25.173   2.011 -43.005  1.00 40.07           C
ATOM    141  N   ILE A  23      26.101  -0.764 -41.642  1.00 45.76           N
ATOM    142  CA  ILE A  23      26.912  -1.980 -41.705  1.00 46.99           C
ATOM    143  C   ILE A  23      26.048  -3.216 -41.432  1.00 49.75           C
ATOM    144  O   ILE A  23      26.416  -4.338 -41.793  1.00 48.55           O
ATOM    145  CB  ILE A  23      28.087  -1.923 -40.699  1.00 44.16           C
ATOM    146  CG1 ILE A  23      28.940  -0.681 -40.969  1.00 34.10           C
ATOM    147  CG2 ILE A  23      28.956  -3.165 -40.821  1.00 44.51           C
ATOM    148  CD1 ILE A  23      30.027  -0.444 -39.946  1.00 25.59           C
ATOM    149  N   GLY A  24      24.902  -2.994 -40.793  1.00 53.58           N
ATOM    150  CA  GLY A  24      23.984  -4.077 -40.491  1.00 57.04           C
ATOM    151  C   GLY A  24      24.529  -5.112 -39.532  1.00 59.67           C
ATOM    152  O   GLY A  24      24.194  -6.295 -39.630  1.00 59.72           O
ATOM    153  N   GLN A  25      25.369  -4.676 -38.600  1.00 61.04           N
ATOM    154  CA  GLN A  25      25.951  -5.588 -37.626  1.00 61.68           C
ATOM    155  C   GLN A  25      25.459  -5.273 -36.223  1.00 61.94           C
ATOM    156  O   GLN A  25      25.058  -4.143 -35.931  1.00 61.41           O
ATOM    157  CB  GLN A  25      27.481  -5.517 -37.658  1.00 63.68           C
ATOM    158  CG  GLN A  25      28.113  -5.966 -38.970  1.00 75.69           C
ATOM    159  CD  GLN A  25      27.811  -7.409 -39.334  1.00 71.59           C
ATOM    160  OE1 GLN A  25      27.318  -8.190 -38.514  1.00 69.78           O
ATOM    161  NE2 GLN A  25      28.115  -7.772 -40.575  1.00 70.23           N
ATOM    162  N   ASN A  26      25.474  -6.287 -35.366  1.00 61.92           N
ATOM    163  CA  ASN A  26      25.053  -6.133 -33.982  1.00 60.88           C
ATOM    164  C   ASN A  26      26.223  -5.520 -33.210  1.00 55.03           C
ATOM    165  O   ASN A  26      26.937  -6.221 -32.487  1.00 54.49           O
ATOM    166  CB  ASN A  26      24.674  -7.497 -33.390  1.00 73.35           C
ATOM    167  CG  ASN A  26      24.205  -7.399 -31.948  1.00 80.07           C
ATOM    168  OD1 ASN A  26      23.528  -6.445 -31.566  1.00 85.51           O
ATOM    169  ND2 ASN A  26      24.562  -8.390 -31.142  1.00 74.87           N
ATOM    170  N   ALA A  27      26.447  -4.224 -33.417  1.00 50.75           N
ATOM    171  CA  ALA A  27      27.531  -3.505 -32.754  1.00 48.22           C
ATOM    172  C   ALA A  27      27.077  -2.097 -32.387  1.00 44.98           C
ATOM    173  O   ALA A  27      26.658  -1.326 -33.249  1.00 42.43           O
ATOM    174  CB  ALA A  27      28.756  -3.445 -33.658  1.00 48.09           C
ATOM    175  N   ASP A  28      27.166  -1.768 -31.104  1.00 42.01           N
ATOM    176  CA  ASP A  28      26.759  -0.460 -30.619  1.00 41.78           C
ATOM    177  C   ASP A  28      27.709  -0.019 -29.514  1.00 40.13           C
ATOM    178  O   ASP A  28      28.400  -0.845 -28.915  1.00 40.17           O
ATOM    179  CB  ASP A  28      25.320  -0.521 -30.089  1.00 48.03           C
ATOM    180  CG  ASP A  28      24.700   0.858 -29.903  1.00 59.22           C
ATOM    181  OD1 ASP A  28      25.104   1.808 -30.611  1.00 62.74           O
ATOM    182  OD2 ASP A  28      23.794   0.987 -29.052  1.00 63.06           O
ATOM    183  N   LEU A  29      27.739   1.284 -29.252  1.00 37.43           N
ATOM    184  CA  LEU A  29      28.605   1.847 -28.217  1.00 35.21           C
ATOM    185  C   LEU A  29      28.123   1.447 -26.823  1.00 35.08           C
ATOM    186  O   LEU A  29      28.878   1.512 -25.853  1.00 36.82           O
ATOM    187  CB  LEU A  29      28.666   3.373 -28.333  1.00 33.63           C
ATOM    188  CG  LEU A  29      29.267   3.991 -29.598  1.00 31.55           C
ATOM    189  CD1 LEU A  29      28.356   3.755 -30.789  1.00 31.05           C
ATOM    190  CD2 LEU A  29      29.467   5.481 -29.389  1.00 31.51           C
ATOM    191  N   ASP A  30      26.850   1.067 -26.735  1.00 32.51           N
ATOM    192  CA  ASP A  30      26.246   0.637 -25.482  1.00 32.26           C
ATOM    193  C   ASP A  30      26.408   1.683 -24.376  1.00 28.89           C
ATOM    194  O   ASP A  30      26.967   1.400 -23.316  1.00 24.48           O
ATOM    195  CB  ASP A  30      26.848  -0.711 -25.050  1.00 41.75           C
ATOM    196  CG  ASP A  30      26.094  -1.361 -23.894  1.00 50.79           C
ATOM    197  OD1 ASP A  30      24.939  -0.967 -23.609  1.00 59.34           O
ATOM    198  OD2 ASP A  30      26.663  -2.283 -23.275  1.00 36.20           O
ATOM    199  N   LEU A  31      25.931   2.896 -24.639  1.00 28.81           N
ATOM    200  CA  LEU A  31      25.999   3.978 -23.657  1.00 29.09           C
ATOM    201  C   LEU A  31      25.261   3.549 -22.388  1.00 26.37           C
ATOM    202  O   LEU A  31      24.133   3.040 -22.451  1.00 26.01           O
ATOM    203  CB  LEU A  31      25.379   5.261 -24.226  1.00 30.32           C
ATOM    204  CG  LEU A  31      26.270   6.190 -25.065  1.00 34.85           C
ATOM    205  CD1 LEU A  31      27.225   5.393 -25.937  1.00 35.62           C
ATOM    206  CD2 LEU A  31      25.408   7.117 -25.917  1.00 36.26           C
ATOM    207  N   PRO A  32      25.903   3.712 -21.224  1.00 19.23           N
ATOM    208  CA  PRO A  32      25.290   3.332 -19.948  1.00 19.72           C
ATOM    209  C   PRO A  32      24.048   4.166 -19.649  1.00 19.64           C
ATOM    210  O   PRO A  32      23.945   5.314 -20.087  1.00 24.05           O
ATOM    211  CB  PRO A  32      26.411   3.606 -18.944  1.00 19.08           C
ATOM    212  CG  PRO A  32      27.146   4.742 -19.561  1.00 16.68           C
ATOM    213  CD  PRO A  32      27.216   4.344 -21.010  1.00 15.69           C
ATOM    214  N   GLN A  33      23.078   3.572 -18.965  1.00 18.33           N
ATOM    215  CA  GLN A  33      21.862   4.301 -18.618  1.00 19.12           C
ATOM    216  C   GLN A  33      22.055   5.019 -17.286  1.00 20.53           C
ATOM    217  O   GLN A  33      22.897   4.625 -16.472  1.00 21.54           O
ATOM    218  CB  GLN A  33      20.648   3.369 -18.559  1.00 26.31           C
ATOM    219  CG  GLN A  33      20.718   2.261 -17.523  1.00 34.65           C
ATOM    220  CD  GLN A  33      19.383   1.548 -17.332  1.00 37.39           C
ATOM    221  OE1 GLN A  33      19.088   1.047 -16.248  1.00 24.04           O
ATOM    222  NE2 GLN A  33      18.572   1.503 -18.384  1.00 34.64           N
ATOM    223  N   ILE A  34      21.293   6.086 -17.078  1.00 19.52           N
ATOM    224  CA  ILE A  34      21.392   6.864 -15.849  1.00 16.22           C
ATOM    225  C   ILE A  34      20.150   6.700 -14.972  1.00 15.56           C
ATOM    226  O   ILE A  34      19.036   6.982 -15.406  1.00 16.26           O
ATOM    227  CB  ILE A  34      21.629   8.359 -16.169  1.00 13.98           C
ATOM    228  CG1 ILE A  34      22.968   8.522 -16.902  1.00 17.31           C
ATOM    229  CG2 ILE A  34      21.629   9.185 -14.884  1.00 14.55           C
ATOM    230  CD1 ILE A  34      23.234   9.923 -17.428  1.00 14.86           C
ATOM    231  N   ALA A  35      20.347   6.233 -13.743  1.00 12.98           N
ATOM    232  CA  ALA A  35      19.239   6.040 -12.817  1.00 13.90           C
ATOM    233  C   ALA A  35      19.413   6.906 -11.580  1.00 15.36           C
ATOM    234  O   ALA A  35      20.520   7.035 -11.055  1.00 15.74           O
ATOM    235  CB  ALA A  35      19.131   4.574 -12.414  1.00 13.66           C
ATOM    236  N   VAL A  36      18.315   7.492 -11.113  1.00 13.84           N
ATOM    237  CA  VAL A  36      18.355   8.334  -9.927  1.00 13.35           C
ATOM    238  C   VAL A  36      17.675   7.601  -8.763  1.00 13.95           C
ATOM    239  O   VAL A  36      16.535   7.136  -8.888  1.00 14.69           O
ATOM    240  CB  VAL A  36      17.713   9.712 -10.212  1.00 15.01           C
ATOM    241  CG1 VAL A  36      16.220   9.583 -10.451  1.00 15.50           C
ATOM    242  CG2 VAL A  36      18.015  10.670  -9.093  1.00 16.35           C
ATOM    243  N   VAL A  37      18.396   7.452  -7.654  1.00 12.18           N
ATOM    244  CA  VAL A  37      17.873   6.746  -6.482  1.00 11.84           C
ATOM    245  C   VAL A  37      18.028   7.534  -5.188  1.00 12.38           C
ATOM    246  O   VAL A  37      18.952   8.341  -5.045  1.00 13.46           O
ATOM    247  CB  VAL A  37      18.576   5.376  -6.279  1.00 12.54           C
ATOM    248  CG1 VAL A  37      18.346   4.469  -7.485  1.00 14.60           C
ATOM    249  CG2 VAL A  37      20.060   5.571  -6.044  1.00 11.43           C
ATOM    250  N   GLY A  38      17.144   7.264  -4.233  1.00 12.08           N
ATOM    251  CA  GLY A  38      17.206   7.940  -2.950  1.00 10.02           C
ATOM    252  C   GLY A  38      15.886   7.921  -2.208  1.00 10.94           C
ATOM    253  O   GLY A  38      14.854   7.528  -2.761  1.00 10.32           O
ATOM    254  N   GLY A  39      15.921   8.339  -0.945  1.00  8.76           N
ATOM    255  CA  GLY A  39      14.714   8.374  -0.140  1.00  7.92           C
ATOM    256  C   GLY A  39      13.678   9.290  -0.757  1.00  7.31           C
ATOM    257  O   GLY A  39      14.017  10.161  -1.559  1.00  8.72           O
ATOM    258  N   GLN A  40      12.413   9.085  -0.409  1.00  5.27           N
ATOM    259  CA  GLN A  40      11.341   9.915  -0.940  1.00  9.04           C
ATOM    260  C   GLN A  40      11.627  11.387  -0.639  1.00 10.08           C
ATOM    261  O   GLN A  40      12.020  11.735   0.478  1.00  7.97           O
ATOM    262  CB  GLN A  40       9.986   9.505  -0.337  1.00  3.94           C
ATOM    263  CG  GLN A  40       8.796  10.212  -0.967  1.00  5.30           C
ATOM    264  CD  GLN A  40       7.459   9.758  -0.407  1.00 22.05           C
ATOM    265  OE1 GLN A  40       7.010   8.642  -0.661  1.00 21.40           O
ATOM    266  NE2 GLN A  40       6.805  10.635   0.338  1.00 18.95           N
ATOM    267  N   SER A  41      11.476  12.232  -1.658  1.00 11.16           N
ATOM    268  CA  SER A  41      11.685  13.676  -1.542  1.00  9.42           C
ATOM    269  C   SER A  41      13.151  14.110  -1.473  1.00 12.83           C
ATOM    270  O   SER A  41      13.445  15.256  -1.137  1.00 17.13           O
ATOM    271  CB  SER A  41      10.924  14.230  -0.328  1.00 11.92           C
ATOM    272  OG  SER A  41      10.691  15.620  -0.448  1.00 24.36           O
ATOM    273  N   ALA A  42      14.072  13.207  -1.792  1.00  9.85           N
ATOM    274  CA  ALA A  42      15.493  13.541  -1.771  1.00  6.79           C
ATOM    275  C   ALA A  42      15.845  14.589  -2.835  1.00  7.64           C
ATOM    276  O   ALA A  42      16.903  15.210  -2.772  1.00  7.77           O
ATOM    277  CB  ALA A  42      16.330  12.288  -1.971  1.00  5.63           C
ATOM    278  N   GLY A  43      14.959  14.769  -3.813  1.00  8.24           N
ATOM    279  CA  GLY A  43      15.194  15.739  -4.873  1.00 12.10           C
ATOM    280  C   GLY A  43      15.642  15.103  -6.178  1.00 10.20           C
ATOM    281  O   GLY A  43      16.273  15.748  -7.011  1.00 10.16           O
ATOM    282  N   LYS A  44      15.247  13.852  -6.378  1.00  9.57           N
ATOM    283  CA  LYS A  44      15.623  13.074  -7.555  1.00  7.09           C
ATOM    284  C   LYS A  44      15.190  13.591  -8.926  1.00  6.95           C
ATOM    285  O   LYS A  44      16.018  13.726  -9.827  1.00  8.46           O
ATOM    286  CB  LYS A  44      15.159  11.632  -7.372  1.00  3.83           C
ATOM    287  CG  LYS A  44      15.727  10.960  -6.134  1.00  1.46           C
ATOM    288  CD  LYS A  44      15.152   9.556  -5.959  1.00  3.53           C
ATOM    289  CE  LYS A  44      13.647   9.602  -5.743  1.00  3.53           C
ATOM    290  NZ  LYS A  44      13.275  10.229  -4.446  1.00  1.46           N
ATOM    291  N   SER A  45      13.893  13.809  -9.109  1.00  5.61           N
ATOM    292  CA  SER A  45      13.370  14.307 -10.373  1.00  1.46           C
ATOM    293  C   SER A  45      14.000  15.635 -10.798  1.00  4.00           C
ATOM    294  O   SER A  45      14.235  15.852 -11.985  1.00  2.87           O
ATOM    295  CB  SER A  45      11.849  14.429 -10.302  1.00  1.71           C
ATOM    296  OG  SER A  45      11.249  13.168 -10.048  1.00  7.71           O
ATOM    297  N   SER A  46      14.263  16.520  -9.835  1.00  6.94           N
ATOM    298  CA  SER A  46      14.880  17.813 -10.127  1.00  7.70           C
ATOM    299  C   SER A  46      16.261  17.564 -10.708  1.00  8.91           C
ATOM    300  O   SER A  46      16.617  18.112 -11.754  1.00 10.42           O
ATOM    301  CB  SER A  46      15.012  18.666  -8.857  1.00  2.19           C
ATOM    302  OG  SER A  46      13.747  18.950  -8.293  1.00  4.47           O
ATOM    303  N   VAL A  47      17.024  16.705 -10.040  1.00  9.24           N
ATOM    304  CA  VAL A  47      18.369  16.370 -10.490  1.00 11.61           C
ATOM    305  C   VAL A  47      18.349  15.823 -11.913  1.00 11.68           C
ATOM    306  O   VAL A  47      19.051  16.329 -12.778  1.00  8.91           O
ATOM    307  CB  VAL A  47      19.036  15.339  -9.564  1.00 13.43           C
ATOM    308  CG1 VAL A  47      20.378  14.902 -10.135  1.00 15.35           C
ATOM    309  CG2 VAL A  47      19.233  15.936  -8.182  1.00 15.18           C
ATOM    310  N   LEU A  48      17.480  14.852 -12.171  1.00 13.38           N
ATOM    311  CA  LEU A  48      17.407  14.240 -13.491  1.00 14.15           C
ATOM    312  C   LEU A  48      17.049  15.212 -14.611  1.00 14.34           C
ATOM    313  O   LEU A  48      17.771  15.308 -15.601  1.00 22.53           O
ATOM    314  CB  LEU A  48      16.440  13.045 -13.478  1.00 13.64           C
ATOM    315  CG  LEU A  48      16.660  11.955 -14.539  1.00 14.10           C
ATOM    316  CD1 LEU A  48      18.003  11.295 -14.350  1.00  9.74           C
ATOM    317  CD2 LEU A  48      15.563  10.908 -14.447  1.00 23.39           C
ATOM    318  N   GLU A  49      15.976  15.978 -14.439  1.00 10.76           N
ATOM    319  CA  GLU A  49      15.562  16.909 -15.486  1.00  8.84           C
ATOM    320  C   GLU A  49      16.578  18.028 -15.706  1.00 10.23           C
ATOM    321  O   GLU A  49      16.659  18.595 -16.795  1.00  8.36           O
ATOM    322  CB  GLU A  49      14.175  17.494 -15.210  1.00  9.79           C
ATOM    323  CG  GLU A  49      14.144  18.527 -14.091  1.00 13.17           C
ATOM    324  CD  GLU A  49      12.855  19.315 -14.055  1.00  4.15           C
ATOM    325  OE1 GLU A  49      11.821  18.810 -14.543  1.00 26.57           O
ATOM    326  OE2 GLU A  49      12.877  20.451 -13.538  1.00 37.00           O
ATOM    327  N   ASN A  50      17.331  18.368 -14.664  1.00 11.81           N
ATOM    328  CA  ASN A  50      18.351  19.400 -14.787  1.00 12.20           C
ATOM    329  C   ASN A  50      19.449  18.882 -15.704  1.00 17.03           C
ATOM    330  O   ASN A  50      19.931  19.607 -16.568  1.00 16.15           O
ATOM    331  CB  ASN A  50      18.925  19.777 -13.423  1.00  1.46           C
ATOM    332  CG  ASN A  50      18.022  20.711 -12.652  1.00 13.72           C
ATOM    333  OD1 ASN A  50      17.031  21.214 -13.183  1.00 15.84           O
ATOM    334  ND2 ASN A  50      18.356  20.952 -11.396  1.00  4.73           N
ATOM    335  N   PHE A  51      19.807  17.610 -15.544  1.00 18.00           N
ATOM    336  CA  PHE A  51      20.830  17.007 -16.390  1.00 18.55           C
ATOM    337  C   PHE A  51      20.394  17.025 -17.854  1.00 19.29           C
ATOM    338  O   PHE A  51      21.209  17.267 -18.743  1.00 18.59           O
ATOM    339  CB  PHE A  51      21.126  15.568 -15.961  1.00 18.92           C
ATOM    340  CG  PHE A  51      22.050  14.846 -16.899  1.00 17.49           C
ATOM    341  CD1 PHE A  51      23.371  15.253 -17.040  1.00 13.08           C
ATOM    342  CD2 PHE A  51      21.581  13.802 -17.691  1.00 19.23           C
ATOM    343  CE1 PHE A  51      24.210  14.637 -17.958  1.00 14.34           C
ATOM    344  CE2 PHE A  51      22.417  13.175 -18.618  1.00 16.39           C
ATOM    345  CZ  PHE A  51      23.734  13.595 -18.752  1.00 14.68           C
ATOM    346  N   VAL A  52      19.117  16.738 -18.097  1.00 20.36           N
ATOM    347  CA  VAL A  52      18.566  16.734 -19.448  1.00 19.98           C
ATOM    348  C   VAL A  52      18.487  18.167 -19.976  1.00 21.88           C
ATOM    349  O   VAL A  52      18.584  18.404 -21.183  1.00 21.53           O
ATOM    350  CB  VAL A  52      17.158  16.102 -19.469  1.00 21.51           C
ATOM    351  CG1 VAL A  52      16.552  16.172 -20.874  1.00 22.22           C
ATOM    352  CG2 VAL A  52      17.227  14.666 -18.992  1.00 20.96           C
ATOM    353  N   GLY A  53      18.294  19.114 -19.061  1.00 21.48           N
ATOM    354  CA  GLY A  53      18.216  20.513 -19.439  1.00 20.74           C
ATOM    355  C   GLY A  53      16.831  21.012 -19.797  1.00 22.42           C
ATOM    356  O   GLY A  53      16.697  21.961 -20.571  1.00 26.59           O
ATOM    357  N   ARG A  54      15.796  20.409 -19.221  1.00 21.20           N
ATOM    358  CA  ARG A  54      14.423  20.826 -19.505  1.00 18.32           C
ATOM    359  C   ARG A  54      13.482  20.566 -18.344  1.00 14.51           C
ATOM    360  O   ARG A  54      13.619  19.571 -17.637  1.00 14.74           O
ATOM    361  CB  ARG A  54      13.886  20.100 -20.746  1.00 27.73           C
ATOM    362  CG  ARG A  54      14.098  20.827 -22.068  1.00 41.56           C
ATOM    363  CD  ARG A  54      12.999  21.853 -22.341  1.00 61.09           C
ATOM    364  NE  ARG A  54      13.089  23.042 -21.494  1.00 60.66           N
ATOM    365  CZ  ARG A  54      12.057  23.600 -20.863  1.00 43.93           C
ATOM    366  NH1 ARG A  54      10.841  23.078 -20.966  1.00 40.41           N
ATOM    367  NH2 ARG A  54      12.235  24.704 -20.151  1.00 53.45           N
ATOM    368  N   ASP A  55      12.527  21.469 -18.148  1.00 15.22           N
ATOM    369  CA  ASP A  55      11.534  21.308 -17.096  1.00 15.77           C
ATOM    370  C   ASP A  55      10.398  20.447 -17.664  1.00 18.13           C
ATOM    371  O   ASP A  55       9.578  20.930 -18.453  1.00 19.95           O
ATOM    372  CB  ASP A  55      10.996  22.672 -16.652  1.00 10.95           C
ATOM    373  CG  ASP A  55      12.033  23.510 -15.906  1.00 14.65           C
ATOM    374  OD1 ASP A  55      13.140  23.009 -15.620  1.00 24.41           O
ATOM    375  OD2 ASP A  55      11.733  24.681 -15.593  1.00 13.39           O
ATOM    376  N   PHE A  56      10.377  19.165 -17.308  1.00 15.21           N
ATOM    377  CA  PHE A  56       9.331  18.268 -17.803  1.00 13.13           C
ATOM    378  C   PHE A  56       8.923  17.169 -16.824  1.00 12.65           C
ATOM    379  O   PHE A  56       7.974  16.432 -17.083  1.00 13.13           O
ATOM    380  CB  PHE A  56       9.764  17.632 -19.133  1.00 13.70           C
ATOM    381  CG  PHE A  56      10.940  16.702 -19.007  1.00 13.57           C
ATOM    382  CD1 PHE A  56      12.234  17.207 -18.894  1.00 13.27           C
ATOM    383  CD2 PHE A  56      10.754  15.323 -18.991  1.00 11.27           C
ATOM    384  CE1 PHE A  56      13.329  16.356 -18.764  1.00 12.88           C
ATOM    385  CE2 PHE A  56      11.840  14.462 -18.862  1.00 14.04           C
ATOM    386  CZ  PHE A  56      13.133  14.980 -18.747  1.00 13.23           C
ATOM    387  N   LEU A  57       9.649  17.037 -15.717  1.00 12.08           N
ATOM    388  CA  LEU A  57       9.339  16.006 -14.733  1.00 10.43           C
ATOM    389  C   LEU A  57       8.548  16.576 -13.562  1.00 10.20           C
ATOM    390  O   LEU A  57       8.860  17.651 -13.052  1.00 10.94           O
ATOM    391  CB  LEU A  57      10.617  15.340 -14.209  1.00 11.03           C
ATOM    392  CG  LEU A  57      11.515  14.533 -15.157  1.00 12.41           C
ATOM    393  CD1 LEU A  57      12.712  14.007 -14.386  1.00  6.09           C
ATOM    394  CD2 LEU A  57      10.744  13.386 -15.783  1.00 12.21           C
ATOM    395  N   PRO A  58       7.489  15.870 -13.140  1.00  9.33           N
ATOM    396  CA  PRO A  58       6.671  16.336 -12.018  1.00 11.20           C
ATOM    397  C   PRO A  58       7.510  16.354 -10.744  1.00  9.58           C
ATOM    398  O   PRO A  58       8.215  15.391 -10.434  1.00  8.70           O
ATOM    399  CB  PRO A  58       5.558  15.287 -11.948  1.00 11.76           C
ATOM    400  CG  PRO A  58       5.450  14.816 -13.386  1.00  9.41           C
ATOM    401  CD  PRO A  58       6.900  14.669 -13.756  1.00  5.78           C
ATOM    402  N   ARG A  59       7.462  17.473 -10.036  1.00  7.50           N
ATOM    403  CA  ARG A  59       8.209  17.647  -8.799  1.00  8.87           C
ATOM    404  C   ARG A  59       7.279  18.301  -7.778  1.00  7.78           C
ATOM    405  O   ARG A  59       6.383  19.060  -8.150  1.00  8.43           O
ATOM    406  CB  ARG A  59       9.440  18.528  -9.049  1.00 11.88           C
ATOM    407  CG  ARG A  59      10.520  17.871  -9.911  1.00  7.22           C
ATOM    408  CD  ARG A  59      11.101  18.835 -10.954  1.00 17.06           C
ATOM    409  NE  ARG A  59      11.722  20.023 -10.364  1.00  6.44           N
ATOM    410  CZ  ARG A  59      11.295  21.268 -10.559  1.00  7.73           C
ATOM    411  NH1 ARG A  59      10.244  21.503 -11.335  1.00 11.16           N
ATOM    412  NH2 ARG A  59      11.887  22.280  -9.939  1.00  6.29           N
ATOM    413  N   GLY A  60       7.459  17.963  -6.506  1.00  2.95           N
ATOM    414  CA  GLY A  60       6.625  18.530  -5.462  1.00  1.46           C
ATOM    415  C   GLY A  60       6.950  17.948  -4.101  1.00 10.31           C
ATOM    416  O   GLY A  60       7.963  17.249  -3.919  1.00  7.26           O
ATOM    417  N   SER A  61       6.096  18.247  -3.132  1.00 15.23           N
ATOM    418  CA  SER A  61       6.275  17.747  -1.778  1.00 14.55           C
ATOM    419  C   SER A  61       5.476  16.452  -1.631  1.00 12.75           C
ATOM    420  O   SER A  61       4.500  16.234  -2.352  1.00 14.16           O
ATOM    421  CB  SER A  61       5.802  18.806  -0.780  1.00  8.22           C
ATOM    422  OG  SER A  61       4.494  19.243  -1.102  1.00 15.88           O
ATOM    423  N   GLY A  62       5.907  15.580  -0.728  1.00 13.08           N
ATOM    424  CA  GLY A  62       5.199  14.328  -0.530  1.00 14.34           C
ATOM    425  C   GLY A  62       5.558  13.333  -1.616  1.00 17.81           C
ATOM    426  O   GLY A  62       6.635  13.424  -2.210  1.00 21.30           O
ATOM    427  N   ILE A  63       4.673  12.379  -1.883  1.00 13.16           N
ATOM    428  CA  ILE A  63       4.950  11.383  -2.903  1.00 14.00           C
ATOM    429  C   ILE A  63       4.539  11.916  -4.268  1.00 16.24           C
ATOM    430  O   ILE A  63       3.369  12.204  -4.515  1.00 17.47           O
ATOM    431  CB  ILE A  63       4.275  10.017  -2.581  1.00 14.15           C
ATOM    432  CG1 ILE A  63       4.636   8.980  -3.648  1.00 14.88           C
ATOM    433  CG2 ILE A  63       2.776  10.168  -2.438  1.00 10.80           C
ATOM    434  CD1 ILE A  63       4.252   7.561  -3.271  1.00 11.86           C
ATOM    435  N   VAL A  64       5.524  12.103  -5.135  1.00 13.00           N
ATOM    436  CA  VAL A  64       5.263  12.630  -6.463  1.00  9.77           C
ATOM    437  C   VAL A  64       5.449  11.577  -7.552  1.00 11.90           C
ATOM    438  O   VAL A  64       4.485  11.188  -8.215  1.00  9.09           O
ATOM    439  CB  VAL A  64       6.160  13.850  -6.758  1.00  5.18           C
ATOM    440  CG1 VAL A  64       5.740  14.508  -8.071  1.00  2.76           C
ATOM    441  CG2 VAL A  64       6.075  14.852  -5.600  1.00  4.17           C
ATOM    442  N   THR A  65       6.692  11.155  -7.761  1.00 14.48           N
ATOM    443  CA  THR A  65       6.997  10.150  -8.772  1.00 13.78           C
ATOM    444  C   THR A  65       6.480   8.822  -8.242  1.00  9.74           C
ATOM    445  O   THR A  65       7.013   8.289  -7.264  1.00 11.18           O
ATOM    446  CB  THR A  65       8.510  10.073  -9.026  1.00  6.20           C
ATOM    447  OG1 THR A  65       9.005  11.386  -9.325  1.00  8.74           O
ATOM    448  CG2 THR A  65       8.795   9.155 -10.195  1.00  1.68           C
ATOM    449  N   ARG A  66       5.425   8.313  -8.871  1.00  8.40           N
ATOM    450  CA  ARG A  66       4.790   7.070  -8.434  1.00 11.34           C
ATOM    451  C   ARG A  66       4.949   5.882  -9.379  1.00 13.26           C
ATOM    452  O   ARG A  66       4.451   4.789  -9.103  1.00 15.35           O
ATOM    453  CB  ARG A  66       3.312   7.334  -8.129  1.00 17.12           C
ATOM    454  CG  ARG A  66       3.088   8.164  -6.865  1.00 19.90           C
ATOM    455  CD  ARG A  66       1.724   8.850  -6.851  1.00 19.11           C
ATOM    456  NE  ARG A  66       1.691  10.014  -7.738  1.00 15.09           N
ATOM    457  CZ  ARG A  66       0.621  10.409  -8.425  1.00 29.06           C
ATOM    458  NH1 ARG A  66      -0.524   9.735  -8.334  1.00  7.40           N
ATOM    459  NH2 ARG A  66       0.702  11.471  -9.222  1.00 22.33           N
ATOM    460  N   ARG A  67       5.662   6.105 -10.478  1.00 15.69           N
ATOM    461  CA  ARG A  67       5.936   5.080 -11.483  1.00 16.82           C
ATOM    462  C   ARG A  67       7.317   5.366 -12.071  1.00 17.04           C
ATOM    463  O   ARG A  67       7.801   6.498 -12.014  1.00 16.46           O
ATOM    464  CB  ARG A  67       4.900   5.132 -12.614  1.00 15.39           C
ATOM    465  CG  ARG A  67       3.503   4.649 -12.231  1.00 18.72           C
ATOM    466  CD  ARG A  67       2.494   4.899 -13.342  1.00  3.81           C
ATOM    467  NE  ARG A  67       2.768   4.094 -14.531  1.00 16.89           N
ATOM    468  CZ  ARG A  67       2.061   4.153 -15.655  1.00  4.82           C
ATOM    469  NH1 ARG A  67       1.034   4.982 -15.745  1.00  9.47           N
ATOM    470  NH2 ARG A  67       2.386   3.390 -16.693  1.00  6.04           N
ATOM    471  N   PRO A  68       8.010   4.330 -12.558  1.00 16.62           N
ATOM    472  CA  PRO A  68       9.331   4.596 -13.136  1.00 15.94           C
ATOM    473  C   PRO A  68       9.117   5.298 -14.472  1.00 18.58           C
ATOM    474  O   PRO A  68       8.142   5.016 -15.177  1.00 20.47           O
ATOM    475  CB  PRO A  68       9.895   3.194 -13.370  1.00 15.47           C
ATOM    476  CG  PRO A  68       9.140   2.332 -12.385  1.00 17.68           C
ATOM    477  CD  PRO A  68       7.752   2.883 -12.464  1.00 15.96           C
ATOM    478  N   LEU A  69       9.968   6.262 -14.791  1.00 16.18           N
ATOM    479  CA  LEU A  69       9.851   6.932 -16.072  1.00 16.86           C
ATOM    480  C   LEU A  69      11.106   6.615 -16.863  1.00 19.45           C
ATOM    481  O   LEU A  69      12.209   7.020 -16.481  1.00 21.65           O
ATOM    482  CB  LEU A  69       9.694   8.445 -15.927  1.00 15.74           C
ATOM    483  CG  LEU A  69       9.568   9.104 -17.304  1.00 17.30           C
ATOM    484  CD1 LEU A  69       8.187   9.691 -17.478  1.00 14.32           C
ATOM    485  CD2 LEU A  69      10.643  10.163 -17.495  1.00 20.96           C
ATOM    486  N   VAL A  70      10.943   5.806 -17.902  1.00 19.70           N
ATOM    487  CA  VAL A  70      12.054   5.427 -18.760  1.00 19.68           C
ATOM    488  C   VAL A  70      12.102   6.444 -19.887  1.00 19.76           C
ATOM    489  O   VAL A  70      11.195   6.518 -20.722  1.00 18.35           O
ATOM    490  CB  VAL A  70      11.876   4.009 -19.328  1.00 17.98           C
ATOM    491  CG1 VAL A  70      13.042   3.663 -20.252  1.00 17.56           C
ATOM    492  CG2 VAL A  70      11.785   3.010 -18.189  1.00 16.52           C
ATOM    493  N   LEU A  71      13.140   7.266 -19.860  1.00 18.36           N
ATOM    494  CA  LEU A  71      13.324   8.314 -20.845  1.00 18.90           C
ATOM    495  C   LEU A  71      14.458   7.991 -21.804  1.00 19.15           C
ATOM    496  O   LEU A  71      15.580   7.703 -21.390  1.00 20.20           O
ATOM    497  CB  LEU A  71      13.593   9.638 -20.126  1.00 18.34           C
ATOM    498  CG  LEU A  71      14.121  10.835 -20.912  1.00 21.61           C
ATOM    499  CD1 LEU A  71      13.170  11.206 -22.033  1.00 23.92           C
ATOM    500  CD2 LEU A  71      14.308  11.999 -19.964  1.00 19.62           C
ATOM    501  N   GLN A  72      14.149   8.008 -23.090  1.00 17.55           N
ATOM    502  CA  GLN A  72      15.154   7.747 -24.102  1.00 18.96           C
ATOM    503  C   GLN A  72      15.338   9.050 -24.858  1.00 19.22           C
ATOM    504  O   GLN A  72      14.373   9.606 -25.380  1.00 21.08           O
ATOM    505  CB  GLN A  72      14.694   6.627 -25.044  1.00 18.00           C
ATOM    506  CG  GLN A  72      15.577   6.409 -26.272  1.00 53.28           C
ATOM    507  CD  GLN A  72      16.969   5.894 -25.938  1.00 64.18           C
ATOM    508  OE1 GLN A  72      17.124   4.823 -25.358  1.00 76.47           O
ATOM    509  NE2 GLN A  72      17.989   6.650 -26.322  1.00 48.37           N
ATOM    510  N   LEU A  73      16.541   9.609 -24.780  1.00 20.58           N
ATOM    511  CA  LEU A  73      16.857  10.840 -25.496  1.00 21.15           C
ATOM    512  C   LEU A  73      17.298  10.366 -26.871  1.00 22.36           C
ATOM    513  O   LEU A  73      18.111   9.446 -26.977  1.00 22.52           O
ATOM    514  CB  LEU A  73      17.990  11.605 -24.810  1.00 21.49           C
ATOM    515  CG  LEU A  73      17.762  12.105 -23.379  1.00 23.82           C
ATOM    516  CD1 LEU A  73      18.961  12.939 -22.938  1.00 23.65           C
ATOM    517  CD2 LEU A  73      16.489  12.933 -23.297  1.00 21.44           C
ATOM    518  N   VAL A  74      16.710  10.941 -27.916  1.00 21.32           N
ATOM    519  CA  VAL A  74      17.030  10.554 -29.281  1.00 20.08           C
ATOM    520  C   VAL A  74      17.467  11.767 -30.098  1.00 22.70           C
ATOM    521  O   VAL A  74      16.753  12.767 -30.169  1.00 23.60           O
ATOM    522  CB  VAL A  74      15.807   9.887 -29.967  1.00 20.57           C
ATOM    523  CG1 VAL A  74      16.153   9.458 -31.386  1.00 21.67           C
ATOM    524  CG2 VAL A  74      15.331   8.692 -29.160  1.00 20.00           C
ATOM    525  N   ASN A  75      18.652  11.684 -30.692  1.00 23.95           N
ATOM    526  CA  ASN A  75      19.166  12.773 -31.512  1.00 24.75           C
ATOM    527  C   ASN A  75      18.314  12.857 -32.779  1.00 27.00           C
ATOM    528  O   ASN A  75      18.080  11.850 -33.449  1.00 25.85           O
ATOM    529  CB  ASN A  75      20.638  12.528 -31.869  1.00 29.06           C
ATOM    530  CG  ASN A  75      21.273  13.707 -32.591  1.00 26.06           C
ATOM    531  OD1 ASN A  75      22.063  14.451 -32.012  1.00 32.24           O
ATOM    532  ND2 ASN A  75      20.949  13.868 -33.866  1.00 16.80           N
ATOM    533  N   ALA A  76      17.841  14.057 -33.094  1.00 29.50           N
ATOM    534  CA  ALA A  76      17.008  14.278 -34.269  1.00 32.08           C
ATOM    535  C   ALA A  76      17.061  15.747 -34.664  1.00 35.15           C
ATOM    536  O   ALA A  76      17.525  16.582 -33.892  1.00 35.94           O
ATOM    537  CB  ALA A  76      15.572  13.866 -33.976  1.00 32.01           C
ATOM    538  N   THR A  77      16.586  16.060 -35.863  1.00 39.16           N
ATOM    539  CA  THR A  77      16.590  17.437 -36.347  1.00 45.92           C
ATOM    540  C   THR A  77      15.566  18.305 -35.609  1.00 49.43           C
ATOM    541  O   THR A  77      15.846  19.456 -35.266  1.00 49.47           O
ATOM    542  CB  THR A  77      16.295  17.496 -37.863  1.00 47.79           C
ATOM    543  OG1 THR A  77      17.092  16.520 -38.550  1.00 43.20           O
ATOM    544  CG2 THR A  77      16.620  18.881 -38.414  1.00 49.79           C
ATOM    545  N   THR A  78      14.388  17.743 -35.357  1.00 50.01           N
ATOM    546  CA  THR A  78      13.319  18.469 -34.675  1.00 50.65           C
ATOM    547  C   THR A  78      13.342  18.229 -33.165  1.00 42.66           C
ATOM    548  O   THR A  78      13.735  17.154 -32.705  1.00 42.25           O
ATOM    549  CB  THR A  78      11.936  18.059 -35.232  1.00 55.01           C
ATOM    550  OG1 THR A  78      11.943  18.174 -36.661  1.00 51.40           O
ATOM    551  CG2 THR A  78      10.841  18.959 -34.671  1.00 62.36           C
ATOM    552  N   GLU A  79      12.939  19.240 -32.402  1.00 39.42           N
ATOM    553  CA  GLU A  79      12.895  19.134 -30.949  1.00 38.57           C
ATOM    554  C   GLU A  79      11.449  18.962 -30.499  1.00 37.14           C
ATOM    555  O   GLU A  79      10.645  19.893 -30.602  1.00 36.35           O
ATOM    556  CB  GLU A  79      13.510  20.376 -30.302  1.00 41.81           C
ATOM    557  CG  GLU A  79      14.999  20.531 -30.568  1.00 51.09           C
ATOM    558  CD  GLU A  79      15.581  21.805 -29.982  1.00 60.73           C
ATOM    559  OE1 GLU A  79      15.323  22.098 -28.793  1.00 43.79           O
ATOM    560  OE2 GLU A  79      16.305  22.512 -30.716  1.00 62.48           O
ATOM    561  N   TYR A  80      11.124  17.757 -30.034  1.00 34.71           N
ATOM    562  CA  TYR A  80       9.780  17.420 -29.569  1.00 30.63           C
ATOM    563  C   TYR A  80       9.855  16.155 -28.717  1.00 29.81           C
ATOM    564  O   TYR A  80      10.923  15.566 -28.579  1.00 32.58           O
ATOM    565  CB  TYR A  80       8.838  17.187 -30.757  1.00 28.92           C
ATOM    566  CG  TYR A  80       9.159  15.956 -31.577  1.00 28.73           C
ATOM    567  CD1 TYR A  80      10.162  15.980 -32.545  1.00 28.41           C
ATOM    568  CD2 TYR A  80       8.447  14.771 -31.396  1.00 29.33           C
ATOM    569  CE1 TYR A  80      10.446  14.855 -33.314  1.00 29.03           C
ATOM    570  CE2 TYR A  80       8.721  13.641 -32.160  1.00 28.67           C
ATOM    571  CZ  TYR A  80       9.719  13.689 -33.118  1.00 32.68           C
ATOM    572  OH  TYR A  80       9.977  12.577 -33.889  1.00 37.54           O
ATOM    573  N   ALA A  81       8.720  15.714 -28.185  1.00 27.11           N
ATOM    574  CA  ALA A  81       8.681  14.515 -27.353  1.00 26.59           C
ATOM    575  C   ALA A  81       7.423  13.709 -27.627  1.00 25.46           C
ATOM    576  O   ALA A  81       6.418  14.254 -28.087  1.00 28.58           O
ATOM    577  CB  ALA A  81       8.749  14.895 -25.873  1.00 26.87           C
ATOM    578  N   GLU A  82       7.482  12.412 -27.349  1.00 21.22           N
ATOM    579  CA  GLU A  82       6.332  11.536 -27.554  1.00 22.19           C
ATOM    580  C   GLU A  82       6.376  10.355 -26.591  1.00 20.23           C
ATOM    581  O   GLU A  82       7.447   9.801 -26.330  1.00 21.08           O
ATOM    582  CB  GLU A  82       6.272  11.039 -29.004  1.00 28.62           C
ATOM    583  CG  GLU A  82       7.508  10.292 -29.477  1.00 40.70           C
ATOM    584  CD  GLU A  82       7.382   9.791 -30.898  1.00 46.50           C
ATOM    585  OE1 GLU A  82       7.042  10.599 -31.789  1.00 65.04           O
ATOM    586  OE2 GLU A  82       7.625   8.587 -31.126  1.00 35.95           O
ATOM    587  N   PHE A  83       5.221  10.010 -26.029  1.00 16.12           N
ATOM    588  CA  PHE A  83       5.112   8.893 -25.095  1.00 16.57           C
ATOM    589  C   PHE A  83       4.679   7.657 -25.868  1.00 20.00           C
ATOM    590  O   PHE A  83       3.898   7.748 -26.814  1.00 24.19           O
ATOM    591  CB  PHE A  83       4.047   9.166 -24.024  1.00 16.18           C
ATOM    592  CG  PHE A  83       4.347  10.327 -23.118  1.00 15.36           C
ATOM    593  CD1 PHE A  83       4.021  11.623 -23.497  1.00 14.10           C
ATOM    594  CD2 PHE A  83       4.884  10.113 -21.852  1.00 14.71           C
ATOM    595  CE1 PHE A  83       4.217  12.689 -22.627  1.00 15.16           C
ATOM    596  CE2 PHE A  83       5.083  11.168 -20.977  1.00 13.43           C
ATOM    597  CZ  PHE A  83       4.750  12.460 -21.362  1.00 14.59           C
ATOM    598  N   LEU A  84       5.135   6.498 -25.420  1.00 17.33           N
ATOM    599  CA  LEU A  84       4.779   5.249 -26.060  1.00 19.84           C
ATOM    600  C   LEU A  84       3.271   5.030 -25.966  1.00 23.31           C
ATOM    601  O   LEU A  84       2.637   4.596 -26.928  1.00 23.98           O
ATOM    602  CB  LEU A  84       5.506   4.097 -25.378  1.00 20.43           C
ATOM    603  CG  LEU A  84       5.293   2.692 -25.937  1.00 17.75           C
ATOM    604  CD1 LEU A  84       5.736   2.631 -27.388  1.00 17.36           C
ATOM    605  CD2 LEU A  84       6.075   1.710 -25.092  1.00 19.30           C
ATOM    606  N   HIS A  85       2.697   5.372 -24.814  1.00 25.21           N
ATOM    607  CA  HIS A  85       1.266   5.204 -24.592  1.00 24.79           C
ATOM    608  C   HIS A  85       0.381   6.200 -25.355  1.00 26.78           C
ATOM    609  O   HIS A  85      -0.844   6.098 -25.305  1.00 26.31           O
ATOM    610  CB  HIS A  85       0.949   5.213 -23.086  1.00 23.91           C
ATOM    611  CG  HIS A  85       0.987   6.571 -22.458  1.00 23.04           C
ATOM    612  ND1 HIS A  85       2.135   7.121 -21.933  1.00 20.98           N
ATOM    613  CD2 HIS A  85       0.010   7.488 -22.265  1.00 22.79           C
ATOM    614  CE1 HIS A  85       1.868   8.317 -21.447  1.00 20.38           C
ATOM    615  NE2 HIS A  85       0.584   8.564 -21.637  1.00 21.87           N
ATOM    616  N   CYS A  86       0.989   7.151 -26.062  1.00 33.51           N
ATOM    617  CA  CYS A  86       0.230   8.132 -26.841  1.00 37.74           C
ATOM    618  C   CYS A  86       0.661   8.038 -28.308  1.00 37.63           C
ATOM    619  O   CYS A  86       1.280   8.960 -28.846  1.00 37.77           O
ATOM    620  CB  CYS A  86       0.471   9.561 -26.333  1.00 39.87           C
ATOM    621  SG  CYS A  86      -0.048   9.911 -24.638  1.00 41.26           S
ATOM    622  N   LYS A  87       0.358   6.909 -28.940  1.00 39.05           N
ATOM    623  CA  LYS A  87       0.705   6.678 -30.340  1.00 37.94           C
ATOM    624  C   LYS A  87       0.248   7.830 -31.220  1.00 36.40           C
ATOM    625  O   LYS A  87      -0.926   8.186 -31.228  1.00 35.29           O
ATOM    626  CB  LYS A  87       0.079   5.360 -30.834  1.00 41.43           C
ATOM    627  CG  LYS A  87      -0.236   5.297 -32.344  1.00 44.02           C
ATOM    628  CD  LYS A  87       1.013   5.145 -33.210  1.00 46.15           C
ATOM    629  CE  LYS A  87       1.133   6.245 -34.264  1.00 51.22           C
ATOM    630  NZ  LYS A  87      -0.076   6.391 -35.117  1.00 53.21           N
ATOM    631  N   GLY A  88       1.199   8.438 -31.920  1.00 37.01           N
ATOM    632  CA  GLY A  88       0.871   9.524 -32.821  1.00 36.61           C
ATOM    633  C   GLY A  88       1.191  10.933 -32.382  1.00 35.27           C
ATOM    634  O   GLY A  88       1.816  11.680 -33.133  1.00 38.08           O
ATOM    635  N   LYS A  89       0.793  11.299 -31.170  1.00 32.30           N
ATOM    636  CA  LYS A  89       1.034  12.657 -30.698  1.00 30.06           C
ATOM    637  C   LYS A  89       2.497  13.035 -30.485  1.00 28.22           C
ATOM    638  O   LYS A  89       3.297  12.234 -29.992  1.00 28.02           O
ATOM    639  CB  LYS A  89       0.233  12.953 -29.431  1.00 26.81           C
ATOM    640  CG  LYS A  89       0.209  14.432 -29.094  1.00 29.53           C
ATOM    641  CD  LYS A  89      -0.565  14.726 -27.832  1.00 31.60           C
ATOM    642  CE  LYS A  89      -0.369  16.176 -27.401  1.00 14.99           C
ATOM    643  NZ  LYS A  89      -1.030  16.456 -26.082  1.00 38.09           N
ATOM    644  N   LYS A  90       2.818  14.274 -30.851  1.00 26.01           N
ATOM    645  CA  LYS A  90       4.155  14.831 -30.712  1.00 26.59           C
ATOM    646  C   LYS A  90       4.041  16.090 -29.846  1.00 25.19           C
ATOM    647  O   LYS A  90       3.495  17.108 -30.277  1.00 24.19           O
ATOM    648  CB  LYS A  90       4.722  15.211 -32.083  1.00 34.95           C
ATOM    649  CG  LYS A  90       5.036  14.031 -33.002  1.00 38.58           C
ATOM    650  CD  LYS A  90       5.672  14.531 -34.298  1.00 42.47           C
ATOM    651  CE  LYS A  90       6.238  13.397 -35.151  1.00 43.79           C
ATOM    652  NZ  LYS A  90       5.211  12.595 -35.879  1.00 55.73           N
ATOM    653  N   PHE A  91       4.494  15.996 -28.602  1.00 24.66           N
ATOM    654  CA  PHE A  91       4.455  17.124 -27.682  1.00 23.11           C
ATOM    655  C   PHE A  91       5.624  18.045 -27.989  1.00 24.74           C
ATOM    656  O   PHE A  91       6.736  17.577 -28.217  1.00 27.67           O
ATOM    657  CB  PHE A  91       4.588  16.639 -26.233  1.00 21.88           C
ATOM    658  CG  PHE A  91       3.390  15.884 -25.719  1.00 20.15           C
ATOM    659  CD1 PHE A  91       3.116  14.593 -26.161  1.00 19.63           C
ATOM    660  CD2 PHE A  91       2.554  16.457 -24.765  1.00 18.69           C
ATOM    661  CE1 PHE A  91       2.026  13.881 -25.659  1.00 19.22           C
ATOM    662  CE2 PHE A  91       1.462  15.756 -24.255  1.00 19.51           C
ATOM    663  CZ  PHE A  91       1.199  14.463 -24.705  1.00 19.41           C
ATOM    664  N   THR A  92       5.366  19.346 -28.016  1.00 23.40           N
ATOM    665  CA  THR A  92       6.416  20.331 -28.257  1.00 19.29           C
ATOM    666  C   THR A  92       6.489  21.261 -27.050  1.00 19.13           C
ATOM    667  O   THR A  92       7.477  21.972 -26.844  1.00 20.14           O
ATOM    668  CB  THR A  92       6.156  21.147 -29.538  1.00 18.29           C
ATOM    669  OG1 THR A  92       4.865  21.764 -29.465  1.00 30.52           O
ATOM    670  CG2 THR A  92       6.210  20.237 -30.760  1.00 19.71           C
ATOM    671  N   ASP A  93       5.429  21.244 -26.249  1.00 16.54           N
ATOM    672  CA  ASP A  93       5.349  22.062 -25.050  1.00 20.53           C
ATOM    673  C   ASP A  93       5.659  21.133 -23.874  1.00 21.93           C
ATOM    674  O   ASP A  93       4.828  20.311 -23.482  1.00 25.33           O
ATOM    675  CB  ASP A  93       3.940  22.664 -24.926  1.00 22.11           C
ATOM    676  CG  ASP A  93       3.804  23.633 -23.757  1.00 25.94           C
ATOM    677  OD1 ASP A  93       4.768  23.812 -22.985  1.00 21.23           O
ATOM    678  OD2 ASP A  93       2.715  24.222 -23.610  1.00 28.86           O
ATOM    679  N   PHE A  94       6.851  21.270 -23.307  1.00 19.01           N
ATOM    680  CA  PHE A  94       7.259  20.417 -22.196  1.00 17.45           C
ATOM    681  C   PHE A  94       6.424  20.517 -20.920  1.00 15.58           C
ATOM    682  O   PHE A  94       6.491  19.644 -20.060  1.00 17.01           O
ATOM    683  CB  PHE A  94       8.755  20.569 -21.920  1.00 16.88           C
ATOM    684  CG  PHE A  94       9.618  19.935 -22.973  1.00 17.92           C
ATOM    685  CD1 PHE A  94       9.793  20.548 -24.211  1.00 22.08           C
ATOM    686  CD2 PHE A  94      10.223  18.705 -22.747  1.00 16.15           C
ATOM    687  CE1 PHE A  94      10.556  19.940 -25.204  1.00 23.04           C
ATOM    688  CE2 PHE A  94      10.985  18.090 -23.728  1.00 17.81           C
ATOM    689  CZ  PHE A  94      11.153  18.706 -24.961  1.00 22.26           C
ATOM    690  N   GLU A  95       5.625  21.566 -20.793  1.00 13.86           N
ATOM    691  CA  GLU A  95       4.769  21.680 -19.625  1.00 14.64           C
ATOM    692  C   GLU A  95       3.663  20.646 -19.819  1.00 14.78           C
ATOM    693  O   GLU A  95       3.202  20.018 -18.867  1.00 14.35           O
ATOM    694  CB  GLU A  95       4.188  23.090 -19.497  1.00 13.45           C
ATOM    695  CG  GLU A  95       3.193  23.263 -18.348  1.00 28.65           C
ATOM    696  CD  GLU A  95       3.689  22.711 -17.009  1.00 27.02           C
ATOM    697  OE1 GLU A  95       4.912  22.726 -16.742  1.00 38.01           O
ATOM    698  OE2 GLU A  95       2.839  22.265 -16.215  1.00 27.92           O
ATOM    699  N   GLU A  96       3.277  20.444 -21.075  1.00 14.81           N
ATOM    700  CA  GLU A  96       2.257  19.462 -21.404  1.00 13.73           C
ATOM    701  C   GLU A  96       2.821  18.070 -21.155  1.00  9.81           C
ATOM    702  O   GLU A  96       2.103  17.176 -20.731  1.00 12.07           O
ATOM    703  CB  GLU A  96       1.807  19.618 -22.859  1.00 16.01           C
ATOM    704  CG  GLU A  96       1.053  20.923 -23.130  1.00 10.29           C
ATOM    705  CD  GLU A  96      -0.233  21.057 -22.319  1.00 29.43           C
ATOM    706  OE1 GLU A  96      -0.883  20.026 -22.027  1.00 26.53           O
ATOM    707  OE2 GLU A  96      -0.595  22.205 -21.975  1.00 46.06           O
ATOM    708  N   VAL A  97       4.120  17.900 -21.391  1.00  9.14           N
ATOM    709  CA  VAL A  97       4.773  16.615 -21.156  1.00  9.35           C
ATOM    710  C   VAL A  97       4.708  16.311 -19.656  1.00  9.52           C
ATOM    711  O   VAL A  97       4.334  15.210 -19.252  1.00  9.08           O
ATOM    712  CB  VAL A  97       6.255  16.626 -21.633  1.00  9.19           C
ATOM    713  CG1 VAL A  97       6.941  15.305 -21.301  1.00  7.34           C
ATOM    714  CG2 VAL A  97       6.324  16.875 -23.128  1.00  8.86           C
ATOM    715  N   ARG A  98       5.047  17.304 -18.839  1.00 11.25           N
ATOM    716  CA  ARG A  98       5.013  17.162 -17.385  1.00 13.46           C
ATOM    717  C   ARG A  98       3.600  16.783 -16.950  1.00 14.08           C
ATOM    718  O   ARG A  98       3.408  15.837 -16.179  1.00 14.01           O
ATOM    719  CB  ARG A  98       5.409  18.485 -16.716  1.00 21.41           C
ATOM    720  CG  ARG A  98       5.653  18.389 -15.215  1.00 12.61           C
ATOM    721  CD  ARG A  98       5.872  19.772 -14.592  1.00 12.16           C
ATOM    722  NE  ARG A  98       4.632  20.546 -14.511  1.00 31.98           N
ATOM    723  CZ  ARG A  98       3.627  20.281 -13.676  1.00 29.25           C
ATOM    724  NH1 ARG A  98       3.700  19.260 -12.829  1.00 29.19           N
ATOM    725  NH2 ARG A  98       2.528  21.020 -13.711  1.00 14.62           N
ATOM    726  N   LEU A  99       2.616  17.510 -17.477  1.00 12.66           N
ATOM    727  CA  LEU A  99       1.217  17.271 -17.148  1.00 14.81           C
ATOM    728  C   LEU A  99       0.781  15.881 -17.566  1.00 16.64           C
ATOM    729  O   LEU A  99       0.073  15.199 -16.825  1.00 17.84           O
ATOM    730  CB  LEU A  99       0.318  18.321 -17.805  1.00 15.24           C
ATOM    731  CG  LEU A  99       0.368  19.728 -17.204  1.00 13.91           C
ATOM    732  CD1 LEU A  99      -0.322  20.714 -18.139  1.00 17.43           C
ATOM    733  CD2 LEU A  99      -0.296  19.731 -15.832  1.00 10.44           C
ATOM    734  N   GLU A 100       1.218  15.456 -18.746  1.00 19.48           N
ATOM    735  CA  GLU A 100       0.864  14.138 -19.240  1.00 19.21           C
ATOM    736  C   GLU A 100       1.451  13.046 -18.361  1.00 17.89           C
ATOM    737  O   GLU A 100       0.789  12.043 -18.100  1.00 20.10           O
ATOM    738  CB  GLU A 100       1.305  13.951 -20.690  1.00 20.86           C
ATOM    739  CG  GLU A 100       0.953  12.576 -21.269  1.00  9.43           C
ATOM    740  CD  GLU A 100      -0.503  12.193 -21.052  1.00 22.10           C
ATOM    741  OE1 GLU A 100      -1.384  13.059 -21.218  1.00 16.02           O
ATOM    742  OE2 GLU A 100      -0.766  11.021 -20.712  1.00 19.34           O
ATOM    743  N   ILE A 101       2.680  13.235 -17.890  1.00 14.78           N
ATOM    744  CA  ILE A 101       3.296  12.232 -17.026  1.00 13.96           C
ATOM    745  C   ILE A 101       2.441  12.094 -15.771  1.00 14.79           C
ATOM    746  O   ILE A 101       2.112  10.980 -15.342  1.00 13.63           O
ATOM    747  CB  ILE A 101       4.743  12.603 -16.643  1.00 13.60           C
ATOM    748  CG1 ILE A 101       5.649  12.516 -17.881  1.00  9.50           C
ATOM    749  CG2 ILE A 101       5.243  11.678 -15.517  1.00 10.69           C
ATOM    750  CD1 ILE A 101       7.008  13.226 -17.746  1.00  1.96           C
ATOM    751  N   GLU A 102       2.042  13.234 -15.218  1.00 13.08           N
ATOM    752  CA  GLU A 102       1.208  13.255 -14.025  1.00 13.96           C
ATOM    753  C   GLU A 102      -0.131  12.558 -14.302  1.00 11.90           C
ATOM    754  O   GLU A 102      -0.524  11.652 -13.570  1.00  9.61           O
ATOM    755  CB  GLU A 102       0.989  14.705 -13.569  1.00 14.04           C
ATOM    756  CG  GLU A 102       0.049  14.868 -12.390  1.00 16.95           C
ATOM    757  CD  GLU A 102       0.026  16.292 -11.862  1.00 55.09           C
ATOM    758  OE1 GLU A 102      -0.688  17.138 -12.446  1.00 56.75           O
ATOM    759  OE2 GLU A 102       0.729  16.567 -10.865  1.00 68.99           O
ATOM    760  N   ALA A 103      -0.782  12.937 -15.401  1.00 13.04           N
ATOM    761  CA  ALA A 103      -2.072  12.362 -15.784  1.00 13.89           C
ATOM    762  C   ALA A 103      -1.995  10.857 -16.017  1.00 13.45           C
ATOM    763  O   ALA A 103      -2.894  10.113 -15.628  1.00 16.89           O
ATOM    764  CB  ALA A 103      -2.620  13.058 -17.023  1.00 13.23           C
ATOM    765  N   GLU A 104      -0.922  10.410 -16.653  1.00 13.60           N
ATOM    766  CA  GLU A 104      -0.733   8.991 -16.924  1.00 12.09           C
ATOM    767  C   GLU A 104      -0.471   8.251 -15.621  1.00 13.30           C
ATOM    768  O   GLU A 104      -0.811   7.070 -15.485  1.00 14.85           O
ATOM    769  CB  GLU A 104       0.421   8.788 -17.913  1.00  8.43           C
ATOM    770  CG  GLU A 104       0.836   7.334 -18.136  1.00 14.49           C
ATOM    771  CD  GLU A 104      -0.308   6.411 -18.553  1.00 23.17           C
ATOM    772  OE1 GLU A 104      -1.312   6.878 -19.135  1.00 15.73           O
ATOM    773  OE2 GLU A 104      -0.192   5.196 -18.300  1.00 21.96           O
ATOM    774  N   THR A 105       0.128   8.948 -14.658  1.00 12.44           N
ATOM    775  CA  THR A 105       0.400   8.345 -13.360  1.00 13.32           C
ATOM    776  C   THR A 105      -0.922   8.164 -12.614  1.00 16.53           C
ATOM    777  O   THR A 105      -1.270   7.045 -12.245  1.00 19.21           O
ATOM    778  CB  THR A 105       1.386   9.192 -12.524  1.00 14.43           C
ATOM    779  OG1 THR A 105       2.646   9.275 -13.209  1.00  8.22           O
ATOM    780  CG2 THR A 105       1.610   8.561 -11.160  1.00 11.91           C
ATOM    781  N   ASP A 106      -1.688   9.246 -12.473  1.00 14.36           N
ATOM    782  CA  ASP A 106      -2.979   9.203 -11.776  1.00 13.63           C
ATOM    783  C   ASP A 106      -3.919   8.166 -12.381  1.00 13.22           C
ATOM    784  O   ASP A 106      -4.613   7.454 -11.662  1.00 11.43           O
ATOM    785  CB  ASP A 106      -3.680  10.570 -11.823  1.00  7.54           C
ATOM    786  CG  ASP A 106      -2.910  11.661 -11.100  1.00 13.20           C
ATOM    787  OD1 ASP A 106      -2.154  11.352 -10.156  1.00 13.77           O
ATOM    788  OD2 ASP A 106      -3.075  12.841 -11.478  1.00 15.97           O
ATOM    789  N   ARG A 107      -3.944   8.099 -13.706  1.00 13.84           N
ATOM    790  CA  ARG A 107      -4.811   7.160 -14.404  1.00 17.68           C
ATOM    791  C   ARG A 107      -4.598   5.736 -13.906  1.00 13.49           C
ATOM    792  O   ARG A 107      -5.554   4.994 -13.681  1.00 15.28           O
ATOM    793  CB  ARG A 107      -4.561   7.224 -15.915  1.00 18.65           C
ATOM    794  CG  ARG A 107      -5.507   6.367 -16.735  1.00 18.95           C
ATOM    795  CD  ARG A 107      -5.083   6.302 -18.196  1.00 24.70           C
ATOM    796  NE  ARG A 107      -3.888   5.481 -18.389  1.00 30.29           N
ATOM    797  CZ  ARG A 107      -3.887   4.150 -18.448  1.00 31.12           C
ATOM    798  NH1 ARG A 107      -5.021   3.469 -18.327  1.00 18.41           N
ATOM    799  NH2 ARG A 107      -2.746   3.496 -18.629  1.00 17.52           N
ATOM    800  N   VAL A 108      -3.340   5.371 -13.705  1.00 12.93           N
ATOM    801  CA  VAL A 108      -3.000   4.030 -13.255  1.00 14.05           C
ATOM    802  C   VAL A 108      -2.932   3.841 -11.742  1.00 16.56           C
ATOM    803  O   VAL A 108      -3.363   2.811 -11.237  1.00 17.43           O
ATOM    804  CB  VAL A 108      -1.664   3.557 -13.898  1.00 13.10           C
ATOM    805  CG1 VAL A 108      -1.231   2.208 -13.325  1.00 13.12           C
ATOM    806  CG2 VAL A 108      -1.827   3.442 -15.410  1.00 11.93           C
ATOM    807  N   THR A 109      -2.394   4.829 -11.030  1.00 19.40           N
ATOM    808  CA  THR A 109      -2.221   4.754  -9.577  1.00 12.46           C
ATOM    809  C   THR A 109      -3.294   5.418  -8.713  1.00 12.79           C
ATOM    810  O   THR A 109      -3.336   5.195  -7.500  1.00 13.04           O
ATOM    811  CB  THR A 109      -0.864   5.377  -9.155  1.00  9.98           C
ATOM    812  OG1 THR A 109      -0.843   6.766  -9.513  1.00 12.93           O
ATOM    813  CG2 THR A 109       0.301   4.670  -9.842  1.00 10.23           C
ATOM    814  N   GLY A 110      -4.138   6.250  -9.311  1.00 12.97           N
ATOM    815  CA  GLY A 110      -5.147   6.949  -8.530  1.00 12.16           C
ATOM    816  C   GLY A 110      -4.506   8.125  -7.802  1.00 14.74           C
ATOM    817  O   GLY A 110      -3.320   8.410  -8.015  1.00 15.61           O
ATOM    818  N   THR A 111      -5.262   8.811  -6.947  1.00  9.72           N
ATOM    819  CA  THR A 111      -4.727   9.961  -6.228  1.00  4.21           C
ATOM    820  C   THR A 111      -4.604   9.776  -4.718  1.00 10.25           C
ATOM    821  O   THR A 111      -4.541  10.754  -3.978  1.00  9.06           O
ATOM    822  CB  THR A 111      -5.532  11.255  -6.518  1.00 10.71           C
ATOM    823  OG1 THR A 111      -6.926  11.036  -6.260  1.00 20.08           O
ATOM    824  CG2 THR A 111      -5.348  11.691  -7.972  1.00 14.89           C
ATOM    825  N   ASN A 112      -4.552   8.531  -4.256  1.00 10.60           N
ATOM    826  CA  ASN A 112      -4.427   8.294  -2.825  1.00 12.23           C
ATOM    827  C   ASN A 112      -3.101   7.610  -2.472  1.00 14.37           C
ATOM    828  O   ASN A 112      -3.075   6.571  -1.801  1.00 11.98           O
ATOM    829  CB  ASN A 112      -5.624   7.497  -2.291  1.00 10.79           C
ATOM    830  CG  ASN A 112      -5.651   7.436  -0.772  1.00 13.13           C
ATOM    831  OD1 ASN A 112      -5.201   8.359  -0.090  1.00  8.21           O
ATOM    832  ND2 ASN A 112      -6.175   6.346  -0.235  1.00 13.84           N
ATOM    833  N   LYS A 113      -2.010   8.184  -2.983  1.00 15.18           N
ATOM    834  CA  LYS A 113      -0.632   7.729  -2.739  1.00 15.68           C
ATOM    835  C   LYS A 113      -0.155   6.409  -3.347  1.00 15.86           C
ATOM    836  O   LYS A 113       0.980   5.991  -3.101  1.00 15.56           O
ATOM    837  CB  LYS A 113      -0.321   7.728  -1.234  1.00 14.88           C
ATOM    838  CG  LYS A 113      -0.849   8.943  -0.464  1.00 16.61           C
ATOM    839  CD  LYS A 113      -0.460  10.260  -1.118  1.00 15.63           C
ATOM    840  CE  LYS A 113      -1.095  11.441  -0.394  1.00 34.27           C
ATOM    841  NZ  LYS A 113      -0.735  11.472   1.049  1.00 18.66           N
ATOM    842  N   GLY A 114      -0.989   5.768  -4.155  1.00 14.80           N
ATOM    843  CA  GLY A 114      -0.599   4.503  -4.755  1.00 12.66           C
ATOM    844  C   GLY A 114       0.588   4.570  -5.700  1.00 13.70           C
ATOM    845  O   GLY A 114       0.927   5.634  -6.223  1.00 14.40           O
ATOM    846  N   ILE A 115       1.234   3.427  -5.907  1.00 13.53           N
ATOM    847  CA  ILE A 115       2.376   3.342  -6.811  1.00 16.69           C
ATOM    848  C   ILE A 115       2.178   2.180  -7.780  1.00 20.30           C
ATOM    849  O   ILE A 115       1.393   1.263  -7.518  1.00 25.62           O
ATOM    850  CB  ILE A 115       3.707   3.116  -6.058  1.00 17.66           C
ATOM    851  CG1 ILE A 115       3.656   1.791  -5.290  1.00 23.02           C
ATOM    852  CG2 ILE A 115       4.008   4.305  -5.143  1.00 12.96           C
ATOM    853  CD1 ILE A 115       4.977   1.061  -5.234  1.00 26.53           C
ATOM    854  N   SER A 116       2.897   2.217  -8.895  1.00 19.48           N
ATOM    855  CA  SER A 116       2.813   1.168  -9.895  1.00 13.38           C
ATOM    856  C   SER A 116       4.197   0.909 -10.467  1.00 16.02           C
ATOM    857  O   SER A 116       4.972   1.846 -10.681  1.00 14.72           O
ATOM    858  CB  SER A 116       1.865   1.578 -11.018  1.00 13.89           C
ATOM    859  OG  SER A 116       1.894   0.642 -12.081  1.00 25.63           O
ATOM    860  N   PRO A 117       4.542  -0.375 -10.680  1.00 15.17           N
ATOM    861  CA  PRO A 117       5.844  -0.756 -11.232  1.00 13.45           C
ATOM    862  C   PRO A 117       5.891  -0.597 -12.752  1.00 12.57           C
ATOM    863  O   PRO A 117       6.953  -0.708 -13.361  1.00 15.75           O
ATOM    864  CB  PRO A 117       5.972  -2.222 -10.805  1.00 14.40           C
ATOM    865  CG  PRO A 117       4.554  -2.706 -10.864  1.00 13.66           C
ATOM    866  CD  PRO A 117       3.798  -1.564 -10.215  1.00 14.32           C
ATOM    867  N   VAL A 118       4.740  -0.339 -13.364  1.00  7.92           N
ATOM    868  CA  VAL A 118       4.666  -0.173 -14.807  1.00 10.28           C
ATOM    869  C   VAL A 118       5.277   1.173 -15.219  1.00 14.51           C
ATOM    870  O   VAL A 118       4.791   2.231 -14.823  1.00 16.00           O
ATOM    871  CB  VAL A 118       3.203  -0.254 -15.308  1.00 11.77           C
ATOM    872  CG1 VAL A 118       3.165  -0.295 -16.830  1.00 11.80           C
ATOM    873  CG2 VAL A 118       2.509  -1.469 -14.717  1.00 11.10           C
ATOM    874  N   PRO A 119       6.348   1.143 -16.028  1.00 15.40           N
ATOM    875  CA  PRO A 119       7.032   2.349 -16.495  1.00 15.74           C
ATOM    876  C   PRO A 119       6.268   3.175 -17.520  1.00 14.79           C
ATOM    877  O   PRO A 119       5.445   2.664 -18.278  1.00 13.69           O
ATOM    878  CB  PRO A 119       8.318   1.797 -17.134  1.00 17.57           C
ATOM    879  CG  PRO A 119       8.480   0.425 -16.516  1.00 20.01           C
ATOM    880  CD  PRO A 119       7.063  -0.062 -16.485  1.00 18.59           C
ATOM    881  N   ILE A 120       6.528   4.474 -17.501  1.00 16.28           N
ATOM    882  CA  ILE A 120       5.948   5.394 -18.461  1.00 17.83           C
ATOM    883  C   ILE A 120       7.149   5.576 -19.383  1.00 18.73           C
ATOM    884  O   ILE A 120       8.266   5.828 -18.909  1.00 13.98           O
ATOM    885  CB  ILE A 120       5.558   6.739 -17.816  1.00 16.07           C
ATOM    886  CG1 ILE A 120       4.398   6.533 -16.839  1.00 18.47           C
ATOM    887  CG2 ILE A 120       5.183   7.756 -18.888  1.00 15.33           C
ATOM    888  CD1 ILE A 120       3.893   7.818 -16.201  1.00 18.33           C
ATOM    889  N   ASN A 121       6.945   5.335 -20.673  1.00 19.64           N
ATOM    890  CA  ASN A 121       8.026   5.444 -21.650  1.00 21.92           C
ATOM    891  C   ASN A 121       7.954   6.750 -22.407  1.00 21.16           C
ATOM    892  O   ASN A 121       6.926   7.079 -23.002  1.00 24.19           O
ATOM    893  CB  ASN A 121       7.987   4.259 -22.613  1.00 22.33           C
ATOM    894  CG  ASN A 121       7.958   2.935 -21.885  1.00 22.06           C
ATOM    895  OD1 ASN A 121       8.996   2.406 -21.488  1.00 25.61           O
ATOM    896  ND2 ASN A 121       6.763   2.414 -21.660  1.00 20.28           N
ATOM    897  N   LEU A 122       9.055   7.488 -22.395  1.00 18.17           N
ATOM    898  CA  LEU A 122       9.098   8.774 -23.057  1.00 17.26           C
ATOM    899  C   LEU A 122      10.339   8.967 -23.905  1.00 18.21           C
ATOM    900  O   LEU A 122      11.456   8.723 -23.456  1.00 19.01           O
ATOM    901  CB  LEU A 122       9.021   9.893 -22.020  1.00 16.25           C
ATOM    902  CG  LEU A 122       9.143  11.319 -22.551  1.00 15.08           C
ATOM    903  CD1 LEU A 122       7.936  11.643 -23.420  1.00 14.20           C
ATOM    904  CD2 LEU A 122       9.258  12.298 -21.385  1.00 12.99           C
ATOM    905  N   ARG A 123      10.121   9.412 -25.139  1.00 18.67           N
ATOM    906  CA  ARG A 123      11.201   9.689 -26.068  1.00 17.08           C
ATOM    907  C   ARG A 123      11.270  11.191 -26.286  1.00 17.53           C
ATOM    908  O   ARG A 123      10.263  11.818 -26.608  1.00 19.83           O
ATOM    909  CB  ARG A 123      10.961   8.989 -27.409  1.00 13.40           C
ATOM    910  CG  ARG A 123      11.308   7.509 -27.418  1.00 16.33           C
ATOM    911  CD  ARG A 123      11.342   6.975 -28.842  1.00 19.61           C
ATOM    912  NE  ARG A 123      12.299   5.878 -28.977  1.00 31.95           N
ATOM    913  CZ  ARG A 123      13.071   5.685 -30.042  1.00 27.11           C
ATOM    914  NH1 ARG A 123      13.003   6.510 -31.079  1.00 41.50           N
ATOM    915  NH2 ARG A 123      13.919   4.668 -30.067  1.00 41.03           N
ATOM    916  N   VAL A 124      12.436  11.777 -26.046  1.00 19.91           N
ATOM    917  CA  VAL A 124      12.626  13.212 -26.254  1.00 22.34           C
ATOM    918  C   VAL A 124      13.610  13.394 -27.408  1.00 25.07           C
ATOM    919  O   VAL A 124      14.769  12.972 -27.325  1.00 26.53           O
ATOM    920  CB  VAL A 124      13.170  13.926 -24.988  1.00 22.24           C
ATOM    921  CG1 VAL A 124      13.508  15.378 -25.305  1.00 22.57           C
ATOM    922  CG2 VAL A 124      12.140  13.874 -23.869  1.00 21.47           C
ATOM    923  N   TYR A 125      13.127  13.976 -28.499  1.00 24.36           N
ATOM    924  CA  TYR A 125      13.948  14.202 -29.677  1.00 26.45           C
ATOM    925  C   TYR A 125      14.585  15.581 -29.648  1.00 28.06           C
ATOM    926  O   TYR A 125      13.936  16.570 -29.289  1.00 27.76           O
ATOM    927  CB  TYR A 125      13.112  14.026 -30.945  1.00 26.54           C
ATOM    928  CG  TYR A 125      12.529  12.640 -31.093  1.00 26.47           C
ATOM    929  CD1 TYR A 125      11.345  12.291 -30.449  1.00 28.04           C
ATOM    930  CD2 TYR A 125      13.155  11.678 -31.881  1.00 25.02           C
ATOM    931  CE1 TYR A 125      10.795  11.020 -30.589  1.00 29.83           C
ATOM    932  CE2 TYR A 125      12.614  10.402 -32.027  1.00 28.12           C
ATOM    933  CZ  TYR A 125      11.432  10.081 -31.380  1.00 28.49           C
ATOM    934  OH  TYR A 125      10.868   8.834 -31.547  1.00 27.50           O
ATOM    935  N   SER A 126      15.861  15.632 -30.020  1.00 29.96           N
ATOM    936  CA  SER A 126      16.635  16.868 -30.046  1.00 30.80           C
ATOM    937  C   SER A 126      17.967  16.602 -30.738  1.00 34.73           C
ATOM    938  O   SER A 126      18.489  15.490 -30.683  1.00 33.56           O
ATOM    939  CB  SER A 126      16.886  17.358 -28.614  1.00 30.40           C
ATOM    940  OG  SER A 126      17.787  18.454 -28.577  1.00 39.24           O
ATOM    941  N   PRO A 127      18.518  17.608 -31.432  1.00 39.28           N
ATOM    942  CA  PRO A 127      19.800  17.432 -32.120  1.00 40.57           C
ATOM    943  C   PRO A 127      21.014  17.647 -31.213  1.00 40.65           C
ATOM    944  O   PRO A 127      22.156  17.498 -31.651  1.00 40.20           O
ATOM    945  CB  PRO A 127      19.736  18.492 -33.218  1.00 42.12           C
ATOM    946  CG  PRO A 127      18.986  19.598 -32.557  1.00 42.21           C
ATOM    947  CD  PRO A 127      17.867  18.865 -31.846  1.00 41.32           C
ATOM    948  N   HIS A 128      20.773  17.984 -29.951  1.00 42.27           N
ATOM    949  CA  HIS A 128      21.869  18.244 -29.020  1.00 43.31           C
ATOM    950  C   HIS A 128      21.954  17.240 -27.876  1.00 40.17           C
ATOM    951  O   HIS A 128      22.318  17.608 -26.758  1.00 41.19           O
ATOM    952  CB  HIS A 128      21.728  19.656 -28.438  1.00 45.56           C
ATOM    953  CG  HIS A 128      21.450  20.709 -29.465  1.00 48.28           C
ATOM    954  ND1 HIS A 128      22.350  21.041 -30.455  1.00 49.29           N
ATOM    955  CD2 HIS A 128      20.363  21.490 -29.668  1.00 49.12           C
ATOM    956  CE1 HIS A 128      21.829  21.980 -31.224  1.00 49.54           C
ATOM    957  NE2 HIS A 128      20.624  22.270 -30.768  1.00 49.56           N
ATOM    958  N   VAL A 129      21.649  15.975 -28.148  1.00 34.80           N
ATOM    959  CA  VAL A 129      21.684  14.958 -27.099  1.00 31.18           C
ATOM    960  C   VAL A 129      22.285  13.639 -27.555  1.00 28.46           C
ATOM    961  O   VAL A 129      22.333  13.344 -28.752  1.00 26.80           O
ATOM    962  CB  VAL A 129      20.257  14.644 -26.558  1.00 30.80           C
ATOM    963  CG1 VAL A 129      19.617  15.886 -25.966  1.00 30.78           C
ATOM    964  CG2 VAL A 129      19.378  14.066 -27.670  1.00 30.49           C
ATOM    965  N   LEU A 130      22.757  12.857 -26.590  1.00 26.83           N
ATOM    966  CA  LEU A 130      23.303  11.534 -26.871  1.00 24.76           C
ATOM    967  C   LEU A 130      22.081  10.625 -26.867  1.00 25.24           C
ATOM    968  O   LEU A 130      21.047  10.968 -26.285  1.00 25.50           O
ATOM    969  CB  LEU A 130      24.247  11.068 -25.757  1.00 23.01           C
ATOM    970  CG  LEU A 130      25.662  11.617 -25.570  1.00 23.83           C
ATOM    971  CD1 LEU A 130      26.481  11.382 -26.824  1.00 24.44           C
ATOM    972  CD2 LEU A 130      25.619  13.085 -25.210  1.00 29.57           C
ATOM    973  N   ASN A 131      22.184   9.474 -27.516  1.00 25.64           N
ATOM    974  CA  ASN A 131      21.075   8.529 -27.538  1.00 22.58           C
ATOM    975  C   ASN A 131      21.126   7.789 -26.200  1.00 25.03           C
ATOM    976  O   ASN A 131      21.513   6.620 -26.126  1.00 27.16           O
ATOM    977  CB  ASN A 131      21.217   7.581 -28.733  1.00  5.76           C
ATOM    978  CG  ASN A 131      20.963   8.284 -30.066  1.00 24.35           C
ATOM    979  OD1 ASN A 131      19.893   8.853 -30.290  1.00 19.69           O
ATOM    980  ND2 ASN A 131      21.951   8.259 -30.947  1.00 30.28           N
ATOM    981  N   LEU A 132      20.759   8.510 -25.141  1.00 22.56           N
ATOM    982  CA  LEU A 132      20.784   8.006 -23.765  1.00 22.81           C
ATOM    983  C   LEU A 132      19.454   7.537 -23.199  1.00 19.69           C
ATOM    984  O   LEU A 132      18.389   7.979 -23.624  1.00 23.16           O
ATOM    985  CB  LEU A 132      21.293   9.101 -22.823  1.00 25.25           C
ATOM    986  CG  LEU A 132      22.761   9.298 -22.473  1.00 29.74           C
ATOM    987  CD1 LEU A 132      22.867  10.522 -21.581  1.00 30.91           C
ATOM    988  CD2 LEU A 132      23.303   8.072 -21.759  1.00 33.24           C
ATOM    989  N   THR A 133      19.544   6.699 -22.176  1.00 14.49           N
ATOM    990  CA  THR A 133      18.381   6.190 -21.474  1.00 19.13           C
ATOM    991  C   THR A 133      18.529   6.621 -20.012  1.00 24.21           C
ATOM    992  O   THR A 133      19.538   6.325 -19.363  1.00 25.11           O
ATOM    993  CB  THR A 133      18.298   4.652 -21.552  1.00 27.67           C
ATOM    994  OG1 THR A 133      17.952   4.257 -22.885  1.00 31.38           O
ATOM    995  CG2 THR A 133      17.243   4.116 -20.584  1.00 27.34           C
ATOM    996  N   LEU A 134      17.550   7.368 -19.516  1.00 23.08           N
ATOM    997  CA  LEU A 134      17.563   7.838 -18.139  1.00 22.11           C
ATOM    998  C   LEU A 134      16.298   7.316 -17.474  1.00 22.55           C
ATOM    999  O   LEU A 134      15.256   7.203 -18.119  1.00 23.23           O
ATOM   1000  CB  LEU A 134      17.603   9.368 -18.084  1.00 22.46           C
ATOM   1001  CG  LEU A 134      18.778  10.083 -18.763  1.00 25.33           C
ATOM   1002  CD1 LEU A 134      18.584  10.122 -20.278  1.00 22.89           C
ATOM   1003  CD2 LEU A 134      18.883  11.493 -18.224  1.00 30.93           C
ATOM   1004  N   VAL A 135      16.392   6.987 -16.193  1.00 19.64           N
ATOM   1005  CA  VAL A 135      15.256   6.455 -15.464  1.00 14.43           C
ATOM   1006  C   VAL A 135      14.964   7.233 -14.191  1.00 12.81           C
ATOM   1007  O   VAL A 135      15.819   7.325 -13.310  1.00 14.83           O
ATOM   1008  CB  VAL A 135      15.489   4.977 -15.065  1.00 14.12           C
ATOM   1009  CG1 VAL A 135      14.266   4.424 -14.365  1.00 14.42           C
ATOM   1010  CG2 VAL A 135      15.827   4.137 -16.290  1.00 14.93           C
ATOM   1011  N   ASP A 136      13.769   7.816 -14.114  1.00  9.98           N
ATOM   1012  CA  ASP A 136      13.349   8.533 -12.914  1.00  9.77           C
ATOM   1013  C   ASP A 136      12.614   7.484 -12.095  1.00 11.96           C
ATOM   1014  O   ASP A 136      11.800   6.738 -12.637  1.00 17.85           O
ATOM   1015  CB  ASP A 136      12.404   9.692 -13.245  1.00  7.26           C
ATOM   1016  CG  ASP A 136      12.171  10.611 -12.053  1.00  9.66           C
ATOM   1017  OD1 ASP A 136      13.009  10.620 -11.126  1.00  8.93           O
ATOM   1018  OD2 ASP A 136      11.151  11.322 -12.036  1.00  8.20           O
ATOM   1019  N   LEU A 137      12.890   7.420 -10.799  1.00 11.36           N
ATOM   1020  CA  LEU A 137      12.265   6.414  -9.948  1.00  9.52           C
ATOM   1021  C   LEU A 137      11.653   6.959  -8.669  1.00  8.54           C
ATOM   1022  O   LEU A 137      12.063   8.008  -8.172  1.00  8.10           O
ATOM   1023  CB  LEU A 137      13.300   5.352  -9.566  1.00  9.65           C
ATOM   1024  CG  LEU A 137      13.865   4.506 -10.702  1.00 10.70           C
ATOM   1025  CD1 LEU A 137      15.200   3.905 -10.305  1.00  8.58           C
ATOM   1026  CD2 LEU A 137      12.856   3.433 -11.072  1.00 14.13           C
ATOM   1027  N   PRO A 138      10.632   6.262  -8.142  1.00  8.96           N
ATOM   1028  CA  PRO A 138       9.939   6.636  -6.908  1.00  9.17           C
ATOM   1029  C   PRO A 138      10.938   6.613  -5.749  1.00  6.84           C
ATOM   1030  O   PRO A 138      11.934   5.891  -5.801  1.00  7.80           O
ATOM   1031  CB  PRO A 138       8.912   5.517  -6.756  1.00 10.14           C
ATOM   1032  CG  PRO A 138       8.575   5.191  -8.174  1.00  9.24           C
ATOM   1033  CD  PRO A 138       9.934   5.147  -8.808  1.00  9.96           C
ATOM   1034  N   GLY A 139      10.684   7.416  -4.723  1.00  4.85           N
ATOM   1035  CA  GLY A 139      11.574   7.455  -3.579  1.00  5.39           C
ATOM   1036  C   GLY A 139      11.356   6.296  -2.625  1.00  9.69           C
ATOM   1037  O   GLY A 139      10.246   5.777  -2.502  1.00 10.64           O
ATOM   1038  N   MET A 140      12.424   5.880  -1.959  1.00  9.47           N
ATOM   1039  CA  MET A 140      12.354   4.795  -0.996  1.00 10.93           C
ATOM   1040  C   MET A 140      11.657   5.277   0.275  1.00 13.92           C
ATOM   1041  O   MET A 140      11.830   6.431   0.685  1.00 15.76           O
ATOM   1042  CB  MET A 140      13.761   4.288  -0.672  1.00  9.90           C
ATOM   1043  CG  MET A 140      14.447   3.646  -1.858  1.00 10.99           C
ATOM   1044  SD  MET A 140      16.103   3.063  -1.511  1.00 16.00           S
ATOM   1045  CE  MET A 140      17.046   4.249  -2.417  1.00 16.31           C
ATOM   1046  N   THR A 141      10.868   4.397   0.884  1.00 13.06           N
ATOM   1047  CA  THR A 141      10.131   4.721   2.102  1.00 10.54           C
ATOM   1048  C   THR A 141      10.248   3.636   3.170  1.00 12.46           C
ATOM   1049  O   THR A 141      10.897   2.612   2.965  1.00 15.90           O
ATOM   1050  CB  THR A 141       8.629   4.970   1.803  1.00  7.89           C
ATOM   1051  OG1 THR A 141       8.093   3.870   1.059  1.00 19.34           O
ATOM   1052  CG2 THR A 141       8.446   6.248   1.007  1.00 11.21           C
ATOM   1053  N   LYS A 142       9.606   3.865   4.310  1.00 15.07           N
ATOM   1054  CA  LYS A 142       9.637   2.920   5.419  1.00 17.71           C
ATOM   1055  C   LYS A 142       8.249   2.475   5.879  1.00 21.17           C
ATOM   1056  O   LYS A 142       8.080   1.341   6.327  1.00 23.96           O
ATOM   1057  CB  LYS A 142      10.418   3.517   6.592  1.00 10.69           C
ATOM   1058  CG  LYS A 142      11.886   3.801   6.268  1.00  7.40           C
ATOM   1059  CD  LYS A 142      12.602   2.529   5.825  1.00 24.15           C
ATOM   1060  CE  LYS A 142      13.960   2.817   5.197  1.00 28.86           C
ATOM   1061  NZ  LYS A 142      13.848   3.582   3.921  1.00 16.07           N
ATOM   1062  N   VAL A 143       7.256   3.351   5.749  1.00 20.06           N
ATOM   1063  CA  VAL A 143       5.889   3.041   6.166  1.00 19.45           C
ATOM   1064  C   VAL A 143       4.872   3.436   5.095  1.00 22.10           C
ATOM   1065  O   VAL A 143       5.003   4.486   4.458  1.00 22.74           O
ATOM   1066  CB  VAL A 143       5.525   3.762   7.485  1.00 18.75           C
ATOM   1067  CG1 VAL A 143       6.431   3.292   8.609  1.00 18.74           C
ATOM   1068  CG2 VAL A 143       5.654   5.260   7.315  1.00 18.08           C
ATOM   1069  N   PRO A 144       3.860   2.582   4.862  1.00 21.91           N
ATOM   1070  CA  PRO A 144       2.820   2.847   3.860  1.00 21.43           C
ATOM   1071  C   PRO A 144       1.833   3.933   4.280  1.00 19.93           C
ATOM   1072  O   PRO A 144       1.562   4.123   5.466  1.00 19.25           O
ATOM   1073  CB  PRO A 144       2.128   1.491   3.722  1.00 22.05           C
ATOM   1074  CG  PRO A 144       2.259   0.906   5.100  1.00 22.56           C
ATOM   1075  CD  PRO A 144       3.691   1.243   5.457  1.00 21.77           C
ATOM   1076  N   VAL A 145       1.327   4.660   3.291  1.00 17.00           N
ATOM   1077  CA  VAL A 145       0.359   5.727   3.511  1.00 14.66           C
ATOM   1078  C   VAL A 145      -0.693   5.626   2.407  1.00 14.77           C
ATOM   1079  O   VAL A 145      -0.432   5.044   1.344  1.00 13.91           O
ATOM   1080  CB  VAL A 145       1.033   7.127   3.467  1.00 13.88           C
ATOM   1081  CG1 VAL A 145       1.965   7.312   4.660  1.00 12.69           C
ATOM   1082  CG2 VAL A 145       1.802   7.303   2.176  1.00 13.28           C
ATOM   1083  N   GLY A 146      -1.878   6.177   2.647  1.00 15.12           N
ATOM   1084  CA  GLY A 146      -2.921   6.109   1.637  1.00 14.33           C
ATOM   1085  C   GLY A 146      -3.281   4.660   1.356  1.00 14.35           C
ATOM   1086  O   GLY A 146      -3.524   3.894   2.289  1.00 17.55           O
ATOM   1087  N   ASP A 147      -3.304   4.261   0.090  1.00 13.82           N
ATOM   1088  CA  ASP A 147      -3.641   2.879  -0.221  1.00 18.08           C
ATOM   1089  C   ASP A 147      -2.455   1.985  -0.583  1.00 17.95           C
ATOM   1090  O   ASP A 147      -2.622   0.959  -1.238  1.00 20.87           O
ATOM   1091  CB  ASP A 147      -4.765   2.786  -1.269  1.00 27.91           C
ATOM   1092  CG  ASP A 147      -4.503   3.617  -2.509  1.00 34.69           C
ATOM   1093  OD1 ASP A 147      -3.332   3.773  -2.907  1.00 40.52           O
ATOM   1094  OD2 ASP A 147      -5.490   4.107  -3.099  1.00 37.01           O
ATOM   1095  N   GLN A 148      -1.264   2.367  -0.130  1.00 14.48           N
ATOM   1096  CA  GLN A 148      -0.062   1.589  -0.393  1.00 15.62           C
ATOM   1097  C   GLN A 148      -0.124   0.284   0.388  1.00 17.66           C
ATOM   1098  O   GLN A 148      -0.705   0.228   1.471  1.00 19.74           O
ATOM   1099  CB  GLN A 148       1.189   2.375   0.019  1.00 11.42           C
ATOM   1100  CG  GLN A 148       1.530   3.534  -0.905  1.00 17.19           C
ATOM   1101  CD  GLN A 148       2.551   4.477  -0.304  1.00  8.83           C
ATOM   1102  OE1 GLN A 148       2.983   4.297   0.831  1.00 13.03           O
ATOM   1103  NE2 GLN A 148       2.922   5.500  -1.054  1.00 13.54           N
ATOM   1104  N   PRO A 149       0.451  -0.793  -0.169  1.00 17.75           N
ATOM   1105  CA  PRO A 149       0.460  -2.102   0.487  1.00 18.05           C
ATOM   1106  C   PRO A 149       1.424  -2.103   1.675  1.00 21.09           C
ATOM   1107  O   PRO A 149       2.345  -1.287   1.739  1.00 21.28           O
ATOM   1108  CB  PRO A 149       0.935  -3.027  -0.626  1.00 15.71           C
ATOM   1109  CG  PRO A 149       1.865  -2.160  -1.387  1.00 16.74           C
ATOM   1110  CD  PRO A 149       1.098  -0.868  -1.490  1.00 17.36           C
ATOM   1111  N   PRO A 150       1.236  -3.037   2.620  1.00 22.23           N
ATOM   1112  CA  PRO A 150       2.091  -3.140   3.808  1.00 21.53           C
ATOM   1113  C   PRO A 150       3.584  -3.280   3.500  1.00 18.10           C
ATOM   1114  O   PRO A 150       4.428  -2.919   4.324  1.00 16.09           O
ATOM   1115  CB  PRO A 150       1.546  -4.389   4.504  1.00 21.64           C
ATOM   1116  CG  PRO A 150       0.087  -4.351   4.152  1.00 21.30           C
ATOM   1117  CD  PRO A 150       0.138  -4.020   2.679  1.00 22.05           C
ATOM   1118  N   ASP A 151       3.906  -3.805   2.322  1.00 14.81           N
ATOM   1119  CA  ASP A 151       5.301  -3.997   1.932  1.00 16.22           C
ATOM   1120  C   ASP A 151       5.802  -2.986   0.892  1.00 15.04           C
ATOM   1121  O   ASP A 151       6.760  -3.259   0.157  1.00 17.41           O
ATOM   1122  CB  ASP A 151       5.526  -5.439   1.451  1.00 15.98           C
ATOM   1123  CG  ASP A 151       4.809  -5.755   0.145  1.00 19.73           C
ATOM   1124  OD1 ASP A 151       3.761  -5.144  -0.155  1.00 21.00           O
ATOM   1125  OD2 ASP A 151       5.306  -6.633  -0.589  1.00 31.01           O
ATOM   1126  N   ILE A 152       5.183  -1.806   0.883  1.00  8.61           N
ATOM   1127  CA  ILE A 152       5.522  -0.726  -0.038  1.00  5.51           C
ATOM   1128  C   ILE A 152       7.036  -0.497  -0.161  1.00  5.69           C
ATOM   1129  O   ILE A 152       7.560  -0.369  -1.267  1.00 10.74           O
ATOM   1130  CB  ILE A 152       4.802   0.601   0.373  1.00  5.43           C
ATOM   1131  CG1 ILE A 152       5.029   1.682  -0.683  1.00 10.95           C
ATOM   1132  CG2 ILE A 152       5.281   1.095   1.741  1.00  5.63           C
ATOM   1133  CD1 ILE A 152       4.451   1.336  -2.021  1.00 14.85           C
ATOM   1134  N   GLU A 153       7.735  -0.500   0.969  1.00  5.48           N
ATOM   1135  CA  GLU A 153       9.175  -0.300   0.990  1.00  7.85           C
ATOM   1136  C   GLU A 153       9.916  -1.248   0.054  1.00 10.89           C
ATOM   1137  O   GLU A 153      10.786  -0.825  -0.709  1.00 13.70           O
ATOM   1138  CB  GLU A 153       9.730  -0.477   2.408  1.00  8.29           C
ATOM   1139  CG  GLU A 153      11.265  -0.461   2.436  1.00  7.33           C
ATOM   1140  CD  GLU A 153      11.871  -0.639   3.814  1.00 10.86           C
ATOM   1141  OE1 GLU A 153      11.123  -0.856   4.792  1.00 15.34           O
ATOM   1142  OE2 GLU A 153      13.116  -0.553   3.915  1.00 15.66           O
ATOM   1143  N   PHE A 154       9.571  -2.530   0.116  1.00 11.33           N
ATOM   1144  CA  PHE A 154      10.223  -3.526  -0.716  1.00 10.98           C
ATOM   1145  C   PHE A 154       9.734  -3.523  -2.153  1.00 11.95           C
ATOM   1146  O   PHE A 154      10.490  -3.860  -3.070  1.00  9.94           O
ATOM   1147  CB  PHE A 154      10.132  -4.897  -0.053  1.00 12.67           C
ATOM   1148  CG  PHE A 154      10.756  -4.920   1.318  1.00 16.13           C
ATOM   1149  CD1 PHE A 154      12.139  -4.930   1.460  1.00 15.39           C
ATOM   1150  CD2 PHE A 154       9.963  -4.825   2.462  1.00 18.13           C
ATOM   1151  CE1 PHE A 154      12.726  -4.837   2.721  1.00 18.71           C
ATOM   1152  CE2 PHE A 154      10.543  -4.732   3.730  1.00 18.58           C
ATOM   1153  CZ  PHE A 154      11.926  -4.736   3.859  1.00 17.59           C
ATOM   1154  N   GLN A 155       8.493  -3.096  -2.366  1.00 11.28           N
ATOM   1155  CA  GLN A 155       7.984  -3.027  -3.725  1.00 12.96           C
ATOM   1156  C   GLN A 155       8.746  -1.919  -4.453  1.00 14.22           C
ATOM   1157  O   GLN A 155       9.038  -2.039  -5.643  1.00 15.95           O
ATOM   1158  CB  GLN A 155       6.473  -2.775  -3.746  1.00 14.73           C
ATOM   1159  CG  GLN A 155       5.651  -4.052  -3.612  1.00 28.02           C
ATOM   1160  CD  GLN A 155       4.155  -3.828  -3.767  1.00 33.40           C
ATOM   1161  OE1 GLN A 155       3.373  -4.186  -2.888  1.00 43.40           O
ATOM   1162  NE2 GLN A 155       3.749  -3.261  -4.894  1.00 22.44           N
ATOM   1163  N   ILE A 156       9.107  -0.865  -3.722  1.00  9.65           N
ATOM   1164  CA  ILE A 156       9.852   0.250  -4.305  1.00  9.61           C
ATOM   1165  C   ILE A 156      11.303  -0.155  -4.494  1.00 10.25           C
ATOM   1166  O   ILE A 156      11.882   0.070  -5.554  1.00 15.34           O
ATOM   1167  CB  ILE A 156       9.770   1.525  -3.440  1.00  5.87           C
ATOM   1168  CG1 ILE A 156       8.312   1.995  -3.348  1.00  8.01           C
ATOM   1169  CG2 ILE A 156      10.643   2.623  -4.051  1.00  3.43           C
ATOM   1170  CD1 ILE A 156       8.064   3.091  -2.327  1.00  9.61           C
ATOM   1171  N   ARG A 157      11.884  -0.765  -3.467  1.00  8.66           N
ATOM   1172  CA  ARG A 157      13.259  -1.233  -3.539  1.00 11.38           C
ATOM   1173  C   ARG A 157      13.439  -2.162  -4.749  1.00 13.10           C
ATOM   1174  O   ARG A 157      14.381  -1.994  -5.524  1.00 14.74           O
ATOM   1175  CB  ARG A 157      13.638  -1.954  -2.243  1.00 18.15           C
ATOM   1176  CG  ARG A 157      15.075  -2.442  -2.197  1.00 34.27           C
ATOM   1177  CD  ARG A 157      15.419  -3.032  -0.838  1.00 32.11           C
ATOM   1178  NE  ARG A 157      16.767  -3.597  -0.813  1.00 41.04           N
ATOM   1179  CZ  ARG A 157      17.106  -4.765  -1.355  1.00 45.70           C
ATOM   1180  NH1 ARG A 157      16.198  -5.513  -1.974  1.00 48.04           N
ATOM   1181  NH2 ARG A 157      18.357  -5.193  -1.270  1.00 42.97           N
ATOM   1182  N   ASP A 158      12.513  -3.104  -4.931  1.00 13.04           N
ATOM   1183  CA  ASP A 158      12.562  -4.051  -6.053  1.00 13.52           C
ATOM   1184  C   ASP A 158      12.516  -3.310  -7.376  1.00 15.87           C
ATOM   1185  O   ASP A 158      13.200  -3.664  -8.339  1.00 11.95           O
ATOM   1186  CB  ASP A 158      11.354  -4.999  -6.016  1.00 19.24           C
ATOM   1187  CG  ASP A 158      11.496  -6.110  -4.997  1.00 22.50           C
ATOM   1188  OD1 ASP A 158      12.455  -6.103  -4.197  1.00 27.11           O
ATOM   1189  OD2 ASP A 158      10.629  -7.004  -5.008  1.00 19.03           O
ATOM   1190  N   MET A 159      11.658  -2.297  -7.411  1.00 20.41           N
ATOM   1191  CA  MET A 159      11.442  -1.464  -8.579  1.00 20.43           C
ATOM   1192  C   MET A 159      12.747  -0.833  -9.074  1.00 19.67           C
ATOM   1193  O   MET A 159      13.054  -0.879 -10.266  1.00 18.64           O
ATOM   1194  CB  MET A 159      10.429  -0.382  -8.209  1.00 22.33           C
ATOM   1195  CG  MET A 159       9.837   0.382  -9.359  1.00 24.94           C
ATOM   1196  SD  MET A 159       8.657   1.583  -8.732  1.00 25.42           S
ATOM   1197  CE  MET A 159       7.326   0.516  -8.180  1.00 25.19           C
ATOM   1198  N   LEU A 160      13.515  -0.245  -8.163  1.00 20.16           N
ATOM   1199  CA  LEU A 160      14.773   0.383  -8.552  1.00 20.30           C
ATOM   1200  C   LEU A 160      15.917  -0.616  -8.742  1.00 19.92           C
ATOM   1201  O   LEU A 160      16.828  -0.381  -9.538  1.00 16.24           O
ATOM   1202  CB  LEU A 160      15.155   1.506  -7.580  1.00 20.28           C
ATOM   1203  CG  LEU A 160      15.232   1.261  -6.075  1.00 24.85           C
ATOM   1204  CD1 LEU A 160      16.504   0.511  -5.729  1.00 28.22           C
ATOM   1205  CD2 LEU A 160      15.197   2.597  -5.351  1.00 20.94           C
ATOM   1206  N   MET A 161      15.852  -1.745  -8.041  1.00 23.95           N
ATOM   1207  CA  MET A 161      16.884  -2.770  -8.163  1.00 24.06           C
ATOM   1208  C   MET A 161      16.991  -3.294  -9.589  1.00 24.49           C
ATOM   1209  O   MET A 161      18.086  -3.568 -10.070  1.00 26.79           O
ATOM   1210  CB  MET A 161      16.633  -3.924  -7.191  1.00 22.96           C
ATOM   1211  CG  MET A 161      17.058  -3.613  -5.774  1.00 22.16           C
ATOM   1212  SD  MET A 161      18.794  -3.148  -5.722  1.00 22.76           S
ATOM   1213  CE  MET A 161      19.235  -3.539  -4.047  1.00 21.31           C
ATOM   1214  N   GLN A 162      15.864  -3.377 -10.286  1.00 24.40           N
ATOM   1215  CA  GLN A 162      15.867  -3.865 -11.660  1.00 24.62           C
ATOM   1216  C   GLN A 162      16.575  -2.908 -12.617  1.00 24.37           C
ATOM   1217  O   GLN A 162      16.941  -3.288 -13.726  1.00 24.28           O
ATOM   1218  CB  GLN A 162      14.441  -4.161 -12.125  1.00 28.92           C
ATOM   1219  CG  GLN A 162      13.830  -5.360 -11.409  1.00 33.55           C
ATOM   1220  CD  GLN A 162      12.368  -5.569 -11.736  1.00 47.58           C
ATOM   1221  OE1 GLN A 162      12.021  -6.163 -12.760  1.00 42.35           O
ATOM   1222  NE2 GLN A 162      11.498  -5.089 -10.860  1.00 57.27           N
ATOM   1223  N   PHE A 163      16.774  -1.670 -12.183  1.00 22.31           N
ATOM   1224  CA  PHE A 163      17.466  -0.694 -13.012  1.00 22.03           C
ATOM   1225  C   PHE A 163      18.926  -0.540 -12.597  1.00 23.11           C
ATOM   1226  O   PHE A 163      19.825  -0.650 -13.429  1.00 26.88           O
ATOM   1227  CB  PHE A 163      16.755   0.659 -12.963  1.00 19.08           C
ATOM   1228  CG  PHE A 163      15.425   0.662 -13.651  1.00 14.98           C
ATOM   1229  CD1 PHE A 163      15.349   0.562 -15.038  1.00 12.86           C
ATOM   1230  CD2 PHE A 163      14.248   0.740 -12.917  1.00 11.36           C
ATOM   1231  CE1 PHE A 163      14.117   0.540 -15.683  1.00 11.71           C
ATOM   1232  CE2 PHE A 163      13.013   0.719 -13.550  1.00 10.54           C
ATOM   1233  CZ  PHE A 163      12.946   0.618 -14.939  1.00 11.29           C
ATOM   1234  N   VAL A 164      19.156  -0.366 -11.299  1.00 19.66           N
ATOM   1235  CA  VAL A 164      20.503  -0.171 -10.770  1.00 23.28           C
ATOM   1236  C   VAL A 164      21.436  -1.385 -10.798  1.00 27.33           C
ATOM   1237  O   VAL A 164      22.643  -1.239 -10.588  1.00 30.14           O
ATOM   1238  CB  VAL A 164      20.476   0.419  -9.331  1.00 23.54           C
ATOM   1239  CG1 VAL A 164      19.707   1.729  -9.311  1.00 22.52           C
ATOM   1240  CG2 VAL A 164      19.876  -0.574  -8.350  1.00 23.88           C
ATOM   1241  N   THR A 165      20.891  -2.580 -11.010  1.00 28.05           N
ATOM   1242  CA  THR A 165      21.736  -3.772 -11.055  1.00 25.87           C
ATOM   1243  C   THR A 165      22.291  -4.005 -12.460  1.00 28.72           C
ATOM   1244  O   THR A 165      23.169  -4.850 -12.653  1.00 27.05           O
ATOM   1245  CB  THR A 165      21.003  -5.046 -10.557  1.00 22.64           C
ATOM   1246  OG1 THR A 165      19.809  -5.256 -11.317  1.00 14.46           O
ATOM   1247  CG2 THR A 165      20.653  -4.926  -9.076  1.00 20.46           C
ATOM   1248  N   LYS A 166      21.768  -3.263 -13.439  1.00 30.04           N
ATOM   1249  CA  LYS A 166      22.232  -3.379 -14.819  1.00 29.68           C
ATOM   1250  C   LYS A 166      23.687  -2.944 -14.873  1.00 29.85           C
ATOM   1251  O   LYS A 166      24.065  -1.929 -14.282  1.00 30.54           O
ATOM   1252  CB  LYS A 166      21.418  -2.488 -15.756  1.00 38.13           C
ATOM   1253  CG  LYS A 166      19.969  -2.895 -15.947  1.00 49.71           C
ATOM   1254  CD  LYS A 166      19.321  -2.010 -16.999  1.00 60.22           C
ATOM   1255  CE  LYS A 166      17.837  -2.289 -17.152  1.00 62.98           C
ATOM   1256  NZ  LYS A 166      17.228  -1.357 -18.141  1.00 49.90           N
ATOM   1257  N   GLU A 167      24.502  -3.709 -15.586  1.00 26.94           N
ATOM   1258  CA  GLU A 167      25.915  -3.398 -15.701  1.00 24.96           C
ATOM   1259  C   GLU A 167      26.155  -2.036 -16.342  1.00 22.95           C
ATOM   1260  O   GLU A 167      25.493  -1.656 -17.308  1.00 21.17           O
ATOM   1261  CB  GLU A 167      26.645  -4.517 -16.454  1.00 25.10           C
ATOM   1262  CG  GLU A 167      26.738  -5.809 -15.636  1.00 44.93           C
ATOM   1263  CD  GLU A 167      27.021  -7.041 -16.479  1.00 63.45           C
ATOM   1264  OE1 GLU A 167      26.181  -7.373 -17.344  1.00 61.27           O
ATOM   1265  OE2 GLU A 167      28.070  -7.689 -16.262  1.00 51.24           O
ATOM   1266  N   ASN A 168      27.058  -1.277 -15.735  1.00 22.92           N
ATOM   1267  CA  ASN A 168      27.419   0.052 -16.210  1.00 27.96           C
ATOM   1268  C   ASN A 168      26.402   1.163 -15.931  1.00 29.58           C
ATOM   1269  O   ASN A 168      26.694   2.328 -16.200  1.00 32.11           O
ATOM   1270  CB  ASN A 168      27.780   0.024 -17.705  1.00 34.19           C
ATOM   1271  CG  ASN A 168      28.997  -0.846 -18.004  1.00 34.56           C
ATOM   1272  OD1 ASN A 168      29.035  -1.551 -19.014  1.00 21.68           O
ATOM   1273  ND2 ASN A 168      29.997  -0.800 -17.126  1.00 25.40           N
ATOM   1274  N   CYS A 169      25.229   0.826 -15.390  1.00 26.74           N
ATOM   1275  CA  CYS A 169      24.221   1.849 -15.084  1.00 23.67           C
ATOM   1276  C   CYS A 169      24.797   2.872 -14.115  1.00 20.49           C
ATOM   1277  O   CYS A 169      25.269   2.513 -13.042  1.00 21.84           O
ATOM   1278  CB  CYS A 169      22.963   1.236 -14.459  1.00 24.01           C
ATOM   1279  SG  CYS A 169      21.747   2.468 -13.833  1.00 24.27           S
ATOM   1280  N   LEU A 170      24.812   4.135 -14.528  1.00 18.83           N
ATOM   1281  CA  LEU A 170      25.319   5.211 -13.691  1.00 17.00           C
ATOM   1282  C   LEU A 170      24.274   5.534 -12.630  1.00 17.15           C
ATOM   1283  O   LEU A 170      23.153   5.958 -12.943  1.00 15.93           O
ATOM   1284  CB  LEU A 170      25.620   6.456 -14.527  1.00 17.26           C
ATOM   1285  CG  LEU A 170      26.885   6.456 -15.383  1.00 20.80           C
ATOM   1286  CD1 LEU A 170      26.970   7.756 -16.177  1.00 22.76           C
ATOM   1287  CD2 LEU A 170      28.108   6.302 -14.489  1.00 18.27           C
ATOM   1288  N   ILE A 171      24.657   5.349 -11.374  1.00 14.70           N
ATOM   1289  CA  ILE A 171      23.760   5.585 -10.260  1.00 13.28           C
ATOM   1290  C   ILE A 171      23.922   6.956  -9.612  1.00 13.99           C
ATOM   1291  O   ILE A 171      24.966   7.267  -9.034  1.00 13.56           O
ATOM   1292  CB  ILE A 171      23.937   4.510  -9.172  1.00 10.52           C
ATOM   1293  CG1 ILE A 171      23.786   3.118  -9.775  1.00 12.19           C
ATOM   1294  CG2 ILE A 171      22.914   4.706  -8.061  1.00 12.33           C
ATOM   1295  CD1 ILE A 171      24.075   2.006  -8.793  1.00 16.28           C
ATOM   1296  N   LEU A 172      22.893   7.783  -9.735  1.00 11.71           N
ATOM   1297  CA  LEU A 172      22.904   9.094  -9.109  1.00 10.10           C
ATOM   1298  C   LEU A 172      22.334   8.887  -7.707  1.00  8.32           C
ATOM   1299  O   LEU A 172      21.124   8.722  -7.534  1.00  9.43           O
ATOM   1300  CB  LEU A 172      22.051  10.086  -9.908  1.00 10.20           C
ATOM   1301  CG  LEU A 172      22.756  10.912 -10.993  1.00  9.48           C
ATOM   1302  CD1 LEU A 172      23.835  10.108 -11.691  1.00 17.15           C
ATOM   1303  CD2 LEU A 172      21.747  11.434 -11.990  1.00  1.70           C
ATOM   1304  N   ALA A 173      23.224   8.762  -6.732  1.00  7.49           N
ATOM   1305  CA  ALA A 173      22.830   8.577  -5.342  1.00  8.18           C
ATOM   1306  C   ALA A 173      22.513   9.958  -4.770  1.00  8.96           C
ATOM   1307  O   ALA A 173      23.416  10.706  -4.386  1.00  8.82           O
ATOM   1308  CB  ALA A 173      23.959   7.919  -4.565  1.00  9.00           C
ATOM   1309  N   VAL A 174      21.228  10.297  -4.753  1.00  9.17           N
ATOM   1310  CA  VAL A 174      20.754  11.591  -4.275  1.00  7.04           C
ATOM   1311  C   VAL A 174      20.411  11.597  -2.781  1.00  8.57           C
ATOM   1312  O   VAL A 174      19.584  10.809  -2.324  1.00 10.25           O
ATOM   1313  CB  VAL A 174      19.514  12.033  -5.092  1.00  6.35           C
ATOM   1314  CG1 VAL A 174      19.071  13.429  -4.689  1.00  6.32           C
ATOM   1315  CG2 VAL A 174      19.829  11.984  -6.577  1.00  5.52           C
ATOM   1316  N   SER A 175      21.031  12.507  -2.034  1.00  9.24           N
ATOM   1317  CA  SER A 175      20.800  12.636  -0.591  1.00 11.97           C
ATOM   1318  C   SER A 175      20.595  14.110  -0.225  1.00  9.21           C
ATOM   1319  O   SER A 175      21.307  14.986  -0.722  1.00 10.40           O
ATOM   1320  CB  SER A 175      21.998  12.096   0.195  1.00 17.65           C
ATOM   1321  OG  SER A 175      22.322  10.771  -0.182  1.00 29.46           O
ATOM   1322  N   PRO A 176      19.607  14.407   0.629  1.00  9.54           N
ATOM   1323  CA  PRO A 176      19.382  15.810   1.005  1.00  8.56           C
ATOM   1324  C   PRO A 176      20.330  16.210   2.130  1.00  9.55           C
ATOM   1325  O   PRO A 176      20.548  15.448   3.065  1.00  9.89           O
ATOM   1326  CB  PRO A 176      17.919  15.810   1.446  1.00  8.86           C
ATOM   1327  CG  PRO A 176      17.765  14.453   2.095  1.00 10.00           C
ATOM   1328  CD  PRO A 176      18.556  13.523   1.178  1.00 11.94           C
ATOM   1329  N   ALA A 177      20.904  17.404   2.032  1.00 12.41           N
ATOM   1330  CA  ALA A 177      21.840  17.892   3.042  1.00 10.04           C
ATOM   1331  C   ALA A 177      21.219  18.093   4.423  1.00  9.51           C
ATOM   1332  O   ALA A 177      21.896  17.942   5.448  1.00  6.43           O
ATOM   1333  CB  ALA A 177      22.479  19.181   2.575  1.00  9.45           C
ATOM   1334  N   ASN A 178      19.930  18.411   4.460  1.00 10.17           N
ATOM   1335  CA  ASN A 178      19.263  18.652   5.734  1.00 13.23           C
ATOM   1336  C   ASN A 178      18.940  17.392   6.535  1.00 14.98           C
ATOM   1337  O   ASN A 178      18.094  17.405   7.428  1.00 16.58           O
ATOM   1338  CB  ASN A 178      18.036  19.557   5.560  1.00  4.00           C
ATOM   1339  CG  ASN A 178      17.028  19.005   4.577  1.00  9.34           C
ATOM   1340  OD1 ASN A 178      17.278  18.002   3.900  1.00  8.00           O
ATOM   1341  ND2 ASN A 178      15.880  19.666   4.484  1.00  3.51           N
ATOM   1342  N   SER A 179      19.655  16.318   6.226  1.00 13.90           N
ATOM   1343  CA  SER A 179      19.526  15.049   6.916  1.00 14.55           C
ATOM   1344  C   SER A 179      20.954  14.520   6.984  1.00 16.51           C
ATOM   1345  O   SER A 179      21.777  14.863   6.136  1.00 17.52           O
ATOM   1346  CB  SER A 179      18.642  14.082   6.126  1.00 17.54           C
ATOM   1347  OG  SER A 179      18.396  12.899   6.875  1.00 24.13           O
ATOM   1348  N   ASP A 180      21.266  13.739   8.013  1.00 16.56           N
ATOM   1349  CA  ASP A 180      22.607  13.179   8.147  1.00 15.51           C
ATOM   1350  C   ASP A 180      22.870  12.182   7.028  1.00 14.33           C
ATOM   1351  O   ASP A 180      22.007  11.366   6.695  1.00 10.89           O
ATOM   1352  CB  ASP A 180      22.797  12.510   9.517  1.00 16.93           C
ATOM   1353  CG  ASP A 180      23.032  13.520  10.641  1.00 26.15           C
ATOM   1354  OD1 ASP A 180      23.113  14.738  10.362  1.00 27.98           O
ATOM   1355  OD2 ASP A 180      23.144  13.095  11.810  1.00 21.90           O
ATOM   1356  N   LEU A 181      24.071  12.249   6.465  1.00 12.74           N
ATOM   1357  CA  LEU A 181      24.483  11.380   5.371  1.00 13.78           C
ATOM   1358  C   LEU A 181      24.404   9.897   5.733  1.00 13.15           C
ATOM   1359  O   LEU A 181      24.162   9.054   4.873  1.00 12.03           O
ATOM   1360  CB  LEU A 181      25.904  11.742   4.939  1.00 14.19           C
ATOM   1361  CG  LEU A 181      26.360  11.220   3.581  1.00 15.26           C
ATOM   1362  CD1 LEU A 181      25.450  11.756   2.483  1.00 17.45           C
ATOM   1363  CD2 LEU A 181      27.786  11.648   3.340  1.00 16.10           C
ATOM   1364  N   ALA A 182      24.585   9.585   7.011  1.00 13.24           N
ATOM   1365  CA  ALA A 182      24.526   8.201   7.473  1.00 11.98           C
ATOM   1366  C   ALA A 182      23.134   7.578   7.306  1.00 13.56           C
ATOM   1367  O   ALA A 182      23.004   6.357   7.318  1.00 17.12           O
ATOM   1368  CB  ALA A 182      24.979   8.111   8.921  1.00 10.88           C
ATOM   1369  N   ASN A 183      22.108   8.416   7.155  1.00  9.32           N
ATOM   1370  CA  ASN A 183      20.722   7.959   6.974  1.00 11.74           C
ATOM   1371  C   ASN A 183      20.362   7.848   5.499  1.00 13.44           C
ATOM   1372  O   ASN A 183      19.211   7.585   5.162  1.00 16.61           O
ATOM   1373  CB  ASN A 183      19.721   8.956   7.583  1.00 23.86           C
ATOM   1374  CG  ASN A 183      19.866   9.111   9.078  1.00 13.45           C
ATOM   1375  OD1 ASN A 183      20.409   8.242   9.760  1.00 25.26           O
ATOM   1376  ND2 ASN A 183      19.386  10.236   9.600  1.00 18.28           N
ATOM   1377  N   SER A 184      21.322   8.084   4.616  1.00 11.73           N
ATOM   1378  CA  SER A 184      21.048   8.028   3.189  1.00 12.54           C
ATOM   1379  C   SER A 184      20.634   6.666   2.638  1.00 13.48           C
ATOM   1380  O   SER A 184      21.411   5.710   2.671  1.00 12.23           O
ATOM   1381  CB  SER A 184      22.248   8.538   2.398  1.00 13.58           C
ATOM   1382  OG  SER A 184      21.992   8.482   1.005  1.00 15.10           O
ATOM   1383  N   ASP A 185      19.406   6.597   2.126  1.00 13.70           N
ATOM   1384  CA  ASP A 185      18.889   5.386   1.502  1.00 14.13           C
ATOM   1385  C   ASP A 185      19.679   5.197   0.203  1.00 17.19           C
ATOM   1386  O   ASP A 185      20.079   4.084  -0.140  1.00 19.06           O
ATOM   1387  CB  ASP A 185      17.402   5.545   1.155  1.00 15.85           C
ATOM   1388  CG  ASP A 185      16.491   5.295   2.338  1.00 20.40           C
ATOM   1389  OD1 ASP A 185      16.488   4.159   2.853  1.00 22.65           O
ATOM   1390  OD2 ASP A 185      15.770   6.226   2.747  1.00 28.86           O
ATOM   1391  N   ALA A 186      19.912   6.308  -0.495  1.00 13.11           N
ATOM   1392  CA  ALA A 186      20.640   6.317  -1.755  1.00 15.36           C
ATOM   1393  C   ALA A 186      21.998   5.639  -1.644  1.00 15.44           C
ATOM   1394  O   ALA A 186      22.342   4.791  -2.467  1.00 15.23           O
ATOM   1395  CB  ALA A 186      20.815   7.753  -2.247  1.00 16.53           C
ATOM   1396  N   LEU A 187      22.764   6.007  -0.621  1.00 16.35           N
ATOM   1397  CA  LEU A 187      24.088   5.427  -0.421  1.00 17.38           C
ATOM   1398  C   LEU A 187      24.031   3.956  -0.033  1.00 18.40           C
ATOM   1399  O   LEU A 187      24.872   3.167  -0.469  1.00 16.97           O
ATOM   1400  CB  LEU A 187      24.879   6.217   0.623  1.00 16.20           C
ATOM   1401  CG  LEU A 187      25.178   7.672   0.251  1.00 16.86           C
ATOM   1402  CD1 LEU A 187      26.004   8.314   1.345  1.00 17.47           C
ATOM   1403  CD2 LEU A 187      25.905   7.742  -1.080  1.00 13.99           C
ATOM   1404  N   LYS A 188      23.042   3.590   0.781  1.00 19.17           N
ATOM   1405  CA  LYS A 188      22.889   2.202   1.211  1.00 18.70           C
ATOM   1406  C   LYS A 188      22.686   1.312  -0.011  1.00 16.33           C
ATOM   1407  O   LYS A 188      23.414   0.333  -0.204  1.00 17.48           O
ATOM   1408  CB  LYS A 188      21.708   2.052   2.173  1.00 18.44           C
ATOM   1409  CG  LYS A 188      21.574   0.649   2.753  1.00 21.22           C
ATOM   1410  CD  LYS A 188      20.313   0.482   3.592  1.00 18.96           C
ATOM   1411  CE  LYS A 188      20.267  -0.912   4.209  1.00 34.91           C
ATOM   1412  NZ  LYS A 188      19.107  -1.118   5.119  1.00 16.43           N
ATOM   1413  N   VAL A 189      21.720   1.678  -0.849  1.00 11.38           N
ATOM   1414  CA  VAL A 189      21.431   0.925  -2.063  1.00 15.11           C
ATOM   1415  C   VAL A 189      22.648   0.893  -2.980  1.00 16.65           C
ATOM   1416  O   VAL A 189      22.993  -0.154  -3.519  1.00 24.63           O
ATOM   1417  CB  VAL A 189      20.229   1.516  -2.825  1.00 16.24           C
ATOM   1418  CG1 VAL A 189      20.045   0.808  -4.157  1.00 17.07           C
ATOM   1419  CG2 VAL A 189      18.970   1.369  -1.989  1.00 17.34           C
ATOM   1420  N   ALA A 190      23.305   2.036  -3.135  1.00 15.08           N
ATOM   1421  CA  ALA A 190      24.488   2.146  -3.980  1.00 14.14           C
ATOM   1422  C   ALA A 190      25.584   1.175  -3.553  1.00 14.73           C
ATOM   1423  O   ALA A 190      26.213   0.529  -4.395  1.00 16.49           O
ATOM   1424  CB  ALA A 190      25.018   3.565  -3.953  1.00 13.85           C
ATOM   1425  N   LYS A 191      25.818   1.082  -2.248  1.00 14.88           N
ATOM   1426  CA  LYS A 191      26.842   0.196  -1.721  1.00 15.84           C
ATOM   1427  C   LYS A 191      26.493  -1.280  -1.866  1.00 17.59           C
ATOM   1428  O   LYS A 191      27.384  -2.122  -1.934  1.00 21.85           O
ATOM   1429  CB  LYS A 191      27.159   0.534  -0.265  1.00 13.84           C
ATOM   1430  CG  LYS A 191      27.996   1.791  -0.114  1.00 37.28           C
ATOM   1431  CD  LYS A 191      28.397   2.023   1.332  1.00 40.11           C
ATOM   1432  CE  LYS A 191      29.441   3.116   1.434  1.00 30.32           C
ATOM   1433  NZ  LYS A 191      30.702   2.756   0.717  1.00 38.22           N
ATOM   1434  N   GLU A 192      25.203  -1.590  -1.918  1.00 14.58           N
ATOM   1435  CA  GLU A 192      24.762  -2.968  -2.082  1.00 16.77           C
ATOM   1436  C   GLU A 192      25.007  -3.451  -3.505  1.00 18.95           C
ATOM   1437  O   GLU A 192      25.533  -4.544  -3.713  1.00 22.98           O
ATOM   1438  CB  GLU A 192      23.268  -3.103  -1.783  1.00 19.77           C
ATOM   1439  CG  GLU A 192      22.875  -2.958  -0.317  1.00 27.08           C
ATOM   1440  CD  GLU A 192      21.367  -3.010  -0.111  1.00 22.89           C
ATOM   1441  OE1 GLU A 192      20.667  -3.633  -0.937  1.00 41.57           O
ATOM   1442  OE2 GLU A 192      20.878  -2.423   0.876  1.00 44.55           O
ATOM   1443  N   VAL A 193      24.633  -2.626  -4.479  1.00 17.57           N
ATOM   1444  CA  VAL A 193      24.762  -2.985  -5.893  1.00 16.15           C
ATOM   1445  C   VAL A 193      26.097  -2.648  -6.551  1.00 18.03           C
ATOM   1446  O   VAL A 193      26.532  -3.329  -7.480  1.00 17.56           O
ATOM   1447  CB  VAL A 193      23.629  -2.358  -6.720  1.00 14.78           C
ATOM   1448  CG1 VAL A 193      22.284  -2.848  -6.217  1.00 13.75           C
ATOM   1449  CG2 VAL A 193      23.697  -0.844  -6.644  1.00 15.65           C
ATOM   1450  N   ASP A 194      26.752  -1.607  -6.056  1.00 19.05           N
ATOM   1451  CA  ASP A 194      28.028  -1.164  -6.599  1.00 16.85           C
ATOM   1452  C   ASP A 194      28.918  -0.839  -5.401  1.00 18.47           C
ATOM   1453  O   ASP A 194      29.340   0.301  -5.214  1.00 18.82           O
ATOM   1454  CB  ASP A 194      27.770   0.067  -7.477  1.00 18.78           C
ATOM   1455  CG  ASP A 194      29.034   0.684  -8.032  1.00 18.83           C
ATOM   1456  OD1 ASP A 194      30.008  -0.044  -8.316  1.00 21.88           O
ATOM   1457  OD2 ASP A 194      29.040   1.919  -8.188  1.00 15.35           O
ATOM   1458  N   PRO A 195      29.273  -1.868  -4.607  1.00 22.41           N
ATOM   1459  CA  PRO A 195      30.109  -1.740  -3.407  1.00 21.69           C
ATOM   1460  C   PRO A 195      31.422  -0.980  -3.528  1.00 24.34           C
ATOM   1461  O   PRO A 195      31.847  -0.314  -2.575  1.00 27.27           O
ATOM   1462  CB  PRO A 195      30.316  -3.194  -2.973  1.00 21.81           C
ATOM   1463  CG  PRO A 195      30.185  -3.964  -4.248  1.00 22.25           C
ATOM   1464  CD  PRO A 195      29.020  -3.289  -4.910  1.00 22.07           C
ATOM   1465  N   GLN A 196      32.064  -1.062  -4.685  1.00 24.30           N
ATOM   1466  CA  GLN A 196      33.329  -0.367  -4.879  1.00 26.12           C
ATOM   1467  C   GLN A 196      33.161   1.060  -5.401  1.00 27.61           C
ATOM   1468  O   GLN A 196      34.134   1.805  -5.510  1.00 31.49           O
ATOM   1469  CB  GLN A 196      34.255  -1.180  -5.787  1.00 27.82           C
ATOM   1470  CG  GLN A 196      35.213  -2.113  -5.044  1.00 23.30           C
ATOM   1471  CD  GLN A 196      34.509  -3.143  -4.172  1.00 40.87           C
ATOM   1472  OE1 GLN A 196      34.636  -3.128  -2.946  1.00 33.14           O
ATOM   1473  NE2 GLN A 196      33.776  -4.053  -4.802  1.00 48.25           N
ATOM   1474  N   GLY A 197      31.926   1.439  -5.714  1.00 23.64           N
ATOM   1475  CA  GLY A 197      31.654   2.778  -6.205  1.00 20.71           C
ATOM   1476  C   GLY A 197      32.139   3.108  -7.608  1.00 18.05           C
ATOM   1477  O   GLY A 197      32.362   4.275  -7.922  1.00 19.44           O
ATOM   1478  N   GLN A 198      32.250   2.101  -8.467  1.00 14.21           N
ATOM   1479  CA  GLN A 198      32.709   2.307  -9.840  1.00 14.51           C
ATOM   1480  C   GLN A 198      31.747   3.113 -10.702  1.00 16.93           C
ATOM   1481  O   GLN A 198      32.166   3.763 -11.662  1.00 15.91           O
ATOM   1482  CB  GLN A 198      32.961   0.964 -10.528  1.00 14.92           C
ATOM   1483  CG  GLN A 198      34.126   0.170  -9.961  1.00 31.65           C
ATOM   1484  CD  GLN A 198      35.456   0.880 -10.129  1.00 35.35           C
ATOM   1485  OE1 GLN A 198      35.736   1.462 -11.176  1.00 34.43           O
ATOM   1486  NE2 GLN A 198      36.284   0.832  -9.096  1.00 40.26           N
ATOM   1487  N   ARG A 199      30.458   3.046 -10.378  1.00 17.86           N
ATOM   1488  CA  ARG A 199      29.431   3.743 -11.152  1.00 15.40           C
ATOM   1489  C   ARG A 199      28.431   4.536 -10.307  1.00 16.37           C
ATOM   1490  O   ARG A 199      27.304   4.787 -10.729  1.00 14.60           O
ATOM   1491  CB  ARG A 199      28.705   2.742 -12.067  1.00 13.39           C
ATOM   1492  CG  ARG A 199      28.211   1.486 -11.354  1.00 15.27           C
ATOM   1493  CD  ARG A 199      27.818   0.379 -12.332  1.00 16.97           C
ATOM   1494  NE  ARG A 199      27.275  -0.794 -11.641  1.00  7.89           N
ATOM   1495  CZ  ARG A 199      26.004  -0.921 -11.259  1.00 16.91           C
ATOM   1496  NH1 ARG A 199      25.130   0.047 -11.501  1.00 16.40           N
ATOM   1497  NH2 ARG A 199      25.607  -2.013 -10.617  1.00 12.12           N
ATOM   1498  N   THR A 200      28.864   4.959  -9.126  1.00 18.39           N
ATOM   1499  CA  THR A 200      28.019   5.735  -8.233  1.00 14.04           C
ATOM   1500  C   THR A 200      28.516   7.177  -8.194  1.00 18.51           C
ATOM   1501  O   THR A 200      29.714   7.418  -8.042  1.00 23.23           O
ATOM   1502  CB  THR A 200      28.042   5.160  -6.811  1.00  9.42           C
ATOM   1503  OG1 THR A 200      27.557   3.814  -6.837  1.00 11.03           O
ATOM   1504  CG2 THR A 200      27.162   5.990  -5.880  1.00 12.31           C
ATOM   1505  N   ILE A 201      27.600   8.121  -8.381  1.00 13.16           N
ATOM   1506  CA  ILE A 201      27.919   9.547  -8.350  1.00 15.26           C
ATOM   1507  C   ILE A 201      27.074  10.120  -7.217  1.00 13.64           C
ATOM   1508  O   ILE A 201      25.842  10.083  -7.281  1.00 16.02           O
ATOM   1509  CB  ILE A 201      27.528  10.258  -9.684  1.00 19.87           C
ATOM   1510  CG1 ILE A 201      28.270   9.636 -10.868  1.00 25.24           C
ATOM   1511  CG2 ILE A 201      27.853  11.750  -9.613  1.00 21.33           C
ATOM   1512  CD1 ILE A 201      29.783   9.766 -10.785  1.00 37.20           C
ATOM   1513  N   GLY A 202      27.731  10.571  -6.155  1.00  9.16           N
ATOM   1514  CA  GLY A 202      27.016  11.131  -5.025  1.00  9.80           C
ATOM   1515  C   GLY A 202      26.521  12.537  -5.298  1.00 12.41           C
ATOM   1516  O   GLY A 202      27.281  13.393  -5.758  1.00 14.46           O
ATOM   1517  N   VAL A 203      25.239  12.774  -5.043  1.00 10.13           N
ATOM   1518  CA  VAL A 203      24.650  14.093  -5.255  1.00  7.23           C
ATOM   1519  C   VAL A 203      23.979  14.573  -3.972  1.00  8.08           C
ATOM   1520  O   VAL A 203      23.089  13.908  -3.439  1.00 10.97           O
ATOM   1521  CB  VAL A 203      23.609  14.083  -6.391  1.00  5.05           C
ATOM   1522  CG1 VAL A 203      23.091  15.487  -6.629  1.00  6.05           C
ATOM   1523  CG2 VAL A 203      24.222  13.514  -7.667  1.00  3.34           C
ATOM   1524  N   ILE A 204      24.438  15.707  -3.457  1.00  5.47           N
ATOM   1525  CA  ILE A 204      23.874  16.262  -2.241  1.00  5.83           C
ATOM   1526  C   ILE A 204      23.039  17.486  -2.598  1.00  6.13           C
ATOM   1527  O   ILE A 204      23.561  18.483  -3.114  1.00  5.76           O
ATOM   1528  CB  ILE A 204      24.974  16.644  -1.216  1.00  7.62           C
ATOM   1529  CG1 ILE A 204      25.856  15.438  -0.891  1.00  7.12           C
ATOM   1530  CG2 ILE A 204      24.344  17.174   0.060  1.00  9.19           C
ATOM   1531  CD1 ILE A 204      25.126  14.265  -0.286  1.00 10.16           C
ATOM   1532  N   THR A 205      21.738  17.386  -2.341  1.00  3.76           N
ATOM   1533  CA  THR A 205      20.795  18.461  -2.625  1.00  2.91           C
ATOM   1534  C   THR A 205      20.447  19.226  -1.353  1.00  7.12           C
ATOM   1535  O   THR A 205      21.017  18.986  -0.283  1.00  5.43           O
ATOM   1536  CB  THR A 205      19.460  17.885  -3.181  1.00  2.83           C
ATOM   1537  OG1 THR A 205      18.863  17.044  -2.185  1.00 12.43           O
ATOM   1538  CG2 THR A 205      19.700  17.058  -4.439  1.00  1.46           C
ATOM   1539  N   LYS A 206      19.515  20.164  -1.497  1.00  7.65           N
ATOM   1540  CA  LYS A 206      18.999  20.958  -0.394  1.00  6.43           C
ATOM   1541  C   LYS A 206      20.031  21.564   0.552  1.00  7.17           C
ATOM   1542  O   LYS A 206      19.784  21.701   1.752  1.00  9.06           O
ATOM   1543  CB  LYS A 206      17.974  20.124   0.375  1.00  1.46           C
ATOM   1544  CG  LYS A 206      16.879  19.591  -0.530  1.00  1.46           C
ATOM   1545  CD  LYS A 206      15.805  18.834   0.218  1.00 10.50           C
ATOM   1546  CE  LYS A 206      14.823  18.229  -0.770  1.00  7.16           C
ATOM   1547  NZ  LYS A 206      13.582  17.742  -0.117  1.00  9.30           N
ATOM   1548  N   LEU A 207      21.157  21.990  -0.007  1.00  6.17           N
ATOM   1549  CA  LEU A 207      22.223  22.593   0.781  1.00  6.85           C
ATOM   1550  C   LEU A 207      21.770  23.906   1.398  1.00  8.34           C
ATOM   1551  O   LEU A 207      22.224  24.287   2.478  1.00  9.38           O
ATOM   1552  CB  LEU A 207      23.482  22.776  -0.077  1.00  5.40           C
ATOM   1553  CG  LEU A 207      24.212  21.443  -0.268  1.00  4.61           C
ATOM   1554  CD1 LEU A 207      25.193  21.488  -1.422  1.00  2.57           C
ATOM   1555  CD2 LEU A 207      24.913  21.067   1.036  1.00  2.02           C
ATOM   1556  N   ASP A 208      20.812  24.545   0.738  1.00  8.98           N
ATOM   1557  CA  ASP A 208      20.240  25.808   1.187  1.00  8.00           C
ATOM   1558  C   ASP A 208      19.292  25.646   2.377  1.00  7.17           C
ATOM   1559  O   ASP A 208      18.816  26.633   2.928  1.00  6.27           O
ATOM   1560  CB  ASP A 208      19.477  26.472   0.033  1.00  7.64           C
ATOM   1561  CG  ASP A 208      18.318  25.617  -0.475  1.00  7.41           C
ATOM   1562  OD1 ASP A 208      18.479  24.386  -0.563  1.00  9.86           O
ATOM   1563  OD2 ASP A 208      17.245  26.170  -0.782  1.00  8.61           O
ATOM   1564  N   LEU A 209      18.985  24.408   2.752  1.00  9.11           N
ATOM   1565  CA  LEU A 209      18.060  24.178   3.864  1.00  9.34           C
ATOM   1566  C   LEU A 209      18.707  23.713   5.159  1.00  9.50           C
ATOM   1567  O   LEU A 209      18.006  23.401   6.119  1.00  7.41           O
ATOM   1568  CB  LEU A 209      16.984  23.166   3.462  1.00  7.91           C
ATOM   1569  CG  LEU A 209      16.132  23.487   2.236  1.00  5.03           C
ATOM   1570  CD1 LEU A 209      15.128  22.365   2.026  1.00  3.67           C
ATOM   1571  CD2 LEU A 209      15.420  24.818   2.416  1.00  3.64           C
ATOM   1572  N   MET A 210      20.031  23.659   5.199  1.00 10.45           N
ATOM   1573  CA  MET A 210      20.700  23.199   6.405  1.00 10.89           C
ATOM   1574  C   MET A 210      20.465  24.112   7.598  1.00 10.97           C
ATOM   1575  O   MET A 210      20.363  25.332   7.458  1.00 10.52           O
ATOM   1576  CB  MET A 210      22.201  23.007   6.165  1.00 11.99           C
ATOM   1577  CG  MET A 210      22.519  21.877   5.202  1.00 11.73           C
ATOM   1578  SD  MET A 210      24.261  21.439   5.171  1.00 11.48           S
ATOM   1579  CE  MET A 210      24.296  20.264   6.525  1.00  9.40           C
ATOM   1580  N   ASP A 211      20.340  23.488   8.764  1.00  9.28           N
ATOM   1581  CA  ASP A 211      20.131  24.175  10.030  1.00  9.53           C
ATOM   1582  C   ASP A 211      21.290  25.147  10.278  1.00 11.68           C
ATOM   1583  O   ASP A 211      22.450  24.813  10.035  1.00 10.62           O
ATOM   1584  CB  ASP A 211      20.080  23.127  11.142  1.00  7.12           C
ATOM   1585  CG  ASP A 211      19.800  23.720  12.501  1.00 11.87           C
ATOM   1586  OD1 ASP A 211      18.895  24.564  12.610  1.00 12.33           O
ATOM   1587  OD2 ASP A 211      20.470  23.316  13.471  1.00  8.35           O
ATOM   1588  N   GLU A 212      20.978  26.357  10.733  1.00 11.38           N
ATOM   1589  CA  GLU A 212      22.022  27.335  11.010  1.00 11.56           C
ATOM   1590  C   GLU A 212      23.017  26.717  11.983  1.00 12.27           C
ATOM   1591  O   GLU A 212      22.630  26.026  12.935  1.00 14.70           O
ATOM   1592  CB  GLU A 212      21.441  28.605  11.628  1.00 14.57           C
ATOM   1593  CG  GLU A 212      20.651  29.468  10.680  1.00 22.86           C
ATOM   1594  CD  GLU A 212      20.218  30.766  11.327  1.00 40.77           C
ATOM   1595  OE1 GLU A 212      19.190  30.761  12.033  1.00 36.64           O
ATOM   1596  OE2 GLU A 212      20.915  31.787  11.141  1.00 63.31           O
ATOM   1597  N   GLY A 213      24.295  26.982  11.746  1.00 10.57           N
ATOM   1598  CA  GLY A 213      25.334  26.431  12.589  1.00 13.43           C
ATOM   1599  C   GLY A 213      25.864  25.103  12.070  1.00 17.04           C
ATOM   1600  O   GLY A 213      26.702  24.483  12.723  1.00 16.16           O
ATOM   1601  N   THR A 214      25.368  24.649  10.921  1.00 18.99           N
ATOM   1602  CA  THR A 214      25.827  23.388  10.339  1.00 17.08           C
ATOM   1603  C   THR A 214      26.179  23.604   8.865  1.00 16.53           C
ATOM   1604  O   THR A 214      25.803  24.621   8.276  1.00 18.33           O
ATOM   1605  CB  THR A 214      24.751  22.258  10.452  1.00  7.03           C
ATOM   1606  OG1 THR A 214      23.687  22.486   9.516  1.00  4.94           O
ATOM   1607  CG2 THR A 214      24.168  22.198  11.851  1.00  1.46           C
ATOM   1608  N   ASP A 215      26.940  22.674   8.292  1.00 13.39           N
ATOM   1609  CA  ASP A 215      27.342  22.739   6.886  1.00 14.69           C
ATOM   1610  C   ASP A 215      27.739  21.333   6.433  1.00 14.09           C
ATOM   1611  O   ASP A 215      27.975  20.463   7.272  1.00 15.03           O
ATOM   1612  CB  ASP A 215      28.502  23.732   6.686  1.00 11.27           C
ATOM   1613  CG  ASP A 215      29.750  23.357   7.478  1.00 13.94           C
ATOM   1614  OD1 ASP A 215      30.469  22.430   7.062  1.00 11.90           O
ATOM   1615  OD2 ASP A 215      30.016  23.994   8.516  1.00 16.36           O
ATOM   1616  N   ALA A 216      27.806  21.105   5.122  1.00 10.30           N
ATOM   1617  CA  ALA A 216      28.165  19.785   4.595  1.00 10.17           C
ATOM   1618  C   ALA A 216      29.581  19.696   4.014  1.00 10.47           C
ATOM   1619  O   ALA A 216      29.857  18.845   3.166  1.00 10.33           O
ATOM   1620  CB  ALA A 216      27.143  19.345   3.551  1.00  8.97           C
ATOM   1621  N   ARG A 217      30.491  20.517   4.524  1.00 14.11           N
ATOM   1622  CA  ARG A 217      31.867  20.544   4.028  1.00 13.96           C
ATOM   1623  C   ARG A 217      32.548  19.172   4.025  1.00 11.28           C
ATOM   1624  O   ARG A 217      33.107  18.762   3.012  1.00 11.09           O
ATOM   1625  CB  ARG A 217      32.690  21.565   4.821  1.00 12.30           C
ATOM   1626  CG  ARG A 217      34.082  21.836   4.266  1.00  9.77           C
ATOM   1627  CD  ARG A 217      34.730  23.014   4.984  1.00 20.78           C
ATOM   1628  NE  ARG A 217      36.118  23.222   4.577  1.00 26.21           N
ATOM   1629  CZ  ARG A 217      36.757  24.387   4.647  1.00 25.61           C
ATOM   1630  NH1 ARG A 217      36.139  25.466   5.108  1.00 16.79           N
ATOM   1631  NH2 ARG A 217      38.021  24.476   4.254  1.00 26.45           N
ATOM   1632  N   ASP A 218      32.477  18.461   5.145  1.00 11.86           N
ATOM   1633  CA  ASP A 218      33.084  17.133   5.257  1.00 15.24           C
ATOM   1634  C   ASP A 218      32.505  16.178   4.218  1.00 13.49           C
ATOM   1635  O   ASP A 218      33.213  15.313   3.705  1.00 12.43           O
ATOM   1636  CB  ASP A 218      32.869  16.548   6.659  1.00 24.02           C
ATOM   1637  CG  ASP A 218      33.461  17.413   7.756  1.00 41.36           C
ATOM   1638  OD1 ASP A 218      34.321  18.269   7.455  1.00 47.11           O
ATOM   1639  OD2 ASP A 218      33.065  17.234   8.928  1.00 51.51           O
ATOM   1640  N   VAL A 219      31.215  16.328   3.928  1.00 14.70           N
ATOM   1641  CA  VAL A 219      30.540  15.485   2.942  1.00 13.36           C
ATOM   1642  C   VAL A 219      31.028  15.829   1.541  1.00  9.50           C
ATOM   1643  O   VAL A 219      31.537  14.967   0.825  1.00  9.37           O
ATOM   1644  CB  VAL A 219      29.000  15.685   2.963  1.00 14.22           C
ATOM   1645  CG1 VAL A 219      28.348  14.899   1.828  1.00 13.29           C
ATOM   1646  CG2 VAL A 219      28.420  15.265   4.301  1.00 15.33           C
ATOM   1647  N   LEU A 220      30.888  17.102   1.178  1.00  8.60           N
ATOM   1648  CA  LEU A 220      31.271  17.606  -0.137  1.00  7.98           C
ATOM   1649  C   LEU A 220      32.765  17.460  -0.435  1.00 11.66           C
ATOM   1650  O   LEU A 220      33.166  17.402  -1.598  1.00 15.72           O
ATOM   1651  CB  LEU A 220      30.829  19.068  -0.292  1.00  7.58           C
ATOM   1652  CG  LEU A 220      29.334  19.377  -0.116  1.00  9.38           C
ATOM   1653  CD1 LEU A 220      29.124  20.880  -0.180  1.00 10.75           C
ATOM   1654  CD2 LEU A 220      28.475  18.662  -1.176  1.00  2.11           C
ATOM   1655  N   GLU A 221      33.595  17.422   0.602  1.00 12.27           N
ATOM   1656  CA  GLU A 221      35.028  17.246   0.387  1.00 14.78           C
ATOM   1657  C   GLU A 221      35.355  15.761   0.256  1.00 17.27           C
ATOM   1658  O   GLU A 221      36.519  15.389   0.101  1.00 19.31           O
ATOM   1659  CB  GLU A 221      35.855  17.880   1.511  1.00 10.41           C
ATOM   1660  CG  GLU A 221      35.903  19.392   1.435  1.00 13.29           C
ATOM   1661  CD  GLU A 221      36.754  20.031   2.509  1.00 10.45           C
ATOM   1662  OE1 GLU A 221      37.136  19.349   3.484  1.00 25.04           O
ATOM   1663  OE2 GLU A 221      37.029  21.238   2.380  1.00 19.31           O
ATOM   1664  N   ASN A 222      34.318  14.927   0.325  1.00 15.21           N
ATOM   1665  CA  ASN A 222      34.453  13.481   0.196  1.00 20.13           C
ATOM   1666  C   ASN A 222      35.244  12.901   1.361  1.00 22.32           C
ATOM   1667  O   ASN A 222      36.056  11.995   1.179  1.00 23.31           O
ATOM   1668  CB  ASN A 222      35.142  13.131  -1.132  1.00 22.59           C
ATOM   1669  CG  ASN A 222      34.907  11.696  -1.550  1.00 14.48           C
ATOM   1670  OD1 ASN A 222      33.850  11.130  -1.285  1.00 17.10           O
ATOM   1671  ND2 ASN A 222      35.883  11.104  -2.221  1.00 19.17           N
ATOM   1672  N   LYS A 223      34.988  13.411   2.561  1.00 19.68           N
ATOM   1673  CA  LYS A 223      35.700  12.951   3.744  1.00 22.07           C
ATOM   1674  C   LYS A 223      34.834  12.268   4.793  1.00 25.43           C
ATOM   1675  O   LYS A 223      35.289  11.334   5.449  1.00 28.80           O
ATOM   1676  CB  LYS A 223      36.500  14.106   4.355  1.00 23.48           C
ATOM   1677  CG  LYS A 223      37.720  14.481   3.515  1.00 26.54           C
ATOM   1678  CD  LYS A 223      38.140  15.929   3.695  1.00  8.73           C
ATOM   1679  CE  LYS A 223      39.304  16.265   2.771  1.00 11.00           C
ATOM   1680  NZ  LYS A 223      39.591  17.731   2.743  1.00 17.15           N
ATOM   1681  N   LEU A 224      33.582  12.696   4.933  1.00 24.39           N
ATOM   1682  CA  LEU A 224      32.690  12.082   5.915  1.00 24.38           C
ATOM   1683  C   LEU A 224      32.417  10.624   5.559  1.00 22.68           C
ATOM   1684  O   LEU A 224      32.522   9.736   6.405  1.00 21.06           O
ATOM   1685  CB  LEU A 224      31.371  12.852   6.019  1.00 24.60           C
ATOM   1686  CG  LEU A 224      30.368  12.314   7.045  1.00 26.33           C
ATOM   1687  CD1 LEU A 224      31.018  12.193   8.422  1.00 25.71           C
ATOM   1688  CD2 LEU A 224      29.161  13.230   7.102  1.00 28.93           C
ATOM   1689  N   LEU A 225      32.065  10.392   4.302  1.00 22.90           N
ATOM   1690  CA  LEU A 225      31.781   9.052   3.816  1.00 21.40           C
ATOM   1691  C   LEU A 225      32.352   9.008   2.405  1.00 22.63           C
ATOM   1692  O   LEU A 225      31.647   9.256   1.431  1.00 24.18           O
ATOM   1693  CB  LEU A 225      30.267   8.812   3.806  1.00 20.83           C
ATOM   1694  CG  LEU A 225      29.781   7.383   4.070  1.00 20.75           C
ATOM   1695  CD1 LEU A 225      28.319   7.415   4.462  1.00 16.86           C
ATOM   1696  CD2 LEU A 225      30.009   6.491   2.857  1.00 19.91           C
ATOM   1697  N   PRO A 226      33.659   8.733   2.285  1.00 23.80           N
ATOM   1698  CA  PRO A 226      34.368   8.661   1.008  1.00 23.20           C
ATOM   1699  C   PRO A 226      33.732   7.807  -0.088  1.00 22.07           C
ATOM   1700  O   PRO A 226      33.407   6.639   0.115  1.00 23.23           O
ATOM   1701  CB  PRO A 226      35.726   8.123   1.426  1.00 24.90           C
ATOM   1702  CG  PRO A 226      35.928   8.773   2.732  1.00 25.11           C
ATOM   1703  CD  PRO A 226      34.599   8.502   3.394  1.00 24.13           C
ATOM   1704  N   LEU A 227      33.612   8.403  -1.266  1.00 17.82           N
ATOM   1705  CA  LEU A 227      33.044   7.755  -2.433  1.00 19.74           C
ATOM   1706  C   LEU A 227      34.117   7.831  -3.513  1.00 22.75           C
ATOM   1707  O   LEU A 227      34.763   8.867  -3.675  1.00 24.62           O
ATOM   1708  CB  LEU A 227      31.804   8.516  -2.891  1.00 19.32           C
ATOM   1709  CG  LEU A 227      30.516   7.740  -3.136  1.00 21.06           C
ATOM   1710  CD1 LEU A 227      30.215   6.867  -1.924  1.00 22.12           C
ATOM   1711  CD2 LEU A 227      29.369   8.714  -3.402  1.00 16.83           C
ATOM   1712  N   ARG A 228      34.299   6.746  -4.254  1.00 23.43           N
ATOM   1713  CA  ARG A 228      35.301   6.698  -5.313  1.00 21.26           C
ATOM   1714  C   ARG A 228      35.152   7.850  -6.310  1.00 17.35           C
ATOM   1715  O   ARG A 228      36.146   8.458  -6.702  1.00 20.05           O
ATOM   1716  CB  ARG A 228      35.230   5.355  -6.042  1.00 16.33           C
ATOM   1717  CG  ARG A 228      36.401   5.064  -6.972  1.00 16.85           C
ATOM   1718  CD  ARG A 228      36.392   3.594  -7.367  1.00 29.69           C
ATOM   1719  NE  ARG A 228      37.455   3.240  -8.305  1.00 36.69           N
ATOM   1720  CZ  ARG A 228      38.627   2.717  -7.953  1.00 53.73           C
ATOM   1721  NH1 ARG A 228      38.909   2.484  -6.674  1.00 50.22           N
ATOM   1722  NH2 ARG A 228      39.510   2.384  -8.888  1.00 42.03           N
ATOM   1723  N   ARG A 229      33.920   8.181  -6.682  1.00 12.11           N
ATOM   1724  CA  ARG A 229      33.680   9.256  -7.641  1.00 20.53           C
ATOM   1725  C   ARG A 229      33.401  10.605  -6.981  1.00 20.97           C
ATOM   1726  O   ARG A 229      33.186  11.606  -7.668  1.00 21.93           O
ATOM   1727  CB  ARG A 229      32.528   8.884  -8.580  1.00 34.31           C
ATOM   1728  CG  ARG A 229      32.795   7.670  -9.461  1.00 39.79           C
ATOM   1729  CD  ARG A 229      33.812   7.983 -10.545  1.00 48.68           C
ATOM   1730  NE  ARG A 229      34.518   6.787 -10.998  1.00 52.09           N
ATOM   1731  CZ  ARG A 229      35.830   6.739 -11.208  1.00 48.14           C
ATOM   1732  NH1 ARG A 229      36.577   7.818 -11.013  1.00 47.59           N
ATOM   1733  NH2 ARG A 229      36.405   5.605 -11.578  1.00 36.41           N
ATOM   1734  N   GLY A 230      33.409  10.629  -5.654  1.00 18.90           N
ATOM   1735  CA  GLY A 230      33.159  11.868  -4.949  1.00 19.91           C
ATOM   1736  C   GLY A 230      31.696  12.260  -4.815  1.00 18.70           C
ATOM   1737  O   GLY A 230      30.782  11.449  -5.020  1.00 18.70           O
ATOM   1738  N   TYR A 231      31.491  13.522  -4.454  1.00 13.24           N
ATOM   1739  CA  TYR A 231      30.169  14.094  -4.253  1.00 11.69           C
ATOM   1740  C   TYR A 231      30.089  15.443  -4.948  1.00 12.67           C
ATOM   1741  O   TYR A 231      31.085  16.169  -5.035  1.00 14.21           O
ATOM   1742  CB  TYR A 231      29.913  14.331  -2.757  1.00 10.25           C
ATOM   1743  CG  TYR A 231      29.738  13.082  -1.916  1.00 11.17           C
ATOM   1744  CD1 TYR A 231      30.837  12.378  -1.429  1.00  9.56           C
ATOM   1745  CD2 TYR A 231      28.466  12.618  -1.590  1.00 11.77           C
ATOM   1746  CE1 TYR A 231      30.668  11.238  -0.634  1.00  5.17           C
ATOM   1747  CE2 TYR A 231      28.290  11.490  -0.800  1.00  8.59           C
ATOM   1748  CZ  TYR A 231      29.391  10.804  -0.328  1.00  3.39           C
ATOM   1749  OH  TYR A 231      29.193   9.674   0.430  1.00  5.67           O
ATOM   1750  N   ILE A 232      28.904  15.774  -5.446  1.00  8.67           N
ATOM   1751  CA  ILE A 232      28.681  17.058  -6.090  1.00  9.34           C
ATOM   1752  C   ILE A 232      27.435  17.639  -5.443  1.00  8.75           C
ATOM   1753  O   ILE A 232      26.410  16.963  -5.335  1.00  7.55           O
ATOM   1754  CB  ILE A 232      28.468  16.948  -7.623  1.00  7.93           C
ATOM   1755  CG1 ILE A 232      29.730  16.419  -8.315  1.00  8.63           C
ATOM   1756  CG2 ILE A 232      28.168  18.325  -8.201  1.00  6.55           C
ATOM   1757  CD1 ILE A 232      29.927  14.923  -8.222  1.00 18.47           C
ATOM   1758  N   GLY A 233      27.537  18.876  -4.978  1.00  8.17           N
ATOM   1759  CA  GLY A 233      26.409  19.509  -4.329  1.00  6.32           C
ATOM   1760  C   GLY A 233      25.604  20.367  -5.274  1.00  9.30           C
ATOM   1761  O   GLY A 233      26.151  20.972  -6.194  1.00 10.89           O
ATOM   1762  N   VAL A 234      24.296  20.412  -5.062  1.00  7.66           N
ATOM   1763  CA  VAL A 234      23.435  21.223  -5.900  1.00  8.68           C
ATOM   1764  C   VAL A 234      22.380  21.913  -5.050  1.00  7.98           C
ATOM   1765  O   VAL A 234      22.082  21.495  -3.930  1.00  8.24           O
ATOM   1766  CB  VAL A 234      22.739  20.381  -6.999  1.00  8.99           C
ATOM   1767  CG1 VAL A 234      23.779  19.662  -7.850  1.00  9.10           C
ATOM   1768  CG2 VAL A 234      21.767  19.386  -6.383  1.00  8.36           C
ATOM   1769  N   VAL A 235      21.856  23.009  -5.567  1.00  5.86           N
ATOM   1770  CA  VAL A 235      20.821  23.751  -4.880  1.00  8.65           C
ATOM   1771  C   VAL A 235      19.757  23.991  -5.928  1.00  7.98           C
ATOM   1772  O   VAL A 235      19.956  24.778  -6.856  1.00  6.12           O
ATOM   1773  CB  VAL A 235      21.333  25.105  -4.351  1.00  9.43           C
ATOM   1774  CG1 VAL A 235      20.209  25.846  -3.639  1.00  7.63           C
ATOM   1775  CG2 VAL A 235      22.497  24.886  -3.416  1.00 11.08           C
ATOM   1776  N   ASN A 236      18.659  23.256  -5.816  1.00  9.48           N
ATOM   1777  CA  ASN A 236      17.564  23.385  -6.764  1.00 11.15           C
ATOM   1778  C   ASN A 236      16.391  24.169  -6.194  1.00 11.19           C
ATOM   1779  O   ASN A 236      16.454  24.663  -5.060  1.00 12.20           O
ATOM   1780  CB  ASN A 236      17.142  22.004  -7.274  1.00 15.25           C
ATOM   1781  CG  ASN A 236      18.196  21.377  -8.179  1.00 17.90           C
ATOM   1782  OD1 ASN A 236      18.801  22.057  -9.010  1.00 25.13           O
ATOM   1783  ND2 ASN A 236      18.439  20.090  -8.007  1.00 11.24           N
ATOM   1784  N   ARG A 237      15.334  24.301  -6.991  1.00  7.04           N
ATOM   1785  CA  ARG A 237      14.139  25.047  -6.599  1.00  9.92           C
ATOM   1786  C   ARG A 237      13.331  24.462  -5.450  1.00 11.70           C
ATOM   1787  O   ARG A 237      13.119  23.252  -5.371  1.00 14.23           O
ATOM   1788  CB  ARG A 237      13.233  25.262  -7.817  1.00  5.34           C
ATOM   1789  CG  ARG A 237      13.810  26.267  -8.817  1.00  5.07           C
ATOM   1790  CD  ARG A 237      13.099  26.235 -10.153  1.00  6.44           C
ATOM   1791  NE  ARG A 237      13.429  25.029 -10.903  1.00  9.15           N
ATOM   1792  CZ  ARG A 237      13.219  24.879 -12.206  1.00 11.47           C
ATOM   1793  NH1 ARG A 237      12.674  25.861 -12.913  1.00 10.20           N
ATOM   1794  NH2 ARG A 237      13.573  23.751 -12.808  1.00 10.52           N
ATOM   1795  N   SER A 238      12.876  25.342  -4.565  1.00  8.54           N
ATOM   1796  CA  SER A 238      12.069  24.954  -3.415  1.00  9.65           C
ATOM   1797  C   SER A 238      10.607  24.869  -3.849  1.00 11.70           C
ATOM   1798  O   SER A 238      10.279  25.177  -5.004  1.00  9.91           O
ATOM   1799  CB  SER A 238      12.213  26.009  -2.323  1.00  7.36           C
ATOM   1800  OG  SER A 238      11.851  27.273  -2.841  1.00  9.06           O
ATOM   1801  N   GLN A 239       9.721  24.494  -2.928  1.00 10.86           N
ATOM   1802  CA  GLN A 239       8.306  24.388  -3.261  1.00 11.84           C
ATOM   1803  C   GLN A 239       7.746  25.753  -3.637  1.00 13.81           C
ATOM   1804  O   GLN A 239       7.019  25.885  -4.624  1.00 12.57           O
ATOM   1805  CB  GLN A 239       7.497  23.769  -2.119  1.00 10.34           C
ATOM   1806  CG  GLN A 239       6.083  23.353  -2.554  1.00  1.46           C
ATOM   1807  CD  GLN A 239       6.095  22.545  -3.850  1.00 14.33           C
ATOM   1808  OE1 GLN A 239       6.841  21.576  -3.979  1.00 10.07           O
ATOM   1809  NE2 GLN A 239       5.295  22.966  -4.825  1.00  3.30           N
ATOM   1810  N   LYS A 240       8.086  26.770  -2.850  1.00 13.78           N
ATOM   1811  CA  LYS A 240       7.639  28.126  -3.137  1.00 10.90           C
ATOM   1812  C   LYS A 240       8.103  28.478  -4.554  1.00  7.83           C
ATOM   1813  O   LYS A 240       7.342  29.044  -5.331  1.00  7.91           O
ATOM   1814  CB  LYS A 240       8.198  29.109  -2.094  1.00 10.90           C
ATOM   1815  CG  LYS A 240       8.547  30.494  -2.626  1.00 21.05           C
ATOM   1816  CD  LYS A 240       7.756  31.605  -1.956  1.00 40.84           C
ATOM   1817  CE  LYS A 240       6.271  31.494  -2.248  1.00 53.19           C
ATOM   1818  NZ  LYS A 240       5.527  32.745  -1.923  1.00 50.21           N
ATOM   1819  N   ASP A 241       9.330  28.090  -4.897  1.00 10.19           N
ATOM   1820  CA  ASP A 241       9.881  28.343  -6.229  1.00 11.55           C
ATOM   1821  C   ASP A 241       9.054  27.650  -7.324  1.00 13.30           C
ATOM   1822  O   ASP A 241       8.748  28.257  -8.354  1.00 12.29           O
ATOM   1823  CB  ASP A 241      11.338  27.869  -6.319  1.00 13.19           C
ATOM   1824  CG  ASP A 241      12.325  28.794  -5.606  1.00 19.18           C
ATOM   1825  OD1 ASP A 241      11.919  29.860  -5.093  1.00 23.53           O
ATOM   1826  OD2 ASP A 241      13.530  28.444  -5.566  1.00 18.86           O
ATOM   1827  N   ILE A 242       8.708  26.380  -7.108  1.00 11.09           N
ATOM   1828  CA  ILE A 242       7.912  25.621  -8.075  1.00  7.19           C
ATOM   1829  C   ILE A 242       6.531  26.255  -8.200  1.00  8.91           C
ATOM   1830  O   ILE A 242       6.009  26.417  -9.309  1.00 14.13           O
ATOM   1831  CB  ILE A 242       7.749  24.136  -7.651  1.00  7.00           C
ATOM   1832  CG1 ILE A 242       9.111  23.450  -7.626  1.00  7.79           C
ATOM   1833  CG2 ILE A 242       6.805  23.388  -8.620  1.00  5.64           C
ATOM   1834  CD1 ILE A 242       9.058  22.014  -7.192  1.00 10.21           C
ATOM   1835  N   ASP A 243       5.949  26.623  -7.062  1.00  6.49           N
ATOM   1836  CA  ASP A 243       4.633  27.253  -7.048  1.00 11.19           C
ATOM   1837  C   ASP A 243       4.644  28.548  -7.848  1.00 10.83           C
ATOM   1838  O   ASP A 243       3.704  28.824  -8.589  1.00 12.39           O
ATOM   1839  CB  ASP A 243       4.178  27.557  -5.614  1.00 16.34           C
ATOM   1840  CG  ASP A 243       3.874  26.300  -4.810  1.00 26.43           C
ATOM   1841  OD1 ASP A 243       3.449  25.288  -5.406  1.00 17.66           O
ATOM   1842  OD2 ASP A 243       4.051  26.333  -3.573  1.00 30.72           O
ATOM   1843  N   GLY A 244       5.712  29.329  -7.691  1.00 12.10           N
ATOM   1844  CA  GLY A 244       5.840  30.600  -8.387  1.00 14.57           C
ATOM   1845  C   GLY A 244       6.379  30.523  -9.807  1.00 18.86           C
ATOM   1846  O   GLY A 244       6.620  31.555 -10.438  1.00 20.77           O
ATOM   1847  N   LYS A 245       6.579  29.308 -10.309  1.00 18.26           N
ATOM   1848  CA  LYS A 245       7.095  29.090 -11.658  1.00 17.83           C
ATOM   1849  C   LYS A 245       8.474  29.722 -11.913  1.00 18.81           C
ATOM   1850  O   LYS A 245       8.738  30.245 -12.998  1.00 20.59           O
ATOM   1851  CB  LYS A 245       6.082  29.571 -12.709  1.00 11.35           C
ATOM   1852  CG  LYS A 245       4.728  28.842 -12.682  1.00 12.63           C
ATOM   1853  CD  LYS A 245       4.895  27.346 -12.930  1.00 25.83           C
ATOM   1854  CE  LYS A 245       3.568  26.665 -13.249  1.00 41.20           C
ATOM   1855  NZ  LYS A 245       3.115  26.939 -14.644  1.00 39.55           N
ATOM   1856  N   LYS A 246       9.357  29.662 -10.922  1.00 17.51           N
ATOM   1857  CA  LYS A 246      10.701  30.221 -11.081  1.00 16.56           C
ATOM   1858  C   LYS A 246      11.382  29.439 -12.199  1.00 14.98           C
ATOM   1859  O   LYS A 246      11.318  28.211 -12.218  1.00 14.02           O
ATOM   1860  CB  LYS A 246      11.487  30.087  -9.774  1.00 18.27           C
ATOM   1861  CG  LYS A 246      12.890  30.667  -9.812  1.00 14.83           C
ATOM   1862  CD  LYS A 246      13.474  30.742  -8.410  1.00 13.60           C
ATOM   1863  CE  LYS A 246      14.902  31.248  -8.437  1.00 15.37           C
ATOM   1864  NZ  LYS A 246      15.454  31.408  -7.074  1.00 11.32           N
ATOM   1865  N   ASP A 247      12.000  30.141 -13.144  1.00 14.43           N
ATOM   1866  CA  ASP A 247      12.650  29.469 -14.267  1.00 17.74           C
ATOM   1867  C   ASP A 247      14.028  28.901 -13.950  1.00 16.14           C
ATOM   1868  O   ASP A 247      14.638  29.253 -12.942  1.00 16.01           O
ATOM   1869  CB  ASP A 247      12.713  30.390 -15.493  1.00 23.29           C
ATOM   1870  CG  ASP A 247      13.419  31.698 -15.207  1.00 33.74           C
ATOM   1871  OD1 ASP A 247      14.663  31.729 -15.272  1.00 31.57           O
ATOM   1872  OD2 ASP A 247      12.728  32.694 -14.916  1.00 44.72           O
ATOM   1873  N   ILE A 248      14.519  28.033 -14.829  1.00 15.14           N
ATOM   1874  CA  ILE A 248      15.821  27.409 -14.644  1.00 15.86           C
ATOM   1875  C   ILE A 248      16.996  28.366 -14.545  1.00 15.12           C
ATOM   1876  O   ILE A 248      17.813  28.224 -13.642  1.00 16.26           O
ATOM   1877  CB  ILE A 248      16.155  26.354 -15.732  1.00 20.81           C
ATOM   1878  CG1 ILE A 248      15.477  26.696 -17.063  1.00 23.94           C
ATOM   1879  CG2 ILE A 248      15.840  24.959 -15.223  1.00 24.06           C
ATOM   1880  CD1 ILE A 248      15.794  25.723 -18.195  1.00 30.18           C
ATOM   1881  N   THR A 249      17.097  29.332 -15.456  1.00 12.94           N
ATOM   1882  CA  THR A 249      18.224  30.264 -15.411  1.00 14.23           C
ATOM   1883  C   THR A 249      18.320  30.951 -14.058  1.00 12.64           C
ATOM   1884  O   THR A 249      19.409  31.102 -13.514  1.00 17.64           O
ATOM   1885  CB  THR A 249      18.185  31.316 -16.551  1.00 17.08           C
ATOM   1886  OG1 THR A 249      17.001  32.114 -16.453  1.00 32.13           O
ATOM   1887  CG2 THR A 249      18.222  30.632 -17.909  1.00  4.15           C
ATOM   1888  N   ALA A 250      17.168  31.291 -13.488  1.00 10.26           N
ATOM   1889  CA  ALA A 250      17.117  31.946 -12.188  1.00 12.98           C
ATOM   1890  C   ALA A 250      17.568  30.993 -11.079  1.00 15.50           C
ATOM   1891  O   ALA A 250      18.320  31.383 -10.185  1.00 19.08           O
ATOM   1892  CB  ALA A 250      15.711  32.465 -11.914  1.00 13.21           C
ATOM   1893  N   ALA A 251      17.117  29.743 -11.144  1.00 15.73           N
ATOM   1894  CA  ALA A 251      17.495  28.738 -10.151  1.00 15.21           C
ATOM   1895  C   ALA A 251      19.006  28.487 -10.206  1.00 13.28           C
ATOM   1896  O   ALA A 251      19.678  28.437  -9.176  1.00 12.26           O
ATOM   1897  CB  ALA A 251      16.729  27.439 -10.397  1.00 14.92           C
ATOM   1898  N   LEU A 252      19.530  28.336 -11.419  1.00 11.06           N
ATOM   1899  CA  LEU A 252      20.954  28.115 -11.636  1.00  9.76           C
ATOM   1900  C   LEU A 252      21.767  29.319 -11.159  1.00 10.45           C
ATOM   1901  O   LEU A 252      22.881  29.158 -10.651  1.00  9.13           O
ATOM   1902  CB  LEU A 252      21.230  27.860 -13.120  1.00 12.51           C
ATOM   1903  CG  LEU A 252      21.076  26.438 -13.687  1.00 19.27           C
ATOM   1904  CD1 LEU A 252      19.865  25.736 -13.108  1.00 23.26           C
ATOM   1905  CD2 LEU A 252      20.987  26.505 -15.210  1.00 17.79           C
ATOM   1906  N   ALA A 253      21.217  30.520 -11.340  1.00  9.53           N
ATOM   1907  CA  ALA A 253      21.889  31.747 -10.918  1.00 13.13           C
ATOM   1908  C   ALA A 253      21.968  31.801  -9.393  1.00 13.52           C
ATOM   1909  O   ALA A 253      22.976  32.233  -8.828  1.00 13.48           O
ATOM   1910  CB  ALA A 253      21.152  32.978 -11.461  1.00 13.36           C
ATOM   1911  N   ALA A 254      20.908  31.341  -8.732  1.00 11.86           N
ATOM   1912  CA  ALA A 254      20.856  31.314  -7.274  1.00  8.64           C
ATOM   1913  C   ALA A 254      21.802  30.255  -6.715  1.00  9.62           C
ATOM   1914  O   ALA A 254      22.401  30.438  -5.651  1.00 11.66           O
ATOM   1915  CB  ALA A 254      19.440  31.055  -6.802  1.00  8.05           C
ATOM   1916  N   GLU A 255      21.923  29.138  -7.421  1.00  9.94           N
ATOM   1917  CA  GLU A 255      22.808  28.056  -6.996  1.00  9.67           C
ATOM   1918  C   GLU A 255      24.264  28.515  -7.062  1.00 11.09           C
ATOM   1919  O   GLU A 255      25.035  28.322  -6.118  1.00 12.19           O
ATOM   1920  CB  GLU A 255      22.593  26.833  -7.889  1.00  7.06           C
ATOM   1921  CG  GLU A 255      23.637  25.750  -7.743  1.00 12.51           C
ATOM   1922  CD  GLU A 255      23.445  24.642  -8.760  1.00 21.65           C
ATOM   1923  OE1 GLU A 255      23.839  24.819  -9.926  1.00 23.61           O
ATOM   1924  OE2 GLU A 255      22.893  23.593  -8.398  1.00  9.22           O
ATOM   1925  N   ARG A 256      24.621  29.157  -8.171  1.00 11.14           N
ATOM   1926  CA  ARG A 256      25.975  29.669  -8.381  1.00 13.73           C
ATOM   1927  C   ARG A 256      26.335  30.684  -7.295  1.00 15.49           C
ATOM   1928  O   ARG A 256      27.423  30.632  -6.716  1.00 16.76           O
ATOM   1929  CB  ARG A 256      26.061  30.330  -9.758  1.00 14.94           C
ATOM   1930  CG  ARG A 256      27.381  31.012 -10.066  1.00 22.17           C
ATOM   1931  CD  ARG A 256      27.300  31.713 -11.416  1.00 37.59           C
ATOM   1932  NE  ARG A 256      28.537  32.400 -11.783  1.00 51.86           N
ATOM   1933  CZ  ARG A 256      28.818  33.662 -11.472  1.00 49.37           C
ATOM   1934  NH1 ARG A 256      27.952  34.388 -10.777  1.00 35.00           N
ATOM   1935  NH2 ARG A 256      29.952  34.209 -11.889  1.00 52.37           N
ATOM   1936  N   LYS A 257      25.419  31.612  -7.031  1.00 10.03           N
ATOM   1937  CA  LYS A 257      25.640  32.625  -6.009  1.00  8.65           C
ATOM   1938  C   LYS A 257      25.838  31.952  -4.651  1.00 11.45           C
ATOM   1939  O   LYS A 257      26.690  32.361  -3.860  1.00 11.47           O
ATOM   1940  CB  LYS A 257      24.451  33.593  -5.944  1.00  3.96           C
ATOM   1941  CG  LYS A 257      24.564  34.615  -4.824  1.00 12.83           C
ATOM   1942  CD  LYS A 257      23.269  35.377  -4.609  1.00 28.85           C
ATOM   1943  CE  LYS A 257      23.376  36.262  -3.376  1.00 43.43           C
ATOM   1944  NZ  LYS A 257      22.142  37.065  -3.138  1.00 61.77           N
ATOM   1945  N   PHE A 258      25.062  30.904  -4.401  1.00 10.92           N
ATOM   1946  CA  PHE A 258      25.141  30.167  -3.145  1.00 10.37           C
ATOM   1947  C   PHE A 258      26.539  29.595  -2.883  1.00 11.25           C
ATOM   1948  O   PHE A 258      27.095  29.766  -1.796  1.00 12.44           O
ATOM   1949  CB  PHE A 258      24.106  29.033  -3.141  1.00 10.48           C
ATOM   1950  CG  PHE A 258      24.146  28.175  -1.908  1.00 10.71           C
ATOM   1951  CD1 PHE A 258      23.519  28.591  -0.736  1.00 10.05           C
ATOM   1952  CD2 PHE A 258      24.823  26.959  -1.915  1.00 10.08           C
ATOM   1953  CE1 PHE A 258      23.566  27.808   0.414  1.00 11.15           C
ATOM   1954  CE2 PHE A 258      24.878  26.167  -0.773  1.00 11.24           C
ATOM   1955  CZ  PHE A 258      24.248  26.591   0.399  1.00 11.13           C
ATOM   1956  N   PHE A 259      27.113  28.921  -3.873  1.00  6.57           N
ATOM   1957  CA  PHE A 259      28.426  28.326  -3.680  1.00  8.20           C
ATOM   1958  C   PHE A 259      29.566  29.330  -3.623  1.00 10.79           C
ATOM   1959  O   PHE A 259      30.508  29.147  -2.866  1.00 12.56           O
ATOM   1960  CB  PHE A 259      28.689  27.241  -4.718  1.00  7.22           C
ATOM   1961  CG  PHE A 259      27.916  25.979  -4.467  1.00  6.51           C
ATOM   1962  CD1 PHE A 259      28.160  25.217  -3.323  1.00  5.09           C
ATOM   1963  CD2 PHE A 259      26.928  25.563  -5.353  1.00  4.11           C
ATOM   1964  CE1 PHE A 259      27.430  24.062  -3.062  1.00  3.72           C
ATOM   1965  CE2 PHE A 259      26.192  24.408  -5.103  1.00  4.76           C
ATOM   1966  CZ  PHE A 259      26.441  23.657  -3.959  1.00  4.46           C
ATOM   1967  N   LEU A 260      29.446  30.418  -4.375  1.00 10.89           N
ATOM   1968  CA  LEU A 260      30.473  31.448  -4.392  1.00 11.75           C
ATOM   1969  C   LEU A 260      30.529  32.249  -3.092  1.00 13.16           C
ATOM   1970  O   LEU A 260      31.587  32.754  -2.720  1.00 11.68           O
ATOM   1971  CB  LEU A 260      30.248  32.411  -5.567  1.00 11.03           C
ATOM   1972  CG  LEU A 260      30.480  31.874  -6.980  1.00 16.48           C
ATOM   1973  CD1 LEU A 260      30.054  32.904  -8.007  1.00 18.40           C
ATOM   1974  CD2 LEU A 260      31.942  31.508  -7.165  1.00 23.65           C
ATOM   1975  N   SER A 261      29.396  32.358  -2.400  1.00 14.84           N
ATOM   1976  CA  SER A 261      29.345  33.145  -1.176  1.00 15.02           C
ATOM   1977  C   SER A 261      29.449  32.387   0.139  1.00 15.73           C
ATOM   1978  O   SER A 261      29.956  32.927   1.124  1.00 17.66           O
ATOM   1979  CB  SER A 261      28.094  34.027  -1.170  1.00 17.64           C
ATOM   1980  OG  SER A 261      26.912  33.251  -1.225  1.00 24.05           O
ATOM   1981  N   HIS A 262      28.974  31.146   0.163  1.00 13.70           N
ATOM   1982  CA  HIS A 262      29.004  30.350   1.384  1.00 11.38           C
ATOM   1983  C   HIS A 262      30.442  30.102   1.852  1.00 10.67           C
ATOM   1984  O   HIS A 262      31.217  29.428   1.174  1.00 13.39           O
ATOM   1985  CB  HIS A 262      28.272  29.026   1.164  1.00 11.31           C
ATOM   1986  CG  HIS A 262      27.804  28.384   2.432  1.00 12.03           C
ATOM   1987  ND1 HIS A 262      28.671  27.841   3.355  1.00 12.23           N
ATOM   1988  CD2 HIS A 262      26.559  28.213   2.937  1.00 10.59           C
ATOM   1989  CE1 HIS A 262      27.981  27.363   4.376  1.00 12.02           C
ATOM   1990  NE2 HIS A 262      26.698  27.576   4.146  1.00 11.70           N
ATOM   1991  N   PRO A 263      30.798  30.604   3.047  1.00 10.11           N
ATOM   1992  CA  PRO A 263      32.142  30.453   3.617  1.00  9.53           C
ATOM   1993  C   PRO A 263      32.662  29.020   3.719  1.00  9.48           C
ATOM   1994  O   PRO A 263      33.869  28.788   3.642  1.00 13.06           O
ATOM   1995  CB  PRO A 263      32.016  31.135   4.987  1.00 10.23           C
ATOM   1996  CG  PRO A 263      30.552  31.026   5.311  1.00 10.67           C
ATOM   1997  CD  PRO A 263      29.918  31.331   3.980  1.00 10.44           C
ATOM   1998  N   SER A 264      31.759  28.060   3.865  1.00  7.80           N
ATOM   1999  CA  SER A 264      32.158  26.663   3.953  1.00  8.18           C
ATOM   2000  C   SER A 264      32.342  25.992   2.593  1.00 10.58           C
ATOM   2001  O   SER A 264      32.940  24.918   2.519  1.00 15.22           O
ATOM   2002  CB  SER A 264      31.140  25.855   4.777  1.00  6.20           C
ATOM   2003  OG  SER A 264      31.048  26.319   6.117  1.00 13.29           O
ATOM   2004  N   TYR A 265      31.878  26.621   1.513  1.00  9.07           N
ATOM   2005  CA  TYR A 265      31.982  25.985   0.198  1.00  7.39           C
ATOM   2006  C   TYR A 265      32.613  26.762  -0.963  1.00  8.53           C
ATOM   2007  O   TYR A 265      32.824  26.179  -2.026  1.00  7.44           O
ATOM   2008  CB  TYR A 265      30.598  25.526  -0.286  1.00  6.11           C
ATOM   2009  CG  TYR A 265      29.668  24.914   0.742  1.00  5.22           C
ATOM   2010  CD1 TYR A 265      30.087  23.886   1.582  1.00  6.86           C
ATOM   2011  CD2 TYR A 265      28.348  25.350   0.844  1.00  4.26           C
ATOM   2012  CE1 TYR A 265      29.211  23.309   2.499  1.00  6.80           C
ATOM   2013  CE2 TYR A 265      27.470  24.784   1.749  1.00  4.55           C
ATOM   2014  CZ  TYR A 265      27.904  23.764   2.575  1.00  6.68           C
ATOM   2015  OH  TYR A 265      27.028  23.193   3.468  1.00  1.46           O
ATOM   2016  N   ARG A 266      32.899  28.053  -0.813  1.00  8.22           N
ATOM   2017  CA  ARG A 266      33.459  28.780  -1.957  1.00 11.61           C
ATOM   2018  C   ARG A 266      34.784  28.267  -2.507  1.00 15.18           C
ATOM   2019  O   ARG A 266      35.046  28.393  -3.703  1.00 18.11           O
ATOM   2020  CB  ARG A 266      33.479  30.293  -1.736  1.00 19.63           C
ATOM   2021  CG  ARG A 266      34.159  30.766  -0.491  1.00 28.41           C
ATOM   2022  CD  ARG A 266      33.881  32.241  -0.311  1.00 35.78           C
ATOM   2023  NE  ARG A 266      34.661  32.793   0.785  1.00 34.78           N
ATOM   2024  CZ  ARG A 266      34.141  33.327   1.882  1.00 21.97           C
ATOM   2025  NH1 ARG A 266      32.824  33.393   2.043  1.00 26.73           N
ATOM   2026  NH2 ARG A 266      34.951  33.781   2.823  1.00 31.21           N
ATOM   2027  N   HIS A 267      35.598  27.641  -1.664  1.00 11.84           N
ATOM   2028  CA  HIS A 267      36.854  27.085  -2.148  1.00 13.25           C
ATOM   2029  C   HIS A 267      36.569  25.845  -3.016  1.00 14.31           C
ATOM   2030  O   HIS A 267      37.451  25.353  -3.715  1.00 14.64           O
ATOM   2031  CB  HIS A 267      37.775  26.721  -0.979  1.00 13.96           C
ATOM   2032  CG  HIS A 267      37.279  25.577  -0.149  1.00 14.62           C
ATOM   2033  ND1 HIS A 267      36.145  25.659   0.629  1.00 12.71           N
ATOM   2034  CD2 HIS A 267      37.756  24.320   0.012  1.00 14.59           C
ATOM   2035  CE1 HIS A 267      35.942  24.503   1.234  1.00 13.03           C
ATOM   2036  NE2 HIS A 267      36.905  23.673   0.876  1.00 14.89           N
ATOM   2037  N   LEU A 268      35.325  25.364  -2.978  1.00 12.63           N
ATOM   2038  CA  LEU A 268      34.898  24.195  -3.751  1.00 12.50           C
ATOM   2039  C   LEU A 268      33.942  24.551  -4.882  1.00 13.90           C
ATOM   2040  O   LEU A 268      33.481  23.659  -5.587  1.00 12.41           O
ATOM   2041  CB  LEU A 268      34.154  23.196  -2.860  1.00 12.46           C
ATOM   2042  CG  LEU A 268      34.783  22.587  -1.618  1.00  9.36           C
ATOM   2043  CD1 LEU A 268      33.728  21.790  -0.870  1.00 10.11           C
ATOM   2044  CD2 LEU A 268      35.942  21.715  -2.019  1.00  8.87           C
ATOM   2045  N   ALA A 269      33.622  25.836  -5.037  1.00 16.25           N
ATOM   2046  CA  ALA A 269      32.683  26.296  -6.064  1.00 17.45           C
ATOM   2047  C   ALA A 269      32.860  25.677  -7.447  1.00 18.06           C
ATOM   2048  O   ALA A 269      31.890  25.238  -8.057  1.00 17.67           O
ATOM   2049  CB  ALA A 269      32.708  27.824  -6.171  1.00 17.61           C
ATOM   2050  N   ASP A 270      34.097  25.646  -7.932  1.00 20.53           N
ATOM   2051  CA  ASP A 270      34.413  25.097  -9.251  1.00 20.19           C
ATOM   2052  C   ASP A 270      34.104  23.606  -9.404  1.00 19.27           C
ATOM   2053  O   ASP A 270      34.179  23.061 -10.508  1.00 20.46           O
ATOM   2054  CB  ASP A 270      35.883  25.377  -9.602  1.00 26.22           C
ATOM   2055  CG  ASP A 270      36.870  24.758  -8.604  1.00 39.74           C
ATOM   2056  OD1 ASP A 270      36.447  24.249  -7.539  1.00 36.33           O
ATOM   2057  OD2 ASP A 270      38.089  24.791  -8.892  1.00 40.60           O
ATOM   2058  N   ARG A 271      33.799  22.945  -8.293  1.00 13.48           N
ATOM   2059  CA  ARG A 271      33.464  21.525  -8.303  1.00 11.04           C
ATOM   2060  C   ARG A 271      32.076  21.285  -7.708  1.00  7.76           C
ATOM   2061  O   ARG A 271      31.761  20.182  -7.295  1.00  5.71           O
ATOM   2062  CB  ARG A 271      34.513  20.726  -7.526  1.00 22.24           C
ATOM   2063  CG  ARG A 271      35.824  20.547  -8.270  1.00 30.40           C
ATOM   2064  CD  ARG A 271      36.913  19.993  -7.362  1.00 38.24           C
ATOM   2065  NE  ARG A 271      37.507  21.033  -6.525  1.00 59.40           N
ATOM   2066  CZ  ARG A 271      37.831  20.880  -5.244  1.00 51.13           C
ATOM   2067  NH1 ARG A 271      37.616  19.722  -4.629  1.00 40.73           N
ATOM   2068  NH2 ARG A 271      38.384  21.886  -4.581  1.00 41.12           N
ATOM   2069  N   MET A 272      31.242  22.320  -7.685  1.00 10.17           N
ATOM   2070  CA  MET A 272      29.894  22.209  -7.131  1.00  8.21           C
ATOM   2071  C   MET A 272      28.887  22.765  -8.113  1.00  8.03           C
ATOM   2072  O   MET A 272      29.228  23.618  -8.933  1.00  7.83           O
ATOM   2073  CB  MET A 272      29.772  23.012  -5.831  1.00  5.96           C
ATOM   2074  CG  MET A 272      30.548  22.476  -4.650  1.00  6.20           C
ATOM   2075  SD  MET A 272      29.860  20.957  -3.995  1.00  8.81           S
ATOM   2076  CE  MET A 272      31.202  19.826  -4.308  1.00  6.35           C
ATOM   2077  N   GLY A 273      27.641  22.314  -7.992  1.00  6.02           N
ATOM   2078  CA  GLY A 273      26.587  22.809  -8.852  1.00  6.76           C
ATOM   2079  C   GLY A 273      26.109  21.893  -9.964  1.00  6.33           C
ATOM   2080  O   GLY A 273      26.780  20.941 -10.356  1.00  4.52           O
ATOM   2081  N   THR A 274      24.934  22.235 -10.480  1.00 11.03           N
ATOM   2082  CA  THR A 274      24.252  21.529 -11.557  1.00 13.00           C
ATOM   2083  C   THR A 274      25.098  21.449 -12.842  1.00 14.91           C
ATOM   2084  O   THR A 274      25.283  20.359 -13.389  1.00 15.94           O
ATOM   2085  CB  THR A 274      22.869  22.193 -11.817  1.00 12.56           C
ATOM   2086  OG1 THR A 274      22.095  22.164 -10.606  1.00  6.87           O
ATOM   2087  CG2 THR A 274      22.108  21.474 -12.925  1.00 10.86           C
ATOM   2088  N   PRO A 275      25.624  22.592 -13.335  1.00 15.30           N
ATOM   2089  CA  PRO A 275      26.445  22.562 -14.552  1.00 15.69           C
ATOM   2090  C   PRO A 275      27.657  21.637 -14.382  1.00 13.55           C
ATOM   2091  O   PRO A 275      28.021  20.895 -15.297  1.00 11.64           O
ATOM   2092  CB  PRO A 275      26.886  24.022 -14.701  1.00 16.63           C
ATOM   2093  CG  PRO A 275      25.730  24.779 -14.131  1.00 15.91           C
ATOM   2094  CD  PRO A 275      25.426  23.984 -12.885  1.00 16.53           C
ATOM   2095  N   TYR A 276      28.283  21.680 -13.212  1.00  9.44           N
ATOM   2096  CA  TYR A 276      29.435  20.830 -12.963  1.00  5.94           C
ATOM   2097  C   TYR A 276      29.027  19.355 -12.877  1.00  6.26           C
ATOM   2098  O   TYR A 276      29.792  18.476 -13.263  1.00  8.78           O
ATOM   2099  CB  TYR A 276      30.172  21.265 -11.699  1.00  5.62           C
ATOM   2100  CG  TYR A 276      31.370  20.403 -11.386  1.00  6.91           C
ATOM   2101  CD1 TYR A 276      32.565  20.558 -12.086  1.00  7.27           C
ATOM   2102  CD2 TYR A 276      31.295  19.400 -10.416  1.00  5.85           C
ATOM   2103  CE1 TYR A 276      33.661  19.729 -11.828  1.00  3.14           C
ATOM   2104  CE2 TYR A 276      32.376  18.572 -10.154  1.00  2.95           C
ATOM   2105  CZ  TYR A 276      33.557  18.742 -10.863  1.00  9.02           C
ATOM   2106  OH  TYR A 276      34.631  17.924 -10.608  1.00 13.63           O
ATOM   2107  N   LEU A 277      27.838  19.078 -12.354  1.00  8.37           N
ATOM   2108  CA  LEU A 277      27.368  17.699 -12.267  1.00 11.34           C
ATOM   2109  C   LEU A 277      27.206  17.175 -13.693  1.00 11.19           C
ATOM   2110  O   LEU A 277      27.585  16.044 -14.003  1.00 10.68           O
ATOM   2111  CB  LEU A 277      26.031  17.619 -11.520  1.00 11.89           C
ATOM   2112  CG  LEU A 277      25.326  16.254 -11.522  1.00 13.37           C
ATOM   2113  CD1 LEU A 277      26.249  15.168 -10.991  1.00 12.11           C
ATOM   2114  CD2 LEU A 277      24.052  16.332 -10.690  1.00 16.07           C
ATOM   2115  N   GLN A 278      26.667  18.021 -14.562  1.00 12.17           N
ATOM   2116  CA  GLN A 278      26.469  17.660 -15.953  1.00 13.87           C
ATOM   2117  C   GLN A 278      27.793  17.258 -16.596  1.00 17.08           C
ATOM   2118  O   GLN A 278      27.874  16.223 -17.268  1.00 18.88           O
ATOM   2119  CB  GLN A 278      25.848  18.827 -16.720  1.00 18.37           C
ATOM   2120  CG  GLN A 278      25.606  18.531 -18.186  1.00 38.87           C
ATOM   2121  CD  GLN A 278      24.545  19.419 -18.783  1.00 42.60           C
ATOM   2122  OE1 GLN A 278      24.837  20.495 -19.306  1.00 41.97           O
ATOM   2123  NE2 GLN A 278      23.299  18.973 -18.711  1.00 37.90           N
ATOM   2124  N   LYS A 279      28.830  18.059 -16.362  1.00 15.33           N
ATOM   2125  CA  LYS A 279      30.153  17.788 -16.918  1.00 16.59           C
ATOM   2126  C   LYS A 279      30.684  16.443 -16.435  1.00 16.12           C
ATOM   2127  O   LYS A 279      31.156  15.635 -17.233  1.00 21.40           O
ATOM   2128  CB  LYS A 279      31.141  18.899 -16.546  1.00 23.57           C
ATOM   2129  CG  LYS A 279      32.519  18.704 -17.160  1.00 21.02           C
ATOM   2130  CD  LYS A 279      33.529  19.726 -16.670  1.00 38.20           C
ATOM   2131  CE  LYS A 279      34.838  19.602 -17.442  1.00 51.12           C
ATOM   2132  NZ  LYS A 279      35.365  18.201 -17.452  1.00 47.64           N
ATOM   2133  N   VAL A 280      30.594  16.209 -15.129  1.00 12.83           N
ATOM   2134  CA  VAL A 280      31.046  14.961 -14.518  1.00 11.41           C
ATOM   2135  C   VAL A 280      30.348  13.749 -15.145  1.00 14.13           C
ATOM   2136  O   VAL A 280      31.000  12.762 -15.502  1.00 17.09           O
ATOM   2137  CB  VAL A 280      30.783  14.965 -12.997  1.00  8.82           C
ATOM   2138  CG1 VAL A 280      31.131  13.617 -12.391  1.00  5.97           C
ATOM   2139  CG2 VAL A 280      31.586  16.073 -12.331  1.00  8.56           C
ATOM   2140  N   LEU A 281      29.026  13.818 -15.272  1.00 15.77           N
ATOM   2141  CA  LEU A 281      28.279  12.714 -15.875  1.00 17.83           C
ATOM   2142  C   LEU A 281      28.671  12.555 -17.346  1.00 16.27           C
ATOM   2143  O   LEU A 281      28.929  11.443 -17.810  1.00 15.07           O
ATOM   2144  CB  LEU A 281      26.767  12.931 -15.748  1.00 18.35           C
ATOM   2145  CG  LEU A 281      26.173  12.886 -14.340  1.00 21.20           C
ATOM   2146  CD1 LEU A 281      24.665  13.009 -14.429  1.00 20.58           C
ATOM   2147  CD2 LEU A 281      26.544  11.583 -13.653  1.00 23.10           C
ATOM   2148  N   ASN A 282      28.757  13.672 -18.065  1.00 16.22           N
ATOM   2149  CA  ASN A 282      29.138  13.628 -19.472  1.00 19.10           C
ATOM   2150  C   ASN A 282      30.540  13.054 -19.639  1.00 20.08           C
ATOM   2151  O   ASN A 282      30.824  12.370 -20.619  1.00 20.36           O
ATOM   2152  CB  ASN A 282      29.046  15.011 -20.122  1.00 15.34           C
ATOM   2153  CG  ASN A 282      27.649  15.325 -20.625  1.00 11.78           C
ATOM   2154  OD1 ASN A 282      26.895  14.428 -20.979  1.00 17.65           O
ATOM   2155  ND2 ASN A 282      27.298  16.602 -20.652  1.00  9.38           N
ATOM   2156  N   GLN A 283      31.399  13.284 -18.652  1.00 22.15           N
ATOM   2157  CA  GLN A 283      32.757  12.765 -18.706  1.00 22.90           C
ATOM   2158  C   GLN A 283      32.734  11.242 -18.620  1.00 23.32           C
ATOM   2159  O   GLN A 283      33.442  10.555 -19.357  1.00 23.75           O
ATOM   2160  CB  GLN A 283      33.601  13.351 -17.571  1.00 18.34           C
ATOM   2161  CG  GLN A 283      35.092  13.098 -17.720  1.00 29.09           C
ATOM   2162  CD  GLN A 283      35.632  13.569 -19.064  1.00 45.84           C
ATOM   2163  OE1 GLN A 283      35.667  14.770 -19.356  1.00 39.22           O
ATOM   2164  NE2 GLN A 283      36.055  12.619 -19.893  1.00 28.24           N
ATOM   2165  N   GLN A 284      31.918  10.720 -17.713  1.00 23.02           N
ATOM   2166  CA  GLN A 284      31.802   9.274 -17.535  1.00 23.38           C
ATOM   2167  C   GLN A 284      31.243   8.630 -18.799  1.00 24.54           C
ATOM   2168  O   GLN A 284      31.619   7.505 -19.145  1.00 29.24           O
ATOM   2169  CB  GLN A 284      30.921   8.933 -16.330  1.00 19.16           C
ATOM   2170  CG  GLN A 284      31.515   9.355 -14.982  1.00 34.00           C
ATOM   2171  CD  GLN A 284      32.845   8.688 -14.689  1.00 47.88           C
ATOM   2172  OE1 GLN A 284      33.862   9.359 -14.491  1.00 54.21           O
ATOM   2173  NE2 GLN A 284      32.842   7.361 -14.638  1.00 59.17           N
ATOM   2174  N   LEU A 285      30.361   9.351 -19.490  1.00 21.53           N
ATOM   2175  CA  LEU A 285      29.770   8.872 -20.734  1.00 18.31           C
ATOM   2176  C   LEU A 285      30.847   8.838 -21.810  1.00 20.78           C
ATOM   2177  O   LEU A 285      30.982   7.853 -22.534  1.00 19.68           O
ATOM   2178  CB  LEU A 285      28.619   9.785 -21.162  1.00 16.78           C
ATOM   2179  CG  LEU A 285      27.400   9.803 -20.234  1.00 17.83           C
ATOM   2180  CD1 LEU A 285      26.366  10.768 -20.771  1.00 11.61           C
ATOM   2181  CD2 LEU A 285      26.807   8.395 -20.078  1.00 21.20           C
ATOM   2182  N   THR A 286      31.618   9.918 -21.896  1.00 24.25           N
ATOM   2183  CA  THR A 286      32.707  10.028 -22.861  1.00 16.33           C
ATOM   2184  C   THR A 286      33.730   8.926 -22.610  1.00 19.16           C
ATOM   2185  O   THR A 286      34.195   8.278 -23.547  1.00 22.60           O
ATOM   2186  CB  THR A 286      33.395  11.402 -22.745  1.00 21.40           C
ATOM   2187  OG1 THR A 286      32.461  12.433 -23.077  1.00 28.88           O
ATOM   2188  CG2 THR A 286      34.588  11.492 -23.675  1.00 22.76           C
ATOM   2189  N   ASN A 287      34.049   8.691 -21.340  1.00 19.84           N
ATOM   2190  CA  ASN A 287      35.013   7.657 -20.970  1.00 19.95           C
ATOM   2191  C   ASN A 287      34.567   6.290 -21.458  1.00 22.74           C
ATOM   2192  O   ASN A 287      35.392   5.494 -21.920  1.00 22.50           O
ATOM   2193  CB  ASN A 287      35.229   7.622 -19.463  1.00 18.97           C
ATOM   2194  CG  ASN A 287      36.151   8.725 -18.989  1.00 32.10           C
ATOM   2195  OD1 ASN A 287      36.556   9.594 -19.768  1.00 32.49           O
ATOM   2196  ND2 ASN A 287      36.486   8.701 -17.717  1.00 37.25           N
ATOM   2197  N   HIS A 288      33.264   6.019 -21.372  1.00 21.02           N
ATOM   2198  CA  HIS A 288      32.727   4.740 -21.830  1.00 22.39           C
ATOM   2199  C   HIS A 288      32.888   4.655 -23.342  1.00 20.05           C
ATOM   2200  O   HIS A 288      33.348   3.647 -23.866  1.00 20.06           O
ATOM   2201  CB  HIS A 288      31.248   4.596 -21.449  1.00 25.12           C
ATOM   2202  CG  HIS A 288      30.606   3.354 -21.982  1.00 28.66           C
ATOM   2203  ND1 HIS A 288      30.680   2.142 -21.331  1.00 29.85           N
ATOM   2204  CD2 HIS A 288      29.905   3.131 -23.118  1.00 30.43           C
ATOM   2205  CE1 HIS A 288      30.054   1.223 -22.045  1.00 30.66           C
ATOM   2206  NE2 HIS A 288      29.575   1.798 -23.134  1.00 31.06           N
ATOM   2207  N   ILE A 289      32.532   5.731 -24.037  1.00 19.48           N
ATOM   2208  CA  ILE A 289      32.640   5.771 -25.491  1.00 18.90           C
ATOM   2209  C   ILE A 289      34.068   5.471 -25.937  1.00 20.22           C
ATOM   2210  O   ILE A 289      34.313   4.503 -26.667  1.00 21.50           O
ATOM   2211  CB  ILE A 289      32.184   7.136 -26.045  1.00 18.06           C
ATOM   2212  CG1 ILE A 289      30.664   7.276 -25.875  1.00 13.77           C
ATOM   2213  CG2 ILE A 289      32.611   7.298 -27.507  1.00 18.75           C
ATOM   2214  CD1 ILE A 289      30.094   8.578 -26.382  1.00  7.34           C
ATOM   2215  N   ARG A 290      35.015   6.259 -25.443  1.00 18.69           N
ATOM   2216  CA  ARG A 290      36.409   6.076 -25.805  1.00 18.51           C
ATOM   2217  C   ARG A 290      36.979   4.738 -25.358  1.00 24.85           C
ATOM   2218  O   ARG A 290      37.882   4.206 -26.002  1.00 27.99           O
ATOM   2219  CB  ARG A 290      37.252   7.244 -25.294  1.00 18.34           C
ATOM   2220  CG  ARG A 290      36.882   8.552 -25.973  1.00 19.15           C
ATOM   2221  CD  ARG A 290      37.961   9.611 -25.854  1.00 40.17           C
ATOM   2222  NE  ARG A 290      37.895  10.542 -26.982  1.00 41.53           N
ATOM   2223  CZ  ARG A 290      37.160  11.650 -27.006  1.00 30.85           C
ATOM   2224  NH1 ARG A 290      36.426  11.990 -25.960  1.00 49.65           N
ATOM   2225  NH2 ARG A 290      37.135  12.408 -28.090  1.00 36.44           N
ATOM   2226  N   ASP A 291      36.431   4.169 -24.288  1.00 26.60           N
ATOM   2227  CA  ASP A 291      36.916   2.880 -23.809  1.00 30.39           C
ATOM   2228  C   ASP A 291      36.376   1.739 -24.672  1.00 30.11           C
ATOM   2229  O   ASP A 291      37.038   0.713 -24.849  1.00 28.61           O
ATOM   2230  CB  ASP A 291      36.527   2.659 -22.344  1.00 38.31           C
ATOM   2231  CG  ASP A 291      37.152   1.402 -21.759  1.00 56.83           C
ATOM   2232  OD1 ASP A 291      38.384   1.392 -21.550  1.00 60.80           O
ATOM   2233  OD2 ASP A 291      36.416   0.419 -21.520  1.00 61.46           O
ATOM   2234  N   THR A 292      35.186   1.940 -25.229  1.00 29.38           N
ATOM   2235  CA  THR A 292      34.531   0.939 -26.065  1.00 26.41           C
ATOM   2236  C   THR A 292      34.967   0.965 -27.538  1.00 23.45           C
ATOM   2237  O   THR A 292      34.942  -0.068 -28.209  1.00 23.59           O
ATOM   2238  CB  THR A 292      32.983   1.083 -25.969  1.00 29.81           C
ATOM   2239  OG1 THR A 292      32.585   1.036 -24.591  1.00 33.06           O
ATOM   2240  CG2 THR A 292      32.272  -0.041 -26.717  1.00 25.49           C
ATOM   2241  N   LEU A 293      35.407   2.123 -28.025  1.00 21.96           N
ATOM   2242  CA  LEU A 293      35.818   2.261 -29.424  1.00 22.46           C
ATOM   2243  C   LEU A 293      36.959   1.391 -29.966  1.00 25.31           C
ATOM   2244  O   LEU A 293      36.865   0.892 -31.089  1.00 25.41           O
ATOM   2245  CB  LEU A 293      36.081   3.726 -29.782  1.00 21.06           C
ATOM   2246  CG  LEU A 293      34.870   4.645 -29.918  1.00 20.54           C
ATOM   2247  CD1 LEU A 293      35.319   5.970 -30.510  1.00 20.03           C
ATOM   2248  CD2 LEU A 293      33.816   4.003 -30.808  1.00 23.83           C
ATOM   2249  N   PRO A 294      38.056   1.215 -29.204  1.00 25.53           N
ATOM   2250  CA  PRO A 294      39.162   0.386 -29.703  1.00 25.90           C
ATOM   2251  C   PRO A 294      38.716  -1.014 -30.137  1.00 25.99           C
ATOM   2252  O   PRO A 294      39.135  -1.514 -31.188  1.00 25.73           O
ATOM   2253  CB  PRO A 294      40.108   0.329 -28.503  1.00 26.72           C
ATOM   2254  CG  PRO A 294      39.897   1.656 -27.851  1.00 25.16           C
ATOM   2255  CD  PRO A 294      38.390   1.780 -27.884  1.00 25.00           C
ATOM   2256  N   GLY A 295      37.851  -1.630 -29.341  1.00 24.40           N
ATOM   2257  CA  GLY A 295      37.365  -2.959 -29.667  1.00 25.38           C
ATOM   2258  C   GLY A 295      36.591  -2.978 -30.970  1.00 27.28           C
ATOM   2259  O   GLY A 295      36.764  -3.880 -31.790  1.00 24.86           O
ATOM   2260  N   LEU A 296      35.741  -1.972 -31.162  1.00 30.75           N
ATOM   2261  CA  LEU A 296      34.930  -1.862 -32.371  1.00 31.47           C
ATOM   2262  C   LEU A 296      35.792  -1.527 -33.581  1.00 30.82           C
ATOM   2263  O   LEU A 296      35.632  -2.114 -34.647  1.00 30.89           O
ATOM   2264  CB  LEU A 296      33.838  -0.800 -32.197  1.00 32.83           C
ATOM   2265  CG  LEU A 296      32.577  -1.181 -31.411  1.00 36.59           C
ATOM   2266  CD1 LEU A 296      31.835  -2.293 -32.138  1.00 37.74           C
ATOM   2267  CD2 LEU A 296      32.923  -1.609 -30.000  1.00 39.74           C
ATOM   2268  N   ARG A 297      36.706  -0.581 -33.396  1.00 30.08           N
ATOM   2269  CA  ARG A 297      37.619  -0.145 -34.442  1.00 29.59           C
ATOM   2270  C   ARG A 297      38.337  -1.344 -35.032  1.00 28.85           C
ATOM   2271  O   ARG A 297      38.334  -1.546 -36.243  1.00 28.44           O
ATOM   2272  CB  ARG A 297      38.650   0.824 -33.857  1.00 37.69           C
ATOM   2273  CG  ARG A 297      39.861   1.085 -34.744  1.00 49.14           C
ATOM   2274  CD  ARG A 297      41.050   1.563 -33.916  1.00 67.86           C
ATOM   2275  NE  ARG A 297      41.345   0.657 -32.804  1.00 79.73           N
ATOM   2276  CZ  ARG A 297      41.817  -0.581 -32.936  1.00 88.41           C
ATOM   2277  NH1 ARG A 297      42.063  -1.087 -34.139  1.00 86.57           N
ATOM   2278  NH2 ARG A 297      42.018  -1.329 -31.859  1.00 90.85           N
ATOM   2279  N   ASN A 298      38.941  -2.145 -34.163  1.00 31.54           N
ATOM   2280  CA  ASN A 298      39.676  -3.319 -34.602  1.00 32.28           C
ATOM   2281  C   ASN A 298      38.765  -4.297 -35.335  1.00 31.65           C
ATOM   2282  O   ASN A 298      39.122  -4.794 -36.403  1.00 33.09           O
ATOM   2283  CB  ASN A 298      40.358  -4.002 -33.416  1.00 49.33           C
ATOM   2284  CG  ASN A 298      41.462  -4.947 -33.848  1.00 65.43           C
ATOM   2285  OD1 ASN A 298      42.211  -4.662 -34.784  1.00 56.42           O
ATOM   2286  ND2 ASN A 298      41.579  -6.071 -33.157  1.00 73.66           N
ATOM   2287  N   LYS A 299      37.571  -4.526 -34.792  1.00 29.44           N
ATOM   2288  CA  LYS A 299      36.615  -5.442 -35.413  1.00 31.05           C
ATOM   2289  C   LYS A 299      36.275  -4.969 -36.830  1.00 33.44           C
ATOM   2290  O   LYS A 299      36.283  -5.759 -37.779  1.00 36.07           O
ATOM   2291  CB  LYS A 299      35.345  -5.556 -34.557  1.00 33.36           C
ATOM   2292  CG  LYS A 299      34.377  -6.663 -34.981  1.00 45.91           C
ATOM   2293  CD  LYS A 299      33.457  -6.226 -36.119  1.00 59.23           C
ATOM   2294  CE  LYS A 299      32.716  -7.405 -36.736  1.00 61.39           C
ATOM   2295  NZ  LYS A 299      31.823  -8.098 -35.768  1.00 46.68           N
ATOM   2296  N   LEU A 300      36.000  -3.675 -36.972  1.00 31.65           N
ATOM   2297  CA  LEU A 300      35.672  -3.102 -38.271  1.00 30.23           C
ATOM   2298  C   LEU A 300      36.854  -3.222 -39.229  1.00 27.49           C
ATOM   2299  O   LEU A 300      36.666  -3.459 -40.420  1.00 25.55           O
ATOM   2300  CB  LEU A 300      35.257  -1.636 -38.128  1.00 31.47           C
ATOM   2301  CG  LEU A 300      33.929  -1.344 -37.421  1.00 35.93           C
ATOM   2302  CD1 LEU A 300      33.748   0.158 -37.279  1.00 36.74           C
ATOM   2303  CD2 LEU A 300      32.772  -1.950 -38.192  1.00 34.56           C
ATOM   2304  N   GLN A 301      38.067  -3.061 -38.704  1.00 26.29           N
ATOM   2305  CA  GLN A 301      39.279  -3.168 -39.513  1.00 29.59           C
ATOM   2306  C   GLN A 301      39.400  -4.578 -40.081  1.00 28.29           C
ATOM   2307  O   GLN A 301      39.728  -4.756 -41.256  1.00 25.97           O
ATOM   2308  CB  GLN A 301      40.524  -2.838 -38.679  1.00 43.55           C
ATOM   2309  CG  GLN A 301      40.675  -1.366 -38.305  1.00 55.92           C
ATOM   2310  CD  GLN A 301      41.451  -0.558 -39.333  1.00 51.21           C
ATOM   2311  OE1 GLN A 301      42.410   0.134 -38.990  1.00 47.50           O
ATOM   2312  NE2 GLN A 301      41.037  -0.632 -40.592  1.00 47.56           N
ATOM   2313  N   SER A 302      39.113  -5.569 -39.243  1.00 29.60           N
ATOM   2314  CA  SER A 302      39.178  -6.969 -39.639  1.00 35.06           C
ATOM   2315  C   SER A 302      38.153  -7.264 -40.731  1.00 38.60           C
ATOM   2316  O   SER A 302      38.451  -7.959 -41.702  1.00 41.17           O
ATOM   2317  CB  SER A 302      38.907  -7.868 -38.430  1.00 40.14           C
ATOM   2318  OG  SER A 302      39.726  -7.514 -37.328  1.00 44.82           O
ATOM   2319  N   GLN A 303      36.948  -6.729 -40.569  1.00 39.03           N
ATOM   2320  CA  GLN A 303      35.883  -6.938 -41.542  1.00 40.91           C
ATOM   2321  C   GLN A 303      36.241  -6.256 -42.861  1.00 41.84           C
ATOM   2322  O   GLN A 303      36.040  -6.819 -43.939  1.00 41.11           O
ATOM   2323  CB  GLN A 303      34.562  -6.400 -40.993  1.00 43.98           C
ATOM   2324  CG  GLN A 303      33.325  -6.888 -41.727  1.00 51.07           C
ATOM   2325  CD  GLN A 303      32.035  -6.475 -41.038  1.00 62.45           C
ATOM   2326  OE1 GLN A 303      32.043  -6.006 -39.899  1.00 68.14           O
ATOM   2327  NE2 GLN A 303      30.917  -6.656 -41.726  1.00 63.77           N
ATOM   2328  N   LEU A 304      36.809  -5.057 -42.765  1.00 42.86           N
ATOM   2329  CA  LEU A 304      37.205  -4.300 -43.944  1.00 43.82           C
ATOM   2330  C   LEU A 304      38.285  -5.038 -44.729  1.00 48.52           C
ATOM   2331  O   LEU A 304      38.115  -5.297 -45.919  1.00 52.20           O
ATOM   2332  CB  LEU A 304      37.709  -2.908 -43.551  1.00 41.02           C
ATOM   2333  CG  LEU A 304      38.212  -2.022 -44.693  1.00 37.80           C
ATOM   2334  CD1 LEU A 304      37.068  -1.661 -45.627  1.00 36.92           C
ATOM   2335  CD2 LEU A 304      38.858  -0.771 -44.133  1.00 38.21           C
ATOM   2336  N   LEU A 305      39.375  -5.399 -44.051  1.00 51.02           N
ATOM   2337  CA  LEU A 305      40.499  -6.101 -44.673  1.00 52.46           C
ATOM   2338  C   LEU A 305      40.115  -7.205 -45.649  1.00 53.90           C
ATOM   2339  O   LEU A 305      40.703  -7.313 -46.726  1.00 55.22           O
ATOM   2340  CB  LEU A 305      41.447  -6.666 -43.611  1.00 52.27           C
ATOM   2341  CG  LEU A 305      42.539  -5.725 -43.099  1.00 52.92           C
ATOM   2342  CD1 LEU A 305      43.401  -6.443 -42.072  1.00 52.41           C
ATOM   2343  CD2 LEU A 305      43.393  -5.251 -44.266  1.00 55.00           C
ATOM   2344  N   SER A 306      39.132  -8.018 -45.275  1.00 55.00           N
ATOM   2345  CA  SER A 306      38.674  -9.109 -46.126  1.00 56.74           C
ATOM   2346  C   SER A 306      38.277  -8.576 -47.501  1.00 59.82           C
ATOM   2347  O   SER A 306      38.832  -8.983 -48.525  1.00 60.41           O
ATOM   2348  CB  SER A 306      37.481  -9.813 -45.477  1.00 56.12           C
ATOM   2349  OG  SER A 306      37.782 -10.199 -44.146  1.00 50.83           O
ATOM   2350  N   ILE A 307      37.345  -7.629 -47.506  1.00 61.35           N
ATOM   2351  CA  ILE A 307      36.852  -7.023 -48.736  1.00 62.45           C
ATOM   2352  C   ILE A 307      37.926  -6.166 -49.411  1.00 62.56           C
ATOM   2353  O   ILE A 307      38.056  -6.168 -50.635  1.00 62.16           O
ATOM   2354  CB  ILE A 307      35.592  -6.150 -48.460  1.00 63.74           C
ATOM   2355  CG1 ILE A 307      34.387  -7.033 -48.115  1.00 66.34           C
ATOM   2356  CG2 ILE A 307      35.262  -5.278 -49.666  1.00 64.73           C
ATOM   2357  CD1 ILE A 307      34.434  -7.674 -46.743  1.00 71.52           C
ATOM   2358  N   GLU A 308      38.722  -5.476 -48.602  1.00 63.34           N
ATOM   2359  CA  GLU A 308      39.768  -4.596 -49.106  1.00 64.09           C
ATOM   2360  C   GLU A 308      40.841  -5.305 -49.927  1.00 66.45           C
ATOM   2361  O   GLU A 308      41.195  -4.842 -51.009  1.00 67.02           O
ATOM   2362  CB  GLU A 308      40.397  -3.813 -47.953  1.00 58.70           C
ATOM   2363  CG  GLU A 308      41.285  -2.670 -48.397  1.00 40.20           C
ATOM   2364  CD  GLU A 308      41.323  -1.541 -47.387  1.00 46.96           C
ATOM   2365  OE1 GLU A 308      41.631  -1.801 -46.204  1.00 44.23           O
ATOM   2366  OE2 GLU A 308      41.034  -0.391 -47.780  1.00 38.24           O
ATOM   2367  N   LYS A 309      41.360  -6.420 -49.419  1.00 69.09           N
ATOM   2368  CA  LYS A 309      42.384  -7.177 -50.138  1.00 71.22           C
ATOM   2369  C   LYS A 309      41.759  -7.808 -51.383  1.00 72.81           C
ATOM   2370  O   LYS A 309      42.430  -8.022 -52.395  1.00 73.17           O
ATOM   2371  CB  LYS A 309      42.968  -8.273 -49.242  1.00 74.93           C
ATOM   2372  CG  LYS A 309      44.148  -9.017 -49.857  1.00 83.20           C
ATOM   2373  CD  LYS A 309      44.470 -10.309 -49.112  1.00 88.77           C
ATOM   2374  CE  LYS A 309      43.529 -11.452 -49.499  1.00 89.94           C
ATOM   2375  NZ  LYS A 309      42.106 -11.228 -49.110  1.00 88.19           N
ATOM   2376  N   GLU A 310      40.465  -8.095 -51.290  1.00 73.21           N
ATOM   2377  CA  GLU A 310      39.706  -8.704 -52.374  1.00 73.26           C
ATOM   2378  C   GLU A 310      39.253  -7.675 -53.413  1.00 73.26           C
ATOM   2379  O   GLU A 310      38.820  -8.043 -54.506  1.00 74.61           O
ATOM   2380  CB  GLU A 310      38.489  -9.424 -51.786  1.00 75.71           C
ATOM   2381  CG  GLU A 310      37.615 -10.156 -52.788  1.00 76.48           C
ATOM   2382  CD  GLU A 310      36.338 -10.670 -52.161  1.00 70.83           C
ATOM   2383  OE1 GLU A 310      35.352  -9.903 -52.110  1.00 66.62           O
ATOM   2384  OE2 GLU A 310      36.322 -11.836 -51.713  1.00 71.77           O
ATOM   2385  N   VAL A 311      39.372  -6.392 -53.077  1.00 72.34           N
ATOM   2386  CA  VAL A 311      38.959  -5.305 -53.967  1.00 72.22           C
ATOM   2387  C   VAL A 311      39.418  -5.511 -55.414  1.00 73.25           C
ATOM   2388  O   VAL A 311      38.929  -4.849 -56.335  1.00 74.16           O
ATOM   2389  CB  VAL A 311      39.476  -3.934 -53.455  1.00 71.54           C
ATOM   2390  CG1 VAL A 311      40.937  -3.727 -53.848  1.00 71.48           C
ATOM   2391  CG2 VAL A 311      38.598  -2.805 -53.971  1.00 71.36           C
ATOM   2392  N   ASP A 726      29.781 -10.363 -54.971  1.00 72.72           N
ATOM   2393  CA  ASP A 726      28.330 -10.278 -54.855  1.00 72.61           C
ATOM   2394  C   ASP A 726      27.830  -8.864 -55.136  1.00 72.69           C
ATOM   2395  O   ASP A 726      26.671  -8.544 -54.871  1.00 73.34           O
ATOM   2396  CB  ASP A 726      27.882 -10.718 -53.459  1.00 70.99           C
ATOM   2397  CG  ASP A 726      28.145 -12.190 -53.198  1.00 65.85           C
ATOM   2398  OD1 ASP A 726      29.316 -12.556 -52.957  1.00 63.06           O
ATOM   2399  OD2 ASP A 726      27.178 -12.979 -53.236  1.00 61.91           O
ATOM   2400  N   GLU A 727      28.723  -8.019 -55.648  1.00 71.33           N
ATOM   2401  CA  GLU A 727      28.401  -6.630 -55.972  1.00 71.03           C
ATOM   2402  C   GLU A 727      28.093  -5.784 -54.734  1.00 70.85           C
ATOM   2403  O   GLU A 727      27.789  -4.594 -54.845  1.00 70.78           O
ATOM   2404  CB  GLU A 727      27.232  -6.568 -56.964  1.00 71.75           C
ATOM   2405  CG  GLU A 727      27.608  -6.059 -58.347  1.00 69.94           C
ATOM   2406  CD  GLU A 727      27.818  -4.556 -58.382  1.00 68.90           C
ATOM   2407  OE1 GLU A 727      28.840  -4.074 -57.844  1.00 64.16           O
ATOM   2408  OE2 GLU A 727      26.954  -3.855 -58.949  1.00 66.56           O
ATOM   2409  N   MET A 728      28.220  -6.390 -53.558  1.00 70.21           N
ATOM   2410  CA  MET A 728      27.959  -5.714 -52.292  1.00 69.12           C
ATOM   2411  C   MET A 728      29.154  -4.829 -51.919  1.00 68.82           C
ATOM   2412  O   MET A 728      29.759  -4.991 -50.857  1.00 69.17           O
ATOM   2413  CB  MET A 728      27.698  -6.757 -51.196  1.00 68.77           C
ATOM   2414  CG  MET A 728      27.100  -6.204 -49.911  1.00 68.12           C
ATOM   2415  SD  MET A 728      25.416  -5.600 -50.122  1.00 67.45           S
ATOM   2416  CE  MET A 728      24.473  -7.060 -49.664  1.00 67.41           C
ATOM   2417  N   LEU A 729      29.477  -3.881 -52.793  1.00 68.03           N
ATOM   2418  CA  LEU A 729      30.595  -2.970 -52.573  1.00 67.43           C
ATOM   2419  C   LEU A 729      30.275  -1.948 -51.483  1.00 65.86           C
ATOM   2420  O   LEU A 729      31.174  -1.294 -50.950  1.00 66.47           O
ATOM   2421  CB  LEU A 729      30.953  -2.253 -53.879  1.00 68.50           C
ATOM   2422  CG  LEU A 729      32.219  -1.391 -53.903  1.00 70.81           C
ATOM   2423  CD1 LEU A 729      33.444  -2.247 -53.606  1.00 71.50           C
ATOM   2424  CD2 LEU A 729      32.355  -0.715 -55.259  1.00 71.69           C
ATOM   2425  N   ARG A 730      28.994  -1.824 -51.145  1.00 62.16           N
ATOM   2426  CA  ARG A 730      28.561  -0.887 -50.114  1.00 57.23           C
ATOM   2427  C   ARG A 730      29.279  -1.127 -48.793  1.00 51.74           C
ATOM   2428  O   ARG A 730      29.687  -0.175 -48.131  1.00 51.97           O
ATOM   2429  CB  ARG A 730      27.043  -0.950 -49.909  1.00 55.12           C
ATOM   2430  CG  ARG A 730      26.490  -2.345 -49.676  1.00 51.01           C
ATOM   2431  CD  ARG A 730      24.994  -2.312 -49.416  1.00 40.09           C
ATOM   2432  NE  ARG A 730      24.676  -2.021 -48.021  1.00 53.57           N
ATOM   2433  CZ  ARG A 730      24.632  -2.938 -47.058  1.00 65.86           C
ATOM   2434  NH1 ARG A 730      24.888  -4.212 -47.332  1.00 71.78           N
ATOM   2435  NH2 ARG A 730      24.319  -2.584 -45.819  1.00 61.65           N
ATOM   2436  N   MET A 731      29.470  -2.395 -48.435  1.00 48.97           N
ATOM   2437  CA  MET A 731      30.150  -2.739 -47.189  1.00 47.84           C
ATOM   2438  C   MET A 731      31.483  -2.015 -47.064  1.00 45.30           C
ATOM   2439  O   MET A 731      31.791  -1.455 -46.012  1.00 43.93           O
ATOM   2440  CB  MET A 731      30.352  -4.251 -47.073  1.00 48.26           C
ATOM   2441  CG  MET A 731      29.155  -4.993 -46.492  1.00 49.04           C
ATOM   2442  SD  MET A 731      28.820  -4.544 -44.771  1.00 49.57           S
ATOM   2443  CE  MET A 731      27.437  -3.448 -44.970  1.00 49.78           C
ATOM   2444  N   TYR A 732      32.237  -1.974 -48.158  1.00 41.64           N
ATOM   2445  CA  TYR A 732      33.530  -1.303 -48.173  1.00 40.26           C
ATOM   2446  C   TYR A 732      33.370   0.141 -47.698  1.00 37.75           C
ATOM   2447  O   TYR A 732      34.076   0.587 -46.794  1.00 37.62           O
ATOM   2448  CB  TYR A 732      34.122  -1.332 -49.590  1.00 40.57           C
ATOM   2449  CG  TYR A 732      35.444  -0.608 -49.742  1.00 41.44           C
ATOM   2450  CD1 TYR A 732      36.639  -1.200 -49.336  1.00 43.49           C
ATOM   2451  CD2 TYR A 732      35.501   0.669 -50.302  1.00 41.78           C
ATOM   2452  CE1 TYR A 732      37.860  -0.538 -49.485  1.00 45.78           C
ATOM   2453  CE2 TYR A 732      36.713   1.340 -50.455  1.00 42.39           C
ATOM   2454  CZ  TYR A 732      37.888   0.732 -50.047  1.00 43.06           C
ATOM   2455  OH  TYR A 732      39.089   1.389 -50.205  1.00 38.81           O
ATOM   2456  N   HIS A 733      32.399   0.840 -48.275  1.00 34.11           N
ATOM   2457  CA  HIS A 733      32.140   2.235 -47.940  1.00 32.99           C
ATOM   2458  C   HIS A 733      31.522   2.439 -46.561  1.00 32.94           C
ATOM   2459  O   HIS A 733      31.849   3.407 -45.872  1.00 36.72           O
ATOM   2460  CB  HIS A 733      31.267   2.881 -49.018  1.00 32.65           C
ATOM   2461  CG  HIS A 733      31.889   2.859 -50.378  1.00 31.57           C
ATOM   2462  ND1 HIS A 733      32.988   3.625 -50.704  1.00 30.90           N
ATOM   2463  CD2 HIS A 733      31.604   2.123 -51.478  1.00 31.05           C
ATOM   2464  CE1 HIS A 733      33.357   3.357 -51.944  1.00 30.82           C
ATOM   2465  NE2 HIS A 733      32.533   2.450 -52.436  1.00 31.02           N
ATOM   2466  N   ALA A 734      30.644   1.528 -46.154  1.00 26.33           N
ATOM   2467  CA  ALA A 734      29.993   1.620 -44.853  1.00 25.38           C
ATOM   2468  C   ALA A 734      31.038   1.501 -43.746  1.00 25.77           C
ATOM   2469  O   ALA A 734      31.098   2.334 -42.837  1.00 25.80           O
ATOM   2470  CB  ALA A 734      28.944   0.526 -44.707  1.00 24.89           C
ATOM   2471  N   LEU A 735      31.867   0.465 -43.843  1.00 25.42           N
ATOM   2472  CA  LEU A 735      32.924   0.211 -42.875  1.00 23.87           C
ATOM   2473  C   LEU A 735      33.890   1.383 -42.900  1.00 23.70           C
ATOM   2474  O   LEU A 735      34.238   1.936 -41.859  1.00 25.48           O
ATOM   2475  CB  LEU A 735      33.663  -1.081 -43.234  1.00 23.31           C
ATOM   2476  CG  LEU A 735      32.818  -2.358 -43.244  1.00 21.98           C
ATOM   2477  CD1 LEU A 735      33.533  -3.471 -43.987  1.00 18.03           C
ATOM   2478  CD2 LEU A 735      32.492  -2.773 -41.828  1.00 24.07           C
ATOM   2479  N   LYS A 736      34.281   1.782 -44.106  1.00 25.20           N
ATOM   2480  CA  LYS A 736      35.200   2.895 -44.308  1.00 24.34           C
ATOM   2481  C   LYS A 736      34.672   4.140 -43.600  1.00 23.27           C
ATOM   2482  O   LYS A 736      35.433   4.868 -42.962  1.00 20.30           O
ATOM   2483  CB  LYS A 736      35.350   3.178 -45.803  1.00 34.00           C
ATOM   2484  CG  LYS A 736      36.729   3.644 -46.228  1.00 33.71           C
ATOM   2485  CD  LYS A 736      37.733   2.509 -46.150  1.00 29.19           C
ATOM   2486  CE  LYS A 736      39.124   2.972 -46.545  1.00 39.83           C
ATOM   2487  NZ  LYS A 736      40.133   1.886 -46.401  1.00 42.99           N
ATOM   2488  N   GLU A 737      33.366   4.373 -43.713  1.00 25.06           N
ATOM   2489  CA  GLU A 737      32.724   5.521 -43.082  1.00 25.96           C
ATOM   2490  C   GLU A 737      32.831   5.446 -41.565  1.00 25.57           C
ATOM   2491  O   GLU A 737      33.300   6.389 -40.923  1.00 29.79           O
ATOM   2492  CB  GLU A 737      31.249   5.610 -43.488  1.00 32.09           C
ATOM   2493  CG  GLU A 737      30.944   6.711 -44.496  1.00 52.86           C
ATOM   2494  CD  GLU A 737      31.192   8.106 -43.939  1.00 72.33           C
ATOM   2495  OE1 GLU A 737      30.255   8.687 -43.348  1.00 67.81           O
ATOM   2496  OE2 GLU A 737      32.321   8.622 -44.092  1.00 77.22           O
ATOM   2497  N   ALA A 738      32.411   4.321 -40.998  1.00 20.36           N
ATOM   2498  CA  ALA A 738      32.459   4.123 -39.554  1.00 20.24           C
ATOM   2499  C   ALA A 738      33.867   4.365 -39.027  1.00 21.94           C
ATOM   2500  O   ALA A 738      34.054   5.093 -38.054  1.00 26.84           O
ATOM   2501  CB  ALA A 738      31.990   2.723 -39.192  1.00 19.72           C
ATOM   2502  N   LEU A 739      34.860   3.787 -39.696  1.00 22.39           N
ATOM   2503  CA  LEU A 739      36.254   3.953 -39.292  1.00 22.77           C
ATOM   2504  C   LEU A 739      36.690   5.414 -39.363  1.00 22.27           C
ATOM   2505  O   LEU A 739      37.440   5.887 -38.508  1.00 23.10           O
ATOM   2506  CB  LEU A 739      37.169   3.056 -40.135  1.00 22.47           C
ATOM   2507  CG  LEU A 739      37.061   1.559 -39.808  1.00 21.14           C
ATOM   2508  CD1 LEU A 739      37.800   0.719 -40.838  1.00 21.19           C
ATOM   2509  CD2 LEU A 739      37.613   1.303 -38.412  1.00 19.52           C
ATOM   2510  N   SER A 740      36.182   6.139 -40.354  1.00 21.77           N
ATOM   2511  CA  SER A 740      36.508   7.555 -40.504  1.00 25.42           C
ATOM   2512  C   SER A 740      35.931   8.345 -39.327  1.00 26.47           C
ATOM   2513  O   SER A 740      36.570   9.269 -38.814  1.00 27.05           O
ATOM   2514  CB  SER A 740      35.945   8.098 -41.822  1.00 27.97           C
ATOM   2515  OG  SER A 740      36.507   7.422 -42.934  1.00 36.22           O
ATOM   2516  N   ILE A 741      34.736   7.955 -38.886  1.00 23.90           N
ATOM   2517  CA  ILE A 741      34.076   8.622 -37.767  1.00 22.60           C
ATOM   2518  C   ILE A 741      34.860   8.375 -36.480  1.00 22.02           C
ATOM   2519  O   ILE A 741      35.143   9.307 -35.732  1.00 22.68           O
ATOM   2520  CB  ILE A 741      32.618   8.130 -37.569  1.00 21.77           C
ATOM   2521  CG1 ILE A 741      31.816   8.281 -38.866  1.00 20.71           C
ATOM   2522  CG2 ILE A 741      31.947   8.918 -36.446  1.00 18.21           C
ATOM   2523  CD1 ILE A 741      31.813   9.679 -39.417  1.00 26.36           C
ATOM   2524  N   ILE A 742      35.220   7.119 -36.237  1.00 22.37           N
ATOM   2525  CA  ILE A 742      35.982   6.755 -35.048  1.00 21.69           C
ATOM   2526  C   ILE A 742      37.263   7.570 -34.984  1.00 24.37           C
ATOM   2527  O   ILE A 742      37.595   8.123 -33.935  1.00 24.88           O
ATOM   2528  CB  ILE A 742      36.315   5.255 -35.030  1.00 18.61           C
ATOM   2529  CG1 ILE A 742      35.035   4.451 -34.798  1.00 11.08           C
ATOM   2530  CG2 ILE A 742      37.347   4.950 -33.951  1.00 20.40           C
ATOM   2531  CD1 ILE A 742      35.246   2.958 -34.758  1.00 18.51           C
ATOM   2532  N   GLY A 743      37.957   7.670 -36.117  1.00 25.76           N
ATOM   2533  CA  GLY A 743      39.186   8.441 -36.174  1.00 22.53           C
ATOM   2534  C   GLY A 743      38.927   9.883 -35.780  1.00 23.26           C
ATOM   2535  O   GLY A 743      39.697  10.479 -35.021  1.00 23.21           O
ATOM   2536  N   ASN A 744      37.822  10.440 -36.271  1.00 23.63           N
ATOM   2537  CA  ASN A 744      37.455  11.816 -35.951  1.00 28.71           C
ATOM   2538  C   ASN A 744      37.159  11.961 -34.467  1.00 30.61           C
ATOM   2539  O   ASN A 744      37.536  12.957 -33.850  1.00 33.30           O
ATOM   2540  CB  ASN A 744      36.249  12.275 -36.773  1.00 39.24           C
ATOM   2541  CG  ASN A 744      36.605  12.587 -38.216  1.00 46.32           C
ATOM   2542  OD1 ASN A 744      35.912  12.169 -39.141  1.00 56.38           O
ATOM   2543  ND2 ASN A 744      37.681  13.339 -38.414  1.00 41.11           N
ATOM   2544  N   ILE A 745      36.505  10.956 -33.891  1.00 29.27           N
ATOM   2545  CA  ILE A 745      36.176  10.971 -32.469  1.00 30.22           C
ATOM   2546  C   ILE A 745      37.458  10.940 -31.645  1.00 30.89           C
ATOM   2547  O   ILE A 745      37.599  11.696 -30.689  1.00 32.84           O
ATOM   2548  CB  ILE A 745      35.282   9.775 -32.074  1.00 28.73           C
ATOM   2549  CG1 ILE A 745      33.911   9.903 -32.744  1.00 24.15           C
ATOM   2550  CG2 ILE A 745      35.151   9.688 -30.553  1.00 23.92           C
ATOM   2551  CD1 ILE A 745      32.971   8.753 -32.452  1.00 18.60           C
ATOM   2552  N   ASN A 746      38.400  10.087 -32.039  1.00 30.99           N
ATOM   2553  CA  ASN A 746      39.680   9.975 -31.341  1.00 32.53           C
ATOM   2554  C   ASN A 746      40.441  11.301 -31.374  1.00 36.18           C
ATOM   2555  O   ASN A 746      41.325  11.541 -30.553  1.00 35.96           O
ATOM   2556  CB  ASN A 746      40.533   8.861 -31.953  1.00 28.85           C
ATOM   2557  CG  ASN A 746      40.083   7.465 -31.529  1.00 33.84           C
ATOM   2558  OD1 ASN A 746      40.279   6.492 -32.260  1.00 42.35           O
ATOM   2559  ND2 ASN A 746      39.506   7.357 -30.339  1.00 32.77           N
ATOM   2560  N   THR A 747      40.101  12.147 -32.342  1.00 39.11           N
ATOM   2561  CA  THR A 747      40.714  13.463 -32.490  1.00 42.04           C
ATOM   2562  C   THR A 747      39.835  14.494 -31.772  1.00 46.88           C
ATOM   2563  O   THR A 747      40.295  15.582 -31.420  1.00 46.87           O
ATOM   2564  CB  THR A 747      40.837  13.848 -33.986  1.00 45.61           C
ATOM   2565  OG1 THR A 747      41.571  12.834 -34.689  1.00 32.85           O
ATOM   2566  CG2 THR A 747      41.560  15.180 -34.144  1.00 49.46           C
ATOM   2567  N   THR A 748      38.572  14.127 -31.559  1.00 48.63           N
ATOM   2568  CA  THR A 748      37.577  14.970 -30.896  1.00 46.31           C
ATOM   2569  C   THR A 748      37.127  16.119 -31.798  1.00 44.16           C
ATOM   2570  O   THR A 748      36.098  16.031 -32.473  1.00 41.61           O
ATOM   2571  CB  THR A 748      38.103  15.548 -29.563  1.00 51.08           C
ATOM   2572  OG1 THR A 748      38.694  14.501 -28.780  1.00 51.78           O
ATOM   2573  CG2 THR A 748      36.961  16.175 -28.775  1.00 50.32           C
TER    2574      THR A 748
HETATM 2575  PG  GCP A1749       9.747  11.642  -5.139  1.00 10.94           P
HETATM 2576  O1G GCP A1749      10.749  10.930  -4.311  1.00  7.46           O
HETATM 2577  O2G GCP A1749       9.689  11.346  -6.591  1.00 13.17           O
HETATM 2578  O3G GCP A1749       8.344  11.696  -4.664  1.00  9.78           O
HETATM 2579  C3B GCP A1749      10.290  13.396  -5.131  1.00  8.52           C
HETATM 2580  PB  GCP A1749      11.964  13.719  -5.774  1.00  6.31           P
HETATM 2581  O1B GCP A1749      12.010  13.594  -7.240  1.00  8.93           O
HETATM 2582  O2B GCP A1749      12.805  12.836  -4.934  1.00  5.62           O
HETATM 2583  O3A GCP A1749      12.369  15.198  -5.332  1.00  6.08           O
HETATM 2584  PA  GCP A1749      11.628  16.356  -6.140  1.00  9.40           P
HETATM 2585  O1A GCP A1749      12.566  16.820  -7.185  1.00 12.42           O
HETATM 2586  O2A GCP A1749      10.255  15.958  -6.533  1.00 12.99           O
HETATM 2587  O5' GCP A1749      11.491  17.528  -5.079  1.00 10.15           O
HETATM 2588  C5' GCP A1749      10.995  17.247  -3.773  1.00  9.33           C
HETATM 2589  C4' GCP A1749      10.735  18.529  -3.024  1.00  8.00           C
HETATM 2590  O4' GCP A1749      11.991  19.090  -2.567  1.00  8.29           O
HETATM 2591  C3' GCP A1749      10.036  19.617  -3.826  1.00  7.58           C
HETATM 2592  O3' GCP A1749       9.134  20.317  -2.979  1.00  5.68           O
HETATM 2593  C2' GCP A1749      11.194  20.508  -4.275  1.00  9.59           C
HETATM 2594  O2' GCP A1749      10.783  21.849  -4.429  1.00 12.95           O
HETATM 2595  C1' GCP A1749      12.156  20.392  -3.094  1.00  8.41           C
HETATM 2596  N9  GCP A1749      13.568  20.545  -3.438  1.00  6.66           N
HETATM 2597  C8  GCP A1749      14.300  19.760  -4.297  1.00  6.89           C
HETATM 2598  N7  GCP A1749      15.561  20.097  -4.353  1.00  6.88           N
HETATM 2599  C5  GCP A1749      15.665  21.179  -3.491  1.00  7.00           C
HETATM 2600  C6  GCP A1749      16.792  21.962  -3.132  1.00  8.20           C
HETATM 2601  O6  GCP A1749      17.972  21.827  -3.486  1.00 10.22           O
HETATM 2602  N1  GCP A1749      16.446  22.983  -2.253  1.00  5.87           N
HETATM 2603  C2  GCP A1749      15.184  23.200  -1.751  1.00  7.18           C
HETATM 2604  N2  GCP A1749      15.046  24.229  -0.902  1.00  7.25           N
HETATM 2605  N3  GCP A1749      14.130  22.464  -2.058  1.00  7.58           N
HETATM 2606  C4  GCP A1749      14.439  21.481  -2.931  1.00  7.13           C
HETATM 2607 MG   MG  A1750      10.612  12.184  -8.148  1.00  5.01          Mg
HETATM 2608  O   HOH A1751       9.512  13.948  -8.136  1.00  4.68           O
HETATM 2609  O   HOH A1752      12.084  10.751  -8.409  1.00  3.52           O
HETATM 2610  O   HOH A2001      32.939  22.176 -23.230  1.00 17.54           O
HETATM 2611  O   HOH A2002      37.550  18.586 -26.632  1.00 52.68           O
HETATM 2612  O   HOH A2003      36.508  19.833 -28.952  1.00 43.38           O
HETATM 2613  O   HOH A2004      32.508  17.471 -34.877  1.00 32.18           O
HETATM 2614  O   HOH A2005      32.578  23.936 -34.022  1.00 28.04           O
HETATM 2615  O   HOH A2006      24.707  13.526 -36.767  1.00 23.01           O
HETATM 2616  O   HOH A2007      -2.309  16.617  -4.223  1.00 47.47           O
HETATM 2617  O   HOH A2008      -5.499  15.527  -6.800  1.00 35.80           O
HETATM 2618  O   HOH A2009      25.926   8.247 -40.318  1.00 34.12           O
HETATM 2619  O   HOH A2010       5.317  13.742   4.072  1.00 30.78           O
HETATM 2620  O   HOH A2011      28.306   3.059 -42.464  1.00 50.55           O
HETATM 2621  O   HOH A2012      21.531  -2.337 -39.070  1.00 37.63           O
HETATM 2622  O   HOH A2013       8.031  22.388 -14.282  1.00 14.70           O
HETATM 2623  O   HOH A2014      24.126  -1.002 -35.154  1.00 37.81           O
HETATM 2624  O   HOH A2015      29.732  -3.761 -36.693  1.00 29.54           O
HETATM 2625  O   HOH A2016      -1.925  13.606  -4.555  1.00 44.15           O
HETATM 2626  O   HOH A2017      -3.002  14.489  -6.880  1.00 27.87           O
HETATM 2627  O   HOH A2018      -0.813  16.627  -6.675  1.00 39.32           O
HETATM 2628  O   HOH A2019      23.875   2.673 -26.359  1.00 45.32           O
HETATM 2629  O   HOH A2020      27.034   0.550 -20.859  1.00 34.64           O
HETATM 2630  O   HOH A2021      25.659  -3.072 -26.533  1.00 29.57           O
HETATM 2631  O   HOH A2022      25.654  -4.151 -21.375  1.00 37.76           O
HETATM 2632  O   HOH A2023      22.027   5.041 -22.195  1.00 21.83           O
HETATM 2633  O   HOH A2024      18.679  31.029   0.147  1.00 30.32           O
HETATM 2634  O   HOH A2025      14.744   5.953  -5.761  1.00 10.94           O
HETATM 2635  O   HOH A2026      18.671   9.305  -0.056  1.00  4.69           O
HETATM 2636  O   HOH A2027      14.031  13.160   1.919  1.00 47.43           O
HETATM 2637  O   HOH A2028      12.682  11.690   3.932  1.00 49.57           O
HETATM 2638  O   HOH A2029       4.640   7.466   0.378  1.00 23.91           O
HETATM 2639  O   HOH A2030       7.949   6.861  -2.767  1.00 10.14           O
HETATM 2640  O   HOH A2031       4.220   9.942   1.470  1.00 18.33           O
HETATM 2641  O   HOH A2032       5.522  11.079   3.572  1.00 31.77           O
HETATM 2642  O   HOH A2033      13.817  16.196   2.120  1.00 15.72           O
HETATM 2643  O   HOH A2034       8.721  15.219  -2.224  1.00 14.21           O
HETATM 2644  O   HOH A2035      11.047  16.125   2.853  1.00 22.13           O
HETATM 2645  O   HOH A2036      17.346  18.480  -6.108  1.00 19.39           O
HETATM 2646  O   HOH A2037      14.793  21.170 -11.640  1.00  9.55           O
HETATM 2647  O   HOH A2038      13.154  21.564  -7.510  1.00  9.66           O
HETATM 2648  O   HOH A2039       1.262  -3.690 -12.066  1.00 30.57           O
HETATM 2649  O   HOH A2040      21.260  17.685 -12.130  1.00 11.55           O
HETATM 2650  O   HOH A2041      15.945  21.960 -16.076  1.00 27.17           O
HETATM 2651  O   HOH A2042       9.195  20.077 -14.004  1.00 11.88           O
HETATM 2652  O   HOH A2043      17.554  24.056 -10.853  1.00 15.07           O
HETATM 2653  O   HOH A2044      20.738  19.369  -9.987  1.00 22.13           O
HETATM 2654  O   HOH A2045       7.595  23.263 -17.851  1.00 31.74           O
HETATM 2655  O   HOH A2046      12.224  27.394 -16.863  1.00 44.88           O
HETATM 2656  O   HOH A2047       7.698  12.737 -11.242  1.00 27.54           O
HETATM 2657  O   HOH A2048       4.342  20.795  -6.984  1.00  5.59           O
HETATM 2658  O   HOH A2049       9.746  24.358 -11.425  1.00 11.52           O
HETATM 2659  O   HOH A2050      15.394  22.960  -9.758  1.00  2.01           O
HETATM 2660  O   HOH A2051       3.021  17.322  -4.304  1.00 17.40           O
HETATM 2661  O   HOH A2052       3.835  19.936  -4.434  1.00 22.43           O
HETATM 2662  O   HOH A2053       2.166  14.502  -2.828  1.00 33.84           O
HETATM 2663  O   HOH A2054       2.575  21.612  -2.690  1.00 20.61           O
HETATM 2664  O   HOH A2055       3.411  21.928  -0.184  1.00 20.53           O
HETATM 2665  O   HOH A2056       2.409  12.263   0.668  1.00  1.46           O
HETATM 2666  O   HOH A2057       0.811  12.245  -5.414  1.00 29.02           O
HETATM 2667  O   HOH A2058       3.079  12.868  -9.994  1.00 23.11           O
HETATM 2668  O   HOH A2059       5.145  12.070 -11.653  1.00 14.08           O
HETATM 2669  O   HOH A2060       8.043   8.605  -4.765  1.00 10.24           O
HETATM 2670  O   HOH A2061       5.049   9.213 -11.694  1.00  8.71           O
HETATM 2671  O   HOH A2062      -1.252  10.495  -5.090  1.00 13.05           O
HETATM 2672  O   HOH A2063       0.389  13.797  -7.585  1.00 18.95           O
HETATM 2673  O   HOH A2064       7.318   8.826 -13.050  1.00  9.95           O
HETATM 2674  O   HOH A2065      22.396  18.814  11.816  1.00 23.51           O
HETATM 2675  O   HOH A2066      27.216  13.800   9.724  1.00 26.19           O
HETATM 2676  O   HOH A2067      15.656  -4.338   6.801  1.00 32.64           O
HETATM 2677  O   HOH A2068      23.604  15.438 -34.446  1.00 31.19           O
HETATM 2678  O   HOH A2069      15.862  13.321 -37.390  1.00 36.56           O
HETATM 2679  O   HOH A2070       8.541  16.790 -36.733  1.00 34.67           O
HETATM 2680  O   HOH A2071      18.258  28.716  -4.490  1.00 17.28           O
HETATM 2681  O   HOH A2072       8.764  10.099 -34.051  1.00 27.44           O
HETATM 2682  O   HOH A2073      17.333  27.782   9.748  1.00 16.10           O
HETATM 2683  O   HOH A2074       7.748   7.210 -27.693  1.00 29.43           O
HETATM 2684  O   HOH A2075       7.716   6.004 -32.609  1.00 32.37           O
HETATM 2685  O   HOH A2076       2.993  10.874 -27.529  1.00 22.65           O
HETATM 2686  O   HOH A2077      41.819  15.722  -1.654  1.00 31.06           O
HETATM 2687  O   HOH A2078       4.590   5.821 -22.352  1.00 20.56           O
HETATM 2688  O   HOH A2079      -0.925   4.681 -27.792  1.00 31.11           O
HETATM 2689  O   HOH A2080      -2.841   6.208 -35.009  1.00 23.14           O
HETATM 2690  O   HOH A2081      16.158  29.889  -0.691  1.00 43.39           O
HETATM 2691  O   HOH A2082      -0.722  24.599  -7.641  1.00 32.85           O
HETATM 2692  O   HOH A2083       4.549  29.651   0.311  1.00 35.06           O
HETATM 2693  O   HOH A2084       2.340  19.950 -26.858  1.00 11.18           O
HETATM 2694  O   HOH A2085       0.912  24.866 -25.531  1.00 30.14           O
HETATM 2695  O   HOH A2086      27.287  26.433 -10.527  1.00 28.31           O
HETATM 2696  O   HOH A2087      25.186  33.329 -13.152  1.00 59.81           O
HETATM 2697  O   HOH A2088      23.027  33.017  -1.719  1.00 25.39           O
HETATM 2698  O   HOH A2089      -3.867  19.217 -21.727  1.00 29.47           O
HETATM 2699  O   HOH A2090      22.602  31.810   0.638  1.00 34.87           O
HETATM 2700  O   HOH A2091       0.103  20.186 -12.099  1.00 30.07           O
HETATM 2701  O   HOH A2092      39.095  30.686  -2.082  1.00 26.07           O
HETATM 2702  O   HOH A2093      37.963  31.494   2.865  1.00 37.64           O
HETATM 2703  O   HOH A2094      -2.031  16.467 -15.218  1.00 25.22           O
HETATM 2704  O   HOH A2095      -4.011  12.301 -20.331  1.00 30.29           O
HETATM 2705  O   HOH A2096      -2.684   9.182 -19.634  1.00 24.04           O
HETATM 2706  O   HOH A2097      36.199  21.433 -14.669  1.00 24.60           O
HETATM 2707  O   HOH A2098      -1.869  14.701  -9.272  1.00 31.15           O
HETATM 2708  O   HOH A2099      -5.699  11.243 -15.245  1.00 19.28           O
HETATM 2709  O   HOH A2100      -5.334   5.728 -21.460  1.00 36.06           O
HETATM 2710  O   HOH A2101      -3.937   5.959  -4.990  1.00 21.14           O
HETATM 2711  O   HOH A2102      -6.425   5.229   2.319  1.00 29.68           O
HETATM 2712  O   HOH A2103       0.665   1.006  -4.124  1.00 18.39           O
HETATM 2713  O   HOH A2104       0.314  -1.323  -7.992  1.00 36.69           O
HETATM 2714  O   HOH A2105      -0.256  -1.097 -10.887  1.00 37.40           O
HETATM 2715  O   HOH A2106      -0.373  -0.968 -13.543  1.00 43.65           O
HETATM 2716  O   HOH A2107       4.209   3.351 -20.869  1.00 52.26           O
HETATM 2717  O   HOH A2108       8.666   5.555 -25.795  1.00 28.19           O
HETATM 2718  O   HOH A2109      24.207  19.141 -32.666  1.00 23.08           O
HETATM 2719  O   HOH A2110      22.746  13.963 -24.009  1.00 21.79           O
HETATM 2720  O   HOH A2111       8.751  11.161 -13.196  1.00  3.97           O
HETATM 2721  O   HOH A2112      11.925   1.671  -0.320  1.00  3.78           O
HETATM 2722  O   HOH A2113       5.296   5.238   1.861  1.00 19.73           O
HETATM 2723  O   HOH A2114       6.247  -0.134   8.093  1.00 30.63           O
HETATM 2724  O   HOH A2115       8.545  -1.338   5.493  1.00 16.31           O
HETATM 2725  O   HOH A2116      14.051   1.370   1.584  1.00 15.19           O
HETATM 2726  O   HOH A2117      -2.478   7.164   5.405  1.00 26.53           O
HETATM 2727  O   HOH A2118      -5.416  -0.585   0.980  1.00 22.03           O
HETATM 2728  O   HOH A2119      -1.090  -1.084   3.880  1.00 35.99           O
HETATM 2729  O   HOH A2120       6.758  -1.534   3.413  1.00 24.73           O
HETATM 2730  O   HOH A2121       7.841  -3.466  -7.626  1.00 19.14           O
HETATM 2731  O   HOH A2122       1.294  -1.607  -5.106  1.00 16.75           O
HETATM 2732  O   HOH A2123      13.848  -6.528  -8.325  1.00 40.01           O
HETATM 2733  O   HOH A2124      14.923  -6.687  -5.504  1.00 32.12           O
HETATM 2734  O   HOH A2125       9.060  -4.182  -9.896  1.00 28.97           O
HETATM 2735  O   HOH A2126      28.796  -2.803 -14.232  1.00 25.29           O
HETATM 2736  O   HOH A2127      22.360  17.511   8.145  1.00 21.12           O
HETATM 2737  O   HOH A2128      24.747  17.043   4.728  1.00 26.83           O
HETATM 2738  O   HOH A2129      15.934  15.917   8.331  1.00 12.04           O
HETATM 2739  O   HOH A2130      18.026  19.162   9.923  1.00 16.43           O
HETATM 2740  O   HOH A2131      17.576  16.119  10.405  1.00 25.65           O
HETATM 2741  O   HOH A2132      20.319  16.841   9.877  1.00 33.49           O
HETATM 2742  O   HOH A2133      15.488  15.841   4.268  1.00  8.23           O
HETATM 2743  O   HOH A2134      13.457  19.025   3.060  1.00 22.82           O
HETATM 2744  O   HOH A2135      15.750  21.787   6.509  1.00  3.28           O
HETATM 2745  O   HOH A2136      23.945  14.530   4.140  1.00 35.61           O
HETATM 2746  O   HOH A2137      20.531  11.273   4.270  1.00 25.91           O
HETATM 2747  O   HOH A2138      23.260  16.421  12.389  1.00 33.75           O
HETATM 2748  O   HOH A2139      26.194  11.270   8.929  1.00 21.09           O
HETATM 2749  O   HOH A2140      25.875  14.310   7.287  1.00 30.07           O
HETATM 2750  O   HOH A2141      18.471   6.412   9.328  1.00 11.61           O
HETATM 2751  O   HOH A2142      24.649  -0.948   2.040  1.00 34.19           O
HETATM 2752  O   HOH A2143      18.005  -3.430   5.648  1.00 23.17           O
HETATM 2753  O   HOH A2144      28.595   2.808  -4.421  1.00 20.14           O
HETATM 2754  O   HOH A2145      30.599  -0.292   0.072  1.00 40.80           O
HETATM 2755  O   HOH A2146      30.744   2.538  -2.320  1.00 22.88           O
HETATM 2756  O   HOH A2147      29.959  -1.908 -10.366  1.00 36.04           O
HETATM 2757  O   HOH A2148      31.459  -2.397  -7.284  1.00 26.83           O
HETATM 2758  O   HOH A2149      32.783   4.266  -3.466  1.00 13.73           O
HETATM 2759  O   HOH A2150      31.773   6.554  -6.297  1.00 17.41           O
HETATM 2760  O   HOH A2151      37.723   3.383 -11.371  1.00 33.66           O
HETATM 2761  O   HOH A2152      12.463  20.318   0.597  1.00 24.12           O
HETATM 2762  O   HOH A2153      24.650  24.585   3.555  1.00  9.12           O
HETATM 2763  O   HOH A2154      16.531  26.950  -3.368  1.00  8.38           O
HETATM 2764  O   HOH A2155      22.575  26.809   6.901  1.00 15.91           O
HETATM 2765  O   HOH A2156      19.972  20.491   8.582  1.00  9.36           O
HETATM 2766  O   HOH A2157      18.161  27.091  12.261  1.00  8.92           O
HETATM 2767  O   HOH A2158      21.477  20.784  13.504  1.00  9.11           O
HETATM 2768  O   HOH A2159      18.685  28.981  14.345  1.00 15.45           O
HETATM 2769  O   HOH A2160      28.313  24.476  14.853  1.00 25.51           O
HETATM 2770  O   HOH A2161      28.341  21.403  13.741  1.00 32.53           O
HETATM 2771  O   HOH A2162      24.908  25.888   5.992  1.00 11.00           O
HETATM 2772  O   HOH A2163      22.503  20.016   9.260  1.00 26.04           O
HETATM 2773  O   HOH A2164      28.173  20.956  10.745  1.00 15.91           O
HETATM 2774  O   HOH A2165      29.379  17.509   7.045  1.00 25.26           O
HETATM 2775  O   HOH A2166      26.510  17.292   6.772  1.00 25.50           O
HETATM 2776  O   HOH A2167      31.081  19.635   7.475  1.00  9.52           O
HETATM 2777  O   HOH A2168      33.032  23.184   8.163  1.00 36.56           O
HETATM 2778  O   HOH A2169      33.557  25.896   7.296  1.00 18.99           O
HETATM 2779  O   HOH A2170      38.023  27.686   5.666  1.00 20.72           O
HETATM 2780  O   HOH A2171      39.431  22.315   2.940  1.00 29.51           O
HETATM 2781  O   HOH A2172      31.778  12.272   2.075  1.00  8.98           O
HETATM 2782  O   HOH A2173      38.856  14.990  -1.550  1.00 28.66           O
HETATM 2783  O   HOH A2174      33.805   7.306   6.668  1.00 24.40           O
HETATM 2784  O   HOH A2175      41.809   1.265  -5.260  1.00 32.88           O
HETATM 2785  O   HOH A2176      33.520  14.229  -9.052  1.00 34.23           O
HETATM 2786  O   HOH A2177      36.541  10.570 -11.115  1.00 27.41           O
HETATM 2787  O   HOH A2178      36.873   9.353 -13.933  1.00 17.03           O
HETATM 2788  O   HOH A2179      35.807   5.030 -14.067  1.00 41.82           O
HETATM 2789  O   HOH A2180      32.730  17.555  -6.806  1.00 36.25           O
HETATM 2790  O   HOH A2181      20.322  24.347  -9.690  1.00 24.81           O
HETATM 2791  O   HOH A2182      18.542  27.161  -6.616  1.00 14.74           O
HETATM 2792  O   HOH A2183      14.701  29.175  -2.960  1.00 20.15           O
HETATM 2793  O   HOH A2184      12.570  29.270  -1.173  1.00 14.98           O
HETATM 2794  O   HOH A2185       4.723  31.177  -4.796  1.00 34.29           O
HETATM 2795  O   HOH A2186       9.339  31.992  -6.259  1.00 36.08           O
HETATM 2796  O   HOH A2187      14.021  31.625  -4.545  1.00 32.46           O
HETATM 2797  O   HOH A2188      15.965  28.660  -6.965  1.00 10.20           O
HETATM 2798  O   HOH A2189       2.694  30.984  -6.755  1.00 29.82           O
HETATM 2799  O   HOH A2190       2.378  24.270  -7.818  1.00 31.41           O
HETATM 2800  O   HOH A2191       4.065  29.249  -2.447  1.00 19.62           O
HETATM 2801  O   HOH A2192      16.666  30.904  -4.572  1.00 22.52           O
HETATM 2802  O   HOH A2193      16.823  33.936  -7.936  1.00 33.01           O
HETATM 2803  O   HOH A2194      15.362  29.883 -17.866  1.00 22.22           O
HETATM 2804  O   HOH A2195      16.044  34.256 -15.377  1.00 40.79           O
HETATM 2805  O   HOH A2196      24.580  27.067 -10.831  1.00  5.84           O
HETATM 2806  O   HOH A2197      25.064  33.639 -10.203  1.00 40.29           O
HETATM 2807  O   HOH A2198      21.449  31.618  -3.378  1.00 14.56           O
HETATM 2808  O   HOH A2199      29.547  29.033  -8.469  1.00 54.93           O
HETATM 2809  O   HOH A2200      28.728  37.123  -9.969  1.00 22.31           O
HETATM 2810  O   HOH A2201      19.760  35.484  -2.218  1.00 27.78           O
HETATM 2811  O   HOH A2202      21.238  37.873  -5.711  1.00 38.52           O
HETATM 2812  O   HOH A2203      25.656  31.381   0.580  1.00 28.00           O
HETATM 2813  O   HOH A2204      40.413   5.805 -42.135  1.00 43.56           O
HETATM 2814  O   HOH A2205      35.673  28.132   1.867  1.00 11.92           O
HETATM 2815  O   HOH A2206      35.725  29.458   5.829  1.00 44.69           O
HETATM 2816  O   HOH A2207      35.249  30.931  -5.183  1.00 23.37           O
HETATM 2817  O   HOH A2208      37.569  30.811   0.092  1.00 36.29           O
HETATM 2818  O   HOH A2209      29.147  26.340  -8.310  1.00 12.74           O
HETATM 2819  O   HOH A2210      36.183  21.675 -11.890  1.00 29.12           O
HETATM 2820  O   HOH A2211      38.452  21.173 -10.022  1.00 40.37           O
HETATM 2821  O   HOH A2212      38.800  20.691  -1.226  1.00 36.50           O
HETATM 2822  O   HOH A2213      28.528  24.200 -11.439  1.00  9.56           O
HETATM 2823  O   HOH A2214      23.246  17.836 -14.017  1.00 14.49           O
HETATM 2824  O   HOH A2215      35.191   6.488 -16.216  1.00 28.59           O
HETATM 2825  O   HOH A2216      38.785   9.268 -21.487  1.00 28.01           O
HETATM 2826  O   HOH A2217      39.437  10.401 -18.581  1.00 31.25           O
HETATM 2827  O   HOH A2218      33.878   2.591 -19.754  1.00 33.61           O
HETATM 2828  O   HOH A2219      31.047   2.698 -18.718  1.00 33.02           O
HETATM 2829  O   HOH A2220      40.457   8.356 -27.290  1.00 36.28           O
HETATM 2830  O   HOH A2221      37.393  -1.494 -26.640  1.00 20.58           O
HETATM 2831  O   HOH A2222      34.871  -2.585 -26.750  1.00 27.96           O
HETATM 2832  O   HOH A2223      41.756  -2.288 -42.606  1.00 38.12           O
HETATM 2833  O   HOH A2224      44.199  -2.205 -45.284  1.00 33.54           O
HETATM 2834  O   HOH A2225      39.083  -1.919 -57.959  1.00 29.38           O
HETATM 2835  O   HOH A2226      38.208   4.808 -43.481  1.00 27.47           O
HETATM 2836  O   HOH A2227       9.848  20.967  -0.528  1.00  9.64           O
CONECT  296 2607
CONECT  447 2607
CONECT 2595 2590 2593 2596
CONECT 2603 2604 2605 2602
CONECT 2593 2595 2594 2591
CONECT 2591 2593 2589 2592
CONECT 2579 2580 2575
CONECT 2606 2596 2605 2599
CONECT 2589 2590 2588 2591
CONECT 2599 2598 2606 2600
CONECT 2588 2587 2589
CONECT 2600 2599 2601 2602
CONECT 2597 2596 2598
CONECT 2602 2603 2600
CONECT 2604 2603
CONECT 2605 2606 2603
CONECT 2598 2597 2599
CONECT 2596 2595 2597 2606
CONECT 2585 2584
CONECT 2581 2580
CONECT 2581 2607
CONECT 2576 2575
CONECT 2594 2593
CONECT 2586 2584
CONECT 2582 2580
CONECT 2577 2575
CONECT 2577 2607
CONECT 2592 2591
CONECT 2583 2580 2584
CONECT 2578 2575
CONECT 2590 2595 2589
CONECT 2587 2584 2588
CONECT 2601 2600
CONECT 2584 2585 2583 2586 2587
CONECT 2580 2579 2583 2581 2582
CONECT 2575 2579 2578 2576 2577
CONECT 2607 2577  296  447 2581
CONECT 2607 2608 2609
CONECT 2608 2607
CONECT 2609 2607
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.