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***  OXIDOREDUCTASE 10-MAR-99 1CET  ***

elNémo ID: 2209191907479779

Job options:

ID        	=	 2209191907479779
JOBID     	=	 OXIDOREDUCTASE 10-MAR-99 1CET
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    OXIDOREDUCTASE                          10-MAR-99   1CET              
TITLE     CHLOROQUINE BINDS IN THE COFACTOR BINDING SITE OF PLASMODIUM          
TITLE    2 FALCIPARUM LACTATE DEHYDROGENASE.                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (L-LACTATE DEHYDROGENASE);                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.1.1.27;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM;                     
SOURCE   4 ORGANISM_TAXID: 5833;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PKK223-3                                  
KEYWDS    OXIDOREDUCTASE, TRICARBOXYLIC ACID CYCLE, INHIBITOR                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.READ,K.W.WILKINSON,R.TRANTER,R.B.SESSIONS,R.L.BRADY               
REVDAT   5   13-JUL-11 1CET    1       VERSN                                    
REVDAT   4   24-FEB-09 1CET    1       VERSN                                    
REVDAT   3   12-OCT-04 1CET    1       REMARK SCALE1 SCALE2 SCALE3              
REVDAT   3 2                   1       MASTER                                   
REVDAT   2   21-JUN-00 1CET    3       JRNL   REMARK COMPND HETATM              
REVDAT   1   19-MAR-99 1CET    0                                                
JRNL        AUTH   J.A.READ,K.W.WILKINSON,R.TRANTER,R.B.SESSIONS,R.L.BRADY      
JRNL        TITL   CHLOROQUINE BINDS IN THE COFACTOR BINDING SITE OF PLASMODIUM 
JRNL        TITL 2 FALCIPARUM LACTATE DEHYDROGENASE.                            
JRNL        REF    J.BIOL.CHEM.                  V. 274 10213 1999              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10187806                                                     
JRNL        DOI    10.1074/JBC.274.15.10213                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.R.DUNN,M.J.BANFIELD,J.J.BARKER,C.W.HIGHAM,K.M.MORETON,     
REMARK   1  AUTH 2 D.TURGUT-BALIK,R.L.BRADY,J.J.HOLBROOK                        
REMARK   1  TITL   THE STRUCTURE OF LACTATE DEHYDROGENASE FROM PLASMODIUM       
REMARK   1  TITL 2 FALCIPARUM REVEALS A NEW TARGET FOR ANTI-MALARIAL DESIGN     
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   3   912 1996              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 20.000                         
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 2.0500                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20115                          
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) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2305                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 252                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.10                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 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) : 0.02                            
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  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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000612.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX7.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20155                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1LDG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       39.96500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.72000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       46.09500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       39.96500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.72000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       46.09500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       39.96500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       42.72000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.09500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       39.96500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       42.72000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       46.09500            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 16970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       79.93000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       85.44000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       79.93000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       85.44000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    17                                                      
REMARK 465     LYS A   101A                                                     
REMARK 465     ALA A   101B                                                     
REMARK 465     PRO A   101C                                                     
REMARK 465     GLY A   101D                                                     
REMARK 465     LYS A   101E                                                     
REMARK 465     SER A   101F                                                     
REMARK 465     ASP A   101G                                                     
REMARK 465     LYS A   101H                                                     
REMARK 465     GLU A   101I                                                     
REMARK 465     TRP A   101J                                                     
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A  19   C     LYS A  20   N      -0.158                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  57      -32.61     64.63                                   
REMARK 500    ASP A  87        3.19    -65.82                                   
REMARK 500    HIS A 243       47.37     70.40                                   
REMARK 500    TYR A 247      -22.20   -149.95                                   
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 A1183        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A1196        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH A1252        DISTANCE = 10.97 ANGSTROMS                       
REMARK 525    HOH A1253        DISTANCE = 11.87 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLQ A 1001                
DBREF  1CET A   17   329  UNP    Q27743   LDH1_PLAFD       1    316             
SEQADV 1CET SER A   91  UNP  Q27743    ALA    73 CONFLICT                       
SEQRES   1 A  316  MET ALA PRO LYS ALA LYS ILE VAL LEU VAL GLY SER GLY          
SEQRES   2 A  316  MET ILE GLY GLY VAL MET ALA THR LEU ILE VAL GLN LYS          
SEQRES   3 A  316  ASN LEU GLY ASP VAL VAL LEU PHE ASP ILE VAL LYS ASN          
SEQRES   4 A  316  MET PRO HIS GLY LYS ALA LEU ASP THR SER HIS THR ASN          
SEQRES   5 A  316  VAL MET ALA TYR SER ASN CYS LYS VAL SER GLY SER ASN          
SEQRES   6 A  316  THR TYR ASP ASP LEU ALA GLY SER ASP VAL VAL ILE VAL          
SEQRES   7 A  316  THR ALA GLY PHE THR LYS ALA PRO GLY LYS SER ASP LYS          
SEQRES   8 A  316  GLU TRP ASN ARG LEU ASP LEU LEU PRO LEU ASN ASN LYS          
SEQRES   9 A  316  ILE MET ILE GLU ILE GLY GLY HIS ILE LYS LYS ASN CYS          
SEQRES  10 A  316  PRO ASN ALA PHE ILE ILE VAL VAL THR ASN PRO VAL ASP          
SEQRES  11 A  316  VAL MET VAL GLN LEU LEU HIS GLN HIS SER GLY VAL PRO          
SEQRES  12 A  316  LYS ASN LYS ILE ILE GLY LEU GLY GLY VAL LEU ASP THR          
SEQRES  13 A  316  SER ARG LEU LYS TYR TYR ILE SER GLN LYS LEU ASN VAL          
SEQRES  14 A  316  CYS PRO ARG ASP VAL ASN ALA HIS ILE VAL GLY ALA HIS          
SEQRES  15 A  316  GLY ASN LYS MET VAL LEU LEU LYS ARG TYR ILE THR VAL          
SEQRES  16 A  316  GLY GLY ILE PRO LEU GLN GLU PHE ILE ASN ASN LYS LEU          
SEQRES  17 A  316  ILE SER ASP ALA GLU LEU GLU ALA ILE PHE ASP ARG THR          
SEQRES  18 A  316  VAL ASN THR ALA LEU GLU ILE VAL ASN LEU HIS ALA SER          
SEQRES  19 A  316  PRO TYR VAL ALA PRO ALA ALA ALA ILE ILE GLU MET ALA          
SEQRES  20 A  316  GLU SER TYR LEU LYS ASP LEU LYS LYS VAL LEU ILE CYS          
SEQRES  21 A  316  SER THR LEU LEU GLU GLY GLN TYR GLY HIS SER ASP ILE          
SEQRES  22 A  316  PHE GLY GLY THR PRO VAL VAL LEU GLY ALA ASN GLY VAL          
SEQRES  23 A  316  GLU GLN VAL ILE GLU LEU GLN LEU ASN SER GLU GLU LYS          
SEQRES  24 A  316  ALA LYS PHE ASP GLU ALA ILE ALA GLU THR LYS ARG MET          
SEQRES  25 A  316  LYS ALA LEU ALA                                              
HET    CLQ  A1001      22                                                       
HETNAM     CLQ N4-(7-CHLORO-QUINOLIN-4-YL)-N1,N1-DIETHYL-PENTANE-1,4-           
HETNAM   2 CLQ  DIAMINE                                                         
HETSYN     CLQ CHLOROQUINE                                                      
FORMUL   2  CLQ    C18 H26 CL N3                                                
FORMUL   3  HOH   *252(H2 O)                                                    
HELIX    1   1 MET A   30  GLN A   42  1                                  12    
HELIX    2   2 MET A   58  ALA A   73A 1                                  16    
HELIX    3   3 TYR A   85  LEU A   88  5                                   4    
HELIX    4   5 ARG A  109  ASN A  130  5                                  22    
HELIX    5   6 VAL A  142  SER A  153  1                                  12    
HELIX    6   7 LYS A  157  LYS A  159  5                                   3    
HELIX    7   8 GLY A  165  LEU A  180  1                                  16    
HELIX    8   9 PRO A  184  ASP A  186  5                                   3    
HELIX    9  10 LYS A  203  TYR A  205  5                                   3    
HELIX   10  11 LEU A  210A ASN A  214  1                                   6    
HELIX   11  12 ASP A  221  LEU A  242  1                                  21    
HELIX   12  13 VAL A  248  LEU A  262  1                                  15    
HELIX   13  14 GLN A  278  GLY A  280  5                                   3    
HELIX   14  15 SER A  309  LYS A  326  1                                  18    
SHEET    1   A 6 ILE A 160  GLY A 162  0                                        
SHEET    2   A 6 PHE A 134  VAL A 137  1  N  ILE A 135   O  ILE A 161           
SHEET    3   A 6 VAL A  93  VAL A  96  1  N  VAL A  94   O  PHE A 134           
SHEET    4   A 6 LYS A  22  VAL A  26  1  N  VAL A  24   O  VAL A  93           
SHEET    5   A 6 ASP A  47  PHE A  52  1  N  ASP A  47   O  ILE A  23           
SHEET    6   A 6 VAL A  78  SER A  81  1  N  SER A  79   O  VAL A  49           
SHEET    1   B 3 LYS A 267  GLU A 276  0                                        
SHEET    2   B 3 SER A 282  GLY A 294 -1  N  LEU A 293   O  LYS A 267           
SHEET    3   B 3 GLY A 297  VAL A 302 -1  N  GLN A 301   O  VAL A 292           
CISPEP   1 ASN A  140    PRO A  141          0         0.02                     
SITE     1 AC1  8 GLY A  27  PHE A  52  ILE A  54  TYR A  85                    
SITE     2 AC1  8 ALA A  98  ILE A 119  GLU A 122  HOH A1193                    
CRYST1   79.930   85.440   92.190  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012511  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011704  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010847        0.00000                         
ATOM      1  N   ALA A  18      48.727  38.163  22.344  1.00 41.44           N  
ATOM      2  CA  ALA A  18      48.171  39.053  21.271  1.00 40.56           C  
ATOM      3  C   ALA A  18      46.644  39.018  21.295  1.00 39.49           C  
ATOM      4  O   ALA A  18      46.060  37.976  21.603  1.00 40.54           O  
ATOM      5  CB  ALA A  18      48.677  38.605  19.895  1.00 40.19           C  
ATOM      6  N   PRO A  19      45.989  40.176  21.069  1.00 37.44           N  
ATOM      7  CA  PRO A  19      44.528  40.329  21.047  1.00 35.08           C  
ATOM      8  C   PRO A  19      43.883  39.770  19.766  1.00 31.03           C  
ATOM      9  O   PRO A  19      42.705  40.034  19.488  1.00 32.29           O  
ATOM     10  CB  PRO A  19      44.337  41.848  21.127  1.00 35.99           C  
ATOM     11  CG  PRO A  19      45.561  42.321  21.840  1.00 37.75           C  
ATOM     12  CD  PRO A  19      46.631  41.500  21.157  1.00 38.66           C  
ATOM     13  N   LYS A  20      44.660  39.125  19.159  1.00 19.18           N  
ATOM     14  CA  LYS A  20      44.206  38.348  17.968  1.00 17.48           C  
ATOM     15  C   LYS A  20      43.252  37.240  18.386  1.00 15.69           C  
ATOM     16  O   LYS A  20      43.528  36.488  19.319  1.00 14.33           O  
ATOM     17  CB  LYS A  20      45.404  37.729  17.248  1.00 21.40           C  
ATOM     18  CG  LYS A  20      45.561  38.182  15.807  1.00 23.94           C  
ATOM     19  CD  LYS A  20      46.428  37.224  15.002  1.00 27.15           C  
ATOM     20  CE  LYS A  20      47.800  37.031  15.636  1.00 29.39           C  
ATOM     21  NZ  LYS A  20      48.687  36.176  14.797  1.00 31.26           N  
ATOM     22  N   ALA A  21      42.127  37.140  17.688  1.00 12.39           N  
ATOM     23  CA  ALA A  21      41.146  36.116  17.992  1.00 10.92           C  
ATOM     24  C   ALA A  21      41.763  34.735  17.820  1.00 11.04           C  
ATOM     25  O   ALA A  21      42.673  34.548  17.012  1.00 10.13           O  
ATOM     26  CB  ALA A  21      39.949  36.263  17.070  1.00  9.85           C  
ATOM     27  N   LYS A  22      41.283  33.775  18.605  1.00 10.82           N  
ATOM     28  CA  LYS A  22      41.755  32.402  18.498  1.00 10.11           C  
ATOM     29  C   LYS A  22      40.553  31.579  18.060  1.00  8.81           C  
ATOM     30  O   LYS A  22      39.526  31.543  18.737  1.00  9.21           O  
ATOM     31  CB  LYS A  22      42.284  31.879  19.838  1.00  9.83           C  
ATOM     32  CG  LYS A  22      42.800  30.450  19.749  1.00  8.78           C  
ATOM     33  CD  LYS A  22      43.359  29.960  21.074  1.00  8.88           C  
ATOM     34  CE  LYS A  22      43.506  28.450  21.066  1.00  8.83           C  
ATOM     35  NZ  LYS A  22      44.339  27.968  22.192  1.00 10.14           N  
ATOM     36  N   ILE A  23      40.681  30.932  16.912  1.00  8.41           N  
ATOM     37  CA  ILE A  23      39.600  30.132  16.372  1.00  7.72           C  
ATOM     38  C   ILE A  23      39.998  28.676  16.405  1.00  6.71           C  
ATOM     39  O   ILE A  23      40.988  28.284  15.793  1.00  6.99           O  
ATOM     40  CB  ILE A  23      39.302  30.544  14.922  1.00  7.68           C  
ATOM     41  CG1 ILE A  23      38.956  32.035  14.878  1.00 10.10           C  
ATOM     42  CG2 ILE A  23      38.166  29.706  14.359  1.00  4.54           C  
ATOM     43  CD1 ILE A  23      39.367  32.727  13.590  1.00 12.97           C  
ATOM     44  N   VAL A  24      39.232  27.876  17.133  1.00  7.87           N  
ATOM     45  CA  VAL A  24      39.521  26.454  17.229  1.00  6.09           C  
ATOM     46  C   VAL A  24      38.499  25.684  16.427  1.00  6.65           C  
ATOM     47  O   VAL A  24      37.297  25.773  16.676  1.00  5.79           O  
ATOM     48  CB  VAL A  24      39.476  25.946  18.678  1.00  4.79           C  
ATOM     49  CG1 VAL A  24      39.686  24.431  18.701  1.00  4.68           C  
ATOM     50  CG2 VAL A  24      40.545  26.628  19.494  1.00  4.56           C  
ATOM     51  N   LEU A  25      38.997  24.934  15.451  1.00  8.20           N  
ATOM     52  CA  LEU A  25      38.156  24.121  14.593  1.00  7.67           C  
ATOM     53  C   LEU A  25      38.158  22.693  15.134  1.00  6.67           C  
ATOM     54  O   LEU A  25      39.107  21.940  14.927  1.00  6.83           O  
ATOM     55  CB  LEU A  25      38.688  24.163  13.154  1.00  6.10           C  
ATOM     56  CG  LEU A  25      38.956  25.572  12.593  1.00  9.02           C  
ATOM     57  CD1 LEU A  25      39.527  25.467  11.181  1.00  7.31           C  
ATOM     58  CD2 LEU A  25      37.661  26.395  12.586  1.00  6.09           C  
ATOM     59  N   VAL A  26      37.097  22.338  15.851  1.00  8.27           N  
ATOM     60  CA  VAL A  26      36.969  21.004  16.421  1.00  8.65           C  
ATOM     61  C   VAL A  26      36.478  20.074  15.315  1.00  9.75           C  
ATOM     62  O   VAL A  26      35.275  19.905  15.102  1.00 10.50           O  
ATOM     63  CB  VAL A  26      35.986  21.017  17.604  1.00  7.33           C  
ATOM     64  CG1 VAL A  26      35.727  19.608  18.096  1.00  9.15           C  
ATOM     65  CG2 VAL A  26      36.565  21.858  18.725  1.00  7.59           C  
ATOM     66  N   GLY A  27      37.445  19.479  14.620  1.00 10.73           N  
ATOM     67  CA  GLY A  27      37.178  18.602  13.494  1.00  9.76           C  
ATOM     68  C   GLY A  27      38.036  19.139  12.356  1.00  9.62           C  
ATOM     69  O   GLY A  27      37.849  20.274  11.909  1.00  8.63           O  
ATOM     70  N   SER A  28      38.984  18.336  11.887  1.00 10.01           N  
ATOM     71  CA  SER A  28      39.881  18.769  10.822  1.00 10.27           C  
ATOM     72  C   SER A  28      39.663  18.047   9.501  1.00 11.58           C  
ATOM     73  O   SER A  28      40.619  17.660   8.826  1.00 11.18           O  
ATOM     74  CB  SER A  28      41.328  18.596  11.278  1.00  9.73           C  
ATOM     75  OG  SER A  28      41.553  19.332  12.469  1.00  9.22           O  
ATOM     76  N   GLY A  29      38.397  17.878   9.135  1.00 12.13           N  
ATOM     77  CA  GLY A  29      38.074  17.208   7.892  1.00 12.42           C  
ATOM     78  C   GLY A  29      38.103  18.158   6.712  1.00 12.81           C  
ATOM     79  O   GLY A  29      38.881  19.116   6.689  1.00 11.38           O  
ATOM     80  N   MET A  30      37.251  17.891   5.728  1.00 13.76           N  
ATOM     81  CA  MET A  30      37.173  18.714   4.529  1.00 14.41           C  
ATOM     82  C   MET A  30      36.671  20.130   4.803  1.00 13.52           C  
ATOM     83  O   MET A  30      37.269  21.100   4.339  1.00 11.54           O  
ATOM     84  CB  MET A  30      36.277  18.041   3.489  1.00 16.74           C  
ATOM     85  CG  MET A  30      36.894  16.791   2.872  1.00 23.02           C  
ATOM     86  SD  MET A  30      38.664  16.986   2.511  1.00 32.32           S  
ATOM     87  CE  MET A  30      38.615  17.814   0.925  1.00 25.46           C  
ATOM     88  N   ILE A  31      35.576  20.259   5.548  1.00 11.90           N  
ATOM     89  CA  ILE A  31      35.048  21.587   5.850  1.00  9.83           C  
ATOM     90  C   ILE A  31      36.076  22.340   6.697  1.00  9.70           C  
ATOM     91  O   ILE A  31      36.301  23.530   6.498  1.00  8.69           O  
ATOM     92  CB  ILE A  31      33.695  21.513   6.612  1.00  9.36           C  
ATOM     93  CG1 ILE A  31      32.621  20.889   5.718  1.00 10.50           C  
ATOM     94  CG2 ILE A  31      33.241  22.912   7.025  1.00  7.03           C  
ATOM     95  CD1 ILE A  31      31.248  20.788   6.382  1.00 11.05           C  
ATOM     96  N   GLY A  32      36.708  21.635   7.631  1.00  7.96           N  
ATOM     97  CA  GLY A  32      37.709  22.264   8.477  1.00  8.39           C  
ATOM     98  C   GLY A  32      38.866  22.852   7.679  1.00  8.15           C  
ATOM     99  O   GLY A  32      39.349  23.946   7.980  1.00  6.92           O  
ATOM    100  N   GLY A  33      39.306  22.126   6.656  1.00  6.68           N  
ATOM    101  CA  GLY A  33      40.407  22.594   5.833  1.00  7.06           C  
ATOM    102  C   GLY A  33      40.125  23.898   5.112  1.00  6.65           C  
ATOM    103  O   GLY A  33      40.967  24.799   5.087  1.00  6.53           O  
ATOM    104  N   VAL A  35      38.942  24.005   4.517  1.00  4.99           N  
ATOM    105  CA  VAL A  35      38.575  25.218   3.797  1.00  5.32           C  
ATOM    106  C   VAL A  35      38.407  26.370   4.786  1.00  5.47           C  
ATOM    107  O   VAL A  35      38.768  27.504   4.497  1.00  6.06           O  
ATOM    108  CB  VAL A  35      37.267  25.028   2.996  1.00  5.16           C  
ATOM    109  CG1 VAL A  35      36.947  26.296   2.207  1.00  3.66           C  
ATOM    110  CG2 VAL A  35      37.399  23.837   2.057  1.00  3.09           C  
ATOM    111  N   MET A  36      37.861  26.084   5.958  1.00  6.25           N  
ATOM    112  CA  MET A  36      37.684  27.128   6.953  1.00  6.65           C  
ATOM    113  C   MET A  36      39.048  27.711   7.331  1.00  8.02           C  
ATOM    114  O   MET A  36      39.218  28.934   7.412  1.00  7.34           O  
ATOM    115  CB  MET A  36      36.988  26.563   8.192  1.00  6.29           C  
ATOM    116  CG  MET A  36      35.504  26.307   7.983  1.00  6.41           C  
ATOM    117  SD  MET A  36      34.643  26.038   9.529  1.00  6.73           S  
ATOM    118  CE  MET A  36      35.493  24.585  10.121  1.00  5.49           C  
ATOM    119  N   ALA A  37      40.021  26.831   7.553  1.00  7.19           N  
ATOM    120  CA  ALA A  37      41.362  27.269   7.916  1.00  5.89           C  
ATOM    121  C   ALA A  37      41.921  28.147   6.790  1.00  5.85           C  
ATOM    122  O   ALA A  37      42.445  29.235   7.030  1.00  5.69           O  
ATOM    123  CB  ALA A  37      42.265  26.053   8.152  1.00  4.47           C  
ATOM    124  N   THR A  38      41.794  27.671   5.558  1.00  6.97           N  
ATOM    125  CA  THR A  38      42.282  28.410   4.398  1.00  6.58           C  
ATOM    126  C   THR A  38      41.645  29.798   4.309  1.00  6.48           C  
ATOM    127  O   THR A  38      42.341  30.806   4.134  1.00  5.63           O  
ATOM    128  CB  THR A  38      41.983  27.635   3.090  1.00  7.55           C  
ATOM    129  OG1 THR A  38      42.572  26.332   3.165  1.00  7.29           O  
ATOM    130  CG2 THR A  38      42.546  28.372   1.876  1.00  8.41           C  
ATOM    131  N   LEU A  39      40.323  29.847   4.443  1.00  6.62           N  
ATOM    132  CA  LEU A  39      39.598  31.106   4.350  1.00  6.47           C  
ATOM    133  C   LEU A  39      39.936  32.056   5.493  1.00  8.19           C  
ATOM    134  O   LEU A  39      39.966  33.275   5.304  1.00  9.01           O  
ATOM    135  CB  LEU A  39      38.088  30.840   4.295  1.00  6.63           C  
ATOM    136  CG  LEU A  39      37.563  30.235   2.977  1.00  9.88           C  
ATOM    137  CD1 LEU A  39      36.044  30.056   3.049  1.00  6.96           C  
ATOM    138  CD2 LEU A  39      37.943  31.133   1.791  1.00  6.87           C  
ATOM    139  N   ILE A  40      40.205  31.511   6.673  1.00  4.00           N  
ATOM    140  CA  ILE A  40      40.553  32.358   7.805  1.00  5.57           C  
ATOM    141  C   ILE A  40      41.869  33.102   7.532  1.00  6.63           C  
ATOM    142  O   ILE A  40      41.978  34.309   7.782  1.00  6.69           O  
ATOM    143  CB  ILE A  40      40.657  31.524   9.098  1.00  6.43           C  
ATOM    144  CG1 ILE A  40      39.244  31.177   9.588  1.00  5.75           C  
ATOM    145  CG2 ILE A  40      41.400  32.300  10.170  1.00  6.32           C  
ATOM    146  CD1 ILE A  40      39.178  30.014  10.578  1.00  3.90           C  
ATOM    147  N   VAL A  41      42.865  32.394   7.010  1.00  6.67           N  
ATOM    148  CA  VAL A  41      44.145  33.024   6.694  1.00  6.54           C  
ATOM    149  C   VAL A  41      43.955  34.051   5.570  1.00  7.99           C  
ATOM    150  O   VAL A  41      44.504  35.153   5.624  1.00  6.30           O  
ATOM    151  CB  VAL A  41      45.196  31.983   6.243  1.00  7.34           C  
ATOM    152  CG1 VAL A  41      46.495  32.684   5.861  1.00  5.64           C  
ATOM    153  CG2 VAL A  41      45.447  30.977   7.361  1.00  5.84           C  
ATOM    154  N   GLN A  42      43.175  33.685   4.553  1.00  6.30           N  
ATOM    155  CA  GLN A  42      42.918  34.581   3.431  1.00  7.03           C  
ATOM    156  C   GLN A  42      42.371  35.905   3.944  1.00  7.22           C  
ATOM    157  O   GLN A  42      42.739  36.977   3.468  1.00  9.09           O  
ATOM    158  CB  GLN A  42      41.896  33.965   2.468  1.00  8.22           C  
ATOM    159  CG  GLN A  42      42.431  32.856   1.577  1.00  8.24           C  
ATOM    160  CD  GLN A  42      43.486  33.341   0.600  1.00 10.50           C  
ATOM    161  OE1 GLN A  42      43.245  34.252  -0.202  1.00  7.95           O  
ATOM    162  NE2 GLN A  42      44.668  32.731   0.662  1.00  9.24           N  
ATOM    163  N   LYS A  43      41.485  35.824   4.928  1.00  8.10           N  
ATOM    164  CA  LYS A  43      40.872  37.015   5.490  1.00  8.35           C  
ATOM    165  C   LYS A  43      41.593  37.529   6.727  1.00  9.29           C  
ATOM    166  O   LYS A  43      41.168  38.522   7.315  1.00 10.68           O  
ATOM    167  CB  LYS A  43      39.407  36.728   5.828  1.00  8.57           C  
ATOM    168  CG  LYS A  43      38.560  36.335   4.619  1.00  7.34           C  
ATOM    169  CD  LYS A  43      37.299  35.587   5.039  1.00  9.13           C  
ATOM    170  CE  LYS A  43      36.356  35.399   3.853  1.00  9.26           C  
ATOM    171  NZ  LYS A  43      35.843  36.711   3.378  1.00 13.54           N  
ATOM    172  N   ASN A  44      42.678  36.860   7.118  1.00  9.40           N  
ATOM    173  CA  ASN A  44      43.447  37.261   8.298  1.00 10.03           C  
ATOM    174  C   ASN A  44      42.507  37.433   9.503  1.00 11.28           C  
ATOM    175  O   ASN A  44      42.649  38.374  10.285  1.00 10.94           O  
ATOM    176  CB  ASN A  44      44.181  38.578   8.007  1.00  8.22           C  
ATOM    177  CG  ASN A  44      45.337  38.833   8.966  1.00 10.50           C  
ATOM    178  OD1 ASN A  44      46.123  37.934   9.272  1.00  9.36           O  
ATOM    179  ND2 ASN A  44      45.443  40.067   9.444  1.00 10.00           N  
ATOM    180  N   LEU A  45      41.557  36.511   9.649  1.00 11.48           N  
ATOM    181  CA  LEU A  45      40.563  36.561  10.726  1.00 11.43           C  
ATOM    182  C   LEU A  45      41.121  36.316  12.125  1.00 12.66           C  
ATOM    183  O   LEU A  45      40.619  36.869  13.110  1.00 10.20           O  
ATOM    184  CB  LEU A  45      39.443  35.550  10.447  1.00 12.79           C  
ATOM    185  CG  LEU A  45      38.021  36.056  10.174  1.00 15.84           C  
ATOM    186  CD1 LEU A  45      38.049  37.262   9.249  1.00 14.96           C  
ATOM    187  CD2 LEU A  45      37.202  34.929   9.553  1.00 13.69           C  
ATOM    188  N   GLY A  46      42.147  35.478  12.218  1.00 11.10           N  
ATOM    189  CA  GLY A  46      42.745  35.205  13.511  1.00 11.14           C  
ATOM    190  C   GLY A  46      43.544  33.922  13.518  1.00 10.52           C  
ATOM    191  O   GLY A  46      43.616  33.231  12.503  1.00 10.84           O  
ATOM    192  N   ASP A  47      44.148  33.602  14.659  1.00 10.75           N  
ATOM    193  CA  ASP A  47      44.928  32.375  14.792  1.00 10.81           C  
ATOM    194  C   ASP A  47      43.989  31.173  14.685  1.00 10.71           C  
ATOM    195  O   ASP A  47      42.866  31.207  15.191  1.00 10.20           O  
ATOM    196  CB  ASP A  47      45.649  32.353  16.137  1.00 12.16           C  
ATOM    197  CG  ASP A  47      46.782  33.360  16.206  1.00 14.82           C  
ATOM    198  OD1 ASP A  47      47.399  33.635  15.152  1.00 13.17           O  
ATOM    199  OD2 ASP A  47      47.056  33.875  17.314  1.00 12.92           O  
ATOM    200  N   VAL A  48      44.461  30.114  14.034  1.00 10.11           N  
ATOM    201  CA  VAL A  48      43.661  28.908  13.836  1.00  9.57           C  
ATOM    202  C   VAL A  48      44.268  27.640  14.437  1.00  9.17           C  
ATOM    203  O   VAL A  48      45.474  27.410  14.361  1.00  9.08           O  
ATOM    204  CB  VAL A  48      43.431  28.627  12.322  1.00 10.03           C  
ATOM    205  CG1 VAL A  48      42.564  27.394  12.143  1.00  8.14           C  
ATOM    206  CG2 VAL A  48      42.788  29.833  11.650  1.00 10.24           C  
ATOM    207  N   VAL A  49      43.412  26.827  15.045  1.00  8.40           N  
ATOM    208  CA  VAL A  49      43.831  25.553  15.598  1.00  6.51           C  
ATOM    209  C   VAL A  49      42.960  24.497  14.927  1.00  8.17           C  
ATOM    210  O   VAL A  49      41.724  24.558  14.988  1.00  6.89           O  
ATOM    211  CB  VAL A  49      43.618  25.459  17.123  1.00  5.59           C  
ATOM    212  CG1 VAL A  49      43.918  24.034  17.595  1.00  4.89           C  
ATOM    213  CG2 VAL A  49      44.517  26.444  17.841  1.00  5.82           C  
ATOM    214  N   LEU A  51      43.606  23.552  14.253  1.00  7.57           N  
ATOM    215  CA  LEU A  51      42.895  22.467  13.603  1.00  6.79           C  
ATOM    216  C   LEU A  51      42.990  21.299  14.577  1.00  6.48           C  
ATOM    217  O   LEU A  51      44.044  20.683  14.727  1.00  5.71           O  
ATOM    218  CB  LEU A  51      43.552  22.127  12.262  1.00  6.61           C  
ATOM    219  CG  LEU A  51      43.089  23.011  11.092  1.00  7.04           C  
ATOM    220  CD1 LEU A  51      44.183  23.126  10.048  1.00  5.25           C  
ATOM    221  CD2 LEU A  51      41.836  22.414  10.480  1.00  6.64           C  
ATOM    222  N   PHE A  52      41.887  21.019  15.263  1.00  7.03           N  
ATOM    223  CA  PHE A  52      41.866  19.943  16.241  1.00  7.70           C  
ATOM    224  C   PHE A  52      41.098  18.728  15.767  1.00  7.97           C  
ATOM    225  O   PHE A  52      40.088  18.842  15.081  1.00  9.33           O  
ATOM    226  CB  PHE A  52      41.251  20.424  17.560  1.00  7.11           C  
ATOM    227  CG  PHE A  52      40.930  19.303  18.522  1.00  8.81           C  
ATOM    228  CD1 PHE A  52      39.752  18.574  18.396  1.00 10.17           C  
ATOM    229  CD2 PHE A  52      41.821  18.962  19.536  1.00  7.92           C  
ATOM    230  CE1 PHE A  52      39.469  17.517  19.262  1.00  9.81           C  
ATOM    231  CE2 PHE A  52      41.552  17.914  20.403  1.00  8.53           C  
ATOM    232  CZ  PHE A  52      40.372  17.189  20.267  1.00 10.40           C  
ATOM    233  N   ASP A  53      41.596  17.560  16.146  1.00  7.77           N  
ATOM    234  CA  ASP A  53      40.951  16.305  15.816  1.00 10.96           C  
ATOM    235  C   ASP A  53      41.613  15.210  16.623  1.00 12.08           C  
ATOM    236  O   ASP A  53      42.676  15.415  17.202  1.00 13.56           O  
ATOM    237  CB  ASP A  53      41.055  15.991  14.325  1.00 10.76           C  
ATOM    238  CG  ASP A  53      39.853  15.210  13.820  1.00 11.79           C  
ATOM    239  OD1 ASP A  53      39.607  14.106  14.346  1.00 10.65           O  
ATOM    240  OD2 ASP A  53      39.150  15.701  12.911  1.00 11.59           O  
ATOM    241  N   ILE A  54      40.972  14.051  16.668  1.00 13.07           N  
ATOM    242  CA  ILE A  54      41.499  12.934  17.420  1.00 14.51           C  
ATOM    243  C   ILE A  54      42.385  12.076  16.544  1.00 15.84           C  
ATOM    244  O   ILE A  54      43.104  11.205  17.031  1.00 16.44           O  
ATOM    245  CB  ILE A  54      40.356  12.134  18.009  1.00 14.51           C  
ATOM    246  CG1 ILE A  54      39.544  11.462  16.897  1.00 14.31           C  
ATOM    247  CG2 ILE A  54      39.475  13.089  18.809  1.00 18.37           C  
ATOM    248  CD1 ILE A  54      38.744  10.252  17.360  1.00 16.90           C  
ATOM    249  N   VAL A  55      42.331  12.335  15.242  1.00 15.22           N  
ATOM    250  CA  VAL A  55      43.180  11.615  14.308  1.00 17.85           C  
ATOM    251  C   VAL A  55      44.592  12.150  14.542  1.00 19.27           C  
ATOM    252  O   VAL A  55      44.816  13.363  14.538  1.00 19.36           O  
ATOM    253  CB  VAL A  55      42.780  11.883  12.846  1.00 16.71           C  
ATOM    254  CG1 VAL A  55      43.668  11.073  11.913  1.00 14.68           C  
ATOM    255  CG2 VAL A  55      41.320  11.525  12.634  1.00 17.13           C  
ATOM    256  N   LYS A  56      45.543  11.250  14.756  1.00 20.13           N  
ATOM    257  CA  LYS A  56      46.916  11.657  15.012  1.00 22.18           C  
ATOM    258  C   LYS A  56      47.640  12.304  13.828  1.00 21.82           C  
ATOM    259  O   LYS A  56      47.575  11.807  12.701  1.00 23.37           O  
ATOM    260  CB  LYS A  56      47.730  10.457  15.495  1.00 25.22           C  
ATOM    261  CG  LYS A  56      49.129  10.811  15.984  1.00 32.59           C  
ATOM    262  CD  LYS A  56      49.865   9.580  16.490  1.00 38.99           C  
ATOM    263  CE  LYS A  56      51.264   9.927  16.973  1.00 43.29           C  
ATOM    264  NZ  LYS A  56      51.963   8.718  17.501  1.00 46.10           N  
ATOM    265  N   ASN A  57      48.309  13.421  14.111  1.00 20.95           N  
ATOM    266  CA  ASN A  57      49.126  14.167  13.142  1.00 19.72           C  
ATOM    267  C   ASN A  57      48.498  14.837  11.922  1.00 18.05           C  
ATOM    268  O   ASN A  57      48.992  15.875  11.467  1.00 15.27           O  
ATOM    269  CB  ASN A  57      50.275  13.273  12.678  1.00 19.59           C  
ATOM    270  CG  ASN A  57      51.294  13.025  13.772  1.00 23.49           C  
ATOM    271  OD1 ASN A  57      51.406  13.811  14.718  1.00 25.05           O  
ATOM    272  ND2 ASN A  57      52.040  11.935  13.654  1.00 21.49           N  
ATOM    273  N   MET A  58      47.437  14.252  11.376  1.00 17.05           N  
ATOM    274  CA  MET A  58      46.790  14.828  10.203  1.00 16.12           C  
ATOM    275  C   MET A  58      46.520  16.333  10.360  1.00 14.44           C  
ATOM    276  O   MET A  58      46.815  17.114   9.457  1.00 14.85           O  
ATOM    277  CB  MET A  58      45.492  14.076   9.897  1.00 15.07           C  
ATOM    278  CG  MET A  58      44.672  14.687   8.778  1.00 17.39           C  
ATOM    279  SD  MET A  58      43.479  15.852   9.431  1.00 18.43           S  
ATOM    280  CE  MET A  58      42.183  14.739   9.970  1.00 15.11           C  
ATOM    281  N   PRO A  59      45.955  16.758  11.506  1.00 14.94           N  
ATOM    282  CA  PRO A  59      45.686  18.193  11.696  1.00 13.26           C  
ATOM    283  C   PRO A  59      46.980  19.003  11.635  1.00 12.73           C  
ATOM    284  O   PRO A  59      46.984  20.153  11.197  1.00 11.26           O  
ATOM    285  CB  PRO A  59      45.037  18.274  13.081  1.00 13.03           C  
ATOM    286  CG  PRO A  59      44.618  16.891  13.407  1.00 14.44           C  
ATOM    287  CD  PRO A  59      45.533  15.959  12.669  1.00 13.35           C  
ATOM    288  N   HIS A  60      48.072  18.399  12.092  1.00 10.84           N  
ATOM    289  CA  HIS A  60      49.365  19.065  12.064  1.00 10.96           C  
ATOM    290  C   HIS A  60      49.805  19.212  10.613  1.00 10.16           C  
ATOM    291  O   HIS A  60      50.340  20.247  10.218  1.00  9.50           O  
ATOM    292  CB  HIS A  60      50.400  18.254  12.841  1.00 11.40           C  
ATOM    293  CG  HIS A  60      50.160  18.228  14.317  1.00 12.99           C  
ATOM    294  ND1 HIS A  60      50.447  19.304  15.138  1.00 13.02           N  
ATOM    295  CD2 HIS A  60      49.663  17.266  15.129  1.00 15.14           C  
ATOM    296  CE1 HIS A  60      50.138  19.001  16.382  1.00 13.17           C  
ATOM    297  NE2 HIS A  60      49.658  17.767  16.406  1.00 15.81           N  
ATOM    298  N   GLY A  61      49.570  18.170   9.823  1.00  9.48           N  
ATOM    299  CA  GLY A  61      49.943  18.196   8.417  1.00 10.18           C  
ATOM    300  C   GLY A  61      49.174  19.231   7.610  1.00 10.75           C  
ATOM    301  O   GLY A  61      49.753  19.933   6.775  1.00 11.05           O  
ATOM    302  N   LYS A  62      47.868  19.322   7.848  1.00 10.08           N  
ATOM    303  CA  LYS A  62      47.019  20.284   7.151  1.00  8.82           C  
ATOM    304  C   LYS A  62      47.360  21.689   7.618  1.00  8.66           C  
ATOM    305  O   LYS A  62      47.347  22.642   6.830  1.00  8.41           O  
ATOM    306  CB  LYS A  62      45.544  20.004   7.442  1.00  7.81           C  
ATOM    307  CG  LYS A  62      45.009  18.749   6.782  1.00  9.54           C  
ATOM    308  CD  LYS A  62      43.517  18.616   7.021  1.00 11.11           C  
ATOM    309  CE  LYS A  62      42.929  17.431   6.273  1.00 12.27           C  
ATOM    310  NZ  LYS A  62      41.449  17.554   6.164  1.00 15.55           N  
ATOM    311  N   ALA A  63      47.659  21.813   8.909  1.00  8.51           N  
ATOM    312  CA  ALA A  63      48.013  23.101   9.491  1.00  6.95           C  
ATOM    313  C   ALA A  63      49.298  23.650   8.876  1.00  7.06           C  
ATOM    314  O   ALA A  63      49.395  24.842   8.586  1.00  7.06           O  
ATOM    315  CB  ALA A  63      48.172  22.963  10.997  1.00  6.41           C  
ATOM    316  N   LEU A  64      50.283  22.777   8.683  1.00  8.13           N  
ATOM    317  CA  LEU A  64      51.565  23.173   8.094  1.00  8.67           C  
ATOM    318  C   LEU A  64      51.357  23.687   6.664  1.00  9.05           C  
ATOM    319  O   LEU A  64      51.828  24.768   6.294  1.00 10.99           O  
ATOM    320  CB  LEU A  64      52.520  21.974   8.086  1.00  8.71           C  
ATOM    321  CG  LEU A  64      53.972  22.234   7.690  1.00 10.61           C  
ATOM    322  CD1 LEU A  64      54.562  23.293   8.607  1.00 13.49           C  
ATOM    323  CD2 LEU A  64      54.767  20.938   7.798  1.00 11.99           C  
ATOM    324  N   ASP A  65      50.643  22.900   5.870  1.00  8.01           N  
ATOM    325  CA  ASP A  65      50.338  23.242   4.484  1.00  8.23           C  
ATOM    326  C   ASP A  65      49.679  24.621   4.426  1.00  8.19           C  
ATOM    327  O   ASP A  65      50.135  25.515   3.706  1.00  6.84           O  
ATOM    328  CB  ASP A  65      49.394  22.171   3.909  1.00  8.55           C  
ATOM    329  CG  ASP A  65      49.055  22.388   2.438  1.00 10.74           C  
ATOM    330  OD1 ASP A  65      49.785  23.122   1.736  1.00 10.64           O  
ATOM    331  OD2 ASP A  65      48.043  21.807   1.983  1.00  7.52           O  
ATOM    332  N   THR A  66      48.612  24.790   5.206  1.00  7.27           N  
ATOM    333  CA  THR A  66      47.864  26.042   5.242  1.00  5.92           C  
ATOM    334  C   THR A  66      48.659  27.229   5.773  1.00  5.96           C  
ATOM    335  O   THR A  66      48.508  28.346   5.277  1.00  7.63           O  
ATOM    336  CB  THR A  66      46.580  25.892   6.093  1.00  7.15           C  
ATOM    337  OG1 THR A  66      45.851  24.741   5.647  1.00  7.45           O  
ATOM    338  CG2 THR A  66      45.689  27.126   5.963  1.00  3.09           C  
ATOM    339  N   SER A  67      49.507  26.997   6.769  1.00  5.67           N  
ATOM    340  CA  SER A  67      50.290  28.080   7.357  1.00  6.78           C  
ATOM    341  C   SER A  67      51.143  28.861   6.353  1.00  7.08           C  
ATOM    342  O   SER A  67      51.326  30.069   6.496  1.00  7.35           O  
ATOM    343  CB  SER A  67      51.169  27.541   8.502  1.00  6.94           C  
ATOM    344  OG  SER A  67      52.334  26.896   8.022  1.00  7.34           O  
ATOM    345  N   HIS A  68      51.644  28.182   5.326  1.00  7.13           N  
ATOM    346  CA  HIS A  68      52.475  28.839   4.316  1.00  7.32           C  
ATOM    347  C   HIS A  68      51.730  29.869   3.465  1.00  8.55           C  
ATOM    348  O   HIS A  68      52.353  30.766   2.886  1.00  7.63           O  
ATOM    349  CB  HIS A  68      53.109  27.786   3.403  1.00  5.75           C  
ATOM    350  CG  HIS A  68      53.826  26.706   4.147  1.00  8.24           C  
ATOM    351  ND1 HIS A  68      53.729  25.374   3.806  1.00  4.89           N  
ATOM    352  CD2 HIS A  68      54.635  26.762   5.232  1.00  4.85           C  
ATOM    353  CE1 HIS A  68      54.449  24.655   4.649  1.00  6.18           C  
ATOM    354  NE2 HIS A  68      55.009  25.473   5.523  1.00  7.05           N  
ATOM    355  N   THR A  69      50.407  29.748   3.389  1.00  8.41           N  
ATOM    356  CA  THR A  69      49.613  30.677   2.590  1.00  6.82           C  
ATOM    357  C   THR A  69      49.599  32.078   3.181  1.00  6.69           C  
ATOM    358  O   THR A  69      49.078  33.007   2.565  1.00  5.90           O  
ATOM    359  CB  THR A  69      48.146  30.188   2.409  1.00  7.51           C  
ATOM    360  OG1 THR A  69      47.457  30.219   3.665  1.00  5.72           O  
ATOM    361  CG2 THR A  69      48.123  28.773   1.848  1.00  5.75           C  
ATOM    362  N   ASN A  70      50.173  32.234   4.372  1.00  5.94           N  
ATOM    363  CA  ASN A  70      50.227  33.545   5.006  1.00  6.48           C  
ATOM    364  C   ASN A  70      51.039  34.503   4.136  1.00  7.50           C  
ATOM    365  O   ASN A  70      50.748  35.700   4.071  1.00  6.58           O  
ATOM    366  CB  ASN A  70      50.876  33.446   6.385  1.00  7.07           C  
ATOM    367  CG  ASN A  70      49.874  33.162   7.478  1.00  7.27           C  
ATOM    368  OD1 ASN A  70      49.069  34.022   7.831  1.00  7.04           O  
ATOM    369  ND2 ASN A  70      49.916  31.949   8.024  1.00  7.72           N  
ATOM    370  N   VAL A  71      52.061  33.963   3.475  1.00  6.44           N  
ATOM    371  CA  VAL A  71      52.933  34.745   2.603  1.00  6.84           C  
ATOM    372  C   VAL A  71      52.176  35.242   1.381  1.00  7.22           C  
ATOM    373  O   VAL A  71      52.219  36.421   1.050  1.00  7.10           O  
ATOM    374  CB  VAL A  71      54.132  33.907   2.107  1.00  6.94           C  
ATOM    375  CG1 VAL A  71      55.053  34.771   1.250  1.00  2.76           C  
ATOM    376  CG2 VAL A  71      54.894  33.332   3.293  1.00  4.13           C  
ATOM    377  N   MET A  72      51.486  34.330   0.707  1.00  9.86           N  
ATOM    378  CA  MET A  72      50.721  34.669  -0.492  1.00 10.01           C  
ATOM    379  C   MET A  72      49.577  35.635  -0.200  1.00 10.08           C  
ATOM    380  O   MET A  72      49.227  36.460  -1.044  1.00  8.89           O  
ATOM    381  CB  MET A  72      50.147  33.401  -1.134  1.00  8.61           C  
ATOM    382  CG  MET A  72      51.126  32.627  -2.008  1.00 12.11           C  
ATOM    383  SD  MET A  72      52.357  31.711  -1.049  1.00 11.83           S  
ATOM    384  CE  MET A  72      51.674  30.067  -1.078  1.00 12.80           C  
ATOM    385  N   ALA A  73A     48.998  35.532   0.992  1.00 10.41           N  
ATOM    386  CA  ALA A  73A     47.864  36.378   1.362  1.00 12.14           C  
ATOM    387  C   ALA A  73A     48.194  37.621   2.194  1.00 13.06           C  
ATOM    388  O   ALA A  73A     47.274  38.350   2.576  1.00 12.40           O  
ATOM    389  CB  ALA A  73A     46.815  35.538   2.087  1.00 11.16           C  
ATOM    390  N   TYR A  73B     49.465  37.867   2.455  1.00 14.48           N  
ATOM    391  CA  TYR A  73B     49.891  39.010   3.272  1.00 17.08           C  
ATOM    392  C   TYR A  73B     49.199  38.963   4.629  1.00 14.72           C  
ATOM    393  O   TYR A  73B     48.771  39.990   5.158  1.00 13.10           O  
ATOM    394  CB  TYR A  73B     49.530  40.344   2.608  1.00 22.47           C  
ATOM    395  CG  TYR A  73B     49.804  40.426   1.133  1.00 29.23           C  
ATOM    396  CD1 TYR A  73B     48.850  40.022   0.205  1.00 32.31           C  
ATOM    397  CD2 TYR A  73B     51.010  40.937   0.658  1.00 34.39           C  
ATOM    398  CE1 TYR A  73B     49.086  40.123  -1.162  1.00 33.76           C  
ATOM    399  CE2 TYR A  73B     51.258  41.044  -0.711  1.00 34.90           C  
ATOM    400  CZ  TYR A  73B     50.291  40.636  -1.612  1.00 34.62           C  
ATOM    401  OH  TYR A  73B     50.533  40.745  -2.963  1.00 35.72           O  
ATOM    402  N   SER A  74      49.076  37.768   5.197  1.00 13.20           N  
ATOM    403  CA  SER A  74      48.424  37.647   6.488  1.00 11.65           C  
ATOM    404  C   SER A  74      49.433  37.273   7.558  1.00 10.68           C  
ATOM    405  O   SER A  74      50.615  37.060   7.271  1.00  7.94           O  
ATOM    406  CB  SER A  74      47.322  36.587   6.425  1.00 12.96           C  
ATOM    407  OG  SER A  74      46.242  37.034   5.627  1.00 17.51           O  
ATOM    408  N   ASN A  75      48.959  37.211   8.798  1.00  9.79           N  
ATOM    409  CA  ASN A  75      49.799  36.835   9.919  1.00 10.85           C  
ATOM    410  C   ASN A  75      48.962  36.055  10.925  1.00 10.88           C  
ATOM    411  O   ASN A  75      48.757  36.498  12.056  1.00  9.80           O  
ATOM    412  CB  ASN A  75      50.403  38.066  10.595  1.00 11.19           C  
ATOM    413  CG  ASN A  75      51.543  37.707  11.523  1.00 15.18           C  
ATOM    414  OD1 ASN A  75      52.092  36.608  11.450  1.00 12.98           O  
ATOM    415  ND2 ASN A  75      51.906  38.630  12.405  1.00 17.58           N  
ATOM    416  N   CYS A  76      48.474  34.894  10.499  1.00  8.71           N  
ATOM    417  CA  CYS A  76      47.665  34.040  11.356  1.00 10.72           C  
ATOM    418  C   CYS A  76      48.380  32.722  11.590  1.00 11.63           C  
ATOM    419  O   CYS A  76      48.773  32.034  10.646  1.00 11.53           O  
ATOM    420  CB  CYS A  76      46.306  33.740  10.714  1.00  9.29           C  
ATOM    421  SG  CYS A  76      45.244  35.150  10.491  1.00 10.32           S  
ATOM    422  N   LYS A  77      48.549  32.371  12.855  1.00 12.60           N  
ATOM    423  CA  LYS A  77      49.191  31.119  13.191  1.00 13.53           C  
ATOM    424  C   LYS A  77      48.196  30.029  12.846  1.00 14.18           C  
ATOM    425  O   LYS A  77      46.994  30.179  13.088  1.00 15.04           O  
ATOM    426  CB  LYS A  77      49.486  31.064  14.688  1.00 16.62           C  
ATOM    427  CG  LYS A  77      50.837  31.616  15.086  1.00 22.17           C  
ATOM    428  CD  LYS A  77      50.939  31.747  16.601  1.00 26.01           C  
ATOM    429  CE  LYS A  77      51.736  32.986  16.995  1.00 28.42           C  
ATOM    430  NZ  LYS A  77      52.682  32.702  18.110  1.00 30.58           N  
ATOM    431  N   VAL A  78      48.681  28.945  12.255  1.00 12.00           N  
ATOM    432  CA  VAL A  78      47.818  27.821  11.931  1.00 11.90           C  
ATOM    433  C   VAL A  78      48.526  26.600  12.483  1.00 11.99           C  
ATOM    434  O   VAL A  78      49.598  26.223  12.000  1.00 12.03           O  
ATOM    435  CB  VAL A  78      47.607  27.657  10.407  1.00 11.60           C  
ATOM    436  CG1 VAL A  78      46.591  26.544  10.146  1.00  8.81           C  
ATOM    437  CG2 VAL A  78      47.124  28.971   9.805  1.00 10.73           C  
ATOM    438  N   SER A  79      47.937  25.997  13.512  1.00 11.47           N  
ATOM    439  CA  SER A  79      48.529  24.826  14.145  1.00 12.52           C  
ATOM    440  C   SER A  79      47.546  23.680  14.296  1.00 12.14           C  
ATOM    441  O   SER A  79      46.333  23.882  14.327  1.00 13.49           O  
ATOM    442  CB  SER A  79      49.062  25.203  15.521  1.00 14.04           C  
ATOM    443  OG  SER A  79      48.037  25.798  16.287  1.00 18.46           O  
ATOM    444  N   GLY A  80      48.082  22.470  14.388  1.00  9.93           N  
ATOM    445  CA  GLY A  80      47.241  21.304  14.549  1.00  9.40           C  
ATOM    446  C   GLY A  80      47.188  20.981  16.021  1.00  9.32           C  
ATOM    447  O   GLY A  80      47.920  21.571  16.816  1.00  9.50           O  
ATOM    448  N   SER A  81      46.324  20.053  16.402  1.00  9.73           N  
ATOM    449  CA  SER A  81      46.220  19.687  17.803  1.00  8.32           C  
ATOM    450  C   SER A  81      45.462  18.385  17.966  1.00 10.04           C  
ATOM    451  O   SER A  81      44.522  18.105  17.215  1.00  8.19           O  
ATOM    452  CB  SER A  81      45.518  20.797  18.589  1.00  7.95           C  
ATOM    453  OG  SER A  81      45.063  20.317  19.847  1.00  7.63           O  
ATOM    454  N   ASN A  83      45.896  17.589  18.942  1.00 10.92           N  
ATOM    455  CA  ASN A  83      45.264  16.315  19.255  1.00 12.03           C  
ATOM    456  C   ASN A  83      44.880  16.302  20.731  1.00 12.75           C  
ATOM    457  O   ASN A  83      44.557  15.252  21.282  1.00 13.57           O  
ATOM    458  CB  ASN A  83      46.219  15.153  18.975  1.00 12.12           C  
ATOM    459  CG  ASN A  83      46.358  14.857  17.500  1.00 16.11           C  
ATOM    460  OD1 ASN A  83      47.468  14.649  17.001  1.00 17.38           O  
ATOM    461  ND2 ASN A  83      45.230  14.834  16.787  1.00 13.36           N  
ATOM    462  N   THR A  84      44.928  17.469  21.371  1.00 12.03           N  
ATOM    463  CA  THR A  84      44.571  17.563  22.781  1.00 14.45           C  
ATOM    464  C   THR A  84      43.545  18.673  23.033  1.00 14.08           C  
ATOM    465  O   THR A  84      43.722  19.820  22.617  1.00 13.10           O  
ATOM    466  CB  THR A  84      45.828  17.779  23.673  1.00 15.45           C  
ATOM    467  OG1 THR A  84      45.496  18.612  24.790  1.00 20.04           O  
ATOM    468  CG2 THR A  84      46.940  18.419  22.886  1.00 17.12           C  
ATOM    469  N   TYR A  85      42.464  18.313  23.718  1.00 13.06           N  
ATOM    470  CA  TYR A  85      41.392  19.250  24.023  1.00 14.43           C  
ATOM    471  C   TYR A  85      41.858  20.495  24.766  1.00 16.52           C  
ATOM    472  O   TYR A  85      41.175  21.519  24.767  1.00 17.15           O  
ATOM    473  CB  TYR A  85      40.314  18.543  24.840  1.00 12.33           C  
ATOM    474  CG  TYR A  85      39.285  17.850  23.989  1.00 11.00           C  
ATOM    475  CD1 TYR A  85      38.369  18.586  23.240  1.00 10.04           C  
ATOM    476  CD2 TYR A  85      39.226  16.457  23.931  1.00 10.14           C  
ATOM    477  CE1 TYR A  85      37.416  17.951  22.449  1.00 11.69           C  
ATOM    478  CE2 TYR A  85      38.279  15.812  23.145  1.00 11.43           C  
ATOM    479  CZ  TYR A  85      37.377  16.565  22.407  1.00 12.62           C  
ATOM    480  OH  TYR A  85      36.438  15.931  21.631  1.00 11.15           O  
ATOM    481  N   ASP A  86      43.023  20.401  25.398  1.00 19.50           N  
ATOM    482  CA  ASP A  86      43.585  21.514  26.150  1.00 22.25           C  
ATOM    483  C   ASP A  86      43.701  22.784  25.307  1.00 20.06           C  
ATOM    484  O   ASP A  86      43.548  23.893  25.817  1.00 19.65           O  
ATOM    485  CB  ASP A  86      44.967  21.131  26.694  1.00 29.18           C  
ATOM    486  CG  ASP A  86      45.528  22.170  27.653  1.00 38.46           C  
ATOM    487  OD1 ASP A  86      44.782  23.106  28.028  1.00 42.05           O  
ATOM    488  OD2 ASP A  86      46.717  22.057  28.034  1.00 42.46           O  
ATOM    489  N   ASP A  87      43.963  22.622  24.014  1.00 16.85           N  
ATOM    490  CA  ASP A  87      44.107  23.769  23.129  1.00 15.30           C  
ATOM    491  C   ASP A  87      42.824  24.584  22.936  1.00 14.68           C  
ATOM    492  O   ASP A  87      42.802  25.548  22.170  1.00 13.58           O  
ATOM    493  CB  ASP A  87      44.667  23.304  21.783  1.00 16.16           C  
ATOM    494  CG  ASP A  87      46.090  22.793  21.908  1.00 16.20           C  
ATOM    495  OD1 ASP A  87      46.848  23.373  22.707  1.00 20.84           O  
ATOM    496  OD2 ASP A  87      46.452  21.815  21.228  1.00 16.14           O  
ATOM    497  N   LEU A  88      41.762  24.197  23.638  1.00 11.79           N  
ATOM    498  CA  LEU A  88      40.499  24.917  23.564  1.00 10.40           C  
ATOM    499  C   LEU A  88      40.608  26.156  24.442  1.00 10.54           C  
ATOM    500  O   LEU A  88      39.818  27.087  24.319  1.00  9.93           O  
ATOM    501  CB  LEU A  88      39.349  24.036  24.063  1.00 10.44           C  
ATOM    502  CG  LEU A  88      38.656  23.173  23.003  1.00 11.14           C  
ATOM    503  CD1 LEU A  88      37.758  22.138  23.672  1.00 11.62           C  
ATOM    504  CD2 LEU A  88      37.853  24.069  22.063  1.00 11.32           C  
ATOM    505  N   ALA A  89      41.604  26.164  25.328  1.00 11.10           N  
ATOM    506  CA  ALA A  89      41.808  27.286  26.239  1.00 11.40           C  
ATOM    507  C   ALA A  89      42.115  28.575  25.491  1.00 13.24           C  
ATOM    508  O   ALA A  89      42.949  28.598  24.585  1.00 13.10           O  
ATOM    509  CB  ALA A  89      42.933  26.973  27.215  1.00 10.56           C  
ATOM    510  N   GLY A  90      41.430  29.646  25.876  1.00 14.12           N  
ATOM    511  CA  GLY A  90      41.650  30.928  25.241  1.00 13.16           C  
ATOM    512  C   GLY A  90      40.877  31.100  23.955  1.00 12.53           C  
ATOM    513  O   GLY A  90      40.982  32.132  23.307  1.00 12.89           O  
ATOM    514  N   SER A  91      40.089  30.097  23.586  1.00 13.34           N  
ATOM    515  CA  SER A  91      39.308  30.163  22.355  1.00 14.76           C  
ATOM    516  C   SER A  91      38.244  31.247  22.375  1.00 12.77           C  
ATOM    517  O   SER A  91      37.488  31.369  23.336  1.00 13.82           O  
ATOM    518  CB  SER A  91      38.615  28.826  22.089  1.00 19.13           C  
ATOM    519  OG  SER A  91      39.555  27.789  21.907  1.00 34.42           O  
ATOM    520  N   ASP A  92      38.180  32.024  21.297  1.00 11.46           N  
ATOM    521  CA  ASP A  92      37.179  33.079  21.173  1.00  9.27           C  
ATOM    522  C   ASP A  92      36.004  32.520  20.382  1.00  8.92           C  
ATOM    523  O   ASP A  92      34.847  32.852  20.644  1.00  8.95           O  
ATOM    524  CB  ASP A  92      37.754  34.288  20.437  1.00  9.11           C  
ATOM    525  CG  ASP A  92      38.831  34.987  21.228  1.00  9.83           C  
ATOM    526  OD1 ASP A  92      38.493  35.674  22.211  1.00 10.29           O  
ATOM    527  OD2 ASP A  92      40.018  34.842  20.869  1.00 12.03           O  
ATOM    528  N   VAL A  93      36.322  31.664  19.414  1.00  7.59           N  
ATOM    529  CA  VAL A  93      35.326  31.033  18.555  1.00  7.83           C  
ATOM    530  C   VAL A  93      35.678  29.559  18.401  1.00  6.96           C  
ATOM    531  O   VAL A  93      36.835  29.213  18.176  1.00  6.45           O  
ATOM    532  CB  VAL A  93      35.310  31.678  17.146  1.00  7.06           C  
ATOM    533  CG1 VAL A  93      34.349  30.923  16.236  1.00  4.46           C  
ATOM    534  CG2 VAL A  93      34.928  33.147  17.247  1.00  5.13           C  
ATOM    535  N   VAL A  94      34.677  28.696  18.525  1.00  9.02           N  
ATOM    536  CA  VAL A  94      34.877  27.255  18.386  1.00  8.38           C  
ATOM    537  C   VAL A  94      33.904  26.739  17.338  1.00  8.12           C  
ATOM    538  O   VAL A  94      32.692  26.929  17.464  1.00  7.14           O  
ATOM    539  CB  VAL A  94      34.619  26.518  19.725  1.00  9.28           C  
ATOM    540  CG1 VAL A  94      34.656  25.009  19.516  1.00  5.92           C  
ATOM    541  CG2 VAL A  94      35.653  26.942  20.754  1.00  7.85           C  
ATOM    542  N   ILE A  95      34.431  26.098  16.299  1.00  7.31           N  
ATOM    543  CA  ILE A  95      33.585  25.570  15.237  1.00  6.35           C  
ATOM    544  C   ILE A  95      33.629  24.044  15.203  1.00  7.82           C  
ATOM    545  O   ILE A  95      34.667  23.434  14.933  1.00  8.69           O  
ATOM    546  CB  ILE A  95      33.993  26.157  13.880  1.00  5.01           C  
ATOM    547  CG1 ILE A  95      34.024  27.688  13.981  1.00  5.34           C  
ATOM    548  CG2 ILE A  95      33.000  25.728  12.814  1.00  4.96           C  
ATOM    549  CD1 ILE A  95      34.726  28.379  12.824  1.00  7.50           C  
ATOM    550  N   VAL A  96      32.480  23.436  15.476  1.00  7.16           N  
ATOM    551  CA  VAL A  96      32.364  21.990  15.533  1.00  7.04           C  
ATOM    552  C   VAL A  96      31.815  21.324  14.272  1.00  8.86           C  
ATOM    553  O   VAL A  96      30.658  21.518  13.909  1.00  9.19           O  
ATOM    554  CB  VAL A  96      31.484  21.586  16.738  1.00  7.92           C  
ATOM    555  CG1 VAL A  96      31.464  20.080  16.893  1.00  5.69           C  
ATOM    556  CG2 VAL A  96      32.014  22.259  18.008  1.00  3.66           C  
ATOM    557  N   THR A  97      32.660  20.531  13.617  1.00  9.28           N  
ATOM    558  CA  THR A  97      32.280  19.808  12.412  1.00  9.08           C  
ATOM    559  C   THR A  97      32.448  18.313  12.663  1.00  9.94           C  
ATOM    560  O   THR A  97      32.028  17.487  11.857  1.00 10.08           O  
ATOM    561  CB  THR A  97      33.157  20.196  11.206  1.00  9.20           C  
ATOM    562  OG1 THR A  97      34.537  20.038  11.552  1.00  9.81           O  
ATOM    563  CG2 THR A  97      32.895  21.644  10.784  1.00  7.09           C  
ATOM    564  N   ALA A  98      33.066  17.974  13.791  1.00 11.12           N  
ATOM    565  CA  ALA A  98      33.294  16.581  14.158  1.00 11.73           C  
ATOM    566  C   ALA A  98      31.982  15.810  14.193  1.00 13.04           C  
ATOM    567  O   ALA A  98      30.927  16.369  14.489  1.00 12.39           O  
ATOM    568  CB  ALA A  98      33.965  16.508  15.517  1.00 11.46           C  
ATOM    569  N   GLY A  99      32.047  14.518  13.891  1.00 12.99           N  
ATOM    570  CA  GLY A  99      30.844  13.716  13.922  1.00 16.68           C  
ATOM    571  C   GLY A  99      30.812  12.585  12.920  1.00 18.53           C  
ATOM    572  O   GLY A  99      31.308  12.711  11.802  1.00 18.74           O  
ATOM    573  N   PHE A 100      30.231  11.463  13.327  1.00 19.86           N  
ATOM    574  CA  PHE A 100      30.121  10.321  12.441  1.00 21.72           C  
ATOM    575  C   PHE A 100      29.142  10.694  11.341  1.00 23.97           C  
ATOM    576  O   PHE A 100      28.212  11.475  11.560  1.00 22.61           O  
ATOM    577  CB  PHE A 100      29.617   9.103  13.211  1.00 22.52           C  
ATOM    578  CG  PHE A 100      30.583   8.605  14.238  1.00 23.11           C  
ATOM    579  CD1 PHE A 100      31.746   7.955  13.849  1.00 25.99           C  
ATOM    580  CD2 PHE A 100      30.339   8.793  15.593  1.00 23.90           C  
ATOM    581  CE1 PHE A 100      32.659   7.497  14.796  1.00 26.62           C  
ATOM    582  CE2 PHE A 100      31.244   8.339  16.552  1.00 25.95           C  
ATOM    583  CZ  PHE A 100      32.407   7.690  16.153  1.00 27.56           C  
ATOM    584  N   THR A 101      29.360  10.138  10.156  1.00 26.97           N  
ATOM    585  CA  THR A 101      28.505  10.416   9.014  1.00 30.59           C  
ATOM    586  C   THR A 101      27.987   9.111   8.407  1.00 31.51           C  
ATOM    587  O   THR A 101      26.933   9.165   7.734  1.00 34.31           O  
ATOM    588  CB  THR A 101      29.283  11.205   7.948  1.00 30.92           C  
ATOM    589  OG1 THR A 101      29.602  12.504   8.457  1.00 34.24           O  
ATOM    590  CG2 THR A 101      28.459  11.356   6.684  1.00 35.96           C  
ATOM    591  N   ASN A 108      20.573   3.009   9.814  1.00 41.13           N  
ATOM    592  CA  ASN A 108      19.973   4.286   9.325  1.00 41.53           C  
ATOM    593  C   ASN A 108      20.807   5.485   9.745  1.00 39.52           C  
ATOM    594  O   ASN A 108      21.805   5.350  10.450  1.00 38.97           O  
ATOM    595  CB  ASN A 108      18.552   4.468   9.875  1.00 44.42           C  
ATOM    596  CG  ASN A 108      18.043   3.247  10.607  1.00 48.43           C  
ATOM    597  OD1 ASN A 108      17.237   2.482  10.074  1.00 51.70           O  
ATOM    598  ND2 ASN A 108      18.508   3.056  11.838  1.00 51.71           N  
ATOM    599  N   ARG A 109      20.381   6.660   9.299  1.00 38.43           N  
ATOM    600  CA  ARG A 109      21.054   7.908   9.631  1.00 36.55           C  
ATOM    601  C   ARG A 109      20.807   8.156  11.113  1.00 33.06           C  
ATOM    602  O   ARG A 109      21.641   8.725  11.818  1.00 31.35           O  
ATOM    603  CB  ARG A 109      20.446   9.052   8.821  1.00 40.97           C  
ATOM    604  CG  ARG A 109      21.432   9.848   7.990  1.00 48.25           C  
ATOM    605  CD  ARG A 109      20.697  10.632   6.913  1.00 53.78           C  
ATOM    606  NE  ARG A 109      21.552  10.952   5.774  1.00 58.03           N  
ATOM    607  CZ  ARG A 109      21.125  11.556   4.669  1.00 60.46           C  
ATOM    608  NH1 ARG A 109      19.852  11.912   4.555  1.00 62.00           N  
ATOM    609  NH2 ARG A 109      21.972  11.816   3.681  1.00 61.91           N  
ATOM    610  N   LEU A 110      19.642   7.708  11.566  1.00 28.33           N  
ATOM    611  CA  LEU A 110      19.215   7.867  12.949  1.00 25.40           C  
ATOM    612  C   LEU A 110      20.048   7.074  13.940  1.00 24.41           C  
ATOM    613  O   LEU A 110      19.989   7.333  15.137  1.00 23.37           O  
ATOM    614  CB  LEU A 110      17.754   7.440  13.090  1.00 24.65           C  
ATOM    615  CG  LEU A 110      16.658   8.500  13.018  1.00 21.45           C  
ATOM    616  CD1 LEU A 110      17.025   9.589  12.019  1.00 20.29           C  
ATOM    617  CD2 LEU A 110      15.363   7.819  12.633  1.00 19.08           C  
ATOM    618  N   ASP A 111      20.806   6.101  13.452  1.00 23.53           N  
ATOM    619  CA  ASP A 111      21.628   5.287  14.338  1.00 24.26           C  
ATOM    620  C   ASP A 111      22.838   6.071  14.828  1.00 24.04           C  
ATOM    621  O   ASP A 111      23.412   5.747  15.869  1.00 25.06           O  
ATOM    622  CB  ASP A 111      22.087   4.012  13.622  1.00 27.19           C  
ATOM    623  CG  ASP A 111      20.993   2.957  13.544  1.00 30.80           C  
ATOM    624  OD1 ASP A 111      20.045   3.010  14.361  1.00 29.91           O  
ATOM    625  OD2 ASP A 111      21.083   2.074  12.661  1.00 34.29           O  
ATOM    626  N   LEU A 112      23.215   7.106  14.080  1.00 22.58           N  
ATOM    627  CA  LEU A 112      24.360   7.940  14.436  1.00 21.75           C  
ATOM    628  C   LEU A 112      24.007   8.974  15.501  1.00 20.48           C  
ATOM    629  O   LEU A 112      24.893   9.506  16.175  1.00 20.74           O  
ATOM    630  CB  LEU A 112      24.899   8.661  13.194  1.00 21.86           C  
ATOM    631  CG  LEU A 112      25.735   7.871  12.180  1.00 24.16           C  
ATOM    632  CD1 LEU A 112      26.587   6.822  12.874  1.00 23.07           C  
ATOM    633  CD2 LEU A 112      24.808   7.219  11.187  1.00 25.76           C  
ATOM    634  N   LEU A 113      22.715   9.254  15.650  1.00 19.00           N  
ATOM    635  CA  LEU A 113      22.244  10.242  16.622  1.00 18.09           C  
ATOM    636  C   LEU A 113      22.834  10.065  18.021  1.00 17.11           C  
ATOM    637  O   LEU A 113      23.437  10.993  18.565  1.00 17.81           O  
ATOM    638  CB  LEU A 113      20.709  10.232  16.693  1.00 16.10           C  
ATOM    639  CG  LEU A 113      20.002  10.871  15.491  1.00 17.84           C  
ATOM    640  CD1 LEU A 113      18.493  10.779  15.659  1.00 14.90           C  
ATOM    641  CD2 LEU A 113      20.437  12.323  15.358  1.00 15.94           C  
ATOM    642  N   PRO A 114      22.666   8.878  18.628  1.00 16.72           N  
ATOM    643  CA  PRO A 114      23.231   8.693  19.971  1.00 15.60           C  
ATOM    644  C   PRO A 114      24.755   8.798  19.965  1.00 14.85           C  
ATOM    645  O   PRO A 114      25.354   9.335  20.894  1.00 13.16           O  
ATOM    646  CB  PRO A 114      22.751   7.301  20.377  1.00 16.38           C  
ATOM    647  CG  PRO A 114      22.462   6.611  19.083  1.00 18.94           C  
ATOM    648  CD  PRO A 114      21.972   7.669  18.149  1.00 16.34           C  
ATOM    649  N   LEU A 115      25.374   8.287  18.907  1.00 15.12           N  
ATOM    650  CA  LEU A 115      26.825   8.321  18.765  1.00 16.27           C  
ATOM    651  C   LEU A 115      27.350   9.755  18.687  1.00 15.58           C  
ATOM    652  O   LEU A 115      28.292  10.122  19.391  1.00 14.56           O  
ATOM    653  CB  LEU A 115      27.245   7.557  17.505  1.00 18.99           C  
ATOM    654  CG  LEU A 115      27.619   6.078  17.641  1.00 22.74           C  
ATOM    655  CD1 LEU A 115      27.148   5.530  18.985  1.00 22.76           C  
ATOM    656  CD2 LEU A 115      26.990   5.295  16.495  1.00 23.15           C  
ATOM    657  N   ASN A 116      26.746  10.561  17.823  1.00 14.68           N  
ATOM    658  CA  ASN A 116      27.171  11.944  17.674  1.00 14.08           C  
ATOM    659  C   ASN A 116      26.861  12.757  18.921  1.00 13.61           C  
ATOM    660  O   ASN A 116      27.532  13.749  19.210  1.00 14.83           O  
ATOM    661  CB  ASN A 116      26.514  12.564  16.441  1.00 14.19           C  
ATOM    662  CG  ASN A 116      27.218  12.163  15.164  1.00 15.83           C  
ATOM    663  OD1 ASN A 116      28.398  11.821  15.186  1.00 15.10           O  
ATOM    664  ND2 ASN A 116      26.500  12.190  14.048  1.00 16.44           N  
ATOM    665  N   ASN A 117      25.838  12.343  19.663  1.00 12.74           N  
ATOM    666  CA  ASN A 117      25.500  13.043  20.890  1.00 13.31           C  
ATOM    667  C   ASN A 117      26.666  12.845  21.864  1.00 13.28           C  
ATOM    668  O   ASN A 117      26.997  13.743  22.639  1.00 12.76           O  
ATOM    669  CB  ASN A 117      24.209  12.487  21.492  1.00 13.69           C  
ATOM    670  CG  ASN A 117      23.814  13.194  22.777  1.00 15.00           C  
ATOM    671  OD1 ASN A 117      24.141  14.367  22.985  1.00 16.83           O  
ATOM    672  ND2 ASN A 117      23.112  12.486  23.648  1.00 13.10           N  
ATOM    673  N   LYS A 118      27.294  11.672  21.806  1.00 13.15           N  
ATOM    674  CA  LYS A 118      28.426  11.363  22.679  1.00 14.80           C  
ATOM    675  C   LYS A 118      29.590  12.294  22.365  1.00 13.55           C  
ATOM    676  O   LYS A 118      30.333  12.706  23.259  1.00 11.78           O  
ATOM    677  CB  LYS A 118      28.869   9.907  22.498  1.00 19.13           C  
ATOM    678  CG  LYS A 118      27.976   8.892  23.203  1.00 25.52           C  
ATOM    679  CD  LYS A 118      28.498   7.471  23.033  1.00 30.85           C  
ATOM    680  CE  LYS A 118      27.783   6.507  23.967  1.00 33.85           C  
ATOM    681  NZ  LYS A 118      28.019   6.868  25.397  1.00 36.93           N  
ATOM    682  N   ILE A 119      29.748  12.618  21.088  1.00 11.89           N  
ATOM    683  CA  ILE A 119      30.803  13.520  20.673  1.00  9.89           C  
ATOM    684  C   ILE A 119      30.467  14.909  21.207  1.00  9.58           C  
ATOM    685  O   ILE A 119      31.338  15.598  21.732  1.00 12.45           O  
ATOM    686  CB  ILE A 119      30.933  13.540  19.140  1.00 10.13           C  
ATOM    687  CG1 ILE A 119      31.479  12.188  18.665  1.00  9.54           C  
ATOM    688  CG2 ILE A 119      31.851  14.674  18.700  1.00 10.47           C  
ATOM    689  CD1 ILE A 119      31.509  12.013  17.157  1.00 10.05           C  
ATOM    690  N   MET A 120      29.202  15.310  21.098  1.00  8.74           N  
ATOM    691  CA  MET A 120      28.775  16.618  21.595  1.00  8.83           C  
ATOM    692  C   MET A 120      29.007  16.725  23.103  1.00  9.14           C  
ATOM    693  O   MET A 120      29.396  17.779  23.606  1.00  7.14           O  
ATOM    694  CB  MET A 120      27.293  16.865  21.285  1.00 10.26           C  
ATOM    695  CG  MET A 120      26.957  16.907  19.800  1.00 12.24           C  
ATOM    696  SD  MET A 120      27.880  18.166  18.882  1.00 13.53           S  
ATOM    697  CE  MET A 120      29.023  17.147  17.971  1.00 11.54           C  
ATOM    698  N   ILE A 121      28.771  15.629  23.820  1.00  9.62           N  
ATOM    699  CA  ILE A 121      28.963  15.607  25.268  1.00  9.49           C  
ATOM    700  C   ILE A 121      30.434  15.806  25.627  1.00 10.05           C  
ATOM    701  O   ILE A 121      30.769  16.615  26.492  1.00 10.02           O  
ATOM    702  CB  ILE A 121      28.472  14.274  25.879  1.00 10.38           C  
ATOM    703  CG1 ILE A 121      26.941  14.255  25.915  1.00  8.39           C  
ATOM    704  CG2 ILE A 121      29.023  14.107  27.297  1.00  7.05           C  
ATOM    705  CD1 ILE A 121      26.343  12.860  25.928  1.00  9.58           C  
ATOM    706  N   GLU A 122      31.308  15.061  24.963  1.00 11.20           N  
ATOM    707  CA  GLU A 122      32.743  15.166  25.204  1.00 10.89           C  
ATOM    708  C   GLU A 122      33.248  16.574  24.902  1.00  9.75           C  
ATOM    709  O   GLU A 122      33.996  17.152  25.689  1.00 10.86           O  
ATOM    710  CB  GLU A 122      33.493  14.158  24.336  1.00 12.91           C  
ATOM    711  CG  GLU A 122      35.007  14.323  24.343  1.00 16.03           C  
ATOM    712  CD  GLU A 122      35.698  13.251  23.520  1.00 17.60           C  
ATOM    713  OE1 GLU A 122      36.025  12.187  24.081  1.00 19.90           O  
ATOM    714  OE2 GLU A 122      35.910  13.471  22.311  1.00 18.44           O  
ATOM    715  N   ILE A 123      32.843  17.124  23.763  1.00  9.07           N  
ATOM    716  CA  ILE A 123      33.272  18.466  23.388  1.00  9.04           C  
ATOM    717  C   ILE A 123      32.694  19.489  24.359  1.00  7.74           C  
ATOM    718  O   ILE A 123      33.401  20.379  24.818  1.00  9.91           O  
ATOM    719  CB  ILE A 123      32.834  18.822  21.947  1.00  8.95           C  
ATOM    720  CG1 ILE A 123      33.556  17.920  20.943  1.00  8.21           C  
ATOM    721  CG2 ILE A 123      33.174  20.273  21.639  1.00  7.90           C  
ATOM    722  CD1 ILE A 123      32.868  17.834  19.587  1.00 11.41           C  
ATOM    723  N   GLY A 124      31.412  19.347  24.681  1.00  6.72           N  
ATOM    724  CA  GLY A 124      30.770  20.271  25.603  1.00  6.15           C  
ATOM    725  C   GLY A 124      31.444  20.367  26.960  1.00  6.43           C  
ATOM    726  O   GLY A 124      31.543  21.446  27.533  1.00  5.17           O  
ATOM    727  N   GLY A 125      31.907  19.238  27.490  1.00  7.78           N  
ATOM    728  CA  GLY A 125      32.567  19.257  28.782  1.00  7.41           C  
ATOM    729  C   GLY A 125      33.858  20.057  28.755  1.00  9.94           C  
ATOM    730  O   GLY A 125      34.180  20.773  29.710  1.00 10.08           O  
ATOM    731  N   HIS A 126      34.602  19.941  27.659  1.00  9.09           N  
ATOM    732  CA  HIS A 126      35.858  20.663  27.526  1.00 10.91           C  
ATOM    733  C   HIS A 126      35.624  22.154  27.277  1.00 11.77           C  
ATOM    734  O   HIS A 126      36.369  22.997  27.787  1.00 10.94           O  
ATOM    735  CB  HIS A 126      36.700  20.039  26.409  1.00  9.63           C  
ATOM    736  CG  HIS A 126      37.249  18.690  26.762  1.00 10.79           C  
ATOM    737  ND1 HIS A 126      38.157  18.502  27.780  1.00 10.94           N  
ATOM    738  CD2 HIS A 126      36.981  17.460  26.263  1.00  8.39           C  
ATOM    739  CE1 HIS A 126      38.423  17.213  27.896  1.00  8.25           C  
ATOM    740  NE2 HIS A 126      37.724  16.560  26.988  1.00  8.39           N  
ATOM    741  N   ILE A 127      34.593  22.487  26.505  1.00 11.55           N  
ATOM    742  CA  ILE A 127      34.279  23.895  26.250  1.00 10.78           C  
ATOM    743  C   ILE A 127      33.965  24.562  27.592  1.00 11.95           C  
ATOM    744  O   ILE A 127      34.473  25.639  27.909  1.00 10.75           O  
ATOM    745  CB  ILE A 127      33.043  24.045  25.328  1.00 10.89           C  
ATOM    746  CG1 ILE A 127      33.435  23.798  23.869  1.00  8.28           C  
ATOM    747  CG2 ILE A 127      32.454  25.443  25.466  1.00  7.34           C  
ATOM    748  CD1 ILE A 127      32.250  23.675  22.931  1.00  5.67           C  
ATOM    749  N   LYS A 128      33.121  23.902  28.380  1.00 13.05           N  
ATOM    750  CA  LYS A 128      32.713  24.408  29.683  1.00 12.81           C  
ATOM    751  C   LYS A 128      33.920  24.656  30.578  1.00 12.63           C  
ATOM    752  O   LYS A 128      33.968  25.636  31.318  1.00 12.66           O  
ATOM    753  CB  LYS A 128      31.772  23.405  30.352  1.00 15.00           C  
ATOM    754  CG  LYS A 128      31.340  23.784  31.759  1.00 16.59           C  
ATOM    755  CD  LYS A 128      30.317  22.794  32.295  1.00 21.63           C  
ATOM    756  CE  LYS A 128      28.911  23.145  31.833  1.00 25.26           C  
ATOM    757  NZ  LYS A 128      27.981  21.981  31.933  1.00 29.85           N  
ATOM    758  N   LYS A 129      34.902  23.767  30.485  1.00 14.98           N  
ATOM    759  CA  LYS A 129      36.113  23.857  31.289  1.00 16.09           C  
ATOM    760  C   LYS A 129      37.189  24.798  30.750  1.00 15.93           C  
ATOM    761  O   LYS A 129      37.797  25.555  31.511  1.00 14.92           O  
ATOM    762  CB  LYS A 129      36.722  22.466  31.450  1.00 18.54           C  
ATOM    763  CG  LYS A 129      37.014  22.082  32.881  1.00 24.67           C  
ATOM    764  CD  LYS A 129      38.314  22.689  33.357  1.00 29.28           C  
ATOM    765  CE  LYS A 129      38.302  22.882  34.865  1.00 33.55           C  
ATOM    766  NZ  LYS A 129      38.939  21.735  35.581  1.00 38.67           N  
ATOM    767  N   ASN A 130      37.420  24.753  29.440  1.00 14.51           N  
ATOM    768  CA  ASN A 130      38.465  25.561  28.816  1.00 14.20           C  
ATOM    769  C   ASN A 130      38.070  26.914  28.229  1.00 10.90           C  
ATOM    770  O   ASN A 130      38.839  27.866  28.311  1.00 10.19           O  
ATOM    771  CB  ASN A 130      39.169  24.731  27.736  1.00 15.73           C  
ATOM    772  CG  ASN A 130      39.616  23.377  28.246  1.00 19.05           C  
ATOM    773  OD1 ASN A 130      39.996  23.240  29.406  1.00 23.62           O  
ATOM    774  ND2 ASN A 130      39.571  22.365  27.382  1.00 20.17           N  
ATOM    775  N   CYS A 131      36.890  27.013  27.635  1.00  9.79           N  
ATOM    776  CA  CYS A 131      36.483  28.280  27.037  1.00 11.42           C  
ATOM    777  C   CYS A 131      34.982  28.535  27.147  1.00 11.67           C  
ATOM    778  O   CYS A 131      34.273  28.564  26.146  1.00 10.56           O  
ATOM    779  CB  CYS A 131      36.914  28.311  25.566  1.00 10.67           C  
ATOM    780  SG  CYS A 131      36.408  26.855  24.610  1.00 11.55           S  
ATOM    781  N   PRO A 132A     34.487  28.750  28.373  1.00 13.79           N  
ATOM    782  CA  PRO A 132A     33.061  29.003  28.611  1.00 13.93           C  
ATOM    783  C   PRO A 132A     32.527  30.275  27.959  1.00 13.81           C  
ATOM    784  O   PRO A 132A     31.323  30.426  27.779  1.00 13.95           O  
ATOM    785  CB  PRO A 132A     32.955  29.062  30.135  1.00 13.13           C  
ATOM    786  CG  PRO A 132A     34.330  29.441  30.592  1.00 14.08           C  
ATOM    787  CD  PRO A 132A     35.267  28.780  29.626  1.00 14.12           C  
ATOM    788  N   ASN A 132B     33.417  31.190  27.598  1.00 14.57           N  
ATOM    789  CA  ASN A 132B     32.968  32.438  26.995  1.00 15.97           C  
ATOM    790  C   ASN A 132B     33.167  32.492  25.494  1.00 13.24           C  
ATOM    791  O   ASN A 132B     32.952  33.529  24.872  1.00 13.67           O  
ATOM    792  CB  ASN A 132B     33.667  33.620  27.669  1.00 19.33           C  
ATOM    793  CG  ASN A 132B     33.435  33.648  29.176  1.00 25.11           C  
ATOM    794  OD1 ASN A 132B     34.344  33.943  29.956  1.00 28.20           O  
ATOM    795  ND2 ASN A 132B     32.209  33.330  29.592  1.00 25.49           N  
ATOM    796  N   ALA A 133      33.569  31.371  24.911  1.00 11.10           N  
ATOM    797  CA  ALA A 133      33.781  31.309  23.477  1.00  7.81           C  
ATOM    798  C   ALA A 133      32.437  31.329  22.766  1.00  9.94           C  
ATOM    799  O   ALA A 133      31.400  31.018  23.366  1.00  7.89           O  
ATOM    800  CB  ALA A 133      34.532  30.042  23.119  1.00  6.09           C  
ATOM    801  N   PHE A 134      32.459  31.716  21.493  1.00  9.58           N  
ATOM    802  CA  PHE A 134      31.256  31.739  20.666  1.00  8.11           C  
ATOM    803  C   PHE A 134      31.310  30.425  19.887  1.00  9.25           C  
ATOM    804  O   PHE A 134      32.316  30.124  19.238  1.00  6.97           O  
ATOM    805  CB  PHE A 134      31.284  32.930  19.707  1.00  9.93           C  
ATOM    806  CG  PHE A 134      30.036  33.073  18.891  1.00 12.39           C  
ATOM    807  CD1 PHE A 134      28.854  33.517  19.479  1.00 12.11           C  
ATOM    808  CD2 PHE A 134      30.028  32.736  17.539  1.00 11.93           C  
ATOM    809  CE1 PHE A 134      27.683  33.616  18.733  1.00 11.67           C  
ATOM    810  CE2 PHE A 134      28.862  32.832  16.788  1.00 11.11           C  
ATOM    811  CZ  PHE A 134      27.688  33.274  17.386  1.00 10.43           C  
ATOM    812  N   ILE A 135      30.234  29.646  19.956  1.00  7.24           N  
ATOM    813  CA  ILE A 135      30.192  28.346  19.299  1.00  6.18           C  
ATOM    814  C   ILE A 135      29.286  28.257  18.071  1.00  6.24           C  
ATOM    815  O   ILE A 135      28.163  28.761  18.069  1.00  4.61           O  
ATOM    816  CB  ILE A 135      29.739  27.243  20.296  1.00  6.29           C  
ATOM    817  CG1 ILE A 135      30.276  27.543  21.702  1.00  9.22           C  
ATOM    818  CG2 ILE A 135      30.173  25.874  19.796  1.00  3.33           C  
ATOM    819  CD1 ILE A 135      31.787  27.481  21.834  1.00 11.27           C  
ATOM    820  N   ILE A 136      29.795  27.603  17.030  1.00  8.03           N  
ATOM    821  CA  ILE A 136      29.060  27.382  15.791  1.00  6.62           C  
ATOM    822  C   ILE A 136      29.078  25.873  15.564  1.00  7.39           C  
ATOM    823  O   ILE A 136      30.143  25.264  15.466  1.00  6.70           O  
ATOM    824  CB  ILE A 136      29.733  28.076  14.586  1.00  6.62           C  
ATOM    825  CG1 ILE A 136      29.676  29.598  14.757  1.00  6.90           C  
ATOM    826  CG2 ILE A 136      29.035  27.662  13.301  1.00  4.23           C  
ATOM    827  CD1 ILE A 136      30.518  30.378  13.746  1.00  7.01           C  
ATOM    828  N   VAL A 137      27.898  25.267  15.492  1.00  5.76           N  
ATOM    829  CA  VAL A 137      27.805  23.823  15.303  1.00  6.97           C  
ATOM    830  C   VAL A 137      27.425  23.495  13.864  1.00  7.99           C  
ATOM    831  O   VAL A 137      26.551  24.137  13.288  1.00  8.39           O  
ATOM    832  CB  VAL A 137      26.762  23.217  16.274  1.00  5.24           C  
ATOM    833  CG1 VAL A 137      26.533  21.736  15.971  1.00  4.16           C  
ATOM    834  CG2 VAL A 137      27.240  23.403  17.699  1.00  4.08           C  
ATOM    835  N   VAL A 138      28.100  22.501  13.293  1.00  7.95           N  
ATOM    836  CA  VAL A 138      27.856  22.071  11.918  1.00  8.16           C  
ATOM    837  C   VAL A 138      27.353  20.621  11.880  1.00  7.43           C  
ATOM    838  O   VAL A 138      26.537  20.252  11.030  1.00  6.64           O  
ATOM    839  CB  VAL A 138      29.159  22.190  11.064  1.00  8.29           C  
ATOM    840  CG1 VAL A 138      28.858  21.890   9.601  1.00  5.94           C  
ATOM    841  CG2 VAL A 138      29.760  23.596  11.217  1.00  6.40           C  
ATOM    842  N   THR A 139      27.841  19.812  12.813  1.00  6.51           N  
ATOM    843  CA  THR A 139      27.461  18.406  12.916  1.00  9.21           C  
ATOM    844  C   THR A 139      25.973  18.178  12.676  1.00 11.99           C  
ATOM    845  O   THR A 139      25.129  18.836  13.290  1.00 11.70           O  
ATOM    846  CB  THR A 139      27.803  17.851  14.299  1.00  8.96           C  
ATOM    847  OG1 THR A 139      29.133  18.245  14.643  1.00 10.29           O  
ATOM    848  CG2 THR A 139      27.696  16.334  14.308  1.00  5.27           C  
ATOM    849  N   ASN A 140      25.658  17.230  11.801  1.00 15.11           N  
ATOM    850  CA  ASN A 140      24.266  16.922  11.479  1.00 18.04           C  
ATOM    851  C   ASN A 140      23.660  15.774  12.283  1.00 14.44           C  
ATOM    852  O   ASN A 140      24.355  14.831  12.658  1.00 13.51           O  
ATOM    853  CB  ASN A 140      24.126  16.601   9.989  1.00 26.31           C  
ATOM    854  CG  ASN A 140      24.995  15.438   9.557  1.00 37.49           C  
ATOM    855  OD1 ASN A 140      26.123  15.629   9.089  1.00 45.16           O  
ATOM    856  ND2 ASN A 140      24.475  14.217   9.706  1.00 42.92           N  
ATOM    857  N   PRO A 141      22.346  15.858  12.576  1.00 13.26           N  
ATOM    858  CA  PRO A 141      21.494  16.983  12.162  1.00 11.11           C  
ATOM    859  C   PRO A 141      21.805  18.199  13.033  1.00 10.31           C  
ATOM    860  O   PRO A 141      21.627  18.161  14.251  1.00  9.57           O  
ATOM    861  CB  PRO A 141      20.078  16.463  12.376  1.00 12.05           C  
ATOM    862  CG  PRO A 141      20.212  15.440  13.452  1.00 13.44           C  
ATOM    863  CD  PRO A 141      21.592  14.838  13.326  1.00 12.22           C  
ATOM    864  N   VAL A 142      22.263  19.270  12.397  1.00  9.37           N  
ATOM    865  CA  VAL A 142      22.659  20.487  13.095  1.00  8.95           C  
ATOM    866  C   VAL A 142      21.687  21.043  14.130  1.00  7.61           C  
ATOM    867  O   VAL A 142      22.101  21.421  15.227  1.00  8.40           O  
ATOM    868  CB  VAL A 142      22.996  21.606  12.081  1.00 10.03           C  
ATOM    869  CG1 VAL A 142      21.738  22.046  11.364  1.00 14.36           C  
ATOM    870  CG2 VAL A 142      23.636  22.783  12.791  1.00 12.36           C  
ATOM    871  N   ASP A 143      20.407  21.095  13.788  1.00  7.22           N  
ATOM    872  CA  ASP A 143      19.398  21.647  14.683  1.00  6.33           C  
ATOM    873  C   ASP A 143      19.273  20.851  15.967  1.00  8.01           C  
ATOM    874  O   ASP A 143      18.919  21.389  17.023  1.00  6.00           O  
ATOM    875  CB  ASP A 143      18.056  21.715  13.969  1.00  8.04           C  
ATOM    876  CG  ASP A 143      18.072  22.686  12.821  1.00  5.80           C  
ATOM    877  OD1 ASP A 143      18.068  23.905  13.079  1.00  8.24           O  
ATOM    878  OD2 ASP A 143      18.100  22.236  11.663  1.00  8.97           O  
ATOM    879  N   VAL A 144      19.564  19.563  15.872  1.00  7.25           N  
ATOM    880  CA  VAL A 144      19.518  18.703  17.033  1.00  6.90           C  
ATOM    881  C   VAL A 144      20.856  18.824  17.765  1.00  8.07           C  
ATOM    882  O   VAL A 144      20.898  19.145  18.952  1.00  8.77           O  
ATOM    883  CB  VAL A 144      19.292  17.235  16.621  1.00  7.87           C  
ATOM    884  CG1 VAL A 144      19.437  16.320  17.829  1.00  7.09           C  
ATOM    885  CG2 VAL A 144      17.913  17.086  15.994  1.00  4.77           C  
ATOM    886  N   MET A 145      21.943  18.592  17.037  1.00  7.42           N  
ATOM    887  CA  MET A 145      23.286  18.634  17.605  1.00  8.52           C  
ATOM    888  C   MET A 145      23.650  19.949  18.291  1.00  8.47           C  
ATOM    889  O   MET A 145      24.393  19.955  19.272  1.00  7.25           O  
ATOM    890  CB  MET A 145      24.319  18.319  16.518  1.00  7.92           C  
ATOM    891  CG  MET A 145      24.311  16.865  16.064  1.00  9.63           C  
ATOM    892  SD  MET A 145      24.571  15.704  17.411  1.00 11.50           S  
ATOM    893  CE  MET A 145      23.387  14.422  16.985  1.00  9.35           C  
ATOM    894  N   VAL A 146      23.118  21.059  17.790  1.00  7.57           N  
ATOM    895  CA  VAL A 146      23.429  22.354  18.370  1.00  6.90           C  
ATOM    896  C   VAL A 146      22.832  22.523  19.759  1.00  8.57           C  
ATOM    897  O   VAL A 146      23.485  23.069  20.654  1.00  6.49           O  
ATOM    898  CB  VAL A 146      22.954  23.512  17.461  1.00  7.10           C  
ATOM    899  CG1 VAL A 146      21.437  23.625  17.492  1.00  4.08           C  
ATOM    900  CG2 VAL A 146      23.609  24.817  17.913  1.00  3.20           C  
ATOM    901  N   GLN A 147      21.598  22.057  19.942  1.00  9.12           N  
ATOM    902  CA  GLN A 147      20.949  22.168  21.245  1.00  9.68           C  
ATOM    903  C   GLN A 147      21.633  21.235  22.233  1.00  8.19           C  
ATOM    904  O   GLN A 147      21.777  21.570  23.401  1.00  7.60           O  
ATOM    905  CB  GLN A 147      19.467  21.804  21.157  1.00  9.26           C  
ATOM    906  CG  GLN A 147      18.793  21.727  22.525  1.00  8.89           C  
ATOM    907  CD  GLN A 147      17.289  21.932  22.455  1.00 10.32           C  
ATOM    908  OE1 GLN A 147      16.597  21.303  21.652  1.00 11.56           O  
ATOM    909  NE2 GLN A 147      16.776  22.816  23.298  1.00  9.29           N  
ATOM    910  N   LEU A 148      22.043  20.065  21.754  1.00  7.86           N  
ATOM    911  CA  LEU A 148      22.725  19.096  22.605  1.00  8.71           C  
ATOM    912  C   LEU A 148      24.022  19.715  23.143  1.00 10.84           C  
ATOM    913  O   LEU A 148      24.305  19.658  24.344  1.00 10.88           O  
ATOM    914  CB  LEU A 148      23.027  17.817  21.811  1.00 10.10           C  
ATOM    915  CG  LEU A 148      21.796  16.994  21.389  1.00 10.60           C  
ATOM    916  CD1 LEU A 148      22.222  15.815  20.528  1.00  8.81           C  
ATOM    917  CD2 LEU A 148      21.061  16.506  22.624  1.00  8.38           C  
ATOM    918  N   LEU A 149      24.802  20.325  22.262  1.00  9.14           N  
ATOM    919  CA  LEU A 149      26.046  20.944  22.689  1.00  9.70           C  
ATOM    920  C   LEU A 149      25.759  22.133  23.596  1.00  8.63           C  
ATOM    921  O   LEU A 149      26.495  22.402  24.542  1.00 12.77           O  
ATOM    922  CB  LEU A 149      26.865  21.399  21.475  1.00 10.02           C  
ATOM    923  CG  LEU A 149      28.238  21.984  21.817  1.00 10.46           C  
ATOM    924  CD1 LEU A 149      29.031  20.996  22.668  1.00  7.80           C  
ATOM    925  CD2 LEU A 149      28.985  22.292  20.539  1.00  9.37           C  
ATOM    926  N   HIS A 150      24.688  22.855  23.304  1.00  8.66           N  
ATOM    927  CA  HIS A 150      24.326  24.002  24.124  1.00  7.64           C  
ATOM    928  C   HIS A 150      24.131  23.490  25.555  1.00  9.06           C  
ATOM    929  O   HIS A 150      24.648  24.067  26.515  1.00  7.49           O  
ATOM    930  CB  HIS A 150      23.030  24.633  23.591  1.00  7.24           C  
ATOM    931  CG  HIS A 150      22.484  25.726  24.455  1.00  6.82           C  
ATOM    932  ND1 HIS A 150      21.157  25.787  24.825  1.00  7.06           N  
ATOM    933  CD2 HIS A 150      23.084  26.793  25.034  1.00  5.79           C  
ATOM    934  CE1 HIS A 150      20.965  26.842  25.596  1.00  6.87           C  
ATOM    935  NE2 HIS A 150      22.119  27.471  25.740  1.00  5.67           N  
ATOM    936  N   GLN A 151      23.411  22.380  25.679  1.00  9.43           N  
ATOM    937  CA  GLN A 151      23.130  21.781  26.979  1.00 13.18           C  
ATOM    938  C   GLN A 151      24.362  21.244  27.706  1.00 12.89           C  
ATOM    939  O   GLN A 151      24.522  21.465  28.904  1.00 13.90           O  
ATOM    940  CB  GLN A 151      22.105  20.658  26.818  1.00 13.92           C  
ATOM    941  CG  GLN A 151      20.686  21.086  27.158  1.00 20.56           C  
ATOM    942  CD  GLN A 151      19.633  20.460  26.260  1.00 22.15           C  
ATOM    943  OE1 GLN A 151      18.624  21.092  25.947  1.00 25.36           O  
ATOM    944  NE2 GLN A 151      19.856  19.215  25.848  1.00 22.77           N  
ATOM    945  N   HIS A 152      25.229  20.546  26.981  1.00 11.79           N  
ATOM    946  CA  HIS A 152      26.429  19.968  27.579  1.00 13.41           C  
ATOM    947  C   HIS A 152      27.533  20.982  27.867  1.00 13.16           C  
ATOM    948  O   HIS A 152      28.347  20.776  28.769  1.00 13.60           O  
ATOM    949  CB  HIS A 152      26.994  18.877  26.669  1.00 13.17           C  
ATOM    950  CG  HIS A 152      25.977  17.879  26.214  1.00 14.37           C  
ATOM    951  ND1 HIS A 152      25.012  17.363  27.052  1.00 16.14           N  
ATOM    952  CD2 HIS A 152      25.789  17.282  25.013  1.00 14.73           C  
ATOM    953  CE1 HIS A 152      24.274  16.492  26.389  1.00 15.79           C  
ATOM    954  NE2 HIS A 152      24.726  16.424  25.148  1.00 16.22           N  
ATOM    955  N   SER A 153      27.564  22.069  27.100  1.00 11.26           N  
ATOM    956  CA  SER A 153      28.594  23.088  27.270  1.00 10.07           C  
ATOM    957  C   SER A 153      28.208  24.152  28.286  1.00 10.11           C  
ATOM    958  O   SER A 153      29.074  24.768  28.909  1.00 10.88           O  
ATOM    959  CB  SER A 153      28.907  23.749  25.925  1.00  7.27           C  
ATOM    960  OG  SER A 153      27.841  24.584  25.509  1.00  8.04           O  
ATOM    961  N   GLY A 154      26.908  24.371  28.442  1.00 10.60           N  
ATOM    962  CA  GLY A 154      26.429  25.362  29.388  1.00  9.64           C  
ATOM    963  C   GLY A 154      26.611  26.822  29.000  1.00  9.17           C  
ATOM    964  O   GLY A 154      26.388  27.700  29.830  1.00 11.03           O  
ATOM    965  N   VAL A 155      27.012  27.103  27.762  1.00  7.98           N  
ATOM    966  CA  VAL A 155      27.199  28.496  27.345  1.00  8.82           C  
ATOM    967  C   VAL A 155      25.850  29.211  27.217  1.00  8.85           C  
ATOM    968  O   VAL A 155      24.806  28.568  27.067  1.00  7.77           O  
ATOM    969  CB  VAL A 155      27.952  28.597  25.988  1.00  8.56           C  
ATOM    970  CG1 VAL A 155      29.303  27.908  26.085  1.00  7.80           C  
ATOM    971  CG2 VAL A 155      27.119  27.984  24.879  1.00  5.74           C  
ATOM    972  N   PRO A 156      25.850  30.552  27.306  1.00  9.54           N  
ATOM    973  CA  PRO A 156      24.584  31.285  27.184  1.00 10.01           C  
ATOM    974  C   PRO A 156      23.950  31.039  25.817  1.00 10.76           C  
ATOM    975  O   PRO A 156      24.645  30.701  24.853  1.00  8.86           O  
ATOM    976  CB  PRO A 156      24.986  32.749  27.379  1.00 10.05           C  
ATOM    977  CG  PRO A 156      26.323  32.698  28.063  1.00  8.98           C  
ATOM    978  CD  PRO A 156      26.989  31.454  27.547  1.00  8.28           C  
ATOM    979  N   LYS A 157      22.633  31.209  25.739  1.00 10.71           N  
ATOM    980  CA  LYS A 157      21.892  30.990  24.495  1.00 11.16           C  
ATOM    981  C   LYS A 157      22.354  31.877  23.333  1.00 10.09           C  
ATOM    982  O   LYS A 157      22.272  31.484  22.175  1.00 10.51           O  
ATOM    983  CB  LYS A 157      20.390  31.210  24.738  1.00 11.11           C  
ATOM    984  CG  LYS A 157      19.994  32.668  24.977  1.00 15.37           C  
ATOM    985  CD  LYS A 157      18.527  32.926  24.620  1.00 22.65           C  
ATOM    986  CE  LYS A 157      18.301  34.334  24.036  1.00 26.72           C  
ATOM    987  NZ  LYS A 157      18.359  34.394  22.530  1.00 23.66           N  
ATOM    988  N   ASN A 158      22.841  33.069  23.649  1.00  9.54           N  
ATOM    989  CA  ASN A 158      23.294  34.015  22.631  1.00  9.55           C  
ATOM    990  C   ASN A 158      24.711  33.738  22.142  1.00  9.47           C  
ATOM    991  O   ASN A 158      25.229  34.473  21.299  1.00  6.97           O  
ATOM    992  CB  ASN A 158      23.237  35.439  23.191  1.00 10.78           C  
ATOM    993  CG  ASN A 158      24.278  35.680  24.283  1.00 15.09           C  
ATOM    994  OD1 ASN A 158      24.264  35.024  25.330  1.00 15.45           O  
ATOM    995  ND2 ASN A 158      25.187  36.619  24.040  1.00 16.06           N  
ATOM    996  N   LYS A 159      25.336  32.684  22.664  1.00  9.65           N  
ATOM    997  CA  LYS A 159      26.711  32.360  22.286  1.00  8.04           C  
ATOM    998  C   LYS A 159      26.888  31.051  21.530  1.00  7.33           C  
ATOM    999  O   LYS A 159      28.007  30.546  21.415  1.00  6.13           O  
ATOM   1000  CB  LYS A 159      27.610  32.351  23.533  1.00  7.27           C  
ATOM   1001  CG  LYS A 159      27.714  33.700  24.241  1.00  9.47           C  
ATOM   1002  CD  LYS A 159      28.557  34.699  23.440  1.00 10.32           C  
ATOM   1003  CE  LYS A 159      30.036  34.344  23.508  1.00 10.92           C  
ATOM   1004  NZ  LYS A 159      30.636  34.796  24.799  1.00 12.47           N  
ATOM   1005  N   ILE A 160      25.797  30.494  21.020  1.00  6.49           N  
ATOM   1006  CA  ILE A 160      25.898  29.257  20.264  1.00  7.57           C  
ATOM   1007  C   ILE A 160      24.829  29.189  19.181  1.00  8.95           C  
ATOM   1008  O   ILE A 160      23.652  29.422  19.448  1.00  9.34           O  
ATOM   1009  CB  ILE A 160      25.784  28.010  21.185  1.00  8.25           C  
ATOM   1010  CG1 ILE A 160      25.826  26.733  20.338  1.00  8.88           C  
ATOM   1011  CG2 ILE A 160      24.503  28.084  22.002  1.00  6.65           C  
ATOM   1012  CD1 ILE A 160      26.259  25.483  21.087  1.00  9.06           C  
ATOM   1013  N   ILE A 161      25.254  28.883  17.957  1.00  6.61           N  
ATOM   1014  CA  ILE A 161      24.342  28.772  16.827  1.00  6.06           C  
ATOM   1015  C   ILE A 161      24.750  27.602  15.945  1.00  6.25           C  
ATOM   1016  O   ILE A 161      25.848  27.064  16.080  1.00  5.30           O  
ATOM   1017  CB  ILE A 161      24.359  30.042  15.962  1.00  6.19           C  
ATOM   1018  CG1 ILE A 161      25.792  30.336  15.501  1.00  3.28           C  
ATOM   1019  CG2 ILE A 161      23.755  31.196  16.733  1.00  5.53           C  
ATOM   1020  CD1 ILE A 161      25.925  31.581  14.645  1.00  4.26           C  
ATOM   1021  N   GLY A 162      23.857  27.207  15.046  1.00  6.65           N  
ATOM   1022  CA  GLY A 162      24.166  26.113  14.143  1.00  6.67           C  
ATOM   1023  C   GLY A 162      24.110  26.594  12.706  1.00  7.48           C  
ATOM   1024  O   GLY A 162      23.355  27.512  12.387  1.00  8.50           O  
ATOM   1025  N   LEU A 163      24.913  25.986  11.838  1.00  6.77           N  
ATOM   1026  CA  LEU A 163      24.931  26.359  10.433  1.00  8.33           C  
ATOM   1027  C   LEU A 163      23.668  25.832   9.779  1.00  7.61           C  
ATOM   1028  O   LEU A 163      23.278  24.696  10.022  1.00  8.26           O  
ATOM   1029  CB  LEU A 163      26.145  25.748   9.723  1.00  6.32           C  
ATOM   1030  CG  LEU A 163      26.100  25.828   8.191  1.00  8.02           C  
ATOM   1031  CD1 LEU A 163      26.359  27.264   7.766  1.00  9.33           C  
ATOM   1032  CD2 LEU A 163      27.129  24.901   7.570  1.00  5.86           C  
ATOM   1033  N   GLY A 164      23.030  26.657   8.955  1.00  8.28           N  
ATOM   1034  CA  GLY A 164      21.825  26.224   8.274  1.00  7.16           C  
ATOM   1035  C   GLY A 164      21.415  27.139   7.134  1.00  9.43           C  
ATOM   1036  O   GLY A 164      21.821  26.944   5.983  1.00  8.78           O  
ATOM   1037  N   GLY A 165      20.620  28.153   7.468  1.00  8.35           N  
ATOM   1038  CA  GLY A 165      20.117  29.095   6.481  1.00  5.14           C  
ATOM   1039  C   GLY A 165      21.094  29.786   5.550  1.00  4.23           C  
ATOM   1040  O   GLY A 165      20.776  30.001   4.380  1.00  5.19           O  
ATOM   1041  N   VAL A 166      22.270  30.160   6.044  1.00  4.70           N  
ATOM   1042  CA  VAL A 166      23.230  30.830   5.182  1.00  4.93           C  
ATOM   1043  C   VAL A 166      23.627  29.911   4.027  1.00  6.71           C  
ATOM   1044  O   VAL A 166      23.690  30.337   2.874  1.00  7.11           O  
ATOM   1045  CB  VAL A 166      24.488  31.256   5.963  1.00  6.11           C  
ATOM   1046  CG1 VAL A 166      25.519  31.868   5.007  1.00  3.97           C  
ATOM   1047  CG2 VAL A 166      24.101  32.273   7.037  1.00  2.64           C  
ATOM   1048  N   LEU A 167      23.879  28.645   4.336  1.00  6.17           N  
ATOM   1049  CA  LEU A 167      24.264  27.682   3.311  1.00  6.61           C  
ATOM   1050  C   LEU A 167      23.095  27.351   2.382  1.00  6.94           C  
ATOM   1051  O   LEU A 167      23.223  27.430   1.159  1.00  8.87           O  
ATOM   1052  CB  LEU A 167      24.789  26.397   3.967  1.00  6.59           C  
ATOM   1053  CG  LEU A 167      24.970  25.177   3.060  1.00  4.88           C  
ATOM   1054  CD1 LEU A 167      26.031  25.466   2.010  1.00  4.00           C  
ATOM   1055  CD2 LEU A 167      25.357  23.980   3.894  1.00  2.00           C  
ATOM   1056  N   ASP A 168      21.959  26.986   2.966  1.00  7.01           N  
ATOM   1057  CA  ASP A 168      20.781  26.640   2.183  1.00  6.19           C  
ATOM   1058  C   ASP A 168      20.329  27.778   1.262  1.00  5.29           C  
ATOM   1059  O   ASP A 168      20.032  27.543   0.089  1.00  5.25           O  
ATOM   1060  CB  ASP A 168      19.625  26.233   3.112  1.00  5.77           C  
ATOM   1061  CG  ASP A 168      19.874  24.903   3.807  1.00  8.83           C  
ATOM   1062  OD1 ASP A 168      20.545  24.037   3.207  1.00  8.94           O  
ATOM   1063  OD2 ASP A 168      19.402  24.723   4.950  1.00  8.36           O  
ATOM   1064  N   THR A 169      20.271  29.004   1.777  1.00  4.28           N  
ATOM   1065  CA  THR A 169      19.838  30.123   0.940  1.00  5.83           C  
ATOM   1066  C   THR A 169      20.870  30.533  -0.101  1.00  5.97           C  
ATOM   1067  O   THR A 169      20.516  31.129  -1.116  1.00  7.19           O  
ATOM   1068  CB  THR A 169      19.455  31.390   1.762  1.00  4.75           C  
ATOM   1069  OG1 THR A 169      20.612  31.918   2.417  1.00  3.85           O  
ATOM   1070  CG2 THR A 169      18.376  31.065   2.778  1.00  2.84           C  
ATOM   1071  N   SER A 170      22.142  30.223   0.135  1.00  6.46           N  
ATOM   1072  CA  SER A 170      23.167  30.576  -0.843  1.00  7.62           C  
ATOM   1073  C   SER A 170      22.869  29.838  -2.151  1.00  8.13           C  
ATOM   1074  O   SER A 170      23.153  30.338  -3.241  1.00  8.53           O  
ATOM   1075  CB  SER A 170      24.570  30.214  -0.324  1.00  7.75           C  
ATOM   1076  OG  SER A 170      24.815  28.813  -0.363  1.00  9.46           O  
ATOM   1077  N   ARG A 171      22.281  28.650  -2.038  1.00  8.34           N  
ATOM   1078  CA  ARG A 171      21.947  27.856  -3.215  1.00  7.48           C  
ATOM   1079  C   ARG A 171      20.789  28.507  -3.951  1.00  8.62           C  
ATOM   1080  O   ARG A 171      20.852  28.717  -5.165  1.00  7.91           O  
ATOM   1081  CB  ARG A 171      21.550  26.433  -2.810  1.00  8.39           C  
ATOM   1082  CG  ARG A 171      22.717  25.464  -2.718  1.00  8.71           C  
ATOM   1083  CD  ARG A 171      23.192  25.328  -1.291  1.00  8.02           C  
ATOM   1084  NE  ARG A 171      24.297  24.384  -1.163  1.00  5.49           N  
ATOM   1085  CZ  ARG A 171      24.293  23.342  -0.342  1.00  3.80           C  
ATOM   1086  NH1 ARG A 171      23.236  23.104   0.425  1.00  3.70           N  
ATOM   1087  NH2 ARG A 171      25.354  22.550  -0.271  1.00  6.17           N  
ATOM   1088  N   LEU A 172      19.733  28.824  -3.202  1.00  6.97           N  
ATOM   1089  CA  LEU A 172      18.549  29.451  -3.766  1.00  6.54           C  
ATOM   1090  C   LEU A 172      18.881  30.821  -4.349  1.00  7.17           C  
ATOM   1091  O   LEU A 172      18.433  31.164  -5.446  1.00  6.72           O  
ATOM   1092  CB  LEU A 172      17.461  29.579  -2.691  1.00  6.52           C  
ATOM   1093  CG  LEU A 172      16.158  30.306  -3.043  1.00  6.52           C  
ATOM   1094  CD1 LEU A 172      15.465  29.622  -4.211  1.00  4.76           C  
ATOM   1095  CD2 LEU A 172      15.256  30.319  -1.822  1.00  4.77           C  
ATOM   1096  N   LYS A 173      19.668  31.606  -3.621  1.00  6.98           N  
ATOM   1097  CA  LYS A 173      20.051  32.928  -4.103  1.00  7.43           C  
ATOM   1098  C   LYS A 173      20.863  32.792  -5.389  1.00  7.93           C  
ATOM   1099  O   LYS A 173      20.654  33.540  -6.346  1.00  9.57           O  
ATOM   1100  CB  LYS A 173      20.893  33.661  -3.057  1.00  6.63           C  
ATOM   1101  CG  LYS A 173      20.142  34.068  -1.790  1.00  4.40           C  
ATOM   1102  CD  LYS A 173      21.137  34.333  -0.665  1.00  2.15           C  
ATOM   1103  CE  LYS A 173      20.468  34.865   0.588  1.00  2.00           C  
ATOM   1104  NZ  LYS A 173      21.412  34.785   1.738  1.00  3.15           N  
ATOM   1105  N   TYR A 174      21.783  31.830  -5.414  1.00  6.22           N  
ATOM   1106  CA  TYR A 174      22.617  31.636  -6.590  1.00  7.79           C  
ATOM   1107  C   TYR A 174      21.860  31.171  -7.832  1.00  7.44           C  
ATOM   1108  O   TYR A 174      22.053  31.716  -8.918  1.00  7.26           O  
ATOM   1109  CB  TYR A 174      23.754  30.648  -6.298  1.00  7.59           C  
ATOM   1110  CG  TYR A 174      24.756  30.589  -7.426  1.00  8.62           C  
ATOM   1111  CD1 TYR A 174      25.658  31.633  -7.634  1.00  8.23           C  
ATOM   1112  CD2 TYR A 174      24.742  29.538  -8.343  1.00  9.68           C  
ATOM   1113  CE1 TYR A 174      26.514  31.637  -8.729  1.00 10.40           C  
ATOM   1114  CE2 TYR A 174      25.597  29.531  -9.443  1.00  8.79           C  
ATOM   1115  CZ  TYR A 174      26.476  30.583  -9.632  1.00 10.23           C  
ATOM   1116  OH  TYR A 174      27.303  30.592 -10.732  1.00 13.34           O  
ATOM   1117  N   TYR A 175      21.009  30.164  -7.687  1.00  7.04           N  
ATOM   1118  CA  TYR A 175      20.265  29.666  -8.836  1.00  8.30           C  
ATOM   1119  C   TYR A 175      19.361  30.745  -9.433  1.00  7.93           C  
ATOM   1120  O   TYR A 175      19.249  30.861 -10.654  1.00  6.21           O  
ATOM   1121  CB  TYR A 175      19.425  28.445  -8.448  1.00  8.22           C  
ATOM   1122  CG  TYR A 175      20.233  27.249  -7.981  1.00 13.14           C  
ATOM   1123  CD1 TYR A 175      21.493  26.963  -8.524  1.00 10.39           C  
ATOM   1124  CD2 TYR A 175      19.742  26.410  -6.976  1.00 12.67           C  
ATOM   1125  CE1 TYR A 175      22.240  25.871  -8.067  1.00 10.05           C  
ATOM   1126  CE2 TYR A 175      20.480  25.322  -6.517  1.00 12.05           C  
ATOM   1127  CZ  TYR A 175      21.723  25.062  -7.062  1.00 10.71           C  
ATOM   1128  OH  TYR A 175      22.445  23.999  -6.575  1.00 12.76           O  
ATOM   1129  N   ILE A 176      18.718  31.535  -8.579  1.00  6.61           N  
ATOM   1130  CA  ILE A 176      17.835  32.594  -9.066  1.00  8.21           C  
ATOM   1131  C   ILE A 176      18.628  33.694  -9.773  1.00  8.33           C  
ATOM   1132  O   ILE A 176      18.177  34.244 -10.777  1.00  8.52           O  
ATOM   1133  CB  ILE A 176      17.014  33.236  -7.914  1.00  7.23           C  
ATOM   1134  CG1 ILE A 176      15.969  32.240  -7.397  1.00  8.45           C  
ATOM   1135  CG2 ILE A 176      16.317  34.491  -8.408  1.00  4.46           C  
ATOM   1136  CD1 ILE A 176      15.182  32.737  -6.206  1.00  7.52           C  
ATOM   1137  N   SER A 177      19.808  34.009  -9.245  1.00  7.66           N  
ATOM   1138  CA  SER A 177      20.645  35.052  -9.821  1.00  6.95           C  
ATOM   1139  C   SER A 177      21.105  34.714 -11.236  1.00  8.99           C  
ATOM   1140  O   SER A 177      21.288  35.604 -12.066  1.00  9.00           O  
ATOM   1141  CB  SER A 177      21.869  35.286  -8.939  1.00  7.13           C  
ATOM   1142  OG  SER A 177      22.824  34.253  -9.114  1.00  8.44           O  
ATOM   1143  N   GLN A 178      21.294  33.430 -11.509  1.00 10.29           N  
ATOM   1144  CA  GLN A 178      21.748  33.001 -12.821  1.00 11.91           C  
ATOM   1145  C   GLN A 178      20.629  33.077 -13.846  1.00 12.52           C  
ATOM   1146  O   GLN A 178      20.869  33.385 -15.012  1.00 13.63           O  
ATOM   1147  CB  GLN A 178      22.313  31.585 -12.738  1.00 14.00           C  
ATOM   1148  CG  GLN A 178      23.580  31.514 -11.904  1.00 16.17           C  
ATOM   1149  CD  GLN A 178      24.587  32.592 -12.285  1.00 22.10           C  
ATOM   1150  OE1 GLN A 178      25.374  32.417 -13.219  1.00 24.36           O  
ATOM   1151  NE2 GLN A 178      24.569  33.715 -11.562  1.00 18.51           N  
ATOM   1152  N   LYS A 179      19.412  32.798 -13.407  1.00 12.51           N  
ATOM   1153  CA  LYS A 179      18.248  32.861 -14.280  1.00 13.65           C  
ATOM   1154  C   LYS A 179      17.973  34.327 -14.618  1.00 12.40           C  
ATOM   1155  O   LYS A 179      17.599  34.655 -15.741  1.00 12.01           O  
ATOM   1156  CB  LYS A 179      17.011  32.268 -13.579  1.00 15.75           C  
ATOM   1157  CG  LYS A 179      16.988  30.750 -13.497  1.00 22.36           C  
ATOM   1158  CD  LYS A 179      16.134  30.159 -14.606  1.00 26.99           C  
ATOM   1159  CE  LYS A 179      16.191  28.635 -14.615  1.00 29.47           C  
ATOM   1160  NZ  LYS A 179      15.594  28.090 -15.877  1.00 29.92           N  
ATOM   1161  N   LEU A 180      18.176  35.207 -13.643  1.00  9.97           N  
ATOM   1162  CA  LEU A 180      17.904  36.628 -13.836  1.00  9.40           C  
ATOM   1163  C   LEU A 180      19.101  37.446 -14.292  1.00  8.57           C  
ATOM   1164  O   LEU A 180      18.970  38.629 -14.600  1.00  9.17           O  
ATOM   1165  CB  LEU A 180      17.333  37.220 -12.546  1.00  7.75           C  
ATOM   1166  CG  LEU A 180      15.961  36.654 -12.169  1.00  8.90           C  
ATOM   1167  CD1 LEU A 180      15.528  37.211 -10.829  1.00  8.11           C  
ATOM   1168  CD2 LEU A 180      14.950  37.009 -13.250  1.00  6.05           C  
ATOM   1169  N   ASN A 181      20.264  36.814 -14.342  1.00  8.80           N  
ATOM   1170  CA  ASN A 181      21.489  37.484 -14.764  1.00  8.98           C  
ATOM   1171  C   ASN A 181      21.837  38.711 -13.933  1.00  7.66           C  
ATOM   1172  O   ASN A 181      22.044  39.804 -14.464  1.00  6.54           O  
ATOM   1173  CB  ASN A 181      21.396  37.862 -16.240  1.00 10.12           C  
ATOM   1174  CG  ASN A 181      21.091  36.672 -17.115  1.00 15.81           C  
ATOM   1175  OD1 ASN A 181      20.030  36.599 -17.741  1.00 21.79           O  
ATOM   1176  ND2 ASN A 181      22.014  35.718 -17.154  1.00 13.92           N  
ATOM   1177  N   VAL A 182      21.888  38.527 -12.621  1.00  5.93           N  
ATOM   1178  CA  VAL A 182      22.252  39.610 -11.723  1.00  5.97           C  
ATOM   1179  C   VAL A 182      23.279  39.053 -10.748  1.00  6.64           C  
ATOM   1180  O   VAL A 182      23.451  37.834 -10.654  1.00  6.26           O  
ATOM   1181  CB  VAL A 182      21.038  40.139 -10.925  1.00  8.05           C  
ATOM   1182  CG1 VAL A 182      20.034  40.775 -11.865  1.00  5.26           C  
ATOM   1183  CG2 VAL A 182      20.398  39.008 -10.135  1.00  7.87           C  
ATOM   1184  N   CYS A 183      23.970  39.943 -10.048  1.00  5.79           N  
ATOM   1185  CA  CYS A 183      24.969  39.544  -9.061  1.00  8.24           C  
ATOM   1186  C   CYS A 183      24.302  38.601  -8.057  1.00  6.36           C  
ATOM   1187  O   CYS A 183      23.235  38.904  -7.535  1.00  6.45           O  
ATOM   1188  CB  CYS A 183      25.498  40.782  -8.331  1.00  9.40           C  
ATOM   1189  SG  CYS A 183      26.918  40.487  -7.263  1.00 13.45           S  
ATOM   1190  N   PRO A 184      24.918  37.439  -7.786  1.00  6.30           N  
ATOM   1191  CA  PRO A 184      24.353  36.470  -6.838  1.00  6.59           C  
ATOM   1192  C   PRO A 184      23.924  37.062  -5.492  1.00  7.59           C  
ATOM   1193  O   PRO A 184      22.852  36.734  -4.976  1.00  8.20           O  
ATOM   1194  CB  PRO A 184      25.464  35.430  -6.683  1.00  4.36           C  
ATOM   1195  CG  PRO A 184      26.207  35.495  -7.974  1.00  6.54           C  
ATOM   1196  CD  PRO A 184      26.169  36.948  -8.390  1.00  8.00           C  
ATOM   1197  N   ARG A 185      24.762  37.930  -4.932  1.00  7.98           N  
ATOM   1198  CA  ARG A 185      24.479  38.565  -3.645  1.00  9.72           C  
ATOM   1199  C   ARG A 185      23.270  39.507  -3.696  1.00 10.06           C  
ATOM   1200  O   ARG A 185      22.686  39.836  -2.660  1.00  9.06           O  
ATOM   1201  CB  ARG A 185      25.719  39.338  -3.161  1.00  9.18           C  
ATOM   1202  CG  ARG A 185      25.590  39.929  -1.757  1.00 11.10           C  
ATOM   1203  CD  ARG A 185      25.900  38.896  -0.707  1.00  9.86           C  
ATOM   1204  NE  ARG A 185      25.786  39.414   0.651  1.00 10.14           N  
ATOM   1205  CZ  ARG A 185      26.242  38.767   1.719  1.00 10.78           C  
ATOM   1206  NH1 ARG A 185      26.842  37.596   1.564  1.00  7.74           N  
ATOM   1207  NH2 ARG A 185      26.095  39.278   2.934  1.00 11.15           N  
ATOM   1208  N   ASP A 186      22.890  39.936  -4.896  1.00  8.23           N  
ATOM   1209  CA  ASP A 186      21.756  40.839  -5.041  1.00  8.90           C  
ATOM   1210  C   ASP A 186      20.415  40.140  -4.839  1.00  9.08           C  
ATOM   1211  O   ASP A 186      19.377  40.795  -4.704  1.00 10.27           O  
ATOM   1212  CB  ASP A 186      21.797  41.513  -6.412  1.00  9.93           C  
ATOM   1213  CG  ASP A 186      22.616  42.781  -6.401  1.00 10.94           C  
ATOM   1214  OD1 ASP A 186      22.860  43.312  -5.300  1.00 15.29           O  
ATOM   1215  OD2 ASP A 186      23.019  43.248  -7.485  1.00 12.65           O  
ATOM   1216  N   VAL A 187      20.429  38.812  -4.829  1.00  7.52           N  
ATOM   1217  CA  VAL A 187      19.198  38.059  -4.604  1.00  8.99           C  
ATOM   1218  C   VAL A 187      19.158  37.699  -3.123  1.00  8.68           C  
ATOM   1219  O   VAL A 187      20.110  37.119  -2.605  1.00 10.84           O  
ATOM   1220  CB  VAL A 187      19.162  36.739  -5.418  1.00  7.61           C  
ATOM   1221  CG1 VAL A 187      17.958  35.897  -4.993  1.00  5.01           C  
ATOM   1222  CG2 VAL A 187      19.104  37.039  -6.898  1.00  7.30           C  
ATOM   1223  N   ASN A 188      18.081  38.051  -2.431  1.00  6.76           N  
ATOM   1224  CA  ASN A 188      17.995  37.695  -1.022  1.00  8.36           C  
ATOM   1225  C   ASN A 188      16.820  36.746  -0.848  1.00  9.31           C  
ATOM   1226  O   ASN A 188      15.787  36.893  -1.503  1.00  8.70           O  
ATOM   1227  CB  ASN A 188      17.833  38.938  -0.133  1.00  9.36           C  
ATOM   1228  CG  ASN A 188      18.541  38.784   1.215  1.00 12.38           C  
ATOM   1229  OD1 ASN A 188      18.766  37.668   1.686  1.00 11.80           O  
ATOM   1230  ND2 ASN A 188      18.895  39.909   1.833  1.00  8.61           N  
ATOM   1231  N   ALA A 189      16.988  35.762   0.027  1.00  7.87           N  
ATOM   1232  CA  ALA A 189      15.952  34.769   0.250  1.00  7.69           C  
ATOM   1233  C   ALA A 189      16.003  34.270   1.680  1.00  8.94           C  
ATOM   1234  O   ALA A 189      17.001  34.458   2.379  1.00  8.76           O  
ATOM   1235  CB  ALA A 189      16.145  33.610  -0.714  1.00  8.67           C  
ATOM   1236  N   HIS A 190      14.923  33.625   2.110  1.00  8.28           N  
ATOM   1237  CA  HIS A 190      14.847  33.101   3.464  1.00  9.59           C  
ATOM   1238  C   HIS A 190      14.391  31.651   3.513  1.00  8.59           C  
ATOM   1239  O   HIS A 190      13.335  31.304   2.981  1.00  9.60           O  
ATOM   1240  CB  HIS A 190      13.888  33.953   4.301  1.00 11.49           C  
ATOM   1241  CG  HIS A 190      14.462  35.269   4.719  1.00 13.70           C  
ATOM   1242  ND1 HIS A 190      14.563  36.343   3.860  1.00 13.41           N  
ATOM   1243  CD2 HIS A 190      15.005  35.672   5.893  1.00 13.35           C  
ATOM   1244  CE1 HIS A 190      15.146  37.351   4.486  1.00 12.76           C  
ATOM   1245  NE2 HIS A 190      15.424  36.970   5.721  1.00 16.71           N  
ATOM   1246  N   ILE A 191      15.202  30.808   4.142  1.00  5.77           N  
ATOM   1247  CA  ILE A 191      14.880  29.395   4.329  1.00  5.73           C  
ATOM   1248  C   ILE A 191      14.977  29.203   5.844  1.00  8.36           C  
ATOM   1249  O   ILE A 191      16.021  29.464   6.449  1.00  8.87           O  
ATOM   1250  CB  ILE A 191      15.880  28.474   3.594  1.00  4.37           C  
ATOM   1251  CG1 ILE A 191      15.619  28.545   2.089  1.00  4.88           C  
ATOM   1252  CG2 ILE A 191      15.710  27.034   4.052  1.00  2.37           C  
ATOM   1253  CD1 ILE A 191      16.731  27.964   1.233  1.00  5.00           C  
ATOM   1254  N   VAL A 192      13.888  28.759   6.457  1.00  7.21           N  
ATOM   1255  CA  VAL A 192      13.854  28.621   7.903  1.00  8.77           C  
ATOM   1256  C   VAL A 192      13.377  27.275   8.445  1.00  9.31           C  
ATOM   1257  O   VAL A 192      13.188  26.316   7.692  1.00  8.16           O  
ATOM   1258  CB  VAL A 192      12.965  29.731   8.494  1.00  8.82           C  
ATOM   1259  CG1 VAL A 192      13.428  31.090   7.979  1.00  8.53           C  
ATOM   1260  CG2 VAL A 192      11.516  29.501   8.089  1.00  9.56           C  
ATOM   1261  N   GLY A 193      13.197  27.221   9.765  1.00  9.22           N  
ATOM   1262  CA  GLY A 193      12.739  26.007  10.418  1.00  8.76           C  
ATOM   1263  C   GLY A 193      13.862  25.071  10.810  1.00 10.05           C  
ATOM   1264  O   GLY A 193      14.188  24.929  11.991  1.00  9.98           O  
ATOM   1265  N   ALA A 194      14.454  24.423   9.812  1.00 10.05           N  
ATOM   1266  CA  ALA A 194      15.546  23.498  10.052  1.00 10.55           C  
ATOM   1267  C   ALA A 194      16.414  23.355   8.811  1.00 13.44           C  
ATOM   1268  O   ALA A 194      16.004  23.711   7.702  1.00 10.79           O  
ATOM   1269  CB  ALA A 194      14.991  22.128  10.450  1.00  7.06           C  
ATOM   1270  N   HIS A 195      17.631  22.857   9.019  1.00 14.20           N  
ATOM   1271  CA  HIS A 195      18.552  22.594   7.926  1.00 16.03           C  
ATOM   1272  C   HIS A 195      18.130  21.185   7.534  1.00 17.16           C  
ATOM   1273  O   HIS A 195      17.728  20.403   8.392  1.00 20.26           O  
ATOM   1274  CB  HIS A 195      19.998  22.592   8.426  1.00 14.43           C  
ATOM   1275  CG  HIS A 195      21.009  22.331   7.353  1.00 15.39           C  
ATOM   1276  ND1 HIS A 195      20.986  22.974   6.134  1.00 15.61           N  
ATOM   1277  CD2 HIS A 195      22.082  21.504   7.321  1.00 14.59           C  
ATOM   1278  CE1 HIS A 195      22.002  22.557   5.398  1.00 15.98           C  
ATOM   1279  NE2 HIS A 195      22.682  21.664   6.095  1.00 13.76           N  
ATOM   1280  N   GLY A 196      18.179  20.859   6.253  1.00 18.14           N  
ATOM   1281  CA  GLY A 196      17.773  19.523   5.857  1.00 17.55           C  
ATOM   1282  C   GLY A 196      16.487  19.451   5.051  1.00 17.44           C  
ATOM   1283  O   GLY A 196      15.878  20.469   4.715  1.00 14.06           O  
ATOM   1284  N   ASN A 197      16.081  18.221   4.754  1.00 17.67           N  
ATOM   1285  CA  ASN A 197      14.889  17.932   3.966  1.00 19.38           C  
ATOM   1286  C   ASN A 197      13.631  18.708   4.337  1.00 17.60           C  
ATOM   1287  O   ASN A 197      12.799  18.988   3.475  1.00 17.44           O  
ATOM   1288  CB  ASN A 197      14.585  16.438   4.041  1.00 26.41           C  
ATOM   1289  CG  ASN A 197      13.528  16.011   3.044  1.00 37.13           C  
ATOM   1290  OD1 ASN A 197      13.784  15.962   1.835  1.00 43.46           O  
ATOM   1291  ND2 ASN A 197      12.329  15.700   3.541  1.00 39.73           N  
ATOM   1292  N   LYS A 198      13.482  19.041   5.612  1.00 15.69           N  
ATOM   1293  CA  LYS A 198      12.303  19.767   6.067  1.00 14.20           C  
ATOM   1294  C   LYS A 198      12.485  21.278   6.047  1.00 12.17           C  
ATOM   1295  O   LYS A 198      11.641  22.015   6.566  1.00 11.92           O  
ATOM   1296  CB  LYS A 198      11.926  19.315   7.478  1.00 15.72           C  
ATOM   1297  CG  LYS A 198      11.647  17.828   7.591  1.00 17.72           C  
ATOM   1298  CD  LYS A 198      10.402  17.451   6.816  1.00 19.83           C  
ATOM   1299  CE  LYS A 198       9.631  16.351   7.525  1.00 23.65           C  
ATOM   1300  NZ  LYS A 198       9.879  15.027   6.898  1.00 27.50           N  
ATOM   1301  N   MET A 199      13.576  21.744   5.450  1.00 11.42           N  
ATOM   1302  CA  MET A 199      13.833  23.180   5.383  1.00  9.61           C  
ATOM   1303  C   MET A 199      12.627  23.891   4.774  1.00  8.08           C  
ATOM   1304  O   MET A 199      12.002  23.388   3.839  1.00  8.72           O  
ATOM   1305  CB  MET A 199      15.096  23.468   4.556  1.00  9.66           C  
ATOM   1306  CG  MET A 199      14.990  23.147   3.064  1.00  9.67           C  
ATOM   1307  SD  MET A 199      16.515  23.537   2.146  1.00 10.14           S  
ATOM   1308  CE  MET A 199      17.596  22.247   2.717  1.00  5.81           C  
ATOM   1309  N   VAL A 200      12.300  25.060   5.309  1.00  7.41           N  
ATOM   1310  CA  VAL A 200      11.154  25.820   4.825  1.00  9.17           C  
ATOM   1311  C   VAL A 200      11.599  26.965   3.919  1.00  9.89           C  
ATOM   1312  O   VAL A 200      12.180  27.939   4.392  1.00 10.71           O  
ATOM   1313  CB  VAL A 200      10.332  26.403   6.012  1.00  8.87           C  
ATOM   1314  CG1 VAL A 200       9.071  27.080   5.502  1.00  6.22           C  
ATOM   1315  CG2 VAL A 200       9.970  25.291   6.988  1.00  6.95           C  
ATOM   1316  N   LEU A 201      11.340  26.834   2.619  1.00  8.92           N  
ATOM   1317  CA  LEU A 201      11.696  27.871   1.652  1.00  9.21           C  
ATOM   1318  C   LEU A 201      10.518  28.835   1.565  1.00  9.24           C  
ATOM   1319  O   LEU A 201       9.390  28.421   1.289  1.00 10.57           O  
ATOM   1320  CB  LEU A 201      11.968  27.258   0.273  1.00  9.34           C  
ATOM   1321  CG  LEU A 201      13.360  26.666   0.035  1.00 10.51           C  
ATOM   1322  CD1 LEU A 201      13.518  25.399   0.848  1.00 12.09           C  
ATOM   1323  CD2 LEU A 201      13.550  26.364  -1.439  1.00  9.93           C  
ATOM   1324  N   LEU A 202      10.774  30.116   1.803  1.00  8.53           N  
ATOM   1325  CA  LEU A 202       9.711  31.119   1.779  1.00  7.20           C  
ATOM   1326  C   LEU A 202       9.735  31.973   0.512  1.00  8.80           C  
ATOM   1327  O   LEU A 202      10.411  33.004   0.449  1.00  8.55           O  
ATOM   1328  CB  LEU A 202       9.808  32.008   3.025  1.00  6.37           C  
ATOM   1329  CG  LEU A 202       9.776  31.255   4.363  1.00  6.41           C  
ATOM   1330  CD1 LEU A 202      10.222  32.178   5.490  1.00  9.51           C  
ATOM   1331  CD2 LEU A 202       8.373  30.722   4.629  1.00  4.03           C  
ATOM   1332  N   LYS A 203       8.980  31.526  -0.490  1.00  8.19           N  
ATOM   1333  CA  LYS A 203       8.879  32.195  -1.785  1.00 10.78           C  
ATOM   1334  C   LYS A 203       8.513  33.666  -1.645  1.00  9.13           C  
ATOM   1335  O   LYS A 203       9.015  34.516  -2.381  1.00  9.61           O  
ATOM   1336  CB  LYS A 203       7.828  31.480  -2.640  1.00 12.49           C  
ATOM   1337  CG  LYS A 203       7.436  32.187  -3.935  1.00 14.71           C  
ATOM   1338  CD  LYS A 203       6.456  31.328  -4.724  1.00 13.67           C  
ATOM   1339  CE  LYS A 203       6.366  31.760  -6.178  1.00 16.17           C  
ATOM   1340  NZ  LYS A 203       5.183  31.154  -6.861  1.00 15.58           N  
ATOM   1341  N   ARG A 204       7.640  33.944  -0.686  1.00  8.35           N  
ATOM   1342  CA  ARG A 204       7.150  35.286  -0.398  1.00  9.64           C  
ATOM   1343  C   ARG A 204       8.233  36.263   0.071  1.00 11.38           C  
ATOM   1344  O   ARG A 204       8.092  37.481  -0.091  1.00 10.84           O  
ATOM   1345  CB  ARG A 204       6.046  35.186   0.662  1.00  9.87           C  
ATOM   1346  CG  ARG A 204       5.316  36.476   0.956  1.00 11.68           C  
ATOM   1347  CD  ARG A 204       3.991  36.206   1.668  1.00 10.57           C  
ATOM   1348  NE  ARG A 204       4.155  35.599   2.991  1.00  9.31           N  
ATOM   1349  CZ  ARG A 204       4.370  36.283   4.112  1.00 11.62           C  
ATOM   1350  NH1 ARG A 204       4.454  37.605   4.090  1.00 11.10           N  
ATOM   1351  NH2 ARG A 204       4.473  35.649   5.272  1.00 11.98           N  
ATOM   1352  N   TYR A 205       9.311  35.734   0.649  1.00 11.02           N  
ATOM   1353  CA  TYR A 205      10.398  36.576   1.148  1.00 11.42           C  
ATOM   1354  C   TYR A 205      11.624  36.650   0.235  1.00 11.45           C  
ATOM   1355  O   TYR A 205      12.732  36.926   0.702  1.00 14.52           O  
ATOM   1356  CB  TYR A 205      10.841  36.102   2.538  1.00  9.35           C  
ATOM   1357  CG  TYR A 205       9.851  36.391   3.643  1.00  9.57           C  
ATOM   1358  CD1 TYR A 205       8.846  35.476   3.960  1.00 10.01           C  
ATOM   1359  CD2 TYR A 205       9.927  37.573   4.386  1.00 11.26           C  
ATOM   1360  CE1 TYR A 205       7.941  35.724   4.991  1.00  9.66           C  
ATOM   1361  CE2 TYR A 205       9.023  37.834   5.423  1.00 10.12           C  
ATOM   1362  CZ  TYR A 205       8.035  36.903   5.719  1.00 11.48           C  
ATOM   1363  OH  TYR A 205       7.150  37.141   6.745  1.00  9.98           O  
ATOM   1364  N   ILE A 206      11.445  36.396  -1.057  1.00  9.51           N  
ATOM   1365  CA  ILE A 206      12.577  36.476  -1.984  1.00  8.71           C  
ATOM   1366  C   ILE A 206      12.584  37.839  -2.686  1.00  8.44           C  
ATOM   1367  O   ILE A 206      11.540  38.314  -3.133  1.00  6.18           O  
ATOM   1368  CB  ILE A 206      12.520  35.365  -3.066  1.00  8.52           C  
ATOM   1369  CG1 ILE A 206      12.593  33.980  -2.415  1.00  5.65           C  
ATOM   1370  CG2 ILE A 206      13.692  35.532  -4.047  1.00  7.89           C  
ATOM   1371  CD1 ILE A 206      12.220  32.836  -3.357  1.00  4.75           C  
ATOM   1372  N   THR A 207      13.756  38.465  -2.770  1.00  7.31           N  
ATOM   1373  CA  THR A 207      13.891  39.761  -3.438  1.00  7.77           C  
ATOM   1374  C   THR A 207      15.095  39.749  -4.372  1.00  8.84           C  
ATOM   1375  O   THR A 207      15.995  38.917  -4.238  1.00  8.73           O  
ATOM   1376  CB  THR A 207      14.079  40.928  -2.431  1.00  8.36           C  
ATOM   1377  OG1 THR A 207      15.134  40.609  -1.515  1.00  7.90           O  
ATOM   1378  CG2 THR A 207      12.791  41.183  -1.645  1.00  6.52           C  
ATOM   1379  N   VAL A 208      15.096  40.675  -5.324  1.00  7.92           N  
ATOM   1380  CA  VAL A 208      16.183  40.809  -6.287  1.00  6.32           C  
ATOM   1381  C   VAL A 208      16.523  42.297  -6.308  1.00  5.86           C  
ATOM   1382  O   VAL A 208      15.716  43.121  -6.736  1.00  4.73           O  
ATOM   1383  CB  VAL A 208      15.738  40.336  -7.703  1.00  9.08           C  
ATOM   1384  CG1 VAL A 208      16.910  40.421  -8.685  1.00  8.53           C  
ATOM   1385  CG2 VAL A 208      15.214  38.902  -7.634  1.00  7.03           C  
ATOM   1386  N   GLY A 209A     17.714  42.645  -5.833  1.00  6.42           N  
ATOM   1387  CA  GLY A 209A     18.086  44.045  -5.785  1.00  5.19           C  
ATOM   1388  C   GLY A 209A     17.132  44.756  -4.837  1.00  7.36           C  
ATOM   1389  O   GLY A 209A     16.881  45.958  -4.976  1.00  7.24           O  
ATOM   1390  N   GLY A 209B     16.595  44.006  -3.873  1.00  5.19           N  
ATOM   1391  CA  GLY A 209B     15.666  44.570  -2.908  1.00  5.06           C  
ATOM   1392  C   GLY A 209B     14.227  44.628  -3.398  1.00  7.04           C  
ATOM   1393  O   GLY A 209B     13.331  45.034  -2.659  1.00  7.37           O  
ATOM   1394  N   ILE A 209C     14.008  44.211  -4.640  1.00  6.02           N  
ATOM   1395  CA  ILE A 209C     12.691  44.221  -5.264  1.00  4.57           C  
ATOM   1396  C   ILE A 209C     12.007  42.864  -5.092  1.00  7.08           C  
ATOM   1397  O   ILE A 209C     12.626  41.819  -5.294  1.00  7.33           O  
ATOM   1398  CB  ILE A 209C     12.826  44.531  -6.774  1.00  5.41           C  
ATOM   1399  CG1 ILE A 209C     13.677  45.788  -6.968  1.00  5.09           C  
ATOM   1400  CG2 ILE A 209C     11.453  44.704  -7.417  1.00  4.70           C  
ATOM   1401  CD1 ILE A 209C     14.202  45.952  -8.386  1.00  3.23           C  
ATOM   1402  N   PRO A 209D     10.719  42.860  -4.705  1.00  8.74           N  
ATOM   1403  CA  PRO A 209D     10.022  41.576  -4.532  1.00  6.42           C  
ATOM   1404  C   PRO A 209D     10.122  40.738  -5.807  1.00  7.64           C  
ATOM   1405  O   PRO A 209D      9.916  41.254  -6.907  1.00  6.97           O  
ATOM   1406  CB  PRO A 209D      8.581  41.984  -4.229  1.00  6.84           C  
ATOM   1407  CG  PRO A 209D      8.685  43.385  -3.705  1.00  5.46           C  
ATOM   1408  CD  PRO A 209D      9.845  44.011  -4.415  1.00  4.76           C  
ATOM   1409  N   LEU A 210A     10.441  39.452  -5.657  1.00  8.38           N  
ATOM   1410  CA  LEU A 210A     10.577  38.552  -6.797  1.00  9.40           C  
ATOM   1411  C   LEU A 210A      9.310  38.496  -7.641  1.00 10.64           C  
ATOM   1412  O   LEU A 210A      9.381  38.343  -8.862  1.00 12.65           O  
ATOM   1413  CB  LEU A 210A     10.936  37.138  -6.319  1.00  8.26           C  
ATOM   1414  CG  LEU A 210A     11.042  36.022  -7.369  1.00  5.69           C  
ATOM   1415  CD1 LEU A 210A     12.280  36.225  -8.228  1.00  7.73           C  
ATOM   1416  CD2 LEU A 210A     11.108  34.670  -6.672  1.00  5.26           C  
ATOM   1417  N   GLN A 210B      8.154  38.626  -6.994  1.00 10.54           N  
ATOM   1418  CA  GLN A 210B      6.882  38.575  -7.705  1.00 10.70           C  
ATOM   1419  C   GLN A 210B      6.831  39.553  -8.871  1.00 11.01           C  
ATOM   1420  O   GLN A 210B      6.180  39.278  -9.878  1.00 12.91           O  
ATOM   1421  CB  GLN A 210B      5.717  38.847  -6.745  1.00 12.45           C  
ATOM   1422  CG  GLN A 210B      4.328  38.633  -7.363  1.00 13.39           C  
ATOM   1423  CD  GLN A 210B      4.127  37.222  -7.911  1.00 16.73           C  
ATOM   1424  OE1 GLN A 210B      4.268  36.236  -7.184  1.00 16.67           O  
ATOM   1425  NE2 GLN A 210B      3.795  37.124  -9.194  1.00 15.00           N  
ATOM   1426  N   GLU A 211       7.509  40.691  -8.746  1.00  9.68           N  
ATOM   1427  CA  GLU A 211       7.508  41.675  -9.827  1.00  9.10           C  
ATOM   1428  C   GLU A 211       8.202  41.110 -11.056  1.00 11.12           C  
ATOM   1429  O   GLU A 211       7.807  41.397 -12.191  1.00 11.62           O  
ATOM   1430  CB  GLU A 211       8.199  42.969  -9.389  1.00  6.90           C  
ATOM   1431  CG  GLU A 211       7.441  43.715  -8.301  1.00  7.77           C  
ATOM   1432  CD  GLU A 211       7.739  45.206  -8.261  1.00  7.88           C  
ATOM   1433  OE1 GLU A 211       8.364  45.738  -9.205  1.00 10.53           O  
ATOM   1434  OE2 GLU A 211       7.342  45.851  -7.272  1.00  9.32           O  
ATOM   1435  N   PHE A 212       9.232  40.298 -10.830  1.00 11.94           N  
ATOM   1436  CA  PHE A 212       9.978  39.687 -11.926  1.00 12.30           C  
ATOM   1437  C   PHE A 212       9.158  38.553 -12.543  1.00 13.64           C  
ATOM   1438  O   PHE A 212       9.315  38.227 -13.722  1.00 12.50           O  
ATOM   1439  CB  PHE A 212      11.325  39.157 -11.423  1.00 10.25           C  
ATOM   1440  CG  PHE A 212      12.340  40.239 -11.167  1.00 12.36           C  
ATOM   1441  CD1 PHE A 212      12.267  41.020 -10.017  1.00  9.88           C  
ATOM   1442  CD2 PHE A 212      13.351  40.497 -12.087  1.00  9.57           C  
ATOM   1443  CE1 PHE A 212      13.187  42.049  -9.787  1.00  9.20           C  
ATOM   1444  CE2 PHE A 212      14.274  41.521 -11.866  1.00 10.79           C  
ATOM   1445  CZ  PHE A 212      14.192  42.300 -10.716  1.00  7.59           C  
ATOM   1446  N   ILE A 213       8.291  37.950 -11.733  1.00 13.14           N  
ATOM   1447  CA  ILE A 213       7.429  36.877 -12.209  1.00 14.22           C  
ATOM   1448  C   ILE A 213       6.329  37.526 -13.054  1.00 14.38           C  
ATOM   1449  O   ILE A 213       5.979  37.021 -14.117  1.00 15.89           O  
ATOM   1450  CB  ILE A 213       6.791  36.091 -11.033  1.00 13.74           C  
ATOM   1451  CG1 ILE A 213       7.884  35.389 -10.220  1.00 11.34           C  
ATOM   1452  CG2 ILE A 213       5.791  35.060 -11.567  1.00 13.16           C  
ATOM   1453  CD1 ILE A 213       7.372  34.686  -8.973  1.00  9.60           C  
ATOM   1454  N   ASN A 214       5.799  38.652 -12.584  1.00 13.64           N  
ATOM   1455  CA  ASN A 214       4.757  39.363 -13.315  1.00 14.92           C  
ATOM   1456  C   ASN A 214       5.296  39.777 -14.683  1.00 16.74           C  
ATOM   1457  O   ASN A 214       4.557  39.829 -15.668  1.00 17.61           O  
ATOM   1458  CB  ASN A 214       4.319  40.614 -12.544  1.00 12.06           C  
ATOM   1459  CG  ASN A 214       3.609  40.284 -11.253  1.00 12.47           C  
ATOM   1460  OD1 ASN A 214       3.084  39.187 -11.086  1.00 14.43           O  
ATOM   1461  ND2 ASN A 214       3.589  41.236 -10.327  1.00 13.34           N  
ATOM   1462  N   ASN A 215       6.594  40.055 -14.727  1.00 17.46           N  
ATOM   1463  CA  ASN A 215       7.283  40.490 -15.938  1.00 19.41           C  
ATOM   1464  C   ASN A 215       7.688  39.364 -16.883  1.00 19.54           C  
ATOM   1465  O   ASN A 215       8.223  39.628 -17.961  1.00 20.12           O  
ATOM   1466  CB  ASN A 215       8.537  41.280 -15.558  1.00 19.12           C  
ATOM   1467  CG  ASN A 215       8.226  42.688 -15.124  1.00 22.39           C  
ATOM   1468  OD1 ASN A 215       8.962  43.292 -14.344  1.00 23.30           O  
ATOM   1469  ND2 ASN A 215       7.124  43.224 -15.630  1.00 21.73           N  
ATOM   1470  N   LYS A 216       7.457  38.118 -16.479  1.00 17.90           N  
ATOM   1471  CA  LYS A 216       7.810  36.962 -17.298  1.00 18.71           C  
ATOM   1472  C   LYS A 216       9.323  36.781 -17.407  1.00 17.27           C  
ATOM   1473  O   LYS A 216       9.811  36.097 -18.309  1.00 17.46           O  
ATOM   1474  CB  LYS A 216       7.207  37.092 -18.706  1.00 19.74           C  
ATOM   1475  CG  LYS A 216       5.716  37.420 -18.741  1.00 22.25           C  
ATOM   1476  CD  LYS A 216       4.933  36.627 -17.700  1.00 26.53           C  
ATOM   1477  CE  LYS A 216       3.691  35.985 -18.296  1.00 28.85           C  
ATOM   1478  NZ  LYS A 216       3.191  34.862 -17.453  1.00 31.29           N  
ATOM   1479  N   LEU A 218      10.060  37.395 -16.484  1.00 16.39           N  
ATOM   1480  CA  LEU A 218      11.519  37.306 -16.472  1.00 14.62           C  
ATOM   1481  C   LEU A 218      11.945  35.969 -15.877  1.00 14.48           C  
ATOM   1482  O   LEU A 218      13.036  35.464 -16.141  1.00 15.18           O  
ATOM   1483  CB  LEU A 218      12.104  38.465 -15.662  1.00 13.63           C  
ATOM   1484  CG  LEU A 218      11.866  39.845 -16.283  1.00 13.04           C  
ATOM   1485  CD1 LEU A 218      12.501  40.917 -15.430  1.00 12.72           C  
ATOM   1486  CD2 LEU A 218      12.453  39.878 -17.690  1.00 15.53           C  
ATOM   1487  N   ILE A 219      11.064  35.405 -15.062  1.00 15.36           N  
ATOM   1488  CA  ILE A 219      11.288  34.110 -14.440  1.00 13.08           C  
ATOM   1489  C   ILE A 219       9.884  33.580 -14.162  1.00 14.11           C  
ATOM   1490  O   ILE A 219       9.010  34.336 -13.736  1.00 14.01           O  
ATOM   1491  CB  ILE A 219      12.107  34.241 -13.137  1.00 13.17           C  
ATOM   1492  CG1 ILE A 219      12.436  32.849 -12.598  1.00 13.79           C  
ATOM   1493  CG2 ILE A 219      11.352  35.078 -12.116  1.00  9.79           C  
ATOM   1494  CD1 ILE A 219      13.492  32.852 -11.501  1.00 15.38           C  
ATOM   1495  N   SER A 220       9.654  32.297 -14.427  1.00 13.20           N  
ATOM   1496  CA  SER A 220       8.325  31.726 -14.227  1.00 11.07           C  
ATOM   1497  C   SER A 220       8.161  31.011 -12.902  1.00 10.37           C  
ATOM   1498  O   SER A 220       9.140  30.697 -12.222  1.00  9.92           O  
ATOM   1499  CB  SER A 220       7.990  30.755 -15.363  1.00 10.47           C  
ATOM   1500  OG  SER A 220       8.633  29.506 -15.170  1.00  8.10           O  
ATOM   1501  N   ASP A 221       6.908  30.757 -12.541  1.00  9.28           N  
ATOM   1502  CA  ASP A 221       6.612  30.056 -11.302  1.00 11.04           C  
ATOM   1503  C   ASP A 221       7.142  28.630 -11.419  1.00 10.83           C  
ATOM   1504  O   ASP A 221       7.673  28.076 -10.452  1.00 10.42           O  
ATOM   1505  CB  ASP A 221       5.102  30.056 -11.036  1.00  9.95           C  
ATOM   1506  CG  ASP A 221       4.604  31.400 -10.515  1.00 12.22           C  
ATOM   1507  OD1 ASP A 221       5.044  31.825  -9.427  1.00 12.28           O  
ATOM   1508  OD2 ASP A 221       3.777  32.039 -11.195  1.00 13.48           O  
ATOM   1509  N   ALA A 222       7.015  28.045 -12.612  1.00  9.05           N  
ATOM   1510  CA  ALA A 222       7.493  26.687 -12.840  1.00 10.08           C  
ATOM   1511  C   ALA A 222       9.011  26.628 -12.691  1.00 11.59           C  
ATOM   1512  O   ALA A 222       9.554  25.670 -12.150  1.00 12.79           O  
ATOM   1513  CB  ALA A 222       7.078  26.201 -14.231  1.00  7.43           C  
ATOM   1514  N   GLU A 223       9.700  27.656 -13.173  1.00 13.03           N  
ATOM   1515  CA  GLU A 223      11.151  27.694 -13.065  1.00 11.48           C  
ATOM   1516  C   GLU A 223      11.535  27.736 -11.596  1.00 11.98           C  
ATOM   1517  O   GLU A 223      12.460  27.052 -11.168  1.00 12.99           O  
ATOM   1518  CB  GLU A 223      11.707  28.933 -13.766  1.00 11.69           C  
ATOM   1519  CG  GLU A 223      11.935  28.759 -15.258  1.00 12.55           C  
ATOM   1520  CD  GLU A 223      12.310  30.057 -15.930  1.00  9.93           C  
ATOM   1521  OE1 GLU A 223      11.505  31.008 -15.858  1.00 12.32           O  
ATOM   1522  OE2 GLU A 223      13.411  30.129 -16.522  1.00 11.58           O  
ATOM   1523  N   LEU A 225      10.811  28.540 -10.824  1.00 12.47           N  
ATOM   1524  CA  LEU A 225      11.091  28.686  -9.401  1.00 14.00           C  
ATOM   1525  C   LEU A 225      10.855  27.407  -8.619  1.00 12.92           C  
ATOM   1526  O   LEU A 225      11.619  27.075  -7.718  1.00 12.31           O  
ATOM   1527  CB  LEU A 225      10.243  29.814  -8.818  1.00 15.43           C  
ATOM   1528  CG  LEU A 225      10.960  31.161  -8.878  1.00 19.37           C  
ATOM   1529  CD1 LEU A 225       9.955  32.278  -9.117  1.00 19.73           C  
ATOM   1530  CD2 LEU A 225      11.723  31.371  -7.575  1.00 18.87           C  
ATOM   1531  N   GLU A 226       9.791  26.692  -8.965  1.00 13.76           N  
ATOM   1532  CA  GLU A 226       9.469  25.442  -8.297  1.00 15.00           C  
ATOM   1533  C   GLU A 226      10.621  24.457  -8.495  1.00 13.21           C  
ATOM   1534  O   GLU A 226      11.006  23.738  -7.574  1.00 11.90           O  
ATOM   1535  CB  GLU A 226       8.173  24.863  -8.873  1.00 19.34           C  
ATOM   1536  CG  GLU A 226       7.354  24.058  -7.881  1.00 28.25           C  
ATOM   1537  CD  GLU A 226       6.242  23.266  -8.551  1.00 33.84           C  
ATOM   1538  OE1 GLU A 226       5.384  23.885  -9.220  1.00 37.14           O  
ATOM   1539  OE2 GLU A 226       6.227  22.025  -8.410  1.00 36.61           O  
ATOM   1540  N   ALA A 227      11.180  24.437  -9.703  1.00 11.37           N  
ATOM   1541  CA  ALA A 227      12.287  23.539 -10.006  1.00 10.53           C  
ATOM   1542  C   ALA A 227      13.531  23.956  -9.216  1.00 10.03           C  
ATOM   1543  O   ALA A 227      14.277  23.109  -8.720  1.00  8.20           O  
ATOM   1544  CB  ALA A 227      12.574  23.552 -11.503  1.00 10.20           C  
ATOM   1545  N   ILE A 228      13.743  25.266  -9.099  1.00  7.76           N  
ATOM   1546  CA  ILE A 228      14.881  25.796  -8.352  1.00  9.09           C  
ATOM   1547  C   ILE A 228      14.724  25.438  -6.870  1.00  9.38           C  
ATOM   1548  O   ILE A 228      15.708  25.144  -6.186  1.00  9.68           O  
ATOM   1549  CB  ILE A 228      14.983  27.349  -8.518  1.00  7.35           C  
ATOM   1550  CG1 ILE A 228      15.688  27.685  -9.837  1.00  8.44           C  
ATOM   1551  CG2 ILE A 228      15.748  27.972  -7.346  1.00  6.37           C  
ATOM   1552  CD1 ILE A 228      15.375  29.079 -10.368  1.00  5.71           C  
ATOM   1553  N   PHE A 229      13.484  25.461  -6.381  1.00  9.91           N  
ATOM   1554  CA  PHE A 229      13.197  25.128  -4.983  1.00 11.43           C  
ATOM   1555  C   PHE A 229      13.583  23.690  -4.680  1.00 12.11           C  
ATOM   1556  O   PHE A 229      14.262  23.409  -3.690  1.00 10.08           O  
ATOM   1557  CB  PHE A 229      11.711  25.317  -4.682  1.00 12.79           C  
ATOM   1558  CG  PHE A 229      11.280  26.753  -4.631  1.00 17.36           C  
ATOM   1559  CD1 PHE A 229      12.220  27.780  -4.574  1.00 16.99           C  
ATOM   1560  CD2 PHE A 229       9.927  27.082  -4.650  1.00 20.65           C  
ATOM   1561  CE1 PHE A 229      11.823  29.111  -4.535  1.00 19.00           C  
ATOM   1562  CE2 PHE A 229       9.517  28.415  -4.611  1.00 22.58           C  
ATOM   1563  CZ  PHE A 229      10.470  29.432  -4.553  1.00 22.53           C  
ATOM   1564  N   ASP A 230      13.131  22.780  -5.534  1.00 12.57           N  
ATOM   1565  CA  ASP A 230      13.441  21.368  -5.372  1.00 13.33           C  
ATOM   1566  C   ASP A 230      14.955  21.191  -5.458  1.00 12.47           C  
ATOM   1567  O   ASP A 230      15.545  20.438  -4.690  1.00 11.70           O  
ATOM   1568  CB  ASP A 230      12.739  20.549  -6.462  1.00 17.96           C  
ATOM   1569  CG  ASP A 230      11.217  20.619  -6.354  1.00 25.30           C  
ATOM   1570  OD1 ASP A 230      10.715  20.923  -5.249  1.00 28.21           O  
ATOM   1571  OD2 ASP A 230      10.522  20.372  -7.368  1.00 29.98           O  
ATOM   1572  N   ARG A 231      15.581  21.900  -6.391  1.00 11.21           N  
ATOM   1573  CA  ARG A 231      17.025  21.820  -6.564  1.00 10.85           C  
ATOM   1574  C   ARG A 231      17.741  22.251  -5.288  1.00 11.95           C  
ATOM   1575  O   ARG A 231      18.733  21.639  -4.869  1.00  9.83           O  
ATOM   1576  CB  ARG A 231      17.459  22.715  -7.723  1.00 11.37           C  
ATOM   1577  CG  ARG A 231      18.452  22.062  -8.658  1.00 13.08           C  
ATOM   1578  CD  ARG A 231      19.385  23.077  -9.266  1.00 14.46           C  
ATOM   1579  NE  ARG A 231      20.662  22.479  -9.628  1.00 12.07           N  
ATOM   1580  CZ  ARG A 231      21.521  23.027 -10.479  1.00 16.48           C  
ATOM   1581  NH1 ARG A 231      21.235  24.191 -11.050  1.00 14.21           N  
ATOM   1582  NH2 ARG A 231      22.666  22.415 -10.753  1.00 16.71           N  
ATOM   1583  N   THR A 232      17.230  23.312  -4.674  1.00 12.32           N  
ATOM   1584  CA  THR A 232      17.803  23.858  -3.448  1.00 10.34           C  
ATOM   1585  C   THR A 232      17.747  22.834  -2.323  1.00 12.60           C  
ATOM   1586  O   THR A 232      18.752  22.569  -1.659  1.00 13.30           O  
ATOM   1587  CB  THR A 232      17.043  25.135  -3.020  1.00 11.40           C  
ATOM   1588  OG1 THR A 232      17.263  26.164  -3.995  1.00 10.03           O  
ATOM   1589  CG2 THR A 232      17.511  25.616  -1.654  1.00  7.65           C  
ATOM   1590  N   VAL A 233      16.572  22.248  -2.117  1.00 13.59           N  
ATOM   1591  CA  VAL A 233      16.392  21.257  -1.063  1.00 12.45           C  
ATOM   1592  C   VAL A 233      17.274  20.031  -1.298  1.00 14.31           C  
ATOM   1593  O   VAL A 233      17.832  19.477  -0.353  1.00 16.54           O  
ATOM   1594  CB  VAL A 233      14.902  20.813  -0.958  1.00 11.58           C  
ATOM   1595  CG1 VAL A 233      14.745  19.741   0.100  1.00  9.42           C  
ATOM   1596  CG2 VAL A 233      14.019  22.012  -0.619  1.00  9.56           C  
ATOM   1597  N   ASN A 234      17.426  19.625  -2.557  1.00 14.41           N  
ATOM   1598  CA  ASN A 234      18.222  18.442  -2.887  1.00 13.96           C  
ATOM   1599  C   ASN A 234      19.646  18.681  -3.386  1.00 14.13           C  
ATOM   1600  O   ASN A 234      20.231  17.793  -4.009  1.00 15.27           O  
ATOM   1601  CB  ASN A 234      17.485  17.600  -3.935  1.00 13.85           C  
ATOM   1602  CG  ASN A 234      16.175  17.050  -3.422  1.00 14.25           C  
ATOM   1603  OD1 ASN A 234      16.148  16.272  -2.475  1.00 13.39           O  
ATOM   1604  ND2 ASN A 234      15.076  17.454  -4.046  1.00 15.09           N  
ATOM   1605  N   THR A 235      20.216  19.849  -3.110  1.00 13.45           N  
ATOM   1606  CA  THR A 235      21.568  20.147  -3.584  1.00 14.22           C  
ATOM   1607  C   THR A 235      22.666  19.224  -3.048  1.00 15.13           C  
ATOM   1608  O   THR A 235      23.495  18.728  -3.823  1.00 15.79           O  
ATOM   1609  CB  THR A 235      21.959  21.593  -3.276  1.00 14.08           C  
ATOM   1610  OG1 THR A 235      21.168  22.475  -4.083  1.00 15.71           O  
ATOM   1611  CG2 THR A 235      23.434  21.819  -3.584  1.00 12.84           C  
ATOM   1612  N   ALA A 236      22.693  19.000  -1.739  1.00 13.94           N  
ATOM   1613  CA  ALA A 236      23.707  18.115  -1.174  1.00 14.09           C  
ATOM   1614  C   ALA A 236      23.624  16.783  -1.907  1.00 15.27           C  
ATOM   1615  O   ALA A 236      24.637  16.250  -2.376  1.00 17.40           O  
ATOM   1616  CB  ALA A 236      23.471  17.908   0.316  1.00 12.45           C  
ATOM   1617  N   LEU A 237      22.406  16.257  -2.020  1.00 15.36           N  
ATOM   1618  CA  LEU A 237      22.182  14.986  -2.700  1.00 15.25           C  
ATOM   1619  C   LEU A 237      22.639  15.055  -4.150  1.00 15.18           C  
ATOM   1620  O   LEU A 237      23.201  14.098  -4.680  1.00 14.11           O  
ATOM   1621  CB  LEU A 237      20.700  14.604  -2.649  1.00 16.03           C  
ATOM   1622  CG  LEU A 237      20.274  13.419  -3.526  1.00 16.98           C  
ATOM   1623  CD1 LEU A 237      20.950  12.139  -3.054  1.00 17.24           C  
ATOM   1624  CD2 LEU A 237      18.765  13.271  -3.477  1.00 18.70           C  
ATOM   1625  N   GLU A 238      22.395  16.190  -4.794  1.00 14.23           N  
ATOM   1626  CA  GLU A 238      22.798  16.350  -6.179  1.00 13.22           C  
ATOM   1627  C   GLU A 238      24.321  16.320  -6.300  1.00 14.92           C  
ATOM   1628  O   GLU A 238      24.867  15.671  -7.198  1.00 13.62           O  
ATOM   1629  CB  GLU A 238      22.258  17.664  -6.742  1.00 14.26           C  
ATOM   1630  CG  GLU A 238      22.617  17.893  -8.208  1.00 15.00           C  
ATOM   1631  CD  GLU A 238      22.065  19.196  -8.768  1.00 15.03           C  
ATOM   1632  OE1 GLU A 238      21.320  19.902  -8.054  1.00 12.88           O  
ATOM   1633  OE2 GLU A 238      22.382  19.512  -9.935  1.00 15.66           O  
ATOM   1634  N   ILE A 239      25.004  17.019  -5.395  1.00 14.98           N  
ATOM   1635  CA  ILE A 239      26.465  17.066  -5.413  1.00 14.12           C  
ATOM   1636  C   ILE A 239      27.042  15.683  -5.150  1.00 14.91           C  
ATOM   1637  O   ILE A 239      28.029  15.284  -5.773  1.00 12.70           O  
ATOM   1638  CB  ILE A 239      27.020  18.049  -4.353  1.00 13.43           C  
ATOM   1639  CG1 ILE A 239      26.694  19.490  -4.760  1.00 11.77           C  
ATOM   1640  CG2 ILE A 239      28.529  17.888  -4.229  1.00 11.02           C  
ATOM   1641  CD1 ILE A 239      26.686  20.479  -3.607  1.00  3.51           C  
ATOM   1642  N   VAL A 240      26.415  14.957  -4.228  1.00 14.49           N  
ATOM   1643  CA  VAL A 240      26.850  13.612  -3.874  1.00 14.02           C  
ATOM   1644  C   VAL A 240      26.675  12.668  -5.062  1.00 16.56           C  
ATOM   1645  O   VAL A 240      27.524  11.812  -5.317  1.00 16.17           O  
ATOM   1646  CB  VAL A 240      26.042  13.066  -2.670  1.00 15.48           C  
ATOM   1647  CG1 VAL A 240      26.128  11.551  -2.619  1.00 15.35           C  
ATOM   1648  CG2 VAL A 240      26.569  13.669  -1.376  1.00 12.75           C  
ATOM   1649  N   ASN A 241      25.575  12.826  -5.788  1.00 16.16           N  
ATOM   1650  CA  ASN A 241      25.309  11.971  -6.937  1.00 18.02           C  
ATOM   1651  C   ASN A 241      26.272  12.252  -8.084  1.00 17.64           C  
ATOM   1652  O   ASN A 241      26.439  11.416  -8.971  1.00 17.73           O  
ATOM   1653  CB  ASN A 241      23.860  12.145  -7.408  1.00 18.75           C  
ATOM   1654  CG  ASN A 241      22.877  11.312  -6.589  1.00 20.71           C  
ATOM   1655  OD1 ASN A 241      23.276  10.491  -5.758  1.00 21.44           O  
ATOM   1656  ND2 ASN A 241      21.586  11.525  -6.825  1.00 18.67           N  
ATOM   1657  N   LEU A 242      26.910  13.418  -8.061  1.00 16.93           N  
ATOM   1658  CA  LEU A 242      27.874  13.782  -9.098  1.00 18.20           C  
ATOM   1659  C   LEU A 242      29.261  13.303  -8.692  1.00 17.96           C  
ATOM   1660  O   LEU A 242      30.256  13.641  -9.323  1.00 19.08           O  
ATOM   1661  CB  LEU A 242      27.894  15.296  -9.306  1.00 16.41           C  
ATOM   1662  CG  LEU A 242      26.671  15.857 -10.028  1.00 17.41           C  
ATOM   1663  CD1 LEU A 242      26.532  17.341  -9.737  1.00 16.81           C  
ATOM   1664  CD2 LEU A 242      26.807  15.608 -11.522  1.00 16.84           C  
ATOM   1665  N   HIS A 243      29.310  12.514  -7.624  1.00 20.22           N  
ATOM   1666  CA  HIS A 243      30.563  11.968  -7.116  1.00 22.01           C  
ATOM   1667  C   HIS A 243      31.457  13.025  -6.476  1.00 21.34           C  
ATOM   1668  O   HIS A 243      32.656  13.108  -6.740  1.00 19.64           O  
ATOM   1669  CB  HIS A 243      31.301  11.234  -8.237  1.00 26.61           C  
ATOM   1670  CG  HIS A 243      30.498  10.128  -8.850  1.00 32.83           C  
ATOM   1671  ND1 HIS A 243      30.275   8.927  -8.207  1.00 35.35           N  
ATOM   1672  CD2 HIS A 243      29.820  10.060 -10.019  1.00 34.70           C  
ATOM   1673  CE1 HIS A 243      29.494   8.171  -8.955  1.00 36.76           C  
ATOM   1674  NE2 HIS A 243      29.203   8.834 -10.060  1.00 36.29           N  
ATOM   1675  N   ALA A 244      30.844  13.831  -5.623  1.00 20.12           N  
ATOM   1676  CA  ALA A 244      31.538  14.875  -4.885  1.00 19.45           C  
ATOM   1677  C   ALA A 244      30.773  15.003  -3.575  1.00 19.03           C  
ATOM   1678  O   ALA A 244      29.856  14.230  -3.307  1.00 19.71           O  
ATOM   1679  CB  ALA A 244      31.503  16.190  -5.657  1.00 18.29           C  
ATOM   1680  N   SER A 245      31.157  15.963  -2.749  1.00 19.37           N  
ATOM   1681  CA  SER A 245      30.470  16.176  -1.482  1.00 19.95           C  
ATOM   1682  C   SER A 245      30.564  17.656  -1.169  1.00 17.86           C  
ATOM   1683  O   SER A 245      31.595  18.282  -1.422  1.00 19.27           O  
ATOM   1684  CB  SER A 245      31.121  15.362  -0.368  1.00 20.96           C  
ATOM   1685  OG  SER A 245      32.471  15.752  -0.193  1.00 27.24           O  
ATOM   1686  N   PRO A 246      29.485  18.243  -0.627  1.00 14.12           N  
ATOM   1687  CA  PRO A 246      29.538  19.671  -0.315  1.00 12.88           C  
ATOM   1688  C   PRO A 246      30.348  19.998   0.930  1.00 11.91           C  
ATOM   1689  O   PRO A 246      30.064  19.487   2.011  1.00 12.99           O  
ATOM   1690  CB  PRO A 246      28.067  20.061  -0.160  1.00 14.37           C  
ATOM   1691  CG  PRO A 246      27.387  18.806   0.274  1.00 13.89           C  
ATOM   1692  CD  PRO A 246      28.179  17.644  -0.293  1.00 14.29           C  
ATOM   1693  N   TYR A 247      31.365  20.835   0.773  1.00 10.41           N  
ATOM   1694  CA  TYR A 247      32.172  21.254   1.915  1.00  9.52           C  
ATOM   1695  C   TYR A 247      32.738  22.655   1.722  1.00  7.21           C  
ATOM   1696  O   TYR A 247      33.056  23.330   2.693  1.00  7.32           O  
ATOM   1697  CB  TYR A 247      33.294  20.242   2.204  1.00 11.87           C  
ATOM   1698  CG  TYR A 247      34.350  20.130   1.133  1.00 14.02           C  
ATOM   1699  CD1 TYR A 247      34.185  19.266   0.049  1.00 15.64           C  
ATOM   1700  CD2 TYR A 247      35.516  20.889   1.199  1.00 15.05           C  
ATOM   1701  CE1 TYR A 247      35.158  19.166  -0.946  1.00 18.03           C  
ATOM   1702  CE2 TYR A 247      36.496  20.799   0.210  1.00 15.71           C  
ATOM   1703  CZ  TYR A 247      36.311  19.940  -0.857  1.00 19.17           C  
ATOM   1704  OH  TYR A 247      37.271  19.878  -1.843  1.00 21.28           O  
ATOM   1705  N   VAL A 248      32.839  23.106   0.476  1.00  7.60           N  
ATOM   1706  CA  VAL A 248      33.367  24.443   0.202  1.00  7.55           C  
ATOM   1707  C   VAL A 248      32.367  25.536   0.598  1.00  6.14           C  
ATOM   1708  O   VAL A 248      32.718  26.458   1.333  1.00  8.55           O  
ATOM   1709  CB  VAL A 248      33.749  24.593  -1.293  1.00  7.13           C  
ATOM   1710  CG1 VAL A 248      34.149  26.017  -1.599  1.00  5.11           C  
ATOM   1711  CG2 VAL A 248      34.895  23.650  -1.623  1.00  5.42           C  
ATOM   1712  N   ALA A 249      31.128  25.436   0.120  1.00  7.40           N  
ATOM   1713  CA  ALA A 249      30.104  26.428   0.462  1.00  6.53           C  
ATOM   1714  C   ALA A 249      29.838  26.390   1.971  1.00  7.31           C  
ATOM   1715  O   ALA A 249      29.750  27.433   2.623  1.00  8.94           O  
ATOM   1716  CB  ALA A 249      28.822  26.164  -0.314  1.00  6.81           C  
ATOM   1717  N   PRO A 250      29.661  25.185   2.541  1.00  6.93           N  
ATOM   1718  CA  PRO A 250      29.417  25.093   3.985  1.00  6.07           C  
ATOM   1719  C   PRO A 250      30.495  25.863   4.754  1.00  6.37           C  
ATOM   1720  O   PRO A 250      30.187  26.643   5.662  1.00  6.28           O  
ATOM   1721  CB  PRO A 250      29.480  23.598   4.264  1.00  6.70           C  
ATOM   1722  CG  PRO A 250      29.081  22.964   2.968  1.00  8.68           C  
ATOM   1723  CD  PRO A 250      29.594  23.870   1.879  1.00  5.66           C  
ATOM   1724  N   ALA A 251      31.751  25.642   4.373  1.00  4.09           N  
ATOM   1725  CA  ALA A 251      32.880  26.311   5.011  1.00  3.76           C  
ATOM   1726  C   ALA A 251      32.780  27.821   4.841  1.00  4.50           C  
ATOM   1727  O   ALA A 251      33.001  28.568   5.792  1.00  5.49           O  
ATOM   1728  CB  ALA A 251      34.193  25.811   4.426  1.00  2.54           C  
ATOM   1729  N   ALA A 252      32.447  28.266   3.632  1.00  2.83           N  
ATOM   1730  CA  ALA A 252      32.318  29.690   3.349  1.00  2.89           C  
ATOM   1731  C   ALA A 252      31.152  30.311   4.127  1.00  5.15           C  
ATOM   1732  O   ALA A 252      31.239  31.447   4.602  1.00  6.08           O  
ATOM   1733  CB  ALA A 252      32.128  29.910   1.851  1.00  3.89           C  
ATOM   1734  N   ALA A 253      30.058  29.568   4.247  1.00  3.80           N  
ATOM   1735  CA  ALA A 253      28.900  30.051   4.985  1.00  5.62           C  
ATOM   1736  C   ALA A 253      29.273  30.189   6.458  1.00  7.14           C  
ATOM   1737  O   ALA A 253      28.920  31.176   7.107  1.00  7.60           O  
ATOM   1738  CB  ALA A 253      27.739  29.078   4.832  1.00  2.87           C  
ATOM   1739  N   ILE A 254      29.990  29.198   6.980  1.00  6.13           N  
ATOM   1740  CA  ILE A 254      30.399  29.217   8.381  1.00  7.46           C  
ATOM   1741  C   ILE A 254      31.300  30.413   8.665  1.00  7.17           C  
ATOM   1742  O   ILE A 254      31.132  31.095   9.677  1.00  8.59           O  
ATOM   1743  CB  ILE A 254      31.152  27.916   8.776  1.00  7.15           C  
ATOM   1744  CG1 ILE A 254      30.204  26.716   8.735  1.00  5.16           C  
ATOM   1745  CG2 ILE A 254      31.714  28.050  10.177  1.00  8.07           C  
ATOM   1746  CD1 ILE A 254      30.907  25.396   8.499  1.00  3.93           C  
ATOM   1747  N   ILE A 255      32.247  30.674   7.767  1.00  4.93           N  
ATOM   1748  CA  ILE A 255      33.155  31.793   7.950  1.00  4.98           C  
ATOM   1749  C   ILE A 255      32.425  33.140   7.873  1.00  6.82           C  
ATOM   1750  O   ILE A 255      32.811  34.091   8.557  1.00  7.20           O  
ATOM   1751  CB  ILE A 255      34.303  31.754   6.915  1.00  4.88           C  
ATOM   1752  CG1 ILE A 255      35.148  30.488   7.114  1.00  3.65           C  
ATOM   1753  CG2 ILE A 255      35.182  32.999   7.051  1.00  4.91           C  
ATOM   1754  CD1 ILE A 255      35.641  30.264   8.536  1.00  3.89           C  
ATOM   1755  N   GLU A 256      31.376  33.237   7.059  1.00  4.90           N  
ATOM   1756  CA  GLU A 256      30.648  34.499   6.987  1.00  4.47           C  
ATOM   1757  C   GLU A 256      30.042  34.765   8.364  1.00  3.85           C  
ATOM   1758  O   GLU A 256      30.041  35.893   8.850  1.00  3.59           O  
ATOM   1759  CB  GLU A 256      29.535  34.449   5.930  1.00  5.65           C  
ATOM   1760  CG  GLU A 256      28.753  35.762   5.848  1.00  4.98           C  
ATOM   1761  CD  GLU A 256      27.894  35.894   4.608  1.00  6.67           C  
ATOM   1762  OE1 GLU A 256      27.620  34.874   3.946  1.00  7.13           O  
ATOM   1763  OE2 GLU A 256      27.483  37.032   4.300  1.00  9.11           O  
ATOM   1764  N   MET A 257      29.540  33.707   8.990  1.00  5.12           N  
ATOM   1765  CA  MET A 257      28.936  33.797  10.313  1.00  3.92           C  
ATOM   1766  C   MET A 257      29.982  34.172  11.357  1.00  5.20           C  
ATOM   1767  O   MET A 257      29.800  35.120  12.122  1.00  4.78           O  
ATOM   1768  CB  MET A 257      28.296  32.457  10.695  1.00  6.68           C  
ATOM   1769  CG  MET A 257      27.062  32.091   9.882  1.00  4.50           C  
ATOM   1770  SD  MET A 257      26.723  30.315   9.853  1.00  8.54           S  
ATOM   1771  CE  MET A 257      26.586  29.940  11.589  1.00  4.13           C  
ATOM   1772  N   ALA A 258      31.077  33.422  11.392  1.00  5.37           N  
ATOM   1773  CA  ALA A 258      32.147  33.684  12.350  1.00  5.20           C  
ATOM   1774  C   ALA A 258      32.715  35.099  12.196  1.00  7.64           C  
ATOM   1775  O   ALA A 258      33.018  35.771  13.187  1.00  6.65           O  
ATOM   1776  CB  ALA A 258      33.264  32.647  12.188  1.00  5.77           C  
ATOM   1777  N   GLU A 259      32.850  35.551  10.951  1.00  7.88           N  
ATOM   1778  CA  GLU A 259      33.387  36.877  10.671  1.00  5.99           C  
ATOM   1779  C   GLU A 259      32.453  37.994  11.133  1.00  6.70           C  
ATOM   1780  O   GLU A 259      32.914  39.044  11.584  1.00  6.14           O  
ATOM   1781  CB  GLU A 259      33.660  37.023   9.178  1.00  6.02           C  
ATOM   1782  CG  GLU A 259      34.146  38.402   8.777  1.00  7.77           C  
ATOM   1783  CD  GLU A 259      34.346  38.521   7.280  1.00  8.37           C  
ATOM   1784  OE1 GLU A 259      33.441  38.109   6.527  1.00  9.98           O  
ATOM   1785  OE2 GLU A 259      35.404  39.021   6.858  1.00  9.07           O  
ATOM   1786  N   SER A 260      31.146  37.774  11.013  1.00  6.55           N  
ATOM   1787  CA  SER A 260      30.173  38.773  11.446  1.00  5.70           C  
ATOM   1788  C   SER A 260      30.325  38.974  12.951  1.00  5.58           C  
ATOM   1789  O   SER A 260      30.236  40.093  13.450  1.00  5.82           O  
ATOM   1790  CB  SER A 260      28.747  38.313  11.130  1.00  6.61           C  
ATOM   1791  OG  SER A 260      27.814  39.356  11.372  1.00  7.33           O  
ATOM   1792  N   TYR A 261      30.560  37.878  13.667  1.00  5.76           N  
ATOM   1793  CA  TYR A 261      30.737  37.929  15.112  1.00  6.17           C  
ATOM   1794  C   TYR A 261      32.050  38.612  15.482  1.00  6.71           C  
ATOM   1795  O   TYR A 261      32.072  39.568  16.249  1.00  8.48           O  
ATOM   1796  CB  TYR A 261      30.717  36.508  15.699  1.00  6.31           C  
ATOM   1797  CG  TYR A 261      31.134  36.439  17.156  1.00  6.88           C  
ATOM   1798  CD1 TYR A 261      30.241  36.778  18.172  1.00  7.29           C  
ATOM   1799  CD2 TYR A 261      32.437  36.084  17.515  1.00  8.21           C  
ATOM   1800  CE1 TYR A 261      30.630  36.774  19.511  1.00  7.44           C  
ATOM   1801  CE2 TYR A 261      32.840  36.076  18.855  1.00  9.52           C  
ATOM   1802  CZ  TYR A 261      31.928  36.426  19.847  1.00  9.28           C  
ATOM   1803  OH  TYR A 261      32.314  36.446  21.170  1.00  9.15           O  
ATOM   1804  N   LEU A 262      33.147  38.119  14.918  1.00  7.45           N  
ATOM   1805  CA  LEU A 262      34.470  38.649  15.207  1.00  7.49           C  
ATOM   1806  C   LEU A 262      34.663  40.126  14.884  1.00  8.06           C  
ATOM   1807  O   LEU A 262      35.311  40.853  15.641  1.00  8.10           O  
ATOM   1808  CB  LEU A 262      35.519  37.813  14.471  1.00  7.56           C  
ATOM   1809  CG  LEU A 262      35.762  36.428  15.080  1.00  9.35           C  
ATOM   1810  CD1 LEU A 262      36.727  35.642  14.199  1.00  8.38           C  
ATOM   1811  CD2 LEU A 262      36.322  36.578  16.489  1.00  6.93           C  
ATOM   1812  N   LYS A 263      34.099  40.573  13.768  1.00  7.73           N  
ATOM   1813  CA  LYS A 263      34.230  41.969  13.356  1.00  8.94           C  
ATOM   1814  C   LYS A 263      33.041  42.844  13.751  1.00 10.13           C  
ATOM   1815  O   LYS A 263      33.001  44.031  13.420  1.00 11.17           O  
ATOM   1816  CB  LYS A 263      34.454  42.042  11.844  1.00 10.26           C  
ATOM   1817  CG  LYS A 263      35.830  41.549  11.423  1.00 11.56           C  
ATOM   1818  CD  LYS A 263      36.122  41.909   9.982  1.00 17.72           C  
ATOM   1819  CE  LYS A 263      37.005  40.864   9.323  1.00 18.41           C  
ATOM   1820  NZ  LYS A 263      36.990  41.007   7.840  1.00 18.96           N  
ATOM   1821  N   ASP A 264      32.083  42.259  14.468  1.00  9.53           N  
ATOM   1822  CA  ASP A 264      30.904  42.994  14.915  1.00  9.36           C  
ATOM   1823  C   ASP A 264      30.194  43.636  13.724  1.00  7.95           C  
ATOM   1824  O   ASP A 264      29.808  44.799  13.776  1.00  9.98           O  
ATOM   1825  CB  ASP A 264      31.317  44.069  15.926  1.00  8.76           C  
ATOM   1826  CG  ASP A 264      30.127  44.713  16.626  1.00 11.28           C  
ATOM   1827  OD1 ASP A 264      29.108  44.028  16.850  1.00 11.78           O  
ATOM   1828  OD2 ASP A 264      30.214  45.914  16.956  1.00 11.72           O  
ATOM   1829  N   LEU A 265      30.017  42.865  12.657  1.00  7.62           N  
ATOM   1830  CA  LEU A 265      29.360  43.364  11.452  1.00  6.49           C  
ATOM   1831  C   LEU A 265      27.857  43.541  11.615  1.00  7.12           C  
ATOM   1832  O   LEU A 265      27.253  44.389  10.960  1.00  4.99           O  
ATOM   1833  CB  LEU A 265      29.637  42.423  10.281  1.00  7.54           C  
ATOM   1834  CG  LEU A 265      31.087  42.457   9.807  1.00  9.58           C  
ATOM   1835  CD1 LEU A 265      31.300  41.425   8.719  1.00  6.67           C  
ATOM   1836  CD2 LEU A 265      31.421  43.850   9.306  1.00 10.65           C  
ATOM   1837  N   LYS A 266      27.263  42.737  12.495  1.00  6.55           N  
ATOM   1838  CA  LYS A 266      25.828  42.779  12.766  1.00  7.96           C  
ATOM   1839  C   LYS A 266      25.006  42.415  11.531  1.00  7.84           C  
ATOM   1840  O   LYS A 266      23.936  42.979  11.285  1.00  5.90           O  
ATOM   1841  CB  LYS A 266      25.417  44.159  13.299  1.00  7.83           C  
ATOM   1842  CG  LYS A 266      26.080  44.522  14.627  1.00  5.83           C  
ATOM   1843  CD  LYS A 266      25.533  45.824  15.191  1.00  7.84           C  
ATOM   1844  CE  LYS A 266      26.399  46.346  16.328  1.00  9.07           C  
ATOM   1845  NZ  LYS A 266      26.676  45.289  17.351  1.00 11.29           N  
ATOM   1846  N   LYS A 267      25.520  41.458  10.763  1.00  5.93           N  
ATOM   1847  CA  LYS A 267      24.839  40.982   9.566  1.00  6.60           C  
ATOM   1848  C   LYS A 267      23.600  40.198   9.983  1.00  7.20           C  
ATOM   1849  O   LYS A 267      23.568  39.603  11.064  1.00  5.36           O  
ATOM   1850  CB  LYS A 267      25.739  40.030   8.772  1.00  5.94           C  
ATOM   1851  CG  LYS A 267      26.777  40.682   7.872  1.00  9.09           C  
ATOM   1852  CD  LYS A 267      27.427  39.612   6.996  1.00  8.07           C  
ATOM   1853  CE  LYS A 267      28.311  40.217   5.930  1.00  7.08           C  
ATOM   1854  NZ  LYS A 267      29.203  39.183   5.338  1.00  7.48           N  
ATOM   1855  N   VAL A 268      22.583  40.209   9.127  1.00  6.40           N  
ATOM   1856  CA  VAL A 268      21.371  39.449   9.380  1.00  4.71           C  
ATOM   1857  C   VAL A 268      21.649  38.145   8.638  1.00  7.60           C  
ATOM   1858  O   VAL A 268      21.757  38.135   7.407  1.00  6.91           O  
ATOM   1859  CB  VAL A 268      20.122  40.123   8.771  1.00  4.63           C  
ATOM   1860  CG1 VAL A 268      18.890  39.279   9.054  1.00  5.75           C  
ATOM   1861  CG2 VAL A 268      19.951  41.514   9.341  1.00  2.52           C  
ATOM   1862  N   LEU A 269      21.800  37.062   9.396  1.00  7.50           N  
ATOM   1863  CA  LEU A 269      22.092  35.750   8.835  1.00  8.28           C  
ATOM   1864  C   LEU A 269      21.141  34.722   9.438  1.00  8.12           C  
ATOM   1865  O   LEU A 269      20.854  34.757  10.633  1.00  9.25           O  
ATOM   1866  CB  LEU A 269      23.551  35.362   9.143  1.00  7.03           C  
ATOM   1867  CG  LEU A 269      24.643  36.329   8.657  1.00  9.20           C  
ATOM   1868  CD1 LEU A 269      25.932  36.095   9.425  1.00  7.01           C  
ATOM   1869  CD2 LEU A 269      24.882  36.140   7.165  1.00 10.03           C  
ATOM   1870  N   ILE A 270      20.647  33.809   8.609  1.00  7.14           N  
ATOM   1871  CA  ILE A 270      19.730  32.784   9.086  1.00  6.77           C  
ATOM   1872  C   ILE A 270      20.531  31.606   9.644  1.00  7.05           C  
ATOM   1873  O   ILE A 270      21.245  30.929   8.904  1.00  5.48           O  
ATOM   1874  CB  ILE A 270      18.804  32.304   7.941  1.00  5.19           C  
ATOM   1875  CG1 ILE A 270      18.157  33.517   7.264  1.00  4.92           C  
ATOM   1876  CG2 ILE A 270      17.738  31.374   8.483  1.00  4.26           C  
ATOM   1877  CD1 ILE A 270      17.267  33.175   6.099  1.00  4.62           C  
ATOM   1878  N   CYS A 271      20.420  31.382  10.954  1.00  6.30           N  
ATOM   1879  CA  CYS A 271      21.132  30.291  11.620  1.00  6.90           C  
ATOM   1880  C   CYS A 271      20.221  29.586  12.606  1.00  7.31           C  
ATOM   1881  O   CYS A 271      19.156  30.095  12.957  1.00  6.90           O  
ATOM   1882  CB  CYS A 271      22.351  30.815  12.393  1.00  5.55           C  
ATOM   1883  SG  CYS A 271      23.269  32.152  11.598  1.00  8.91           S  
ATOM   1884  N   SER A 272      20.649  28.415  13.063  1.00  7.66           N  
ATOM   1885  CA  SER A 272      19.868  27.667  14.039  1.00  9.30           C  
ATOM   1886  C   SER A 272      20.138  28.303  15.404  1.00  9.48           C  
ATOM   1887  O   SER A 272      21.287  28.382  15.854  1.00 11.34           O  
ATOM   1888  CB  SER A 272      20.286  26.197  14.051  1.00  7.66           C  
ATOM   1889  OG  SER A 272      19.347  25.420  14.773  1.00  7.97           O  
ATOM   1890  N   THR A 273      19.077  28.762  16.053  1.00  8.78           N  
ATOM   1891  CA  THR A 273      19.203  29.409  17.349  1.00  8.60           C  
ATOM   1892  C   THR A 273      18.092  28.913  18.272  1.00  8.89           C  
ATOM   1893  O   THR A 273      17.104  28.345  17.810  1.00  9.72           O  
ATOM   1894  CB  THR A 273      19.116  30.944  17.180  1.00  8.65           C  
ATOM   1895  OG1 THR A 273      19.697  31.599  18.314  1.00  7.89           O  
ATOM   1896  CG2 THR A 273      17.673  31.378  17.012  1.00  8.13           C  
ATOM   1897  N   LEU A 274      18.259  29.123  19.574  1.00  9.37           N  
ATOM   1898  CA  LEU A 274      17.261  28.690  20.547  1.00  9.68           C  
ATOM   1899  C   LEU A 274      15.989  29.515  20.408  1.00 10.29           C  
ATOM   1900  O   LEU A 274      16.026  30.744  20.469  1.00 10.15           O  
ATOM   1901  CB  LEU A 274      17.799  28.830  21.977  1.00  7.07           C  
ATOM   1902  CG  LEU A 274      16.786  28.612  23.110  1.00  8.06           C  
ATOM   1903  CD1 LEU A 274      16.357  27.150  23.139  1.00  5.55           C  
ATOM   1904  CD2 LEU A 274      17.398  29.008  24.447  1.00  7.43           C  
ATOM   1905  N   LEU A 275      14.868  28.832  20.219  1.00  8.98           N  
ATOM   1906  CA  LEU A 275      13.585  29.505  20.092  1.00 10.62           C  
ATOM   1907  C   LEU A 275      12.946  29.604  21.473  1.00 11.44           C  
ATOM   1908  O   LEU A 275      12.925  28.636  22.228  1.00 10.93           O  
ATOM   1909  CB  LEU A 275      12.667  28.719  19.145  1.00 10.33           C  
ATOM   1910  CG  LEU A 275      13.153  28.510  17.707  1.00  7.85           C  
ATOM   1911  CD1 LEU A 275      12.060  27.846  16.877  1.00  7.67           C  
ATOM   1912  CD2 LEU A 275      13.536  29.857  17.102  1.00  7.13           C  
ATOM   1913  N   GLU A 276      12.434  30.783  21.805  1.00 13.03           N  
ATOM   1914  CA  GLU A 276      11.789  30.993  23.096  1.00 14.48           C  
ATOM   1915  C   GLU A 276      10.367  31.510  22.882  1.00 13.95           C  
ATOM   1916  O   GLU A 276       9.971  32.523  23.453  1.00 14.81           O  
ATOM   1917  CB  GLU A 276      12.596  31.993  23.931  1.00 14.69           C  
ATOM   1918  CG  GLU A 276      13.967  31.482  24.358  1.00 19.18           C  
ATOM   1919  CD  GLU A 276      14.857  32.588  24.904  1.00 20.87           C  
ATOM   1920  OE1 GLU A 276      15.289  33.455  24.116  1.00 24.44           O  
ATOM   1921  OE2 GLU A 276      15.126  32.591  26.122  1.00 22.60           O  
ATOM   1922  N   GLY A 277       9.602  30.811  22.050  1.00 11.99           N  
ATOM   1923  CA  GLY A 277       8.241  31.237  21.795  1.00 12.85           C  
ATOM   1924  C   GLY A 277       7.993  31.704  20.372  1.00 14.06           C  
ATOM   1925  O   GLY A 277       6.846  31.774  19.936  1.00 13.36           O  
ATOM   1926  N   GLN A 278       9.056  32.024  19.638  1.00 12.06           N  
ATOM   1927  CA  GLN A 278       8.894  32.475  18.261  1.00 11.54           C  
ATOM   1928  C   GLN A 278       8.265  31.366  17.426  1.00 11.29           C  
ATOM   1929  O   GLN A 278       8.610  30.194  17.572  1.00 12.23           O  
ATOM   1930  CB  GLN A 278      10.245  32.880  17.667  1.00 11.92           C  
ATOM   1931  CG  GLN A 278      10.888  34.086  18.348  1.00 11.08           C  
ATOM   1932  CD  GLN A 278      11.903  33.683  19.399  1.00 10.73           C  
ATOM   1933  OE1 GLN A 278      11.930  32.535  19.836  1.00 13.70           O  
ATOM   1934  NE2 GLN A 278      12.741  34.623  19.808  1.00 10.72           N  
ATOM   1935  N   TYR A 279       7.330  31.742  16.560  1.00 10.87           N  
ATOM   1936  CA  TYR A 279       6.637  30.788  15.699  1.00 10.13           C  
ATOM   1937  C   TYR A 279       5.817  29.786  16.517  1.00 11.45           C  
ATOM   1938  O   TYR A 279       5.291  28.814  15.974  1.00 12.36           O  
ATOM   1939  CB  TYR A 279       7.645  30.046  14.819  1.00 10.30           C  
ATOM   1940  CG  TYR A 279       8.613  30.954  14.088  1.00  9.81           C  
ATOM   1941  CD1 TYR A 279       8.193  31.719  13.002  1.00 10.66           C  
ATOM   1942  CD2 TYR A 279       9.955  31.035  14.471  1.00  9.89           C  
ATOM   1943  CE1 TYR A 279       9.082  32.542  12.309  1.00 11.43           C  
ATOM   1944  CE2 TYR A 279      10.856  31.857  13.784  1.00  9.19           C  
ATOM   1945  CZ  TYR A 279      10.411  32.606  12.702  1.00 11.95           C  
ATOM   1946  OH  TYR A 279      11.283  33.410  12.001  1.00  9.69           O  
ATOM   1947  N   GLY A 280       5.704  30.032  17.820  1.00 11.46           N  
ATOM   1948  CA  GLY A 280       4.948  29.141  18.682  1.00 11.15           C  
ATOM   1949  C   GLY A 280       5.756  27.982  19.243  1.00 11.52           C  
ATOM   1950  O   GLY A 280       5.187  27.047  19.802  1.00 11.17           O  
ATOM   1951  N   HIS A 281       7.078  28.045  19.101  1.00 13.23           N  
ATOM   1952  CA  HIS A 281       7.964  26.989  19.591  1.00 12.50           C  
ATOM   1953  C   HIS A 281       8.928  27.473  20.669  1.00 11.30           C  
ATOM   1954  O   HIS A 281       9.411  28.605  20.631  1.00 10.50           O  
ATOM   1955  CB  HIS A 281       8.754  26.383  18.430  1.00 10.08           C  
ATOM   1956  CG  HIS A 281       7.886  25.836  17.343  1.00 10.76           C  
ATOM   1957  ND1 HIS A 281       7.305  24.588  17.415  1.00 10.16           N  
ATOM   1958  CD2 HIS A 281       7.457  26.386  16.183  1.00  9.36           C  
ATOM   1959  CE1 HIS A 281       6.552  24.396  16.346  1.00 12.02           C  
ATOM   1960  NE2 HIS A 281       6.627  25.472  15.583  1.00 10.08           N  
ATOM   1961  N   SER A 282       9.203  26.591  21.626  1.00 10.74           N  
ATOM   1962  CA  SER A 282      10.094  26.887  22.739  1.00 11.29           C  
ATOM   1963  C   SER A 282      10.975  25.689  23.077  1.00 12.39           C  
ATOM   1964  O   SER A 282      10.672  24.556  22.701  1.00 11.49           O  
ATOM   1965  CB  SER A 282       9.276  27.260  23.976  1.00 12.35           C  
ATOM   1966  OG  SER A 282       9.241  28.664  24.166  1.00 20.10           O  
ATOM   1967  N   ASP A 283      12.064  25.951  23.794  1.00 11.95           N  
ATOM   1968  CA  ASP A 283      12.987  24.909  24.225  1.00 13.85           C  
ATOM   1969  C   ASP A 283      13.434  24.007  23.081  1.00 13.91           C  
ATOM   1970  O   ASP A 283      13.509  22.782  23.229  1.00 12.74           O  
ATOM   1971  CB  ASP A 283      12.330  24.076  25.330  1.00 17.06           C  
ATOM   1972  CG  ASP A 283      11.818  24.939  26.479  1.00 24.60           C  
ATOM   1973  OD1 ASP A 283      12.653  25.474  27.247  1.00 24.48           O  
ATOM   1974  OD2 ASP A 283      10.580  25.090  26.611  1.00 24.90           O  
ATOM   1975  N   ILE A 285      13.740  24.627  21.945  1.00 10.51           N  
ATOM   1976  CA  ILE A 285      14.172  23.899  20.763  1.00  8.43           C  
ATOM   1977  C   ILE A 285      14.907  24.885  19.860  1.00  7.60           C  
ATOM   1978  O   ILE A 285      14.643  26.086  19.912  1.00  8.29           O  
ATOM   1979  CB  ILE A 285      12.943  23.299  20.011  1.00  7.72           C  
ATOM   1980  CG1 ILE A 285      13.389  22.174  19.082  1.00  7.02           C  
ATOM   1981  CG2 ILE A 285      12.215  24.384  19.230  1.00  8.26           C  
ATOM   1982  CD1 ILE A 285      13.562  20.855  19.785  1.00  9.97           C  
ATOM   1983  N   PHE A 286      15.833  24.387  19.048  1.00  6.00           N  
ATOM   1984  CA  PHE A 286      16.585  25.251  18.142  1.00  7.09           C  
ATOM   1985  C   PHE A 286      15.986  25.130  16.748  1.00  5.29           C  
ATOM   1986  O   PHE A 286      15.586  24.044  16.330  1.00  6.11           O  
ATOM   1987  CB  PHE A 286      18.061  24.832  18.090  1.00  6.48           C  
ATOM   1988  CG  PHE A 286      18.915  25.441  19.172  1.00  7.16           C  
ATOM   1989  CD1 PHE A 286      18.680  25.149  20.513  1.00  5.33           C  
ATOM   1990  CD2 PHE A 286      19.975  26.280  18.847  1.00  4.95           C  
ATOM   1991  CE1 PHE A 286      19.485  25.683  21.507  1.00  4.22           C  
ATOM   1992  CE2 PHE A 286      20.789  26.820  19.837  1.00  3.83           C  
ATOM   1993  CZ  PHE A 286      20.542  26.520  21.169  1.00  5.59           C  
ATOM   1994  N   GLY A 287      15.929  26.245  16.034  1.00  4.67           N  
ATOM   1995  CA  GLY A 287      15.384  26.231  14.692  1.00  4.90           C  
ATOM   1996  C   GLY A 287      16.008  27.326  13.856  1.00  5.43           C  
ATOM   1997  O   GLY A 287      16.535  28.299  14.393  1.00  4.55           O  
ATOM   1998  N   GLY A 288      15.949  27.172  12.540  1.00  5.33           N  
ATOM   1999  CA  GLY A 288      16.523  28.168  11.661  1.00  4.66           C  
ATOM   2000  C   GLY A 288      15.663  29.408  11.541  1.00  6.29           C  
ATOM   2001  O   GLY A 288      14.467  29.324  11.263  1.00  6.29           O  
ATOM   2002  N   THR A 289      16.278  30.566  11.752  1.00  6.25           N  
ATOM   2003  CA  THR A 289      15.571  31.835  11.652  1.00  7.32           C  
ATOM   2004  C   THR A 289      16.605  32.940  11.539  1.00  8.08           C  
ATOM   2005  O   THR A 289      17.733  32.786  12.001  1.00  9.60           O  
ATOM   2006  CB  THR A 289      14.705  32.094  12.912  1.00  7.36           C  
ATOM   2007  OG1 THR A 289      13.958  33.306  12.747  1.00  7.66           O  
ATOM   2008  CG2 THR A 289      15.584  32.221  14.146  1.00  4.74           C  
ATOM   2009  N   PRO A 290      16.253  34.056  10.885  1.00  7.49           N  
ATOM   2010  CA  PRO A 290      17.237  35.133  10.782  1.00  8.26           C  
ATOM   2011  C   PRO A 290      17.582  35.695  12.161  1.00  8.22           C  
ATOM   2012  O   PRO A 290      16.705  35.889  13.010  1.00  9.46           O  
ATOM   2013  CB  PRO A 290      16.543  36.178   9.904  1.00  6.93           C  
ATOM   2014  CG  PRO A 290      15.084  35.864  10.015  1.00  8.15           C  
ATOM   2015  CD  PRO A 290      15.002  34.377  10.175  1.00  7.66           C  
ATOM   2016  N   VAL A 291      18.869  35.935  12.379  1.00  7.67           N  
ATOM   2017  CA  VAL A 291      19.354  36.502  13.633  1.00  4.80           C  
ATOM   2018  C   VAL A 291      20.387  37.556  13.252  1.00  6.27           C  
ATOM   2019  O   VAL A 291      20.774  37.656  12.084  1.00  6.08           O  
ATOM   2020  CB  VAL A 291      20.043  35.436  14.526  1.00  3.75           C  
ATOM   2021  CG1 VAL A 291      19.047  34.373  14.948  1.00  2.97           C  
ATOM   2022  CG2 VAL A 291      21.207  34.803  13.781  1.00  3.71           C  
ATOM   2023  N   VAL A 292      20.824  38.347  14.223  1.00  7.58           N  
ATOM   2024  CA  VAL A 292      21.840  39.362  13.973  1.00  5.96           C  
ATOM   2025  C   VAL A 292      23.073  38.955  14.777  1.00  7.46           C  
ATOM   2026  O   VAL A 292      23.003  38.841  16.002  1.00  8.23           O  
ATOM   2027  CB  VAL A 292      21.364  40.755  14.442  1.00  6.31           C  
ATOM   2028  CG1 VAL A 292      22.440  41.801  14.155  1.00  4.96           C  
ATOM   2029  CG2 VAL A 292      20.062  41.117  13.742  1.00  6.96           C  
ATOM   2030  N   LEU A 293      24.193  38.722  14.092  1.00  6.61           N  
ATOM   2031  CA  LEU A 293      25.430  38.323  14.767  1.00  7.24           C  
ATOM   2032  C   LEU A 293      26.413  39.483  14.873  1.00  6.66           C  
ATOM   2033  O   LEU A 293      26.824  40.056  13.866  1.00  7.19           O  
ATOM   2034  CB  LEU A 293      26.104  37.154  14.026  1.00  4.06           C  
ATOM   2035  CG  LEU A 293      25.279  35.884  13.805  1.00  4.48           C  
ATOM   2036  CD1 LEU A 293      26.109  34.867  13.039  1.00  2.06           C  
ATOM   2037  CD2 LEU A 293      24.841  35.308  15.143  1.00  4.10           C  
ATOM   2038  N   GLY A 294      26.793  39.809  16.104  1.00  9.35           N  
ATOM   2039  CA  GLY A 294      27.728  40.892  16.344  1.00  9.25           C  
ATOM   2040  C   GLY A 294      28.663  40.510  17.472  1.00  8.82           C  
ATOM   2041  O   GLY A 294      28.737  39.336  17.828  1.00  9.54           O  
ATOM   2042  N   ALA A 295      29.362  41.491  18.038  1.00  9.28           N  
ATOM   2043  CA  ALA A 295      30.307  41.235  19.125  1.00 11.22           C  
ATOM   2044  C   ALA A 295      29.677  40.533  20.327  1.00 11.69           C  
ATOM   2045  O   ALA A 295      30.373  39.851  21.080  1.00 14.23           O  
ATOM   2046  CB  ALA A 295      30.955  42.536  19.568  1.00  8.11           C  
ATOM   2047  N   ASN A 296      28.369  40.693  20.507  1.00 12.18           N  
ATOM   2048  CA  ASN A 296      27.670  40.062  21.625  1.00 12.71           C  
ATOM   2049  C   ASN A 296      27.005  38.743  21.234  1.00 11.27           C  
ATOM   2050  O   ASN A 296      26.108  38.262  21.926  1.00 11.32           O  
ATOM   2051  CB  ASN A 296      26.619  41.016  22.189  1.00 17.01           C  
ATOM   2052  CG  ASN A 296      27.235  42.174  22.955  1.00 24.06           C  
ATOM   2053  OD1 ASN A 296      27.989  41.970  23.908  1.00 29.12           O  
ATOM   2054  ND2 ASN A 296      26.917  43.398  22.540  1.00 27.86           N  
ATOM   2055  N   GLY A 297      27.451  38.163  20.126  1.00  9.78           N  
ATOM   2056  CA  GLY A 297      26.885  36.908  19.657  1.00  9.75           C  
ATOM   2057  C   GLY A 297      25.570  37.132  18.941  1.00  9.85           C  
ATOM   2058  O   GLY A 297      25.479  37.969  18.042  1.00  8.09           O  
ATOM   2059  N   VAL A 298      24.550  36.369  19.327  1.00  9.32           N  
ATOM   2060  CA  VAL A 298      23.225  36.522  18.747  1.00  8.37           C  
ATOM   2061  C   VAL A 298      22.632  37.742  19.461  1.00 10.62           C  
ATOM   2062  O   VAL A 298      22.117  37.640  20.576  1.00  8.55           O  
ATOM   2063  CB  VAL A 298      22.346  35.287  19.025  1.00  8.39           C  
ATOM   2064  CG1 VAL A 298      20.946  35.513  18.478  1.00  8.09           C  
ATOM   2065  CG2 VAL A 298      22.975  34.049  18.404  1.00  4.89           C  
ATOM   2066  N   GLU A 299      22.725  38.898  18.818  1.00  9.55           N  
ATOM   2067  CA  GLU A 299      22.229  40.134  19.401  1.00  9.05           C  
ATOM   2068  C   GLU A 299      20.737  40.328  19.215  1.00  9.31           C  
ATOM   2069  O   GLU A 299      20.103  41.050  19.978  1.00  9.49           O  
ATOM   2070  CB  GLU A 299      22.998  41.309  18.811  1.00  9.44           C  
ATOM   2071  CG  GLU A 299      24.485  41.050  18.814  1.00 10.57           C  
ATOM   2072  CD  GLU A 299      25.306  42.289  18.589  1.00 12.64           C  
ATOM   2073  OE1 GLU A 299      24.804  43.242  17.950  1.00 13.95           O  
ATOM   2074  OE2 GLU A 299      26.465  42.302  19.049  1.00 12.93           O  
ATOM   2075  N   GLN A 301      20.180  39.684  18.197  1.00  9.26           N  
ATOM   2076  CA  GLN A 301      18.755  39.778  17.929  1.00  9.33           C  
ATOM   2077  C   GLN A 301      18.283  38.502  17.255  1.00  8.52           C  
ATOM   2078  O   GLN A 301      18.984  37.940  16.414  1.00  9.71           O  
ATOM   2079  CB  GLN A 301      18.436  40.947  16.990  1.00 11.76           C  
ATOM   2080  CG  GLN A 301      19.016  42.293  17.368  1.00 12.91           C  
ATOM   2081  CD  GLN A 301      18.586  43.387  16.403  1.00 16.94           C  
ATOM   2082  OE1 GLN A 301      17.413  43.477  16.031  1.00 17.60           O  
ATOM   2083  NE2 GLN A 301      19.535  44.222  15.990  1.00 13.67           N  
ATOM   2084  N   VAL A 302      17.107  38.036  17.650  1.00  8.78           N  
ATOM   2085  CA  VAL A 302      16.506  36.864  17.029  1.00  7.10           C  
ATOM   2086  C   VAL A 302      15.306  37.470  16.311  1.00  9.64           C  
ATOM   2087  O   VAL A 302      14.408  38.023  16.946  1.00  8.05           O  
ATOM   2088  CB  VAL A 302      16.023  35.826  18.062  1.00  6.07           C  
ATOM   2089  CG1 VAL A 302      15.309  34.685  17.351  1.00  2.85           C  
ATOM   2090  CG2 VAL A 302      17.203  35.276  18.839  1.00  3.28           C  
ATOM   2091  N   ILE A 303      15.310  37.405  14.981  1.00 10.62           N  
ATOM   2092  CA  ILE A 303      14.220  37.977  14.210  1.00 10.06           C  
ATOM   2093  C   ILE A 303      13.162  36.934  13.880  1.00  9.63           C  
ATOM   2094  O   ILE A 303      13.475  35.846  13.393  1.00  8.55           O  
ATOM   2095  CB  ILE A 303      14.749  38.618  12.904  1.00 10.13           C  
ATOM   2096  CG1 ILE A 303      15.650  39.810  13.244  1.00 10.04           C  
ATOM   2097  CG2 ILE A 303      13.594  39.080  12.040  1.00  8.70           C  
ATOM   2098  CD1 ILE A 303      16.698  40.101  12.197  1.00  9.88           C  
ATOM   2099  N   GLU A 304      11.909  37.268  14.171  1.00 10.15           N  
ATOM   2100  CA  GLU A 304      10.799  36.364  13.893  1.00  9.20           C  
ATOM   2101  C   GLU A 304      10.029  36.871  12.691  1.00  9.18           C  
ATOM   2102  O   GLU A 304       9.436  37.952  12.731  1.00  9.14           O  
ATOM   2103  CB  GLU A 304       9.854  36.269  15.093  1.00 10.61           C  
ATOM   2104  CG  GLU A 304       8.639  35.387  14.837  1.00 10.61           C  
ATOM   2105  CD  GLU A 304       7.770  35.214  16.068  1.00 13.52           C  
ATOM   2106  OE1 GLU A 304       8.057  35.865  17.097  1.00 11.98           O  
ATOM   2107  OE2 GLU A 304       6.800  34.425  16.003  1.00 10.83           O  
ATOM   2108  N   LEU A 305      10.063  36.097  11.613  1.00  8.39           N  
ATOM   2109  CA  LEU A 305       9.350  36.458  10.400  1.00  8.43           C  
ATOM   2110  C   LEU A 305       7.859  36.309  10.671  1.00  8.59           C  
ATOM   2111  O   LEU A 305       7.429  35.356  11.321  1.00 10.11           O  
ATOM   2112  CB  LEU A 305       9.762  35.538   9.245  1.00  7.19           C  
ATOM   2113  CG  LEU A 305      11.248  35.518   8.860  1.00  7.75           C  
ATOM   2114  CD1 LEU A 305      11.492  34.489   7.766  1.00  3.29           C  
ATOM   2115  CD2 LEU A 305      11.666  36.896   8.377  1.00  4.54           C  
ATOM   2116  N   GLN A 306       7.071  37.260  10.184  1.00  9.32           N  
ATOM   2117  CA  GLN A 306       5.633  37.208  10.381  1.00 10.12           C  
ATOM   2118  C   GLN A 306       5.008  36.291   9.333  1.00 11.11           C  
ATOM   2119  O   GLN A 306       4.344  36.738   8.397  1.00 11.48           O  
ATOM   2120  CB  GLN A 306       5.050  38.621  10.304  1.00 11.20           C  
ATOM   2121  CG  GLN A 306       5.187  39.383  11.618  1.00 13.33           C  
ATOM   2122  CD  GLN A 306       5.394  40.877  11.436  1.00 15.98           C  
ATOM   2123  OE1 GLN A 306       4.812  41.500  10.545  1.00 14.09           O  
ATOM   2124  NE2 GLN A 306       6.227  41.463  12.291  1.00 18.96           N  
ATOM   2125  N   LEU A 307       5.235  34.994   9.502  1.00 10.20           N  
ATOM   2126  CA  LEU A 307       4.716  33.990   8.584  1.00 11.58           C  
ATOM   2127  C   LEU A 307       3.200  33.828   8.658  1.00 12.30           C  
ATOM   2128  O   LEU A 307       2.578  34.098   9.698  1.00 10.63           O  
ATOM   2129  CB  LEU A 307       5.374  32.637   8.869  1.00 12.58           C  
ATOM   2130  CG  LEU A 307       6.905  32.619   8.999  1.00 13.81           C  
ATOM   2131  CD1 LEU A 307       7.373  31.191   9.277  1.00 10.73           C  
ATOM   2132  CD2 LEU A 307       7.544  33.162   7.721  1.00  7.63           C  
ATOM   2133  N   ASN A 308       2.606  33.395   7.550  1.00 10.69           N  
ATOM   2134  CA  ASN A 308       1.171  33.157   7.525  1.00 11.54           C  
ATOM   2135  C   ASN A 308       0.960  31.732   8.026  1.00 13.70           C  
ATOM   2136  O   ASN A 308       1.926  31.010   8.278  1.00 13.25           O  
ATOM   2137  CB  ASN A 308       0.608  33.324   6.110  1.00 11.84           C  
ATOM   2138  CG  ASN A 308       1.322  32.472   5.091  1.00 13.47           C  
ATOM   2139  OD1 ASN A 308       1.617  31.301   5.335  1.00 11.93           O  
ATOM   2140  ND2 ASN A 308       1.602  33.054   3.929  1.00 12.68           N  
ATOM   2141  N   SER A 309      -0.294  31.325   8.176  1.00 15.55           N  
ATOM   2142  CA  SER A 309      -0.590  29.991   8.678  1.00 17.75           C  
ATOM   2143  C   SER A 309       0.007  28.870   7.835  1.00 17.82           C  
ATOM   2144  O   SER A 309       0.430  27.850   8.377  1.00 18.06           O  
ATOM   2145  CB  SER A 309      -2.099  29.792   8.792  1.00 18.70           C  
ATOM   2146  OG  SER A 309      -2.707  29.829   7.515  1.00 22.50           O  
ATOM   2147  N   GLU A 310       0.045  29.053   6.520  1.00 17.74           N  
ATOM   2148  CA  GLU A 310       0.586  28.029   5.626  1.00 17.64           C  
ATOM   2149  C   GLU A 310       2.087  27.831   5.816  1.00 17.01           C  
ATOM   2150  O   GLU A 310       2.575  26.702   5.865  1.00 16.47           O  
ATOM   2151  CB  GLU A 310       0.288  28.395   4.172  1.00 21.62           C  
ATOM   2152  CG  GLU A 310      -1.200  28.442   3.840  1.00 28.30           C  
ATOM   2153  CD  GLU A 310      -1.854  29.753   4.245  1.00 31.83           C  
ATOM   2154  OE1 GLU A 310      -1.253  30.820   4.003  1.00 35.00           O  
ATOM   2155  OE2 GLU A 310      -2.970  29.718   4.805  1.00 34.38           O  
ATOM   2156  N   GLU A 311       2.821  28.932   5.922  1.00 16.25           N  
ATOM   2157  CA  GLU A 311       4.264  28.855   6.120  1.00 15.63           C  
ATOM   2158  C   GLU A 311       4.548  28.296   7.510  1.00 16.25           C  
ATOM   2159  O   GLU A 311       5.464  27.496   7.697  1.00 14.36           O  
ATOM   2160  CB  GLU A 311       4.888  30.243   5.976  1.00 14.35           C  
ATOM   2161  CG  GLU A 311       4.723  30.833   4.587  1.00 11.66           C  
ATOM   2162  CD  GLU A 311       4.731  32.346   4.593  1.00 12.72           C  
ATOM   2163  OE1 GLU A 311       4.635  32.935   5.689  1.00 12.06           O  
ATOM   2164  OE2 GLU A 311       4.832  32.945   3.500  1.00 15.36           O  
ATOM   2165  N   LYS A 312       3.741  28.722   8.479  1.00 14.35           N  
ATOM   2166  CA  LYS A 312       3.880  28.278   9.858  1.00 15.31           C  
ATOM   2167  C   LYS A 312       3.681  26.770   9.965  1.00 13.80           C  
ATOM   2168  O   LYS A 312       4.330  26.108  10.773  1.00 14.43           O  
ATOM   2169  CB  LYS A 312       2.859  29.002  10.742  1.00 18.82           C  
ATOM   2170  CG  LYS A 312       3.391  29.421  12.102  1.00 25.31           C  
ATOM   2171  CD  LYS A 312       2.712  30.695  12.603  1.00 29.82           C  
ATOM   2172  CE  LYS A 312       1.561  30.390  13.561  1.00 31.80           C  
ATOM   2173  NZ  LYS A 312       1.870  29.273  14.507  1.00 34.72           N  
ATOM   2174  N   ALA A 313       2.780  26.232   9.150  1.00 13.33           N  
ATOM   2175  CA  ALA A 313       2.500  24.797   9.155  1.00 12.79           C  
ATOM   2176  C   ALA A 313       3.749  24.024   8.757  1.00 13.37           C  
ATOM   2177  O   ALA A 313       4.053  22.967   9.323  1.00 12.51           O  
ATOM   2178  CB  ALA A 313       1.355  24.474   8.189  1.00 11.87           C  
ATOM   2179  N   LYS A 314       4.470  24.563   7.780  1.00 14.57           N  
ATOM   2180  CA  LYS A 314       5.697  23.943   7.291  1.00 13.29           C  
ATOM   2181  C   LYS A 314       6.809  24.042   8.334  1.00 12.89           C  
ATOM   2182  O   LYS A 314       7.604  23.113   8.505  1.00 13.60           O  
ATOM   2183  CB  LYS A 314       6.134  24.622   5.994  1.00 14.66           C  
ATOM   2184  CG  LYS A 314       5.295  24.224   4.794  1.00 19.02           C  
ATOM   2185  CD  LYS A 314       5.136  22.715   4.725  1.00 22.71           C  
ATOM   2186  CE  LYS A 314       4.486  22.273   3.427  1.00 26.44           C  
ATOM   2187  NZ  LYS A 314       4.052  20.847   3.499  1.00 28.04           N  
ATOM   2188  N   PHE A 315       6.865  25.178   9.022  1.00  8.98           N  
ATOM   2189  CA  PHE A 315       7.859  25.392  10.058  1.00  9.19           C  
ATOM   2190  C   PHE A 315       7.593  24.345  11.142  1.00 10.95           C  
ATOM   2191  O   PHE A 315       8.526  23.707  11.639  1.00 11.99           O  
ATOM   2192  CB  PHE A 315       7.721  26.812  10.617  1.00  7.88           C  
ATOM   2193  CG  PHE A 315       8.905  27.282  11.429  1.00  9.52           C  
ATOM   2194  CD1 PHE A 315       9.172  26.738  12.682  1.00  8.75           C  
ATOM   2195  CD2 PHE A 315       9.720  28.310  10.961  1.00  9.03           C  
ATOM   2196  CE1 PHE A 315      10.233  27.211  13.462  1.00  7.46           C  
ATOM   2197  CE2 PHE A 315      10.784  28.789  11.733  1.00  9.82           C  
ATOM   2198  CZ  PHE A 315      11.039  28.236  12.987  1.00  8.87           C  
ATOM   2199  N   ASP A 316       6.317  24.156  11.491  1.00 10.51           N  
ATOM   2200  CA  ASP A 316       5.935  23.170  12.511  1.00 10.74           C  
ATOM   2201  C   ASP A 316       6.493  21.802  12.135  1.00 10.98           C  
ATOM   2202  O   ASP A 316       7.004  21.061  12.981  1.00 11.59           O  
ATOM   2203  CB  ASP A 316       4.409  23.068  12.630  1.00  8.97           C  
ATOM   2204  CG  ASP A 316       3.791  24.261  13.333  1.00  9.17           C  
ATOM   2205  OD1 ASP A 316       4.537  25.052  13.949  1.00  9.67           O  
ATOM   2206  OD2 ASP A 316       2.551  24.408  13.268  1.00 11.72           O  
ATOM   2207  N   GLU A 317       6.388  21.476  10.854  1.00 11.54           N  
ATOM   2208  CA  GLU A 317       6.880  20.206  10.341  1.00 14.41           C  
ATOM   2209  C   GLU A 317       8.378  20.069  10.573  1.00 13.15           C  
ATOM   2210  O   GLU A 317       8.871  18.995  10.940  1.00 10.74           O  
ATOM   2211  CB  GLU A 317       6.600  20.109   8.845  1.00 18.62           C  
ATOM   2212  CG  GLU A 317       5.368  19.314   8.497  1.00 24.14           C  
ATOM   2213  CD  GLU A 317       5.223  19.125   7.006  1.00 26.66           C  
ATOM   2214  OE1 GLU A 317       5.949  18.281   6.435  1.00 29.11           O  
ATOM   2215  OE2 GLU A 317       4.384  19.824   6.406  1.00 30.03           O  
ATOM   2216  N   ALA A 318       9.101  21.160  10.345  1.00 11.65           N  
ATOM   2217  CA  ALA A 318      10.547  21.155  10.528  1.00 11.93           C  
ATOM   2218  C   ALA A 318      10.891  20.880  11.989  1.00 10.14           C  
ATOM   2219  O   ALA A 318      11.710  20.012  12.289  1.00 10.01           O  
ATOM   2220  CB  ALA A 318      11.135  22.486  10.084  1.00 11.53           C  
ATOM   2221  N   ILE A 319      10.252  21.615  12.895  1.00 11.00           N  
ATOM   2222  CA  ILE A 319      10.491  21.454  14.326  1.00 10.85           C  
ATOM   2223  C   ILE A 319      10.172  20.026  14.785  1.00 11.30           C  
ATOM   2224  O   ILE A 319      10.915  19.440  15.577  1.00 11.14           O  
ATOM   2225  CB  ILE A 319       9.640  22.468  15.141  1.00 11.06           C  
ATOM   2226  CG1 ILE A 319      10.015  23.900  14.745  1.00 12.17           C  
ATOM   2227  CG2 ILE A 319       9.862  22.269  16.626  1.00 11.88           C  
ATOM   2228  CD1 ILE A 319      11.496  24.229  14.925  1.00 16.12           C  
ATOM   2229  N   ALA A 320       9.073  19.469  14.276  1.00 10.44           N  
ATOM   2230  CA  ALA A 320       8.660  18.113  14.624  1.00 10.42           C  
ATOM   2231  C   ALA A 320       9.747  17.080  14.318  1.00 10.17           C  
ATOM   2232  O   ALA A 320       9.993  16.174  15.116  1.00  9.88           O  
ATOM   2233  CB  ALA A 320       7.389  17.751  13.877  1.00  7.27           C  
ATOM   2234  N   GLU A 321      10.389  17.211  13.162  1.00  9.97           N  
ATOM   2235  CA  GLU A 321      11.438  16.279  12.771  1.00  9.04           C  
ATOM   2236  C   GLU A 321      12.660  16.441  13.682  1.00  9.28           C  
ATOM   2237  O   GLU A 321      13.323  15.463  14.023  1.00 10.19           O  
ATOM   2238  CB  GLU A 321      11.825  16.512  11.308  1.00  9.85           C  
ATOM   2239  CG  GLU A 321      12.968  15.639  10.809  1.00 11.04           C  
ATOM   2240  CD  GLU A 321      12.681  14.153  10.953  1.00 14.33           C  
ATOM   2241  OE1 GLU A 321      11.512  13.791  11.197  1.00 13.49           O  
ATOM   2242  OE2 GLU A 321      13.628  13.346  10.821  1.00 15.85           O  
ATOM   2243  N   THR A 322      12.948  17.676  14.074  1.00  7.21           N  
ATOM   2244  CA  THR A 322      14.076  17.962  14.959  1.00  8.89           C  
ATOM   2245  C   THR A 322      13.824  17.323  16.326  1.00  9.78           C  
ATOM   2246  O   THR A 322      14.721  16.721  16.920  1.00  9.50           O  
ATOM   2247  CB  THR A 322      14.264  19.487  15.128  1.00  7.94           C  
ATOM   2248  OG1 THR A 322      14.643  20.054  13.870  1.00  7.93           O  
ATOM   2249  CG2 THR A 322      15.336  19.797  16.180  1.00  3.54           C  
ATOM   2250  N   LYS A 323      12.595  17.461  16.816  1.00 12.22           N  
ATOM   2251  CA  LYS A 323      12.210  16.889  18.102  1.00 14.97           C  
ATOM   2252  C   LYS A 323      12.272  15.376  18.024  1.00 14.26           C  
ATOM   2253  O   LYS A 323      12.702  14.714  18.966  1.00 15.98           O  
ATOM   2254  CB  LYS A 323      10.790  17.308  18.473  1.00 16.13           C  
ATOM   2255  CG  LYS A 323      10.656  18.761  18.874  1.00 18.44           C  
ATOM   2256  CD  LYS A 323       9.226  19.084  19.279  1.00 20.83           C  
ATOM   2257  CE  LYS A 323       9.091  19.176  20.785  1.00 22.92           C  
ATOM   2258  NZ  LYS A 323       9.179  20.588  21.260  1.00 26.56           N  
ATOM   2259  N   ARG A 324      11.828  14.831  16.896  1.00 13.99           N  
ATOM   2260  CA  ARG A 324      11.840  13.390  16.694  1.00 14.40           C  
ATOM   2261  C   ARG A 324      13.261  12.857  16.857  1.00 15.92           C  
ATOM   2262  O   ARG A 324      13.506  11.919  17.616  1.00 16.72           O  
ATOM   2263  CB  ARG A 324      11.323  13.042  15.296  1.00 12.56           C  
ATOM   2264  CG  ARG A 324      11.217  11.545  15.031  1.00 14.80           C  
ATOM   2265  CD  ARG A 324      10.882  11.258  13.574  1.00 12.98           C  
ATOM   2266  NE  ARG A 324      12.043  11.387  12.696  1.00 13.76           N  
ATOM   2267  CZ  ARG A 324      13.083  10.557  12.699  1.00 12.69           C  
ATOM   2268  NH1 ARG A 324      13.107   9.526  13.531  1.00 11.80           N  
ATOM   2269  NH2 ARG A 324      14.096  10.754  11.866  1.00 11.37           N  
ATOM   2270  N   MET A 325      14.201  13.467  16.145  1.00 15.56           N  
ATOM   2271  CA  MET A 325      15.584  13.026  16.210  1.00 14.18           C  
ATOM   2272  C   MET A 325      16.236  13.333  17.553  1.00 14.66           C  
ATOM   2273  O   MET A 325      17.066  12.561  18.038  1.00 14.53           O  
ATOM   2274  CB  MET A 325      16.374  13.646  15.059  1.00 14.12           C  
ATOM   2275  CG  MET A 325      16.002  13.042  13.708  1.00 13.70           C  
ATOM   2276  SD  MET A 325      17.022  13.610  12.351  1.00 16.12           S  
ATOM   2277  CE  MET A 325      16.583  15.317  12.319  1.00  9.51           C  
ATOM   2278  N   LYS A 326      15.856  14.448  18.166  1.00 14.87           N  
ATOM   2279  CA  LYS A 326      16.420  14.806  19.457  1.00 14.48           C  
ATOM   2280  C   LYS A 326      16.105  13.695  20.457  1.00 15.07           C  
ATOM   2281  O   LYS A 326      16.955  13.290  21.248  1.00 15.46           O  
ATOM   2282  CB  LYS A 326      15.825  16.128  19.940  1.00 15.59           C  
ATOM   2283  CG  LYS A 326      16.424  16.650  21.230  1.00 15.85           C  
ATOM   2284  CD  LYS A 326      16.044  18.105  21.449  1.00 18.27           C  
ATOM   2285  CE  LYS A 326      14.908  18.233  22.446  1.00 18.90           C  
ATOM   2286  NZ  LYS A 326      14.657  19.653  22.830  1.00 19.65           N  
ATOM   2287  N   ALA A 327      14.878  13.192  20.399  1.00 15.12           N  
ATOM   2288  CA  ALA A 327      14.441  12.139  21.298  1.00 15.04           C  
ATOM   2289  C   ALA A 327      15.250  10.847  21.172  1.00 17.64           C  
ATOM   2290  O   ALA A 327      15.276  10.048  22.106  1.00 18.33           O  
ATOM   2291  CB  ALA A 327      12.965  11.849  21.069  1.00 15.28           C  
ATOM   2292  N   LEU A 328      15.916  10.642  20.038  1.00 17.75           N  
ATOM   2293  CA  LEU A 328      16.701   9.424  19.826  1.00 18.12           C  
ATOM   2294  C   LEU A 328      18.184   9.545  20.158  1.00 19.95           C  
ATOM   2295  O   LEU A 328      18.937   8.584  19.997  1.00 18.48           O  
ATOM   2296  CB  LEU A 328      16.565   8.953  18.378  1.00 18.69           C  
ATOM   2297  CG  LEU A 328      15.145   8.618  17.923  1.00 19.42           C  
ATOM   2298  CD1 LEU A 328      15.105   8.519  16.409  1.00 18.04           C  
ATOM   2299  CD2 LEU A 328      14.698   7.314  18.563  1.00 16.45           C  
ATOM   2300  N   ALA A 329      18.607  10.718  20.616  1.00 21.25           N  
ATOM   2301  CA  ALA A 329      20.011  10.933  20.948  1.00 22.90           C  
ATOM   2302  C   ALA A 329      20.329  10.530  22.382  1.00 24.81           C  
ATOM   2303  O   ALA A 329      21.519  10.265  22.652  1.00 28.14           O  
ATOM   2304  CB  ALA A 329      20.381  12.389  20.725  1.00 20.69           C  
ATOM   2305  OXT ALA A 329      19.399  10.485  23.214  1.00 27.46           O  
TER    2306      ALA A 329                                                      
HETATM 2307 CL   CLQ A1001      37.297  16.530  16.467  1.00 22.69          CL  
HETATM 2308  N1  CLQ A1001      35.701  11.650  16.106  1.00 34.43           N  
HETATM 2309  C1  CLQ A1001      35.183  10.503  16.591  1.00 35.26           C  
HETATM 2310  C2  CLQ A1001      34.822  10.374  17.926  1.00 34.24           C  
HETATM 2311  C3  CLQ A1001      35.015  11.469  18.876  1.00 31.96           C  
HETATM 2312  C4  CLQ A1001      35.592  12.727  18.358  1.00 33.68           C  
HETATM 2313  C5  CLQ A1001      35.842  13.931  19.150  1.00 34.90           C  
HETATM 2314  C6  CLQ A1001      36.377  15.090  18.572  1.00 32.93           C  
HETATM 2315  C7  CLQ A1001      36.675  15.093  17.170  1.00 31.88           C  
HETATM 2316  C8  CLQ A1001      36.455  13.968  16.359  1.00 32.37           C  
HETATM 2317  C9  CLQ A1001      35.916  12.783  16.930  1.00 35.42           C  
HETATM 2318  N2  CLQ A1001      34.672  11.370  20.198  1.00 30.60           N  
HETATM 2319  C10 CLQ A1001      34.214  10.146  20.938  1.00 29.84           C  
HETATM 2320  C11 CLQ A1001      35.312   9.073  20.884  1.00 31.56           C  
HETATM 2321  C12 CLQ A1001      36.619   9.399  21.583  1.00 32.62           C  
HETATM 2322  C13 CLQ A1001      37.706   8.452  21.099  1.00 31.65           C  
HETATM 2323  N3  CLQ A1001      37.415   7.004  21.379  1.00 36.76           N  
HETATM 2324  C14 CLQ A1001      38.266   6.049  20.513  1.00 36.54           C  
HETATM 2325  C15 CLQ A1001      38.079   4.548  20.707  1.00 37.02           C  
HETATM 2326  C16 CLQ A1001      37.314   6.691  22.846  1.00 33.74           C  
HETATM 2327  C17 CLQ A1001      38.620   6.542  23.554  1.00 35.69           C  
HETATM 2328  C18 CLQ A1001      33.802  10.510  22.357  1.00 30.59           C  
HETATM 2329  O   HOH A1002      44.770  30.624   2.693  1.00  9.25           O  
HETATM 2330  O   HOH A1003      14.621  22.755  13.972  1.00  8.79           O  
HETATM 2331  O   HOH A1004      30.008  31.528  25.758  1.00  7.42           O  
HETATM 2332  O   HOH A1005      35.698  22.190  12.514  1.00  7.43           O  
HETATM 2333  O   HOH A1006      35.479  15.268   6.277  1.00  2.10           O  
HETATM 2334  O   HOH A1007      25.221  34.950   2.584  1.00  4.56           O  
HETATM 2335  O   HOH A1008       2.741  26.948  21.017  1.00 11.82           O  
HETATM 2336  O   HOH A1009      19.298  28.103   9.905  1.00  3.37           O  
HETATM 2337  O   HOH A1010      17.444  41.559  -2.795  1.00  4.52           O  
HETATM 2338  O   HOH A1011      52.229  37.868   5.252  1.00 11.34           O  
HETATM 2339  O   HOH A1012      17.176  27.859   8.233  1.00  3.18           O  
HETATM 2340  O   HOH A1013      23.331  36.869   1.407  1.00  8.13           O  
HETATM 2341  O   HOH A1014      17.932  25.759   6.902  1.00 10.55           O  
HETATM 2342  O   HOH A1015      30.716  38.299   7.417  1.00  8.19           O  
HETATM 2343  O   HOH A1016      21.977  38.177  -0.535  1.00  9.22           O  
HETATM 2344  O   HOH A1017      23.787  45.908  -5.742  1.00  6.38           O  
HETATM 2345  O   HOH A1018      33.381  20.356  32.299  1.00  9.35           O  
HETATM 2346  O   HOH A1019      24.791  20.629   2.372  1.00 12.88           O  
HETATM 2347  O   HOH A1020      18.150  32.424  20.604  1.00  6.45           O  
HETATM 2348  O   HOH A1021      22.994  35.128   4.278  1.00  9.99           O  
HETATM 2349  O   HOH A1022      23.558  29.503   8.958  1.00  7.23           O  
HETATM 2350  O   HOH A1023      34.454  13.109  13.654  1.00 22.61           O  
HETATM 2351  O   HOH A1024      21.085  30.180  20.167  1.00  7.31           O  
HETATM 2352  O   HOH A1025      36.243  21.279  -4.116  1.00 15.04           O  
HETATM 2353  O   HOH A1026      18.844  25.927 -11.183  1.00  6.40           O  
HETATM 2354  O   HOH A1027      14.542  39.053   0.531  1.00 11.78           O  
HETATM 2355  O   HOH A1028      34.129  17.985   7.286  1.00 13.61           O  
HETATM 2356  O   HOH A1029      29.634  29.671  29.507  1.00 14.58           O  
HETATM 2357  O   HOH A1030      11.274  43.372 -12.574  1.00 10.22           O  
HETATM 2358  O   HOH A1031      52.522  23.638   1.809  1.00  5.98           O  
HETATM 2359  O   HOH A1032       5.777  34.157  13.274  1.00 16.68           O  
HETATM 2360  O   HOH A1033       7.691  38.480  -4.061  1.00 13.58           O  
HETATM 2361  O   HOH A1034      23.578  33.026   1.709  1.00  6.92           O  
HETATM 2362  O   HOH A1035       9.190  39.340  -1.708  1.00 13.75           O  
HETATM 2363  O   HOH A1036      18.754  19.628  11.612  1.00  8.84           O  
HETATM 2364  O   HOH A1037       8.919  21.550   6.744  1.00  7.96           O  
HETATM 2365  O   HOH A1038      46.662  33.733  -1.105  1.00  9.60           O  
HETATM 2366  O   HOH A1039      20.700  20.137   0.286  1.00  9.20           O  
HETATM 2367  O   HOH A1040      10.346  45.372 -11.078  1.00  7.12           O  
HETATM 2368  O   HOH A1041      34.284  34.978  21.923  1.00  8.39           O  
HETATM 2369  O   HOH A1042      18.814  24.303  25.177  1.00 13.67           O  
HETATM 2370  O   HOH A1043      28.171  16.185  10.169  1.00 27.39           O  
HETATM 2371  O   HOH A1044      32.770  35.960   5.025  1.00 18.56           O  
HETATM 2372  O   HOH A1045      33.140  33.358   3.865  1.00  8.59           O  
HETATM 2373  O   HOH A1046      22.222  44.111  16.907  1.00 13.03           O  
HETATM 2374  O   HOH A1047       6.729  28.810  -7.562  1.00 26.83           O  
HETATM 2375  O   HOH A1048      39.423  20.839   2.745  1.00 16.80           O  
HETATM 2376  O   HOH A1049      46.441  20.585   3.858  1.00 17.58           O  
HETATM 2377  O   HOH A1050      38.552  19.701  -4.207  1.00 27.08           O  
HETATM 2378  O   HOH A1051      23.832  41.377   0.965  1.00 13.31           O  
HETATM 2379  O   HOH A1052      16.209  18.487  12.122  1.00 15.41           O  
HETATM 2380  O   HOH A1053      29.854  26.923  30.274  1.00 24.75           O  
HETATM 2381  O   HOH A1054      34.296  16.294  28.356  1.00 11.70           O  
HETATM 2382  O   HOH A1055      53.339  26.316  10.629  1.00 15.92           O  
HETATM 2383  O   HOH A1056      19.372  35.122   3.823  1.00 11.91           O  
HETATM 2384  O   HOH A1057      16.760  21.578  18.980  1.00  9.74           O  
HETATM 2385  O   HOH A1058      43.518  23.615   5.386  1.00  6.78           O  
HETATM 2386  O   HOH A1059      41.101  24.934   1.227  1.00 12.05           O  
HETATM 2387  O   HOH A1060      41.182  19.591  28.637  1.00 22.68           O  
HETATM 2388  O   HOH A1061      21.145  33.799   5.719  1.00  4.10           O  
HETATM 2389  O   HOH A1062       6.830  29.594  -0.057  1.00 28.60           O  
HETATM 2390  O   HOH A1063      36.189  31.403  27.831  1.00 14.02           O  
HETATM 2391  O   HOH A1064       4.783  32.044 -13.891  1.00 19.93           O  
HETATM 2392  O   HOH A1065      15.061  18.471   8.046  1.00 14.95           O  
HETATM 2393  O   HOH A1066      25.073  36.490 -12.582  1.00 12.80           O  
HETATM 2394  O   HOH A1067      28.364  28.624 -11.951  1.00 17.39           O  
HETATM 2395  O   HOH A1068      14.051  18.815  10.574  1.00 14.52           O  
HETATM 2396  O   HOH A1069      13.117  27.981  25.108  1.00 18.31           O  
HETATM 2397  O   HOH A1070      38.148  13.834  26.320  1.00 17.63           O  
HETATM 2398  O   HOH A1071      10.784  45.207  -1.565  1.00 18.78           O  
HETATM 2399  O   HOH A1072      22.615  37.884   3.739  1.00 17.37           O  
HETATM 2400  O   HOH A1073      16.231  39.715 -14.769  1.00 11.47           O  
HETATM 2401  O   HOH A1074      45.205  36.215  -0.666  1.00 15.73           O  
HETATM 2402  O   HOH A1075      35.757  43.417  16.297  1.00 18.00           O  
HETATM 2403  O   HOH A1076      12.456  15.745  21.497  1.00 29.83           O  
HETATM 2404  O   HOH A1077      33.407  17.837  -3.531  1.00 25.76           O  
HETATM 2405  O   HOH A1078       6.559  32.160   1.374  1.00 16.06           O  
HETATM 2406  O   HOH A1079       7.840  16.424  10.294  1.00 19.50           O  
HETATM 2407  O   HOH A1080      29.065  18.853  30.455  1.00 29.33           O  
HETATM 2408  O   HOH A1081      14.519  20.675  -9.787  1.00 19.14           O  
HETATM 2409  O   HOH A1082      51.691  21.877  11.976  1.00 16.92           O  
HETATM 2410  O   HOH A1083      10.722  32.470 -17.879  1.00 14.58           O  
HETATM 2411  O   HOH A1084       7.788  27.966 -17.188  1.00 19.32           O  
HETATM 2412  O   HOH A1085      20.436  23.964   0.065  1.00 15.50           O  
HETATM 2413  O   HOH A1086      11.890   9.904  18.480  1.00 18.77           O  
HETATM 2414  O   HOH A1087      14.407  26.514 -13.067  1.00 12.81           O  
HETATM 2415  O   HOH A1088      20.362  19.523 -11.938  1.00 30.06           O  
HETATM 2416  O   HOH A1089      13.051  32.781   0.516  1.00 17.43           O  
HETATM 2417  O   HOH A1090       6.193  20.951  15.624  1.00 16.55           O  
HETATM 2418  O   HOH A1091      25.555  20.673  31.351  1.00 21.45           O  
HETATM 2419  O   HOH A1092      48.871  20.769  21.093  1.00 31.75           O  
HETATM 2420  O   HOH A1093      30.663  11.209  25.719  1.00 23.96           O  
HETATM 2421  O   HOH A1094      -0.164  27.032  10.883  1.00 25.46           O  
HETATM 2422  O   HOH A1095      47.230  28.562  16.155  1.00 12.39           O  
HETATM 2423  O   HOH A1096      11.232  20.769   2.712  1.00 14.05           O  
HETATM 2424  O   HOH A1097      40.835  35.367  -0.950  1.00 11.11           O  
HETATM 2425  O   HOH A1098      13.239  24.786 -14.831  1.00 15.87           O  
HETATM 2426  O   HOH A1099      20.684  44.154  -3.642  1.00  9.69           O  
HETATM 2427  O   HOH A1100       3.122  41.046   8.572  1.00 25.65           O  
HETATM 2428  O   HOH A1101       7.720  39.335  14.330  1.00 13.18           O  
HETATM 2429  O   HOH A1102      42.218  36.177  21.827  1.00 22.02           O  
HETATM 2430  O   HOH A1103      19.403  25.203  10.790  1.00 25.36           O  
HETATM 2431  O   HOH A1104      51.458  33.369  10.749  1.00 25.77           O  
HETATM 2432  O   HOH A1105      44.945   8.416  14.636  1.00 21.65           O  
HETATM 2433  O   HOH A1106      35.865  19.183   9.064  1.00 16.53           O  
HETATM 2434  O   HOH A1107      26.472  13.577  11.165  1.00 21.34           O  
HETATM 2435  O   HOH A1108      41.728  38.706  15.335  1.00 18.29           O  
HETATM 2436  O   HOH A1109      15.398  42.722  17.753  1.00 26.59           O  
HETATM 2437  O   HOH A1110       2.938  31.979   1.525  1.00 24.49           O  
HETATM 2438  O   HOH A1111      40.291  14.824   5.526  1.00 25.88           O  
HETATM 2439  O   HOH A1112       9.697  37.807  18.190  1.00 15.97           O  
HETATM 2440  O   HOH A1113      17.708  15.743  -0.393  1.00 18.04           O  
HETATM 2441  O   HOH A1114      13.482  40.574  16.852  1.00 21.22           O  
HETATM 2442  O   HOH A1115      38.014  37.873   1.621  1.00 19.65           O  
HETATM 2443  O   HOH A1116      25.497  30.357 -14.648  1.00 29.53           O  
HETATM 2444  O   HOH A1117      32.581  12.443  27.101  1.00 22.37           O  
HETATM 2445  O   HOH A1118      36.133  38.319  20.056  1.00 20.85           O  
HETATM 2446  O   HOH A1119      17.380  15.798   5.750  1.00 25.39           O  
HETATM 2447  O   HOH A1120       2.556  21.020  10.331  1.00 19.44           O  
HETATM 2448  O   HOH A1121       4.889  28.703 -14.518  1.00 19.98           O  
HETATM 2449  O   HOH A1122      46.381  29.500  18.552  1.00 22.72           O  
HETATM 2450  O   HOH A1123      25.969  20.910   6.293  1.00 23.48           O  
HETATM 2451  O   HOH A1124      46.406  14.071  23.125  1.00 22.59           O  
HETATM 2452  O   HOH A1125      15.006  36.689 -17.303  1.00 23.38           O  
HETATM 2453  O   HOH A1126      21.278  31.796  28.283  1.00 15.95           O  
HETATM 2454  O   HOH A1127       1.530  24.585   4.723  1.00 22.53           O  
HETATM 2455  O   HOH A1128       2.130  34.440 -10.900  1.00 28.45           O  
HETATM 2456  O   HOH A1129      21.975   8.392  -9.234  1.00 34.53           O  
HETATM 2457  O   HOH A1130      23.989  12.580  13.874  1.00 10.04           O  
HETATM 2458  O   HOH A1131      19.551  28.522 -12.059  1.00 21.17           O  
HETATM 2459  O   HOH A1132      12.488  37.332  18.612  1.00 14.51           O  
HETATM 2460  O   HOH A1133      50.967  22.194  14.378  1.00 10.86           O  
HETATM 2461  O   HOH A1134      20.033  17.098  -0.485  1.00 25.06           O  
HETATM 2462  O   HOH A1135       8.285  24.509  25.772  1.00 16.18           O  
HETATM 2463  O   HOH A1136       8.835  14.223  11.718  1.00 17.39           O  
HETATM 2464  O   HOH A1137      30.263  16.758  29.239  1.00 13.41           O  
HETATM 2465  O   HOH A1138      48.919  37.359  -3.664  1.00 16.71           O  
HETATM 2466  O   HOH A1139      15.402  14.141   9.166  1.00 24.47           O  
HETATM 2467  O   HOH A1140      37.522  12.381  10.660  1.00 22.11           O  
HETATM 2468  O   HOH A1141       9.982  27.687  27.731  1.00 25.34           O  
HETATM 2469  O   HOH A1142      43.178  20.660  29.869  1.00 25.16           O  
HETATM 2470  O   HOH A1143      32.713  39.574   4.290  1.00 39.96           O  
HETATM 2471  O   HOH A1144      23.134  16.984 -11.621  1.00 23.44           O  
HETATM 2472  O   HOH A1145      23.992  26.035 -11.147  1.00 26.74           O  
HETATM 2473  O   HOH A1146      36.871  14.519  12.297  1.00 21.01           O  
HETATM 2474  O   HOH A1147      16.480  16.394   1.983  1.00 23.50           O  
HETATM 2475  O   HOH A1148      20.617  41.336  -1.380  1.00 20.63           O  
HETATM 2476  O   HOH A1149       9.909  24.503   1.797  1.00 18.25           O  
HETATM 2477  O   HOH A1150      41.229  41.008   9.581  1.00 21.70           O  
HETATM 2478  O   HOH A1151      22.292  11.193  11.917  1.00 21.12           O  
HETATM 2479  O   HOH A1152      20.702  13.840  -8.536  1.00 31.89           O  
HETATM 2480  O   HOH A1153      44.445  37.694   1.438  1.00 24.09           O  
HETATM 2481  O   HOH A1154      19.369  19.407  -6.365  1.00 18.46           O  
HETATM 2482  O   HOH A1155      18.025  17.789  -7.636  1.00 25.73           O  
HETATM 2483  O   HOH A1156      17.002   4.583  15.504  1.00 35.55           O  
HETATM 2484  O   HOH A1157       9.152  23.014 -13.180  1.00 20.10           O  
HETATM 2485  O   HOH A1158       5.956  34.385 -15.219  1.00 19.15           O  
HETATM 2486  O   HOH A1159      11.470   8.339  15.313  1.00 27.93           O  
HETATM 2487  O   HOH A1160       8.017  36.024  -4.454  1.00 17.92           O  
HETATM 2488  O   HOH A1161      32.393  46.030  11.794  1.00 20.53           O  
HETATM 2489  O   HOH A1162      10.008  21.569 -10.286  1.00 22.71           O  
HETATM 2490  O   HOH A1163      46.124  45.330  18.583  1.00 24.79           O  
HETATM 2491  O   HOH A1164      45.413  34.525  19.348  1.00 21.99           O  
HETATM 2492  O   HOH A1165       4.663  26.200 -10.646  1.00 35.54           O  
HETATM 2493  O   HOH A1166      37.098  44.742  14.141  1.00 18.71           O  
HETATM 2494  O   HOH A1167       8.057  14.645  16.344  1.00 21.82           O  
HETATM 2495  O   HOH A1168      47.067   9.000  11.345  1.00 25.86           O  
HETATM 2496  O   HOH A1169      35.167  14.355  -5.477  1.00 23.88           O  
HETATM 2497  O   HOH A1170      14.947  33.232  21.343  1.00 18.19           O  
HETATM 2498  O   HOH A1171      35.489  16.336  11.102  1.00 24.62           O  
HETATM 2499  O   HOH A1172       8.988  23.325  20.187  1.00 29.72           O  
HETATM 2500  O   HOH A1173      21.327  21.396   2.566  1.00 30.51           O  
HETATM 2501  O   HOH A1174      51.735  24.592  11.518  1.00 12.20           O  
HETATM 2502  O   HOH A1175      22.931  28.253 -11.697  1.00 23.67           O  
HETATM 2503  O   HOH A1176      49.158  35.131  18.227  1.00 21.95           O  
HETATM 2504  O   HOH A1177      23.950  12.466 -11.088  1.00 36.51           O  
HETATM 2505  O   HOH A1178      40.758  22.413   1.308  1.00 29.75           O  
HETATM 2506  O   HOH A1179      40.472  39.278   2.497  1.00 23.45           O  
HETATM 2507  O   HOH A1180      44.543  39.512   4.612  1.00 38.86           O  
HETATM 2508  O   HOH A1181      27.661  23.012  35.220  1.00 31.78           O  
HETATM 2509  O   HOH A1182      22.136  19.297   9.422  1.00 21.82           O  
HETATM 2510  O   HOH A1183      11.164  43.536 -19.505  1.00 33.42           O  
HETATM 2511  O   HOH A1184      15.595  39.921  19.432  1.00 22.79           O  
HETATM 2512  O   HOH A1185      38.055  31.714  26.127  1.00 20.03           O  
HETATM 2513  O   HOH A1186      45.081  11.188   7.687  1.00 41.18           O  
HETATM 2514  O   HOH A1187      24.031   8.805  23.649  1.00 34.26           O  
HETATM 2515  O   HOH A1188       3.847  38.876   7.053  1.00 21.50           O  
HETATM 2516  O   HOH A1189      15.611  19.845  25.535  1.00 28.01           O  
HETATM 2517  O   HOH A1190       3.255  26.449  15.921  1.00 25.43           O  
HETATM 2518  O   HOH A1191       7.523  33.579 -17.434  1.00 23.95           O  
HETATM 2519  O   HOH A1192      14.471  14.352  23.719  1.00 44.07           O  
HETATM 2520  O   HOH A1193      37.573  11.986  13.969  1.00 20.05           O  
HETATM 2521  O   HOH A1194      41.382  24.409  32.823  1.00 25.24           O  
HETATM 2522  O   HOH A1195      20.036  36.407  22.094  1.00 19.66           O  
HETATM 2523  O   HOH A1196      38.733   9.429  11.346  1.00 28.89           O  
HETATM 2524  O   HOH A1197      24.522  18.833   8.585  1.00 23.35           O  
HETATM 2525  O   HOH A1198      20.476  14.381   8.986  1.00 29.60           O  
HETATM 2526  O   HOH A1199      39.237  39.810   6.120  1.00 35.06           O  
HETATM 2527  O   HOH A1200      19.618  47.550  -5.047  1.00 24.21           O  
HETATM 2528  O   HOH A1201      18.607  14.229  24.490  1.00 42.01           O  
HETATM 2529  O   HOH A1202      23.138  23.080  30.445  1.00 41.09           O  
HETATM 2530  O   HOH A1203      16.813  31.953 -18.569  1.00 25.84           O  
HETATM 2531  O   HOH A1204      28.489  47.480  18.545  1.00 37.41           O  
HETATM 2532  O   HOH A1205      48.632  43.181   5.092  1.00 33.91           O  
HETATM 2533  O   HOH A1206      52.295  23.356  16.358  1.00 35.91           O  
HETATM 2534  O   HOH A1207      18.366  15.010  -6.743  1.00 35.19           O  
HETATM 2535  O   HOH A1208      23.239  14.809  -9.595  1.00 29.28           O  
HETATM 2536  O   HOH A1209      17.963  19.029   2.240  1.00 22.30           O  
HETATM 2537  O   HOH A1210      18.823   6.082  17.211  1.00 26.61           O  
HETATM 2538  O   HOH A1211      21.207  29.409  28.022  1.00 27.65           O  
HETATM 2539  O   HOH A1212      18.665   6.066  20.061  1.00 24.88           O  
HETATM 2540  O   HOH A1213       2.756  30.868 -16.255  1.00 34.33           O  
HETATM 2541  O   HOH A1214      24.840  37.215 -15.096  1.00 32.71           O  
HETATM 2542  O   HOH A1215      35.335  16.004  -3.502  1.00 25.19           O  
HETATM 2543  O   HOH A1216      46.851  45.880  20.760  1.00 38.91           O  
HETATM 2544  O   HOH A1217       9.521  43.872   0.434  1.00 28.30           O  
HETATM 2545  O   HOH A1218      13.710  10.452  24.422  1.00 30.38           O  
HETATM 2546  O   HOH A1219      24.774  36.454  27.890  1.00 25.49           O  
HETATM 2547  O   HOH A1220      -1.660  30.295  12.720  1.00 34.92           O  
HETATM 2548  O   HOH A1221       5.639  40.454   5.307  1.00 30.76           O  
HETATM 2549  O   HOH A1222       9.058  13.577  19.073  1.00 33.40           O  
HETATM 2550  O   HOH A1223      27.440   7.350 -11.981  1.00 37.89           O  
HETATM 2551  O   HOH A1224      22.386   0.839   9.328  1.00 39.52           O  
HETATM 2552  O   HOH A1225      21.107  43.243  20.986  1.00 34.86           O  
HETATM 2553  O   HOH A1226      34.252  11.110  11.684  1.00 35.46           O  
HETATM 2554  O   HOH A1227      23.203  27.886  29.506  1.00 42.93           O  
HETATM 2555  O   HOH A1228      22.551  13.383  27.874  1.00 30.60           O  
HETATM 2556  O   HOH A1229       5.580  34.876  -4.816  1.00 33.56           O  
HETATM 2557  O   HOH A1230      11.505  40.127  14.996  1.00 32.35           O  
HETATM 2558  O   HOH A1231      30.626  15.214  10.374  1.00 24.36           O  
HETATM 2559  O   HOH A1232      40.906  15.486  29.660  1.00 50.05           O  
HETATM 2560  O   HOH A1233      28.837  35.581  27.283  1.00 33.09           O  
HETATM 2561  O   HOH A1234      56.074  33.181  16.154  1.00 33.76           O  
HETATM 2562  O   HOH A1235      36.496  39.485   4.213  1.00 37.26           O  
HETATM 2563  O   HOH A1236      41.120  20.370  33.745  1.00 37.32           O  
HETATM 2564  O   HOH A1237      41.652  22.000  31.545  1.00 35.70           O  
HETATM 2565  O   HOH A1238      32.852  36.993  24.308  1.00 42.21           O  
HETATM 2566  O   HOH A1239      21.601  14.338  25.735  1.00 31.62           O  
HETATM 2567  O   HOH A1240       9.040  22.990  -5.595  1.00 37.91           O  
HETATM 2568  O   HOH A1241      -2.680  26.787   7.577  1.00 39.87           O  
HETATM 2569  O   HOH A1242      25.065  22.418   9.144  1.00 41.25           O  
HETATM 2570  O   HOH A1243      15.314  36.161  22.011  1.00 46.18           O  
HETATM 2571  O   HOH A1244      16.330  24.519 -11.317  1.00 38.25           O  
HETATM 2572  O   HOH A1245      28.055   8.268  -4.522  1.00 39.57           O  
HETATM 2573  O   HOH A1246       9.298  40.310  16.987  1.00 41.16           O  
HETATM 2574  O   HOH A1247      17.275  42.122  21.265  1.00 42.33           O  
HETATM 2575  O   HOH A1248      40.992  14.346  26.975  1.00 39.63           O  
HETATM 2576  O   HOH A1249       0.598  35.990   3.573  1.00 30.71           O  
HETATM 2577  O   HOH A1250      42.499  12.088  26.763  1.00 39.74           O  
HETATM 2578  O   HOH A1251       3.539  24.838  18.727  1.00 33.30           O  
HETATM 2579  O   HOH A1252       8.402   8.099  -3.603  1.00 45.15           O  
HETATM 2580  O   HOH A1253      41.072   5.263  -3.809  1.00 42.36           O  
CONECT 2307 2315                                                                
CONECT 2308 2309 2317                                                           
CONECT 2309 2308 2310                                                           
CONECT 2310 2309 2311                                                           
CONECT 2311 2310 2312 2318                                                      
CONECT 2312 2311 2313 2317                                                      
CONECT 2313 2312 2314                                                           
CONECT 2314 2313 2315                                                           
CONECT 2315 2307 2314 2316                                                      
CONECT 2316 2315 2317                                                           
CONECT 2317 2308 2312 2316                                                      
CONECT 2318 2311 2319                                                           
CONECT 2319 2318 2320 2328                                                      
CONECT 2320 2319 2321                                                           
CONECT 2321 2320 2322                                                           
CONECT 2322 2321 2323                                                           
CONECT 2323 2322 2324 2326                                                      
CONECT 2324 2323 2325                                                           
CONECT 2325 2324                                                                
CONECT 2326 2323 2327                                                           
CONECT 2327 2326                                                                
CONECT 2328 2319                                                                
MASTER      315    0    1   14    9    0    2    6 2579    1   22   25          
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.