HEADER    LYASE                                   15-APR-03   1OFM              
TITLE     CRYSTAL STRUCTURE OF CHONDROITINASE B COMPLEXED TO CHONDROITIN 4-     
TITLE    2 SULFATE TETRASACCHARIDE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHONDROITINASE B;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 4.2.2.4;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: HYDROXY-PROLINE AT N-TERMINUS GLYCOSYLATION AT SER234 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PEDOBACTER HEPARINUS;                           
SOURCE   3 ORGANISM_TAXID: 984;                                                 
SOURCE   4 ATCC: 13125;                                                         
SOURCE   5 EXPRESSION_SYSTEM: PEDOBACTER HEPARINUS;                             
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 984                                         
KEYWDS    ACTIVE SITE, BETA-ELIMINATION, CHONDROITIN 4-SULFATE, LYASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MICHEL,M.CYGLER                                                     
REVDAT  10   13-DEC-23 1OFM    1       HETSYN LINK                              
REVDAT   9   29-JUL-20 1OFM    1       COMPND REMARK HETNAM LINK                
REVDAT   9 2                   1       SITE   ATOM                              
REVDAT   8   11-MAR-20 1OFM    1       SEQRES LINK   ATOM                       
REVDAT   7   14-JUN-17 1OFM    1       ATOM                                     
REVDAT   6   23-JAN-13 1OFM    1       COMPND REMARK VERSN  HET                 
REVDAT   6 2                   1       HETNAM HETSYN FORMUL LINK                
REVDAT   6 3                   1       SITE   SCALE1 SCALE2 SCALE3              
REVDAT   6 4                   1       TER    HETATM CONECT                     
REVDAT   5   24-NOV-09 1OFM    1       VERSN                                    
REVDAT   4   24-FEB-09 1OFM    1       VERSN                                    
REVDAT   3   29-JUL-04 1OFM    1       JRNL                                     
REVDAT   2   27-MAY-04 1OFM    1       JRNL                                     
REVDAT   1   19-APR-04 1OFM    0                                                
JRNL        AUTH   G.MICHEL,K.POJASEK,Y.LI,T.SULEA,R.LINHARDT,R.RAMAN,          
JRNL        AUTH 2 V.PRABHAKAR,R.SASISEKHARAN,M.CYGLER                          
JRNL        TITL   THE STRUCTURE OF CHONDROITIN B LYASE COMPLEXED WITH          
JRNL        TITL 2 GLYCOSAMINOGLYCAN OLIGOSACCHARIDES UNRAVELS A                
JRNL        TITL 3 CALCIUM-DEPENDENT CATALYTIC MACHINERY                        
JRNL        REF    J.BIOL.CHEM.                  V. 279 32882 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15155751                                                     
JRNL        DOI    10.1074/JBC.M403421200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1399907.180                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 40151                          
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) : 0.142                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2010                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6279                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1380                       
REMARK   3   BIN FREE R VALUE                    : 0.1800                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 302                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3784                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 135                                     
REMARK   3   SOLVENT ATOMS            : 806                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.50                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.68000                                             
REMARK   3    B22 (A**2) : 0.21000                                              
REMARK   3    B33 (A**2) : 0.47000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.01000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.14                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.04                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.700                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.960                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 41.46                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.PARAM                             
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OFM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-03.                  
REMARK 100 THE DEPOSITION ID IS D_1290012596.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.750                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1DBG                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, 2-METHYL-2,4- PENTADIOL,        
REMARK 280  AMMONIUM ACETATE, TRIS, PH 8.70                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.03450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR A   182     O    HOH A   701              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A 148   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 107       42.54   -161.83                                   
REMARK 500    ASP A 139     -160.05   -161.64                                   
REMARK 500    SER A 143      169.73    173.61                                   
REMARK 500    ASP A 174      163.15     88.77                                   
REMARK 500    LYS A 187     -159.94     34.03                                   
REMARK 500    ASP A 188       30.04    104.09                                   
REMARK 500    SER A 190      -15.37    -45.73                                   
REMARK 500    TYR A 222      -38.51   -131.34                                   
REMARK 500    ASN A 358       46.51   -160.25                                   
REMARK 500    PRO A 393       24.46    -66.55                                   
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 A1497        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A1498        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A1499        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A1500        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A1501        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A1502        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH A1503        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A1504        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A1505        DISTANCE =  7.26 ANGSTROMS                       
REMARK 525    HOH A1506        DISTANCE =  7.74 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DBG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CHONDROITINASE B                                
REMARK 900 RELATED ID: 1DBO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CHONDROITINASE B                                
REMARK 900 RELATED ID: 1OFL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CHONDROITINASE B COMPLEXED TO DERMATAN SULFATE  
REMARK 900 HEXASACCHARIDE                                                       
DBREF  1OFM A   26    26  PDB    1OFM     1OFM            26     26             
DBREF  1OFM A   27   506  UNP    Q46079   CSLB_PEDHD      27    506             
SEQRES   1 A  481  PCA VAL VAL ALA SER ASN GLU THR LEU TYR GLN VAL VAL          
SEQRES   2 A  481  LYS GLU VAL LYS PRO GLY GLY LEU VAL GLN ILE ALA ASP          
SEQRES   3 A  481  GLY THR TYR LYS ASP VAL GLN LEU ILE VAL SER ASN SER          
SEQRES   4 A  481  GLY LYS SER GLY LEU PRO ILE THR ILE LYS ALA LEU ASN          
SEQRES   5 A  481  PRO GLY LYS VAL PHE PHE THR GLY ASP ALA LYS VAL GLU          
SEQRES   6 A  481  LEU ARG GLY GLU HIS LEU ILE LEU GLU GLY ILE TRP PHE          
SEQRES   7 A  481  LYS ASP GLY ASN ARG ALA ILE GLN ALA TRP LYS SER HIS          
SEQRES   8 A  481  GLY PRO GLY LEU VAL ALA ILE TYR GLY SER TYR ASN ARG          
SEQRES   9 A  481  ILE THR ALA CYS VAL PHE ASP CYS PHE ASP GLU ALA ASN          
SEQRES  10 A  481  SER ALA TYR ILE THR THR SER LEU THR GLU ASP GLY LYS          
SEQRES  11 A  481  VAL PRO GLN HIS CYS ARG ILE ASP HIS CYS SER PHE THR          
SEQRES  12 A  481  ASP LYS ILE THR PHE ASP GLN VAL ILE ASN LEU ASN ASN          
SEQRES  13 A  481  THR ALA ARG ALA ILE LYS ASP GLY SER VAL GLY GLY PRO          
SEQRES  14 A  481  ALA MET TYR HIS ARG VAL ASP HIS CYS PHE PHE SER ASN          
SEQRES  15 A  481  PRO GLN LYS PRO GLY ASN ALA GLY GLY GLY ILE ARG ILE          
SEQRES  16 A  481  GLY TYR TYR ARG ASN ASP ILE GLY ARG CYS LEU VAL ASP          
SEQRES  17 A  481  SER ASN LEU PHE MET ARG GLN ASP SER GLU ALA GLU ILE          
SEQRES  18 A  481  ILE THR SER LYS SER GLN GLU ASN VAL TYR TYR GLY ASN          
SEQRES  19 A  481  THR TYR LEU ASN CYS GLN GLY THR MET ASN PHE ARG HIS          
SEQRES  20 A  481  GLY ASP HIS GLN VAL ALA ILE ASN ASN PHE TYR ILE GLY          
SEQRES  21 A  481  ASN ASP GLN ARG PHE GLY TYR GLY GLY MET PHE VAL TRP          
SEQRES  22 A  481  GLY SER ARG HIS VAL ILE ALA CYS ASN TYR PHE GLU LEU          
SEQRES  23 A  481  SER GLU THR ILE LYS SER ARG GLY ASN ALA ALA LEU TYR          
SEQRES  24 A  481  LEU ASN PRO GLY ALA MET ALA SER GLU HIS ALA LEU ALA          
SEQRES  25 A  481  PHE ASP MET LEU ILE ALA ASN ASN ALA PHE ILE ASN VAL          
SEQRES  26 A  481  ASN GLY TYR ALA ILE HIS PHE ASN PRO LEU ASP GLU ARG          
SEQRES  27 A  481  ARG LYS GLU TYR CYS ALA ALA ASN ARG LEU LYS PHE GLU          
SEQRES  28 A  481  THR PRO HIS GLN LEU MET LEU LYS GLY ASN LEU PHE PHE          
SEQRES  29 A  481  LYS ASP LYS PRO TYR VAL TYR PRO PHE PHE LYS ASP ASP          
SEQRES  30 A  481  TYR PHE ILE ALA GLY LYS ASN SER TRP THR GLY ASN VAL          
SEQRES  31 A  481  ALA LEU GLY VAL GLU LYS GLY ILE PRO VAL ASN ILE SER          
SEQRES  32 A  481  ALA ASN ARG SER ALA TYR LYS PRO VAL LYS ILE LYS ASP          
SEQRES  33 A  481  ILE GLN PRO ILE GLU GLY ILE ALA LEU ASP LEU ASN ALA          
SEQRES  34 A  481  LEU ILE SER LYS GLY ILE THR GLY LYS PRO LEU SER TRP          
SEQRES  35 A  481  ASP GLU VAL ARG PRO TYR TRP LEU LYS GLU MET PRO GLY          
SEQRES  36 A  481  THR TYR ALA LEU THR ALA ARG LEU SER ALA ASP ARG ALA          
SEQRES  37 A  481  ALA LYS PHE LYS ALA VAL ILE LYS ARG ASN LYS GLU HIS          
MODRES 1OFM SER A  234  SER  GLYCOSYLATION SITE                                 
MODRES 1OFM PCA A   26  GLU  PYROGLUTAMIC ACID                                  
HET    PCA  A  26       8                                                       
HET    MAN  B   1      11                                                       
HET    GCU  B   2      12                                                       
HET    XYP  B   3       9                                                       
HET    MXZ  B   4      11                                                       
HET    GLA  B   5      11                                                       
HET    BGC  B   6      11                                                       
HET    RAM  B   7      10                                                       
HET    ASG  C   1      19                                                       
HET    BDP  C   2      12                                                       
HET    ASG  C   3      18                                                       
HET    GCD  C   4      11                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     GCU ALPHA-D-GLUCOPYRANURONIC ACID                                    
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM     MXZ 2-O-METHYL-ALPHA-L-FUCOPYRANOSE                                  
HETNAM     GLA ALPHA-D-GALACTOPYRANOSE                                          
HETNAM     BGC BETA-D-GLUCOPYRANOSE                                             
HETNAM     RAM ALPHA-L-RHAMNOPYRANOSE                                           
HETNAM     ASG 2-ACETAMIDO-2-DEOXY-4-O-SULFO-BETA-D-GALACTOPYRANOSE             
HETNAM     BDP BETA-D-GLUCOPYRANURONIC ACID                                     
HETNAM     GCD 4-DEOXY-ALPHA-L-THREO-HEX-4-ENOPYRANURONIC ACID                  
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
HETSYN     GCU ALPHA-D-GLUCURONIC ACID; D-GLUCURONIC ACID; GLUCURONIC           
HETSYN   2 GCU  ACID                                                            
HETSYN     XYP BETA-D-XYLOSE; D-XYLOSE; XYLOSE                                  
HETSYN     MXZ 6-DEOXY-2-O-METHYL-ALPHA-L-GALACTOPYRANOSE; 2-O-METHYL-          
HETSYN   2 MXZ  ALPHA-L-FUCOSE; 2-O-METHYL-L-FUCOSE; 2-O-METHYL-FUCOSE          
HETSYN     GLA ALPHA-D-GALACTOSE; D-GALACTOSE; GALACTOSE; ALPHA D-              
HETSYN   2 GLA  GALACTOSE                                                       
HETSYN     BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE                               
HETSYN     RAM ALPHA-L-RHAMNOSE; 6-DEOXY-ALPHA-L-MANNOPYRANOSE; L-              
HETSYN   2 RAM  RHAMNOSE; RHAMNOSE                                              
HETSYN     ASG 2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE; N-               
HETSYN   2 ASG  ACETYL-4-O-SULFO-BETA-D-GALACTOSAMINE; 2-ACETAMIDO-2-           
HETSYN   3 ASG  DEOXY-4-O-SULFO-BETA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-          
HETSYN   4 ASG  4-O-SULFO-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-4-O-SULFO-           
HETSYN   5 ASG  GALACTOSE                                                       
HETSYN     BDP BETA-D-GLUCURONIC ACID; D-GLUCURONIC ACID; GLUCURONIC            
HETSYN   2 BDP  ACID                                                            
HETSYN     GCD 4,5-DEHYDRO-D-GLUCURONIC ACID; 4-DEOXY-ALPHA-L-THREO-            
HETSYN   2 GCD  HEX-4-ENURONIC ACID; 4-DEOXY-L-THREO-HEX-4-ENURONIC             
HETSYN   3 GCD  ACID; 4-DEOXY-THREO-HEX-4-ENURONIC ACID                         
FORMUL   1  PCA    C5 H7 N O3                                                   
FORMUL   2  MAN    C6 H12 O6                                                    
FORMUL   2  GCU    C6 H10 O7                                                    
FORMUL   2  XYP    C5 H10 O5                                                    
FORMUL   2  MXZ    C7 H14 O5                                                    
FORMUL   2  GLA    C6 H12 O6                                                    
FORMUL   2  BGC    C6 H12 O6                                                    
FORMUL   2  RAM    C6 H12 O5                                                    
FORMUL   3  ASG    2(C8 H15 N O9 S)                                             
FORMUL   3  BDP    C6 H10 O7                                                    
FORMUL   3  GCD    C6 H8 O6                                                     
FORMUL   4  HOH   *806(H2 O)                                                    
HELIX    1 AA1 SER A   30  VAL A   41  1                                  12    
HELIX    2 AA2 LEU A  360  ARG A  372  1                                  13    
HELIX    3 AA3 ASN A  430  TYR A  434  5                                   5    
HELIX    4 AA4 ASP A  451  GLY A  459  1                                   9    
HELIX    5 AA5 SER A  466  ARG A  471  1                                   6    
HELIX    6 AA6 SER A  489  ASN A  503  1                                  15    
SHEET    1 AA114 VAL A  27  VAL A  28  0                                        
SHEET    2 AA114 LEU A  46  ILE A  49  1  O  GLN A  48   N  VAL A  28           
SHEET    3 AA114 ILE A  71  ALA A  75  1  O  THR A  72   N  VAL A  47           
SHEET    4 AA114 LEU A  96  GLU A  99  1  O  ILE A  97   N  ILE A  73           
SHEET    5 AA114 ARG A 129  THR A 131  1  O  THR A 131   N  LEU A  98           
SHEET    6 AA114 ARG A 161  ASP A 163  1  O  ASP A 163   N  ILE A 130           
SHEET    7 AA114 ARG A 199  ASP A 201  1  O  ARG A 199   N  ILE A 162           
SHEET    8 AA114 LEU A 231  ASP A 233  1  O  LEU A 231   N  VAL A 200           
SHEET    9 AA114 VAL A 255  TYR A 257  1  O  VAL A 255   N  VAL A 232           
SHEET   10 AA114 VAL A 277  ILE A 279  1  O  VAL A 277   N  TYR A 256           
SHEET   11 AA114 VAL A 303  ALA A 305  1  O  VAL A 303   N  ALA A 278           
SHEET   12 AA114 LEU A 341  ALA A 343  1  O  LEU A 341   N  ILE A 304           
SHEET   13 AA114 MET A 382  LYS A 384  1  O  MET A 382   N  ILE A 342           
SHEET   14 AA114 SER A 410  THR A 412  1  O  SER A 410   N  LEU A 383           
SHEET    1 AA213 GLY A  52  LYS A  55  0                                        
SHEET    2 AA213 VAL A  81  GLY A  85  1  O  PHE A  82   N  TYR A  54           
SHEET    3 AA213 TRP A 102  GLY A 106  1  O  ASP A 105   N  GLY A  85           
SHEET    4 AA213 VAL A 134  ASP A 136  1  O  VAL A 134   N  PHE A 103           
SHEET    5 AA213 SER A 166  THR A 168  1  O  SER A 166   N  PHE A 135           
SHEET    6 AA213 PHE A 204  ASN A 207  1  O  PHE A 204   N  PHE A 167           
SHEET    7 AA213 LEU A 236  GLN A 240  1  O  MET A 238   N  PHE A 205           
SHEET    8 AA213 THR A 260  LEU A 262  1  O  LEU A 262   N  PHE A 237           
SHEET    9 AA213 PHE A 282  GLY A 285  1  O  PHE A 282   N  TYR A 261           
SHEET   10 AA213 TYR A 308  LEU A 311  1  O  TYR A 308   N  TYR A 283           
SHEET   11 AA213 ALA A 346  ILE A 348  1  O  ALA A 346   N  PHE A 309           
SHEET   12 AA213 LEU A 387  PHE A 389  1  O  PHE A 389   N  PHE A 347           
SHEET   13 AA213 VAL A 415  LEU A 417  1  O  VAL A 415   N  PHE A 388           
SHEET    1 AA312 GLN A  58  VAL A  61  0                                        
SHEET    2 AA312 LYS A  88  LEU A  91  1  O  GLU A  90   N  LEU A  59           
SHEET    3 AA312 VAL A 121  ILE A 123  1  O  ALA A 122   N  VAL A  89           
SHEET    4 AA312 ILE A 146  THR A 148  1  O  THR A 147   N  ILE A 123           
SHEET    5 AA312 ILE A 177  LEU A 179  1  O  ASN A 178   N  ILE A 146           
SHEET    6 AA312 ILE A 218  ILE A 220  1  O  ARG A 219   N  LEU A 179           
SHEET    7 AA312 GLU A 245  LYS A 250  1  O  THR A 248   N  ILE A 218           
SHEET    8 AA312 THR A 267  HIS A 272  1  O  THR A 267   N  ILE A 246           
SHEET    9 AA312 MET A 295  VAL A 297  1  O  PHE A 296   N  PHE A 270           
SHEET   10 AA312 ALA A 321  LEU A 325  1  O  TYR A 324   N  MET A 295           
SHEET   11 AA312 TYR A 353  HIS A 356  1  O  HIS A 356   N  LEU A 325           
SHEET   12 AA312 PHE A 399  LYS A 400  1  O  LYS A 400   N  ILE A 355           
LINK         C   PCA A  26                 N   VAL A  27     1555   1555  1.33  
LINK         OG  SER A 234                 C1  MAN B   1     1555   1555  1.40  
LINK         O2  MAN B   1                 C1  GCU B   2     1555   1555  1.40  
LINK         O4  MAN B   1                 C1  RAM B   7     1555   1555  1.40  
LINK         O4  GCU B   2                 C1  XYP B   3     1555   1555  1.38  
LINK         O4  XYP B   3                 C1  MXZ B   4     1555   1555  1.40  
LINK         O3  MXZ B   4                 C1  GLA B   5     1555   1555  1.40  
LINK         O4  MXZ B   4                 C1  BGC B   6     1555   1555  1.38  
LINK         O3  ASG C   1                 C1  BDP C   2     1555   1555  1.38  
LINK         O4  BDP C   2                 C1  ASG C   3     1555   1555  1.38  
LINK         O3  ASG C   3                 C1  GCD C   4     1555   1555  1.38  
CISPEP   1 GLY A  293    GLY A  294          0         1.26                     
CRYST1   50.537   74.069   58.989  90.00  93.76  90.00 P 1 21 1      2          
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      0.019787  0.000000  0.001300        0.00000                         
SCALE2      0.000000  0.013501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016989        0.00000                         
HETATM    1  N   PCA A  26      52.549  -8.515  25.868  1.00  9.15           N  
HETATM    2  CA  PCA A  26      53.934  -8.865  25.541  1.00  8.04           C  
HETATM    3  CB  PCA A  26      53.915 -10.274  24.963  1.00 10.74           C  
HETATM    4  CG  PCA A  26      52.695 -10.874  25.671  1.00 11.24           C  
HETATM    5  CD  PCA A  26      51.684  -9.698  25.719  1.00 12.95           C  
HETATM    6  OE  PCA A  26      50.550  -9.584  26.164  1.00 14.01           O  
HETATM    7  C   PCA A  26      54.489  -7.912  24.505  1.00  6.90           C  
HETATM    8  O   PCA A  26      53.742  -7.150  23.880  1.00  7.57           O  
ATOM      9  N   VAL A  27      55.801  -7.969  24.330  1.00  6.11           N  
ATOM     10  CA  VAL A  27      56.476  -7.154  23.321  1.00  6.18           C  
ATOM     11  C   VAL A  27      56.463  -7.956  22.022  1.00  6.63           C  
ATOM     12  O   VAL A  27      56.788  -9.151  22.014  1.00  6.77           O  
ATOM     13  CB  VAL A  27      57.944  -6.858  23.695  1.00  6.05           C  
ATOM     14  CG1 VAL A  27      58.612  -6.003  22.599  1.00  5.93           C  
ATOM     15  CG2 VAL A  27      57.998  -6.115  25.025  1.00  5.36           C  
ATOM     16  N   VAL A  28      56.072  -7.303  20.929  1.00  6.67           N  
ATOM     17  CA  VAL A  28      56.040  -7.952  19.612  1.00  6.01           C  
ATOM     18  C   VAL A  28      56.866  -7.094  18.656  1.00  5.75           C  
ATOM     19  O   VAL A  28      56.871  -5.864  18.763  1.00  6.31           O  
ATOM     20  CB  VAL A  28      54.599  -8.096  19.090  1.00  6.49           C  
ATOM     21  CG1 VAL A  28      53.846  -9.079  19.975  1.00  7.76           C  
ATOM     22  CG2 VAL A  28      53.887  -6.734  19.092  1.00  6.94           C  
ATOM     23  N   ALA A  29      57.558  -7.742  17.725  1.00  5.38           N  
ATOM     24  CA  ALA A  29      58.434  -7.036  16.807  1.00  6.60           C  
ATOM     25  C   ALA A  29      58.157  -7.261  15.327  1.00  8.58           C  
ATOM     26  O   ALA A  29      58.970  -6.893  14.490  1.00 10.19           O  
ATOM     27  CB  ALA A  29      59.877  -7.397  17.121  1.00  7.10           C  
ATOM     28  N   SER A  30      57.023  -7.863  14.997  1.00  7.96           N  
ATOM     29  CA  SER A  30      56.696  -8.082  13.577  1.00  8.78           C  
ATOM     30  C   SER A  30      55.181  -8.080  13.409  1.00  7.69           C  
ATOM     31  O   SER A  30      54.454  -8.207  14.382  1.00  6.66           O  
ATOM     32  CB  SER A  30      57.257  -9.426  13.110  1.00  7.78           C  
ATOM     33  OG  SER A  30      56.542 -10.508  13.684  1.00  8.55           O  
ATOM     34  N   ASN A  31      54.695  -7.944  12.175  1.00  7.40           N  
ATOM     35  CA  ASN A  31      53.251  -7.970  11.957  1.00  7.64           C  
ATOM     36  C   ASN A  31      52.654  -9.283  12.469  1.00  7.72           C  
ATOM     37  O   ASN A  31      51.650  -9.289  13.183  1.00  6.86           O  
ATOM     38  CB  ASN A  31      52.909  -7.829  10.460  1.00  7.18           C  
ATOM     39  CG  ASN A  31      53.192  -6.443   9.914  1.00  9.58           C  
ATOM     40  OD1 ASN A  31      53.493  -5.526  10.662  1.00  8.24           O  
ATOM     41  ND2 ASN A  31      53.080  -6.284   8.598  1.00  9.83           N  
ATOM     42  N   GLU A  32      53.274 -10.400  12.092  1.00  8.49           N  
ATOM     43  CA  GLU A  32      52.775 -11.707  12.500  1.00 11.72           C  
ATOM     44  C   GLU A  32      52.647 -11.909  14.006  1.00 10.39           C  
ATOM     45  O   GLU A  32      51.618 -12.403  14.488  1.00  9.44           O  
ATOM     46  CB  GLU A  32      53.658 -12.801  11.903  1.00 15.47           C  
ATOM     47  CG  GLU A  32      53.306 -13.112  10.468  1.00 22.45           C  
ATOM     48  CD  GLU A  32      51.871 -13.587  10.346  1.00 26.68           C  
ATOM     49  OE1 GLU A  32      51.504 -14.558  11.049  1.00 31.10           O  
ATOM     50  OE2 GLU A  32      51.108 -12.989   9.559  1.00 30.18           O  
ATOM     51  N   THR A  33      53.682 -11.539  14.751  1.00  9.18           N  
ATOM     52  CA  THR A  33      53.624 -11.707  16.194  1.00  9.41           C  
ATOM     53  C   THR A  33      52.610 -10.761  16.830  1.00  8.38           C  
ATOM     54  O   THR A  33      51.970 -11.113  17.816  1.00  9.19           O  
ATOM     55  CB  THR A  33      55.024 -11.575  16.874  1.00  9.59           C  
ATOM     56  OG1 THR A  33      55.650 -10.346  16.506  1.00 10.65           O  
ATOM     57  CG2 THR A  33      55.923 -12.737  16.442  1.00 10.41           C  
ATOM     58  N   LEU A  34      52.448  -9.572  16.251  1.00  7.26           N  
ATOM     59  CA  LEU A  34      51.450  -8.626  16.737  1.00  5.52           C  
ATOM     60  C   LEU A  34      50.050  -9.228  16.546  1.00  6.54           C  
ATOM     61  O   LEU A  34      49.222  -9.169  17.459  1.00  7.07           O  
ATOM     62  CB  LEU A  34      51.553  -7.286  15.968  1.00  3.81           C  
ATOM     63  CG  LEU A  34      50.411  -6.266  16.188  1.00  5.44           C  
ATOM     64  CD1 LEU A  34      50.436  -5.721  17.622  1.00  7.37           C  
ATOM     65  CD2 LEU A  34      50.580  -5.106  15.200  1.00  6.86           C  
ATOM     66  N   TYR A  35      49.783  -9.813  15.371  1.00  6.93           N  
ATOM     67  CA  TYR A  35      48.481 -10.420  15.077  1.00  8.02           C  
ATOM     68  C   TYR A  35      48.142 -11.502  16.102  1.00  8.23           C  
ATOM     69  O   TYR A  35      47.016 -11.584  16.594  1.00  9.05           O  
ATOM     70  CB  TYR A  35      48.481 -11.058  13.671  1.00  8.37           C  
ATOM     71  CG  TYR A  35      48.711 -10.086  12.530  1.00  7.59           C  
ATOM     72  CD1 TYR A  35      48.528  -8.705  12.701  1.00  8.70           C  
ATOM     73  CD2 TYR A  35      49.130 -10.546  11.284  1.00  8.04           C  
ATOM     74  CE1 TYR A  35      48.768  -7.808  11.628  1.00 10.29           C  
ATOM     75  CE2 TYR A  35      49.379  -9.677  10.224  1.00  8.90           C  
ATOM     76  CZ  TYR A  35      49.196  -8.307  10.400  1.00  9.20           C  
ATOM     77  OH  TYR A  35      49.466  -7.458   9.345  1.00  8.60           O  
ATOM     78  N   GLN A  36      49.134 -12.325  16.414  1.00 10.32           N  
ATOM     79  CA  GLN A  36      48.952 -13.423  17.361  1.00 11.84           C  
ATOM     80  C   GLN A  36      48.700 -12.963  18.798  1.00 11.44           C  
ATOM     81  O   GLN A  36      47.758 -13.429  19.441  1.00 12.14           O  
ATOM     82  CB  GLN A  36      50.167 -14.363  17.318  1.00 12.91           C  
ATOM     83  CG  GLN A  36      50.039 -15.608  18.222  1.00 17.66           C  
ATOM     84  CD  GLN A  36      48.902 -16.534  17.811  1.00 20.52           C  
ATOM     85  OE1 GLN A  36      48.752 -16.873  16.631  1.00 23.80           O  
ATOM     86  NE2 GLN A  36      48.103 -16.961  18.786  1.00 23.06           N  
ATOM     87  N   VAL A  37      49.510 -12.036  19.292  1.00  9.27           N  
ATOM     88  CA  VAL A  37      49.340 -11.578  20.665  1.00 10.01           C  
ATOM     89  C   VAL A  37      47.999 -10.875  20.858  1.00  9.91           C  
ATOM     90  O   VAL A  37      47.339 -11.012  21.911  1.00  8.89           O  
ATOM     91  CB  VAL A  37      50.488 -10.658  21.101  1.00  9.78           C  
ATOM     92  CG1 VAL A  37      50.285 -10.238  22.553  1.00 11.07           C  
ATOM     93  CG2 VAL A  37      51.809 -11.393  20.976  1.00 13.23           C  
ATOM     94  N   VAL A  38      47.578 -10.138  19.838  1.00 11.66           N  
ATOM     95  CA  VAL A  38      46.303  -9.433  19.911  1.00 12.74           C  
ATOM     96  C   VAL A  38      45.115 -10.401  19.984  1.00 14.05           C  
ATOM     97  O   VAL A  38      44.066 -10.058  20.512  1.00 15.08           O  
ATOM     98  CB  VAL A  38      46.169  -8.448  18.711  1.00 14.94           C  
ATOM     99  CG1 VAL A  38      44.730  -8.096  18.454  1.00 16.79           C  
ATOM    100  CG2 VAL A  38      46.968  -7.174  19.018  1.00 12.57           C  
ATOM    101  N   LYS A  39      45.274 -11.621  19.482  1.00 15.71           N  
ATOM    102  CA  LYS A  39      44.183 -12.598  19.545  1.00 17.26           C  
ATOM    103  C   LYS A  39      44.126 -13.271  20.923  1.00 17.49           C  
ATOM    104  O   LYS A  39      43.103 -13.854  21.306  1.00 17.73           O  
ATOM    105  CB  LYS A  39      44.383 -13.670  18.475  1.00 19.88           C  
ATOM    106  CG  LYS A  39      44.329 -13.132  17.067  1.00 24.59           C  
ATOM    107  CD  LYS A  39      44.907 -14.118  16.061  1.00 29.90           C  
ATOM    108  CE  LYS A  39      44.133 -15.426  16.022  1.00 32.05           C  
ATOM    109  NZ  LYS A  39      44.661 -16.315  14.949  1.00 36.73           N  
ATOM    110  N   GLU A  40      45.227 -13.183  21.662  1.00 16.98           N  
ATOM    111  CA  GLU A  40      45.337 -13.813  22.976  1.00 17.95           C  
ATOM    112  C   GLU A  40      45.212 -12.867  24.163  1.00 17.08           C  
ATOM    113  O   GLU A  40      44.898 -13.300  25.273  1.00 16.22           O  
ATOM    114  CB  GLU A  40      46.692 -14.538  23.097  1.00 19.81           C  
ATOM    115  CG  GLU A  40      47.098 -15.333  21.866  1.00 22.26           C  
ATOM    116  CD  GLU A  40      48.544 -15.829  21.924  1.00 25.35           C  
ATOM    117  OE1 GLU A  40      49.411 -15.108  22.484  1.00 25.60           O  
ATOM    118  OE2 GLU A  40      48.815 -16.930  21.388  1.00 26.03           O  
ATOM    119  N   VAL A  41      45.441 -11.577  23.940  1.00 16.17           N  
ATOM    120  CA  VAL A  41      45.420 -10.631  25.043  1.00 15.36           C  
ATOM    121  C   VAL A  41      44.107 -10.602  25.828  1.00 15.02           C  
ATOM    122  O   VAL A  41      43.019 -10.698  25.264  1.00 14.14           O  
ATOM    123  CB  VAL A  41      45.810  -9.211  24.554  1.00 14.93           C  
ATOM    124  CG1 VAL A  41      44.767  -8.666  23.595  1.00 14.06           C  
ATOM    125  CG2 VAL A  41      46.036  -8.316  25.734  1.00 13.47           C  
ATOM    126  N   LYS A  42      44.238 -10.493  27.144  1.00 15.70           N  
ATOM    127  CA  LYS A  42      43.091 -10.483  28.040  1.00 16.55           C  
ATOM    128  C   LYS A  42      42.886  -9.115  28.652  1.00 15.10           C  
ATOM    129  O   LYS A  42      43.758  -8.255  28.569  1.00 13.30           O  
ATOM    130  CB  LYS A  42      43.319 -11.489  29.167  1.00 19.60           C  
ATOM    131  CG  LYS A  42      43.505 -12.925  28.696  1.00 24.36           C  
ATOM    132  CD  LYS A  42      43.829 -13.844  29.868  1.00 28.85           C  
ATOM    133  CE  LYS A  42      45.058 -13.358  30.621  1.00 31.14           C  
ATOM    134  NZ  LYS A  42      45.463 -14.300  31.689  1.00 34.81           N  
ATOM    135  N   PRO A  43      41.725  -8.891  29.290  1.00 14.22           N  
ATOM    136  CA  PRO A  43      41.466  -7.591  29.912  1.00 13.76           C  
ATOM    137  C   PRO A  43      42.631  -7.154  30.794  1.00 14.65           C  
ATOM    138  O   PRO A  43      43.190  -7.965  31.543  1.00 14.67           O  
ATOM    139  CB  PRO A  43      40.197  -7.854  30.712  1.00 13.17           C  
ATOM    140  CG  PRO A  43      39.461  -8.767  29.824  1.00 11.50           C  
ATOM    141  CD  PRO A  43      40.534  -9.755  29.389  1.00 14.33           C  
ATOM    142  N   GLY A  44      42.999  -5.879  30.693  1.00 13.62           N  
ATOM    143  CA  GLY A  44      44.093  -5.337  31.478  1.00 12.78           C  
ATOM    144  C   GLY A  44      45.448  -5.604  30.853  1.00 12.75           C  
ATOM    145  O   GLY A  44      46.470  -5.168  31.381  1.00 13.95           O  
ATOM    146  N   GLY A  45      45.446  -6.312  29.727  1.00 11.15           N  
ATOM    147  CA  GLY A  45      46.684  -6.650  29.044  1.00 11.10           C  
ATOM    148  C   GLY A  45      47.401  -5.461  28.437  1.00  9.51           C  
ATOM    149  O   GLY A  45      46.808  -4.413  28.206  1.00  8.90           O  
ATOM    150  N   LEU A  46      48.695  -5.633  28.179  1.00  8.93           N  
ATOM    151  CA  LEU A  46      49.521  -4.577  27.602  1.00  7.15           C  
ATOM    152  C   LEU A  46      50.368  -5.190  26.484  1.00  7.04           C  
ATOM    153  O   LEU A  46      51.200  -6.059  26.748  1.00  6.85           O  
ATOM    154  CB  LEU A  46      50.434  -3.961  28.697  1.00  7.77           C  
ATOM    155  CG  LEU A  46      51.589  -3.036  28.292  1.00  7.72           C  
ATOM    156  CD1 LEU A  46      51.052  -1.927  27.381  1.00  6.86           C  
ATOM    157  CD2 LEU A  46      52.251  -2.420  29.545  1.00 11.30           C  
ATOM    158  N   VAL A  47      50.106  -4.761  25.242  1.00  5.11           N  
ATOM    159  CA  VAL A  47      50.852  -5.207  24.066  1.00  4.94           C  
ATOM    160  C   VAL A  47      51.750  -4.026  23.685  1.00  5.10           C  
ATOM    161  O   VAL A  47      51.265  -2.903  23.451  1.00  6.54           O  
ATOM    162  CB  VAL A  47      49.917  -5.518  22.867  1.00  4.53           C  
ATOM    163  CG1 VAL A  47      50.739  -5.905  21.648  1.00  6.82           C  
ATOM    164  CG2 VAL A  47      48.961  -6.649  23.227  1.00  7.54           C  
ATOM    165  N   GLN A  48      53.051  -4.269  23.666  1.00  4.12           N  
ATOM    166  CA  GLN A  48      54.028  -3.237  23.328  1.00  4.81           C  
ATOM    167  C   GLN A  48      54.730  -3.594  22.034  1.00  5.61           C  
ATOM    168  O   GLN A  48      55.286  -4.674  21.901  1.00  4.66           O  
ATOM    169  CB  GLN A  48      55.025  -3.095  24.472  1.00  4.24           C  
ATOM    170  CG  GLN A  48      54.401  -2.360  25.666  1.00  5.97           C  
ATOM    171  CD  GLN A  48      55.260  -2.448  26.902  1.00  7.47           C  
ATOM    172  OE1 GLN A  48      55.688  -3.537  27.281  1.00  7.48           O  
ATOM    173  NE2 GLN A  48      55.514  -1.314  27.541  1.00  7.51           N  
ATOM    174  N   ILE A  49      54.713  -2.659  21.090  1.00  5.45           N  
ATOM    175  CA  ILE A  49      55.305  -2.883  19.783  1.00  4.82           C  
ATOM    176  C   ILE A  49      56.745  -2.383  19.741  1.00  4.62           C  
ATOM    177  O   ILE A  49      56.997  -1.217  19.997  1.00  5.82           O  
ATOM    178  CB  ILE A  49      54.455  -2.166  18.716  1.00  5.66           C  
ATOM    179  CG1 ILE A  49      53.014  -2.701  18.791  1.00  6.06           C  
ATOM    180  CG2 ILE A  49      55.072  -2.374  17.323  1.00  4.79           C  
ATOM    181  CD1 ILE A  49      52.016  -2.025  17.799  1.00  7.11           C  
ATOM    182  N   ALA A  50      57.684  -3.275  19.436  1.00  4.54           N  
ATOM    183  CA  ALA A  50      59.096  -2.915  19.398  1.00  4.92           C  
ATOM    184  C   ALA A  50      59.393  -1.880  18.331  1.00  5.59           C  
ATOM    185  O   ALA A  50      58.658  -1.767  17.346  1.00  5.83           O  
ATOM    186  CB  ALA A  50      59.942  -4.152  19.143  1.00  4.66           C  
ATOM    187  N   ASP A  51      60.473  -1.134  18.525  1.00  5.09           N  
ATOM    188  CA  ASP A  51      60.870  -0.124  17.539  1.00  6.53           C  
ATOM    189  C   ASP A  51      60.917  -0.736  16.140  1.00  6.31           C  
ATOM    190  O   ASP A  51      61.444  -1.843  15.938  1.00  6.60           O  
ATOM    191  CB  ASP A  51      62.272   0.418  17.840  1.00  7.30           C  
ATOM    192  CG  ASP A  51      62.381   1.136  19.177  1.00  9.14           C  
ATOM    193  OD1 ASP A  51      61.392   1.266  19.934  1.00  7.55           O  
ATOM    194  OD2 ASP A  51      63.516   1.586  19.467  1.00 10.84           O  
ATOM    195  N   GLY A  52      60.380  -0.026  15.163  1.00  6.48           N  
ATOM    196  CA  GLY A  52      60.443  -0.551  13.812  1.00  6.21           C  
ATOM    197  C   GLY A  52      59.325  -0.094  12.918  1.00  6.47           C  
ATOM    198  O   GLY A  52      58.471   0.685  13.333  1.00  6.03           O  
ATOM    199  N   THR A  53      59.346  -0.592  11.683  1.00  6.58           N  
ATOM    200  CA  THR A  53      58.339  -0.254  10.693  1.00  5.73           C  
ATOM    201  C   THR A  53      57.462  -1.477  10.486  1.00  6.55           C  
ATOM    202  O   THR A  53      57.965  -2.606  10.324  1.00  6.06           O  
ATOM    203  CB  THR A  53      59.015   0.190   9.366  1.00  6.10           C  
ATOM    204  OG1 THR A  53      59.694   1.432   9.593  1.00  6.54           O  
ATOM    205  CG2 THR A  53      57.975   0.343   8.229  1.00  6.24           C  
ATOM    206  N   TYR A  54      56.146  -1.257  10.556  1.00  3.28           N  
ATOM    207  CA  TYR A  54      55.173  -2.327  10.376  1.00  4.99           C  
ATOM    208  C   TYR A  54      54.399  -2.041   9.092  1.00  6.02           C  
ATOM    209  O   TYR A  54      53.337  -1.415   9.098  1.00  6.02           O  
ATOM    210  CB  TYR A  54      54.289  -2.411  11.613  1.00  5.26           C  
ATOM    211  CG  TYR A  54      55.142  -2.774  12.828  1.00  4.22           C  
ATOM    212  CD1 TYR A  54      55.938  -1.812  13.455  1.00  4.35           C  
ATOM    213  CD2 TYR A  54      55.251  -4.096  13.244  1.00  6.24           C  
ATOM    214  CE1 TYR A  54      56.843  -2.163  14.474  1.00  6.84           C  
ATOM    215  CE2 TYR A  54      56.142  -4.462  14.255  1.00  4.86           C  
ATOM    216  CZ  TYR A  54      56.929  -3.489  14.861  1.00  6.22           C  
ATOM    217  OH  TYR A  54      57.796  -3.850  15.870  1.00  7.42           O  
ATOM    218  N   LYS A  55      54.975  -2.533   7.995  1.00  5.11           N  
ATOM    219  CA  LYS A  55      54.470  -2.320   6.647  1.00  5.42           C  
ATOM    220  C   LYS A  55      53.333  -3.242   6.231  1.00  5.19           C  
ATOM    221  O   LYS A  55      53.405  -4.463   6.408  1.00  5.06           O  
ATOM    222  CB  LYS A  55      55.648  -2.419   5.660  1.00  4.68           C  
ATOM    223  CG  LYS A  55      55.274  -2.116   4.228  1.00  6.83           C  
ATOM    224  CD  LYS A  55      56.512  -2.062   3.348  1.00  8.22           C  
ATOM    225  CE  LYS A  55      56.115  -2.174   1.883  1.00 10.12           C  
ATOM    226  NZ  LYS A  55      55.699  -3.571   1.551  1.00  7.49           N  
ATOM    227  N   ASP A  56      52.277  -2.633   5.692  1.00  6.14           N  
ATOM    228  CA  ASP A  56      51.090  -3.361   5.254  1.00  5.88           C  
ATOM    229  C   ASP A  56      50.429  -4.030   6.447  1.00  5.80           C  
ATOM    230  O   ASP A  56      49.757  -5.043   6.297  1.00  5.69           O  
ATOM    231  CB  ASP A  56      51.465  -4.431   4.211  1.00  5.42           C  
ATOM    232  CG  ASP A  56      52.272  -3.860   3.054  1.00  6.97           C  
ATOM    233  OD1 ASP A  56      52.008  -2.710   2.655  1.00  6.44           O  
ATOM    234  OD2 ASP A  56      53.157  -4.561   2.513  1.00  6.26           O  
ATOM    235  N   VAL A  57      50.602  -3.465   7.632  1.00  5.23           N  
ATOM    236  CA  VAL A  57      50.032  -4.071   8.838  1.00  5.69           C  
ATOM    237  C   VAL A  57      48.494  -4.018   8.850  1.00  6.81           C  
ATOM    238  O   VAL A  57      47.870  -2.985   8.550  1.00  6.95           O  
ATOM    239  CB  VAL A  57      50.652  -3.403  10.098  1.00  5.95           C  
ATOM    240  CG1 VAL A  57      50.263  -1.922  10.174  1.00  4.36           C  
ATOM    241  CG2 VAL A  57      50.235  -4.149  11.350  1.00  5.51           C  
ATOM    242  N   GLN A  58      47.887  -5.154   9.165  1.00  7.07           N  
ATOM    243  CA  GLN A  58      46.435  -5.283   9.218  1.00  7.89           C  
ATOM    244  C   GLN A  58      46.087  -5.634  10.664  1.00  8.31           C  
ATOM    245  O   GLN A  58      45.927  -6.819  11.012  1.00  8.07           O  
ATOM    246  CB  GLN A  58      45.969  -6.417   8.298  1.00  9.13           C  
ATOM    247  CG  GLN A  58      46.343  -6.270   6.837  1.00 10.68           C  
ATOM    248  CD  GLN A  58      45.491  -5.249   6.125  1.00 12.61           C  
ATOM    249  OE1 GLN A  58      44.264  -5.361   6.094  1.00 10.59           O  
ATOM    250  NE2 GLN A  58      46.132  -4.243   5.554  1.00 12.39           N  
ATOM    251  N   LEU A  59      45.977  -4.605  11.501  1.00  6.09           N  
ATOM    252  CA  LEU A  59      45.694  -4.813  12.910  1.00  7.00           C  
ATOM    253  C   LEU A  59      44.198  -4.851  13.203  1.00  7.53           C  
ATOM    254  O   LEU A  59      43.521  -3.827  13.146  1.00  6.43           O  
ATOM    255  CB  LEU A  59      46.371  -3.718  13.734  1.00  5.88           C  
ATOM    256  CG  LEU A  59      46.085  -3.735  15.240  1.00  6.28           C  
ATOM    257  CD1 LEU A  59      46.545  -5.052  15.834  1.00  6.69           C  
ATOM    258  CD2 LEU A  59      46.776  -2.560  15.895  1.00  6.06           C  
ATOM    259  N   ILE A  60      43.692  -6.041  13.517  1.00  7.30           N  
ATOM    260  CA  ILE A  60      42.276  -6.228  13.820  1.00  8.01           C  
ATOM    261  C   ILE A  60      42.176  -6.700  15.268  1.00  8.17           C  
ATOM    262  O   ILE A  60      42.626  -7.801  15.596  1.00  8.13           O  
ATOM    263  CB  ILE A  60      41.645  -7.316  12.929  1.00 10.10           C  
ATOM    264  CG1 ILE A  60      41.982  -7.056  11.457  1.00 11.63           C  
ATOM    265  CG2 ILE A  60      40.141  -7.353  13.159  1.00 10.18           C  
ATOM    266  CD1 ILE A  60      41.414  -5.786  10.885  1.00 11.57           C  
ATOM    267  N   VAL A  61      41.588  -5.882  16.130  1.00  6.99           N  
ATOM    268  CA  VAL A  61      41.469  -6.245  17.542  1.00  7.60           C  
ATOM    269  C   VAL A  61      39.995  -6.503  17.847  1.00  8.73           C  
ATOM    270  O   VAL A  61      39.198  -5.574  17.933  1.00  7.88           O  
ATOM    271  CB  VAL A  61      41.994  -5.125  18.471  1.00  8.03           C  
ATOM    272  CG1 VAL A  61      42.080  -5.649  19.913  1.00  8.76           C  
ATOM    273  CG2 VAL A  61      43.380  -4.660  18.013  1.00  9.45           C  
ATOM    274  N   SER A  62      39.649  -7.776  18.003  1.00 11.32           N  
ATOM    275  CA  SER A  62      38.274  -8.177  18.286  1.00 12.88           C  
ATOM    276  C   SER A  62      38.041  -8.478  19.757  1.00 12.49           C  
ATOM    277  O   SER A  62      36.899  -8.394  20.238  1.00 13.91           O  
ATOM    278  CB  SER A  62      37.918  -9.390  17.432  1.00 15.01           C  
ATOM    279  OG  SER A  62      38.085  -9.055  16.067  1.00 20.96           O  
ATOM    280  N   ASN A  63      39.104  -8.831  20.474  1.00 10.52           N  
ATOM    281  CA  ASN A  63      38.978  -9.105  21.909  1.00 12.88           C  
ATOM    282  C   ASN A  63      38.587  -7.816  22.617  1.00 12.45           C  
ATOM    283  O   ASN A  63      38.741  -6.726  22.062  1.00 11.47           O  
ATOM    284  CB  ASN A  63      40.297  -9.597  22.503  1.00 14.10           C  
ATOM    285  CG  ASN A  63      40.567 -11.055  22.210  1.00 16.82           C  
ATOM    286  OD1 ASN A  63      39.764 -11.736  21.573  1.00 17.92           O  
ATOM    287  ND2 ASN A  63      41.714 -11.546  22.687  1.00 17.46           N  
ATOM    288  N   SER A  64      38.090  -7.949  23.845  1.00 10.95           N  
ATOM    289  CA  SER A  64      37.669  -6.798  24.630  1.00  9.43           C  
ATOM    290  C   SER A  64      38.321  -6.742  25.995  1.00 10.00           C  
ATOM    291  O   SER A  64      38.648  -7.781  26.604  1.00 10.37           O  
ATOM    292  CB  SER A  64      36.147  -6.817  24.878  1.00 10.08           C  
ATOM    293  OG  SER A  64      35.393  -6.401  23.761  1.00 10.43           O  
ATOM    294  N   GLY A  65      38.517  -5.520  26.471  1.00  9.09           N  
ATOM    295  CA  GLY A  65      39.005  -5.333  27.823  1.00 10.24           C  
ATOM    296  C   GLY A  65      37.704  -5.164  28.612  1.00 11.32           C  
ATOM    297  O   GLY A  65      36.623  -5.483  28.102  1.00 12.11           O  
ATOM    298  N   LYS A  66      37.792  -4.656  29.832  1.00 14.47           N  
ATOM    299  CA  LYS A  66      36.614  -4.438  30.666  1.00 16.53           C  
ATOM    300  C   LYS A  66      36.758  -3.092  31.345  1.00 16.62           C  
ATOM    301  O   LYS A  66      37.841  -2.532  31.361  1.00 16.26           O  
ATOM    302  CB  LYS A  66      36.519  -5.525  31.738  1.00 18.32           C  
ATOM    303  CG  LYS A  66      36.167  -6.895  31.213  1.00 22.35           C  
ATOM    304  CD  LYS A  66      35.981  -7.844  32.386  1.00 26.96           C  
ATOM    305  CE  LYS A  66      35.468  -9.193  31.942  1.00 28.30           C  
ATOM    306  NZ  LYS A  66      35.478 -10.138  33.085  1.00 30.18           N  
ATOM    307  N   SER A  67      35.675  -2.568  31.919  1.00 18.78           N  
ATOM    308  CA  SER A  67      35.769  -1.282  32.617  1.00 20.09           C  
ATOM    309  C   SER A  67      36.842  -1.401  33.703  1.00 19.90           C  
ATOM    310  O   SER A  67      36.816  -2.340  34.496  1.00 19.72           O  
ATOM    311  CB  SER A  67      34.426  -0.913  33.259  1.00 23.30           C  
ATOM    312  OG  SER A  67      34.502   0.368  33.880  1.00 27.16           O  
ATOM    313  N   GLY A  68      37.782  -0.460  33.734  1.00 17.78           N  
ATOM    314  CA  GLY A  68      38.853  -0.509  34.719  1.00 17.52           C  
ATOM    315  C   GLY A  68      39.991  -1.452  34.332  1.00 17.29           C  
ATOM    316  O   GLY A  68      41.042  -1.487  34.982  1.00 17.32           O  
ATOM    317  N   LEU A  69      39.779  -2.224  33.275  1.00 15.16           N  
ATOM    318  CA  LEU A  69      40.784  -3.168  32.797  1.00 13.77           C  
ATOM    319  C   LEU A  69      40.860  -3.108  31.285  1.00 12.08           C  
ATOM    320  O   LEU A  69      40.592  -4.090  30.598  1.00 10.81           O  
ATOM    321  CB  LEU A  69      40.433  -4.593  33.200  1.00 15.45           C  
ATOM    322  CG  LEU A  69      40.613  -5.028  34.658  1.00 17.54           C  
ATOM    323  CD1 LEU A  69      40.067  -6.437  34.780  1.00 18.15           C  
ATOM    324  CD2 LEU A  69      42.098  -4.952  35.087  1.00 17.61           C  
ATOM    325  N   PRO A  70      41.247  -1.951  30.741  1.00 10.96           N  
ATOM    326  CA  PRO A  70      41.329  -1.857  29.281  1.00 10.48           C  
ATOM    327  C   PRO A  70      42.486  -2.706  28.744  1.00  9.91           C  
ATOM    328  O   PRO A  70      43.313  -3.207  29.514  1.00 11.03           O  
ATOM    329  CB  PRO A  70      41.559  -0.362  29.054  1.00 10.18           C  
ATOM    330  CG  PRO A  70      42.380   0.022  30.243  1.00 12.71           C  
ATOM    331  CD  PRO A  70      41.653  -0.692  31.380  1.00 12.21           C  
ATOM    332  N   ILE A  71      42.514  -2.897  27.432  1.00  9.21           N  
ATOM    333  CA  ILE A  71      43.607  -3.613  26.781  1.00  8.80           C  
ATOM    334  C   ILE A  71      44.341  -2.478  26.073  1.00  8.25           C  
ATOM    335  O   ILE A  71      43.722  -1.691  25.364  1.00  8.79           O  
ATOM    336  CB  ILE A  71      43.099  -4.622  25.741  1.00  8.50           C  
ATOM    337  CG1 ILE A  71      42.476  -5.825  26.464  1.00  8.85           C  
ATOM    338  CG2 ILE A  71      44.259  -5.021  24.792  1.00  8.64           C  
ATOM    339  CD1 ILE A  71      41.877  -6.877  25.538  1.00  7.50           C  
ATOM    340  N   THR A  72      45.645  -2.371  26.288  1.00  7.19           N  
ATOM    341  CA  THR A  72      46.442  -1.305  25.687  1.00  7.39           C  
ATOM    342  C   THR A  72      47.414  -1.870  24.664  1.00  8.02           C  
ATOM    343  O   THR A  72      48.139  -2.829  24.955  1.00  6.00           O  
ATOM    344  CB  THR A  72      47.270  -0.578  26.765  1.00  9.84           C  
ATOM    345  OG1 THR A  72      46.378  -0.034  27.752  1.00  8.96           O  
ATOM    346  CG2 THR A  72      48.141   0.545  26.140  1.00  8.57           C  
ATOM    347  N   ILE A  73      47.400  -1.289  23.462  1.00  6.17           N  
ATOM    348  CA  ILE A  73      48.304  -1.681  22.383  1.00  4.89           C  
ATOM    349  C   ILE A  73      49.041  -0.379  22.092  1.00  5.65           C  
ATOM    350  O   ILE A  73      48.437   0.614  21.667  1.00  6.13           O  
ATOM    351  CB  ILE A  73      47.515  -2.172  21.130  1.00  6.31           C  
ATOM    352  CG1 ILE A  73      46.701  -3.423  21.501  1.00  8.01           C  
ATOM    353  CG2 ILE A  73      48.478  -2.481  19.996  1.00  5.97           C  
ATOM    354  CD1 ILE A  73      45.566  -3.753  20.546  1.00 11.24           C  
ATOM    355  N   LYS A  74      50.340  -0.369  22.357  1.00  5.02           N  
ATOM    356  CA  LYS A  74      51.115   0.844  22.177  1.00  4.34           C  
ATOM    357  C   LYS A  74      52.520   0.580  21.750  1.00  5.23           C  
ATOM    358  O   LYS A  74      53.023  -0.540  21.854  1.00  5.51           O  
ATOM    359  CB  LYS A  74      51.150   1.622  23.491  1.00  5.54           C  
ATOM    360  CG  LYS A  74      52.001   0.918  24.570  1.00  7.55           C  
ATOM    361  CD  LYS A  74      51.993   1.698  25.902  1.00 10.55           C  
ATOM    362  CE  LYS A  74      52.545   3.109  25.736  1.00 14.60           C  
ATOM    363  NZ  LYS A  74      54.004   3.160  25.397  1.00 17.65           N  
ATOM    364  N   ALA A  75      53.172   1.629  21.267  1.00  5.23           N  
ATOM    365  CA  ALA A  75      54.557   1.502  20.886  1.00  5.48           C  
ATOM    366  C   ALA A  75      55.326   1.413  22.214  1.00  7.53           C  
ATOM    367  O   ALA A  75      54.972   2.090  23.189  1.00  6.50           O  
ATOM    368  CB  ALA A  75      54.997   2.737  20.112  1.00  5.21           C  
ATOM    369  N   LEU A  76      56.335   0.549  22.269  1.00  5.99           N  
ATOM    370  CA  LEU A  76      57.165   0.446  23.467  1.00  6.54           C  
ATOM    371  C   LEU A  76      57.820   1.822  23.632  1.00  6.50           C  
ATOM    372  O   LEU A  76      57.929   2.358  24.742  1.00  7.07           O  
ATOM    373  CB  LEU A  76      58.231  -0.634  23.281  1.00  6.58           C  
ATOM    374  CG  LEU A  76      59.258  -0.762  24.414  1.00  8.06           C  
ATOM    375  CD1 LEU A  76      58.551  -1.152  25.724  1.00  8.97           C  
ATOM    376  CD2 LEU A  76      60.312  -1.812  24.026  1.00  7.64           C  
ATOM    377  N   ASN A  77      58.217   2.408  22.508  1.00  6.23           N  
ATOM    378  CA  ASN A  77      58.838   3.732  22.485  1.00  6.14           C  
ATOM    379  C   ASN A  77      58.149   4.586  21.426  1.00  7.86           C  
ATOM    380  O   ASN A  77      58.546   4.570  20.261  1.00  7.62           O  
ATOM    381  CB  ASN A  77      60.315   3.609  22.148  1.00  7.09           C  
ATOM    382  CG  ASN A  77      61.070   2.802  23.167  1.00  9.42           C  
ATOM    383  OD1 ASN A  77      61.060   3.122  24.369  1.00  9.07           O  
ATOM    384  ND2 ASN A  77      61.725   1.745  22.711  1.00  8.01           N  
ATOM    385  N   PRO A  78      57.106   5.338  21.822  1.00  8.59           N  
ATOM    386  CA  PRO A  78      56.349   6.208  20.906  1.00  8.52           C  
ATOM    387  C   PRO A  78      57.317   7.107  20.157  1.00  8.42           C  
ATOM    388  O   PRO A  78      58.215   7.717  20.770  1.00  6.84           O  
ATOM    389  CB  PRO A  78      55.413   6.967  21.848  1.00  8.18           C  
ATOM    390  CG  PRO A  78      55.179   5.987  22.939  1.00 11.05           C  
ATOM    391  CD  PRO A  78      56.558   5.408  23.187  1.00  8.33           C  
ATOM    392  N   GLY A  79      57.130   7.179  18.838  1.00  6.86           N  
ATOM    393  CA  GLY A  79      58.016   7.935  17.975  1.00  7.73           C  
ATOM    394  C   GLY A  79      58.927   6.980  17.208  1.00  7.26           C  
ATOM    395  O   GLY A  79      59.538   7.370  16.209  1.00  9.96           O  
ATOM    396  N   LYS A  80      59.005   5.721  17.645  1.00  6.15           N  
ATOM    397  CA  LYS A  80      59.869   4.730  16.990  1.00  6.16           C  
ATOM    398  C   LYS A  80      59.084   3.625  16.276  1.00  6.07           C  
ATOM    399  O   LYS A  80      59.678   2.700  15.702  1.00  5.57           O  
ATOM    400  CB  LYS A  80      60.800   4.065  18.011  1.00  9.19           C  
ATOM    401  CG  LYS A  80      61.560   5.020  18.934  1.00 13.50           C  
ATOM    402  CD  LYS A  80      62.616   5.814  18.202  1.00 16.05           C  
ATOM    403  CE  LYS A  80      63.388   6.717  19.172  1.00 19.09           C  
ATOM    404  NZ  LYS A  80      64.448   7.486  18.453  1.00 21.22           N  
ATOM    405  N   VAL A  81      57.756   3.708  16.328  1.00  3.12           N  
ATOM    406  CA  VAL A  81      56.902   2.711  15.671  1.00  3.39           C  
ATOM    407  C   VAL A  81      56.110   3.333  14.543  1.00  3.05           C  
ATOM    408  O   VAL A  81      55.338   4.281  14.761  1.00  4.29           O  
ATOM    409  CB  VAL A  81      55.905   2.078  16.654  1.00  3.91           C  
ATOM    410  CG1 VAL A  81      54.863   1.217  15.883  1.00  5.29           C  
ATOM    411  CG2 VAL A  81      56.682   1.199  17.668  1.00  3.65           C  
ATOM    412  N   PHE A  82      56.294   2.785  13.347  1.00  3.32           N  
ATOM    413  CA  PHE A  82      55.598   3.269  12.161  1.00  4.59           C  
ATOM    414  C   PHE A  82      54.701   2.241  11.501  1.00  4.62           C  
ATOM    415  O   PHE A  82      55.128   1.122  11.218  1.00  5.67           O  
ATOM    416  CB  PHE A  82      56.617   3.758  11.137  1.00  4.68           C  
ATOM    417  CG  PHE A  82      57.571   4.769  11.697  1.00  7.21           C  
ATOM    418  CD1 PHE A  82      57.169   6.095  11.865  1.00  8.25           C  
ATOM    419  CD2 PHE A  82      58.844   4.385  12.135  1.00  7.12           C  
ATOM    420  CE1 PHE A  82      58.010   7.022  12.465  1.00  9.36           C  
ATOM    421  CE2 PHE A  82      59.700   5.317  12.741  1.00  9.44           C  
ATOM    422  CZ  PHE A  82      59.282   6.626  12.904  1.00  9.70           C  
ATOM    423  N   PHE A  83      53.443   2.627  11.262  1.00  4.76           N  
ATOM    424  CA  PHE A  83      52.498   1.778  10.553  1.00  3.15           C  
ATOM    425  C   PHE A  83      52.485   2.375   9.142  1.00  4.29           C  
ATOM    426  O   PHE A  83      52.105   3.541   8.968  1.00  3.36           O  
ATOM    427  CB  PHE A  83      51.104   1.846  11.178  1.00  3.72           C  
ATOM    428  CG  PHE A  83      50.922   0.912  12.356  1.00  4.75           C  
ATOM    429  CD1 PHE A  83      52.028   0.373  13.025  1.00  5.01           C  
ATOM    430  CD2 PHE A  83      49.649   0.630  12.825  1.00  7.06           C  
ATOM    431  CE1 PHE A  83      51.851  -0.439  14.166  1.00  5.76           C  
ATOM    432  CE2 PHE A  83      49.454  -0.172  13.960  1.00  6.32           C  
ATOM    433  CZ  PHE A  83      50.569  -0.707  14.632  1.00  5.10           C  
ATOM    434  N   THR A  84      52.888   1.581   8.148  1.00  3.67           N  
ATOM    435  CA  THR A  84      53.022   2.082   6.782  1.00  3.83           C  
ATOM    436  C   THR A  84      52.445   1.153   5.724  1.00  4.81           C  
ATOM    437  O   THR A  84      51.889   0.102   6.034  1.00  3.11           O  
ATOM    438  CB  THR A  84      54.525   2.268   6.443  1.00  4.40           C  
ATOM    439  OG1 THR A  84      55.153   0.964   6.377  1.00  5.74           O  
ATOM    440  CG2 THR A  84      55.216   3.098   7.525  1.00  5.76           C  
ATOM    441  N   GLY A  85      52.590   1.548   4.461  1.00  5.53           N  
ATOM    442  CA  GLY A  85      52.099   0.713   3.380  1.00  5.78           C  
ATOM    443  C   GLY A  85      50.584   0.554   3.308  1.00  4.98           C  
ATOM    444  O   GLY A  85      49.820   1.469   3.639  1.00  5.49           O  
ATOM    445  N   ASP A  86      50.156  -0.615   2.850  1.00  4.76           N  
ATOM    446  CA  ASP A  86      48.732  -0.938   2.697  1.00  5.02           C  
ATOM    447  C   ASP A  86      48.246  -1.431   4.055  1.00  3.95           C  
ATOM    448  O   ASP A  86      48.016  -2.614   4.256  1.00  4.36           O  
ATOM    449  CB  ASP A  86      48.596  -2.032   1.636  1.00  6.96           C  
ATOM    450  CG  ASP A  86      47.159  -2.363   1.300  1.00  9.64           C  
ATOM    451  OD1 ASP A  86      46.228  -1.707   1.812  1.00 13.19           O  
ATOM    452  OD2 ASP A  86      46.970  -3.307   0.502  1.00  8.19           O  
ATOM    453  N   ALA A  87      48.077  -0.480   4.963  1.00  5.15           N  
ATOM    454  CA  ALA A  87      47.689  -0.743   6.337  1.00  4.30           C  
ATOM    455  C   ALA A  87      46.228  -0.464   6.668  1.00  6.38           C  
ATOM    456  O   ALA A  87      45.504   0.201   5.921  1.00  5.82           O  
ATOM    457  CB  ALA A  87      48.596   0.061   7.274  1.00  4.51           C  
ATOM    458  N   LYS A  88      45.809  -0.972   7.818  1.00  6.05           N  
ATOM    459  CA  LYS A  88      44.440  -0.795   8.278  1.00  9.27           C  
ATOM    460  C   LYS A  88      44.408  -1.207   9.748  1.00  8.48           C  
ATOM    461  O   LYS A  88      45.120  -2.132  10.132  1.00  7.65           O  
ATOM    462  CB  LYS A  88      43.534  -1.697   7.428  1.00 12.70           C  
ATOM    463  CG  LYS A  88      42.306  -2.292   8.078  1.00 18.36           C  
ATOM    464  CD  LYS A  88      41.646  -3.261   7.114  1.00 18.77           C  
ATOM    465  CE  LYS A  88      40.735  -4.239   7.834  1.00 23.68           C  
ATOM    466  NZ  LYS A  88      40.161  -5.293   6.941  1.00 24.34           N  
ATOM    467  N   VAL A  89      43.655  -0.473  10.572  1.00  4.66           N  
ATOM    468  CA  VAL A  89      43.477  -0.834  11.985  1.00  5.49           C  
ATOM    469  C   VAL A  89      41.965  -0.878  12.245  1.00  6.24           C  
ATOM    470  O   VAL A  89      41.231   0.019  11.824  1.00  5.35           O  
ATOM    471  CB  VAL A  89      44.060   0.219  12.950  1.00  6.10           C  
ATOM    472  CG1 VAL A  89      43.793  -0.207  14.401  1.00  6.79           C  
ATOM    473  CG2 VAL A  89      45.541   0.357  12.731  1.00  7.11           C  
ATOM    474  N   GLU A  90      41.498  -1.930  12.913  1.00  4.97           N  
ATOM    475  CA  GLU A  90      40.079  -2.036  13.259  1.00  7.17           C  
ATOM    476  C   GLU A  90      39.987  -2.349  14.748  1.00  5.61           C  
ATOM    477  O   GLU A  90      40.569  -3.332  15.186  1.00  7.52           O  
ATOM    478  CB  GLU A  90      39.409  -3.163  12.469  1.00  6.40           C  
ATOM    479  CG  GLU A  90      39.304  -2.895  10.983  1.00  9.23           C  
ATOM    480  CD  GLU A  90      38.516  -3.967  10.225  1.00 12.78           C  
ATOM    481  OE1 GLU A  90      38.205  -5.038  10.790  1.00 12.01           O  
ATOM    482  OE2 GLU A  90      38.218  -3.719   9.042  1.00 11.87           O  
ATOM    483  N   LEU A  91      39.303  -1.507  15.526  1.00  6.78           N  
ATOM    484  CA  LEU A  91      39.136  -1.763  16.958  1.00  6.55           C  
ATOM    485  C   LEU A  91      37.681  -2.190  17.054  1.00  7.03           C  
ATOM    486  O   LEU A  91      36.763  -1.348  17.067  1.00  8.56           O  
ATOM    487  CB  LEU A  91      39.414  -0.509  17.796  1.00  5.29           C  
ATOM    488  CG  LEU A  91      40.823   0.094  17.608  1.00  6.02           C  
ATOM    489  CD1 LEU A  91      41.042   1.272  18.558  1.00  8.27           C  
ATOM    490  CD2 LEU A  91      41.873  -0.975  17.870  1.00  7.81           C  
ATOM    491  N   ARG A  92      37.475  -3.504  17.059  1.00  5.88           N  
ATOM    492  CA  ARG A  92      36.134  -4.076  17.090  1.00  6.19           C  
ATOM    493  C   ARG A  92      35.652  -4.445  18.480  1.00  7.80           C  
ATOM    494  O   ARG A  92      34.436  -4.431  18.763  1.00 10.14           O  
ATOM    495  CB  ARG A  92      36.083  -5.270  16.144  1.00  6.36           C  
ATOM    496  CG  ARG A  92      36.180  -4.803  14.677  1.00  6.40           C  
ATOM    497  CD  ARG A  92      35.993  -5.934  13.703  1.00  8.05           C  
ATOM    498  NE  ARG A  92      36.006  -5.470  12.322  1.00 10.05           N  
ATOM    499  CZ  ARG A  92      34.915  -5.139  11.635  1.00  9.53           C  
ATOM    500  NH1 ARG A  92      33.722  -5.218  12.202  1.00  8.95           N  
ATOM    501  NH2 ARG A  92      35.025  -4.767  10.370  1.00  8.49           N  
ATOM    502  N   GLY A  93      36.600  -4.783  19.340  1.00  7.41           N  
ATOM    503  CA  GLY A  93      36.274  -5.089  20.722  1.00  8.60           C  
ATOM    504  C   GLY A  93      36.015  -3.790  21.465  1.00  9.13           C  
ATOM    505  O   GLY A  93      36.059  -2.717  20.854  1.00 10.60           O  
ATOM    506  N   GLU A  94      35.729  -3.883  22.763  1.00 10.34           N  
ATOM    507  CA  GLU A  94      35.462  -2.718  23.605  1.00  8.48           C  
ATOM    508  C   GLU A  94      36.601  -2.554  24.605  1.00  7.12           C  
ATOM    509  O   GLU A  94      37.386  -3.477  24.825  1.00  8.48           O  
ATOM    510  CB  GLU A  94      34.153  -2.886  24.402  1.00 11.70           C  
ATOM    511  CG  GLU A  94      32.867  -3.014  23.601  1.00 15.59           C  
ATOM    512  CD  GLU A  94      31.628  -2.806  24.476  1.00 16.41           C  
ATOM    513  OE1 GLU A  94      31.736  -2.954  25.710  1.00 21.66           O  
ATOM    514  OE2 GLU A  94      30.549  -2.500  23.933  1.00 18.37           O  
ATOM    515  N   HIS A  95      36.697  -1.369  25.192  1.00  7.51           N  
ATOM    516  CA  HIS A  95      37.712  -1.061  26.202  1.00  7.21           C  
ATOM    517  C   HIS A  95      39.125  -1.316  25.732  1.00  7.31           C  
ATOM    518  O   HIS A  95      39.920  -1.983  26.399  1.00  6.11           O  
ATOM    519  CB  HIS A  95      37.411  -1.853  27.480  1.00  8.75           C  
ATOM    520  CG  HIS A  95      36.152  -1.415  28.147  1.00  9.82           C  
ATOM    521  ND1 HIS A  95      36.055  -0.218  28.818  1.00 10.51           N  
ATOM    522  CD2 HIS A  95      34.927  -1.991  28.219  1.00 11.91           C  
ATOM    523  CE1 HIS A  95      34.821  -0.075  29.276  1.00  9.76           C  
ATOM    524  NE2 HIS A  95      34.119  -1.135  28.923  1.00 11.16           N  
ATOM    525  N   LEU A  96      39.426  -0.758  24.571  1.00  6.30           N  
ATOM    526  CA  LEU A  96      40.736  -0.887  23.956  1.00  5.47           C  
ATOM    527  C   LEU A  96      41.372   0.493  23.878  1.00  7.15           C  
ATOM    528  O   LEU A  96      40.667   1.499  23.766  1.00  7.87           O  
ATOM    529  CB  LEU A  96      40.579  -1.437  22.534  1.00  6.38           C  
ATOM    530  CG  LEU A  96      39.804  -2.749  22.369  1.00  6.49           C  
ATOM    531  CD1 LEU A  96      39.658  -3.067  20.869  1.00  7.84           C  
ATOM    532  CD2 LEU A  96      40.557  -3.872  23.066  1.00  6.63           C  
ATOM    533  N   ILE A  97      42.698   0.526  23.942  1.00  6.75           N  
ATOM    534  CA  ILE A  97      43.453   1.766  23.820  1.00  6.62           C  
ATOM    535  C   ILE A  97      44.575   1.559  22.806  1.00  6.71           C  
ATOM    536  O   ILE A  97      45.348   0.610  22.929  1.00  7.10           O  
ATOM    537  CB  ILE A  97      44.113   2.186  25.148  1.00  7.98           C  
ATOM    538  CG1 ILE A  97      43.036   2.453  26.210  1.00  9.70           C  
ATOM    539  CG2 ILE A  97      45.011   3.429  24.914  1.00 10.71           C  
ATOM    540  CD1 ILE A  97      43.610   2.682  27.618  1.00  8.12           C  
ATOM    541  N   LEU A  98      44.636   2.417  21.782  1.00  5.31           N  
ATOM    542  CA  LEU A  98      45.712   2.362  20.788  1.00  4.80           C  
ATOM    543  C   LEU A  98      46.507   3.638  21.034  1.00  4.29           C  
ATOM    544  O   LEU A  98      45.968   4.760  20.946  1.00  4.71           O  
ATOM    545  CB  LEU A  98      45.184   2.348  19.336  1.00  4.88           C  
ATOM    546  CG  LEU A  98      46.306   2.287  18.279  1.00  6.87           C  
ATOM    547  CD1 LEU A  98      47.007   0.935  18.336  1.00  8.42           C  
ATOM    548  CD2 LEU A  98      45.725   2.503  16.867  1.00  7.55           C  
ATOM    549  N   GLU A  99      47.794   3.472  21.316  1.00  3.60           N  
ATOM    550  CA  GLU A  99      48.644   4.609  21.680  1.00  4.72           C  
ATOM    551  C   GLU A  99      50.045   4.665  21.078  1.00  3.65           C  
ATOM    552  O   GLU A  99      50.727   3.642  20.940  1.00  3.44           O  
ATOM    553  CB  GLU A  99      48.774   4.627  23.222  1.00  6.38           C  
ATOM    554  CG  GLU A  99      49.792   5.639  23.800  1.00  5.86           C  
ATOM    555  CD  GLU A  99      49.975   5.498  25.318  1.00  9.90           C  
ATOM    556  OE1 GLU A  99      49.267   4.689  25.943  1.00  9.63           O  
ATOM    557  OE2 GLU A  99      50.833   6.205  25.889  1.00  9.58           O  
ATOM    558  N   GLY A 100      50.466   5.885  20.741  1.00  5.49           N  
ATOM    559  CA  GLY A 100      51.813   6.140  20.268  1.00  5.18           C  
ATOM    560  C   GLY A 100      52.266   5.614  18.927  1.00  5.41           C  
ATOM    561  O   GLY A 100      53.439   5.311  18.755  1.00  5.01           O  
ATOM    562  N   ILE A 101      51.345   5.532  17.977  1.00  5.95           N  
ATOM    563  CA  ILE A 101      51.660   5.011  16.645  1.00  4.25           C  
ATOM    564  C   ILE A 101      51.802   6.158  15.656  1.00  4.25           C  
ATOM    565  O   ILE A 101      51.039   7.117  15.729  1.00  4.94           O  
ATOM    566  CB  ILE A 101      50.512   4.082  16.147  1.00  4.04           C  
ATOM    567  CG1 ILE A 101      50.194   3.000  17.200  1.00  5.07           C  
ATOM    568  CG2 ILE A 101      50.917   3.406  14.848  1.00  4.87           C  
ATOM    569  CD1 ILE A 101      51.383   2.089  17.584  1.00  4.94           C  
ATOM    570  N   TRP A 102      52.777   6.079  14.751  1.00  2.88           N  
ATOM    571  CA  TRP A 102      52.973   7.105  13.724  1.00  4.93           C  
ATOM    572  C   TRP A 102      52.585   6.462  12.401  1.00  3.63           C  
ATOM    573  O   TRP A 102      53.234   5.499  11.967  1.00  5.06           O  
ATOM    574  CB  TRP A 102      54.445   7.547  13.669  1.00  4.24           C  
ATOM    575  CG  TRP A 102      54.737   8.736  12.784  1.00  5.39           C  
ATOM    576  CD1 TRP A 102      54.376   8.904  11.469  1.00  6.06           C  
ATOM    577  CD2 TRP A 102      55.506   9.891  13.137  1.00  7.57           C  
ATOM    578  NE1 TRP A 102      54.879  10.089  10.988  1.00  5.72           N  
ATOM    579  CE2 TRP A 102      55.574  10.716  11.992  1.00  9.52           C  
ATOM    580  CE3 TRP A 102      56.147  10.310  14.316  1.00 10.37           C  
ATOM    581  CZ2 TRP A 102      56.263  11.938  11.985  1.00 10.15           C  
ATOM    582  CZ3 TRP A 102      56.832  11.527  14.310  1.00 12.11           C  
ATOM    583  CH2 TRP A 102      56.882  12.325  13.147  1.00 12.28           C  
ATOM    584  N   PHE A 103      51.544   6.990  11.761  1.00  3.92           N  
ATOM    585  CA  PHE A 103      51.081   6.462  10.462  1.00  3.03           C  
ATOM    586  C   PHE A 103      51.653   7.333   9.360  1.00  3.08           C  
ATOM    587  O   PHE A 103      51.360   8.524   9.315  1.00  3.21           O  
ATOM    588  CB  PHE A 103      49.546   6.514  10.338  1.00  2.46           C  
ATOM    589  CG  PHE A 103      48.818   5.641  11.308  1.00  4.47           C  
ATOM    590  CD1 PHE A 103      48.635   6.047  12.631  1.00  4.86           C  
ATOM    591  CD2 PHE A 103      48.324   4.395  10.900  1.00  3.67           C  
ATOM    592  CE1 PHE A 103      47.963   5.215  13.551  1.00  5.76           C  
ATOM    593  CE2 PHE A 103      47.653   3.560  11.804  1.00  2.94           C  
ATOM    594  CZ  PHE A 103      47.473   3.968  13.130  1.00  1.89           C  
ATOM    595  N   LYS A 104      52.459   6.744   8.477  1.00  2.49           N  
ATOM    596  CA  LYS A 104      53.047   7.477   7.352  1.00  2.87           C  
ATOM    597  C   LYS A 104      53.401   6.499   6.239  1.00  3.96           C  
ATOM    598  O   LYS A 104      53.327   5.268   6.416  1.00  3.23           O  
ATOM    599  CB  LYS A 104      54.354   8.178   7.762  1.00  3.24           C  
ATOM    600  CG  LYS A 104      55.462   7.198   8.220  1.00  4.17           C  
ATOM    601  CD  LYS A 104      56.811   7.922   8.453  1.00  5.93           C  
ATOM    602  CE  LYS A 104      57.969   6.916   8.618  1.00  6.36           C  
ATOM    603  NZ  LYS A 104      59.277   7.621   8.733  1.00  7.96           N  
ATOM    604  N   ASP A 105      53.824   7.060   5.107  1.00  3.67           N  
ATOM    605  CA  ASP A 105      54.281   6.241   3.973  1.00  4.72           C  
ATOM    606  C   ASP A 105      53.307   5.130   3.624  1.00  4.77           C  
ATOM    607  O   ASP A 105      53.704   3.975   3.433  1.00  5.25           O  
ATOM    608  CB  ASP A 105      55.646   5.626   4.307  1.00  6.53           C  
ATOM    609  CG  ASP A 105      56.721   6.673   4.566  1.00 10.24           C  
ATOM    610  OD1 ASP A 105      56.546   7.843   4.139  1.00 10.30           O  
ATOM    611  OD2 ASP A 105      57.756   6.315   5.182  1.00  8.33           O  
ATOM    612  N   GLY A 106      52.037   5.505   3.514  1.00  4.53           N  
ATOM    613  CA  GLY A 106      50.981   4.565   3.195  1.00  2.42           C  
ATOM    614  C   GLY A 106      50.863   4.246   1.717  1.00  3.97           C  
ATOM    615  O   GLY A 106      51.441   4.921   0.857  1.00  4.26           O  
ATOM    616  N   ASN A 107      50.082   3.215   1.424  1.00  3.92           N  
ATOM    617  CA  ASN A 107      49.917   2.768   0.045  1.00  5.01           C  
ATOM    618  C   ASN A 107      48.667   1.895  -0.098  1.00  4.54           C  
ATOM    619  O   ASN A 107      48.696   0.866  -0.780  1.00  4.92           O  
ATOM    620  CB  ASN A 107      51.167   1.968  -0.360  1.00  8.42           C  
ATOM    621  CG  ASN A 107      51.069   1.422  -1.763  1.00 12.76           C  
ATOM    622  OD1 ASN A 107      50.684   2.143  -2.683  1.00 12.56           O  
ATOM    623  ND2 ASN A 107      51.413   0.140  -1.934  1.00 12.35           N  
ATOM    624  N   ARG A 108      47.566   2.295   0.537  1.00  2.78           N  
ATOM    625  CA  ARG A 108      46.335   1.517   0.395  1.00  2.16           C  
ATOM    626  C   ARG A 108      45.875   1.620  -1.061  1.00  3.44           C  
ATOM    627  O   ARG A 108      46.222   2.580  -1.780  1.00  3.67           O  
ATOM    628  CB  ARG A 108      45.231   2.030   1.328  1.00  2.29           C  
ATOM    629  CG  ARG A 108      45.539   1.798   2.807  1.00  2.55           C  
ATOM    630  CD  ARG A 108      44.519   2.510   3.676  1.00  2.30           C  
ATOM    631  NE  ARG A 108      44.569   3.965   3.482  1.00  2.65           N  
ATOM    632  CZ  ARG A 108      43.610   4.788   3.898  1.00  4.34           C  
ATOM    633  NH1 ARG A 108      42.542   4.298   4.522  1.00  1.77           N  
ATOM    634  NH2 ARG A 108      43.710   6.095   3.688  1.00  3.11           N  
ATOM    635  N   ALA A 109      45.097   0.636  -1.487  1.00  5.02           N  
ATOM    636  CA  ALA A 109      44.603   0.569  -2.869  1.00  6.47           C  
ATOM    637  C   ALA A 109      43.548   1.636  -3.118  1.00  6.94           C  
ATOM    638  O   ALA A 109      42.502   1.659  -2.463  1.00  6.78           O  
ATOM    639  CB  ALA A 109      44.029  -0.825  -3.152  1.00  5.97           C  
ATOM    640  N   ILE A 110      43.799   2.509  -4.084  1.00  5.48           N  
ATOM    641  CA  ILE A 110      42.834   3.569  -4.334  1.00  6.16           C  
ATOM    642  C   ILE A 110      41.450   3.069  -4.763  1.00  6.53           C  
ATOM    643  O   ILE A 110      40.460   3.754  -4.539  1.00  7.99           O  
ATOM    644  CB  ILE A 110      43.373   4.595  -5.373  1.00  7.26           C  
ATOM    645  CG1 ILE A 110      43.788   3.888  -6.657  1.00  8.98           C  
ATOM    646  CG2 ILE A 110      44.581   5.368  -4.789  1.00  6.66           C  
ATOM    647  CD1 ILE A 110      44.066   4.877  -7.808  1.00 12.48           C  
ATOM    648  N   GLN A 111      41.366   1.884  -5.368  1.00  7.45           N  
ATOM    649  CA  GLN A 111      40.077   1.346  -5.793  1.00  7.50           C  
ATOM    650  C   GLN A 111      39.358   0.617  -4.655  1.00  7.65           C  
ATOM    651  O   GLN A 111      38.249   0.113  -4.847  1.00  7.57           O  
ATOM    652  CB  GLN A 111      40.272   0.347  -6.947  1.00  9.36           C  
ATOM    653  CG  GLN A 111      41.080  -0.910  -6.563  1.00 11.24           C  
ATOM    654  CD  GLN A 111      42.610  -0.796  -6.808  1.00 15.65           C  
ATOM    655  OE1 GLN A 111      43.231   0.261  -6.609  1.00 15.78           O  
ATOM    656  NE2 GLN A 111      43.217  -1.913  -7.239  1.00 16.72           N  
ATOM    657  N   ALA A 112      39.983   0.548  -3.479  1.00  6.95           N  
ATOM    658  CA  ALA A 112      39.416  -0.193  -2.351  1.00  6.73           C  
ATOM    659  C   ALA A 112      38.906   0.602  -1.156  1.00  5.88           C  
ATOM    660  O   ALA A 112      38.387   0.022  -0.218  1.00  6.90           O  
ATOM    661  CB  ALA A 112      40.443  -1.217  -1.850  1.00  6.09           C  
ATOM    662  N   TRP A 113      39.040   1.919  -1.190  1.00  3.50           N  
ATOM    663  CA  TRP A 113      38.605   2.736  -0.072  1.00  2.50           C  
ATOM    664  C   TRP A 113      37.724   3.863  -0.589  1.00  3.98           C  
ATOM    665  O   TRP A 113      37.933   4.343  -1.705  1.00  4.03           O  
ATOM    666  CB  TRP A 113      39.829   3.319   0.657  1.00  2.90           C  
ATOM    667  CG  TRP A 113      40.657   2.267   1.365  1.00  3.95           C  
ATOM    668  CD1 TRP A 113      41.527   1.382   0.795  1.00  4.59           C  
ATOM    669  CD2 TRP A 113      40.611   1.948   2.760  1.00  5.24           C  
ATOM    670  NE1 TRP A 113      42.024   0.520   1.756  1.00  4.40           N  
ATOM    671  CE2 TRP A 113      41.475   0.849   2.969  1.00  5.45           C  
ATOM    672  CE3 TRP A 113      39.923   2.485   3.855  1.00  5.69           C  
ATOM    673  CZ2 TRP A 113      41.662   0.274   4.231  1.00  4.46           C  
ATOM    674  CZ3 TRP A 113      40.109   1.913   5.118  1.00  7.48           C  
ATOM    675  CH2 TRP A 113      40.974   0.816   5.292  1.00  5.91           C  
ATOM    676  N   LYS A 114      36.742   4.282   0.218  1.00  4.33           N  
ATOM    677  CA  LYS A 114      35.831   5.360  -0.199  1.00  3.95           C  
ATOM    678  C   LYS A 114      35.542   6.377   0.891  1.00  5.59           C  
ATOM    679  O   LYS A 114      35.618   6.077   2.087  1.00  4.21           O  
ATOM    680  CB  LYS A 114      34.470   4.786  -0.591  1.00  3.66           C  
ATOM    681  CG  LYS A 114      33.764   4.091   0.607  1.00  4.71           C  
ATOM    682  CD  LYS A 114      32.335   3.669   0.248  1.00  6.35           C  
ATOM    683  CE  LYS A 114      31.618   3.071   1.467  1.00  9.47           C  
ATOM    684  NZ  LYS A 114      30.284   2.471   1.090  1.00 10.24           N  
ATOM    685  N   SER A 115      35.189   7.584   0.466  1.00  5.36           N  
ATOM    686  CA  SER A 115      34.755   8.575   1.435  1.00  6.82           C  
ATOM    687  C   SER A 115      33.449   7.962   1.948  1.00  6.12           C  
ATOM    688  O   SER A 115      32.762   7.253   1.203  1.00  6.47           O  
ATOM    689  CB  SER A 115      34.483   9.910   0.750  1.00  7.88           C  
ATOM    690  OG  SER A 115      35.688  10.402   0.210  1.00 12.80           O  
ATOM    691  N   HIS A 116      33.118   8.230   3.210  1.00  5.03           N  
ATOM    692  CA  HIS A 116      31.909   7.711   3.878  1.00  6.24           C  
ATOM    693  C   HIS A 116      32.052   6.245   4.278  1.00  6.69           C  
ATOM    694  O   HIS A 116      31.088   5.608   4.709  1.00  6.18           O  
ATOM    695  CB  HIS A 116      30.675   7.896   2.998  1.00  6.76           C  
ATOM    696  CG  HIS A 116      30.424   9.318   2.610  1.00  7.74           C  
ATOM    697  ND1 HIS A 116      29.817  10.221   3.457  1.00 10.04           N  
ATOM    698  CD2 HIS A 116      30.678   9.990   1.461  1.00  9.37           C  
ATOM    699  CE1 HIS A 116      29.703  11.388   2.845  1.00  9.86           C  
ATOM    700  NE2 HIS A 116      30.219  11.276   1.632  1.00 10.03           N  
ATOM    701  N   GLY A 117      33.253   5.709   4.121  1.00  5.27           N  
ATOM    702  CA  GLY A 117      33.502   4.337   4.528  1.00  6.50           C  
ATOM    703  C   GLY A 117      34.314   4.334   5.819  1.00  5.66           C  
ATOM    704  O   GLY A 117      34.434   5.362   6.510  1.00  5.46           O  
ATOM    705  N   PRO A 118      34.886   3.189   6.190  1.00  5.73           N  
ATOM    706  CA  PRO A 118      35.680   3.162   7.424  1.00  5.67           C  
ATOM    707  C   PRO A 118      36.970   3.967   7.259  1.00  5.71           C  
ATOM    708  O   PRO A 118      37.494   4.119   6.138  1.00  5.61           O  
ATOM    709  CB  PRO A 118      35.971   1.678   7.619  1.00  6.23           C  
ATOM    710  CG  PRO A 118      35.999   1.145   6.200  1.00  6.85           C  
ATOM    711  CD  PRO A 118      34.823   1.859   5.553  1.00  4.67           C  
ATOM    712  N   GLY A 119      37.479   4.484   8.367  1.00  5.90           N  
ATOM    713  CA  GLY A 119      38.736   5.217   8.307  1.00  6.03           C  
ATOM    714  C   GLY A 119      39.935   4.270   8.322  1.00  5.60           C  
ATOM    715  O   GLY A 119      39.794   3.056   8.480  1.00  4.10           O  
ATOM    716  N   LEU A 120      41.122   4.843   8.139  1.00  3.67           N  
ATOM    717  CA  LEU A 120      42.392   4.111   8.177  1.00  3.97           C  
ATOM    718  C   LEU A 120      42.353   3.387   9.508  1.00  4.23           C  
ATOM    719  O   LEU A 120      42.738   2.218   9.595  1.00  4.82           O  
ATOM    720  CB  LEU A 120      43.556   5.106   8.111  1.00  2.33           C  
ATOM    721  CG  LEU A 120      44.961   4.540   8.377  1.00  2.46           C  
ATOM    722  CD1 LEU A 120      45.293   3.393   7.390  1.00  5.71           C  
ATOM    723  CD2 LEU A 120      45.950   5.677   8.221  1.00  3.78           C  
ATOM    724  N   VAL A 121      41.932   4.105  10.553  1.00  4.33           N  
ATOM    725  CA  VAL A 121      41.694   3.474  11.845  1.00  2.84           C  
ATOM    726  C   VAL A 121      40.171   3.542  11.939  1.00  2.85           C  
ATOM    727  O   VAL A 121      39.613   4.634  11.919  1.00  4.45           O  
ATOM    728  CB  VAL A 121      42.276   4.252  13.030  1.00  3.01           C  
ATOM    729  CG1 VAL A 121      41.776   3.623  14.361  1.00  4.41           C  
ATOM    730  CG2 VAL A 121      43.792   4.211  12.983  1.00  1.73           C  
ATOM    731  N   ALA A 122      39.509   2.391  12.053  1.00  3.68           N  
ATOM    732  CA  ALA A 122      38.049   2.335  12.155  1.00  3.50           C  
ATOM    733  C   ALA A 122      37.688   1.751  13.521  1.00  4.37           C  
ATOM    734  O   ALA A 122      38.111   0.655  13.868  1.00  3.85           O  
ATOM    735  CB  ALA A 122      37.470   1.454  11.035  1.00  3.62           C  
ATOM    736  N   ILE A 123      36.914   2.499  14.294  1.00  3.99           N  
ATOM    737  CA  ILE A 123      36.514   2.059  15.636  1.00  4.21           C  
ATOM    738  C   ILE A 123      35.075   1.548  15.594  1.00  4.34           C  
ATOM    739  O   ILE A 123      34.136   2.331  15.444  1.00  5.71           O  
ATOM    740  CB  ILE A 123      36.614   3.237  16.621  1.00  4.54           C  
ATOM    741  CG1 ILE A 123      37.998   3.872  16.503  1.00  4.43           C  
ATOM    742  CG2 ILE A 123      36.345   2.758  18.039  1.00  7.05           C  
ATOM    743  CD1 ILE A 123      38.208   5.067  17.433  1.00  5.80           C  
ATOM    744  N   TYR A 124      34.918   0.234  15.734  1.00  4.28           N  
ATOM    745  CA  TYR A 124      33.600  -0.400  15.695  1.00  4.80           C  
ATOM    746  C   TYR A 124      33.015  -0.716  17.061  1.00  6.49           C  
ATOM    747  O   TYR A 124      31.826  -0.970  17.160  1.00  8.87           O  
ATOM    748  CB  TYR A 124      33.656  -1.700  14.883  1.00  5.46           C  
ATOM    749  CG  TYR A 124      33.957  -1.514  13.408  1.00  5.94           C  
ATOM    750  CD1 TYR A 124      32.934  -1.319  12.480  1.00  8.00           C  
ATOM    751  CD2 TYR A 124      35.271  -1.564  12.940  1.00  6.68           C  
ATOM    752  CE1 TYR A 124      33.218  -1.179  11.117  1.00  8.01           C  
ATOM    753  CE2 TYR A 124      35.563  -1.434  11.595  1.00  8.03           C  
ATOM    754  CZ  TYR A 124      34.535  -1.239  10.689  1.00  7.94           C  
ATOM    755  OH  TYR A 124      34.829  -1.111   9.362  1.00  9.97           O  
ATOM    756  N   GLY A 125      33.844  -0.702  18.106  1.00  7.51           N  
ATOM    757  CA  GLY A 125      33.354  -1.007  19.439  1.00  6.82           C  
ATOM    758  C   GLY A 125      33.296   0.205  20.338  1.00  7.51           C  
ATOM    759  O   GLY A 125      33.935   1.216  20.054  1.00  7.91           O  
ATOM    760  N   SER A 126      32.545   0.105  21.432  1.00  7.86           N  
ATOM    761  CA  SER A 126      32.430   1.213  22.365  1.00  6.58           C  
ATOM    762  C   SER A 126      33.574   1.275  23.385  1.00  5.79           C  
ATOM    763  O   SER A 126      34.373   0.341  23.506  1.00  7.58           O  
ATOM    764  CB  SER A 126      31.097   1.128  23.105  1.00  7.01           C  
ATOM    765  OG  SER A 126      30.030   1.254  22.192  1.00  6.85           O  
ATOM    766  N   TYR A 127      33.639   2.392  24.114  1.00  5.21           N  
ATOM    767  CA  TYR A 127      34.649   2.621  25.149  1.00  6.83           C  
ATOM    768  C   TYR A 127      36.087   2.416  24.678  1.00  6.72           C  
ATOM    769  O   TYR A 127      36.915   1.852  25.397  1.00  6.66           O  
ATOM    770  CB  TYR A 127      34.388   1.729  26.372  1.00  9.42           C  
ATOM    771  CG  TYR A 127      32.950   1.729  26.827  1.00 10.13           C  
ATOM    772  CD1 TYR A 127      32.435   2.764  27.598  1.00 14.34           C  
ATOM    773  CD2 TYR A 127      32.093   0.708  26.438  1.00 15.09           C  
ATOM    774  CE1 TYR A 127      31.063   2.777  27.969  1.00 16.48           C  
ATOM    775  CE2 TYR A 127      30.749   0.707  26.799  1.00 17.51           C  
ATOM    776  CZ  TYR A 127      30.237   1.736  27.554  1.00 17.54           C  
ATOM    777  OH  TYR A 127      28.882   1.716  27.854  1.00 21.69           O  
ATOM    778  N   ASN A 128      36.379   2.877  23.465  1.00  5.50           N  
ATOM    779  CA  ASN A 128      37.721   2.755  22.904  1.00  6.38           C  
ATOM    780  C   ASN A 128      38.378   4.118  22.826  1.00  5.94           C  
ATOM    781  O   ASN A 128      37.689   5.134  22.701  1.00  6.18           O  
ATOM    782  CB  ASN A 128      37.661   2.127  21.510  1.00  6.45           C  
ATOM    783  CG  ASN A 128      37.324   0.650  21.569  1.00  8.20           C  
ATOM    784  OD1 ASN A 128      37.719  -0.035  22.510  1.00  8.61           O  
ATOM    785  ND2 ASN A 128      36.598   0.154  20.573  1.00  7.11           N  
ATOM    786  N   ARG A 129      39.704   4.131  22.906  1.00  5.75           N  
ATOM    787  CA  ARG A 129      40.472   5.378  22.878  1.00  6.04           C  
ATOM    788  C   ARG A 129      41.684   5.268  21.964  1.00  6.63           C  
ATOM    789  O   ARG A 129      42.384   4.258  21.985  1.00  5.48           O  
ATOM    790  CB  ARG A 129      40.962   5.706  24.294  1.00  7.15           C  
ATOM    791  CG  ARG A 129      41.860   6.950  24.390  1.00  4.26           C  
ATOM    792  CD  ARG A 129      42.332   7.185  25.848  1.00  6.02           C  
ATOM    793  NE  ARG A 129      43.105   8.422  25.966  1.00  3.63           N  
ATOM    794  CZ  ARG A 129      43.878   8.737  26.996  1.00  6.57           C  
ATOM    795  NH1 ARG A 129      43.991   7.903  28.025  1.00  9.43           N  
ATOM    796  NH2 ARG A 129      44.555   9.876  26.991  1.00  5.81           N  
ATOM    797  N   ILE A 130      41.911   6.302  21.153  1.00  5.11           N  
ATOM    798  CA  ILE A 130      43.089   6.345  20.296  1.00  4.87           C  
ATOM    799  C   ILE A 130      43.751   7.619  20.789  1.00  4.43           C  
ATOM    800  O   ILE A 130      43.140   8.683  20.790  1.00  5.30           O  
ATOM    801  CB  ILE A 130      42.749   6.439  18.795  0.50  3.88           C  
ATOM    802  CG1 ILE A 130      44.047   6.640  18.003  0.50  3.57           C  
ATOM    803  CG2 ILE A 130      41.766   7.539  18.544  0.50  6.99           C  
ATOM    804  CD1 ILE A 130      43.925   6.279  16.558  1.00 12.08           C  
ATOM    805  N   THR A 131      44.982   7.499  21.277  1.00  3.55           N  
ATOM    806  CA  THR A 131      45.669   8.655  21.828  1.00  4.38           C  
ATOM    807  C   THR A 131      47.135   8.726  21.454  1.00  4.16           C  
ATOM    808  O   THR A 131      47.801   7.701  21.214  1.00  2.83           O  
ATOM    809  CB  THR A 131      45.550   8.662  23.387  1.00  4.54           C  
ATOM    810  OG1 THR A 131      46.220   9.813  23.923  1.00  5.61           O  
ATOM    811  CG2 THR A 131      46.184   7.383  23.976  1.00  6.85           C  
ATOM    812  N   ALA A 132      47.633   9.959  21.381  1.00  3.52           N  
ATOM    813  CA  ALA A 132      49.027  10.217  21.084  1.00  3.05           C  
ATOM    814  C   ALA A 132      49.550   9.531  19.827  1.00  4.33           C  
ATOM    815  O   ALA A 132      50.636   8.922  19.829  1.00  4.33           O  
ATOM    816  CB  ALA A 132      49.880   9.853  22.304  1.00  4.28           C  
ATOM    817  N   CYS A 133      48.755   9.623  18.759  1.00  3.59           N  
ATOM    818  CA  CYS A 133      49.105   9.063  17.448  1.00  3.74           C  
ATOM    819  C   CYS A 133      49.267  10.182  16.426  1.00  4.10           C  
ATOM    820  O   CYS A 133      48.655  11.249  16.542  1.00  4.45           O  
ATOM    821  CB  CYS A 133      48.030   8.093  16.950  1.00  2.48           C  
ATOM    822  SG  CYS A 133      47.967   6.503  17.850  1.00  5.62           S  
ATOM    823  N   VAL A 134      50.089   9.908  15.424  1.00  3.47           N  
ATOM    824  CA  VAL A 134      50.404  10.859  14.374  1.00  3.43           C  
ATOM    825  C   VAL A 134      49.929  10.291  13.042  1.00  3.36           C  
ATOM    826  O   VAL A 134      50.184   9.132  12.745  1.00  3.36           O  
ATOM    827  CB  VAL A 134      51.937  11.086  14.318  1.00  4.87           C  
ATOM    828  CG1 VAL A 134      52.325  11.814  13.035  1.00  5.35           C  
ATOM    829  CG2 VAL A 134      52.390  11.871  15.563  1.00  3.51           C  
ATOM    830  N   PHE A 135      49.210  11.107  12.271  1.00  1.62           N  
ATOM    831  CA  PHE A 135      48.722  10.725  10.941  1.00  2.48           C  
ATOM    832  C   PHE A 135      49.249  11.845  10.051  1.00  1.81           C  
ATOM    833  O   PHE A 135      48.805  12.995  10.156  1.00  3.07           O  
ATOM    834  CB  PHE A 135      47.194  10.695  10.889  1.00  1.18           C  
ATOM    835  CG  PHE A 135      46.572   9.638  11.753  1.00  3.20           C  
ATOM    836  CD1 PHE A 135      46.378   9.857  13.117  1.00  4.39           C  
ATOM    837  CD2 PHE A 135      46.145   8.429  11.195  1.00  5.44           C  
ATOM    838  CE1 PHE A 135      45.762   8.888  13.918  1.00  3.42           C  
ATOM    839  CE2 PHE A 135      45.526   7.451  11.996  1.00  5.79           C  
ATOM    840  CZ  PHE A 135      45.339   7.693  13.364  1.00  5.04           C  
ATOM    841  N   ASP A 136      50.195  11.508   9.171  1.00  4.15           N  
ATOM    842  CA  ASP A 136      50.834  12.528   8.339  1.00  3.63           C  
ATOM    843  C   ASP A 136      50.914  12.159   6.855  1.00  3.86           C  
ATOM    844  O   ASP A 136      51.705  11.292   6.474  1.00  5.33           O  
ATOM    845  CB  ASP A 136      52.237  12.788   8.946  1.00  2.14           C  
ATOM    846  CG  ASP A 136      53.009  13.890   8.231  1.00  6.29           C  
ATOM    847  OD1 ASP A 136      52.386  14.884   7.806  1.00  4.17           O  
ATOM    848  OD2 ASP A 136      54.253  13.759   8.124  1.00  4.47           O  
ATOM    849  N   CYS A 137      50.082  12.822   6.035  1.00  3.62           N  
ATOM    850  CA  CYS A 137      50.012  12.602   4.582  1.00  3.65           C  
ATOM    851  C   CYS A 137      50.127  11.100   4.316  1.00  5.02           C  
ATOM    852  O   CYS A 137      50.988  10.626   3.567  1.00  2.82           O  
ATOM    853  CB  CYS A 137      51.139  13.377   3.886  1.00  3.25           C  
ATOM    854  SG  CYS A 137      50.904  13.491   2.104  1.00  5.93           S  
ATOM    855  N   PHE A 138      49.198  10.350   4.893  1.00  3.68           N  
ATOM    856  CA  PHE A 138      49.309   8.903   4.824  1.00  3.02           C  
ATOM    857  C   PHE A 138      49.406   8.299   3.443  1.00  3.27           C  
ATOM    858  O   PHE A 138      50.402   7.639   3.130  1.00  4.68           O  
ATOM    859  CB  PHE A 138      48.185   8.211   5.595  1.00  2.11           C  
ATOM    860  CG  PHE A 138      48.445   6.720   5.787  1.00  3.71           C  
ATOM    861  CD1 PHE A 138      49.498   6.297   6.592  1.00  2.94           C  
ATOM    862  CD2 PHE A 138      47.699   5.762   5.099  1.00  4.27           C  
ATOM    863  CE1 PHE A 138      49.815   4.932   6.717  1.00  2.94           C  
ATOM    864  CE2 PHE A 138      47.997   4.402   5.215  1.00  2.97           C  
ATOM    865  CZ  PHE A 138      49.069   3.987   6.033  1.00  3.73           C  
ATOM    866  N   ASP A 139      48.395   8.493   2.612  1.00  2.98           N  
ATOM    867  CA  ASP A 139      48.468   7.920   1.268  1.00  4.55           C  
ATOM    868  C   ASP A 139      47.487   8.589   0.339  1.00  4.68           C  
ATOM    869  O   ASP A 139      47.047   9.706   0.610  1.00  5.83           O  
ATOM    870  CB  ASP A 139      48.286   6.374   1.295  1.00  3.38           C  
ATOM    871  CG  ASP A 139      46.909   5.917   1.763  1.00  5.06           C  
ATOM    872  OD1 ASP A 139      45.981   6.743   1.926  1.00  5.00           O  
ATOM    873  OD2 ASP A 139      46.770   4.682   1.983  1.00  4.28           O  
ATOM    874  N   GLU A 140      47.154   7.923  -0.764  1.00  4.18           N  
ATOM    875  CA  GLU A 140      46.253   8.508  -1.754  1.00  4.27           C  
ATOM    876  C   GLU A 140      44.863   7.880  -1.781  1.00  3.61           C  
ATOM    877  O   GLU A 140      44.062   8.177  -2.668  1.00  4.69           O  
ATOM    878  CB  GLU A 140      46.896   8.409  -3.153  1.00  2.86           C  
ATOM    879  CG  GLU A 140      48.131   9.336  -3.315  1.00  6.45           C  
ATOM    880  CD  GLU A 140      48.854   9.151  -4.638  1.00  8.72           C  
ATOM    881  OE1 GLU A 140      48.186   8.809  -5.637  1.00  8.91           O  
ATOM    882  OE2 GLU A 140      50.083   9.365  -4.679  1.00  8.74           O  
ATOM    883  N   ALA A 141      44.570   7.019  -0.817  1.00  3.02           N  
ATOM    884  CA  ALA A 141      43.264   6.355  -0.781  1.00  4.15           C  
ATOM    885  C   ALA A 141      42.262   7.225  -0.025  1.00  3.66           C  
ATOM    886  O   ALA A 141      42.544   7.681   1.089  1.00  4.03           O  
ATOM    887  CB  ALA A 141      43.394   5.003  -0.106  1.00  3.74           C  
ATOM    888  N   ASN A 142      41.104   7.463  -0.629  1.00  3.40           N  
ATOM    889  CA  ASN A 142      40.085   8.311  -0.017  1.00  3.25           C  
ATOM    890  C   ASN A 142      39.342   7.647   1.133  1.00  5.37           C  
ATOM    891  O   ASN A 142      38.738   6.591   0.963  1.00  4.66           O  
ATOM    892  CB  ASN A 142      39.092   8.782  -1.087  1.00  3.83           C  
ATOM    893  CG  ASN A 142      39.760   9.639  -2.140  1.00  5.48           C  
ATOM    894  OD1 ASN A 142      40.552  10.522  -1.808  1.00  4.46           O  
ATOM    895  ND2 ASN A 142      39.448   9.383  -3.420  1.00  5.73           N  
ATOM    896  N   SER A 143      39.388   8.298   2.291  1.00  4.12           N  
ATOM    897  CA  SER A 143      38.743   7.824   3.506  1.00  3.86           C  
ATOM    898  C   SER A 143      39.180   8.774   4.609  1.00  3.36           C  
ATOM    899  O   SER A 143      40.072   9.600   4.416  1.00  3.74           O  
ATOM    900  CB  SER A 143      39.246   6.426   3.901  1.00  4.94           C  
ATOM    901  OG  SER A 143      40.530   6.518   4.529  1.00  5.55           O  
ATOM    902  N   ALA A 144      38.549   8.662   5.767  1.00  3.41           N  
ATOM    903  CA  ALA A 144      38.965   9.487   6.907  1.00  3.31           C  
ATOM    904  C   ALA A 144      40.192   8.829   7.495  1.00  3.98           C  
ATOM    905  O   ALA A 144      40.531   7.698   7.138  1.00  5.61           O  
ATOM    906  CB  ALA A 144      37.878   9.517   7.959  1.00  3.80           C  
ATOM    907  N   TYR A 145      40.864   9.529   8.405  1.00  3.72           N  
ATOM    908  CA  TYR A 145      42.018   8.952   9.074  1.00  4.24           C  
ATOM    909  C   TYR A 145      41.475   8.130  10.267  1.00  3.50           C  
ATOM    910  O   TYR A 145      42.008   7.063  10.564  1.00  2.38           O  
ATOM    911  CB  TYR A 145      42.990  10.036   9.526  1.00  4.74           C  
ATOM    912  CG  TYR A 145      43.904  10.536   8.412  1.00  5.01           C  
ATOM    913  CD1 TYR A 145      43.948   9.892   7.168  1.00  7.27           C  
ATOM    914  CD2 TYR A 145      44.756  11.620   8.624  1.00  7.80           C  
ATOM    915  CE1 TYR A 145      44.840  10.328   6.157  1.00 10.18           C  
ATOM    916  CE2 TYR A 145      45.645  12.056   7.623  1.00  8.62           C  
ATOM    917  CZ  TYR A 145      45.677  11.404   6.401  1.00  9.07           C  
ATOM    918  OH  TYR A 145      46.527  11.858   5.399  1.00  7.67           O  
ATOM    919  N   ILE A 146      40.425   8.620  10.939  1.00  2.48           N  
ATOM    920  CA  ILE A 146      39.808   7.831  12.020  1.00  2.47           C  
ATOM    921  C   ILE A 146      38.290   7.934  11.919  1.00  2.99           C  
ATOM    922  O   ILE A 146      37.756   8.994  11.626  1.00  2.54           O  
ATOM    923  CB  ILE A 146      40.164   8.316  13.455  1.00  2.53           C  
ATOM    924  CG1 ILE A 146      41.672   8.300  13.701  1.00  2.53           C  
ATOM    925  CG2 ILE A 146      39.481   7.368  14.520  1.00  3.02           C  
ATOM    926  CD1 ILE A 146      42.025   8.977  15.077  1.00  1.50           C  
ATOM    927  N   THR A 147      37.592   6.825  12.130  1.00  2.36           N  
ATOM    928  CA  THR A 147      36.131   6.875  12.147  1.00  2.26           C  
ATOM    929  C   THR A 147      35.615   6.040  13.307  1.00  3.41           C  
ATOM    930  O   THR A 147      36.323   5.161  13.804  1.00  3.63           O  
ATOM    931  CB  THR A 147      35.440   6.226  10.890  1.00  2.26           C  
ATOM    932  OG1 THR A 147      35.842   4.846  10.759  1.00  3.49           O  
ATOM    933  CG2 THR A 147      35.777   7.008   9.603  1.00  3.02           C  
ATOM    934  N   THR A 148      34.415   6.356  13.788  1.00  3.47           N  
ATOM    935  CA  THR A 148      33.751   5.429  14.710  1.00  4.07           C  
ATOM    936  C   THR A 148      32.760   4.917  13.646  1.00  5.38           C  
ATOM    937  O   THR A 148      32.118   5.717  12.944  1.00  4.78           O  
ATOM    938  CB  THR A 148      33.025   6.092  15.935  1.00  4.14           C  
ATOM    939  OG1 THR A 148      32.131   7.145  15.516  1.00  5.07           O  
ATOM    940  CG2 THR A 148      34.060   6.626  16.917  1.00  4.69           C  
ATOM    941  N   SER A 149      32.684   3.600  13.473  1.00  3.61           N  
ATOM    942  CA  SER A 149      31.865   3.009  12.414  1.00  4.06           C  
ATOM    943  C   SER A 149      30.852   1.981  12.883  1.00  5.85           C  
ATOM    944  O   SER A 149      31.115   1.217  13.816  1.00  6.20           O  
ATOM    945  CB  SER A 149      32.786   2.323  11.383  1.00  5.98           C  
ATOM    946  OG  SER A 149      33.627   3.266  10.735  1.00  8.51           O  
ATOM    947  N   LEU A 150      29.698   1.940  12.224  1.00  6.38           N  
ATOM    948  CA  LEU A 150      28.678   0.952  12.596  1.00  7.16           C  
ATOM    949  C   LEU A 150      29.087  -0.405  12.057  1.00  8.07           C  
ATOM    950  O   LEU A 150      29.643  -0.506  10.948  1.00  9.72           O  
ATOM    951  CB  LEU A 150      27.315   1.295  11.985  1.00  8.14           C  
ATOM    952  CG  LEU A 150      26.438   2.358  12.663  1.00  7.42           C  
ATOM    953  CD1 LEU A 150      27.142   3.693  12.608  1.00  6.26           C  
ATOM    954  CD2 LEU A 150      25.097   2.434  11.940  1.00  8.85           C  
ATOM    955  N   THR A 151      28.803  -1.450  12.829  1.00  9.16           N  
ATOM    956  CA  THR A 151      29.076  -2.809  12.368  1.00 11.81           C  
ATOM    957  C   THR A 151      27.947  -3.171  11.395  1.00 12.68           C  
ATOM    958  O   THR A 151      26.943  -2.464  11.314  1.00 10.30           O  
ATOM    959  CB  THR A 151      29.094  -3.803  13.535  1.00 12.08           C  
ATOM    960  OG1 THR A 151      28.027  -3.500  14.430  1.00 12.67           O  
ATOM    961  CG2 THR A 151      30.414  -3.720  14.282  1.00 14.13           C  
ATOM    962  N   GLU A 152      28.095  -4.270  10.660  1.00 13.95           N  
ATOM    963  CA  GLU A 152      27.066  -4.640   9.686  1.00 17.45           C  
ATOM    964  C   GLU A 152      25.675  -4.819  10.274  1.00 16.91           C  
ATOM    965  O   GLU A 152      24.679  -4.619   9.583  1.00 17.18           O  
ATOM    966  CB  GLU A 152      27.457  -5.916   8.933  1.00 20.79           C  
ATOM    967  CG  GLU A 152      28.471  -5.725   7.807  1.00 28.55           C  
ATOM    968  CD  GLU A 152      28.559  -6.954   6.895  1.00 33.48           C  
ATOM    969  OE1 GLU A 152      27.490  -7.454   6.452  1.00 36.06           O  
ATOM    970  OE2 GLU A 152      29.689  -7.420   6.614  1.00 35.99           O  
ATOM    971  N   ASP A 153      25.593  -5.193  11.548  1.00 16.85           N  
ATOM    972  CA  ASP A 153      24.293  -5.386  12.176  1.00 17.49           C  
ATOM    973  C   ASP A 153      23.720  -4.083  12.722  1.00 16.79           C  
ATOM    974  O   ASP A 153      22.731  -4.087  13.447  1.00 16.74           O  
ATOM    975  CB  ASP A 153      24.389  -6.431  13.290  1.00 20.15           C  
ATOM    976  CG  ASP A 153      25.357  -6.032  14.388  1.00 23.04           C  
ATOM    977  OD1 ASP A 153      26.202  -5.147  14.158  1.00 24.38           O  
ATOM    978  OD2 ASP A 153      25.270  -6.613  15.483  1.00 25.07           O  
ATOM    979  N   GLY A 154      24.365  -2.973  12.379  1.00 14.32           N  
ATOM    980  CA  GLY A 154      23.887  -1.672  12.804  1.00 14.14           C  
ATOM    981  C   GLY A 154      24.235  -1.168  14.196  1.00 13.11           C  
ATOM    982  O   GLY A 154      23.731  -0.111  14.596  1.00 15.33           O  
ATOM    983  N   LYS A 155      25.084  -1.868  14.941  1.00 11.69           N  
ATOM    984  CA  LYS A 155      25.424  -1.388  16.276  1.00 11.31           C  
ATOM    985  C   LYS A 155      26.305  -0.143  16.174  1.00 10.19           C  
ATOM    986  O   LYS A 155      27.258  -0.089  15.379  1.00  8.57           O  
ATOM    987  CB  LYS A 155      26.120  -2.478  17.092  1.00 13.79           C  
ATOM    988  CG  LYS A 155      25.238  -3.702  17.341  1.00 19.84           C  
ATOM    989  CD  LYS A 155      25.886  -4.682  18.321  1.00 22.27           C  
ATOM    990  CE  LYS A 155      25.084  -5.986  18.435  1.00 26.27           C  
ATOM    991  NZ  LYS A 155      23.669  -5.746  18.861  1.00 28.21           N  
ATOM    992  N   VAL A 156      25.972   0.858  16.982  1.00  8.41           N  
ATOM    993  CA  VAL A 156      26.683   2.139  16.977  1.00  7.75           C  
ATOM    994  C   VAL A 156      27.665   2.276  18.133  1.00  8.00           C  
ATOM    995  O   VAL A 156      27.279   2.144  19.295  1.00  6.83           O  
ATOM    996  CB  VAL A 156      25.660   3.302  17.068  1.00  7.48           C  
ATOM    997  CG1 VAL A 156      26.384   4.647  17.112  1.00  8.09           C  
ATOM    998  CG2 VAL A 156      24.694   3.239  15.880  1.00  8.01           C  
ATOM    999  N   PRO A 157      28.954   2.545  17.838  1.00  6.92           N  
ATOM   1000  CA  PRO A 157      29.947   2.697  18.919  1.00  7.11           C  
ATOM   1001  C   PRO A 157      29.620   3.934  19.752  1.00  6.44           C  
ATOM   1002  O   PRO A 157      29.190   4.965  19.212  1.00  6.26           O  
ATOM   1003  CB  PRO A 157      31.272   2.904  18.170  1.00  7.88           C  
ATOM   1004  CG  PRO A 157      31.059   2.264  16.866  1.00  7.33           C  
ATOM   1005  CD  PRO A 157      29.606   2.514  16.511  1.00  6.58           C  
ATOM   1006  N   GLN A 158      29.848   3.861  21.054  1.00  5.52           N  
ATOM   1007  CA  GLN A 158      29.575   5.021  21.904  1.00  5.07           C  
ATOM   1008  C   GLN A 158      30.718   5.175  22.883  1.00  5.91           C  
ATOM   1009  O   GLN A 158      31.508   4.243  23.061  1.00  5.41           O  
ATOM   1010  CB  GLN A 158      28.332   4.788  22.763  1.00  7.28           C  
ATOM   1011  CG  GLN A 158      27.020   4.602  22.049  1.00  6.71           C  
ATOM   1012  CD  GLN A 158      25.927   4.335  23.066  1.00 10.83           C  
ATOM   1013  OE1 GLN A 158      25.912   3.282  23.701  1.00 11.99           O  
ATOM   1014  NE2 GLN A 158      25.033   5.301  23.254  1.00  9.55           N  
ATOM   1015  N   HIS A 159      30.774   6.346  23.527  1.00  6.03           N  
ATOM   1016  CA  HIS A 159      31.758   6.606  24.572  1.00  6.61           C  
ATOM   1017  C   HIS A 159      33.222   6.382  24.199  1.00  5.32           C  
ATOM   1018  O   HIS A 159      34.002   5.848  25.000  1.00  5.11           O  
ATOM   1019  CB  HIS A 159      31.417   5.737  25.804  1.00  7.53           C  
ATOM   1020  CG  HIS A 159      30.045   5.981  26.360  1.00  9.25           C  
ATOM   1021  ND1 HIS A 159      29.699   7.156  27.000  1.00  8.81           N  
ATOM   1022  CD2 HIS A 159      28.934   5.206  26.373  1.00 11.23           C  
ATOM   1023  CE1 HIS A 159      28.436   7.092  27.384  1.00 10.73           C  
ATOM   1024  NE2 HIS A 159      27.949   5.920  27.017  1.00 10.83           N  
ATOM   1025  N   CYS A 160      33.605   6.764  22.986  1.00  4.52           N  
ATOM   1026  CA  CYS A 160      34.994   6.618  22.586  1.00  5.13           C  
ATOM   1027  C   CYS A 160      35.701   7.952  22.745  1.00  5.61           C  
ATOM   1028  O   CYS A 160      35.056   8.989  22.946  1.00  6.26           O  
ATOM   1029  CB  CYS A 160      35.088   6.154  21.131  1.00  4.20           C  
ATOM   1030  SG  CYS A 160      34.454   4.496  20.871  1.00  6.06           S  
ATOM   1031  N   ARG A 161      37.029   7.925  22.700  1.00  4.77           N  
ATOM   1032  CA  ARG A 161      37.796   9.155  22.807  1.00  4.39           C  
ATOM   1033  C   ARG A 161      38.947   9.160  21.816  1.00  5.65           C  
ATOM   1034  O   ARG A 161      39.611   8.131  21.629  1.00  4.85           O  
ATOM   1035  CB  ARG A 161      38.347   9.319  24.229  1.00  5.34           C  
ATOM   1036  CG  ARG A 161      39.209  10.557  24.429  1.00  4.70           C  
ATOM   1037  CD  ARG A 161      39.686  10.716  25.897  1.00  7.26           C  
ATOM   1038  NE  ARG A 161      40.424  11.971  26.074  1.00  4.27           N  
ATOM   1039  CZ  ARG A 161      41.296  12.201  27.053  1.00  7.61           C  
ATOM   1040  NH1 ARG A 161      41.541  11.265  27.969  1.00  8.93           N  
ATOM   1041  NH2 ARG A 161      41.970  13.348  27.085  1.00  6.22           N  
ATOM   1042  N   ILE A 162      39.146  10.303  21.152  1.00  4.46           N  
ATOM   1043  CA  ILE A 162      40.257  10.491  20.216  1.00  4.32           C  
ATOM   1044  C   ILE A 162      40.955  11.720  20.802  1.00  4.27           C  
ATOM   1045  O   ILE A 162      40.365  12.804  20.859  1.00  4.59           O  
ATOM   1046  CB  ILE A 162      39.768  10.806  18.789  1.00  3.70           C  
ATOM   1047  CG1 ILE A 162      38.948   9.624  18.253  1.00  5.28           C  
ATOM   1048  CG2 ILE A 162      40.970  11.149  17.897  1.00  4.28           C  
ATOM   1049  CD1 ILE A 162      38.231   9.887  16.913  1.00  6.19           C  
ATOM   1050  N   ASP A 163      42.187  11.558  21.266  1.00  3.56           N  
ATOM   1051  CA  ASP A 163      42.883  12.683  21.891  1.00  4.47           C  
ATOM   1052  C   ASP A 163      44.381  12.726  21.670  1.00  3.98           C  
ATOM   1053  O   ASP A 163      45.025  11.701  21.423  1.00  3.41           O  
ATOM   1054  CB  ASP A 163      42.616  12.690  23.406  1.00  4.17           C  
ATOM   1055  CG  ASP A 163      43.274  11.519  24.124  1.00  5.74           C  
ATOM   1056  OD1 ASP A 163      42.717  10.399  24.092  1.00  5.43           O  
ATOM   1057  OD2 ASP A 163      44.354  11.724  24.712  1.00  5.76           O  
ATOM   1058  N   HIS A 164      44.930  13.934  21.761  1.00  3.68           N  
ATOM   1059  CA  HIS A 164      46.371  14.139  21.602  1.00  2.47           C  
ATOM   1060  C   HIS A 164      46.909  13.481  20.341  1.00  2.16           C  
ATOM   1061  O   HIS A 164      47.999  12.925  20.332  1.00  3.90           O  
ATOM   1062  CB  HIS A 164      47.122  13.646  22.854  1.00  4.55           C  
ATOM   1063  CG  HIS A 164      46.760  14.404  24.099  1.00  4.13           C  
ATOM   1064  ND1 HIS A 164      45.686  14.061  24.892  1.00  4.90           N  
ATOM   1065  CD2 HIS A 164      47.267  15.550  24.625  1.00  5.87           C  
ATOM   1066  CE1 HIS A 164      45.545  14.962  25.852  1.00  4.39           C  
ATOM   1067  NE2 HIS A 164      46.487  15.877  25.710  1.00  3.37           N  
ATOM   1068  N   CYS A 165      46.130  13.575  19.264  1.00  3.85           N  
ATOM   1069  CA  CYS A 165      46.551  13.044  17.965  1.00  3.44           C  
ATOM   1070  C   CYS A 165      46.819  14.215  17.024  1.00  2.21           C  
ATOM   1071  O   CYS A 165      46.196  15.268  17.163  1.00  3.28           O  
ATOM   1072  CB  CYS A 165      45.466  12.162  17.365  1.00  3.32           C  
ATOM   1073  SG  CYS A 165      45.318  10.528  18.172  1.00  4.31           S  
ATOM   1074  N   SER A 166      47.739  14.026  16.075  1.00  1.87           N  
ATOM   1075  CA  SER A 166      48.082  15.065  15.110  1.00  1.82           C  
ATOM   1076  C   SER A 166      47.674  14.567  13.724  1.00  3.19           C  
ATOM   1077  O   SER A 166      48.018  13.445  13.353  1.00  2.70           O  
ATOM   1078  CB  SER A 166      49.597  15.334  15.152  1.00  3.73           C  
ATOM   1079  OG  SER A 166      49.968  16.315  14.183  1.00  3.56           O  
ATOM   1080  N   PHE A 167      46.938  15.400  12.980  1.00  2.71           N  
ATOM   1081  CA  PHE A 167      46.456  15.060  11.637  1.00  1.36           C  
ATOM   1082  C   PHE A 167      46.931  16.139  10.670  1.00  2.98           C  
ATOM   1083  O   PHE A 167      46.381  17.243  10.639  1.00  1.69           O  
ATOM   1084  CB  PHE A 167      44.929  15.026  11.632  1.00  2.04           C  
ATOM   1085  CG  PHE A 167      44.334  14.141  12.692  1.00  4.40           C  
ATOM   1086  CD1 PHE A 167      44.308  12.760  12.533  1.00  3.83           C  
ATOM   1087  CD2 PHE A 167      43.784  14.692  13.844  1.00  5.06           C  
ATOM   1088  CE1 PHE A 167      43.732  11.931  13.518  1.00  2.72           C  
ATOM   1089  CE2 PHE A 167      43.203  13.873  14.836  1.00  3.61           C  
ATOM   1090  CZ  PHE A 167      43.177  12.505  14.671  1.00  4.18           C  
ATOM   1091  N   THR A 168      47.926  15.816   9.860  1.00  2.33           N  
ATOM   1092  CA  THR A 168      48.494  16.808   8.967  1.00  2.31           C  
ATOM   1093  C   THR A 168      48.650  16.355   7.529  1.00  3.18           C  
ATOM   1094  O   THR A 168      48.850  15.176   7.249  1.00  4.11           O  
ATOM   1095  CB  THR A 168      49.885  17.204   9.460  1.00  3.70           C  
ATOM   1096  OG1 THR A 168      50.662  16.004   9.650  1.00  5.14           O  
ATOM   1097  CG2 THR A 168      49.788  17.968  10.799  1.00  2.91           C  
ATOM   1098  N   ASP A 169      48.564  17.334   6.631  1.00  3.34           N  
ATOM   1099  CA  ASP A 169      48.761  17.117   5.207  1.00  4.25           C  
ATOM   1100  C   ASP A 169      47.920  16.013   4.584  1.00  3.42           C  
ATOM   1101  O   ASP A 169      48.419  15.261   3.741  1.00  2.20           O  
ATOM   1102  CB  ASP A 169      50.256  16.835   4.940  1.00  3.31           C  
ATOM   1103  CG  ASP A 169      51.138  18.073   5.145  1.00  4.59           C  
ATOM   1104  OD1 ASP A 169      50.605  19.123   5.558  1.00  5.08           O  
ATOM   1105  OD2 ASP A 169      52.366  18.000   4.891  1.00  7.43           O  
ATOM   1106  N   LYS A 170      46.651  15.918   4.977  1.00  3.08           N  
ATOM   1107  CA  LYS A 170      45.766  14.900   4.409  1.00  3.92           C  
ATOM   1108  C   LYS A 170      45.488  15.333   2.962  1.00  4.97           C  
ATOM   1109  O   LYS A 170      44.975  16.427   2.729  1.00  4.63           O  
ATOM   1110  CB  LYS A 170      44.462  14.821   5.215  1.00  3.24           C  
ATOM   1111  CG  LYS A 170      43.480  13.756   4.695  1.00  1.49           C  
ATOM   1112  CD  LYS A 170      42.416  13.442   5.719  1.00  3.56           C  
ATOM   1113  CE  LYS A 170      41.582  12.229   5.317  1.00  1.93           C  
ATOM   1114  NZ  LYS A 170      40.680  12.441   4.122  1.00  2.46           N  
ATOM   1115  N   ILE A 171      45.830  14.470   1.996  1.00  4.92           N  
ATOM   1116  CA  ILE A 171      45.672  14.811   0.579  1.00  3.68           C  
ATOM   1117  C   ILE A 171      44.583  13.999  -0.089  1.00  3.46           C  
ATOM   1118  O   ILE A 171      44.527  13.895  -1.317  1.00  5.23           O  
ATOM   1119  CB  ILE A 171      46.989  14.594  -0.204  1.00  4.20           C  
ATOM   1120  CG1 ILE A 171      47.494  13.163  -0.008  1.00  5.33           C  
ATOM   1121  CG2 ILE A 171      48.053  15.593   0.263  1.00  2.61           C  
ATOM   1122  CD1 ILE A 171      48.691  12.807  -0.932  1.00  5.96           C  
ATOM   1123  N   THR A 172      43.707  13.443   0.733  1.00  3.21           N  
ATOM   1124  CA  THR A 172      42.615  12.610   0.251  1.00  1.37           C  
ATOM   1125  C   THR A 172      41.252  13.145   0.650  1.00  3.03           C  
ATOM   1126  O   THR A 172      41.125  13.901   1.610  1.00  4.56           O  
ATOM   1127  CB  THR A 172      42.727  11.216   0.856  1.00  0.92           C  
ATOM   1128  OG1 THR A 172      42.984  11.346   2.261  1.00  3.74           O  
ATOM   1129  CG2 THR A 172      43.869  10.431   0.200  1.00  2.77           C  
ATOM   1130  N   PHE A 173      40.233  12.701  -0.072  1.00  3.47           N  
ATOM   1131  CA  PHE A 173      38.868  13.129   0.201  1.00  4.12           C  
ATOM   1132  C   PHE A 173      38.332  12.498   1.480  1.00  4.11           C  
ATOM   1133  O   PHE A 173      38.907  11.535   2.013  1.00  4.47           O  
ATOM   1134  CB  PHE A 173      37.980  12.812  -1.012  1.00  4.53           C  
ATOM   1135  CG  PHE A 173      38.315  13.651  -2.225  1.00  6.18           C  
ATOM   1136  CD1 PHE A 173      37.715  14.896  -2.403  1.00  8.18           C  
ATOM   1137  CD2 PHE A 173      39.266  13.224  -3.154  1.00  8.96           C  
ATOM   1138  CE1 PHE A 173      38.056  15.710  -3.498  1.00  9.51           C  
ATOM   1139  CE2 PHE A 173      39.612  14.032  -4.251  1.00  9.11           C  
ATOM   1140  CZ  PHE A 173      39.003  15.271  -4.418  1.00  8.50           C  
ATOM   1141  N   ASP A 174      37.245  13.101   1.970  1.00  3.11           N  
ATOM   1142  CA  ASP A 174      36.545  12.745   3.205  1.00  3.00           C  
ATOM   1143  C   ASP A 174      37.186  13.526   4.347  1.00  2.37           C  
ATOM   1144  O   ASP A 174      38.287  14.085   4.212  1.00  3.53           O  
ATOM   1145  CB  ASP A 174      36.583  11.237   3.517  1.00  2.04           C  
ATOM   1146  CG  ASP A 174      35.373  10.792   4.366  1.00  3.34           C  
ATOM   1147  OD1 ASP A 174      34.583  11.673   4.800  1.00  4.02           O  
ATOM   1148  OD2 ASP A 174      35.182   9.574   4.603  1.00  3.88           O  
ATOM   1149  N   GLN A 175      36.463  13.590   5.456  1.00  2.27           N  
ATOM   1150  CA  GLN A 175      36.910  14.273   6.660  1.00  1.55           C  
ATOM   1151  C   GLN A 175      38.143  13.601   7.248  1.00  3.90           C  
ATOM   1152  O   GLN A 175      38.511  12.481   6.866  1.00  4.46           O  
ATOM   1153  CB  GLN A 175      35.816  14.205   7.751  1.00  1.18           C  
ATOM   1154  CG  GLN A 175      34.806  15.340   7.738  1.00  3.54           C  
ATOM   1155  CD  GLN A 175      33.787  15.244   6.598  1.00  4.20           C  
ATOM   1156  OE1 GLN A 175      33.521  16.232   5.933  1.00  5.94           O  
ATOM   1157  NE2 GLN A 175      33.198  14.065   6.398  1.00  3.01           N  
ATOM   1158  N   VAL A 176      38.791  14.304   8.171  1.00  3.33           N  
ATOM   1159  CA  VAL A 176      39.903  13.720   8.895  1.00  2.80           C  
ATOM   1160  C   VAL A 176      39.302  12.666   9.844  1.00  2.43           C  
ATOM   1161  O   VAL A 176      39.820  11.536   9.974  1.00  1.59           O  
ATOM   1162  CB  VAL A 176      40.638  14.792   9.704  1.00  2.00           C  
ATOM   1163  CG1 VAL A 176      41.690  14.133  10.610  1.00  3.10           C  
ATOM   1164  CG2 VAL A 176      41.307  15.783   8.732  1.00  1.76           C  
ATOM   1165  N   ILE A 177      38.206  13.040  10.506  1.00  2.27           N  
ATOM   1166  CA  ILE A 177      37.496  12.165  11.455  1.00  2.65           C  
ATOM   1167  C   ILE A 177      35.979  12.188  11.172  1.00  2.07           C  
ATOM   1168  O   ILE A 177      35.399  13.272  10.997  1.00  3.63           O  
ATOM   1169  CB  ILE A 177      37.643  12.670  12.953  1.00  2.54           C  
ATOM   1170  CG1 ILE A 177      39.113  12.707  13.379  1.00  2.64           C  
ATOM   1171  CG2 ILE A 177      36.802  11.805  13.901  1.00  3.05           C  
ATOM   1172  CD1 ILE A 177      39.293  13.230  14.824  1.00  4.16           C  
ATOM   1173  N   ASN A 178      35.352  11.011  11.108  1.00  1.84           N  
ATOM   1174  CA  ASN A 178      33.892  10.931  10.984  1.00  2.85           C  
ATOM   1175  C   ASN A 178      33.428  10.170  12.225  1.00  2.01           C  
ATOM   1176  O   ASN A 178      34.001   9.130  12.539  1.00  3.25           O  
ATOM   1177  CB  ASN A 178      33.434  10.104   9.774  1.00  3.50           C  
ATOM   1178  CG  ASN A 178      33.755  10.776   8.445  1.00  2.36           C  
ATOM   1179  OD1 ASN A 178      33.617  11.987   8.307  1.00  3.96           O  
ATOM   1180  ND2 ASN A 178      34.162   9.981   7.462  1.00  3.54           N  
ATOM   1181  N   LEU A 179      32.424  10.695  12.927  1.00  2.05           N  
ATOM   1182  CA  LEU A 179      31.829  10.035  14.097  1.00  3.33           C  
ATOM   1183  C   LEU A 179      30.417   9.670  13.611  1.00  2.92           C  
ATOM   1184  O   LEU A 179      29.545  10.538  13.488  1.00  2.84           O  
ATOM   1185  CB  LEU A 179      31.771  10.992  15.295  1.00  1.92           C  
ATOM   1186  CG  LEU A 179      33.166  11.490  15.734  1.00  1.70           C  
ATOM   1187  CD1 LEU A 179      33.006  12.373  16.987  1.00  2.03           C  
ATOM   1188  CD2 LEU A 179      34.086  10.309  16.034  1.00  2.94           C  
ATOM   1189  N   ASN A 180      30.206   8.383  13.331  1.00  2.18           N  
ATOM   1190  CA  ASN A 180      28.951   7.904  12.759  1.00  3.15           C  
ATOM   1191  C   ASN A 180      27.949   7.234  13.680  1.00  4.13           C  
ATOM   1192  O   ASN A 180      28.317   6.389  14.500  1.00  3.21           O  
ATOM   1193  CB  ASN A 180      29.243   6.889  11.641  1.00  1.88           C  
ATOM   1194  CG  ASN A 180      30.014   7.483  10.479  1.00  1.77           C  
ATOM   1195  OD1 ASN A 180      29.525   8.379   9.791  1.00  4.00           O  
ATOM   1196  ND2 ASN A 180      31.214   6.962  10.240  1.00  1.51           N  
ATOM   1197  N   ASN A 181      26.680   7.622  13.541  1.00  5.47           N  
ATOM   1198  CA  ASN A 181      25.624   6.945  14.284  1.00  5.58           C  
ATOM   1199  C   ASN A 181      24.510   6.415  13.373  1.00  6.27           C  
ATOM   1200  O   ASN A 181      23.496   5.888  13.844  1.00  5.16           O  
ATOM   1201  CB  ASN A 181      25.090   7.791  15.452  1.00  3.71           C  
ATOM   1202  CG  ASN A 181      24.431   9.090  15.032  1.00  6.44           C  
ATOM   1203  OD1 ASN A 181      24.420   9.487  13.868  1.00  6.34           O  
ATOM   1204  ND2 ASN A 181      23.868   9.768  16.018  1.00  5.74           N  
ATOM   1205  N   THR A 182      24.720   6.542  12.065  1.00  7.81           N  
ATOM   1206  CA  THR A 182      23.811   6.000  11.062  1.00 10.71           C  
ATOM   1207  C   THR A 182      24.621   5.661   9.803  1.00 13.44           C  
ATOM   1208  O   THR A 182      25.713   6.209   9.568  1.00 11.00           O  
ATOM   1209  CB  THR A 182      22.688   6.973  10.621  1.00 13.02           C  
ATOM   1210  OG1 THR A 182      23.265   8.050   9.881  1.00 14.22           O  
ATOM   1211  CG2 THR A 182      21.916   7.506  11.815  1.00 11.87           C  
ATOM   1212  N   ALA A 183      24.095   4.730   9.016  1.00 14.56           N  
ATOM   1213  CA  ALA A 183      24.737   4.359   7.760  1.00 16.48           C  
ATOM   1214  C   ALA A 183      24.324   5.459   6.780  1.00 18.21           C  
ATOM   1215  O   ALA A 183      23.223   6.023   6.888  1.00 18.01           O  
ATOM   1216  CB  ALA A 183      24.223   3.004   7.289  1.00 17.55           C  
ATOM   1217  N   ARG A 184      25.196   5.784   5.832  1.00 17.80           N  
ATOM   1218  CA  ARG A 184      24.863   6.837   4.872  1.00 20.03           C  
ATOM   1219  C   ARG A 184      23.643   6.434   4.046  1.00 21.62           C  
ATOM   1220  O   ARG A 184      23.557   5.302   3.589  1.00 19.94           O  
ATOM   1221  CB  ARG A 184      26.043   7.094   3.937  1.00 19.32           C  
ATOM   1222  CG  ARG A 184      25.903   8.359   3.130  1.00 20.19           C  
ATOM   1223  CD  ARG A 184      26.993   8.461   2.080  1.00 21.45           C  
ATOM   1224  NE  ARG A 184      26.908   9.736   1.378  1.00 23.36           N  
ATOM   1225  CZ  ARG A 184      27.444   9.966   0.185  1.00 24.71           C  
ATOM   1226  NH1 ARG A 184      28.104   9.002  -0.441  1.00 24.87           N  
ATOM   1227  NH2 ARG A 184      27.317  11.162  -0.379  1.00 27.02           N  
ATOM   1228  N   ALA A 185      22.709   7.360   3.858  1.00 23.60           N  
ATOM   1229  CA  ALA A 185      21.503   7.086   3.079  1.00 27.94           C  
ATOM   1230  C   ALA A 185      20.927   8.409   2.600  1.00 32.13           C  
ATOM   1231  O   ALA A 185      21.146   9.443   3.226  1.00 31.78           O  
ATOM   1232  CB  ALA A 185      20.478   6.358   3.935  1.00 27.87           C  
ATOM   1233  N   ILE A 186      20.192   8.388   1.489  1.00 36.28           N  
ATOM   1234  CA  ILE A 186      19.588   9.619   0.971  1.00 41.33           C  
ATOM   1235  C   ILE A 186      18.584  10.185   2.001  1.00 43.96           C  
ATOM   1236  O   ILE A 186      18.067  11.294   1.868  1.00 45.33           O  
ATOM   1237  CB  ILE A 186      18.981   9.360  -0.445  1.00 41.00           C  
ATOM   1238  CG1 ILE A 186      19.946   9.944  -1.487  1.00 41.21           C  
ATOM   1239  CG2 ILE A 186      17.573   9.922  -0.561  1.00 41.80           C  
ATOM   1240  CD1 ILE A 186      19.583   9.689  -2.923  1.00 41.79           C  
ATOM   1241  N   LYS A 187      18.352   9.380   3.034  1.00 47.28           N  
ATOM   1242  CA  LYS A 187      17.532   9.674   4.211  1.00 50.38           C  
ATOM   1243  C   LYS A 187      16.270  10.538   4.181  1.00 51.86           C  
ATOM   1244  O   LYS A 187      15.636  10.727   3.135  1.00 52.20           O  
ATOM   1245  CB  LYS A 187      18.457  10.235   5.290  1.00 51.61           C  
ATOM   1246  CG  LYS A 187      18.160   9.766   6.702  1.00 52.77           C  
ATOM   1247  CD  LYS A 187      17.995   8.256   6.715  1.00 54.31           C  
ATOM   1248  CE  LYS A 187      18.005   7.703   8.123  1.00 54.87           C  
ATOM   1249  NZ  LYS A 187      17.577   6.272   8.116  1.00 56.64           N  
ATOM   1250  N   ASP A 188      15.928  11.020   5.382  1.00 53.11           N  
ATOM   1251  CA  ASP A 188      14.800  11.896   5.703  1.00 53.89           C  
ATOM   1252  C   ASP A 188      13.575  11.253   6.389  1.00 53.26           C  
ATOM   1253  O   ASP A 188      12.440  11.703   6.224  1.00 53.71           O  
ATOM   1254  CB  ASP A 188      14.408  12.754   4.482  1.00 55.73           C  
ATOM   1255  CG  ASP A 188      13.236  12.184   3.677  1.00 57.93           C  
ATOM   1256  OD1 ASP A 188      13.042  10.947   3.642  1.00 59.21           O  
ATOM   1257  OD2 ASP A 188      12.530  12.993   3.045  1.00 58.90           O  
ATOM   1258  N   GLY A 189      13.816  10.201   7.170  1.00 52.60           N  
ATOM   1259  CA  GLY A 189      12.741   9.570   7.925  1.00 50.79           C  
ATOM   1260  C   GLY A 189      12.932  10.075   9.346  1.00 49.61           C  
ATOM   1261  O   GLY A 189      14.076  10.147   9.796  1.00 50.26           O  
ATOM   1262  N   SER A 190      11.851  10.433  10.046  1.00 47.38           N  
ATOM   1263  CA  SER A 190      11.957  10.976  11.411  1.00 45.36           C  
ATOM   1264  C   SER A 190      12.909  10.211  12.356  1.00 43.34           C  
ATOM   1265  O   SER A 190      13.311  10.736  13.404  1.00 43.99           O  
ATOM   1266  CB  SER A 190      10.577  11.100  12.083  1.00 45.52           C  
ATOM   1267  OG  SER A 190      10.157   9.889  12.694  1.00 44.55           O  
ATOM   1268  N   VAL A 191      13.286   8.994  11.976  1.00 40.55           N  
ATOM   1269  CA  VAL A 191      14.197   8.188  12.779  1.00 36.53           C  
ATOM   1270  C   VAL A 191      15.620   8.732  12.653  1.00 32.03           C  
ATOM   1271  O   VAL A 191      16.084   8.997  11.542  1.00 34.58           O  
ATOM   1272  CB  VAL A 191      14.229   6.730  12.296  1.00 38.16           C  
ATOM   1273  CG1 VAL A 191      12.849   6.113  12.404  1.00 39.56           C  
ATOM   1274  CG2 VAL A 191      14.732   6.656  10.855  1.00 39.10           C  
ATOM   1275  N   GLY A 192      16.308   8.902  13.777  1.00 25.19           N  
ATOM   1276  CA  GLY A 192      17.671   9.411  13.731  1.00 18.15           C  
ATOM   1277  C   GLY A 192      18.622   8.502  14.482  1.00 13.35           C  
ATOM   1278  O   GLY A 192      18.189   7.633  15.237  1.00 11.68           O  
ATOM   1279  N   GLY A 193      19.923   8.697  14.303  1.00 10.21           N  
ATOM   1280  CA  GLY A 193      20.884   7.856  15.005  1.00  8.18           C  
ATOM   1281  C   GLY A 193      20.929   8.174  16.489  1.00  8.36           C  
ATOM   1282  O   GLY A 193      20.591   9.288  16.919  1.00  8.25           O  
ATOM   1283  N   PRO A 194      21.345   7.204  17.312  1.00  5.95           N  
ATOM   1284  CA  PRO A 194      21.434   7.377  18.761  1.00  7.86           C  
ATOM   1285  C   PRO A 194      22.609   8.229  19.226  1.00  7.45           C  
ATOM   1286  O   PRO A 194      23.636   8.310  18.544  1.00  5.39           O  
ATOM   1287  CB  PRO A 194      21.554   5.946  19.257  1.00  7.85           C  
ATOM   1288  CG  PRO A 194      22.398   5.309  18.189  1.00  8.57           C  
ATOM   1289  CD  PRO A 194      21.790   5.853  16.910  1.00  7.01           C  
ATOM   1290  N   ALA A 195      22.469   8.827  20.406  1.00  7.48           N  
ATOM   1291  CA  ALA A 195      23.534   9.631  20.996  1.00  5.26           C  
ATOM   1292  C   ALA A 195      24.840   8.804  21.069  1.00  7.78           C  
ATOM   1293  O   ALA A 195      24.831   7.623  21.432  1.00  7.25           O  
ATOM   1294  CB  ALA A 195      23.123  10.099  22.406  1.00  6.94           C  
ATOM   1295  N   MET A 196      25.965   9.442  20.760  1.00  5.51           N  
ATOM   1296  CA  MET A 196      27.256   8.755  20.754  1.00  5.94           C  
ATOM   1297  C   MET A 196      28.138   8.952  21.982  1.00  5.96           C  
ATOM   1298  O   MET A 196      28.850   8.033  22.389  1.00  5.12           O  
ATOM   1299  CB  MET A 196      28.033   9.166  19.498  1.00  5.14           C  
ATOM   1300  CG  MET A 196      27.417   8.622  18.218  1.00  4.84           C  
ATOM   1301  SD  MET A 196      28.246   9.215  16.717  1.00  6.01           S  
ATOM   1302  CE  MET A 196      27.493  10.830  16.609  1.00  5.44           C  
ATOM   1303  N   TYR A 197      28.114  10.151  22.554  1.00  5.71           N  
ATOM   1304  CA  TYR A 197      28.922  10.452  23.746  1.00  5.79           C  
ATOM   1305  C   TYR A 197      30.425  10.267  23.563  1.00  5.96           C  
ATOM   1306  O   TYR A 197      31.106   9.798  24.487  1.00  5.40           O  
ATOM   1307  CB  TYR A 197      28.491   9.592  24.940  1.00  6.20           C  
ATOM   1308  CG  TYR A 197      27.014   9.677  25.243  1.00  6.14           C  
ATOM   1309  CD1 TYR A 197      26.466  10.824  25.827  1.00  8.07           C  
ATOM   1310  CD2 TYR A 197      26.168   8.619  24.933  1.00  7.64           C  
ATOM   1311  CE1 TYR A 197      25.085  10.904  26.087  1.00  8.36           C  
ATOM   1312  CE2 TYR A 197      24.804   8.678  25.188  1.00  8.97           C  
ATOM   1313  CZ  TYR A 197      24.267   9.824  25.761  1.00  8.38           C  
ATOM   1314  OH  TYR A 197      22.906   9.893  25.978  1.00 12.64           O  
ATOM   1315  N   HIS A 198      30.948  10.630  22.396  1.00  4.72           N  
ATOM   1316  CA  HIS A 198      32.395  10.538  22.171  1.00  4.26           C  
ATOM   1317  C   HIS A 198      33.016  11.864  22.582  1.00  5.33           C  
ATOM   1318  O   HIS A 198      32.322  12.844  22.832  1.00  5.22           O  
ATOM   1319  CB  HIS A 198      32.745  10.338  20.675  1.00  5.16           C  
ATOM   1320  CG  HIS A 198      32.148   9.120  20.056  1.00  5.62           C  
ATOM   1321  ND1 HIS A 198      32.212   7.877  20.644  1.00  4.60           N  
ATOM   1322  CD2 HIS A 198      31.467   8.958  18.896  1.00  5.05           C  
ATOM   1323  CE1 HIS A 198      31.586   7.001  19.880  1.00  4.96           C  
ATOM   1324  NE2 HIS A 198      31.125   7.631  18.812  1.00  6.05           N  
ATOM   1325  N   ARG A 199      34.341  11.888  22.661  1.00  4.48           N  
ATOM   1326  CA  ARG A 199      35.064  13.124  22.936  1.00  4.15           C  
ATOM   1327  C   ARG A 199      36.254  13.176  21.993  1.00  2.99           C  
ATOM   1328  O   ARG A 199      36.943  12.166  21.789  1.00  3.81           O  
ATOM   1329  CB  ARG A 199      35.595  13.180  24.373  1.00  3.51           C  
ATOM   1330  CG  ARG A 199      36.417  14.449  24.686  1.00  2.37           C  
ATOM   1331  CD  ARG A 199      36.904  14.465  26.166  1.00  3.13           C  
ATOM   1332  NE  ARG A 199      37.613  15.710  26.477  1.00  4.97           N  
ATOM   1333  CZ  ARG A 199      38.544  15.847  27.416  1.00  5.21           C  
ATOM   1334  NH1 ARG A 199      38.908  14.802  28.163  1.00  6.96           N  
ATOM   1335  NH2 ARG A 199      39.113  17.032  27.614  1.00  5.43           N  
ATOM   1336  N   VAL A 200      36.467  14.338  21.383  1.00  3.18           N  
ATOM   1337  CA  VAL A 200      37.645  14.540  20.538  1.00  2.74           C  
ATOM   1338  C   VAL A 200      38.296  15.747  21.216  1.00  2.95           C  
ATOM   1339  O   VAL A 200      37.711  16.843  21.254  1.00  4.01           O  
ATOM   1340  CB  VAL A 200      37.289  14.919  19.083  1.00  2.76           C  
ATOM   1341  CG1 VAL A 200      38.607  15.192  18.296  1.00  3.76           C  
ATOM   1342  CG2 VAL A 200      36.497  13.773  18.418  1.00  2.38           C  
ATOM   1343  N   ASP A 201      39.490  15.548  21.766  1.00  1.93           N  
ATOM   1344  CA  ASP A 201      40.163  16.624  22.473  1.00  2.71           C  
ATOM   1345  C   ASP A 201      41.669  16.612  22.259  1.00  3.73           C  
ATOM   1346  O   ASP A 201      42.276  15.566  21.980  1.00  3.38           O  
ATOM   1347  CB  ASP A 201      39.861  16.542  23.989  1.00  2.82           C  
ATOM   1348  CG  ASP A 201      40.472  15.316  24.641  1.00  3.08           C  
ATOM   1349  OD1 ASP A 201      39.865  14.234  24.525  1.00  4.81           O  
ATOM   1350  OD2 ASP A 201      41.559  15.423  25.255  1.00  4.63           O  
ATOM   1351  N   HIS A 202      42.263  17.795  22.391  1.00  3.46           N  
ATOM   1352  CA  HIS A 202      43.687  17.974  22.248  1.00  2.56           C  
ATOM   1353  C   HIS A 202      44.268  17.409  20.974  1.00  3.12           C  
ATOM   1354  O   HIS A 202      45.349  16.834  20.979  1.00  3.92           O  
ATOM   1355  CB  HIS A 202      44.406  17.411  23.489  1.00  2.74           C  
ATOM   1356  CG  HIS A 202      43.982  18.089  24.752  1.00  3.49           C  
ATOM   1357  ND1 HIS A 202      42.937  17.637  25.532  1.00  3.22           N  
ATOM   1358  CD2 HIS A 202      44.392  19.257  25.308  1.00  4.18           C  
ATOM   1359  CE1 HIS A 202      42.721  18.503  26.510  1.00  4.11           C  
ATOM   1360  NE2 HIS A 202      43.587  19.494  26.397  1.00  4.55           N  
ATOM   1361  N   CYS A 203      43.531  17.576  19.881  1.00  3.18           N  
ATOM   1362  CA  CYS A 203      44.026  17.123  18.597  1.00  3.41           C  
ATOM   1363  C   CYS A 203      44.461  18.334  17.765  1.00  2.94           C  
ATOM   1364  O   CYS A 203      44.002  19.458  17.990  1.00  5.40           O  
ATOM   1365  CB  CYS A 203      42.958  16.310  17.858  1.00  3.40           C  
ATOM   1366  SG  CYS A 203      42.738  14.667  18.575  1.00  4.15           S  
ATOM   1367  N   PHE A 204      45.375  18.093  16.824  1.00  2.72           N  
ATOM   1368  CA  PHE A 204      45.914  19.146  15.951  1.00  1.69           C  
ATOM   1369  C   PHE A 204      45.492  18.831  14.536  1.00  3.00           C  
ATOM   1370  O   PHE A 204      45.675  17.698  14.077  1.00  3.13           O  
ATOM   1371  CB  PHE A 204      47.444  19.134  16.010  1.00  3.38           C  
ATOM   1372  CG  PHE A 204      48.084  20.191  15.168  1.00  2.98           C  
ATOM   1373  CD1 PHE A 204      47.932  21.531  15.495  1.00  2.58           C  
ATOM   1374  CD2 PHE A 204      48.801  19.847  14.029  1.00  3.93           C  
ATOM   1375  CE1 PHE A 204      48.490  22.527  14.690  1.00  2.33           C  
ATOM   1376  CE2 PHE A 204      49.363  20.836  13.218  1.00  4.64           C  
ATOM   1377  CZ  PHE A 204      49.201  22.174  13.555  1.00  3.78           C  
ATOM   1378  N   PHE A 205      44.938  19.824  13.846  1.00  1.98           N  
ATOM   1379  CA  PHE A 205      44.496  19.634  12.466  1.00  3.55           C  
ATOM   1380  C   PHE A 205      45.052  20.712  11.545  1.00  3.62           C  
ATOM   1381  O   PHE A 205      44.796  21.893  11.767  1.00  4.83           O  
ATOM   1382  CB  PHE A 205      42.967  19.720  12.354  1.00  1.64           C  
ATOM   1383  CG  PHE A 205      42.215  18.728  13.198  1.00  2.88           C  
ATOM   1384  CD1 PHE A 205      42.044  18.944  14.570  1.00  3.41           C  
ATOM   1385  CD2 PHE A 205      41.664  17.583  12.616  1.00  3.25           C  
ATOM   1386  CE1 PHE A 205      41.331  18.035  15.351  1.00  5.73           C  
ATOM   1387  CE2 PHE A 205      40.948  16.664  13.393  1.00  4.65           C  
ATOM   1388  CZ  PHE A 205      40.783  16.894  14.761  1.00  4.35           C  
ATOM   1389  N   SER A 206      45.787  20.319  10.504  1.00  3.57           N  
ATOM   1390  CA  SER A 206      46.303  21.287   9.524  1.00  1.62           C  
ATOM   1391  C   SER A 206      46.378  20.521   8.221  1.00  1.84           C  
ATOM   1392  O   SER A 206      47.240  19.668   8.069  1.00  2.23           O  
ATOM   1393  CB  SER A 206      47.701  21.783   9.884  1.00  1.01           C  
ATOM   1394  OG  SER A 206      48.040  22.761   8.915  1.00  3.13           O  
ATOM   1395  N   ASN A 207      45.502  20.855   7.276  1.00  2.96           N  
ATOM   1396  CA  ASN A 207      45.403  20.105   6.019  1.00  2.60           C  
ATOM   1397  C   ASN A 207      45.072  21.027   4.849  1.00  3.03           C  
ATOM   1398  O   ASN A 207      44.303  21.987   4.998  1.00  3.91           O  
ATOM   1399  CB  ASN A 207      44.331  19.023   6.217  1.00  1.85           C  
ATOM   1400  CG  ASN A 207      44.703  18.043   7.320  1.00  4.21           C  
ATOM   1401  OD1 ASN A 207      45.543  17.166   7.114  1.00  3.53           O  
ATOM   1402  ND2 ASN A 207      44.094  18.195   8.504  1.00  1.94           N  
ATOM   1403  N   PRO A 208      45.598  20.712   3.660  1.00  2.67           N  
ATOM   1404  CA  PRO A 208      45.397  21.521   2.454  1.00  4.15           C  
ATOM   1405  C   PRO A 208      44.011  21.556   1.820  1.00  4.93           C  
ATOM   1406  O   PRO A 208      43.217  20.638   1.953  1.00  3.06           O  
ATOM   1407  CB  PRO A 208      46.489  20.994   1.516  1.00  3.61           C  
ATOM   1408  CG  PRO A 208      46.469  19.511   1.821  1.00  2.67           C  
ATOM   1409  CD  PRO A 208      46.409  19.510   3.361  1.00  2.08           C  
ATOM   1410  N   GLN A 209      43.742  22.629   1.091  1.00  5.16           N  
ATOM   1411  CA  GLN A 209      42.437  22.802   0.458  1.00  7.24           C  
ATOM   1412  C   GLN A 209      42.187  21.918  -0.758  1.00  5.66           C  
ATOM   1413  O   GLN A 209      42.981  21.905  -1.716  1.00  5.61           O  
ATOM   1414  CB  GLN A 209      42.277  24.267   0.055  1.00  7.65           C  
ATOM   1415  CG  GLN A 209      40.888  24.644  -0.421  1.00 10.41           C  
ATOM   1416  CD  GLN A 209      40.816  26.141  -0.685  1.00 14.70           C  
ATOM   1417  OE1 GLN A 209      40.042  26.861  -0.057  1.00 15.55           O  
ATOM   1418  NE2 GLN A 209      41.646  26.613  -1.610  1.00 13.56           N  
ATOM   1419  N   LYS A 210      41.086  21.171  -0.698  1.00  5.09           N  
ATOM   1420  CA  LYS A 210      40.638  20.297  -1.771  1.00  5.66           C  
ATOM   1421  C   LYS A 210      39.515  21.030  -2.502  1.00  7.23           C  
ATOM   1422  O   LYS A 210      38.967  22.019  -1.990  1.00  7.66           O  
ATOM   1423  CB  LYS A 210      40.078  18.974  -1.204  1.00  3.52           C  
ATOM   1424  CG  LYS A 210      41.137  18.052  -0.614  1.00  3.49           C  
ATOM   1425  CD  LYS A 210      40.509  16.857   0.155  1.00  3.03           C  
ATOM   1426  CE  LYS A 210      40.040  17.318   1.551  1.00  1.17           C  
ATOM   1427  NZ  LYS A 210      39.410  16.161   2.293  1.00  2.96           N  
ATOM   1428  N   PRO A 211      39.153  20.557  -3.701  1.00  7.35           N  
ATOM   1429  CA  PRO A 211      38.075  21.221  -4.438  1.00  9.21           C  
ATOM   1430  C   PRO A 211      36.674  20.733  -4.038  1.00  9.97           C  
ATOM   1431  O   PRO A 211      36.476  19.562  -3.712  1.00  7.79           O  
ATOM   1432  CB  PRO A 211      38.413  20.892  -5.888  1.00 11.32           C  
ATOM   1433  CG  PRO A 211      38.972  19.500  -5.789  1.00  9.28           C  
ATOM   1434  CD  PRO A 211      39.865  19.584  -4.552  1.00  8.75           C  
ATOM   1435  N   GLY A 212      35.705  21.643  -4.056  1.00 10.17           N  
ATOM   1436  CA  GLY A 212      34.326  21.273  -3.766  1.00 13.21           C  
ATOM   1437  C   GLY A 212      33.969  20.719  -2.405  1.00 12.48           C  
ATOM   1438  O   GLY A 212      34.571  21.073  -1.403  1.00 14.17           O  
ATOM   1439  N   ASN A 213      32.962  19.854  -2.373  1.00 14.15           N  
ATOM   1440  CA  ASN A 213      32.504  19.249  -1.118  1.00 14.39           C  
ATOM   1441  C   ASN A 213      33.420  18.054  -0.860  1.00 12.40           C  
ATOM   1442  O   ASN A 213      33.029  16.891  -0.976  1.00 14.58           O  
ATOM   1443  CB  ASN A 213      31.046  18.811  -1.271  1.00 19.62           C  
ATOM   1444  CG  ASN A 213      30.442  18.349   0.030  1.00 23.92           C  
ATOM   1445  OD1 ASN A 213      30.740  17.258   0.511  1.00 28.85           O  
ATOM   1446  ND2 ASN A 213      29.585  19.181   0.614  1.00 29.12           N  
ATOM   1447  N   ALA A 214      34.645  18.373  -0.466  1.00  7.29           N  
ATOM   1448  CA  ALA A 214      35.690  17.381  -0.312  1.00  6.04           C  
ATOM   1449  C   ALA A 214      35.929  16.664   0.999  1.00  5.09           C  
ATOM   1450  O   ALA A 214      36.789  15.783   1.039  1.00  5.18           O  
ATOM   1451  CB  ALA A 214      37.000  18.021  -0.761  1.00  3.68           C  
ATOM   1452  N   GLY A 215      35.201  17.019   2.054  1.00  3.71           N  
ATOM   1453  CA  GLY A 215      35.436  16.390   3.349  1.00  4.01           C  
ATOM   1454  C   GLY A 215      36.332  17.324   4.140  1.00  4.14           C  
ATOM   1455  O   GLY A 215      37.416  17.679   3.666  1.00  5.73           O  
ATOM   1456  N   GLY A 216      35.896  17.716   5.342  1.00  3.99           N  
ATOM   1457  CA  GLY A 216      36.668  18.646   6.144  1.00  4.91           C  
ATOM   1458  C   GLY A 216      37.474  18.079   7.298  1.00  3.81           C  
ATOM   1459  O   GLY A 216      38.215  17.099   7.138  1.00  4.41           O  
ATOM   1460  N   GLY A 217      37.374  18.724   8.456  1.00  3.39           N  
ATOM   1461  CA  GLY A 217      38.088  18.253   9.630  1.00  3.12           C  
ATOM   1462  C   GLY A 217      37.324  17.132  10.327  1.00  2.65           C  
ATOM   1463  O   GLY A 217      37.778  15.983  10.361  1.00  4.47           O  
ATOM   1464  N   ILE A 218      36.167  17.461  10.888  1.00  3.12           N  
ATOM   1465  CA  ILE A 218      35.364  16.468  11.590  1.00  2.27           C  
ATOM   1466  C   ILE A 218      33.896  16.516  11.163  1.00  2.11           C  
ATOM   1467  O   ILE A 218      33.343  17.594  10.984  1.00  3.05           O  
ATOM   1468  CB  ILE A 218      35.362  16.748  13.132  1.00  1.52           C  
ATOM   1469  CG1 ILE A 218      36.799  16.834  13.665  1.00  1.81           C  
ATOM   1470  CG2 ILE A 218      34.585  15.660  13.849  1.00  4.21           C  
ATOM   1471  CD1 ILE A 218      36.885  17.332  15.129  1.00  4.04           C  
ATOM   1472  N   ARG A 219      33.271  15.348  10.997  1.00  3.07           N  
ATOM   1473  CA  ARG A 219      31.829  15.306  10.722  1.00  1.83           C  
ATOM   1474  C   ARG A 219      31.251  14.489  11.890  1.00  2.14           C  
ATOM   1475  O   ARG A 219      31.841  13.481  12.302  1.00  2.52           O  
ATOM   1476  CB  ARG A 219      31.473  14.604   9.398  1.00  1.48           C  
ATOM   1477  CG  ARG A 219      29.954  14.272   9.308  1.00  1.66           C  
ATOM   1478  CD  ARG A 219      29.533  13.689   7.961  1.00  3.45           C  
ATOM   1479  NE  ARG A 219      30.182  12.409   7.648  1.00  3.59           N  
ATOM   1480  CZ  ARG A 219      29.951  11.260   8.273  1.00  3.91           C  
ATOM   1481  NH1 ARG A 219      29.079  11.194   9.271  1.00  3.25           N  
ATOM   1482  NH2 ARG A 219      30.605  10.167   7.890  1.00  2.91           N  
ATOM   1483  N   ILE A 220      30.124  14.933  12.434  1.00  2.78           N  
ATOM   1484  CA  ILE A 220      29.473  14.186  13.513  1.00  3.29           C  
ATOM   1485  C   ILE A 220      28.011  13.984  13.110  1.00  3.70           C  
ATOM   1486  O   ILE A 220      27.242  14.932  13.059  1.00  2.68           O  
ATOM   1487  CB  ILE A 220      29.570  14.944  14.873  1.00  3.26           C  
ATOM   1488  CG1 ILE A 220      31.049  15.201  15.213  1.00  4.18           C  
ATOM   1489  CG2 ILE A 220      28.904  14.084  15.988  1.00  3.11           C  
ATOM   1490  CD1 ILE A 220      31.287  15.775  16.615  1.00  3.36           C  
ATOM   1491  N   GLY A 221      27.635  12.745  12.800  1.00  4.72           N  
ATOM   1492  CA  GLY A 221      26.261  12.474  12.388  1.00  3.96           C  
ATOM   1493  C   GLY A 221      26.052  12.789  10.914  1.00  5.15           C  
ATOM   1494  O   GLY A 221      27.020  13.101  10.198  1.00  4.16           O  
ATOM   1495  N   TYR A 222      24.801  12.693  10.451  1.00  4.81           N  
ATOM   1496  CA  TYR A 222      24.480  13.000   9.057  1.00  4.23           C  
ATOM   1497  C   TYR A 222      23.293  13.931   8.830  1.00  4.79           C  
ATOM   1498  O   TYR A 222      23.322  14.751   7.917  1.00  5.90           O  
ATOM   1499  CB  TYR A 222      24.199  11.724   8.259  1.00  4.48           C  
ATOM   1500  CG  TYR A 222      25.404  11.068   7.604  1.00  3.49           C  
ATOM   1501  CD1 TYR A 222      26.262  11.786   6.746  1.00  7.17           C  
ATOM   1502  CD2 TYR A 222      25.648   9.709   7.797  1.00  4.46           C  
ATOM   1503  CE1 TYR A 222      27.328  11.141   6.093  1.00  5.87           C  
ATOM   1504  CE2 TYR A 222      26.702   9.064   7.156  1.00  5.79           C  
ATOM   1505  CZ  TYR A 222      27.535   9.782   6.303  1.00  5.09           C  
ATOM   1506  OH  TYR A 222      28.555   9.111   5.663  1.00  8.22           O  
ATOM   1507  N   TYR A 223      22.239  13.787   9.626  1.00  4.77           N  
ATOM   1508  CA  TYR A 223      21.024  14.583   9.434  1.00  7.09           C  
ATOM   1509  C   TYR A 223      20.412  15.073  10.743  1.00  6.89           C  
ATOM   1510  O   TYR A 223      20.756  14.592  11.826  1.00  5.27           O  
ATOM   1511  CB  TYR A 223      19.983  13.773   8.657  1.00 10.73           C  
ATOM   1512  CG  TYR A 223      20.372  13.471   7.232  1.00 14.29           C  
ATOM   1513  CD1 TYR A 223      20.360  14.471   6.259  1.00 16.40           C  
ATOM   1514  CD2 TYR A 223      20.732  12.175   6.846  1.00 16.56           C  
ATOM   1515  CE1 TYR A 223      20.693  14.187   4.921  1.00 18.99           C  
ATOM   1516  CE2 TYR A 223      21.070  11.883   5.520  1.00 19.14           C  
ATOM   1517  CZ  TYR A 223      21.044  12.889   4.568  1.00 19.89           C  
ATOM   1518  OH  TYR A 223      21.345  12.588   3.248  1.00 25.34           O  
ATOM   1519  N   ARG A 224      19.460  15.998  10.638  1.00  5.23           N  
ATOM   1520  CA  ARG A 224      18.928  16.619  11.834  1.00  5.92           C  
ATOM   1521  C   ARG A 224      18.280  15.770  12.895  1.00  5.71           C  
ATOM   1522  O   ARG A 224      18.264  16.180  14.031  1.00  6.55           O  
ATOM   1523  CB  ARG A 224      18.011  17.798  11.463  1.00  6.04           C  
ATOM   1524  CG  ARG A 224      16.644  17.397  10.920  1.00  6.53           C  
ATOM   1525  CD  ARG A 224      15.852  18.664  10.535  1.00  7.91           C  
ATOM   1526  NE  ARG A 224      15.519  19.493  11.693  1.00  8.88           N  
ATOM   1527  CZ  ARG A 224      14.476  19.290  12.497  1.00 10.36           C  
ATOM   1528  NH1 ARG A 224      13.656  18.269  12.277  1.00 10.26           N  
ATOM   1529  NH2 ARG A 224      14.248  20.104  13.528  1.00  9.13           N  
ATOM   1530  N   ASN A 225      17.779  14.588  12.558  1.00  7.54           N  
ATOM   1531  CA  ASN A 225      17.170  13.743  13.580  1.00  7.50           C  
ATOM   1532  C   ASN A 225      18.193  12.982  14.405  1.00  7.29           C  
ATOM   1533  O   ASN A 225      17.860  12.414  15.458  1.00  6.71           O  
ATOM   1534  CB  ASN A 225      16.196  12.756  12.951  1.00 10.21           C  
ATOM   1535  CG  ASN A 225      15.030  13.448  12.282  1.00 14.53           C  
ATOM   1536  OD1 ASN A 225      14.594  14.497  12.724  1.00 16.43           O  
ATOM   1537  ND2 ASN A 225      14.511  12.846  11.219  1.00 19.44           N  
ATOM   1538  N   ASP A 226      19.446  12.993  13.955  1.00  6.31           N  
ATOM   1539  CA  ASP A 226      20.514  12.308  14.668  1.00  7.45           C  
ATOM   1540  C   ASP A 226      20.876  13.042  15.954  1.00  7.81           C  
ATOM   1541  O   ASP A 226      20.935  14.267  15.970  1.00  8.97           O  
ATOM   1542  CB  ASP A 226      21.787  12.239  13.806  1.00  7.31           C  
ATOM   1543  CG  ASP A 226      21.603  11.417  12.550  1.00  7.13           C  
ATOM   1544  OD1 ASP A 226      20.664  10.594  12.508  1.00  7.52           O  
ATOM   1545  OD2 ASP A 226      22.400  11.589  11.601  1.00  7.05           O  
ATOM   1546  N   ILE A 227      21.143  12.287  17.014  1.00  6.74           N  
ATOM   1547  CA  ILE A 227      21.542  12.855  18.302  1.00  6.92           C  
ATOM   1548  C   ILE A 227      23.032  12.591  18.464  1.00  6.36           C  
ATOM   1549  O   ILE A 227      23.471  11.455  18.336  1.00  7.52           O  
ATOM   1550  CB  ILE A 227      20.819  12.172  19.456  1.00  7.17           C  
ATOM   1551  CG1 ILE A 227      19.308  12.186  19.200  1.00 10.16           C  
ATOM   1552  CG2 ILE A 227      21.199  12.841  20.772  1.00  6.25           C  
ATOM   1553  CD1 ILE A 227      18.707  13.552  19.039  1.00 14.65           C  
ATOM   1554  N   GLY A 228      23.806  13.631  18.753  1.00  6.71           N  
ATOM   1555  CA  GLY A 228      25.244  13.443  18.890  1.00  5.56           C  
ATOM   1556  C   GLY A 228      25.739  13.339  20.319  1.00  6.04           C  
ATOM   1557  O   GLY A 228      26.241  12.290  20.729  1.00  4.79           O  
ATOM   1558  N   ARG A 229      25.591  14.430  21.070  1.00  5.06           N  
ATOM   1559  CA  ARG A 229      26.055  14.516  22.444  1.00  4.63           C  
ATOM   1560  C   ARG A 229      27.537  14.174  22.551  1.00  4.72           C  
ATOM   1561  O   ARG A 229      28.003  13.528  23.492  1.00  4.15           O  
ATOM   1562  CB  ARG A 229      25.194  13.652  23.365  1.00  3.16           C  
ATOM   1563  CG  ARG A 229      23.814  14.283  23.563  1.00  4.66           C  
ATOM   1564  CD  ARG A 229      22.915  13.441  24.451  1.00  8.85           C  
ATOM   1565  NE  ARG A 229      21.547  13.940  24.350  1.00 10.39           N  
ATOM   1566  CZ  ARG A 229      20.467  13.213  24.609  1.00 14.04           C  
ATOM   1567  NH1 ARG A 229      20.595  11.954  24.993  1.00 14.49           N  
ATOM   1568  NH2 ARG A 229      19.260  13.743  24.460  1.00 13.92           N  
ATOM   1569  N   CYS A 230      28.287  14.664  21.571  1.00  4.02           N  
ATOM   1570  CA  CYS A 230      29.728  14.485  21.555  1.00  4.29           C  
ATOM   1571  C   CYS A 230      30.367  15.775  22.057  1.00  3.75           C  
ATOM   1572  O   CYS A 230      29.846  16.872  21.809  1.00  4.84           O  
ATOM   1573  CB  CYS A 230      30.208  14.200  20.136  1.00  5.18           C  
ATOM   1574  SG  CYS A 230      29.779  12.575  19.550  1.00  6.10           S  
ATOM   1575  N   LEU A 231      31.480  15.632  22.771  1.00  3.88           N  
ATOM   1576  CA  LEU A 231      32.218  16.781  23.293  1.00  4.24           C  
ATOM   1577  C   LEU A 231      33.484  16.939  22.448  1.00  3.98           C  
ATOM   1578  O   LEU A 231      34.266  16.003  22.328  1.00  5.56           O  
ATOM   1579  CB  LEU A 231      32.608  16.546  24.758  1.00  4.91           C  
ATOM   1580  CG  LEU A 231      33.519  17.606  25.398  1.00  5.08           C  
ATOM   1581  CD1 LEU A 231      32.815  18.963  25.453  1.00  5.65           C  
ATOM   1582  CD2 LEU A 231      33.894  17.152  26.811  1.00  4.41           C  
ATOM   1583  N   VAL A 232      33.678  18.120  21.857  1.00  4.16           N  
ATOM   1584  CA  VAL A 232      34.849  18.399  21.024  1.00  4.23           C  
ATOM   1585  C   VAL A 232      35.460  19.598  21.733  1.00  4.21           C  
ATOM   1586  O   VAL A 232      34.915  20.702  21.689  1.00  3.81           O  
ATOM   1587  CB  VAL A 232      34.431  18.754  19.568  1.00  5.09           C  
ATOM   1588  CG1 VAL A 232      35.644  19.209  18.753  1.00  4.64           C  
ATOM   1589  CG2 VAL A 232      33.790  17.523  18.912  1.00  6.03           C  
ATOM   1590  N   ASP A 233      36.546  19.364  22.463  1.00  1.67           N  
ATOM   1591  CA  ASP A 233      37.146  20.462  23.202  1.00  3.62           C  
ATOM   1592  C   ASP A 233      38.669  20.529  23.147  1.00  2.49           C  
ATOM   1593  O   ASP A 233      39.341  19.535  22.943  1.00  3.41           O  
ATOM   1594  CB  ASP A 233      36.683  20.415  24.679  1.00  3.06           C  
ATOM   1595  CG  ASP A 233      37.189  19.185  25.441  1.00  5.87           C  
ATOM   1596  OD1 ASP A 233      37.047  18.060  24.946  1.00  3.58           O  
ATOM   1597  OD2 ASP A 233      37.702  19.339  26.583  1.00  4.96           O  
ATOM   1598  N   SER A 234      39.187  21.739  23.299  1.00  3.26           N  
ATOM   1599  CA  SER A 234      40.619  21.949  23.341  1.00  3.06           C  
ATOM   1600  C   SER A 234      41.389  21.378  22.173  1.00  3.85           C  
ATOM   1601  O   SER A 234      42.429  20.768  22.372  1.00  3.71           O  
ATOM   1602  CB  SER A 234      41.176  21.379  24.648  1.00  4.95           C  
ATOM   1603  OG  SER A 234      40.476  21.950  25.698  1.00  4.47           O  
ATOM   1604  N   ASN A 235      40.871  21.564  20.965  1.00  3.01           N  
ATOM   1605  CA  ASN A 235      41.590  21.125  19.763  1.00  3.36           C  
ATOM   1606  C   ASN A 235      42.131  22.372  19.098  1.00  3.40           C  
ATOM   1607  O   ASN A 235      41.605  23.480  19.301  1.00  3.96           O  
ATOM   1608  CB  ASN A 235      40.647  20.421  18.804  1.00  1.27           C  
ATOM   1609  CG  ASN A 235      40.088  19.144  19.391  1.00  3.14           C  
ATOM   1610  OD1 ASN A 235      40.789  18.137  19.491  1.00  3.80           O  
ATOM   1611  ND2 ASN A 235      38.819  19.178  19.789  1.00  2.94           N  
ATOM   1612  N   LEU A 236      43.201  22.193  18.333  1.00  0.92           N  
ATOM   1613  CA  LEU A 236      43.803  23.287  17.594  1.00  3.30           C  
ATOM   1614  C   LEU A 236      43.721  22.990  16.107  1.00  3.76           C  
ATOM   1615  O   LEU A 236      44.337  22.034  15.615  1.00  4.00           O  
ATOM   1616  CB  LEU A 236      45.272  23.482  18.003  1.00  2.56           C  
ATOM   1617  CG  LEU A 236      46.124  24.478  17.192  1.00  3.39           C  
ATOM   1618  CD1 LEU A 236      45.490  25.870  17.242  1.00  4.38           C  
ATOM   1619  CD2 LEU A 236      47.551  24.520  17.746  1.00  5.43           C  
ATOM   1620  N   PHE A 237      42.926  23.796  15.408  1.00  3.53           N  
ATOM   1621  CA  PHE A 237      42.779  23.701  13.951  1.00  3.64           C  
ATOM   1622  C   PHE A 237      43.625  24.894  13.431  1.00  3.84           C  
ATOM   1623  O   PHE A 237      43.299  26.062  13.690  1.00  4.62           O  
ATOM   1624  CB  PHE A 237      41.303  23.861  13.563  1.00  3.30           C  
ATOM   1625  CG  PHE A 237      40.396  22.807  14.157  1.00  6.13           C  
ATOM   1626  CD1 PHE A 237      39.904  22.943  15.443  1.00  6.29           C  
ATOM   1627  CD2 PHE A 237      40.034  21.674  13.411  1.00  5.19           C  
ATOM   1628  CE1 PHE A 237      39.052  21.970  15.997  1.00  5.69           C  
ATOM   1629  CE2 PHE A 237      39.187  20.690  13.955  1.00  6.10           C  
ATOM   1630  CZ  PHE A 237      38.697  20.853  15.256  1.00  4.04           C  
ATOM   1631  N   MET A 238      44.726  24.595  12.737  1.00  2.12           N  
ATOM   1632  CA  MET A 238      45.639  25.638  12.244  1.00  3.69           C  
ATOM   1633  C   MET A 238      45.763  25.395  10.747  1.00  3.70           C  
ATOM   1634  O   MET A 238      46.366  24.431  10.306  1.00  2.56           O  
ATOM   1635  CB  MET A 238      46.985  25.491  12.958  1.00  2.81           C  
ATOM   1636  CG  MET A 238      48.003  26.563  12.608  1.00  4.71           C  
ATOM   1637  SD  MET A 238      49.518  26.249  13.533  1.00  7.33           S  
ATOM   1638  CE  MET A 238      50.537  27.615  12.955  1.00  8.53           C  
ATOM   1639  N   ARG A 239      45.204  26.312   9.969  1.00  3.99           N  
ATOM   1640  CA  ARG A 239      45.130  26.127   8.534  1.00  3.47           C  
ATOM   1641  C   ARG A 239      44.469  24.780   8.206  1.00  3.55           C  
ATOM   1642  O   ARG A 239      44.962  24.012   7.381  1.00  2.83           O  
ATOM   1643  CB  ARG A 239      46.492  26.261   7.844  1.00  4.54           C  
ATOM   1644  CG  ARG A 239      47.145  27.640   8.050  1.00  2.80           C  
ATOM   1645  CD  ARG A 239      48.228  27.922   6.979  1.00  5.56           C  
ATOM   1646  NE  ARG A 239      48.923  29.174   7.293  1.00  6.88           N  
ATOM   1647  CZ  ARG A 239      48.424  30.389   7.093  1.00  7.96           C  
ATOM   1648  NH1 ARG A 239      47.224  30.550   6.523  1.00  7.13           N  
ATOM   1649  NH2 ARG A 239      49.140  31.452   7.447  1.00  7.77           N  
ATOM   1650  N   GLN A 240      43.366  24.488   8.908  1.00  2.86           N  
ATOM   1651  CA  GLN A 240      42.550  23.320   8.604  1.00  3.43           C  
ATOM   1652  C   GLN A 240      41.769  23.924   7.438  1.00  4.26           C  
ATOM   1653  O   GLN A 240      40.789  24.649   7.634  1.00  5.99           O  
ATOM   1654  CB  GLN A 240      41.610  22.985   9.764  1.00  2.66           C  
ATOM   1655  CG  GLN A 240      40.535  21.963   9.390  1.00  2.90           C  
ATOM   1656  CD  GLN A 240      41.105  20.773   8.615  1.00  3.10           C  
ATOM   1657  OE1 GLN A 240      42.171  20.255   8.939  1.00  4.08           O  
ATOM   1658  NE2 GLN A 240      40.385  20.342   7.593  1.00  1.84           N  
ATOM   1659  N   ASP A 241      42.223  23.635   6.221  1.00  3.68           N  
ATOM   1660  CA  ASP A 241      41.644  24.228   5.014  1.00  3.75           C  
ATOM   1661  C   ASP A 241      41.014  23.239   4.045  1.00  5.05           C  
ATOM   1662  O   ASP A 241      40.671  23.620   2.915  1.00  5.99           O  
ATOM   1663  CB  ASP A 241      42.738  24.968   4.222  1.00  3.70           C  
ATOM   1664  CG  ASP A 241      43.390  26.124   4.990  1.00  4.91           C  
ATOM   1665  OD1 ASP A 241      42.886  26.548   6.040  1.00  3.67           O  
ATOM   1666  OD2 ASP A 241      44.432  26.624   4.497  1.00  6.65           O  
ATOM   1667  N   SER A 242      40.850  21.987   4.466  1.00  4.11           N  
ATOM   1668  CA  SER A 242      40.337  20.955   3.571  1.00  4.37           C  
ATOM   1669  C   SER A 242      39.196  21.344   2.662  1.00  3.94           C  
ATOM   1670  O   SER A 242      39.229  21.043   1.467  1.00  4.49           O  
ATOM   1671  CB  SER A 242      39.951  19.704   4.368  1.00  3.66           C  
ATOM   1672  OG  SER A 242      41.100  19.160   5.010  1.00  5.07           O  
ATOM   1673  N   GLU A 243      38.171  21.966   3.227  1.00  3.70           N  
ATOM   1674  CA  GLU A 243      37.026  22.391   2.416  1.00  2.73           C  
ATOM   1675  C   GLU A 243      36.301  23.482   3.177  1.00  3.73           C  
ATOM   1676  O   GLU A 243      36.807  23.972   4.186  1.00  6.06           O  
ATOM   1677  CB  GLU A 243      36.105  21.197   2.126  1.00  5.52           C  
ATOM   1678  CG  GLU A 243      35.472  20.575   3.354  1.00  5.36           C  
ATOM   1679  CD  GLU A 243      33.978  20.359   3.166  1.00  6.62           C  
ATOM   1680  OE1 GLU A 243      33.198  21.291   3.472  1.00  5.25           O  
ATOM   1681  OE2 GLU A 243      33.585  19.270   2.688  1.00  8.57           O  
ATOM   1682  N   ALA A 244      35.129  23.881   2.695  1.00  3.39           N  
ATOM   1683  CA  ALA A 244      34.402  24.962   3.347  1.00  4.94           C  
ATOM   1684  C   ALA A 244      34.099  24.721   4.821  1.00  5.25           C  
ATOM   1685  O   ALA A 244      34.041  25.666   5.606  1.00  3.91           O  
ATOM   1686  CB  ALA A 244      33.098  25.224   2.602  1.00  6.91           C  
ATOM   1687  N   GLU A 245      33.898  23.464   5.203  1.00  4.16           N  
ATOM   1688  CA  GLU A 245      33.543  23.174   6.587  1.00  5.12           C  
ATOM   1689  C   GLU A 245      34.693  22.627   7.404  1.00  4.74           C  
ATOM   1690  O   GLU A 245      35.221  21.552   7.095  1.00  4.42           O  
ATOM   1691  CB  GLU A 245      32.363  22.184   6.626  1.00  3.56           C  
ATOM   1692  CG  GLU A 245      31.179  22.610   5.716  1.00  5.26           C  
ATOM   1693  CD  GLU A 245      29.953  21.735   5.913  1.00  4.89           C  
ATOM   1694  OE1 GLU A 245      29.200  22.002   6.872  1.00  5.34           O  
ATOM   1695  OE2 GLU A 245      29.751  20.780   5.119  1.00  5.64           O  
ATOM   1696  N   ILE A 246      35.089  23.375   8.438  1.00  2.75           N  
ATOM   1697  CA  ILE A 246      36.174  22.950   9.326  1.00  2.39           C  
ATOM   1698  C   ILE A 246      35.592  21.741  10.072  1.00  2.26           C  
ATOM   1699  O   ILE A 246      36.196  20.660  10.151  1.00  2.22           O  
ATOM   1700  CB  ILE A 246      36.520  24.065  10.350  1.00  2.55           C  
ATOM   1701  CG1 ILE A 246      36.969  25.345   9.631  1.00  3.73           C  
ATOM   1702  CG2 ILE A 246      37.638  23.587  11.260  1.00  3.61           C  
ATOM   1703  CD1 ILE A 246      37.265  26.522  10.620  1.00  5.04           C  
ATOM   1704  N   ILE A 247      34.407  21.952  10.619  1.00  2.84           N  
ATOM   1705  CA  ILE A 247      33.678  20.882  11.280  1.00  2.57           C  
ATOM   1706  C   ILE A 247      32.256  20.940  10.713  1.00  2.90           C  
ATOM   1707  O   ILE A 247      31.657  22.017  10.632  1.00  3.17           O  
ATOM   1708  CB  ILE A 247      33.600  21.089  12.813  1.00  2.80           C  
ATOM   1709  CG1 ILE A 247      34.983  20.919  13.429  1.00  2.62           C  
ATOM   1710  CG2 ILE A 247      32.594  20.061  13.460  1.00  1.91           C  
ATOM   1711  CD1 ILE A 247      35.006  21.202  14.959  1.00  1.94           C  
ATOM   1712  N   THR A 248      31.723  19.805  10.273  1.00  2.94           N  
ATOM   1713  CA  THR A 248      30.342  19.832   9.834  1.00  3.22           C  
ATOM   1714  C   THR A 248      29.617  18.983  10.890  1.00  2.87           C  
ATOM   1715  O   THR A 248      29.647  17.740  10.861  1.00  2.55           O  
ATOM   1716  CB  THR A 248      30.157  19.334   8.358  1.00  2.67           C  
ATOM   1717  OG1 THR A 248      28.795  19.545   7.960  1.00  2.72           O  
ATOM   1718  CG2 THR A 248      30.512  17.855   8.199  1.00  4.97           C  
ATOM   1719  N   SER A 249      29.030  19.687  11.872  1.00  3.16           N  
ATOM   1720  CA  SER A 249      28.317  19.052  12.982  1.00  1.93           C  
ATOM   1721  C   SER A 249      26.898  18.796  12.473  1.00  3.77           C  
ATOM   1722  O   SER A 249      26.097  19.724  12.314  1.00  2.82           O  
ATOM   1723  CB  SER A 249      28.298  19.969  14.204  1.00  2.99           C  
ATOM   1724  OG  SER A 249      27.873  19.247  15.359  1.00  2.31           O  
ATOM   1725  N   LYS A 250      26.615  17.518  12.238  1.00  3.05           N  
ATOM   1726  CA  LYS A 250      25.350  17.079  11.659  1.00  3.45           C  
ATOM   1727  C   LYS A 250      24.518  16.210  12.584  1.00  5.46           C  
ATOM   1728  O   LYS A 250      24.006  15.154  12.178  1.00  5.08           O  
ATOM   1729  CB  LYS A 250      25.642  16.333  10.350  1.00  2.61           C  
ATOM   1730  CG  LYS A 250      26.213  17.220   9.233  1.00  4.38           C  
ATOM   1731  CD  LYS A 250      26.481  16.406   7.967  1.00  3.22           C  
ATOM   1732  CE  LYS A 250      26.638  17.333   6.751  1.00  8.56           C  
ATOM   1733  NZ  LYS A 250      26.669  16.555   5.486  1.00 10.13           N  
ATOM   1734  N   SER A 251      24.421  16.642  13.844  1.00  4.00           N  
ATOM   1735  CA  SER A 251      23.607  15.953  14.837  1.00  4.12           C  
ATOM   1736  C   SER A 251      23.339  16.900  16.002  1.00  4.47           C  
ATOM   1737  O   SER A 251      24.013  17.919  16.185  1.00  2.20           O  
ATOM   1738  CB  SER A 251      24.250  14.627  15.317  1.00  2.27           C  
ATOM   1739  OG  SER A 251      25.633  14.773  15.583  1.00  3.68           O  
ATOM   1740  N   GLN A 252      22.301  16.592  16.757  1.00  4.08           N  
ATOM   1741  CA  GLN A 252      21.910  17.430  17.873  1.00  3.47           C  
ATOM   1742  C   GLN A 252      22.811  17.331  19.079  1.00  3.85           C  
ATOM   1743  O   GLN A 252      23.490  16.342  19.294  1.00  3.89           O  
ATOM   1744  CB  GLN A 252      20.485  17.051  18.332  1.00  2.29           C  
ATOM   1745  CG  GLN A 252      19.397  17.190  17.266  1.00  3.84           C  
ATOM   1746  CD  GLN A 252      18.063  16.619  17.745  1.00  8.60           C  
ATOM   1747  OE1 GLN A 252      17.669  16.843  18.895  1.00  8.76           O  
ATOM   1748  NE2 GLN A 252      17.359  15.884  16.867  1.00  9.36           N  
ATOM   1749  N   GLU A 253      22.794  18.398  19.862  1.00  5.29           N  
ATOM   1750  CA  GLU A 253      23.457  18.454  21.146  1.00  4.39           C  
ATOM   1751  C   GLU A 253      24.924  18.121  21.298  1.00  5.06           C  
ATOM   1752  O   GLU A 253      25.326  17.542  22.294  1.00  6.79           O  
ATOM   1753  CB  GLU A 253      22.614  17.651  22.149  1.00  6.90           C  
ATOM   1754  CG  GLU A 253      21.141  18.137  22.143  1.00  7.05           C  
ATOM   1755  CD  GLU A 253      20.270  17.599  23.264  1.00 12.76           C  
ATOM   1756  OE1 GLU A 253      20.689  16.672  24.001  1.00 12.07           O  
ATOM   1757  OE2 GLU A 253      19.135  18.130  23.386  1.00 11.26           O  
ATOM   1758  N   ASN A 254      25.721  18.514  20.316  1.00  4.51           N  
ATOM   1759  CA  ASN A 254      27.159  18.359  20.417  1.00  4.12           C  
ATOM   1760  C   ASN A 254      27.617  19.645  21.081  1.00  4.50           C  
ATOM   1761  O   ASN A 254      26.973  20.687  20.930  1.00  4.31           O  
ATOM   1762  CB  ASN A 254      27.746  18.222  19.017  1.00  3.80           C  
ATOM   1763  CG  ASN A 254      27.353  16.919  18.403  1.00  4.11           C  
ATOM   1764  OD1 ASN A 254      27.558  15.863  19.013  1.00  3.58           O  
ATOM   1765  ND2 ASN A 254      26.775  16.964  17.217  1.00  4.67           N  
ATOM   1766  N   VAL A 255      28.695  19.562  21.845  1.00  4.16           N  
ATOM   1767  CA  VAL A 255      29.225  20.711  22.548  1.00  4.09           C  
ATOM   1768  C   VAL A 255      30.663  20.937  22.098  1.00  2.97           C  
ATOM   1769  O   VAL A 255      31.505  20.035  22.206  1.00  4.14           O  
ATOM   1770  CB  VAL A 255      29.220  20.481  24.083  1.00  4.15           C  
ATOM   1771  CG1 VAL A 255      29.811  21.699  24.798  1.00  4.16           C  
ATOM   1772  CG2 VAL A 255      27.781  20.214  24.570  1.00  4.59           C  
ATOM   1773  N   TYR A 256      30.924  22.144  21.596  1.00  3.22           N  
ATOM   1774  CA  TYR A 256      32.244  22.551  21.134  1.00  4.26           C  
ATOM   1775  C   TYR A 256      32.734  23.587  22.132  1.00  3.65           C  
ATOM   1776  O   TYR A 256      32.218  24.716  22.193  1.00  6.05           O  
ATOM   1777  CB  TYR A 256      32.153  23.147  19.725  1.00  3.37           C  
ATOM   1778  CG  TYR A 256      31.653  22.131  18.728  1.00  4.24           C  
ATOM   1779  CD1 TYR A 256      32.542  21.269  18.100  1.00  3.63           C  
ATOM   1780  CD2 TYR A 256      30.288  21.947  18.517  1.00  3.45           C  
ATOM   1781  CE1 TYR A 256      32.077  20.228  17.293  1.00  3.57           C  
ATOM   1782  CE2 TYR A 256      29.816  20.924  17.711  1.00  3.53           C  
ATOM   1783  CZ  TYR A 256      30.729  20.064  17.110  1.00  2.24           C  
ATOM   1784  OH  TYR A 256      30.289  19.003  16.366  1.00  3.29           O  
ATOM   1785  N   TYR A 257      33.721  23.193  22.930  1.00  3.10           N  
ATOM   1786  CA  TYR A 257      34.245  24.055  23.979  1.00  3.36           C  
ATOM   1787  C   TYR A 257      35.746  24.248  23.953  1.00  3.19           C  
ATOM   1788  O   TYR A 257      36.495  23.281  23.913  1.00  3.64           O  
ATOM   1789  CB  TYR A 257      33.847  23.461  25.348  1.00  3.42           C  
ATOM   1790  CG  TYR A 257      34.453  24.175  26.543  1.00  4.30           C  
ATOM   1791  CD1 TYR A 257      34.145  25.507  26.809  1.00  5.93           C  
ATOM   1792  CD2 TYR A 257      35.355  23.520  27.384  1.00  7.25           C  
ATOM   1793  CE1 TYR A 257      34.729  26.185  27.892  1.00  6.10           C  
ATOM   1794  CE2 TYR A 257      35.953  24.194  28.477  1.00  7.56           C  
ATOM   1795  CZ  TYR A 257      35.626  25.526  28.713  1.00  7.47           C  
ATOM   1796  OH  TYR A 257      36.191  26.212  29.773  1.00  7.14           O  
ATOM   1797  N   GLY A 258      36.169  25.508  23.982  1.00  1.97           N  
ATOM   1798  CA  GLY A 258      37.589  25.816  24.040  1.00  4.44           C  
ATOM   1799  C   GLY A 258      38.492  25.345  22.924  1.00  4.10           C  
ATOM   1800  O   GLY A 258      39.642  24.982  23.175  1.00  4.15           O  
ATOM   1801  N   ASN A 259      37.980  25.354  21.700  1.00  2.37           N  
ATOM   1802  CA  ASN A 259      38.783  24.973  20.555  1.00  2.58           C  
ATOM   1803  C   ASN A 259      39.356  26.244  19.951  1.00  3.11           C  
ATOM   1804  O   ASN A 259      38.749  27.307  20.059  1.00  4.90           O  
ATOM   1805  CB  ASN A 259      37.904  24.302  19.498  1.00  3.39           C  
ATOM   1806  CG  ASN A 259      37.302  23.013  19.987  1.00  3.97           C  
ATOM   1807  OD1 ASN A 259      37.999  22.000  20.110  1.00  4.30           O  
ATOM   1808  ND2 ASN A 259      36.002  23.035  20.270  1.00  3.09           N  
ATOM   1809  N   THR A 260      40.522  26.135  19.321  1.00  3.54           N  
ATOM   1810  CA  THR A 260      41.144  27.284  18.650  1.00  4.23           C  
ATOM   1811  C   THR A 260      41.182  26.990  17.156  1.00  4.18           C  
ATOM   1812  O   THR A 260      41.585  25.894  16.744  1.00  3.29           O  
ATOM   1813  CB  THR A 260      42.583  27.538  19.153  1.00  3.98           C  
ATOM   1814  OG1 THR A 260      42.518  28.033  20.495  1.00  7.15           O  
ATOM   1815  CG2 THR A 260      43.305  28.579  18.282  1.00  6.91           C  
ATOM   1816  N   TYR A 261      40.718  27.960  16.364  1.00  2.85           N  
ATOM   1817  CA  TYR A 261      40.686  27.862  14.906  1.00  2.33           C  
ATOM   1818  C   TYR A 261      41.524  29.024  14.435  1.00  4.00           C  
ATOM   1819  O   TYR A 261      41.073  30.180  14.464  1.00  6.58           O  
ATOM   1820  CB  TYR A 261      39.250  28.011  14.380  1.00  3.49           C  
ATOM   1821  CG  TYR A 261      38.300  26.993  14.965  1.00  1.55           C  
ATOM   1822  CD1 TYR A 261      37.656  27.235  16.183  1.00  4.74           C  
ATOM   1823  CD2 TYR A 261      38.072  25.761  14.325  1.00  5.46           C  
ATOM   1824  CE1 TYR A 261      36.797  26.277  16.758  1.00  3.40           C  
ATOM   1825  CE2 TYR A 261      37.221  24.802  14.898  1.00  2.95           C  
ATOM   1826  CZ  TYR A 261      36.591  25.077  16.109  1.00  4.65           C  
ATOM   1827  OH  TYR A 261      35.731  24.160  16.689  1.00  3.79           O  
ATOM   1828  N   LEU A 262      42.751  28.713  14.029  1.00  4.60           N  
ATOM   1829  CA  LEU A 262      43.707  29.721  13.585  1.00  3.97           C  
ATOM   1830  C   LEU A 262      43.944  29.682  12.095  1.00  4.21           C  
ATOM   1831  O   LEU A 262      44.389  28.666  11.558  1.00  3.09           O  
ATOM   1832  CB  LEU A 262      45.038  29.527  14.319  1.00  3.42           C  
ATOM   1833  CG  LEU A 262      46.207  30.374  13.824  1.00  4.91           C  
ATOM   1834  CD1 LEU A 262      45.878  31.856  13.984  1.00  6.74           C  
ATOM   1835  CD2 LEU A 262      47.452  29.989  14.634  1.00  5.96           C  
ATOM   1836  N   ASN A 263      43.655  30.801  11.436  1.00  2.89           N  
ATOM   1837  CA  ASN A 263      43.844  30.926   9.986  1.00  2.32           C  
ATOM   1838  C   ASN A 263      43.267  29.724   9.215  1.00  4.16           C  
ATOM   1839  O   ASN A 263      43.956  29.097   8.385  1.00  2.83           O  
ATOM   1840  CB  ASN A 263      45.339  31.079   9.676  1.00  5.30           C  
ATOM   1841  CG  ASN A 263      45.921  32.335  10.288  1.00  4.50           C  
ATOM   1842  OD1 ASN A 263      45.212  33.317  10.456  1.00  7.12           O  
ATOM   1843  ND2 ASN A 263      47.218  32.311  10.626  1.00  5.48           N  
ATOM   1844  N   CYS A 264      42.005  29.388   9.496  1.00  2.74           N  
ATOM   1845  CA  CYS A 264      41.380  28.258   8.804  1.00  2.21           C  
ATOM   1846  C   CYS A 264      40.511  28.766   7.667  1.00  2.92           C  
ATOM   1847  O   CYS A 264      39.669  29.647   7.861  1.00  3.94           O  
ATOM   1848  CB  CYS A 264      40.488  27.456   9.770  1.00  2.52           C  
ATOM   1849  SG  CYS A 264      41.411  26.659  11.076  1.00  4.38           S  
ATOM   1850  N   GLN A 265      40.698  28.197   6.479  1.00  4.19           N  
ATOM   1851  CA  GLN A 265      39.900  28.589   5.327  1.00  3.90           C  
ATOM   1852  C   GLN A 265      38.587  27.804   5.355  1.00  5.67           C  
ATOM   1853  O   GLN A 265      38.383  26.855   4.586  1.00  3.70           O  
ATOM   1854  CB  GLN A 265      40.636  28.271   4.045  1.00  2.53           C  
ATOM   1855  CG  GLN A 265      41.875  29.118   3.804  1.00  3.35           C  
ATOM   1856  CD  GLN A 265      42.312  29.006   2.365  1.00  5.91           C  
ATOM   1857  OE1 GLN A 265      41.671  29.562   1.450  1.00  5.39           O  
ATOM   1858  NE2 GLN A 265      43.377  28.256   2.136  1.00  6.70           N  
ATOM   1859  N   GLY A 266      37.702  28.204   6.251  1.00  4.96           N  
ATOM   1860  CA  GLY A 266      36.428  27.525   6.365  1.00  3.40           C  
ATOM   1861  C   GLY A 266      35.703  28.043   7.592  1.00  3.84           C  
ATOM   1862  O   GLY A 266      36.149  29.007   8.222  1.00  4.12           O  
ATOM   1863  N   THR A 267      34.579  27.415   7.925  1.00  2.45           N  
ATOM   1864  CA  THR A 267      33.823  27.815   9.094  1.00  2.14           C  
ATOM   1865  C   THR A 267      33.474  26.579   9.912  1.00  3.47           C  
ATOM   1866  O   THR A 267      33.427  25.471   9.374  1.00  3.23           O  
ATOM   1867  CB  THR A 267      32.500  28.600   8.717  1.00  3.17           C  
ATOM   1868  OG1 THR A 267      31.686  27.822   7.830  1.00  3.15           O  
ATOM   1869  CG2 THR A 267      32.847  29.955   8.038  1.00  3.51           C  
ATOM   1870  N   MET A 268      33.281  26.761  11.217  1.00  2.84           N  
ATOM   1871  CA  MET A 268      32.887  25.658  12.091  1.00  3.90           C  
ATOM   1872  C   MET A 268      31.363  25.737  11.985  1.00  4.07           C  
ATOM   1873  O   MET A 268      30.753  26.787  12.236  1.00  3.20           O  
ATOM   1874  CB  MET A 268      33.418  25.908  13.520  1.00  4.76           C  
ATOM   1875  CG  MET A 268      33.157  24.780  14.520  1.00  6.72           C  
ATOM   1876  SD  MET A 268      31.504  24.941  15.206  1.00  5.26           S  
ATOM   1877  CE  MET A 268      30.962  23.196  15.068  1.00  4.70           C  
ATOM   1878  N   ASN A 269      30.738  24.625  11.611  1.00  3.29           N  
ATOM   1879  CA  ASN A 269      29.307  24.647  11.342  1.00  2.50           C  
ATOM   1880  C   ASN A 269      28.337  23.803  12.159  1.00  3.89           C  
ATOM   1881  O   ASN A 269      28.607  22.645  12.439  1.00  2.99           O  
ATOM   1882  CB  ASN A 269      29.065  24.222   9.881  1.00  2.86           C  
ATOM   1883  CG  ASN A 269      29.715  25.130   8.860  1.00  2.40           C  
ATOM   1884  OD1 ASN A 269      30.178  26.213   9.164  1.00  4.26           O  
ATOM   1885  ND2 ASN A 269      29.718  24.679   7.609  1.00  4.14           N  
ATOM   1886  N   PHE A 270      27.182  24.394  12.477  1.00  2.95           N  
ATOM   1887  CA  PHE A 270      26.088  23.654  13.091  1.00  2.79           C  
ATOM   1888  C   PHE A 270      25.307  23.409  11.787  1.00  3.87           C  
ATOM   1889  O   PHE A 270      24.413  24.171  11.440  1.00  4.26           O  
ATOM   1890  CB  PHE A 270      25.275  24.545  14.029  1.00  3.25           C  
ATOM   1891  CG  PHE A 270      25.926  24.799  15.361  1.00  3.55           C  
ATOM   1892  CD1 PHE A 270      27.094  24.134  15.739  1.00  3.43           C  
ATOM   1893  CD2 PHE A 270      25.325  25.691  16.266  1.00  3.74           C  
ATOM   1894  CE1 PHE A 270      27.652  24.353  17.000  1.00  3.60           C  
ATOM   1895  CE2 PHE A 270      25.873  25.916  17.541  1.00  4.25           C  
ATOM   1896  CZ  PHE A 270      27.042  25.245  17.907  1.00  4.21           C  
ATOM   1897  N   ARG A 271      25.652  22.340  11.065  1.00  2.54           N  
ATOM   1898  CA  ARG A 271      25.059  22.076   9.748  1.00  2.56           C  
ATOM   1899  C   ARG A 271      23.666  21.451   9.769  1.00  3.95           C  
ATOM   1900  O   ARG A 271      22.769  21.882   9.033  1.00  3.32           O  
ATOM   1901  CB  ARG A 271      26.026  21.212   8.930  1.00  4.33           C  
ATOM   1902  CG  ARG A 271      25.537  20.855   7.517  1.00  4.61           C  
ATOM   1903  CD  ARG A 271      25.447  22.065   6.591  1.00  5.13           C  
ATOM   1904  NE  ARG A 271      24.812  21.683   5.315  1.00  6.27           N  
ATOM   1905  CZ  ARG A 271      23.493  21.672   5.123  1.00  6.96           C  
ATOM   1906  NH1 ARG A 271      22.675  22.023   6.102  1.00  4.59           N  
ATOM   1907  NH2 ARG A 271      22.988  21.305   3.950  1.00  5.39           N  
ATOM   1908  N   HIS A 272      23.506  20.402  10.568  1.00  3.71           N  
ATOM   1909  CA  HIS A 272      22.205  19.729  10.749  1.00  3.91           C  
ATOM   1910  C   HIS A 272      22.044  19.451  12.231  1.00  3.90           C  
ATOM   1911  O   HIS A 272      23.025  19.168  12.925  1.00  3.71           O  
ATOM   1912  CB  HIS A 272      22.144  18.375  10.025  1.00  5.40           C  
ATOM   1913  CG  HIS A 272      22.067  18.484   8.537  1.00  6.70           C  
ATOM   1914  ND1 HIS A 272      21.061  19.169   7.887  1.00  6.74           N  
ATOM   1915  CD2 HIS A 272      22.861  17.966   7.569  1.00  7.58           C  
ATOM   1916  CE1 HIS A 272      21.240  19.067   6.580  1.00  8.52           C  
ATOM   1917  NE2 HIS A 272      22.322  18.341   6.360  1.00  6.78           N  
ATOM   1918  N   GLY A 273      20.818  19.533  12.734  1.00  3.24           N  
ATOM   1919  CA  GLY A 273      20.612  19.235  14.142  1.00  2.52           C  
ATOM   1920  C   GLY A 273      20.464  20.481  14.988  1.00  4.84           C  
ATOM   1921  O   GLY A 273      21.340  21.348  14.998  1.00  4.49           O  
ATOM   1922  N   ASP A 274      19.340  20.575  15.686  1.00  5.15           N  
ATOM   1923  CA  ASP A 274      19.076  21.711  16.548  1.00  5.07           C  
ATOM   1924  C   ASP A 274      19.754  21.500  17.894  1.00  5.13           C  
ATOM   1925  O   ASP A 274      20.309  20.433  18.173  1.00  5.47           O  
ATOM   1926  CB  ASP A 274      17.561  21.866  16.772  1.00  6.92           C  
ATOM   1927  CG  ASP A 274      16.814  22.230  15.497  1.00  7.41           C  
ATOM   1928  OD1 ASP A 274      17.431  22.843  14.606  1.00  3.84           O  
ATOM   1929  OD2 ASP A 274      15.613  21.917  15.399  1.00  7.74           O  
ATOM   1930  N   HIS A 275      19.719  22.549  18.704  1.00  5.09           N  
ATOM   1931  CA  HIS A 275      20.256  22.541  20.060  1.00  5.72           C  
ATOM   1932  C   HIS A 275      21.717  22.137  20.184  1.00  5.52           C  
ATOM   1933  O   HIS A 275      22.053  21.216  20.933  1.00  5.47           O  
ATOM   1934  CB  HIS A 275      19.402  21.628  20.936  1.00  7.13           C  
ATOM   1935  CG  HIS A 275      19.608  21.831  22.407  1.00  8.66           C  
ATOM   1936  ND1 HIS A 275      19.260  20.878  23.340  1.00 10.29           N  
ATOM   1937  CD2 HIS A 275      20.122  22.869  23.105  1.00 11.17           C  
ATOM   1938  CE1 HIS A 275      19.554  21.320  24.549  1.00 10.00           C  
ATOM   1939  NE2 HIS A 275      20.077  22.526  24.436  1.00 11.16           N  
ATOM   1940  N   GLN A 276      22.582  22.819  19.441  1.00  4.28           N  
ATOM   1941  CA  GLN A 276      24.018  22.561  19.533  1.00  3.80           C  
ATOM   1942  C   GLN A 276      24.663  23.693  20.339  1.00  3.90           C  
ATOM   1943  O   GLN A 276      24.105  24.781  20.458  1.00  3.69           O  
ATOM   1944  CB  GLN A 276      24.625  22.454  18.136  1.00  3.91           C  
ATOM   1945  CG  GLN A 276      24.003  21.306  17.351  1.00  4.98           C  
ATOM   1946  CD  GLN A 276      24.887  20.833  16.231  1.00  4.68           C  
ATOM   1947  OE1 GLN A 276      26.052  20.491  16.454  1.00  5.73           O  
ATOM   1948  NE2 GLN A 276      24.339  20.785  15.016  1.00  3.99           N  
ATOM   1949  N   VAL A 277      25.842  23.432  20.885  1.00  3.43           N  
ATOM   1950  CA  VAL A 277      26.508  24.387  21.761  1.00  3.61           C  
ATOM   1951  C   VAL A 277      27.940  24.716  21.371  1.00  3.04           C  
ATOM   1952  O   VAL A 277      28.724  23.826  21.075  1.00  2.91           O  
ATOM   1953  CB  VAL A 277      26.521  23.812  23.229  1.00  1.87           C  
ATOM   1954  CG1 VAL A 277      27.195  24.786  24.191  1.00  5.65           C  
ATOM   1955  CG2 VAL A 277      25.094  23.477  23.684  1.00  4.33           C  
ATOM   1956  N   ALA A 278      28.284  26.001  21.344  1.00  2.82           N  
ATOM   1957  CA  ALA A 278      29.662  26.400  21.060  1.00  2.89           C  
ATOM   1958  C   ALA A 278      29.991  27.464  22.102  1.00  4.49           C  
ATOM   1959  O   ALA A 278      29.412  28.552  22.099  1.00  5.19           O  
ATOM   1960  CB  ALA A 278      29.806  26.966  19.656  1.00  3.57           C  
ATOM   1961  N   ILE A 279      30.913  27.134  22.997  1.00  4.70           N  
ATOM   1962  CA  ILE A 279      31.298  28.050  24.061  1.00  3.95           C  
ATOM   1963  C   ILE A 279      32.806  28.239  24.154  1.00  3.62           C  
ATOM   1964  O   ILE A 279      33.578  27.286  24.105  1.00  4.86           O  
ATOM   1965  CB  ILE A 279      30.794  27.520  25.428  1.00  4.35           C  
ATOM   1966  CG1 ILE A 279      29.261  27.494  25.421  1.00  4.54           C  
ATOM   1967  CG2 ILE A 279      31.342  28.373  26.570  1.00  5.56           C  
ATOM   1968  CD1 ILE A 279      28.640  26.776  26.642  1.00  3.47           C  
ATOM   1969  N   ASN A 280      33.206  29.491  24.284  1.00  4.19           N  
ATOM   1970  CA  ASN A 280      34.593  29.847  24.478  1.00  4.04           C  
ATOM   1971  C   ASN A 280      35.595  29.296  23.463  1.00  4.96           C  
ATOM   1972  O   ASN A 280      36.671  28.824  23.836  1.00  4.13           O  
ATOM   1973  CB  ASN A 280      34.997  29.448  25.913  1.00  5.10           C  
ATOM   1974  CG  ASN A 280      35.924  30.459  26.558  1.00  7.27           C  
ATOM   1975  OD1 ASN A 280      35.550  31.149  27.514  1.00  6.88           O  
ATOM   1976  ND2 ASN A 280      37.132  30.578  26.016  1.00  5.44           N  
ATOM   1977  N   ASN A 281      35.231  29.328  22.180  1.00  4.60           N  
ATOM   1978  CA  ASN A 281      36.145  28.914  21.133  1.00  4.13           C  
ATOM   1979  C   ASN A 281      36.778  30.197  20.616  1.00  4.23           C  
ATOM   1980  O   ASN A 281      36.184  31.268  20.732  1.00  5.76           O  
ATOM   1981  CB  ASN A 281      35.386  28.235  19.999  1.00  1.61           C  
ATOM   1982  CG  ASN A 281      34.711  26.986  20.459  1.00  3.15           C  
ATOM   1983  OD1 ASN A 281      35.354  25.961  20.614  1.00  5.27           O  
ATOM   1984  ND2 ASN A 281      33.399  27.070  20.715  1.00  3.07           N  
ATOM   1985  N   PHE A 282      37.971  30.077  20.048  1.00  3.56           N  
ATOM   1986  CA  PHE A 282      38.700  31.217  19.490  1.00  4.13           C  
ATOM   1987  C   PHE A 282      38.793  31.084  17.978  1.00  4.41           C  
ATOM   1988  O   PHE A 282      39.249  30.060  17.479  1.00  5.27           O  
ATOM   1989  CB  PHE A 282      40.116  31.267  20.078  1.00  3.35           C  
ATOM   1990  CG  PHE A 282      40.151  31.665  21.533  1.00  4.37           C  
ATOM   1991  CD1 PHE A 282      40.017  30.706  22.532  1.00  5.97           C  
ATOM   1992  CD2 PHE A 282      40.278  33.011  21.893  1.00  4.35           C  
ATOM   1993  CE1 PHE A 282      40.003  31.064  23.872  1.00  6.64           C  
ATOM   1994  CE2 PHE A 282      40.263  33.388  23.245  1.00  8.75           C  
ATOM   1995  CZ  PHE A 282      40.124  32.405  24.236  1.00  6.12           C  
ATOM   1996  N   TYR A 283      38.338  32.104  17.257  1.00  4.05           N  
ATOM   1997  CA  TYR A 283      38.388  32.111  15.796  1.00  4.79           C  
ATOM   1998  C   TYR A 283      39.293  33.277  15.429  1.00  4.59           C  
ATOM   1999  O   TYR A 283      38.890  34.459  15.450  1.00  6.13           O  
ATOM   2000  CB  TYR A 283      36.979  32.283  15.207  1.00  4.13           C  
ATOM   2001  CG  TYR A 283      36.013  31.188  15.612  1.00  4.16           C  
ATOM   2002  CD1 TYR A 283      35.976  29.969  14.923  1.00  4.26           C  
ATOM   2003  CD2 TYR A 283      35.140  31.366  16.689  1.00  4.27           C  
ATOM   2004  CE1 TYR A 283      35.090  28.951  15.303  1.00  6.65           C  
ATOM   2005  CE2 TYR A 283      34.249  30.356  17.079  1.00  3.74           C  
ATOM   2006  CZ  TYR A 283      34.235  29.145  16.372  1.00  5.74           C  
ATOM   2007  OH  TYR A 283      33.367  28.133  16.745  1.00  4.52           O  
ATOM   2008  N   ILE A 284      40.523  32.927  15.081  1.00  3.97           N  
ATOM   2009  CA  ILE A 284      41.554  33.908  14.796  1.00  4.99           C  
ATOM   2010  C   ILE A 284      42.094  33.846  13.365  1.00  4.92           C  
ATOM   2011  O   ILE A 284      42.429  32.771  12.848  1.00  4.63           O  
ATOM   2012  CB  ILE A 284      42.765  33.676  15.752  1.00  4.91           C  
ATOM   2013  CG1 ILE A 284      42.293  33.517  17.211  1.00  6.83           C  
ATOM   2014  CG2 ILE A 284      43.794  34.795  15.573  1.00  6.21           C  
ATOM   2015  CD1 ILE A 284      41.725  34.790  17.854  1.00  8.97           C  
ATOM   2016  N   GLY A 285      42.194  35.014  12.744  1.00  4.93           N  
ATOM   2017  CA  GLY A 285      42.757  35.119  11.405  1.00  5.84           C  
ATOM   2018  C   GLY A 285      43.800  36.200  11.599  1.00  6.62           C  
ATOM   2019  O   GLY A 285      43.423  37.301  11.982  1.00  7.79           O  
ATOM   2020  N   ASN A 286      45.084  35.920  11.370  1.00  5.48           N  
ATOM   2021  CA  ASN A 286      46.076  36.961  11.628  1.00  8.15           C  
ATOM   2022  C   ASN A 286      46.986  37.399  10.504  1.00  8.63           C  
ATOM   2023  O   ASN A 286      48.050  37.980  10.756  1.00 10.51           O  
ATOM   2024  CB  ASN A 286      46.916  36.627  12.873  1.00  8.08           C  
ATOM   2025  CG  ASN A 286      47.708  35.340  12.741  1.00 10.87           C  
ATOM   2026  OD1 ASN A 286      47.959  34.846  11.644  1.00 12.24           O  
ATOM   2027  ND2 ASN A 286      48.123  34.796  13.884  1.00 12.34           N  
ATOM   2028  N   ASP A 287      46.592  37.114   9.271  1.00  7.48           N  
ATOM   2029  CA  ASP A 287      47.351  37.585   8.116  1.00  9.63           C  
ATOM   2030  C   ASP A 287      46.356  37.819   6.979  1.00  9.05           C  
ATOM   2031  O   ASP A 287      45.164  37.652   7.175  1.00  7.97           O  
ATOM   2032  CB  ASP A 287      48.495  36.627   7.719  1.00  8.23           C  
ATOM   2033  CG  ASP A 287      48.013  35.247   7.298  1.00  9.71           C  
ATOM   2034  OD1 ASP A 287      46.972  35.163   6.623  1.00  9.63           O  
ATOM   2035  OD2 ASP A 287      48.710  34.252   7.616  1.00  9.78           O  
ATOM   2036  N   GLN A 288      46.833  38.240   5.811  1.00  9.44           N  
ATOM   2037  CA  GLN A 288      45.925  38.530   4.686  1.00 12.12           C  
ATOM   2038  C   GLN A 288      46.021  37.484   3.582  1.00  9.73           C  
ATOM   2039  O   GLN A 288      45.599  37.732   2.451  1.00 11.33           O  
ATOM   2040  CB  GLN A 288      46.284  39.882   4.046  1.00 15.77           C  
ATOM   2041  CG  GLN A 288      46.613  41.022   4.974  1.00 23.19           C  
ATOM   2042  CD  GLN A 288      47.506  42.054   4.268  1.00 27.14           C  
ATOM   2043  OE1 GLN A 288      47.192  42.520   3.166  1.00 27.53           O  
ATOM   2044  NE2 GLN A 288      48.625  42.397   4.899  1.00 29.46           N  
ATOM   2045  N   ARG A 289      46.557  36.312   3.893  1.00  7.24           N  
ATOM   2046  CA  ARG A 289      46.749  35.306   2.860  1.00  9.02           C  
ATOM   2047  C   ARG A 289      45.486  34.722   2.250  1.00  8.65           C  
ATOM   2048  O   ARG A 289      45.430  34.476   1.046  1.00  7.52           O  
ATOM   2049  CB  ARG A 289      47.637  34.169   3.386  1.00  8.72           C  
ATOM   2050  CG  ARG A 289      48.241  33.344   2.256  1.00 12.80           C  
ATOM   2051  CD  ARG A 289      49.235  32.310   2.756  1.00 17.75           C  
ATOM   2052  NE  ARG A 289      49.960  31.685   1.648  1.00 17.98           N  
ATOM   2053  CZ  ARG A 289      51.013  32.229   1.043  1.00 20.16           C  
ATOM   2054  NH1 ARG A 289      51.476  33.410   1.444  1.00 18.62           N  
ATOM   2055  NH2 ARG A 289      51.602  31.599   0.032  1.00 19.63           N  
ATOM   2056  N   PHE A 290      44.480  34.480   3.086  1.00  7.07           N  
ATOM   2057  CA  PHE A 290      43.213  33.904   2.619  1.00  7.59           C  
ATOM   2058  C   PHE A 290      42.091  34.437   3.504  1.00  6.18           C  
ATOM   2059  O   PHE A 290      42.344  35.090   4.506  1.00  7.25           O  
ATOM   2060  CB  PHE A 290      43.173  32.376   2.813  1.00  6.64           C  
ATOM   2061  CG  PHE A 290      44.366  31.641   2.291  1.00  7.43           C  
ATOM   2062  CD1 PHE A 290      44.495  31.385   0.925  1.00  8.91           C  
ATOM   2063  CD2 PHE A 290      45.324  31.130   3.167  1.00  6.97           C  
ATOM   2064  CE1 PHE A 290      45.547  30.633   0.438  1.00 10.00           C  
ATOM   2065  CE2 PHE A 290      46.395  30.366   2.689  1.00  7.11           C  
ATOM   2066  CZ  PHE A 290      46.508  30.114   1.315  1.00 10.62           C  
ATOM   2067  N   GLY A 291      40.851  34.125   3.131  1.00  6.98           N  
ATOM   2068  CA  GLY A 291      39.721  34.507   3.963  1.00  5.29           C  
ATOM   2069  C   GLY A 291      39.611  33.385   4.996  1.00  6.09           C  
ATOM   2070  O   GLY A 291      39.816  32.208   4.670  1.00  4.90           O  
ATOM   2071  N   TYR A 292      39.292  33.751   6.234  1.00  5.43           N  
ATOM   2072  CA  TYR A 292      39.203  32.810   7.337  1.00  5.07           C  
ATOM   2073  C   TYR A 292      37.860  32.866   8.039  1.00  5.02           C  
ATOM   2074  O   TYR A 292      37.114  33.823   7.874  1.00  4.74           O  
ATOM   2075  CB  TYR A 292      40.292  33.146   8.343  1.00  3.66           C  
ATOM   2076  CG  TYR A 292      41.679  33.125   7.743  1.00  4.84           C  
ATOM   2077  CD1 TYR A 292      42.174  31.964   7.139  1.00  3.92           C  
ATOM   2078  CD2 TYR A 292      42.506  34.249   7.818  1.00  3.18           C  
ATOM   2079  CE1 TYR A 292      43.480  31.907   6.625  1.00  4.20           C  
ATOM   2080  CE2 TYR A 292      43.801  34.214   7.309  1.00  4.79           C  
ATOM   2081  CZ  TYR A 292      44.285  33.042   6.719  1.00  4.80           C  
ATOM   2082  OH  TYR A 292      45.580  33.011   6.254  1.00  5.22           O  
ATOM   2083  N   GLY A 293      37.562  31.839   8.838  1.00  3.09           N  
ATOM   2084  CA  GLY A 293      36.303  31.800   9.566  1.00  4.25           C  
ATOM   2085  C   GLY A 293      36.527  31.331  10.999  1.00  5.57           C  
ATOM   2086  O   GLY A 293      37.639  30.906  11.332  1.00  6.89           O  
ATOM   2087  N   GLY A 294      35.506  31.354  11.856  1.00  5.00           N  
ATOM   2088  CA  GLY A 294      34.167  31.780  11.497  1.00  4.31           C  
ATOM   2089  C   GLY A 294      33.206  30.633  11.788  1.00  3.75           C  
ATOM   2090  O   GLY A 294      33.629  29.494  11.945  1.00  4.45           O  
ATOM   2091  N   MET A 295      31.916  30.938  11.879  1.00  4.19           N  
ATOM   2092  CA  MET A 295      30.887  29.924  12.145  1.00  3.52           C  
ATOM   2093  C   MET A 295      29.702  30.119  11.209  1.00  2.72           C  
ATOM   2094  O   MET A 295      29.236  31.255  11.038  1.00  3.22           O  
ATOM   2095  CB  MET A 295      30.353  30.043  13.575  1.00  3.84           C  
ATOM   2096  CG  MET A 295      31.287  29.522  14.650  1.00  2.97           C  
ATOM   2097  SD  MET A 295      30.547  29.606  16.319  1.00  6.68           S  
ATOM   2098  CE  MET A 295      29.312  28.316  16.240  1.00  9.03           C  
ATOM   2099  N   PHE A 296      29.189  29.029  10.629  1.00  2.68           N  
ATOM   2100  CA  PHE A 296      27.985  29.130   9.772  1.00  2.64           C  
ATOM   2101  C   PHE A 296      26.977  28.249  10.510  1.00  4.06           C  
ATOM   2102  O   PHE A 296      27.240  27.069  10.779  1.00  3.39           O  
ATOM   2103  CB  PHE A 296      28.231  28.592   8.358  1.00  3.53           C  
ATOM   2104  CG  PHE A 296      27.335  29.207   7.308  1.00  2.80           C  
ATOM   2105  CD1 PHE A 296      25.976  28.928   7.270  1.00  5.00           C  
ATOM   2106  CD2 PHE A 296      27.875  30.062   6.345  1.00  3.95           C  
ATOM   2107  CE1 PHE A 296      25.156  29.498   6.276  1.00  4.12           C  
ATOM   2108  CE2 PHE A 296      27.079  30.632   5.358  1.00  5.94           C  
ATOM   2109  CZ  PHE A 296      25.715  30.352   5.322  1.00  4.15           C  
ATOM   2110  N   VAL A 297      25.835  28.843  10.844  1.00  4.04           N  
ATOM   2111  CA  VAL A 297      24.815  28.176  11.652  1.00  5.36           C  
ATOM   2112  C   VAL A 297      23.459  27.953  10.989  1.00  5.72           C  
ATOM   2113  O   VAL A 297      22.858  28.891  10.481  1.00  5.36           O  
ATOM   2114  CB  VAL A 297      24.584  29.000  12.956  1.00  6.45           C  
ATOM   2115  CG1 VAL A 297      23.473  28.374  13.817  1.00  6.96           C  
ATOM   2116  CG2 VAL A 297      25.869  29.088  13.762  1.00  7.64           C  
ATOM   2117  N   TRP A 298      23.017  26.698  10.981  1.00  4.95           N  
ATOM   2118  CA  TRP A 298      21.708  26.297  10.470  1.00  4.43           C  
ATOM   2119  C   TRP A 298      20.940  25.823  11.699  1.00  4.27           C  
ATOM   2120  O   TRP A 298      21.551  25.405  12.686  1.00  4.65           O  
ATOM   2121  CB  TRP A 298      21.828  25.093   9.538  1.00  3.46           C  
ATOM   2122  CG  TRP A 298      22.394  25.352   8.174  1.00  4.64           C  
ATOM   2123  CD1 TRP A 298      21.685  25.374   6.993  1.00  4.00           C  
ATOM   2124  CD2 TRP A 298      23.783  25.429   7.808  1.00  3.60           C  
ATOM   2125  NE1 TRP A 298      22.554  25.444   5.929  1.00  4.29           N  
ATOM   2126  CE2 TRP A 298      23.841  25.478   6.398  1.00  5.11           C  
ATOM   2127  CE3 TRP A 298      24.989  25.447   8.536  1.00  3.53           C  
ATOM   2128  CZ2 TRP A 298      25.058  25.536   5.695  1.00  3.06           C  
ATOM   2129  CZ3 TRP A 298      26.199  25.505   7.830  1.00  5.85           C  
ATOM   2130  CH2 TRP A 298      26.217  25.549   6.429  1.00  3.34           C  
ATOM   2131  N   GLY A 299      19.608  25.864  11.658  1.00  4.21           N  
ATOM   2132  CA  GLY A 299      18.857  25.357  12.791  1.00  4.06           C  
ATOM   2133  C   GLY A 299      18.593  26.261  13.979  1.00  5.42           C  
ATOM   2134  O   GLY A 299      19.066  27.390  14.034  1.00  5.80           O  
ATOM   2135  N   SER A 300      17.849  25.731  14.950  1.00  5.11           N  
ATOM   2136  CA  SER A 300      17.451  26.487  16.133  1.00  4.71           C  
ATOM   2137  C   SER A 300      17.855  25.912  17.484  1.00  6.24           C  
ATOM   2138  O   SER A 300      18.428  24.814  17.583  1.00  5.63           O  
ATOM   2139  CB  SER A 300      15.925  26.657  16.124  1.00  6.48           C  
ATOM   2140  OG  SER A 300      15.282  25.394  16.155  1.00  5.34           O  
ATOM   2141  N   ARG A 301      17.528  26.687  18.523  1.00  5.50           N  
ATOM   2142  CA  ARG A 301      17.759  26.338  19.927  1.00  6.70           C  
ATOM   2143  C   ARG A 301      19.225  26.197  20.344  1.00  6.52           C  
ATOM   2144  O   ARG A 301      19.535  25.589  21.367  1.00  6.80           O  
ATOM   2145  CB  ARG A 301      16.987  25.053  20.277  1.00  8.67           C  
ATOM   2146  CG  ARG A 301      15.472  25.153  20.044  1.00 11.97           C  
ATOM   2147  CD  ARG A 301      14.686  24.030  20.747  1.00 16.67           C  
ATOM   2148  NE  ARG A 301      14.881  22.730  20.111  1.00 19.85           N  
ATOM   2149  CZ  ARG A 301      15.438  21.659  20.682  1.00 22.14           C  
ATOM   2150  NH1 ARG A 301      15.871  21.695  21.943  1.00 21.53           N  
ATOM   2151  NH2 ARG A 301      15.554  20.537  19.974  1.00 20.01           N  
ATOM   2152  N   HIS A 302      20.118  26.815  19.582  1.00  6.56           N  
ATOM   2153  CA  HIS A 302      21.548  26.721  19.875  1.00  5.66           C  
ATOM   2154  C   HIS A 302      21.973  27.651  20.999  1.00  5.74           C  
ATOM   2155  O   HIS A 302      21.248  28.575  21.377  1.00  5.68           O  
ATOM   2156  CB  HIS A 302      22.359  27.074  18.625  1.00  6.03           C  
ATOM   2157  CG  HIS A 302      22.018  26.242  17.431  1.00  4.04           C  
ATOM   2158  ND1 HIS A 302      22.022  24.867  17.458  1.00  3.12           N  
ATOM   2159  CD2 HIS A 302      21.674  26.593  16.167  1.00  3.63           C  
ATOM   2160  CE1 HIS A 302      21.698  24.403  16.263  1.00  3.14           C  
ATOM   2161  NE2 HIS A 302      21.483  25.433  15.461  1.00  5.12           N  
ATOM   2162  N   VAL A 303      23.159  27.376  21.530  1.00  6.07           N  
ATOM   2163  CA  VAL A 303      23.768  28.211  22.560  1.00  5.20           C  
ATOM   2164  C   VAL A 303      25.162  28.521  22.014  1.00  4.16           C  
ATOM   2165  O   VAL A 303      26.028  27.647  21.937  1.00  5.93           O  
ATOM   2166  CB  VAL A 303      23.839  27.462  23.895  1.00  5.58           C  
ATOM   2167  CG1 VAL A 303      24.522  28.320  24.951  1.00  8.66           C  
ATOM   2168  CG2 VAL A 303      22.428  27.126  24.351  1.00  5.87           C  
ATOM   2169  N   ILE A 304      25.368  29.770  21.617  1.00  4.63           N  
ATOM   2170  CA  ILE A 304      26.640  30.225  21.035  1.00  3.62           C  
ATOM   2171  C   ILE A 304      27.071  31.355  21.957  1.00  4.77           C  
ATOM   2172  O   ILE A 304      26.541  32.473  21.881  1.00  5.16           O  
ATOM   2173  CB  ILE A 304      26.392  30.755  19.617  1.00  5.67           C  
ATOM   2174  CG1 ILE A 304      25.804  29.628  18.758  1.00  6.60           C  
ATOM   2175  CG2 ILE A 304      27.673  31.340  19.036  1.00  5.05           C  
ATOM   2176  CD1 ILE A 304      25.369  30.057  17.346  1.00  7.68           C  
ATOM   2177  N   ALA A 305      28.019  31.046  22.838  1.00  3.98           N  
ATOM   2178  CA  ALA A 305      28.440  31.994  23.872  1.00  4.87           C  
ATOM   2179  C   ALA A 305      29.927  32.017  24.163  1.00  6.07           C  
ATOM   2180  O   ALA A 305      30.627  31.025  23.980  1.00  5.17           O  
ATOM   2181  CB  ALA A 305      27.698  31.668  25.169  1.00  4.57           C  
ATOM   2182  N   CYS A 306      30.388  33.176  24.621  1.00  5.84           N  
ATOM   2183  CA  CYS A 306      31.781  33.398  25.002  1.00  6.05           C  
ATOM   2184  C   CYS A 306      32.824  33.039  23.953  1.00  5.80           C  
ATOM   2185  O   CYS A 306      33.950  32.682  24.298  1.00  5.18           O  
ATOM   2186  CB  CYS A 306      32.073  32.650  26.311  1.00  7.20           C  
ATOM   2187  SG  CYS A 306      30.811  33.035  27.561  1.00  8.43           S  
ATOM   2188  N   ASN A 307      32.452  33.118  22.683  1.00  5.89           N  
ATOM   2189  CA  ASN A 307      33.384  32.830  21.603  1.00  4.66           C  
ATOM   2190  C   ASN A 307      34.056  34.143  21.244  1.00  5.85           C  
ATOM   2191  O   ASN A 307      33.442  35.209  21.340  1.00  6.19           O  
ATOM   2192  CB  ASN A 307      32.632  32.280  20.387  1.00  5.46           C  
ATOM   2193  CG  ASN A 307      31.983  30.944  20.666  1.00  5.07           C  
ATOM   2194  OD1 ASN A 307      32.669  29.920  20.818  1.00  5.11           O  
ATOM   2195  ND2 ASN A 307      30.646  30.938  20.742  1.00  4.38           N  
ATOM   2196  N   TYR A 308      35.309  34.050  20.809  1.00  4.36           N  
ATOM   2197  CA  TYR A 308      36.109  35.210  20.444  1.00  5.87           C  
ATOM   2198  C   TYR A 308      36.442  35.132  18.959  1.00  5.80           C  
ATOM   2199  O   TYR A 308      37.007  34.129  18.495  1.00  4.82           O  
ATOM   2200  CB  TYR A 308      37.382  35.204  21.288  1.00  5.93           C  
ATOM   2201  CG  TYR A 308      38.290  36.373  21.051  1.00  8.07           C  
ATOM   2202  CD1 TYR A 308      39.281  36.333  20.069  1.00  9.36           C  
ATOM   2203  CD2 TYR A 308      38.151  37.531  21.811  1.00 10.74           C  
ATOM   2204  CE1 TYR A 308      40.118  37.429  19.847  1.00 11.81           C  
ATOM   2205  CE2 TYR A 308      38.971  38.621  21.602  1.00  9.46           C  
ATOM   2206  CZ  TYR A 308      39.945  38.569  20.628  1.00 11.07           C  
ATOM   2207  OH  TYR A 308      40.737  39.669  20.430  1.00 11.77           O  
ATOM   2208  N   PHE A 309      36.062  36.175  18.222  1.00  4.27           N  
ATOM   2209  CA  PHE A 309      36.286  36.251  16.775  1.00  5.58           C  
ATOM   2210  C   PHE A 309      37.154  37.460  16.451  1.00  6.10           C  
ATOM   2211  O   PHE A 309      36.733  38.601  16.691  1.00  6.63           O  
ATOM   2212  CB  PHE A 309      34.965  36.450  15.996  1.00  4.10           C  
ATOM   2213  CG  PHE A 309      33.935  35.354  16.190  1.00  4.99           C  
ATOM   2214  CD1 PHE A 309      33.082  35.367  17.291  1.00  5.06           C  
ATOM   2215  CD2 PHE A 309      33.782  34.348  15.231  1.00  5.09           C  
ATOM   2216  CE1 PHE A 309      32.083  34.399  17.439  1.00  4.10           C  
ATOM   2217  CE2 PHE A 309      32.772  33.358  15.369  1.00  4.56           C  
ATOM   2218  CZ  PHE A 309      31.934  33.388  16.461  1.00  5.63           C  
ATOM   2219  N   GLU A 310      38.348  37.219  15.916  1.00  6.18           N  
ATOM   2220  CA  GLU A 310      39.237  38.306  15.494  1.00  5.47           C  
ATOM   2221  C   GLU A 310      39.800  37.813  14.177  1.00  5.99           C  
ATOM   2222  O   GLU A 310      40.788  37.086  14.151  1.00  5.66           O  
ATOM   2223  CB  GLU A 310      40.358  38.569  16.511  1.00  6.52           C  
ATOM   2224  CG  GLU A 310      41.248  39.738  16.067  1.00  8.05           C  
ATOM   2225  CD  GLU A 310      42.153  40.268  17.179  1.00 12.53           C  
ATOM   2226  OE1 GLU A 310      42.202  39.667  18.277  1.00 16.67           O  
ATOM   2227  OE2 GLU A 310      42.820  41.304  16.943  1.00 11.96           O  
ATOM   2228  N   LEU A 311      39.135  38.202  13.088  1.00  6.36           N  
ATOM   2229  CA  LEU A 311      39.480  37.730  11.745  1.00  5.86           C  
ATOM   2230  C   LEU A 311      39.976  38.822  10.799  1.00  6.41           C  
ATOM   2231  O   LEU A 311      39.199  39.663  10.338  1.00  6.18           O  
ATOM   2232  CB  LEU A 311      38.243  37.037  11.128  1.00  5.20           C  
ATOM   2233  CG  LEU A 311      37.686  35.810  11.861  1.00  5.60           C  
ATOM   2234  CD1 LEU A 311      36.279  35.463  11.326  1.00  5.82           C  
ATOM   2235  CD2 LEU A 311      38.639  34.611  11.659  1.00  5.92           C  
ATOM   2236  N   SER A 312      41.273  38.784  10.504  1.00  6.86           N  
ATOM   2237  CA  SER A 312      41.922  39.763   9.632  1.00  8.19           C  
ATOM   2238  C   SER A 312      41.374  39.779   8.206  1.00  8.37           C  
ATOM   2239  O   SER A 312      41.507  40.775   7.487  1.00  8.57           O  
ATOM   2240  CB  SER A 312      43.427  39.492   9.611  1.00  9.95           C  
ATOM   2241  OG  SER A 312      43.672  38.155   9.208  1.00 15.08           O  
ATOM   2242  N   GLU A 313      40.786  38.662   7.789  1.00  7.23           N  
ATOM   2243  CA  GLU A 313      40.171  38.533   6.472  1.00  7.24           C  
ATOM   2244  C   GLU A 313      39.042  37.514   6.619  1.00  6.81           C  
ATOM   2245  O   GLU A 313      39.201  36.506   7.325  1.00  5.29           O  
ATOM   2246  CB  GLU A 313      41.139  37.977   5.426  1.00 10.34           C  
ATOM   2247  CG  GLU A 313      42.297  38.860   5.028  1.00 15.10           C  
ATOM   2248  CD  GLU A 313      41.893  40.071   4.202  1.00 17.00           C  
ATOM   2249  OE1 GLU A 313      40.756  40.126   3.671  1.00 14.31           O  
ATOM   2250  OE2 GLU A 313      42.755  40.969   4.081  1.00 19.29           O  
ATOM   2251  N   THR A 314      37.915  37.767   5.957  1.00  6.20           N  
ATOM   2252  CA  THR A 314      36.803  36.826   6.013  1.00  6.16           C  
ATOM   2253  C   THR A 314      36.578  36.215   4.636  1.00  6.78           C  
ATOM   2254  O   THR A 314      37.203  36.615   3.646  1.00  6.38           O  
ATOM   2255  CB  THR A 314      35.526  37.475   6.545  1.00  5.48           C  
ATOM   2256  OG1 THR A 314      35.250  38.670   5.807  1.00  6.63           O  
ATOM   2257  CG2 THR A 314      35.699  37.820   8.023  1.00  6.11           C  
ATOM   2258  N   ILE A 315      35.683  35.241   4.575  1.00  5.36           N  
ATOM   2259  CA  ILE A 315      35.459  34.493   3.354  1.00  5.84           C  
ATOM   2260  C   ILE A 315      34.443  35.089   2.379  1.00  5.52           C  
ATOM   2261  O   ILE A 315      33.234  35.098   2.637  1.00  7.39           O  
ATOM   2262  CB  ILE A 315      35.052  33.061   3.714  1.00  4.38           C  
ATOM   2263  CG1 ILE A 315      36.090  32.449   4.667  1.00  5.75           C  
ATOM   2264  CG2 ILE A 315      34.954  32.219   2.439  1.00  4.76           C  
ATOM   2265  CD1 ILE A 315      35.631  31.159   5.331  1.00  6.10           C  
ATOM   2266  N   LYS A 316      34.943  35.566   1.240  1.00  6.42           N  
ATOM   2267  CA  LYS A 316      34.074  36.172   0.243  1.00  8.83           C  
ATOM   2268  C   LYS A 316      32.898  35.308  -0.193  1.00  8.46           C  
ATOM   2269  O   LYS A 316      31.764  35.776  -0.207  1.00 10.29           O  
ATOM   2270  CB  LYS A 316      34.877  36.567  -1.006  1.00 11.13           C  
ATOM   2271  CG  LYS A 316      34.027  37.204  -2.118  1.00 17.50           C  
ATOM   2272  CD  LYS A 316      34.852  37.365  -3.395  1.00 22.10           C  
ATOM   2273  CE  LYS A 316      34.033  37.913  -4.561  1.00 25.80           C  
ATOM   2274  NZ  LYS A 316      34.900  38.028  -5.788  1.00 26.88           N  
ATOM   2275  N   SER A 317      33.153  34.041  -0.508  1.00  7.24           N  
ATOM   2276  CA  SER A 317      32.095  33.172  -1.007  1.00  7.61           C  
ATOM   2277  C   SER A 317      30.923  32.960  -0.045  1.00  9.04           C  
ATOM   2278  O   SER A 317      29.798  32.698  -0.485  1.00  8.74           O  
ATOM   2279  CB  SER A 317      32.677  31.815  -1.443  1.00  8.57           C  
ATOM   2280  OG  SER A 317      32.913  30.959  -0.334  1.00  7.79           O  
ATOM   2281  N   ARG A 318      31.184  33.090   1.256  1.00  6.97           N  
ATOM   2282  CA  ARG A 318      30.150  32.894   2.267  1.00  6.07           C  
ATOM   2283  C   ARG A 318      29.400  34.185   2.594  1.00  6.40           C  
ATOM   2284  O   ARG A 318      28.287  34.139   3.120  1.00  6.50           O  
ATOM   2285  CB  ARG A 318      30.759  32.364   3.575  1.00  6.29           C  
ATOM   2286  CG  ARG A 318      31.538  31.054   3.498  1.00  7.07           C  
ATOM   2287  CD  ARG A 318      30.689  29.952   2.933  1.00  6.96           C  
ATOM   2288  NE  ARG A 318      30.873  29.892   1.487  1.00 10.01           N  
ATOM   2289  CZ  ARG A 318      30.257  29.010   0.706  1.00 14.69           C  
ATOM   2290  NH1 ARG A 318      29.417  28.129   1.244  1.00 12.34           N  
ATOM   2291  NH2 ARG A 318      30.493  28.999  -0.605  1.00 11.84           N  
ATOM   2292  N   GLY A 319      30.027  35.327   2.321  1.00  5.62           N  
ATOM   2293  CA  GLY A 319      29.426  36.614   2.614  1.00  6.58           C  
ATOM   2294  C   GLY A 319      30.283  37.559   3.457  1.00  6.32           C  
ATOM   2295  O   GLY A 319      29.780  38.574   3.912  1.00  7.97           O  
ATOM   2296  N   ASN A 320      31.555  37.226   3.685  1.00  5.26           N  
ATOM   2297  CA  ASN A 320      32.497  38.066   4.472  1.00  5.90           C  
ATOM   2298  C   ASN A 320      32.057  38.407   5.894  1.00  6.04           C  
ATOM   2299  O   ASN A 320      31.800  39.579   6.215  1.00  5.82           O  
ATOM   2300  CB  ASN A 320      32.802  39.377   3.733  1.00  6.85           C  
ATOM   2301  CG  ASN A 320      33.741  39.183   2.556  1.00  8.04           C  
ATOM   2302  OD1 ASN A 320      34.929  38.881   2.731  1.00  9.47           O  
ATOM   2303  ND2 ASN A 320      33.218  39.360   1.346  1.00  3.96           N  
ATOM   2304  N   ALA A 321      31.971  37.398   6.754  1.00  4.99           N  
ATOM   2305  CA  ALA A 321      31.550  37.631   8.128  1.00  4.99           C  
ATOM   2306  C   ALA A 321      32.196  36.670   9.114  1.00  4.92           C  
ATOM   2307  O   ALA A 321      32.850  35.704   8.715  1.00  5.56           O  
ATOM   2308  CB  ALA A 321      30.012  37.530   8.229  1.00  5.94           C  
ATOM   2309  N   ALA A 322      32.016  36.952  10.406  1.00  4.87           N  
ATOM   2310  CA  ALA A 322      32.523  36.098  11.470  1.00  3.62           C  
ATOM   2311  C   ALA A 322      31.485  35.023  11.792  1.00  4.18           C  
ATOM   2312  O   ALA A 322      31.810  33.832  11.831  1.00  4.31           O  
ATOM   2313  CB  ALA A 322      32.815  36.932  12.731  1.00  3.05           C  
ATOM   2314  N   LEU A 323      30.243  35.453  12.019  1.00  3.66           N  
ATOM   2315  CA  LEU A 323      29.136  34.552  12.331  1.00  4.94           C  
ATOM   2316  C   LEU A 323      28.060  34.678  11.249  1.00  6.01           C  
ATOM   2317  O   LEU A 323      27.523  35.761  11.019  1.00  3.96           O  
ATOM   2318  CB  LEU A 323      28.536  34.899  13.708  1.00  5.50           C  
ATOM   2319  CG  LEU A 323      27.273  34.137  14.136  1.00  6.01           C  
ATOM   2320  CD1 LEU A 323      27.556  32.645  14.270  1.00  6.41           C  
ATOM   2321  CD2 LEU A 323      26.756  34.701  15.442  1.00  5.65           C  
ATOM   2322  N   TYR A 324      27.763  33.566  10.588  1.00  5.23           N  
ATOM   2323  CA  TYR A 324      26.769  33.526   9.509  1.00  5.46           C  
ATOM   2324  C   TYR A 324      25.511  32.792   9.971  1.00  6.04           C  
ATOM   2325  O   TYR A 324      25.593  31.619  10.331  1.00  3.73           O  
ATOM   2326  CB  TYR A 324      27.333  32.759   8.313  1.00  3.62           C  
ATOM   2327  CG  TYR A 324      28.620  33.303   7.729  1.00  3.92           C  
ATOM   2328  CD1 TYR A 324      28.584  34.240   6.692  1.00  3.22           C  
ATOM   2329  CD2 TYR A 324      29.870  32.835   8.163  1.00  5.10           C  
ATOM   2330  CE1 TYR A 324      29.758  34.699   6.083  1.00  5.14           C  
ATOM   2331  CE2 TYR A 324      31.052  33.289   7.557  1.00  4.63           C  
ATOM   2332  CZ  TYR A 324      30.985  34.212   6.518  1.00  3.46           C  
ATOM   2333  OH  TYR A 324      32.144  34.595   5.871  1.00  4.27           O  
ATOM   2334  N   LEU A 325      24.352  33.456   9.919  1.00  6.05           N  
ATOM   2335  CA  LEU A 325      23.103  32.833  10.361  1.00  5.05           C  
ATOM   2336  C   LEU A 325      22.264  32.484   9.143  1.00  5.50           C  
ATOM   2337  O   LEU A 325      21.775  33.348   8.415  1.00  5.64           O  
ATOM   2338  CB  LEU A 325      22.354  33.770  11.321  1.00  5.06           C  
ATOM   2339  CG  LEU A 325      23.176  34.161  12.560  1.00  6.99           C  
ATOM   2340  CD1 LEU A 325      22.319  34.999  13.505  1.00  5.90           C  
ATOM   2341  CD2 LEU A 325      23.688  32.929  13.274  1.00  4.52           C  
ATOM   2342  N   ASN A 326      22.086  31.188   8.940  1.00  4.02           N  
ATOM   2343  CA  ASN A 326      21.388  30.694   7.764  1.00  4.36           C  
ATOM   2344  C   ASN A 326      19.935  31.034   7.517  1.00  3.55           C  
ATOM   2345  O   ASN A 326      19.089  30.816   8.386  1.00  5.18           O  
ATOM   2346  CB  ASN A 326      21.466  29.164   7.719  1.00  4.17           C  
ATOM   2347  CG  ASN A 326      20.920  28.610   6.418  1.00  2.93           C  
ATOM   2348  OD1 ASN A 326      21.514  28.826   5.364  1.00  4.44           O  
ATOM   2349  ND2 ASN A 326      19.775  27.918   6.478  1.00  3.85           N  
ATOM   2350  N   PRO A 327      19.622  31.564   6.322  1.00  4.65           N  
ATOM   2351  CA  PRO A 327      18.227  31.885   5.986  1.00  5.23           C  
ATOM   2352  C   PRO A 327      17.687  30.663   5.235  1.00  6.16           C  
ATOM   2353  O   PRO A 327      18.453  29.931   4.603  1.00  6.52           O  
ATOM   2354  CB  PRO A 327      18.350  33.095   5.069  1.00  4.73           C  
ATOM   2355  CG  PRO A 327      19.592  32.766   4.271  1.00  3.66           C  
ATOM   2356  CD  PRO A 327      20.555  32.222   5.377  1.00  4.14           C  
ATOM   2357  N   GLY A 328      16.382  30.444   5.272  1.00  6.81           N  
ATOM   2358  CA  GLY A 328      15.847  29.283   4.569  1.00  7.73           C  
ATOM   2359  C   GLY A 328      14.559  28.773   5.178  1.00  5.71           C  
ATOM   2360  O   GLY A 328      13.869  29.505   5.876  1.00  7.95           O  
ATOM   2361  N   ALA A 329      14.249  27.509   4.910  1.00  6.05           N  
ATOM   2362  CA  ALA A 329      13.029  26.888   5.408  1.00  6.06           C  
ATOM   2363  C   ALA A 329      13.285  26.186   6.732  1.00  7.49           C  
ATOM   2364  O   ALA A 329      14.306  25.503   6.910  1.00  6.85           O  
ATOM   2365  CB  ALA A 329      12.491  25.898   4.381  1.00  6.34           C  
ATOM   2366  N   MET A 330      12.342  26.355   7.653  1.00  6.67           N  
ATOM   2367  CA  MET A 330      12.469  25.781   8.981  1.00  8.31           C  
ATOM   2368  C   MET A 330      12.603  24.270   8.943  1.00  8.69           C  
ATOM   2369  O   MET A 330      11.869  23.578   8.223  1.00  7.91           O  
ATOM   2370  CB  MET A 330      11.264  26.180   9.839  1.00 10.96           C  
ATOM   2371  CG  MET A 330      11.405  25.753  11.285  1.00 13.39           C  
ATOM   2372  SD  MET A 330      10.004  26.285  12.292  1.00 23.03           S  
ATOM   2373  CE  MET A 330       9.586  27.834  11.511  1.00 15.31           C  
ATOM   2374  N   ALA A 331      13.583  23.778   9.697  1.00  8.32           N  
ATOM   2375  CA  ALA A 331      13.861  22.351   9.824  1.00  9.61           C  
ATOM   2376  C   ALA A 331      14.047  21.592   8.518  1.00  9.08           C  
ATOM   2377  O   ALA A 331      13.758  20.392   8.463  1.00  9.34           O  
ATOM   2378  CB  ALA A 331      12.759  21.694  10.644  1.00 10.84           C  
ATOM   2379  N   SER A 332      14.545  22.264   7.479  1.00  7.95           N  
ATOM   2380  CA  SER A 332      14.743  21.627   6.181  1.00  7.98           C  
ATOM   2381  C   SER A 332      16.191  21.169   6.035  1.00  9.04           C  
ATOM   2382  O   SER A 332      16.933  21.155   7.012  1.00  7.07           O  
ATOM   2383  CB  SER A 332      14.422  22.611   5.055  1.00  9.89           C  
ATOM   2384  OG  SER A 332      15.376  23.662   5.017  1.00  7.95           O  
ATOM   2385  N   GLU A 333      16.570  20.801   4.807  1.00  8.65           N  
ATOM   2386  CA  GLU A 333      17.921  20.363   4.475  1.00 10.34           C  
ATOM   2387  C   GLU A 333      18.885  21.546   4.674  1.00  8.96           C  
ATOM   2388  O   GLU A 333      20.078  21.360   4.816  1.00  7.17           O  
ATOM   2389  CB  GLU A 333      17.956  19.885   3.016  1.00 15.30           C  
ATOM   2390  CG  GLU A 333      19.352  19.555   2.471  1.00 22.52           C  
ATOM   2391  CD  GLU A 333      19.968  18.301   3.100  1.00 24.94           C  
ATOM   2392  OE1 GLU A 333      19.257  17.576   3.829  1.00 28.50           O  
ATOM   2393  OE2 GLU A 333      21.164  18.036   2.857  1.00 28.33           O  
ATOM   2394  N   HIS A 334      18.347  22.759   4.646  1.00  8.46           N  
ATOM   2395  CA  HIS A 334      19.134  23.978   4.890  1.00  6.66           C  
ATOM   2396  C   HIS A 334      18.274  24.733   5.892  1.00  5.98           C  
ATOM   2397  O   HIS A 334      17.698  25.794   5.608  1.00  5.30           O  
ATOM   2398  CB  HIS A 334      19.323  24.778   3.596  1.00  6.69           C  
ATOM   2399  CG  HIS A 334      20.491  24.316   2.781  1.00  7.59           C  
ATOM   2400  ND1 HIS A 334      21.793  24.477   3.198  1.00  8.78           N  
ATOM   2401  CD2 HIS A 334      20.554  23.683   1.586  1.00  8.27           C  
ATOM   2402  CE1 HIS A 334      22.611  23.962   2.296  1.00  8.26           C  
ATOM   2403  NE2 HIS A 334      21.883  23.473   1.307  1.00  8.56           N  
ATOM   2404  N   ALA A 335      18.204  24.161   7.092  1.00  6.00           N  
ATOM   2405  CA  ALA A 335      17.358  24.687   8.151  1.00  5.90           C  
ATOM   2406  C   ALA A 335      17.615  26.118   8.566  1.00  5.71           C  
ATOM   2407  O   ALA A 335      18.747  26.517   8.840  1.00  4.81           O  
ATOM   2408  CB  ALA A 335      17.440  23.778   9.374  1.00  5.43           C  
ATOM   2409  N   LEU A 336      16.523  26.873   8.618  1.00  4.09           N  
ATOM   2410  CA  LEU A 336      16.522  28.254   9.066  1.00  4.90           C  
ATOM   2411  C   LEU A 336      17.197  28.379  10.423  1.00  4.52           C  
ATOM   2412  O   LEU A 336      16.950  27.580  11.334  1.00  3.09           O  
ATOM   2413  CB  LEU A 336      15.075  28.734   9.225  1.00  3.31           C  
ATOM   2414  CG  LEU A 336      14.887  30.104   9.881  1.00  3.27           C  
ATOM   2415  CD1 LEU A 336      15.396  31.215   8.931  1.00  6.41           C  
ATOM   2416  CD2 LEU A 336      13.395  30.318  10.194  1.00  7.69           C  
ATOM   2417  N   ALA A 337      18.020  29.411  10.566  1.00  5.41           N  
ATOM   2418  CA  ALA A 337      18.670  29.683  11.834  1.00  4.84           C  
ATOM   2419  C   ALA A 337      17.736  30.645  12.575  1.00  5.75           C  
ATOM   2420  O   ALA A 337      17.528  31.774  12.112  1.00  5.91           O  
ATOM   2421  CB  ALA A 337      20.034  30.359  11.585  1.00  4.17           C  
ATOM   2422  N   PHE A 338      17.161  30.208  13.693  1.00  6.25           N  
ATOM   2423  CA  PHE A 338      16.266  31.063  14.486  1.00  6.19           C  
ATOM   2424  C   PHE A 338      16.158  30.541  15.930  1.00  6.57           C  
ATOM   2425  O   PHE A 338      16.656  29.458  16.245  1.00  7.12           O  
ATOM   2426  CB  PHE A 338      14.858  31.113  13.831  1.00  6.18           C  
ATOM   2427  CG  PHE A 338      14.020  29.868  14.071  1.00  8.21           C  
ATOM   2428  CD1 PHE A 338      14.319  28.659  13.430  1.00  6.86           C  
ATOM   2429  CD2 PHE A 338      12.937  29.915  14.946  1.00  7.51           C  
ATOM   2430  CE1 PHE A 338      13.532  27.503  13.669  1.00  9.00           C  
ATOM   2431  CE2 PHE A 338      12.156  28.782  15.192  1.00  8.60           C  
ATOM   2432  CZ  PHE A 338      12.457  27.570  14.549  1.00  7.87           C  
ATOM   2433  N   ASP A 339      15.547  31.332  16.814  1.00  5.42           N  
ATOM   2434  CA  ASP A 339      15.343  30.938  18.211  1.00  6.71           C  
ATOM   2435  C   ASP A 339      16.580  30.369  18.901  1.00  7.93           C  
ATOM   2436  O   ASP A 339      16.622  29.192  19.278  1.00  7.95           O  
ATOM   2437  CB  ASP A 339      14.174  29.941  18.284  1.00 10.32           C  
ATOM   2438  CG  ASP A 339      13.843  29.516  19.715  1.00 13.16           C  
ATOM   2439  OD1 ASP A 339      14.144  30.283  20.655  1.00 14.00           O  
ATOM   2440  OD2 ASP A 339      13.276  28.415  19.891  1.00 15.58           O  
ATOM   2441  N   MET A 340      17.597  31.207  19.071  1.00  6.51           N  
ATOM   2442  CA  MET A 340      18.813  30.754  19.738  1.00  6.83           C  
ATOM   2443  C   MET A 340      19.413  31.885  20.552  1.00  7.87           C  
ATOM   2444  O   MET A 340      19.051  33.058  20.379  1.00  8.24           O  
ATOM   2445  CB  MET A 340      19.842  30.258  18.708  1.00  6.66           C  
ATOM   2446  CG  MET A 340      20.474  31.371  17.877  1.00  6.21           C  
ATOM   2447  SD  MET A 340      21.537  30.678  16.572  1.00  7.29           S  
ATOM   2448  CE  MET A 340      20.287  30.120  15.425  1.00  7.54           C  
ATOM   2449  N   LEU A 341      20.339  31.520  21.432  1.00  7.34           N  
ATOM   2450  CA  LEU A 341      21.018  32.462  22.308  1.00  7.72           C  
ATOM   2451  C   LEU A 341      22.419  32.723  21.798  1.00  7.02           C  
ATOM   2452  O   LEU A 341      23.184  31.780  21.607  1.00  5.89           O  
ATOM   2453  CB  LEU A 341      21.116  31.876  23.710  1.00  6.78           C  
ATOM   2454  CG  LEU A 341      21.890  32.696  24.734  1.00 10.41           C  
ATOM   2455  CD1 LEU A 341      21.179  34.046  24.959  1.00  8.82           C  
ATOM   2456  CD2 LEU A 341      21.972  31.883  26.031  1.00 11.34           C  
ATOM   2457  N   ILE A 342      22.739  33.994  21.559  1.00  6.97           N  
ATOM   2458  CA  ILE A 342      24.067  34.410  21.091  1.00  6.13           C  
ATOM   2459  C   ILE A 342      24.461  35.361  22.210  1.00  7.47           C  
ATOM   2460  O   ILE A 342      24.009  36.515  22.260  1.00  5.46           O  
ATOM   2461  CB  ILE A 342      23.975  35.138  19.734  1.00  6.67           C  
ATOM   2462  CG1 ILE A 342      23.430  34.160  18.679  1.00  6.32           C  
ATOM   2463  CG2 ILE A 342      25.333  35.711  19.349  1.00  6.64           C  
ATOM   2464  CD1 ILE A 342      22.991  34.799  17.363  1.00  5.80           C  
ATOM   2465  N   ALA A 343      25.306  34.867  23.114  1.00  7.54           N  
ATOM   2466  CA  ALA A 343      25.662  35.638  24.297  1.00  7.72           C  
ATOM   2467  C   ALA A 343      27.118  35.720  24.684  1.00  7.82           C  
ATOM   2468  O   ALA A 343      27.874  34.758  24.555  1.00  6.71           O  
ATOM   2469  CB  ALA A 343      24.868  35.082  25.493  1.00  8.07           C  
ATOM   2470  N   ASN A 344      27.490  36.884  25.207  1.00  8.11           N  
ATOM   2471  CA  ASN A 344      28.833  37.122  25.711  1.00  7.13           C  
ATOM   2472  C   ASN A 344      29.975  36.843  24.756  1.00  7.67           C  
ATOM   2473  O   ASN A 344      31.096  36.589  25.190  1.00  7.35           O  
ATOM   2474  CB  ASN A 344      29.040  36.326  27.005  1.00  8.37           C  
ATOM   2475  CG  ASN A 344      28.097  36.763  28.102  1.00  9.55           C  
ATOM   2476  OD1 ASN A 344      27.552  37.866  28.040  1.00 12.24           O  
ATOM   2477  ND2 ASN A 344      27.895  35.912  29.103  1.00 10.15           N  
ATOM   2478  N   ASN A 345      29.716  36.911  23.454  1.00  7.27           N  
ATOM   2479  CA  ASN A 345      30.771  36.692  22.469  1.00  6.64           C  
ATOM   2480  C   ASN A 345      31.444  38.045  22.246  1.00  7.57           C  
ATOM   2481  O   ASN A 345      30.901  39.086  22.615  1.00  7.47           O  
ATOM   2482  CB  ASN A 345      30.188  36.226  21.115  1.00  6.66           C  
ATOM   2483  CG  ASN A 345      29.404  34.929  21.216  1.00  6.57           C  
ATOM   2484  OD1 ASN A 345      29.978  33.835  21.316  1.00  6.68           O  
ATOM   2485  ND2 ASN A 345      28.072  35.044  21.186  1.00  5.04           N  
ATOM   2486  N   ALA A 346      32.629  38.019  21.659  1.00  6.25           N  
ATOM   2487  CA  ALA A 346      33.350  39.238  21.346  1.00  6.78           C  
ATOM   2488  C   ALA A 346      33.816  39.145  19.893  1.00  6.80           C  
ATOM   2489  O   ALA A 346      34.387  38.127  19.458  1.00  7.54           O  
ATOM   2490  CB  ALA A 346      34.561  39.421  22.305  1.00  7.90           C  
ATOM   2491  N   PHE A 347      33.538  40.204  19.137  1.00  6.47           N  
ATOM   2492  CA  PHE A 347      33.931  40.314  17.736  1.00  5.71           C  
ATOM   2493  C   PHE A 347      34.869  41.510  17.761  1.00  7.58           C  
ATOM   2494  O   PHE A 347      34.425  42.659  17.872  1.00  8.73           O  
ATOM   2495  CB  PHE A 347      32.714  40.602  16.855  1.00  5.67           C  
ATOM   2496  CG  PHE A 347      31.666  39.523  16.904  1.00  6.90           C  
ATOM   2497  CD1 PHE A 347      30.740  39.472  17.941  1.00  6.78           C  
ATOM   2498  CD2 PHE A 347      31.638  38.530  15.928  1.00  4.75           C  
ATOM   2499  CE1 PHE A 347      29.786  38.433  18.012  1.00  7.62           C  
ATOM   2500  CE2 PHE A 347      30.708  37.492  15.981  1.00  5.54           C  
ATOM   2501  CZ  PHE A 347      29.775  37.441  17.029  1.00  7.12           C  
ATOM   2502  N   ILE A 348      36.161  41.215  17.670  1.00  6.72           N  
ATOM   2503  CA  ILE A 348      37.227  42.205  17.752  1.00  9.08           C  
ATOM   2504  C   ILE A 348      37.959  42.371  16.421  1.00  7.77           C  
ATOM   2505  O   ILE A 348      38.634  41.456  15.947  1.00  8.86           O  
ATOM   2506  CB  ILE A 348      38.267  41.788  18.829  1.00  8.73           C  
ATOM   2507  CG1 ILE A 348      37.578  41.535  20.178  1.00 10.00           C  
ATOM   2508  CG2 ILE A 348      39.345  42.878  18.955  1.00 11.18           C  
ATOM   2509  CD1 ILE A 348      36.760  42.721  20.726  1.00  9.09           C  
ATOM   2510  N   ASN A 349      37.831  43.539  15.808  1.00  8.62           N  
ATOM   2511  CA  ASN A 349      38.510  43.787  14.533  1.00  8.75           C  
ATOM   2512  C   ASN A 349      38.311  42.716  13.455  1.00  8.81           C  
ATOM   2513  O   ASN A 349      39.267  42.208  12.838  1.00  7.82           O  
ATOM   2514  CB  ASN A 349      40.009  44.036  14.779  1.00 11.78           C  
ATOM   2515  CG  ASN A 349      40.265  45.412  15.374  1.00 15.11           C  
ATOM   2516  OD1 ASN A 349      39.657  46.382  14.943  1.00 13.83           O  
ATOM   2517  ND2 ASN A 349      41.153  45.500  16.360  1.00 14.55           N  
ATOM   2518  N   VAL A 350      37.054  42.362  13.235  1.00  8.39           N  
ATOM   2519  CA  VAL A 350      36.716  41.401  12.196  1.00  7.58           C  
ATOM   2520  C   VAL A 350      36.694  42.198  10.900  1.00  7.86           C  
ATOM   2521  O   VAL A 350      36.035  43.233  10.828  1.00  8.29           O  
ATOM   2522  CB  VAL A 350      35.310  40.807  12.418  1.00  6.41           C  
ATOM   2523  CG1 VAL A 350      34.863  40.024  11.166  1.00  7.76           C  
ATOM   2524  CG2 VAL A 350      35.318  39.906  13.655  1.00  8.73           C  
ATOM   2525  N   ASN A 351      37.413  41.731   9.893  1.00  7.34           N  
ATOM   2526  CA  ASN A 351      37.425  42.406   8.610  1.00  8.01           C  
ATOM   2527  C   ASN A 351      36.296  41.796   7.804  1.00  7.63           C  
ATOM   2528  O   ASN A 351      36.517  41.013   6.894  1.00  7.37           O  
ATOM   2529  CB  ASN A 351      38.770  42.209   7.907  1.00  8.01           C  
ATOM   2530  CG  ASN A 351      38.819  42.885   6.544  1.00  8.33           C  
ATOM   2531  OD1 ASN A 351      37.978  43.744   6.215  1.00  7.41           O  
ATOM   2532  ND2 ASN A 351      39.812  42.514   5.745  1.00  7.60           N  
ATOM   2533  N   GLY A 352      35.083  42.161   8.199  1.00  6.98           N  
ATOM   2534  CA  GLY A 352      33.865  41.684   7.569  1.00  7.64           C  
ATOM   2535  C   GLY A 352      32.756  41.990   8.560  1.00  6.86           C  
ATOM   2536  O   GLY A 352      33.003  42.647   9.572  1.00  6.83           O  
ATOM   2537  N   TYR A 353      31.533  41.544   8.288  1.00  5.77           N  
ATOM   2538  CA  TYR A 353      30.445  41.765   9.242  1.00  5.48           C  
ATOM   2539  C   TYR A 353      30.704  40.910  10.477  1.00  5.93           C  
ATOM   2540  O   TYR A 353      31.267  39.819  10.367  1.00  6.26           O  
ATOM   2541  CB  TYR A 353      29.109  41.313   8.647  1.00  3.89           C  
ATOM   2542  CG  TYR A 353      28.793  42.005   7.349  1.00  7.98           C  
ATOM   2543  CD1 TYR A 353      28.385  43.352   7.340  1.00  6.46           C  
ATOM   2544  CD2 TYR A 353      28.970  41.355   6.125  1.00  8.41           C  
ATOM   2545  CE1 TYR A 353      28.177  44.029   6.141  1.00  9.89           C  
ATOM   2546  CE2 TYR A 353      28.760  42.018   4.918  1.00  8.82           C  
ATOM   2547  CZ  TYR A 353      28.369  43.355   4.937  1.00 11.76           C  
ATOM   2548  OH  TYR A 353      28.186  44.035   3.758  1.00 13.16           O  
ATOM   2549  N   ALA A 354      30.314  41.398  11.649  1.00  5.55           N  
ATOM   2550  CA  ALA A 354      30.443  40.585  12.854  1.00  6.29           C  
ATOM   2551  C   ALA A 354      29.400  39.473  12.664  1.00  6.33           C  
ATOM   2552  O   ALA A 354      29.692  38.285  12.816  1.00  6.71           O  
ATOM   2553  CB  ALA A 354      30.121  41.418  14.106  1.00  6.47           C  
ATOM   2554  N   ILE A 355      28.173  39.857  12.323  1.00  5.74           N  
ATOM   2555  CA  ILE A 355      27.118  38.871  12.101  1.00  4.86           C  
ATOM   2556  C   ILE A 355      26.411  39.179  10.791  1.00  5.29           C  
ATOM   2557  O   ILE A 355      26.039  40.331  10.541  1.00  6.48           O  
ATOM   2558  CB  ILE A 355      26.048  38.867  13.230  1.00  5.67           C  
ATOM   2559  CG1 ILE A 355      26.723  38.717  14.600  1.00  5.18           C  
ATOM   2560  CG2 ILE A 355      25.042  37.689  12.997  1.00  6.24           C  
ATOM   2561  CD1 ILE A 355      25.741  38.711  15.778  1.00  7.14           C  
ATOM   2562  N   HIS A 356      26.245  38.152   9.955  1.00  5.32           N  
ATOM   2563  CA  HIS A 356      25.550  38.283   8.668  1.00  5.56           C  
ATOM   2564  C   HIS A 356      24.242  37.522   8.882  1.00  6.37           C  
ATOM   2565  O   HIS A 356      24.248  36.308   9.147  1.00  3.91           O  
ATOM   2566  CB  HIS A 356      26.354  37.634   7.544  1.00  6.21           C  
ATOM   2567  CG  HIS A 356      25.845  37.946   6.167  1.00  6.43           C  
ATOM   2568  ND1 HIS A 356      24.502  37.942   5.841  1.00  6.41           N  
ATOM   2569  CD2 HIS A 356      26.508  38.251   5.023  1.00  7.22           C  
ATOM   2570  CE1 HIS A 356      24.361  38.229   4.557  1.00  6.96           C  
ATOM   2571  NE2 HIS A 356      25.563  38.421   4.036  1.00  7.90           N  
ATOM   2572  N   PHE A 357      23.122  38.239   8.780  1.00  5.85           N  
ATOM   2573  CA  PHE A 357      21.815  37.651   9.036  1.00  4.70           C  
ATOM   2574  C   PHE A 357      21.088  37.014   7.846  1.00  4.77           C  
ATOM   2575  O   PHE A 357      19.953  36.570   7.986  1.00  6.85           O  
ATOM   2576  CB  PHE A 357      20.888  38.700   9.701  1.00  3.00           C  
ATOM   2577  CG  PHE A 357      21.347  39.146  11.070  1.00  5.84           C  
ATOM   2578  CD1 PHE A 357      22.285  40.174  11.209  1.00  4.26           C  
ATOM   2579  CD2 PHE A 357      20.843  38.534  12.221  1.00  6.47           C  
ATOM   2580  CE1 PHE A 357      22.720  40.597  12.470  1.00  5.43           C  
ATOM   2581  CE2 PHE A 357      21.276  38.955  13.510  1.00  6.50           C  
ATOM   2582  CZ  PHE A 357      22.219  39.991  13.623  1.00  7.46           C  
ATOM   2583  N   ASN A 358      21.734  36.952   6.688  1.00  4.83           N  
ATOM   2584  CA  ASN A 358      21.091  36.331   5.543  1.00  5.68           C  
ATOM   2585  C   ASN A 358      22.043  35.888   4.435  1.00  4.98           C  
ATOM   2586  O   ASN A 358      21.796  36.103   3.251  1.00  6.78           O  
ATOM   2587  CB  ASN A 358      19.972  37.247   4.985  1.00  6.46           C  
ATOM   2588  CG  ASN A 358      20.460  38.630   4.579  1.00  6.49           C  
ATOM   2589  OD1 ASN A 358      20.327  39.596   5.339  1.00  9.65           O  
ATOM   2590  ND2 ASN A 358      21.003  38.742   3.376  1.00  8.25           N  
ATOM   2591  N   PRO A 359      23.140  35.211   4.810  1.00  6.33           N  
ATOM   2592  CA  PRO A 359      24.096  34.754   3.797  1.00  5.26           C  
ATOM   2593  C   PRO A 359      23.500  33.740   2.807  1.00  6.48           C  
ATOM   2594  O   PRO A 359      22.632  32.952   3.166  1.00  4.35           O  
ATOM   2595  CB  PRO A 359      25.232  34.162   4.643  1.00  5.31           C  
ATOM   2596  CG  PRO A 359      24.486  33.602   5.848  1.00  6.02           C  
ATOM   2597  CD  PRO A 359      23.512  34.736   6.155  1.00  4.87           C  
ATOM   2598  N   LEU A 360      23.968  33.793   1.560  1.00  6.26           N  
ATOM   2599  CA  LEU A 360      23.543  32.867   0.502  1.00  7.33           C  
ATOM   2600  C   LEU A 360      22.028  32.846   0.317  1.00  7.53           C  
ATOM   2601  O   LEU A 360      21.461  31.817  -0.060  1.00  6.64           O  
ATOM   2602  CB  LEU A 360      24.041  31.452   0.841  1.00  6.86           C  
ATOM   2603  CG  LEU A 360      25.544  31.346   1.158  1.00  8.92           C  
ATOM   2604  CD1 LEU A 360      25.910  29.912   1.493  1.00  8.17           C  
ATOM   2605  CD2 LEU A 360      26.352  31.824  -0.040  1.00  7.78           C  
ATOM   2606  N   ASP A 361      21.362  33.977   0.565  1.00  7.29           N  
ATOM   2607  CA  ASP A 361      19.910  33.969   0.455  1.00  9.12           C  
ATOM   2608  C   ASP A 361      19.364  33.651  -0.932  1.00  9.61           C  
ATOM   2609  O   ASP A 361      18.316  33.007  -1.042  1.00  7.58           O  
ATOM   2610  CB  ASP A 361      19.293  35.255   1.041  1.00  9.54           C  
ATOM   2611  CG  ASP A 361      19.870  36.524   0.454  1.00 12.42           C  
ATOM   2612  OD1 ASP A 361      21.071  36.565   0.118  1.00 15.21           O  
ATOM   2613  OD2 ASP A 361      19.107  37.491   0.351  1.00 16.55           O  
ATOM   2614  N   GLU A 362      20.068  34.051  -1.989  1.00 10.42           N  
ATOM   2615  CA  GLU A 362      19.575  33.736  -3.329  1.00 12.25           C  
ATOM   2616  C   GLU A 362      19.558  32.223  -3.575  1.00 11.23           C  
ATOM   2617  O   GLU A 362      18.588  31.705  -4.146  1.00 11.29           O  
ATOM   2618  CB  GLU A 362      20.394  34.459  -4.408  1.00 12.42           C  
ATOM   2619  CG  GLU A 362      20.208  35.973  -4.404  1.00 16.79           C  
ATOM   2620  CD  GLU A 362      21.234  36.690  -3.540  1.00 20.74           C  
ATOM   2621  OE1 GLU A 362      21.964  36.002  -2.801  1.00 22.65           O  
ATOM   2622  OE2 GLU A 362      21.316  37.943  -3.591  1.00 23.50           O  
ATOM   2623  N   ARG A 363      20.596  31.495  -3.156  1.00 10.63           N  
ATOM   2624  CA  ARG A 363      20.580  30.032  -3.343  1.00 11.45           C  
ATOM   2625  C   ARG A 363      19.499  29.383  -2.498  1.00 11.60           C  
ATOM   2626  O   ARG A 363      18.904  28.385  -2.895  1.00 10.98           O  
ATOM   2627  CB  ARG A 363      21.849  29.361  -2.867  1.00 14.78           C  
ATOM   2628  CG  ARG A 363      23.090  30.020  -3.138  1.00 17.26           C  
ATOM   2629  CD  ARG A 363      24.122  29.107  -2.523  1.00 16.57           C  
ATOM   2630  NE  ARG A 363      25.416  29.482  -3.016  1.00 16.76           N  
ATOM   2631  CZ  ARG A 363      26.526  28.813  -2.789  1.00 14.52           C  
ATOM   2632  NH1 ARG A 363      26.510  27.706  -2.052  1.00 12.70           N  
ATOM   2633  NH2 ARG A 363      27.647  29.250  -3.333  1.00 16.58           N  
ATOM   2634  N   ARG A 364      19.296  29.912  -1.292  1.00 10.20           N  
ATOM   2635  CA  ARG A 364      18.281  29.359  -0.405  1.00  8.99           C  
ATOM   2636  C   ARG A 364      16.871  29.570  -0.949  1.00  9.28           C  
ATOM   2637  O   ARG A 364      15.995  28.724  -0.757  1.00  8.58           O  
ATOM   2638  CB  ARG A 364      18.415  29.965   0.985  1.00  8.79           C  
ATOM   2639  CG  ARG A 364      19.752  29.624   1.645  1.00  6.68           C  
ATOM   2640  CD  ARG A 364      19.893  28.129   2.010  1.00  7.39           C  
ATOM   2641  NE  ARG A 364      21.102  28.002   2.823  1.00  4.78           N  
ATOM   2642  CZ  ARG A 364      22.271  27.551   2.391  1.00  6.85           C  
ATOM   2643  NH1 ARG A 364      22.426  27.137   1.134  1.00  6.12           N  
ATOM   2644  NH2 ARG A 364      23.316  27.589   3.217  1.00  5.16           N  
ATOM   2645  N   LYS A 365      16.637  30.691  -1.622  1.00 10.31           N  
ATOM   2646  CA  LYS A 365      15.314  30.921  -2.211  1.00 11.84           C  
ATOM   2647  C   LYS A 365      15.094  29.905  -3.333  1.00 12.95           C  
ATOM   2648  O   LYS A 365      13.981  29.401  -3.535  1.00 11.15           O  
ATOM   2649  CB  LYS A 365      15.208  32.343  -2.752  1.00 14.27           C  
ATOM   2650  CG  LYS A 365      14.871  33.352  -1.692  1.00 16.12           C  
ATOM   2651  CD  LYS A 365      14.699  34.719  -2.310  1.00 20.02           C  
ATOM   2652  CE  LYS A 365      13.677  35.533  -1.548  1.00 25.02           C  
ATOM   2653  NZ  LYS A 365      12.261  35.033  -1.692  1.00 24.31           N  
ATOM   2654  N   GLU A 366      16.162  29.584  -4.054  1.00 13.55           N  
ATOM   2655  CA  GLU A 366      16.062  28.593  -5.118  1.00 14.77           C  
ATOM   2656  C   GLU A 366      15.714  27.228  -4.532  1.00 14.67           C  
ATOM   2657  O   GLU A 366      14.836  26.529  -5.044  1.00 13.40           O  
ATOM   2658  CB  GLU A 366      17.374  28.517  -5.909  1.00 17.77           C  
ATOM   2659  CG  GLU A 366      17.312  29.311  -7.198  1.00 24.15           C  
ATOM   2660  CD  GLU A 366      18.584  29.230  -8.019  1.00 27.75           C  
ATOM   2661  OE1 GLU A 366      19.192  28.132  -8.077  1.00 29.36           O  
ATOM   2662  OE2 GLU A 366      18.964  30.268  -8.611  1.00 28.07           O  
ATOM   2663  N   TYR A 367      16.403  26.845  -3.460  1.00 13.04           N  
ATOM   2664  CA  TYR A 367      16.138  25.560  -2.801  1.00 12.59           C  
ATOM   2665  C   TYR A 367      14.705  25.523  -2.286  1.00 12.21           C  
ATOM   2666  O   TYR A 367      14.013  24.506  -2.424  1.00 11.51           O  
ATOM   2667  CB  TYR A 367      17.108  25.344  -1.621  1.00 14.16           C  
ATOM   2668  CG  TYR A 367      16.700  24.243  -0.645  1.00 14.26           C  
ATOM   2669  CD1 TYR A 367      16.886  22.889  -0.950  1.00 16.93           C  
ATOM   2670  CD2 TYR A 367      16.086  24.562   0.564  1.00 15.27           C  
ATOM   2671  CE1 TYR A 367      16.456  21.876  -0.066  1.00 15.88           C  
ATOM   2672  CE2 TYR A 367      15.654  23.565   1.452  1.00 14.95           C  
ATOM   2673  CZ  TYR A 367      15.837  22.230   1.135  1.00 14.97           C  
ATOM   2674  OH  TYR A 367      15.380  21.259   2.001  1.00 14.53           O  
ATOM   2675  N   CYS A 368      14.238  26.626  -1.707  1.00  9.54           N  
ATOM   2676  CA  CYS A 368      12.875  26.639  -1.175  1.00  9.89           C  
ATOM   2677  C   CYS A 368      11.838  26.571  -2.293  1.00 11.57           C  
ATOM   2678  O   CYS A 368      10.847  25.849  -2.175  1.00 10.99           O  
ATOM   2679  CB  CYS A 368      12.642  27.876  -0.308  1.00  9.53           C  
ATOM   2680  SG  CYS A 368      13.525  27.794   1.272  1.00  9.00           S  
ATOM   2681  N   ALA A 369      12.076  27.287  -3.389  1.00 12.47           N  
ATOM   2682  CA  ALA A 369      11.118  27.253  -4.507  1.00 14.14           C  
ATOM   2683  C   ALA A 369      11.014  25.854  -5.116  1.00 14.16           C  
ATOM   2684  O   ALA A 369       9.919  25.377  -5.410  1.00 14.68           O  
ATOM   2685  CB  ALA A 369      11.522  28.258  -5.585  1.00 13.49           C  
ATOM   2686  N   ALA A 370      12.151  25.193  -5.297  1.00 14.68           N  
ATOM   2687  CA  ALA A 370      12.171  23.858  -5.882  1.00 14.91           C  
ATOM   2688  C   ALA A 370      11.410  22.825  -5.049  1.00 15.42           C  
ATOM   2689  O   ALA A 370      10.734  21.947  -5.592  1.00 17.47           O  
ATOM   2690  CB  ALA A 370      13.604  23.400  -6.064  1.00 16.30           C  
ATOM   2691  N   ASN A 371      11.506  22.926  -3.732  1.00 13.32           N  
ATOM   2692  CA  ASN A 371      10.855  21.953  -2.871  1.00 13.44           C  
ATOM   2693  C   ASN A 371       9.529  22.396  -2.304  1.00 13.14           C  
ATOM   2694  O   ASN A 371       8.912  21.682  -1.504  1.00 11.23           O  
ATOM   2695  CB  ASN A 371      11.819  21.570  -1.758  1.00 14.19           C  
ATOM   2696  CG  ASN A 371      13.032  20.858  -2.297  1.00 16.39           C  
ATOM   2697  OD1 ASN A 371      12.952  19.683  -2.676  1.00 18.28           O  
ATOM   2698  ND2 ASN A 371      14.154  21.563  -2.370  1.00 15.78           N  
ATOM   2699  N   ARG A 372       9.098  23.569  -2.753  1.00 12.56           N  
ATOM   2700  CA  ARG A 372       7.847  24.171  -2.335  1.00 13.27           C  
ATOM   2701  C   ARG A 372       7.849  24.356  -0.822  1.00 12.58           C  
ATOM   2702  O   ARG A 372       6.895  24.004  -0.124  1.00 12.62           O  
ATOM   2703  CB  ARG A 372       6.658  23.309  -2.792  1.00 16.50           C  
ATOM   2704  CG  ARG A 372       5.379  24.111  -2.929  1.00 21.90           C  
ATOM   2705  CD  ARG A 372       4.259  23.340  -3.606  1.00 26.17           C  
ATOM   2706  NE  ARG A 372       4.466  23.152  -5.038  1.00 29.32           N  
ATOM   2707  CZ  ARG A 372       3.512  22.758  -5.879  1.00 31.20           C  
ATOM   2708  NH1 ARG A 372       2.289  22.518  -5.423  1.00 32.03           N  
ATOM   2709  NH2 ARG A 372       3.776  22.601  -7.174  1.00 31.30           N  
ATOM   2710  N   LEU A 373       8.944  24.930  -0.331  1.00 10.14           N  
ATOM   2711  CA  LEU A 373       9.108  25.201   1.083  1.00  9.72           C  
ATOM   2712  C   LEU A 373       9.012  26.704   1.314  1.00 10.36           C  
ATOM   2713  O   LEU A 373       9.146  27.495   0.382  1.00  9.72           O  
ATOM   2714  CB  LEU A 373      10.466  24.692   1.557  1.00  9.35           C  
ATOM   2715  CG  LEU A 373      10.692  23.217   1.247  1.00 10.85           C  
ATOM   2716  CD1 LEU A 373      12.080  22.798   1.721  1.00 10.61           C  
ATOM   2717  CD2 LEU A 373       9.600  22.401   1.921  1.00  9.49           C  
ATOM   2718  N   LYS A 374       8.796  27.085   2.565  1.00  9.89           N  
ATOM   2719  CA  LYS A 374       8.665  28.492   2.934  1.00  9.92           C  
ATOM   2720  C   LYS A 374       9.990  29.137   3.329  1.00  9.85           C  
ATOM   2721  O   LYS A 374      10.561  28.808   4.355  1.00  7.72           O  
ATOM   2722  CB  LYS A 374       7.689  28.630   4.094  1.00 10.90           C  
ATOM   2723  CG  LYS A 374       7.500  30.050   4.599  1.00 10.93           C  
ATOM   2724  CD  LYS A 374       6.477  30.061   5.737  1.00 13.91           C  
ATOM   2725  CE  LYS A 374       6.324  31.439   6.363  1.00 16.58           C  
ATOM   2726  NZ  LYS A 374       5.768  32.449   5.406  1.00 17.36           N  
ATOM   2727  N   PHE A 375      10.448  30.086   2.524  1.00  8.43           N  
ATOM   2728  CA  PHE A 375      11.697  30.775   2.808  1.00  8.45           C  
ATOM   2729  C   PHE A 375      11.458  31.806   3.900  1.00  8.43           C  
ATOM   2730  O   PHE A 375      10.533  32.607   3.804  1.00  9.48           O  
ATOM   2731  CB  PHE A 375      12.218  31.474   1.541  1.00  8.38           C  
ATOM   2732  CG  PHE A 375      13.442  32.329   1.780  1.00  8.78           C  
ATOM   2733  CD1 PHE A 375      14.716  31.762   1.786  1.00  7.77           C  
ATOM   2734  CD2 PHE A 375      13.319  33.695   2.001  1.00  7.06           C  
ATOM   2735  CE1 PHE A 375      15.856  32.545   2.006  1.00  7.71           C  
ATOM   2736  CE2 PHE A 375      14.460  34.498   2.227  1.00  8.15           C  
ATOM   2737  CZ  PHE A 375      15.727  33.918   2.227  1.00  5.73           C  
ATOM   2738  N   GLU A 376      12.305  31.783   4.928  1.00  7.16           N  
ATOM   2739  CA  GLU A 376      12.226  32.699   6.061  1.00  7.25           C  
ATOM   2740  C   GLU A 376      13.642  33.186   6.341  1.00  6.10           C  
ATOM   2741  O   GLU A 376      14.605  32.637   5.796  1.00  6.22           O  
ATOM   2742  CB  GLU A 376      11.716  31.961   7.300  1.00  7.90           C  
ATOM   2743  CG  GLU A 376      10.422  31.202   7.077  1.00 11.44           C  
ATOM   2744  CD  GLU A 376       9.864  30.664   8.379  1.00 12.16           C  
ATOM   2745  OE1 GLU A 376       9.670  31.467   9.298  1.00 15.60           O  
ATOM   2746  OE2 GLU A 376       9.626  29.447   8.491  1.00 15.89           O  
ATOM   2747  N   THR A 377      13.757  34.219   7.176  1.00  6.57           N  
ATOM   2748  CA  THR A 377      15.053  34.765   7.539  1.00  7.59           C  
ATOM   2749  C   THR A 377      15.163  34.738   9.062  1.00  7.38           C  
ATOM   2750  O   THR A 377      14.155  34.787   9.764  1.00  8.32           O  
ATOM   2751  CB  THR A 377      15.214  36.174   6.952  1.00  9.08           C  
ATOM   2752  OG1 THR A 377      13.991  36.903   7.113  1.00 10.03           O  
ATOM   2753  CG2 THR A 377      15.512  36.074   5.432  1.00 11.08           C  
ATOM   2754  N   PRO A 378      16.392  34.656   9.594  1.00  8.41           N  
ATOM   2755  CA  PRO A 378      16.650  34.597  11.038  1.00  8.72           C  
ATOM   2756  C   PRO A 378      15.859  35.561  11.903  1.00  8.97           C  
ATOM   2757  O   PRO A 378      15.819  36.755  11.639  1.00  8.84           O  
ATOM   2758  CB  PRO A 378      18.154  34.825  11.130  1.00  8.30           C  
ATOM   2759  CG  PRO A 378      18.662  34.198   9.858  1.00  7.35           C  
ATOM   2760  CD  PRO A 378      17.657  34.721   8.841  1.00  8.91           C  
ATOM   2761  N   HIS A 379      15.232  35.019  12.939  1.00  8.86           N  
ATOM   2762  CA  HIS A 379      14.440  35.814  13.867  1.00 10.72           C  
ATOM   2763  C   HIS A 379      14.412  35.103  15.204  1.00  9.84           C  
ATOM   2764  O   HIS A 379      14.863  33.962  15.317  1.00 10.43           O  
ATOM   2765  CB  HIS A 379      13.010  36.010  13.340  1.00 12.08           C  
ATOM   2766  CG  HIS A 379      12.235  34.739  13.180  1.00 15.37           C  
ATOM   2767  ND1 HIS A 379      12.332  33.943  12.058  1.00 17.83           N  
ATOM   2768  CD2 HIS A 379      11.342  34.132  13.998  1.00 15.84           C  
ATOM   2769  CE1 HIS A 379      11.532  32.898  12.192  1.00 17.78           C  
ATOM   2770  NE2 HIS A 379      10.921  32.990  13.360  1.00 18.53           N  
ATOM   2771  N   GLN A 380      13.861  35.768  16.208  1.00 10.49           N  
ATOM   2772  CA  GLN A 380      13.798  35.227  17.554  1.00 10.84           C  
ATOM   2773  C   GLN A 380      15.179  34.960  18.146  1.00 10.68           C  
ATOM   2774  O   GLN A 380      15.353  34.073  18.990  1.00 10.73           O  
ATOM   2775  CB  GLN A 380      12.980  33.943  17.574  1.00 15.00           C  
ATOM   2776  CG  GLN A 380      11.625  34.103  18.182  1.00 21.23           C  
ATOM   2777  CD  GLN A 380      10.936  32.770  18.351  1.00 25.48           C  
ATOM   2778  OE1 GLN A 380      10.715  32.053  17.375  1.00 27.00           O  
ATOM   2779  NE2 GLN A 380      10.606  32.419  19.593  1.00 27.95           N  
ATOM   2780  N   LEU A 381      16.169  35.718  17.696  1.00  9.29           N  
ATOM   2781  CA  LEU A 381      17.512  35.557  18.228  1.00  8.71           C  
ATOM   2782  C   LEU A 381      17.616  36.396  19.498  1.00  9.86           C  
ATOM   2783  O   LEU A 381      17.095  37.511  19.550  1.00 11.57           O  
ATOM   2784  CB  LEU A 381      18.534  36.044  17.201  1.00  7.93           C  
ATOM   2785  CG  LEU A 381      18.367  35.451  15.796  1.00  7.04           C  
ATOM   2786  CD1 LEU A 381      19.292  36.218  14.841  1.00  8.77           C  
ATOM   2787  CD2 LEU A 381      18.693  33.940  15.782  1.00  7.07           C  
ATOM   2788  N   MET A 382      18.255  35.851  20.529  1.00  9.68           N  
ATOM   2789  CA  MET A 382      18.457  36.598  21.770  1.00 10.25           C  
ATOM   2790  C   MET A 382      19.936  36.944  21.753  1.00  9.84           C  
ATOM   2791  O   MET A 382      20.779  36.066  21.963  1.00  9.93           O  
ATOM   2792  CB  MET A 382      18.146  35.729  22.993  1.00 11.44           C  
ATOM   2793  CG  MET A 382      16.789  35.055  22.943  1.00 19.07           C  
ATOM   2794  SD  MET A 382      15.444  36.265  22.942  1.00 22.73           S  
ATOM   2795  CE  MET A 382      15.597  36.876  24.625  1.00 22.75           C  
ATOM   2796  N   LEU A 383      20.250  38.203  21.465  1.00  7.84           N  
ATOM   2797  CA  LEU A 383      21.638  38.667  21.418  1.00  8.45           C  
ATOM   2798  C   LEU A 383      21.887  39.396  22.724  1.00  9.76           C  
ATOM   2799  O   LEU A 383      21.443  40.530  22.903  1.00  9.94           O  
ATOM   2800  CB  LEU A 383      21.830  39.590  20.222  1.00  9.27           C  
ATOM   2801  CG  LEU A 383      21.605  38.807  18.920  1.00  9.54           C  
ATOM   2802  CD1 LEU A 383      20.425  39.420  18.144  1.00  9.68           C  
ATOM   2803  CD2 LEU A 383      22.886  38.833  18.103  1.00 12.18           C  
ATOM   2804  N   LYS A 384      22.602  38.736  23.634  1.00  8.91           N  
ATOM   2805  CA  LYS A 384      22.839  39.296  24.963  1.00 10.70           C  
ATOM   2806  C   LYS A 384      24.288  39.409  25.346  1.00 10.62           C  
ATOM   2807  O   LYS A 384      25.043  38.443  25.225  1.00 10.41           O  
ATOM   2808  CB  LYS A 384      22.173  38.432  26.036  1.00 12.31           C  
ATOM   2809  CG  LYS A 384      20.696  38.162  25.868  1.00 18.40           C  
ATOM   2810  CD  LYS A 384      20.189  37.513  27.163  1.00 19.62           C  
ATOM   2811  CE  LYS A 384      18.684  37.463  27.232  1.00 22.28           C  
ATOM   2812  NZ  LYS A 384      18.276  36.706  28.451  1.00 22.25           N  
ATOM   2813  N   GLY A 385      24.674  40.588  25.816  1.00  9.22           N  
ATOM   2814  CA  GLY A 385      26.031  40.798  26.294  1.00 10.07           C  
ATOM   2815  C   GLY A 385      27.209  40.618  25.349  1.00  8.99           C  
ATOM   2816  O   GLY A 385      28.306  40.282  25.802  1.00  8.92           O  
ATOM   2817  N   ASN A 386      27.002  40.834  24.056  1.00  7.75           N  
ATOM   2818  CA  ASN A 386      28.071  40.683  23.085  1.00  6.85           C  
ATOM   2819  C   ASN A 386      28.827  41.976  22.923  1.00  7.78           C  
ATOM   2820  O   ASN A 386      28.262  43.055  23.065  1.00 10.38           O  
ATOM   2821  CB  ASN A 386      27.510  40.265  21.719  1.00  7.55           C  
ATOM   2822  CG  ASN A 386      26.759  38.958  21.782  1.00  9.13           C  
ATOM   2823  OD1 ASN A 386      27.355  37.870  21.850  1.00  8.00           O  
ATOM   2824  ND2 ASN A 386      25.436  39.050  21.775  1.00  5.60           N  
ATOM   2825  N   LEU A 387      30.115  41.860  22.632  1.00  7.96           N  
ATOM   2826  CA  LEU A 387      30.954  43.028  22.422  1.00  8.40           C  
ATOM   2827  C   LEU A 387      31.325  43.079  20.954  1.00  7.58           C  
ATOM   2828  O   LEU A 387      31.836  42.094  20.414  1.00  6.88           O  
ATOM   2829  CB  LEU A 387      32.230  42.941  23.270  1.00  9.73           C  
ATOM   2830  CG  LEU A 387      33.298  43.989  22.918  1.00 10.21           C  
ATOM   2831  CD1 LEU A 387      32.764  45.404  23.195  1.00 11.14           C  
ATOM   2832  CD2 LEU A 387      34.558  43.737  23.754  1.00 11.02           C  
ATOM   2833  N   PHE A 388      31.051  44.213  20.302  1.00  7.67           N  
ATOM   2834  CA  PHE A 388      31.386  44.398  18.889  1.00  7.85           C  
ATOM   2835  C   PHE A 388      32.324  45.583  18.899  1.00  9.63           C  
ATOM   2836  O   PHE A 388      31.944  46.688  19.282  1.00 10.53           O  
ATOM   2837  CB  PHE A 388      30.140  44.697  18.065  1.00  8.16           C  
ATOM   2838  CG  PHE A 388      29.067  43.663  18.213  1.00  7.41           C  
ATOM   2839  CD1 PHE A 388      29.073  42.518  17.410  1.00  7.51           C  
ATOM   2840  CD2 PHE A 388      28.076  43.809  19.177  1.00  7.10           C  
ATOM   2841  CE1 PHE A 388      28.101  41.531  17.565  1.00  7.39           C  
ATOM   2842  CE2 PHE A 388      27.093  42.826  19.348  1.00  6.87           C  
ATOM   2843  CZ  PHE A 388      27.110  41.678  18.532  1.00  6.99           C  
ATOM   2844  N   PHE A 389      33.561  45.351  18.493  1.00  8.85           N  
ATOM   2845  CA  PHE A 389      34.548  46.408  18.568  1.00 11.42           C  
ATOM   2846  C   PHE A 389      35.457  46.408  17.368  1.00 11.84           C  
ATOM   2847  O   PHE A 389      35.818  45.351  16.856  1.00 12.38           O  
ATOM   2848  CB  PHE A 389      35.392  46.203  19.829  1.00 10.99           C  
ATOM   2849  CG  PHE A 389      36.542  47.155  19.946  1.00 13.03           C  
ATOM   2850  CD1 PHE A 389      36.317  48.501  20.216  1.00 14.36           C  
ATOM   2851  CD2 PHE A 389      37.851  46.715  19.749  1.00 13.04           C  
ATOM   2852  CE1 PHE A 389      37.385  49.408  20.284  1.00 14.55           C  
ATOM   2853  CE2 PHE A 389      38.930  47.616  19.815  1.00 15.24           C  
ATOM   2854  CZ  PHE A 389      38.689  48.962  20.081  1.00 15.80           C  
ATOM   2855  N   LYS A 390      35.825  47.602  16.922  1.00 10.89           N  
ATOM   2856  CA  LYS A 390      36.723  47.729  15.793  1.00 12.55           C  
ATOM   2857  C   LYS A 390      37.514  49.019  15.946  1.00 13.81           C  
ATOM   2858  O   LYS A 390      36.948  50.058  16.291  1.00 14.30           O  
ATOM   2859  CB  LYS A 390      35.912  47.764  14.497  1.00 13.97           C  
ATOM   2860  CG  LYS A 390      36.678  47.979  13.218  1.00 16.62           C  
ATOM   2861  CD  LYS A 390      35.650  48.117  12.108  1.00 19.20           C  
ATOM   2862  CE  LYS A 390      36.173  48.805  10.889  1.00 21.19           C  
ATOM   2863  NZ  LYS A 390      36.657  50.178  11.175  1.00 20.24           N  
ATOM   2864  N   ASP A 391      38.828  48.944  15.760  1.00 15.22           N  
ATOM   2865  CA  ASP A 391      39.632  50.156  15.791  1.00 16.08           C  
ATOM   2866  C   ASP A 391      40.652  50.107  14.663  1.00 16.28           C  
ATOM   2867  O   ASP A 391      41.605  50.893  14.626  1.00 17.64           O  
ATOM   2868  CB  ASP A 391      40.284  50.398  17.163  1.00 15.96           C  
ATOM   2869  CG  ASP A 391      41.373  49.397  17.510  1.00 16.01           C  
ATOM   2870  OD1 ASP A 391      41.641  48.456  16.731  1.00 13.44           O  
ATOM   2871  OD2 ASP A 391      41.958  49.566  18.606  1.00 17.18           O  
ATOM   2872  N   LYS A 392      40.447  49.164  13.743  1.00 16.09           N  
ATOM   2873  CA  LYS A 392      41.296  49.027  12.556  1.00 15.28           C  
ATOM   2874  C   LYS A 392      40.440  49.518  11.397  1.00 17.31           C  
ATOM   2875  O   LYS A 392      39.212  49.405  11.446  1.00 17.62           O  
ATOM   2876  CB  LYS A 392      41.717  47.570  12.319  1.00 17.18           C  
ATOM   2877  CG  LYS A 392      42.664  47.056  13.368  1.00 16.07           C  
ATOM   2878  CD  LYS A 392      43.297  45.740  12.979  1.00 16.64           C  
ATOM   2879  CE  LYS A 392      44.219  45.235  14.091  1.00 19.99           C  
ATOM   2880  NZ  LYS A 392      45.037  44.081  13.598  1.00 21.53           N  
ATOM   2881  N   PRO A 393      41.070  50.057  10.338  1.00 16.89           N  
ATOM   2882  CA  PRO A 393      40.394  50.594   9.148  1.00 16.91           C  
ATOM   2883  C   PRO A 393      39.619  49.686   8.190  1.00 16.32           C  
ATOM   2884  O   PRO A 393      39.453  50.045   7.025  1.00 15.73           O  
ATOM   2885  CB  PRO A 393      41.518  51.357   8.434  1.00 18.27           C  
ATOM   2886  CG  PRO A 393      42.740  50.547   8.789  1.00 17.62           C  
ATOM   2887  CD  PRO A 393      42.522  50.300  10.264  1.00 18.00           C  
ATOM   2888  N   TYR A 394      39.138  48.532   8.659  1.00 14.68           N  
ATOM   2889  CA  TYR A 394      38.352  47.650   7.791  1.00 13.93           C  
ATOM   2890  C   TYR A 394      37.069  48.428   7.447  1.00 13.90           C  
ATOM   2891  O   TYR A 394      36.646  49.289   8.227  1.00 14.87           O  
ATOM   2892  CB  TYR A 394      38.031  46.346   8.517  1.00 13.53           C  
ATOM   2893  CG  TYR A 394      39.263  45.596   8.998  1.00 12.80           C  
ATOM   2894  CD1 TYR A 394      40.364  45.417   8.165  1.00 12.48           C  
ATOM   2895  CD2 TYR A 394      39.309  45.049  10.280  1.00 13.13           C  
ATOM   2896  CE1 TYR A 394      41.494  44.700   8.599  1.00 13.30           C  
ATOM   2897  CE2 TYR A 394      40.437  44.331  10.731  1.00 13.79           C  
ATOM   2898  CZ  TYR A 394      41.516  44.162   9.882  1.00 13.25           C  
ATOM   2899  OH  TYR A 394      42.605  43.427  10.300  1.00 14.47           O  
ATOM   2900  N   VAL A 395      36.429  48.108   6.319  1.00 12.64           N  
ATOM   2901  CA  VAL A 395      35.262  48.876   5.872  1.00 12.69           C  
ATOM   2902  C   VAL A 395      33.856  48.388   6.195  1.00 12.48           C  
ATOM   2903  O   VAL A 395      32.878  49.112   5.994  1.00 10.61           O  
ATOM   2904  CB  VAL A 395      35.332  49.112   4.347  1.00 13.54           C  
ATOM   2905  CG1 VAL A 395      36.672  49.790   3.993  1.00 16.65           C  
ATOM   2906  CG2 VAL A 395      35.215  47.795   3.599  1.00 15.46           C  
ATOM   2907  N   TYR A 396      33.758  47.185   6.731  1.00 10.80           N  
ATOM   2908  CA  TYR A 396      32.459  46.607   7.035  1.00  9.54           C  
ATOM   2909  C   TYR A 396      31.743  47.038   8.298  1.00  8.50           C  
ATOM   2910  O   TYR A 396      32.328  47.071   9.390  1.00  7.90           O  
ATOM   2911  CB  TYR A 396      32.567  45.088   7.117  1.00  7.82           C  
ATOM   2912  CG  TYR A 396      33.048  44.415   5.869  1.00  8.64           C  
ATOM   2913  CD1 TYR A 396      34.413  44.268   5.610  1.00  9.69           C  
ATOM   2914  CD2 TYR A 396      32.138  43.883   4.958  1.00  8.78           C  
ATOM   2915  CE1 TYR A 396      34.857  43.601   4.474  1.00  7.96           C  
ATOM   2916  CE2 TYR A 396      32.563  43.222   3.832  1.00 10.34           C  
ATOM   2917  CZ  TYR A 396      33.915  43.076   3.587  1.00 10.83           C  
ATOM   2918  OH  TYR A 396      34.316  42.387   2.460  1.00 14.21           O  
ATOM   2919  N   PRO A 397      30.454  47.375   8.171  1.00  8.16           N  
ATOM   2920  CA  PRO A 397      29.699  47.762   9.356  1.00  8.52           C  
ATOM   2921  C   PRO A 397      29.589  46.437  10.126  1.00  8.71           C  
ATOM   2922  O   PRO A 397      29.869  45.383   9.552  1.00  8.78           O  
ATOM   2923  CB  PRO A 397      28.368  48.231   8.775  1.00 11.45           C  
ATOM   2924  CG  PRO A 397      28.243  47.442   7.519  1.00 12.98           C  
ATOM   2925  CD  PRO A 397      29.632  47.471   6.952  1.00  9.25           C  
ATOM   2926  N   PHE A 398      29.186  46.471  11.394  1.00  9.09           N  
ATOM   2927  CA  PHE A 398      29.114  45.237  12.193  1.00  8.00           C  
ATOM   2928  C   PHE A 398      28.090  44.210  11.714  1.00  7.87           C  
ATOM   2929  O   PHE A 398      28.332  43.009  11.811  1.00  5.36           O  
ATOM   2930  CB  PHE A 398      28.786  45.537  13.657  1.00  8.41           C  
ATOM   2931  CG  PHE A 398      29.895  46.228  14.421  1.00 10.13           C  
ATOM   2932  CD1 PHE A 398      31.171  45.669  14.501  1.00 10.25           C  
ATOM   2933  CD2 PHE A 398      29.634  47.415  15.101  1.00 10.55           C  
ATOM   2934  CE1 PHE A 398      32.176  46.285  15.253  1.00 10.02           C  
ATOM   2935  CE2 PHE A 398      30.629  48.041  15.858  1.00 10.74           C  
ATOM   2936  CZ  PHE A 398      31.902  47.475  15.932  1.00  9.62           C  
ATOM   2937  N   PHE A 399      26.956  44.675  11.190  1.00  7.77           N  
ATOM   2938  CA  PHE A 399      25.898  43.756  10.769  1.00  7.59           C  
ATOM   2939  C   PHE A 399      25.347  43.922   9.352  1.00  8.79           C  
ATOM   2940  O   PHE A 399      25.340  45.028   8.786  1.00  8.38           O  
ATOM   2941  CB  PHE A 399      24.718  43.879  11.739  1.00  8.46           C  
ATOM   2942  CG  PHE A 399      25.118  43.875  13.188  1.00  8.09           C  
ATOM   2943  CD1 PHE A 399      25.699  42.751  13.752  1.00  6.97           C  
ATOM   2944  CD2 PHE A 399      24.957  45.018  13.970  1.00  7.41           C  
ATOM   2945  CE1 PHE A 399      26.125  42.748  15.078  1.00  8.31           C  
ATOM   2946  CE2 PHE A 399      25.372  45.037  15.293  1.00  8.35           C  
ATOM   2947  CZ  PHE A 399      25.963  43.890  15.857  1.00  7.62           C  
ATOM   2948  N   LYS A 400      24.886  42.812   8.788  1.00  8.24           N  
ATOM   2949  CA  LYS A 400      24.251  42.834   7.469  1.00  7.02           C  
ATOM   2950  C   LYS A 400      22.920  42.099   7.634  1.00  6.94           C  
ATOM   2951  O   LYS A 400      22.897  40.921   7.985  1.00  5.27           O  
ATOM   2952  CB  LYS A 400      25.100  42.119   6.412  1.00  8.93           C  
ATOM   2953  CG  LYS A 400      24.418  42.103   5.039  1.00  9.78           C  
ATOM   2954  CD  LYS A 400      25.348  41.674   3.916  1.00 13.32           C  
ATOM   2955  CE  LYS A 400      24.609  41.510   2.592  1.00 15.70           C  
ATOM   2956  NZ  LYS A 400      24.010  42.786   2.105  1.00 18.39           N  
ATOM   2957  N   ASP A 401      21.808  42.815   7.470  1.00  6.53           N  
ATOM   2958  CA  ASP A 401      20.498  42.171   7.546  1.00  6.62           C  
ATOM   2959  C   ASP A 401      19.604  42.873   6.532  1.00  7.52           C  
ATOM   2960  O   ASP A 401      19.010  43.910   6.808  1.00  8.67           O  
ATOM   2961  CB  ASP A 401      19.871  42.239   8.954  1.00  5.13           C  
ATOM   2962  CG  ASP A 401      18.623  41.375   9.060  1.00  8.43           C  
ATOM   2963  OD1 ASP A 401      18.166  40.910   7.980  1.00  7.52           O  
ATOM   2964  OD2 ASP A 401      18.097  41.159  10.189  1.00  7.83           O  
ATOM   2965  N   ASP A 402      19.540  42.296   5.341  1.00  6.41           N  
ATOM   2966  CA  ASP A 402      18.749  42.841   4.249  1.00  8.32           C  
ATOM   2967  C   ASP A 402      17.257  42.635   4.454  1.00  8.05           C  
ATOM   2968  O   ASP A 402      16.454  43.135   3.671  1.00  8.37           O  
ATOM   2969  CB  ASP A 402      19.157  42.177   2.942  1.00  9.97           C  
ATOM   2970  CG  ASP A 402      20.574  42.508   2.535  1.00 14.89           C  
ATOM   2971  OD1 ASP A 402      20.897  43.710   2.399  1.00 13.18           O  
ATOM   2972  OD2 ASP A 402      21.358  41.560   2.338  1.00 14.30           O  
ATOM   2973  N   TYR A 403      16.897  41.897   5.504  1.00  6.40           N  
ATOM   2974  CA  TYR A 403      15.503  41.605   5.811  1.00  7.64           C  
ATOM   2975  C   TYR A 403      15.148  42.068   7.215  1.00  8.17           C  
ATOM   2976  O   TYR A 403      14.303  41.475   7.890  1.00  8.95           O  
ATOM   2977  CB  TYR A 403      15.234  40.107   5.716  1.00  6.23           C  
ATOM   2978  CG  TYR A 403      15.607  39.509   4.391  1.00  6.00           C  
ATOM   2979  CD1 TYR A 403      16.937  39.184   4.095  1.00  7.95           C  
ATOM   2980  CD2 TYR A 403      14.628  39.229   3.436  1.00  4.67           C  
ATOM   2981  CE1 TYR A 403      17.276  38.583   2.882  1.00  5.43           C  
ATOM   2982  CE2 TYR A 403      14.956  38.632   2.232  1.00  4.27           C  
ATOM   2983  CZ  TYR A 403      16.282  38.310   1.960  1.00  6.75           C  
ATOM   2984  OH  TYR A 403      16.595  37.694   0.767  1.00  8.79           O  
ATOM   2985  N   PHE A 404      15.789  43.140   7.649  1.00  8.67           N  
ATOM   2986  CA  PHE A 404      15.552  43.661   8.987  1.00  7.76           C  
ATOM   2987  C   PHE A 404      14.104  44.038   9.234  1.00  9.01           C  
ATOM   2988  O   PHE A 404      13.479  44.727   8.421  1.00  9.58           O  
ATOM   2989  CB  PHE A 404      16.407  44.894   9.236  1.00  8.86           C  
ATOM   2990  CG  PHE A 404      16.221  45.455  10.595  1.00  7.56           C  
ATOM   2991  CD1 PHE A 404      16.941  44.944  11.670  1.00  7.69           C  
ATOM   2992  CD2 PHE A 404      15.252  46.423  10.834  1.00  8.31           C  
ATOM   2993  CE1 PHE A 404      16.702  45.374  12.958  1.00  7.53           C  
ATOM   2994  CE2 PHE A 404      15.003  46.863  12.129  1.00  8.53           C  
ATOM   2995  CZ  PHE A 404      15.734  46.332  13.199  1.00  9.03           C  
ATOM   2996  N   ILE A 405      13.575  43.577  10.358  1.00  8.24           N  
ATOM   2997  CA  ILE A 405      12.209  43.887  10.752  1.00  8.83           C  
ATOM   2998  C   ILE A 405      12.262  44.232  12.229  1.00  9.22           C  
ATOM   2999  O   ILE A 405      12.734  43.444  13.042  1.00  8.02           O  
ATOM   3000  CB  ILE A 405      11.266  42.687  10.542  1.00 10.20           C  
ATOM   3001  CG1 ILE A 405      11.039  42.462   9.041  1.00  9.58           C  
ATOM   3002  CG2 ILE A 405       9.939  42.932  11.244  1.00  9.67           C  
ATOM   3003  CD1 ILE A 405      10.142  41.254   8.760  1.00 12.09           C  
ATOM   3004  N   ALA A 406      11.796  45.425  12.571  1.00  9.22           N  
ATOM   3005  CA  ALA A 406      11.809  45.875  13.961  1.00  9.68           C  
ATOM   3006  C   ALA A 406      11.197  44.851  14.907  1.00  9.11           C  
ATOM   3007  O   ALA A 406      10.100  44.351  14.667  1.00  9.82           O  
ATOM   3008  CB  ALA A 406      11.041  47.213  14.082  1.00  8.27           C  
ATOM   3009  N   GLY A 407      11.923  44.538  15.976  1.00  9.40           N  
ATOM   3010  CA  GLY A 407      11.426  43.613  16.978  1.00  9.81           C  
ATOM   3011  C   GLY A 407      11.546  42.112  16.743  1.00 10.41           C  
ATOM   3012  O   GLY A 407      11.212  41.353  17.646  1.00 10.33           O  
ATOM   3013  N   LYS A 408      12.007  41.677  15.568  1.00  8.43           N  
ATOM   3014  CA  LYS A 408      12.109  40.242  15.297  1.00  9.63           C  
ATOM   3015  C   LYS A 408      13.141  39.539  16.178  1.00  9.92           C  
ATOM   3016  O   LYS A 408      13.005  38.338  16.461  1.00  8.90           O  
ATOM   3017  CB  LYS A 408      12.412  39.977  13.816  1.00 10.52           C  
ATOM   3018  CG  LYS A 408      13.836  40.306  13.344  1.00 12.12           C  
ATOM   3019  CD  LYS A 408      14.040  39.901  11.860  1.00 12.89           C  
ATOM   3020  CE  LYS A 408      15.485  40.128  11.410  1.00 13.59           C  
ATOM   3021  NZ  LYS A 408      15.838  39.287  10.215  1.00 14.53           N  
ATOM   3022  N   ASN A 409      14.155  40.298  16.602  1.00  9.92           N  
ATOM   3023  CA  ASN A 409      15.218  39.825  17.478  1.00  9.21           C  
ATOM   3024  C   ASN A 409      15.248  40.689  18.739  1.00 12.06           C  
ATOM   3025  O   ASN A 409      14.698  41.798  18.768  1.00 11.69           O  
ATOM   3026  CB  ASN A 409      16.579  39.918  16.794  1.00  9.64           C  
ATOM   3027  CG  ASN A 409      16.688  39.001  15.600  1.00  8.92           C  
ATOM   3028  OD1 ASN A 409      16.150  37.902  15.614  1.00  9.47           O  
ATOM   3029  ND2 ASN A 409      17.402  39.447  14.563  1.00  7.86           N  
ATOM   3030  N   SER A 410      15.895  40.169  19.771  1.00 10.12           N  
ATOM   3031  CA  SER A 410      16.008  40.859  21.050  1.00 12.36           C  
ATOM   3032  C   SER A 410      17.490  41.145  21.349  1.00 12.10           C  
ATOM   3033  O   SER A 410      18.305  40.223  21.381  1.00 12.77           O  
ATOM   3034  CB  SER A 410      15.400  39.978  22.138  1.00 14.02           C  
ATOM   3035  OG  SER A 410      15.590  40.518  23.436  1.00 16.45           O  
ATOM   3036  N   TRP A 411      17.823  42.420  21.559  1.00 10.92           N  
ATOM   3037  CA  TRP A 411      19.188  42.836  21.861  1.00 10.72           C  
ATOM   3038  C   TRP A 411      19.256  43.446  23.261  1.00 12.47           C  
ATOM   3039  O   TRP A 411      18.564  44.430  23.546  1.00 10.68           O  
ATOM   3040  CB  TRP A 411      19.664  43.888  20.861  1.00 10.58           C  
ATOM   3041  CG  TRP A 411      19.665  43.468  19.414  1.00  9.44           C  
ATOM   3042  CD1 TRP A 411      18.586  43.342  18.576  1.00 10.93           C  
ATOM   3043  CD2 TRP A 411      20.820  43.193  18.623  1.00  9.83           C  
ATOM   3044  NE1 TRP A 411      19.012  43.012  17.300  1.00  8.58           N  
ATOM   3045  CE2 TRP A 411      20.379  42.913  17.308  1.00  9.61           C  
ATOM   3046  CE3 TRP A 411      22.189  43.157  18.900  1.00  8.66           C  
ATOM   3047  CZ2 TRP A 411      21.264  42.608  16.271  1.00  8.36           C  
ATOM   3048  CZ3 TRP A 411      23.072  42.856  17.873  1.00  7.95           C  
ATOM   3049  CH2 TRP A 411      22.604  42.583  16.567  1.00  9.37           C  
ATOM   3050  N   THR A 412      20.097  42.886  24.124  1.00 12.31           N  
ATOM   3051  CA  THR A 412      20.239  43.404  25.482  1.00 14.59           C  
ATOM   3052  C   THR A 412      21.671  43.289  25.977  1.00 14.00           C  
ATOM   3053  O   THR A 412      22.315  42.238  25.838  1.00 11.86           O  
ATOM   3054  CB  THR A 412      19.368  42.623  26.509  1.00 16.53           C  
ATOM   3055  OG1 THR A 412      18.001  42.612  26.086  1.00 19.67           O  
ATOM   3056  CG2 THR A 412      19.430  43.296  27.889  1.00 17.38           C  
ATOM   3057  N   GLY A 413      22.157  44.375  26.561  1.00 11.84           N  
ATOM   3058  CA  GLY A 413      23.479  44.365  27.147  1.00 12.02           C  
ATOM   3059  C   GLY A 413      24.670  44.254  26.238  1.00 11.37           C  
ATOM   3060  O   GLY A 413      25.766  43.967  26.716  1.00 10.90           O  
ATOM   3061  N   ASN A 414      24.483  44.501  24.946  1.00 10.03           N  
ATOM   3062  CA  ASN A 414      25.600  44.434  24.020  1.00 10.90           C  
ATOM   3063  C   ASN A 414      26.293  45.785  24.015  1.00 12.69           C  
ATOM   3064  O   ASN A 414      25.760  46.772  24.534  1.00 12.77           O  
ATOM   3065  CB  ASN A 414      25.108  44.139  22.607  1.00 10.55           C  
ATOM   3066  CG  ASN A 414      24.294  42.870  22.532  1.00 10.64           C  
ATOM   3067  OD1 ASN A 414      24.847  41.764  22.530  1.00 11.01           O  
ATOM   3068  ND2 ASN A 414      22.968  43.018  22.477  1.00  8.97           N  
ATOM   3069  N   VAL A 415      27.498  45.817  23.467  1.00 11.71           N  
ATOM   3070  CA  VAL A 415      28.225  47.065  23.315  1.00 12.73           C  
ATOM   3071  C   VAL A 415      28.767  47.057  21.896  1.00 12.32           C  
ATOM   3072  O   VAL A 415      29.305  46.048  21.430  1.00 11.72           O  
ATOM   3073  CB  VAL A 415      29.385  47.197  24.310  1.00 13.88           C  
ATOM   3074  CG1 VAL A 415      30.325  48.301  23.854  1.00 15.74           C  
ATOM   3075  CG2 VAL A 415      28.842  47.516  25.691  1.00 15.28           C  
ATOM   3076  N   ALA A 416      28.610  48.168  21.192  1.00 11.25           N  
ATOM   3077  CA  ALA A 416      29.095  48.233  19.820  1.00 11.67           C  
ATOM   3078  C   ALA A 416      29.807  49.545  19.602  1.00 13.72           C  
ATOM   3079  O   ALA A 416      29.243  50.618  19.864  1.00 12.51           O  
ATOM   3080  CB  ALA A 416      27.932  48.103  18.820  1.00 12.15           C  
ATOM   3081  N   LEU A 417      31.042  49.479  19.127  1.00 12.42           N  
ATOM   3082  CA  LEU A 417      31.762  50.721  18.880  1.00 14.30           C  
ATOM   3083  C   LEU A 417      32.913  50.566  17.922  1.00 13.56           C  
ATOM   3084  O   LEU A 417      33.635  49.564  17.947  1.00 13.26           O  
ATOM   3085  CB  LEU A 417      32.255  51.330  20.191  1.00 15.25           C  
ATOM   3086  CG  LEU A 417      33.555  50.836  20.821  1.00 18.55           C  
ATOM   3087  CD1 LEU A 417      34.148  51.937  21.698  1.00 18.63           C  
ATOM   3088  CD2 LEU A 417      33.287  49.573  21.636  1.00 20.25           C  
ATOM   3089  N   GLY A 418      33.074  51.560  17.051  1.00 13.57           N  
ATOM   3090  CA  GLY A 418      34.155  51.525  16.084  1.00 12.89           C  
ATOM   3091  C   GLY A 418      33.735  51.694  14.638  1.00 14.33           C  
ATOM   3092  O   GLY A 418      34.551  52.060  13.781  1.00 13.49           O  
ATOM   3093  N   VAL A 419      32.465  51.424  14.352  1.00 13.46           N  
ATOM   3094  CA  VAL A 419      31.953  51.541  12.988  1.00 14.85           C  
ATOM   3095  C   VAL A 419      30.423  51.514  13.034  1.00 15.41           C  
ATOM   3096  O   VAL A 419      29.835  51.073  14.034  1.00 14.68           O  
ATOM   3097  CB  VAL A 419      32.477  50.377  12.102  1.00 15.26           C  
ATOM   3098  CG1 VAL A 419      31.875  49.042  12.580  1.00 15.16           C  
ATOM   3099  CG2 VAL A 419      32.149  50.626  10.649  1.00 15.97           C  
ATOM   3100  N   GLU A 420      29.769  52.001  11.983  1.00 15.86           N  
ATOM   3101  CA  GLU A 420      28.307  51.990  11.974  1.00 17.62           C  
ATOM   3102  C   GLU A 420      27.824  50.553  12.160  1.00 15.63           C  
ATOM   3103  O   GLU A 420      28.507  49.602  11.778  1.00 13.98           O  
ATOM   3104  CB  GLU A 420      27.758  52.563  10.659  1.00 21.22           C  
ATOM   3105  CG  GLU A 420      28.060  51.715   9.435  1.00 26.81           C  
ATOM   3106  CD  GLU A 420      27.230  52.122   8.230  1.00 30.94           C  
ATOM   3107  OE1 GLU A 420      27.353  53.283   7.783  1.00 34.48           O  
ATOM   3108  OE2 GLU A 420      26.451  51.283   7.729  1.00 34.24           O  
ATOM   3109  N   LYS A 421      26.647  50.389  12.753  1.00 14.35           N  
ATOM   3110  CA  LYS A 421      26.130  49.051  12.988  1.00 13.10           C  
ATOM   3111  C   LYS A 421      25.607  48.375  11.723  1.00 13.41           C  
ATOM   3112  O   LYS A 421      25.701  47.149  11.585  1.00 11.54           O  
ATOM   3113  CB  LYS A 421      25.056  49.114  14.069  1.00 13.56           C  
ATOM   3114  CG  LYS A 421      25.659  49.355  15.448  1.00 15.90           C  
ATOM   3115  CD  LYS A 421      24.619  49.729  16.475  1.00 18.27           C  
ATOM   3116  CE  LYS A 421      24.263  51.204  16.374  1.00 19.20           C  
ATOM   3117  NZ  LYS A 421      25.446  52.071  16.698  1.00 19.59           N  
ATOM   3118  N   GLY A 422      25.070  49.169  10.801  1.00 12.07           N  
ATOM   3119  CA  GLY A 422      24.559  48.605   9.559  1.00 12.79           C  
ATOM   3120  C   GLY A 422      23.086  48.250   9.613  1.00 12.19           C  
ATOM   3121  O   GLY A 422      22.473  47.964   8.580  1.00 13.88           O  
ATOM   3122  N   ILE A 423      22.518  48.242  10.814  1.00 12.70           N  
ATOM   3123  CA  ILE A 423      21.099  47.960  10.986  1.00 12.84           C  
ATOM   3124  C   ILE A 423      20.540  48.927  12.028  1.00 14.40           C  
ATOM   3125  O   ILE A 423      21.293  49.443  12.862  1.00 13.28           O  
ATOM   3126  CB  ILE A 423      20.852  46.502  11.417  1.00 12.91           C  
ATOM   3127  CG1 ILE A 423      21.650  46.165  12.681  1.00 10.50           C  
ATOM   3128  CG2 ILE A 423      21.237  45.567  10.262  1.00 10.47           C  
ATOM   3129  CD1 ILE A 423      21.213  44.828  13.336  1.00 10.58           C  
ATOM   3130  N   PRO A 424      19.217  49.199  11.991  1.00 14.99           N  
ATOM   3131  CA  PRO A 424      18.649  50.130  12.972  1.00 16.11           C  
ATOM   3132  C   PRO A 424      18.386  49.550  14.351  1.00 16.78           C  
ATOM   3133  O   PRO A 424      17.238  49.288  14.722  1.00 17.13           O  
ATOM   3134  CB  PRO A 424      17.375  50.622  12.280  1.00 17.17           C  
ATOM   3135  CG  PRO A 424      16.944  49.439  11.512  1.00 16.89           C  
ATOM   3136  CD  PRO A 424      18.224  48.854  10.954  1.00 15.45           C  
ATOM   3137  N   VAL A 425      19.461  49.338  15.107  1.00 15.30           N  
ATOM   3138  CA  VAL A 425      19.347  48.821  16.454  1.00 14.27           C  
ATOM   3139  C   VAL A 425      20.178  49.747  17.335  1.00 15.02           C  
ATOM   3140  O   VAL A 425      21.308  50.112  16.986  1.00 14.25           O  
ATOM   3141  CB  VAL A 425      19.898  47.383  16.569  1.00 14.27           C  
ATOM   3142  CG1 VAL A 425      19.839  46.913  18.020  1.00 13.91           C  
ATOM   3143  CG2 VAL A 425      19.101  46.444  15.663  1.00 13.73           C  
ATOM   3144  N   ASN A 426      19.593  50.126  18.462  1.00 15.98           N  
ATOM   3145  CA  ASN A 426      20.230  51.008  19.424  1.00 18.25           C  
ATOM   3146  C   ASN A 426      21.067  50.162  20.378  1.00 17.28           C  
ATOM   3147  O   ASN A 426      20.527  49.360  21.137  1.00 19.05           O  
ATOM   3148  CB  ASN A 426      19.146  51.767  20.199  1.00 21.24           C  
ATOM   3149  CG  ASN A 426      19.718  52.745  21.217  1.00 25.70           C  
ATOM   3150  OD1 ASN A 426      18.970  53.477  21.872  1.00 29.77           O  
ATOM   3151  ND2 ASN A 426      21.038  52.759  21.361  1.00 26.92           N  
ATOM   3152  N   ILE A 427      22.381  50.338  20.330  1.00 16.35           N  
ATOM   3153  CA  ILE A 427      23.269  49.584  21.212  1.00 14.24           C  
ATOM   3154  C   ILE A 427      24.219  50.534  21.923  1.00 14.25           C  
ATOM   3155  O   ILE A 427      24.729  51.490  21.331  1.00 14.46           O  
ATOM   3156  CB  ILE A 427      24.110  48.538  20.432  1.00 13.75           C  
ATOM   3157  CG1 ILE A 427      23.192  47.585  19.647  1.00 12.75           C  
ATOM   3158  CG2 ILE A 427      24.947  47.730  21.407  1.00  9.72           C  
ATOM   3159  CD1 ILE A 427      23.976  46.600  18.721  1.00 12.13           C  
ATOM   3160  N   SER A 428      24.440  50.284  23.209  1.00 15.30           N  
ATOM   3161  CA  SER A 428      25.339  51.136  23.960  1.00 16.20           C  
ATOM   3162  C   SER A 428      26.690  51.130  23.261  1.00 16.80           C  
ATOM   3163  O   SER A 428      27.087  50.116  22.672  1.00 16.93           O  
ATOM   3164  CB  SER A 428      25.496  50.621  25.386  1.00 16.30           C  
ATOM   3165  OG  SER A 428      26.558  51.300  26.035  1.00 16.16           O  
ATOM   3166  N   ALA A 429      27.387  52.261  23.302  1.00 15.36           N  
ATOM   3167  CA  ALA A 429      28.708  52.362  22.683  1.00 16.89           C  
ATOM   3168  C   ALA A 429      29.746  52.525  23.799  1.00 16.76           C  
ATOM   3169  O   ALA A 429      30.914  52.820  23.546  1.00 17.54           O  
ATOM   3170  CB  ALA A 429      28.757  53.564  21.733  1.00 16.09           C  
ATOM   3171  N   ASN A 430      29.296  52.301  25.031  1.00 20.08           N  
ATOM   3172  CA  ASN A 430      30.124  52.446  26.226  1.00 21.74           C  
ATOM   3173  C   ASN A 430      30.970  51.203  26.520  1.00 23.27           C  
ATOM   3174  O   ASN A 430      30.545  50.306  27.248  1.00 22.11           O  
ATOM   3175  CB  ASN A 430      29.224  52.751  27.425  1.00 23.58           C  
ATOM   3176  CG  ASN A 430      30.002  53.203  28.637  1.00 25.85           C  
ATOM   3177  OD1 ASN A 430      31.222  53.058  28.690  1.00 25.95           O  
ATOM   3178  ND2 ASN A 430      29.293  53.746  29.630  1.00 26.95           N  
ATOM   3179  N   ARG A 431      32.172  51.170  25.958  1.00 24.83           N  
ATOM   3180  CA  ARG A 431      33.087  50.046  26.149  1.00 27.77           C  
ATOM   3181  C   ARG A 431      33.470  49.834  27.619  1.00 29.71           C  
ATOM   3182  O   ARG A 431      33.465  48.704  28.116  1.00 29.02           O  
ATOM   3183  CB  ARG A 431      34.350  50.271  25.319  1.00 29.56           C  
ATOM   3184  CG  ARG A 431      35.439  49.234  25.528  1.00 32.58           C  
ATOM   3185  CD  ARG A 431      35.164  47.975  24.737  1.00 35.37           C  
ATOM   3186  NE  ARG A 431      36.137  46.920  25.018  1.00 37.13           N  
ATOM   3187  CZ  ARG A 431      36.275  46.322  26.199  1.00 38.91           C  
ATOM   3188  NH1 ARG A 431      35.504  46.674  27.224  1.00 39.62           N  
ATOM   3189  NH2 ARG A 431      37.175  45.356  26.353  1.00 39.21           N  
ATOM   3190  N   SER A 432      33.806  50.915  28.316  1.00 31.07           N  
ATOM   3191  CA  SER A 432      34.198  50.806  29.720  1.00 32.75           C  
ATOM   3192  C   SER A 432      33.137  50.142  30.589  1.00 33.04           C  
ATOM   3193  O   SER A 432      33.459  49.494  31.586  1.00 34.74           O  
ATOM   3194  CB  SER A 432      34.525  52.190  30.293  1.00 32.75           C  
ATOM   3195  OG  SER A 432      35.654  52.743  29.647  1.00 35.51           O  
ATOM   3196  N   ALA A 433      31.875  50.299  30.210  1.00 32.44           N  
ATOM   3197  CA  ALA A 433      30.772  49.720  30.965  1.00 31.66           C  
ATOM   3198  C   ALA A 433      30.441  48.297  30.516  1.00 30.94           C  
ATOM   3199  O   ALA A 433      29.518  47.670  31.048  1.00 31.71           O  
ATOM   3200  CB  ALA A 433      29.536  50.601  30.831  1.00 32.58           C  
ATOM   3201  N   TYR A 434      31.188  47.784  29.545  1.00 28.94           N  
ATOM   3202  CA  TYR A 434      30.924  46.435  29.053  1.00 26.84           C  
ATOM   3203  C   TYR A 434      31.170  45.347  30.085  1.00 26.08           C  
ATOM   3204  O   TYR A 434      32.198  45.324  30.751  1.00 26.15           O  
ATOM   3205  CB  TYR A 434      31.767  46.102  27.820  1.00 25.01           C  
ATOM   3206  CG  TYR A 434      31.529  44.673  27.383  1.00 23.22           C  
ATOM   3207  CD1 TYR A 434      30.292  44.284  26.868  1.00 22.00           C  
ATOM   3208  CD2 TYR A 434      32.494  43.685  27.589  1.00 23.80           C  
ATOM   3209  CE1 TYR A 434      30.011  42.947  26.575  1.00 19.10           C  
ATOM   3210  CE2 TYR A 434      32.221  42.341  27.297  1.00 20.84           C  
ATOM   3211  CZ  TYR A 434      30.976  41.983  26.796  1.00 20.12           C  
ATOM   3212  OH  TYR A 434      30.683  40.662  26.545  1.00 17.55           O  
ATOM   3213  N   LYS A 435      30.218  44.432  30.186  1.00 25.46           N  
ATOM   3214  CA  LYS A 435      30.321  43.310  31.103  1.00 25.15           C  
ATOM   3215  C   LYS A 435      29.539  42.136  30.547  1.00 22.59           C  
ATOM   3216  O   LYS A 435      28.411  42.310  30.076  1.00 22.08           O  
ATOM   3217  CB  LYS A 435      29.720  43.656  32.466  1.00 26.50           C  
ATOM   3218  CG  LYS A 435      30.655  44.318  33.452  1.00 30.23           C  
ATOM   3219  CD  LYS A 435      29.961  44.431  34.801  1.00 33.27           C  
ATOM   3220  CE  LYS A 435      30.941  44.239  35.946  1.00 35.25           C  
ATOM   3221  NZ  LYS A 435      30.249  44.253  37.259  1.00 36.50           N  
ATOM   3222  N   PRO A 436      30.121  40.928  30.574  1.00 20.86           N  
ATOM   3223  CA  PRO A 436      29.330  39.810  30.048  1.00 19.60           C  
ATOM   3224  C   PRO A 436      28.134  39.652  30.980  1.00 18.95           C  
ATOM   3225  O   PRO A 436      28.204  40.037  32.148  1.00 18.99           O  
ATOM   3226  CB  PRO A 436      30.306  38.627  30.119  1.00 18.61           C  
ATOM   3227  CG  PRO A 436      31.247  39.026  31.248  1.00 19.38           C  
ATOM   3228  CD  PRO A 436      31.476  40.488  30.964  1.00 20.52           C  
ATOM   3229  N   VAL A 437      27.043  39.090  30.477  1.00 18.46           N  
ATOM   3230  CA  VAL A 437      25.835  38.910  31.271  1.00 21.34           C  
ATOM   3231  C   VAL A 437      25.797  37.561  31.989  1.00 22.25           C  
ATOM   3232  O   VAL A 437      26.347  36.575  31.499  1.00 21.68           O  
ATOM   3233  CB  VAL A 437      24.572  39.028  30.369  1.00 20.37           C  
ATOM   3234  CG1 VAL A 437      23.308  38.857  31.187  1.00 23.08           C  
ATOM   3235  CG2 VAL A 437      24.562  40.366  29.677  1.00 20.63           C  
ATOM   3236  N   LYS A 438      25.155  37.531  33.160  1.00 22.98           N  
ATOM   3237  CA  LYS A 438      25.012  36.299  33.925  1.00 23.84           C  
ATOM   3238  C   LYS A 438      23.812  35.562  33.359  1.00 24.72           C  
ATOM   3239  O   LYS A 438      22.753  36.151  33.158  1.00 24.62           O  
ATOM   3240  CB  LYS A 438      24.746  36.590  35.410  1.00 25.89           C  
ATOM   3241  CG  LYS A 438      25.956  36.477  36.320  1.00 30.01           C  
ATOM   3242  CD  LYS A 438      26.986  37.556  36.039  1.00 33.20           C  
ATOM   3243  CE  LYS A 438      28.144  37.482  37.039  1.00 35.23           C  
ATOM   3244  NZ  LYS A 438      29.130  38.597  36.868  1.00 35.83           N  
ATOM   3245  N   ILE A 439      23.980  34.273  33.099  1.00 25.62           N  
ATOM   3246  CA  ILE A 439      22.901  33.457  32.561  1.00 26.77           C  
ATOM   3247  C   ILE A 439      22.788  32.225  33.449  1.00 26.67           C  
ATOM   3248  O   ILE A 439      23.799  31.646  33.849  1.00 25.85           O  
ATOM   3249  CB  ILE A 439      23.197  33.058  31.093  1.00 27.72           C  
ATOM   3250  CG1 ILE A 439      23.223  34.322  30.227  1.00 28.80           C  
ATOM   3251  CG2 ILE A 439      22.143  32.080  30.577  1.00 27.97           C  
ATOM   3252  CD1 ILE A 439      23.437  34.066  28.754  1.00 29.94           C  
ATOM   3253  N   LYS A 440      21.567  31.825  33.773  1.00 26.78           N  
ATOM   3254  CA  LYS A 440      21.400  30.672  34.651  1.00 28.13           C  
ATOM   3255  C   LYS A 440      20.259  29.733  34.277  1.00 27.57           C  
ATOM   3256  O   LYS A 440      19.951  28.784  35.002  1.00 28.58           O  
ATOM   3257  CB  LYS A 440      21.249  31.185  36.089  1.00 29.95           C  
ATOM   3258  CG  LYS A 440      22.545  31.849  36.597  1.00 33.34           C  
ATOM   3259  CD  LYS A 440      22.308  33.029  37.550  1.00 35.36           C  
ATOM   3260  CE  LYS A 440      23.650  33.648  37.967  1.00 36.85           C  
ATOM   3261  NZ  LYS A 440      23.512  34.857  38.842  1.00 39.52           N  
ATOM   3262  N   ASP A 441      19.655  29.973  33.124  1.00 26.60           N  
ATOM   3263  CA  ASP A 441      18.543  29.147  32.694  1.00 26.02           C  
ATOM   3264  C   ASP A 441      18.907  28.125  31.629  1.00 23.91           C  
ATOM   3265  O   ASP A 441      18.031  27.450  31.110  1.00 23.79           O  
ATOM   3266  CB  ASP A 441      17.421  30.046  32.172  1.00 28.38           C  
ATOM   3267  CG  ASP A 441      17.836  30.842  30.945  1.00 31.05           C  
ATOM   3268  OD1 ASP A 441      19.001  31.289  30.889  1.00 31.93           O  
ATOM   3269  OD2 ASP A 441      16.993  31.029  30.041  1.00 33.81           O  
ATOM   3270  N   ILE A 442      20.188  27.985  31.308  1.00 20.39           N  
ATOM   3271  CA  ILE A 442      20.563  27.045  30.255  1.00 17.35           C  
ATOM   3272  C   ILE A 442      20.694  25.600  30.733  1.00 16.59           C  
ATOM   3273  O   ILE A 442      21.465  25.301  31.632  1.00 14.67           O  
ATOM   3274  CB  ILE A 442      21.883  27.473  29.574  1.00 17.99           C  
ATOM   3275  CG1 ILE A 442      21.764  28.908  29.066  1.00 18.81           C  
ATOM   3276  CG2 ILE A 442      22.182  26.553  28.391  1.00 17.55           C  
ATOM   3277  CD1 ILE A 442      20.475  29.193  28.309  1.00 20.09           C  
ATOM   3278  N   GLN A 443      19.928  24.698  30.137  1.00 15.64           N  
ATOM   3279  CA  GLN A 443      20.017  23.310  30.543  1.00 15.75           C  
ATOM   3280  C   GLN A 443      21.333  22.738  30.015  1.00 15.74           C  
ATOM   3281  O   GLN A 443      21.786  23.122  28.935  1.00 15.48           O  
ATOM   3282  CB  GLN A 443      18.830  22.523  29.989  1.00 19.38           C  
ATOM   3283  CG  GLN A 443      17.504  22.933  30.617  1.00 22.65           C  
ATOM   3284  CD  GLN A 443      17.506  22.724  32.127  1.00 24.69           C  
ATOM   3285  OE1 GLN A 443      17.725  21.608  32.607  1.00 26.44           O  
ATOM   3286  NE2 GLN A 443      17.273  23.796  32.882  1.00 26.51           N  
ATOM   3287  N   PRO A 444      21.976  21.850  30.786  1.00 13.19           N  
ATOM   3288  CA  PRO A 444      23.232  21.242  30.366  1.00 13.02           C  
ATOM   3289  C   PRO A 444      22.889  20.123  29.396  1.00 12.31           C  
ATOM   3290  O   PRO A 444      21.710  19.757  29.241  1.00 12.52           O  
ATOM   3291  CB  PRO A 444      23.809  20.722  31.675  1.00 11.89           C  
ATOM   3292  CG  PRO A 444      22.584  20.250  32.393  1.00 13.62           C  
ATOM   3293  CD  PRO A 444      21.576  21.353  32.119  1.00 13.61           C  
ATOM   3294  N   ILE A 445      23.899  19.596  28.715  1.00 12.66           N  
ATOM   3295  CA  ILE A 445      23.665  18.505  27.777  1.00 10.00           C  
ATOM   3296  C   ILE A 445      23.930  17.196  28.503  1.00 10.07           C  
ATOM   3297  O   ILE A 445      25.000  16.983  29.077  1.00  9.48           O  
ATOM   3298  CB  ILE A 445      24.597  18.586  26.545  1.00  9.97           C  
ATOM   3299  CG1 ILE A 445      24.357  19.897  25.782  1.00  9.51           C  
ATOM   3300  CG2 ILE A 445      24.331  17.369  25.630  1.00 10.00           C  
ATOM   3301  CD1 ILE A 445      22.939  20.030  25.185  1.00  9.71           C  
ATOM   3302  N   GLU A 446      22.950  16.308  28.480  1.00 12.02           N  
ATOM   3303  CA  GLU A 446      23.096  15.033  29.165  1.00 13.57           C  
ATOM   3304  C   GLU A 446      24.336  14.293  28.655  1.00 12.20           C  
ATOM   3305  O   GLU A 446      24.618  14.274  27.453  1.00 12.23           O  
ATOM   3306  CB  GLU A 446      21.813  14.207  28.964  1.00 17.15           C  
ATOM   3307  CG  GLU A 446      21.778  12.868  29.663  1.00 20.39           C  
ATOM   3308  CD  GLU A 446      22.357  11.766  28.802  1.00 23.45           C  
ATOM   3309  OE1 GLU A 446      21.989  11.712  27.601  1.00 25.32           O  
ATOM   3310  OE2 GLU A 446      23.164  10.957  29.319  1.00 21.44           O  
ATOM   3311  N   GLY A 447      25.105  13.724  29.572  1.00  9.74           N  
ATOM   3312  CA  GLY A 447      26.294  12.986  29.165  1.00 10.97           C  
ATOM   3313  C   GLY A 447      27.558  13.808  28.992  1.00 10.08           C  
ATOM   3314  O   GLY A 447      28.651  13.258  28.799  1.00 10.89           O  
ATOM   3315  N   ILE A 448      27.432  15.127  29.067  1.00 10.06           N  
ATOM   3316  CA  ILE A 448      28.596  15.999  28.922  1.00  8.37           C  
ATOM   3317  C   ILE A 448      28.745  16.796  30.212  1.00 10.03           C  
ATOM   3318  O   ILE A 448      27.910  17.636  30.537  1.00  9.51           O  
ATOM   3319  CB  ILE A 448      28.440  16.915  27.681  1.00  9.44           C  
ATOM   3320  CG1 ILE A 448      28.494  16.049  26.407  1.00  9.02           C  
ATOM   3321  CG2 ILE A 448      29.553  17.970  27.653  1.00 10.25           C  
ATOM   3322  CD1 ILE A 448      28.234  16.816  25.088  1.00  7.14           C  
ATOM   3323  N   ALA A 449      29.820  16.512  30.945  1.00 11.42           N  
ATOM   3324  CA  ALA A 449      30.074  17.153  32.241  1.00 13.91           C  
ATOM   3325  C   ALA A 449      30.584  18.585  32.218  1.00 13.63           C  
ATOM   3326  O   ALA A 449      31.697  18.865  32.674  1.00 15.42           O  
ATOM   3327  CB  ALA A 449      31.025  16.290  33.063  1.00 15.90           C  
ATOM   3328  N   LEU A 450      29.767  19.493  31.696  1.00 12.42           N  
ATOM   3329  CA  LEU A 450      30.126  20.902  31.664  1.00 10.20           C  
ATOM   3330  C   LEU A 450      28.923  21.693  32.143  1.00 10.26           C  
ATOM   3331  O   LEU A 450      27.787  21.432  31.735  1.00 10.83           O  
ATOM   3332  CB  LEU A 450      30.502  21.352  30.239  1.00 10.61           C  
ATOM   3333  CG  LEU A 450      31.797  20.774  29.649  1.00  9.70           C  
ATOM   3334  CD1 LEU A 450      31.959  21.224  28.202  1.00 11.50           C  
ATOM   3335  CD2 LEU A 450      33.006  21.234  30.463  1.00 12.57           C  
ATOM   3336  N   ASP A 451      29.186  22.657  33.012  1.00  9.01           N  
ATOM   3337  CA  ASP A 451      28.162  23.529  33.582  1.00  9.94           C  
ATOM   3338  C   ASP A 451      28.031  24.720  32.638  1.00  9.97           C  
ATOM   3339  O   ASP A 451      28.754  25.707  32.754  1.00  9.12           O  
ATOM   3340  CB  ASP A 451      28.625  24.006  34.962  1.00 12.32           C  
ATOM   3341  CG  ASP A 451      27.559  24.755  35.702  1.00 11.76           C  
ATOM   3342  OD1 ASP A 451      26.660  25.337  35.043  1.00 11.28           O  
ATOM   3343  OD2 ASP A 451      27.637  24.781  36.956  1.00 12.35           O  
ATOM   3344  N   LEU A 452      27.097  24.633  31.702  1.00  9.80           N  
ATOM   3345  CA  LEU A 452      26.963  25.694  30.724  1.00  9.53           C  
ATOM   3346  C   LEU A 452      26.648  27.043  31.335  1.00 11.05           C  
ATOM   3347  O   LEU A 452      27.188  28.061  30.897  1.00 11.06           O  
ATOM   3348  CB  LEU A 452      25.922  25.300  29.671  1.00  9.51           C  
ATOM   3349  CG  LEU A 452      26.118  23.891  29.106  1.00  7.44           C  
ATOM   3350  CD1 LEU A 452      25.137  23.700  27.959  1.00  8.42           C  
ATOM   3351  CD2 LEU A 452      27.559  23.673  28.602  1.00  9.84           C  
ATOM   3352  N   ASN A 453      25.790  27.075  32.356  1.00 11.79           N  
ATOM   3353  CA  ASN A 453      25.486  28.364  32.989  1.00 13.18           C  
ATOM   3354  C   ASN A 453      26.735  28.996  33.574  1.00 12.66           C  
ATOM   3355  O   ASN A 453      26.971  30.192  33.414  1.00 13.74           O  
ATOM   3356  CB  ASN A 453      24.471  28.204  34.118  1.00 14.35           C  
ATOM   3357  CG  ASN A 453      23.119  27.823  33.621  1.00 14.83           C  
ATOM   3358  OD1 ASN A 453      22.528  28.523  32.790  1.00 16.26           O  
ATOM   3359  ND2 ASN A 453      22.596  26.707  34.135  1.00 14.29           N  
ATOM   3360  N   ALA A 454      27.528  28.192  34.270  1.00 12.82           N  
ATOM   3361  CA  ALA A 454      28.738  28.709  34.888  1.00 13.26           C  
ATOM   3362  C   ALA A 454      29.713  29.211  33.831  1.00 12.48           C  
ATOM   3363  O   ALA A 454      30.239  30.327  33.937  1.00 11.91           O  
ATOM   3364  CB  ALA A 454      29.409  27.622  35.745  1.00 12.34           C  
ATOM   3365  N   LEU A 455      29.957  28.400  32.808  1.00 11.38           N  
ATOM   3366  CA  LEU A 455      30.903  28.801  31.773  1.00  9.84           C  
ATOM   3367  C   LEU A 455      30.483  30.070  31.034  1.00  9.72           C  
ATOM   3368  O   LEU A 455      31.300  30.947  30.786  1.00  9.63           O  
ATOM   3369  CB  LEU A 455      31.100  27.658  30.770  1.00 11.54           C  
ATOM   3370  CG  LEU A 455      31.676  26.396  31.415  1.00 11.70           C  
ATOM   3371  CD1 LEU A 455      31.581  25.220  30.445  1.00 13.22           C  
ATOM   3372  CD2 LEU A 455      33.119  26.659  31.822  1.00 13.01           C  
ATOM   3373  N   ILE A 456      29.211  30.174  30.682  1.00  8.98           N  
ATOM   3374  CA  ILE A 456      28.753  31.357  29.961  1.00 10.30           C  
ATOM   3375  C   ILE A 456      28.828  32.608  30.822  1.00 11.14           C  
ATOM   3376  O   ILE A 456      29.227  33.672  30.342  1.00 10.33           O  
ATOM   3377  CB  ILE A 456      27.318  31.181  29.481  1.00 10.33           C  
ATOM   3378  CG1 ILE A 456      27.267  30.014  28.495  1.00 12.14           C  
ATOM   3379  CG2 ILE A 456      26.813  32.473  28.829  1.00 10.88           C  
ATOM   3380  CD1 ILE A 456      25.886  29.512  28.241  1.00 12.48           C  
ATOM   3381  N   SER A 457      28.452  32.470  32.088  1.00 13.20           N  
ATOM   3382  CA  SER A 457      28.455  33.607  33.008  1.00 15.29           C  
ATOM   3383  C   SER A 457      29.841  34.149  33.302  1.00 16.83           C  
ATOM   3384  O   SER A 457      29.978  35.322  33.656  1.00 19.23           O  
ATOM   3385  CB  SER A 457      27.753  33.244  34.325  1.00 14.22           C  
ATOM   3386  OG  SER A 457      26.363  33.038  34.119  1.00 14.86           O  
ATOM   3387  N   LYS A 458      30.865  33.308  33.162  1.00 17.39           N  
ATOM   3388  CA  LYS A 458      32.254  33.719  33.395  1.00 18.45           C  
ATOM   3389  C   LYS A 458      32.748  34.663  32.306  1.00 17.03           C  
ATOM   3390  O   LYS A 458      33.670  35.449  32.528  1.00 17.79           O  
ATOM   3391  CB  LYS A 458      33.194  32.512  33.376  1.00 20.68           C  
ATOM   3392  CG  LYS A 458      33.019  31.528  34.485  1.00 26.90           C  
ATOM   3393  CD  LYS A 458      33.979  30.373  34.255  1.00 28.72           C  
ATOM   3394  CE  LYS A 458      33.991  29.409  35.414  1.00 31.04           C  
ATOM   3395  NZ  LYS A 458      35.234  28.609  35.344  1.00 31.22           N  
ATOM   3396  N   GLY A 459      32.140  34.584  31.126  1.00 13.52           N  
ATOM   3397  CA  GLY A 459      32.601  35.398  30.019  1.00 11.84           C  
ATOM   3398  C   GLY A 459      33.669  34.612  29.249  1.00 11.37           C  
ATOM   3399  O   GLY A 459      33.784  33.397  29.402  1.00 10.84           O  
ATOM   3400  N   ILE A 460      34.471  35.294  28.439  1.00  9.19           N  
ATOM   3401  CA  ILE A 460      35.515  34.620  27.655  1.00  8.42           C  
ATOM   3402  C   ILE A 460      36.778  34.371  28.502  1.00  9.40           C  
ATOM   3403  O   ILE A 460      37.385  35.312  29.001  1.00 11.52           O  
ATOM   3404  CB  ILE A 460      35.895  35.472  26.440  1.00  8.22           C  
ATOM   3405  CG1 ILE A 460      34.639  35.768  25.598  1.00  8.72           C  
ATOM   3406  CG2 ILE A 460      36.985  34.759  25.622  1.00  7.55           C  
ATOM   3407  CD1 ILE A 460      34.878  36.691  24.409  1.00  7.90           C  
ATOM   3408  N   THR A 461      37.180  33.117  28.669  1.00  7.32           N  
ATOM   3409  CA  THR A 461      38.364  32.830  29.479  1.00  6.33           C  
ATOM   3410  C   THR A 461      39.522  32.313  28.646  1.00  6.24           C  
ATOM   3411  O   THR A 461      39.334  31.849  27.519  1.00  7.08           O  
ATOM   3412  CB  THR A 461      38.057  31.774  30.565  1.00  5.56           C  
ATOM   3413  OG1 THR A 461      37.894  30.473  29.973  1.00  8.05           O  
ATOM   3414  CG2 THR A 461      36.782  32.130  31.278  1.00  5.06           C  
ATOM   3415  N   GLY A 462      40.728  32.409  29.190  1.00  5.17           N  
ATOM   3416  CA  GLY A 462      41.884  31.898  28.465  1.00  5.22           C  
ATOM   3417  C   GLY A 462      42.293  32.589  27.183  1.00  5.48           C  
ATOM   3418  O   GLY A 462      42.019  33.780  26.962  1.00  4.77           O  
ATOM   3419  N   LYS A 463      42.971  31.841  26.318  1.00  4.33           N  
ATOM   3420  CA  LYS A 463      43.458  32.400  25.064  1.00  4.95           C  
ATOM   3421  C   LYS A 463      43.661  31.276  24.046  1.00  5.85           C  
ATOM   3422  O   LYS A 463      43.493  30.096  24.370  1.00  6.98           O  
ATOM   3423  CB  LYS A 463      44.780  33.130  25.325  1.00  8.24           C  
ATOM   3424  CG  LYS A 463      45.927  32.249  25.746  1.00 13.27           C  
ATOM   3425  CD  LYS A 463      47.176  33.125  25.870  1.00 19.15           C  
ATOM   3426  CE  LYS A 463      48.455  32.373  25.619  1.00 22.63           C  
ATOM   3427  NZ  LYS A 463      49.581  33.354  25.529  1.00 22.84           N  
ATOM   3428  N   PRO A 464      44.005  31.624  22.795  1.00  5.41           N  
ATOM   3429  CA  PRO A 464      44.204  30.579  21.787  1.00  6.90           C  
ATOM   3430  C   PRO A 464      45.209  29.513  22.219  1.00  7.69           C  
ATOM   3431  O   PRO A 464      46.230  29.822  22.816  1.00  6.14           O  
ATOM   3432  CB  PRO A 464      44.677  31.366  20.569  1.00  5.73           C  
ATOM   3433  CG  PRO A 464      43.958  32.680  20.722  1.00  8.00           C  
ATOM   3434  CD  PRO A 464      44.136  32.962  22.195  1.00  7.23           C  
ATOM   3435  N   LEU A 465      44.909  28.254  21.913  1.00  7.12           N  
ATOM   3436  CA  LEU A 465      45.816  27.161  22.257  1.00  7.48           C  
ATOM   3437  C   LEU A 465      46.988  27.092  21.291  1.00  8.38           C  
ATOM   3438  O   LEU A 465      46.854  27.409  20.112  1.00  9.01           O  
ATOM   3439  CB  LEU A 465      45.099  25.817  22.190  1.00  7.38           C  
ATOM   3440  CG  LEU A 465      44.017  25.536  23.228  1.00  7.04           C  
ATOM   3441  CD1 LEU A 465      43.183  24.391  22.703  1.00  7.11           C  
ATOM   3442  CD2 LEU A 465      44.631  25.202  24.600  1.00  7.79           C  
ATOM   3443  N   SER A 466      48.132  26.650  21.806  1.00  8.97           N  
ATOM   3444  CA  SER A 466      49.330  26.498  20.991  1.00  8.29           C  
ATOM   3445  C   SER A 466      49.605  25.008  20.788  1.00  7.02           C  
ATOM   3446  O   SER A 466      49.002  24.149  21.439  1.00  7.65           O  
ATOM   3447  CB  SER A 466      50.528  27.141  21.691  1.00  7.42           C  
ATOM   3448  OG  SER A 466      50.822  26.440  22.887  1.00 12.58           O  
ATOM   3449  N   TRP A 467      50.494  24.700  19.859  1.00  7.98           N  
ATOM   3450  CA  TRP A 467      50.866  23.316  19.587  1.00  7.47           C  
ATOM   3451  C   TRP A 467      51.327  22.584  20.866  1.00  8.78           C  
ATOM   3452  O   TRP A 467      50.943  21.444  21.107  1.00  7.36           O  
ATOM   3453  CB  TRP A 467      51.968  23.302  18.518  1.00  8.44           C  
ATOM   3454  CG  TRP A 467      52.794  22.016  18.387  1.00  9.23           C  
ATOM   3455  CD1 TRP A 467      54.114  21.860  18.708  1.00  9.59           C  
ATOM   3456  CD2 TRP A 467      52.353  20.740  17.885  1.00  9.48           C  
ATOM   3457  NE1 TRP A 467      54.524  20.576  18.442  1.00 10.46           N  
ATOM   3458  CE2 TRP A 467      53.462  19.866  17.937  1.00 10.09           C  
ATOM   3459  CE3 TRP A 467      51.130  20.254  17.400  1.00  7.05           C  
ATOM   3460  CZ2 TRP A 467      53.386  18.529  17.527  1.00  9.80           C  
ATOM   3461  CZ3 TRP A 467      51.051  18.918  16.990  1.00  8.37           C  
ATOM   3462  CH2 TRP A 467      52.176  18.072  17.056  1.00  8.97           C  
ATOM   3463  N   ASP A 468      52.140  23.231  21.694  1.00  9.16           N  
ATOM   3464  CA  ASP A 468      52.611  22.555  22.903  1.00 11.87           C  
ATOM   3465  C   ASP A 468      51.510  22.170  23.880  1.00 11.42           C  
ATOM   3466  O   ASP A 468      51.702  21.292  24.721  1.00 12.12           O  
ATOM   3467  CB  ASP A 468      53.675  23.397  23.621  1.00 15.77           C  
ATOM   3468  CG  ASP A 468      55.025  23.322  22.930  1.00 22.12           C  
ATOM   3469  OD1 ASP A 468      55.449  22.190  22.614  1.00 24.45           O  
ATOM   3470  OD2 ASP A 468      55.664  24.379  22.700  1.00 23.87           O  
ATOM   3471  N   GLU A 469      50.349  22.809  23.775  1.00 10.07           N  
ATOM   3472  CA  GLU A 469      49.252  22.487  24.683  1.00  9.06           C  
ATOM   3473  C   GLU A 469      48.418  21.289  24.248  1.00  9.84           C  
ATOM   3474  O   GLU A 469      47.635  20.751  25.042  1.00  8.90           O  
ATOM   3475  CB  GLU A 469      48.355  23.709  24.869  1.00  9.08           C  
ATOM   3476  CG  GLU A 469      49.095  24.862  25.519  1.00 13.25           C  
ATOM   3477  CD  GLU A 469      48.249  26.106  25.655  1.00 15.03           C  
ATOM   3478  OE1 GLU A 469      48.223  26.900  24.700  1.00 14.88           O  
ATOM   3479  OE2 GLU A 469      47.611  26.280  26.716  1.00 16.05           O  
ATOM   3480  N   VAL A 470      48.584  20.866  22.996  1.00  8.86           N  
ATOM   3481  CA  VAL A 470      47.825  19.738  22.501  1.00  8.36           C  
ATOM   3482  C   VAL A 470      48.678  18.574  21.980  1.00  8.20           C  
ATOM   3483  O   VAL A 470      48.173  17.468  21.880  1.00  6.50           O  
ATOM   3484  CB  VAL A 470      46.843  20.151  21.346  1.00  7.71           C  
ATOM   3485  CG1 VAL A 470      45.960  21.310  21.774  1.00  7.06           C  
ATOM   3486  CG2 VAL A 470      47.632  20.509  20.057  1.00  8.20           C  
ATOM   3487  N   ARG A 471      49.956  18.805  21.670  1.00  6.60           N  
ATOM   3488  CA  ARG A 471      50.808  17.752  21.074  1.00  8.27           C  
ATOM   3489  C   ARG A 471      50.961  16.415  21.806  1.00  9.64           C  
ATOM   3490  O   ARG A 471      50.798  16.330  23.019  1.00  9.54           O  
ATOM   3491  CB  ARG A 471      52.232  18.293  20.811  1.00  7.44           C  
ATOM   3492  CG  ARG A 471      53.016  18.617  22.095  1.00  9.73           C  
ATOM   3493  CD  ARG A 471      54.430  19.141  21.794  1.00 12.43           C  
ATOM   3494  NE  ARG A 471      55.242  19.352  23.004  1.00 14.54           N  
ATOM   3495  CZ  ARG A 471      55.737  18.386  23.779  1.00 16.98           C  
ATOM   3496  NH1 ARG A 471      55.524  17.100  23.507  1.00 14.92           N  
ATOM   3497  NH2 ARG A 471      56.458  18.709  24.853  1.00 19.12           N  
ATOM   3498  N   PRO A 472      51.217  15.334  21.048  1.00  9.54           N  
ATOM   3499  CA  PRO A 472      51.405  14.023  21.684  1.00 10.33           C  
ATOM   3500  C   PRO A 472      52.556  14.211  22.690  1.00 10.80           C  
ATOM   3501  O   PRO A 472      53.537  14.939  22.417  1.00 10.26           O  
ATOM   3502  CB  PRO A 472      51.812  13.128  20.522  1.00 10.80           C  
ATOM   3503  CG  PRO A 472      51.051  13.716  19.357  1.00 10.05           C  
ATOM   3504  CD  PRO A 472      51.181  15.222  19.580  1.00 10.00           C  
ATOM   3505  N   TYR A 473      52.460  13.544  23.834  1.00 10.03           N  
ATOM   3506  CA  TYR A 473      53.472  13.726  24.872  1.00 11.13           C  
ATOM   3507  C   TYR A 473      54.898  13.459  24.441  1.00 10.67           C  
ATOM   3508  O   TYR A 473      55.826  14.076  24.951  1.00 12.44           O  
ATOM   3509  CB  TYR A 473      53.167  12.856  26.100  1.00 10.98           C  
ATOM   3510  CG  TYR A 473      53.130  11.359  25.841  1.00 11.73           C  
ATOM   3511  CD1 TYR A 473      54.307  10.607  25.823  1.00 12.17           C  
ATOM   3512  CD2 TYR A 473      51.919  10.689  25.637  1.00 13.88           C  
ATOM   3513  CE1 TYR A 473      54.278   9.222  25.609  1.00 11.66           C  
ATOM   3514  CE2 TYR A 473      51.884   9.299  25.425  1.00 12.93           C  
ATOM   3515  CZ  TYR A 473      53.069   8.583  25.414  1.00 11.49           C  
ATOM   3516  OH  TYR A 473      53.065   7.213  25.207  1.00 12.07           O  
ATOM   3517  N   TRP A 474      55.061  12.568  23.479  1.00  9.08           N  
ATOM   3518  CA  TRP A 474      56.386  12.161  23.020  1.00  9.35           C  
ATOM   3519  C   TRP A 474      56.934  12.889  21.804  1.00  9.86           C  
ATOM   3520  O   TRP A 474      58.096  12.667  21.408  1.00  8.92           O  
ATOM   3521  CB  TRP A 474      56.329  10.685  22.703  1.00  7.32           C  
ATOM   3522  CG  TRP A 474      55.214  10.357  21.740  1.00  7.69           C  
ATOM   3523  CD1 TRP A 474      53.936   9.989  22.059  1.00  7.65           C  
ATOM   3524  CD2 TRP A 474      55.285  10.351  20.308  1.00  7.07           C  
ATOM   3525  NE1 TRP A 474      53.211   9.747  20.916  1.00  6.57           N  
ATOM   3526  CE2 TRP A 474      54.013   9.963  19.828  1.00  8.51           C  
ATOM   3527  CE3 TRP A 474      56.299  10.633  19.381  1.00  7.31           C  
ATOM   3528  CZ2 TRP A 474      53.732   9.852  18.460  1.00  8.34           C  
ATOM   3529  CZ3 TRP A 474      56.018  10.524  18.029  1.00  7.48           C  
ATOM   3530  CH2 TRP A 474      54.742  10.136  17.579  1.00  8.18           C  
ATOM   3531  N   LEU A 475      56.116  13.757  21.215  1.00  9.80           N  
ATOM   3532  CA  LEU A 475      56.492  14.484  19.999  1.00 11.10           C  
ATOM   3533  C   LEU A 475      56.715  15.978  20.208  1.00 12.59           C  
ATOM   3534  O   LEU A 475      55.783  16.724  20.471  1.00 14.18           O  
ATOM   3535  CB  LEU A 475      55.393  14.298  18.954  1.00 11.81           C  
ATOM   3536  CG  LEU A 475      55.659  14.851  17.559  1.00 10.50           C  
ATOM   3537  CD1 LEU A 475      56.856  14.153  16.955  1.00 13.38           C  
ATOM   3538  CD2 LEU A 475      54.420  14.666  16.691  1.00 14.45           C  
ATOM   3539  N   LYS A 476      57.952  16.424  20.067  1.00 13.88           N  
ATOM   3540  CA  LYS A 476      58.239  17.839  20.246  1.00 15.02           C  
ATOM   3541  C   LYS A 476      57.960  18.662  18.981  1.00 13.33           C  
ATOM   3542  O   LYS A 476      57.341  19.726  19.053  1.00 12.72           O  
ATOM   3543  CB  LYS A 476      59.704  18.021  20.642  1.00 18.89           C  
ATOM   3544  CG  LYS A 476      60.147  17.133  21.792  1.00 26.05           C  
ATOM   3545  CD  LYS A 476      61.674  17.101  21.910  1.00 29.73           C  
ATOM   3546  CE  LYS A 476      62.133  15.934  22.789  1.00 31.72           C  
ATOM   3547  NZ  LYS A 476      63.607  15.948  23.020  1.00 33.72           N  
ATOM   3548  N   GLU A 477      58.408  18.170  17.828  1.00 11.87           N  
ATOM   3549  CA  GLU A 477      58.243  18.894  16.575  1.00 11.28           C  
ATOM   3550  C   GLU A 477      56.930  18.673  15.843  1.00 10.67           C  
ATOM   3551  O   GLU A 477      56.515  17.536  15.609  1.00 10.32           O  
ATOM   3552  CB  GLU A 477      59.393  18.559  15.621  1.00 14.15           C  
ATOM   3553  CG  GLU A 477      60.754  18.853  16.208  1.00 17.59           C  
ATOM   3554  CD  GLU A 477      61.886  18.753  15.189  1.00 21.16           C  
ATOM   3555  OE1 GLU A 477      61.693  18.152  14.099  1.00 16.26           O  
ATOM   3556  OE2 GLU A 477      62.976  19.280  15.504  1.00 23.85           O  
ATOM   3557  N   MET A 478      56.285  19.770  15.463  1.00  9.62           N  
ATOM   3558  CA  MET A 478      55.024  19.685  14.747  1.00  9.46           C  
ATOM   3559  C   MET A 478      55.266  19.048  13.379  1.00 10.24           C  
ATOM   3560  O   MET A 478      56.134  19.491  12.619  1.00 11.27           O  
ATOM   3561  CB  MET A 478      54.430  21.093  14.571  1.00 12.62           C  
ATOM   3562  CG  MET A 478      53.137  21.153  13.764  1.00 12.75           C  
ATOM   3563  SD  MET A 478      52.744  22.855  13.354  1.00 16.42           S  
ATOM   3564  CE  MET A 478      52.162  23.382  14.901  1.00 10.55           C  
ATOM   3565  N   PRO A 479      54.519  17.984  13.050  1.00  9.66           N  
ATOM   3566  CA  PRO A 479      54.721  17.352  11.749  1.00  9.64           C  
ATOM   3567  C   PRO A 479      53.999  18.143  10.671  1.00  9.10           C  
ATOM   3568  O   PRO A 479      53.303  19.118  10.966  1.00 10.94           O  
ATOM   3569  CB  PRO A 479      54.100  15.959  11.904  1.00 10.44           C  
ATOM   3570  CG  PRO A 479      53.613  15.871  13.300  1.00 11.26           C  
ATOM   3571  CD  PRO A 479      53.509  17.264  13.849  1.00  9.33           C  
ATOM   3572  N   GLY A 480      54.163  17.704   9.433  1.00  9.56           N  
ATOM   3573  CA  GLY A 480      53.487  18.343   8.320  1.00  8.94           C  
ATOM   3574  C   GLY A 480      54.274  19.467   7.664  1.00  7.82           C  
ATOM   3575  O   GLY A 480      55.216  20.011   8.235  1.00  7.36           O  
ATOM   3576  N   THR A 481      53.856  19.829   6.465  1.00  7.67           N  
ATOM   3577  CA  THR A 481      54.520  20.879   5.721  1.00  9.53           C  
ATOM   3578  C   THR A 481      53.610  22.075   5.498  1.00  8.39           C  
ATOM   3579  O   THR A 481      54.082  23.164   5.156  1.00 10.21           O  
ATOM   3580  CB  THR A 481      54.988  20.343   4.326  1.00 11.23           C  
ATOM   3581  OG1 THR A 481      53.847  20.023   3.508  1.00 12.36           O  
ATOM   3582  CG2 THR A 481      55.806  19.069   4.497  1.00 11.55           C  
ATOM   3583  N   TYR A 482      52.314  21.879   5.722  1.00  6.73           N  
ATOM   3584  CA  TYR A 482      51.297  22.904   5.456  1.00  6.31           C  
ATOM   3585  C   TYR A 482      50.980  23.929   6.537  1.00  6.31           C  
ATOM   3586  O   TYR A 482      50.747  25.094   6.229  1.00  6.84           O  
ATOM   3587  CB  TYR A 482      49.992  22.193   5.054  1.00  6.23           C  
ATOM   3588  CG  TYR A 482      48.935  23.092   4.464  1.00  6.16           C  
ATOM   3589  CD1 TYR A 482      49.008  23.503   3.126  1.00  4.84           C  
ATOM   3590  CD2 TYR A 482      47.852  23.519   5.228  1.00  6.95           C  
ATOM   3591  CE1 TYR A 482      48.030  24.308   2.567  1.00  5.62           C  
ATOM   3592  CE2 TYR A 482      46.863  24.325   4.671  1.00  6.65           C  
ATOM   3593  CZ  TYR A 482      46.960  24.716   3.346  1.00  6.23           C  
ATOM   3594  OH  TYR A 482      45.995  25.524   2.801  1.00  5.76           O  
ATOM   3595  N   ALA A 483      50.966  23.498   7.793  1.00  6.69           N  
ATOM   3596  CA  ALA A 483      50.616  24.374   8.905  1.00  7.66           C  
ATOM   3597  C   ALA A 483      51.361  25.696   8.962  1.00 10.12           C  
ATOM   3598  O   ALA A 483      50.758  26.757   9.128  1.00  9.00           O  
ATOM   3599  CB  ALA A 483      50.796  23.627  10.222  1.00 10.69           C  
ATOM   3600  N   LEU A 484      52.675  25.625   8.830  1.00 10.09           N  
ATOM   3601  CA  LEU A 484      53.506  26.816   8.913  1.00 11.12           C  
ATOM   3602  C   LEU A 484      53.760  27.559   7.610  1.00 12.42           C  
ATOM   3603  O   LEU A 484      54.319  28.654   7.634  1.00 11.04           O  
ATOM   3604  CB  LEU A 484      54.859  26.431   9.515  1.00 12.24           C  
ATOM   3605  CG  LEU A 484      54.817  25.724  10.866  1.00 13.18           C  
ATOM   3606  CD1 LEU A 484      56.244  25.334  11.291  1.00 14.23           C  
ATOM   3607  CD2 LEU A 484      54.188  26.651  11.894  1.00 11.22           C  
ATOM   3608  N   THR A 485      53.321  26.994   6.487  1.00 12.11           N  
ATOM   3609  CA  THR A 485      53.616  27.571   5.175  1.00 12.20           C  
ATOM   3610  C   THR A 485      52.453  27.790   4.193  1.00 12.53           C  
ATOM   3611  O   THR A 485      52.599  28.520   3.209  1.00 11.26           O  
ATOM   3612  CB  THR A 485      54.574  26.658   4.450  1.00 12.23           C  
ATOM   3613  OG1 THR A 485      53.853  25.476   4.078  1.00 12.63           O  
ATOM   3614  CG2 THR A 485      55.718  26.254   5.349  1.00 11.46           C  
ATOM   3615  N   ALA A 486      51.324  27.139   4.444  1.00 11.35           N  
ATOM   3616  CA  ALA A 486      50.162  27.213   3.561  1.00 11.56           C  
ATOM   3617  C   ALA A 486      50.492  26.611   2.181  1.00 10.86           C  
ATOM   3618  O   ALA A 486      49.844  26.925   1.177  1.00 11.00           O  
ATOM   3619  CB  ALA A 486      49.660  28.672   3.428  1.00 11.08           C  
ATOM   3620  N   ARG A 487      51.474  25.713   2.144  1.00 10.90           N  
ATOM   3621  CA  ARG A 487      51.856  25.061   0.894  1.00 13.05           C  
ATOM   3622  C   ARG A 487      52.445  23.674   1.174  1.00 12.81           C  
ATOM   3623  O   ARG A 487      53.258  23.513   2.073  1.00 14.02           O  
ATOM   3624  CB  ARG A 487      52.911  25.904   0.156  1.00 15.78           C  
ATOM   3625  CG  ARG A 487      54.330  25.659   0.653  1.00 19.54           C  
ATOM   3626  CD  ARG A 487      55.249  26.856   0.424  1.00 25.63           C  
ATOM   3627  NE  ARG A 487      54.908  27.949   1.331  1.00 28.41           N  
ATOM   3628  CZ  ARG A 487      55.444  29.166   1.295  1.00 28.27           C  
ATOM   3629  NH1 ARG A 487      56.364  29.472   0.382  1.00 27.45           N  
ATOM   3630  NH2 ARG A 487      55.056  30.071   2.185  1.00 26.03           N  
ATOM   3631  N   LEU A 488      52.045  22.669   0.404  1.00 10.39           N  
ATOM   3632  CA  LEU A 488      52.597  21.337   0.598  1.00  9.60           C  
ATOM   3633  C   LEU A 488      53.984  21.328  -0.005  1.00 11.73           C  
ATOM   3634  O   LEU A 488      54.260  22.092  -0.936  1.00 12.70           O  
ATOM   3635  CB  LEU A 488      51.741  20.270  -0.112  1.00  8.30           C  
ATOM   3636  CG  LEU A 488      50.387  19.900   0.505  1.00  6.68           C  
ATOM   3637  CD1 LEU A 488      49.667  18.978  -0.476  1.00  5.68           C  
ATOM   3638  CD2 LEU A 488      50.588  19.195   1.870  1.00  5.46           C  
ATOM   3639  N   SER A 489      54.861  20.486   0.530  1.00 11.89           N  
ATOM   3640  CA  SER A 489      56.214  20.362  -0.021  1.00 12.47           C  
ATOM   3641  C   SER A 489      56.057  19.772  -1.427  1.00 12.18           C  
ATOM   3642  O   SER A 489      55.006  19.222  -1.751  1.00 10.78           O  
ATOM   3643  CB  SER A 489      57.051  19.443   0.866  1.00 14.29           C  
ATOM   3644  OG  SER A 489      56.405  18.204   1.056  1.00 16.53           O  
ATOM   3645  N   ALA A 490      57.083  19.884  -2.270  1.00 11.84           N  
ATOM   3646  CA  ALA A 490      56.964  19.381  -3.641  1.00 12.73           C  
ATOM   3647  C   ALA A 490      56.434  17.957  -3.788  1.00 11.75           C  
ATOM   3648  O   ALA A 490      55.505  17.724  -4.568  1.00 11.84           O  
ATOM   3649  CB  ALA A 490      58.308  19.521  -4.376  1.00 12.11           C  
ATOM   3650  N   ASP A 491      57.013  17.005  -3.056  1.00 12.43           N  
ATOM   3651  CA  ASP A 491      56.584  15.608  -3.138  1.00 11.55           C  
ATOM   3652  C   ASP A 491      55.113  15.385  -2.773  1.00 10.25           C  
ATOM   3653  O   ASP A 491      54.387  14.640  -3.448  1.00  7.36           O  
ATOM   3654  CB  ASP A 491      57.469  14.719  -2.236  1.00 16.08           C  
ATOM   3655  CG  ASP A 491      57.583  15.248  -0.787  1.00 21.61           C  
ATOM   3656  OD1 ASP A 491      56.896  16.231  -0.423  1.00 24.55           O  
ATOM   3657  OD2 ASP A 491      58.370  14.672  -0.001  1.00 25.73           O  
ATOM   3658  N   ARG A 492      54.680  16.012  -1.688  1.00  7.34           N  
ATOM   3659  CA  ARG A 492      53.302  15.861  -1.256  1.00  6.76           C  
ATOM   3660  C   ARG A 492      52.329  16.569  -2.184  1.00  7.41           C  
ATOM   3661  O   ARG A 492      51.203  16.102  -2.383  1.00  7.74           O  
ATOM   3662  CB  ARG A 492      53.155  16.357   0.177  1.00  5.64           C  
ATOM   3663  CG  ARG A 492      53.968  15.501   1.108  1.00  8.28           C  
ATOM   3664  CD  ARG A 492      53.847  15.909   2.554  1.00  6.63           C  
ATOM   3665  NE  ARG A 492      54.504  14.904   3.386  1.00  8.80           N  
ATOM   3666  CZ  ARG A 492      54.364  14.810   4.703  1.00  7.60           C  
ATOM   3667  NH1 ARG A 492      53.599  15.660   5.356  1.00  5.75           N  
ATOM   3668  NH2 ARG A 492      54.977  13.836   5.357  1.00  9.44           N  
ATOM   3669  N   ALA A 493      52.762  17.688  -2.760  1.00  6.46           N  
ATOM   3670  CA  ALA A 493      51.917  18.416  -3.691  1.00  6.59           C  
ATOM   3671  C   ALA A 493      51.675  17.587  -4.953  1.00  5.89           C  
ATOM   3672  O   ALA A 493      50.574  17.626  -5.514  1.00  7.36           O  
ATOM   3673  CB  ALA A 493      52.558  19.757  -4.057  1.00  7.42           C  
ATOM   3674  N   ALA A 494      52.689  16.839  -5.405  1.00  5.18           N  
ATOM   3675  CA  ALA A 494      52.530  16.014  -6.601  1.00  5.71           C  
ATOM   3676  C   ALA A 494      51.504  14.909  -6.345  1.00  6.03           C  
ATOM   3677  O   ALA A 494      50.638  14.637  -7.189  1.00  5.87           O  
ATOM   3678  CB  ALA A 494      53.887  15.406  -7.039  1.00  7.13           C  
ATOM   3679  N   LYS A 495      51.577  14.283  -5.171  1.00  6.70           N  
ATOM   3680  CA  LYS A 495      50.609  13.240  -4.836  1.00  6.02           C  
ATOM   3681  C   LYS A 495      49.190  13.815  -4.724  1.00  5.28           C  
ATOM   3682  O   LYS A 495      48.215  13.197  -5.189  1.00  5.31           O  
ATOM   3683  CB  LYS A 495      51.008  12.564  -3.521  1.00  6.75           C  
ATOM   3684  CG  LYS A 495      52.276  11.754  -3.639  1.00  7.91           C  
ATOM   3685  CD  LYS A 495      52.719  11.196  -2.287  1.00 10.47           C  
ATOM   3686  CE  LYS A 495      51.816  10.058  -1.774  1.00 11.28           C  
ATOM   3687  NZ  LYS A 495      51.840   8.849  -2.662  1.00 11.06           N  
ATOM   3688  N   PHE A 496      49.068  14.997  -4.119  1.00  4.33           N  
ATOM   3689  CA  PHE A 496      47.761  15.669  -3.948  1.00  6.13           C  
ATOM   3690  C   PHE A 496      47.173  15.930  -5.338  1.00  5.72           C  
ATOM   3691  O   PHE A 496      45.992  15.677  -5.612  1.00  4.16           O  
ATOM   3692  CB  PHE A 496      47.978  17.004  -3.199  1.00  6.72           C  
ATOM   3693  CG  PHE A 496      46.712  17.670  -2.702  1.00  7.20           C  
ATOM   3694  CD1 PHE A 496      45.621  16.922  -2.265  1.00  7.63           C  
ATOM   3695  CD2 PHE A 496      46.660  19.056  -2.600  1.00  6.69           C  
ATOM   3696  CE1 PHE A 496      44.503  17.546  -1.728  1.00  7.88           C  
ATOM   3697  CE2 PHE A 496      45.553  19.701  -2.067  1.00  8.10           C  
ATOM   3698  CZ  PHE A 496      44.459  18.943  -1.620  1.00  7.17           C  
ATOM   3699  N   LYS A 497      48.016  16.424  -6.237  1.00  6.59           N  
ATOM   3700  CA  LYS A 497      47.559  16.703  -7.598  1.00  7.73           C  
ATOM   3701  C   LYS A 497      47.001  15.449  -8.265  1.00  7.01           C  
ATOM   3702  O   LYS A 497      45.986  15.514  -8.970  1.00  8.55           O  
ATOM   3703  CB  LYS A 497      48.731  17.268  -8.416  1.00  9.07           C  
ATOM   3704  CG  LYS A 497      48.363  17.953  -9.715  1.00 15.66           C  
ATOM   3705  CD  LYS A 497      49.633  18.561 -10.334  1.00 16.76           C  
ATOM   3706  CE  LYS A 497      49.343  19.391 -11.574  1.00 21.51           C  
ATOM   3707  NZ  LYS A 497      50.629  19.938 -12.120  1.00 22.09           N  
ATOM   3708  N   ALA A 498      47.654  14.305  -8.055  1.00  6.41           N  
ATOM   3709  CA  ALA A 498      47.196  13.055  -8.661  1.00  6.10           C  
ATOM   3710  C   ALA A 498      45.846  12.587  -8.088  1.00  6.66           C  
ATOM   3711  O   ALA A 498      44.983  12.110  -8.824  1.00  6.12           O  
ATOM   3712  CB  ALA A 498      48.255  11.960  -8.481  1.00  8.68           C  
ATOM   3713  N   VAL A 499      45.662  12.740  -6.776  1.00  5.33           N  
ATOM   3714  CA  VAL A 499      44.405  12.347  -6.133  1.00  5.84           C  
ATOM   3715  C   VAL A 499      43.255  13.199  -6.688  1.00  6.36           C  
ATOM   3716  O   VAL A 499      42.166  12.698  -6.997  1.00  6.22           O  
ATOM   3717  CB  VAL A 499      44.474  12.588  -4.597  1.00  5.22           C  
ATOM   3718  CG1 VAL A 499      43.101  12.463  -3.993  1.00  5.10           C  
ATOM   3719  CG2 VAL A 499      45.428  11.594  -3.943  1.00  5.90           C  
ATOM   3720  N   ILE A 500      43.493  14.500  -6.782  1.00  5.59           N  
ATOM   3721  CA  ILE A 500      42.474  15.411  -7.270  1.00  6.56           C  
ATOM   3722  C   ILE A 500      42.095  15.098  -8.721  1.00  6.60           C  
ATOM   3723  O   ILE A 500      40.910  15.063  -9.075  1.00  8.11           O  
ATOM   3724  CB  ILE A 500      42.958  16.872  -7.152  1.00  7.14           C  
ATOM   3725  CG1 ILE A 500      43.091  17.259  -5.672  1.00  9.29           C  
ATOM   3726  CG2 ILE A 500      41.995  17.798  -7.866  1.00  9.17           C  
ATOM   3727  CD1 ILE A 500      43.806  18.592  -5.452  1.00 10.84           C  
ATOM   3728  N   LYS A 501      43.107  14.868  -9.554  1.00  6.65           N  
ATOM   3729  CA  LYS A 501      42.867  14.576 -10.966  1.00  8.60           C  
ATOM   3730  C   LYS A 501      42.051  13.294 -11.185  1.00  9.39           C  
ATOM   3731  O   LYS A 501      41.168  13.248 -12.055  1.00  7.07           O  
ATOM   3732  CB  LYS A 501      44.198  14.478 -11.713  1.00  9.96           C  
ATOM   3733  CG  LYS A 501      44.056  14.270 -13.232  1.00 12.61           C  
ATOM   3734  CD  LYS A 501      45.422  14.298 -13.929  1.00 14.12           C  
ATOM   3735  CE  LYS A 501      45.305  13.990 -15.432  1.00 16.66           C  
ATOM   3736  NZ  LYS A 501      46.614  14.142 -16.170  1.00 17.99           N  
ATOM   3737  N   ARG A 502      42.303  12.261 -10.393  1.00  9.94           N  
ATOM   3738  CA  ARG A 502      41.549  11.032 -10.630  1.00 11.68           C  
ATOM   3739  C   ARG A 502      40.121  11.064 -10.080  1.00 12.45           C  
ATOM   3740  O   ARG A 502      39.303  10.198 -10.386  1.00 12.33           O  
ATOM   3741  CB  ARG A 502      42.328   9.803 -10.118  1.00 13.99           C  
ATOM   3742  CG  ARG A 502      42.437   9.641  -8.629  1.00 14.31           C  
ATOM   3743  CD  ARG A 502      43.079   8.289  -8.281  1.00 15.01           C  
ATOM   3744  NE  ARG A 502      44.469   8.202  -8.729  1.00 14.63           N  
ATOM   3745  CZ  ARG A 502      45.528   8.482  -7.966  1.00 15.00           C  
ATOM   3746  NH1 ARG A 502      45.373   8.865  -6.704  1.00 12.55           N  
ATOM   3747  NH2 ARG A 502      46.747   8.385  -8.469  1.00 16.01           N  
ATOM   3748  N   ASN A 503      39.803  12.094  -9.311  1.00 13.24           N  
ATOM   3749  CA  ASN A 503      38.475  12.201  -8.734  1.00 17.50           C  
ATOM   3750  C   ASN A 503      37.538  13.043  -9.590  1.00 18.74           C  
ATOM   3751  O   ASN A 503      36.345  13.135  -9.297  1.00 18.91           O  
ATOM   3752  CB  ASN A 503      38.578  12.790  -7.325  1.00 17.39           C  
ATOM   3753  CG  ASN A 503      37.270  12.728  -6.569  1.00 21.94           C  
ATOM   3754  OD1 ASN A 503      36.559  13.727  -6.454  1.00 23.54           O  
ATOM   3755  ND2 ASN A 503      36.939  11.547  -6.053  1.00 22.39           N  
ATOM   3756  N   LYS A 504      38.072  13.657 -10.643  1.00 19.66           N  
ATOM   3757  CA  LYS A 504      37.248  14.491 -11.513  1.00 22.09           C  
ATOM   3758  C   LYS A 504      37.041  13.908 -12.909  1.00 22.27           C  
ATOM   3759  O   LYS A 504      37.592  12.869 -13.259  1.00 20.40           O  
ATOM   3760  CB  LYS A 504      37.838  15.896 -11.633  1.00 24.63           C  
ATOM   3761  CG  LYS A 504      39.059  15.996 -12.532  1.00 28.20           C  
ATOM   3762  CD  LYS A 504      39.397  17.462 -12.838  1.00 32.38           C  
ATOM   3763  CE  LYS A 504      39.603  18.266 -11.558  1.00 35.04           C  
ATOM   3764  NZ  LYS A 504      39.852  19.718 -11.821  1.00 37.22           N  
ATOM   3765  N   GLU A 505      36.244  14.601 -13.708  1.00 24.38           N  
ATOM   3766  CA  GLU A 505      35.926  14.146 -15.046  1.00 27.09           C  
ATOM   3767  C   GLU A 505      37.137  13.734 -15.849  1.00 28.17           C  
ATOM   3768  O   GLU A 505      38.206  14.335 -15.750  1.00 26.98           O  
ATOM   3769  CB  GLU A 505      35.179  15.234 -15.800  1.00 29.52           C  
ATOM   3770  CG  GLU A 505      34.090  14.688 -16.673  1.00 34.01           C  
ATOM   3771  CD  GLU A 505      33.131  15.762 -17.107  1.00 35.81           C  
ATOM   3772  OE1 GLU A 505      33.513  16.550 -17.996  1.00 37.34           O  
ATOM   3773  OE2 GLU A 505      32.010  15.823 -16.543  1.00 36.56           O  
ATOM   3774  N   HIS A 506      36.964  12.695 -16.647  1.00 30.17           N  
ATOM   3775  CA  HIS A 506      38.045  12.238 -17.482  1.00 33.08           C  
ATOM   3776  C   HIS A 506      38.237  13.294 -18.564  1.00 33.03           C  
ATOM   3777  O   HIS A 506      39.404  13.598 -18.876  1.00 33.98           O  
ATOM   3778  CB  HIS A 506      37.706  10.891 -18.111  1.00 35.63           C  
ATOM   3779  CG  HIS A 506      38.860  10.263 -18.823  1.00 38.80           C  
ATOM   3780  ND1 HIS A 506      40.030   9.915 -18.179  1.00 40.24           N  
ATOM   3781  CD2 HIS A 506      39.040   9.951 -20.127  1.00 39.69           C  
ATOM   3782  CE1 HIS A 506      40.881   9.417 -19.058  1.00 40.33           C  
ATOM   3783  NE2 HIS A 506      40.305   9.428 -20.247  1.00 40.86           N  
ATOM   3784  OXT HIS A 506      37.219  13.802 -19.081  1.00 34.76           O  
TER    3785      HIS A 506                                                      
HETATM 3786  C1  MAN B   1      40.534  21.416  26.985  1.00  5.18           C  
HETATM 3787  C2  MAN B   1      39.621  22.230  27.883  1.00  4.57           C  
HETATM 3788  C3  MAN B   1      40.077  23.696  27.873  1.00  4.88           C  
HETATM 3789  C4  MAN B   1      41.581  23.836  28.248  1.00  5.63           C  
HETATM 3790  C5  MAN B   1      42.435  22.851  27.463  1.00  4.53           C  
HETATM 3791  C6  MAN B   1      43.834  22.748  28.057  1.00  7.41           C  
HETATM 3792  O2  MAN B   1      39.655  21.705  29.228  1.00  6.26           O  
HETATM 3793  O3  MAN B   1      39.277  24.415  28.787  1.00  4.33           O  
HETATM 3794  O4  MAN B   1      42.071  25.152  27.897  1.00  5.29           O  
HETATM 3795  O5  MAN B   1      41.874  21.519  27.462  1.00  5.13           O  
HETATM 3796  O6  MAN B   1      44.655  21.945  27.239  1.00  7.18           O  
HETATM 3797  C1  GCU B   2      39.247  20.371  29.373  1.00  5.33           C  
HETATM 3798  C2  GCU B   2      38.653  20.180  30.780  1.00  6.28           C  
HETATM 3799  C3  GCU B   2      39.705  20.402  31.856  1.00  7.02           C  
HETATM 3800  C4  GCU B   2      40.890  19.459  31.615  1.00  7.54           C  
HETATM 3801  C5  GCU B   2      41.441  19.760  30.214  1.00  7.94           C  
HETATM 3802  C6  GCU B   2      42.639  18.914  29.806  1.00 10.82           C  
HETATM 3803  O2  GCU B   2      37.604  21.100  30.986  1.00  5.93           O  
HETATM 3804  O3  GCU B   2      39.122  20.172  33.137  1.00  6.71           O  
HETATM 3805  O4  GCU B   2      41.920  19.721  32.596  1.00  9.83           O  
HETATM 3806  O5  GCU B   2      40.398  19.541  29.220  1.00  7.56           O  
HETATM 3807  O6A GCU B   2      42.491  17.676  29.707  1.00  9.88           O  
HETATM 3808  O6B GCU B   2      43.751  19.514  29.787  1.00 13.82           O  
HETATM 3809  C1  XYP B   3      42.323  18.664  33.389  1.00 12.30           C  
HETATM 3810  C2  XYP B   3      43.632  19.040  34.106  1.00 16.90           C  
HETATM 3811  C3  XYP B   3      44.033  17.949  35.099  1.00 18.54           C  
HETATM 3812  C4  XYP B   3      42.869  17.679  36.040  1.00 18.81           C  
HETATM 3813  C5  XYP B   3      41.609  17.335  35.234  1.00 18.98           C  
HETATM 3814  O2  XYP B   3      44.673  19.208  33.155  1.00 17.60           O  
HETATM 3815  O3  XYP B   3      45.171  18.391  35.839  1.00 19.59           O  
HETATM 3816  O4  XYP B   3      43.191  16.595  36.926  1.00 20.42           O  
HETATM 3817  O5  XYP B   3      41.290  18.429  34.347  1.00 16.65           O  
HETATM 3818  C1  MXZ B   4      43.003  16.918  38.278  1.00 23.63           C  
HETATM 3819  C2  MXZ B   4      42.725  15.647  39.079  1.00 25.31           C  
HETATM 3820  C3  MXZ B   4      43.921  14.701  38.971  1.00 26.05           C  
HETATM 3821  C4  MXZ B   4      45.179  15.415  39.460  1.00 24.21           C  
HETATM 3822  C5  MXZ B   4      45.374  16.721  38.655  1.00 24.39           C  
HETATM 3823  O2  MXZ B   4      41.528  15.007  38.600  1.00 28.72           O  
HETATM 3824  O3  MXZ B   4      43.672  13.543  39.788  1.00 29.10           O  
HETATM 3825  O4  MXZ B   4      45.010  15.722  40.854  1.00 24.97           O  
HETATM 3826  O5  MXZ B   4      44.192  17.541  38.753  1.00 22.59           O  
HETATM 3827  CM  MXZ B   4      40.399  15.813  38.969  1.00 28.93           C  
HETATM 3828  C6  MXZ B   4      46.543  17.582  39.117  1.00 23.79           C  
HETATM 3829  C1  GLA B   5      43.492  12.348  39.080  1.00 31.68           C  
HETATM 3830  C2  GLA B   5      42.823  11.308  39.985  1.00 33.65           C  
HETATM 3831  C3  GLA B   5      43.750  10.874  41.133  1.00 35.21           C  
HETATM 3832  C4  GLA B   5      45.167  10.531  40.641  1.00 35.95           C  
HETATM 3833  C5  GLA B   5      45.713  11.625  39.715  1.00 35.44           C  
HETATM 3834  C6  GLA B   5      47.028  11.228  39.068  1.00 35.72           C  
HETATM 3835  O2  GLA B   5      41.629  11.857  40.532  1.00 32.27           O  
HETATM 3836  O3  GLA B   5      43.192   9.736  41.776  1.00 36.34           O  
HETATM 3837  O4  GLA B   5      45.167   9.286  39.956  1.00 37.78           O  
HETATM 3838  O5  GLA B   5      44.772  11.888  38.644  1.00 34.03           O  
HETATM 3839  O6  GLA B   5      47.626  12.328  38.395  1.00 35.33           O  
HETATM 3840  C2  BGC B   6      45.839  16.406  42.968  1.00 27.35           C  
HETATM 3841  C3  BGC B   6      47.053  16.310  43.902  1.00 27.46           C  
HETATM 3842  C4  BGC B   6      47.530  14.855  44.027  1.00 26.95           C  
HETATM 3843  C5  BGC B   6      47.734  14.250  42.641  1.00 26.74           C  
HETATM 3844  C6  BGC B   6      48.136  12.789  42.686  1.00 26.39           C  
HETATM 3845  C1  BGC B   6      46.138  15.701  41.647  1.00 25.89           C  
HETATM 3846  O2  BGC B   6      45.521  17.771  42.713  1.00 28.01           O  
HETATM 3847  O3  BGC B   6      46.696  16.794  45.189  1.00 27.91           O  
HETATM 3848  O4  BGC B   6      48.747  14.804  44.758  1.00 26.78           O  
HETATM 3849  O5  BGC B   6      46.502  14.340  41.889  1.00 26.28           O  
HETATM 3850  O6  BGC B   6      47.035  11.979  43.064  1.00 26.64           O  
HETATM 3851  C1  RAM B   7      41.765  26.206  28.773  1.00  4.45           C  
HETATM 3852  C2  RAM B   7      42.825  27.279  28.630  1.00  5.82           C  
HETATM 3853  C3  RAM B   7      42.859  27.820  27.190  1.00  5.31           C  
HETATM 3854  C4  RAM B   7      41.461  28.270  26.731  1.00  5.53           C  
HETATM 3855  C5  RAM B   7      40.390  27.196  27.035  1.00  6.60           C  
HETATM 3856  C6  RAM B   7      38.979  27.713  26.822  1.00  5.69           C  
HETATM 3857  O2  RAM B   7      42.540  28.331  29.537  1.00  7.47           O  
HETATM 3858  O3  RAM B   7      43.748  28.923  27.131  1.00  6.78           O  
HETATM 3859  O4  RAM B   7      41.489  28.489  25.327  1.00  4.83           O  
HETATM 3860  O5  RAM B   7      40.484  26.743  28.411  1.00  4.32           O  
HETATM 3861  C1  ASG C   1      25.795  20.903   1.482  1.00 14.86           C  
HETATM 3862  C2  ASG C   1      25.303  21.735   0.281  1.00 13.98           C  
HETATM 3863  C3  ASG C   1      26.442  22.592  -0.258  1.00 12.99           C  
HETATM 3864  C4  ASG C   1      27.008  23.439   0.861  1.00 11.85           C  
HETATM 3865  C5  ASG C   1      27.505  22.532   1.988  1.00 13.47           C  
HETATM 3866  C6  ASG C   1      28.038  23.326   3.187  1.00 13.09           C  
HETATM 3867  C7  ASG C   1      23.690  21.084  -1.408  1.00 15.19           C  
HETATM 3868  C8  ASG C   1      23.315  20.138  -2.542  1.00 15.84           C  
HETATM 3869  O1  ASG C   1      24.712  20.263   2.060  1.00 17.46           O  
HETATM 3870  N2  ASG C   1      24.835  20.844  -0.769  1.00 14.25           N  
HETATM 3871  O3  ASG C   1      25.969  23.433  -1.327  1.00 11.02           O  
HETATM 3872  O4  ASG C   1      26.017  24.304   1.443  1.00  9.79           O  
HETATM 3873  O5  ASG C   1      26.401  21.741   2.486  1.00 14.21           O  
HETATM 3874  O6  ASG C   1      29.290  23.944   2.903  1.00 13.76           O  
HETATM 3875  O7  ASG C   1      22.931  22.008  -1.118  1.00 14.15           O  
HETATM 3876  OSA ASG C   1      25.734  26.515   2.445  1.00  8.62           O  
HETATM 3877  OSB ASG C   1      27.387  26.211   0.715  1.00  7.32           O  
HETATM 3878  OSC ASG C   1      25.114  26.261   0.049  1.00  9.34           O  
HETATM 3879  S   ASG C   1      26.020  25.870   1.147  1.00  8.68           S  
HETATM 3880  C1  BDP C   2      26.822  23.598  -2.402  1.00 13.28           C  
HETATM 3881  C2  BDP C   2      26.003  23.979  -3.643  1.00 13.63           C  
HETATM 3882  C3  BDP C   2      26.930  24.303  -4.806  1.00 15.57           C  
HETATM 3883  C4  BDP C   2      27.949  25.344  -4.384  1.00 16.32           C  
HETATM 3884  C5  BDP C   2      28.705  24.882  -3.144  1.00 16.05           C  
HETATM 3885  C6  BDP C   2      29.697  25.915  -2.641  1.00 17.64           C  
HETATM 3886  O2  BDP C   2      25.161  22.892  -3.999  1.00 13.80           O  
HETATM 3887  O3  BDP C   2      26.174  24.823  -5.892  1.00 15.53           O  
HETATM 3888  O4  BDP C   2      28.861  25.542  -5.466  1.00 19.75           O  
HETATM 3889  O5  BDP C   2      27.769  24.637  -2.078  1.00 13.59           O  
HETATM 3890  O6A BDP C   2      30.902  25.582  -2.639  1.00 18.61           O  
HETATM 3891  O6B BDP C   2      29.258  27.030  -2.291  1.00 15.79           O  
HETATM 3892  C1  ASG C   3      29.103  26.854  -5.822  1.00 24.59           C  
HETATM 3893  C2  ASG C   3      30.269  26.891  -6.804  1.00 26.39           C  
HETATM 3894  C3  ASG C   3      30.455  28.307  -7.330  1.00 28.38           C  
HETATM 3895  C4  ASG C   3      29.137  28.807  -7.951  1.00 28.79           C  
HETATM 3896  C5  ASG C   3      28.068  28.753  -6.855  1.00 29.42           C  
HETATM 3897  C6  ASG C   3      26.704  29.253  -7.291  1.00 31.22           C  
HETATM 3898  C7  ASG C   3      32.125  25.374  -6.570  1.00 31.63           C  
HETATM 3899  C8  ASG C   3      33.301  24.889  -5.729  1.00 32.51           C  
HETATM 3900  N2  ASG C   3      31.476  26.449  -6.133  1.00 28.80           N  
HETATM 3901  O3  ASG C   3      31.538  28.340  -8.281  1.00 30.96           O  
HETATM 3902  O4  ASG C   3      28.744  27.962  -9.055  1.00 34.14           O  
HETATM 3903  O5  ASG C   3      27.907  27.388  -6.421  1.00 26.39           O  
HETATM 3904  O6  ASG C   3      25.825  29.389  -6.182  1.00 32.87           O  
HETATM 3905  O7  ASG C   3      31.819  24.776  -7.605  1.00 32.93           O  
HETATM 3906  OSA ASG C   3      27.507  29.527 -10.520  1.00 38.61           O  
HETATM 3907  OSB ASG C   3      29.898  29.410 -10.792  1.00 38.16           O  
HETATM 3908  OSC ASG C   3      28.480  27.583 -11.536  1.00 38.58           O  
HETATM 3909  S   ASG C   3      28.674  28.631 -10.515  1.00 37.27           S  
HETATM 3910  C1  GCD C   4      32.466  29.337  -8.048  1.00 34.58           C  
HETATM 3911  C2  GCD C   4      33.771  29.011  -8.701  1.00 38.10           C  
HETATM 3912  C3  GCD C   4      34.682  30.268  -8.428  1.00 40.08           C  
HETATM 3913  C4  GCD C   4      34.052  31.710  -8.471  1.00 38.89           C  
HETATM 3914  C5  GCD C   4      32.712  31.796  -8.672  1.00 38.77           C  
HETATM 3915  C6  GCD C   4      31.864  33.040  -8.755  1.00 39.19           C  
HETATM 3916  O2  GCD C   4      34.378  27.851  -8.059  1.00 42.99           O  
HETATM 3917  O3  GCD C   4      35.882  29.977  -9.159  1.00 38.28           O  
HETATM 3918  O5  GCD C   4      31.950  30.538  -8.810  1.00 35.72           O  
HETATM 3919  O6A GCD C   4      31.498  33.292  -9.968  1.00 38.82           O  
HETATM 3920  O6B GCD C   4      31.561  33.626  -7.642  1.00 39.46           O  
HETATM 3921  O   HOH A 701      23.886   9.641  11.128  1.00 17.90           O  
HETATM 3922  O   HOH A 702      10.051  27.755   6.849  1.00 12.59           O  
HETATM 3923  O   HOH A 703      60.498  19.331  12.336  1.00 24.95           O  
HETATM 3924  O   HOH A 704      26.368  51.342  19.529  1.00 17.37           O  
HETATM 3925  O   HOH A 705      48.525  17.960  46.338  1.00 24.45           O  
HETATM 3926  O   HOH A 706      50.602  17.377  25.235  1.00 34.49           O  
HETATM 3927  O   HOH A 707      31.172  19.296   3.192  1.00 16.78           O  
HETATM 3928  O   HOH A 708      29.239  39.734  34.375  1.00 35.13           O  
HETATM 3929  O   HOH A 709      16.139  25.999  31.775  1.00 31.40           O  
HETATM 3930  O   HOH A 710      19.465  12.532   0.242  1.00 44.37           O  
HETATM 3931  O   HOH A 711      49.063 -14.321  10.636  1.00 37.63           O  
HETATM 3932  O   HOH A 712      40.478  49.689   4.786  1.00 26.45           O  
HETATM 3933  O   HOH A 713      30.747  -2.100  21.475  1.00 15.20           O  
HETATM 3934  O   HOH A 714      14.701  19.079   0.974  1.00 26.34           O  
HETATM 3935  O   HOH A 715      21.869  19.661   1.080  1.00 32.61           O  
HETATM 3936  O   HOH A 716      21.778  45.646   3.731  1.00 21.41           O  
HETATM 3937  O   HOH A 717      44.293  16.485  45.847  1.00 31.62           O  
HETATM 3938  O   HOH A 718      58.144   9.783   4.294  1.00 34.37           O  
HETATM 3939  O   HOH A 719      24.617  26.723  -5.312  1.00 21.34           O  
HETATM 3940  O   HOH A 720      40.309  20.471 -14.187  1.00 37.13           O  
HETATM 3941  O   HOH A 721      12.056  36.350  -3.843  1.00 18.67           O  
HETATM 3942  O   HOH A 722       8.696   9.817  10.628  1.00 14.16           O  
HETATM 3943  O   HOH A 723      28.534  42.740   1.608  1.00 16.24           O  
HETATM 3944  O   HOH A 724      44.866  43.172   9.179  1.00 35.62           O  
HETATM 3945  O   HOH A 725      34.884  15.185  -8.964  1.00 27.02           O  
HETATM 3946  O   HOH A 726      23.313  17.138   3.871  1.00 16.70           O  
HETATM 3947  O   HOH A 727      17.381  19.439  31.329  1.00 35.07           O  
HETATM 3948  O   HOH A 728      23.208  23.358  -5.567  1.00 32.54           O  
HETATM 3949  O   HOH A 729      13.990  14.906  15.165  1.00 40.56           O  
HETATM 3950  O   HOH A 730      45.587  -4.197  -1.446  1.00 26.98           O  
HETATM 3951  O   HOH A 731      29.969  24.758  37.986  1.00 34.43           O  
HETATM 3952  O   HOH A 732      51.040  14.981  -9.687  1.00 12.34           O  
HETATM 3953  O   HOH A 733      57.187  21.739  11.992  1.00 29.97           O  
HETATM 3954  O   HOH A 734      36.416  16.221  -7.017  1.00 26.32           O  
HETATM 3955  O   HOH A 735       8.079  33.329   3.663  1.00 13.33           O  
HETATM 3956  O   HOH A 736      49.408  -8.674   7.087  1.00 27.15           O  
HETATM 3957  O   HOH A 737      52.927   9.930   2.036  1.00 19.42           O  
HETATM 3958  O   HOH A 738      31.979  15.342   1.687  1.00 21.83           O  
HETATM 3959  O   HOH A 739      40.923  10.233  42.878  1.00 41.58           O  
HETATM 3960  O   HOH A 740      36.038  28.934  32.922  1.00 21.85           O  
HETATM 3961  O   HOH A 741      20.191  39.713  -5.081  1.00 32.84           O  
HETATM 3962  O   HOH A 742      23.970  36.406  -1.234  1.00 37.52           O  
HETATM 3963  O   HOH A 743      19.578  47.343  22.431  1.00 25.39           O  
HETATM 3964  O   HOH A 744      38.042  -7.494  10.016  1.00 21.47           O  
HETATM 3965  O   HOH A 745      47.442  17.976  26.876  1.00 22.58           O  
HETATM 3966  O   HOH A 746      46.210  19.896  44.015  1.00 35.95           O  
HETATM 3967  O   HOH A 747      39.015 -10.612  14.224  1.00 33.75           O  
HETATM 3968  O   HOH A 748      29.250  -1.194  17.197  1.00 17.60           O  
HETATM 3969  O   HOH A 749      33.120  25.410  -1.315  1.00 54.03           O  
HETATM 3970  O   HOH A 750      60.341   9.712  15.446  1.00 13.34           O  
HETATM 3971  O   HOH A 751      47.209  21.691  27.592  1.00 18.71           O  
HETATM 3972  O   HOH A 752      20.161  18.043  30.416  1.00 15.81           O  
HETATM 3973  O   HOH A 753      37.368  -1.330   8.501  1.00 22.17           O  
HETATM 3974  O   HOH A 754      40.646  15.951  30.299  1.00 12.36           O  
HETATM 3975  O   HOH A 755      41.800  30.249  -1.050  1.00 16.97           O  
HETATM 3976  O   HOH A 756      61.834   1.763  11.027  1.00 20.68           O  
HETATM 3977  O   HOH A 757      42.702  43.720  17.891  1.00 18.84           O  
HETATM 3978  O   HOH A 758      30.159  -2.686  27.759  1.00 40.08           O  
HETATM 3979  O   HOH A 759      38.148  46.113  23.577  1.00 29.25           O  
HETATM 3980  O   HOH A 760      49.047 -11.709  26.227  1.00 26.79           O  
HETATM 3981  O   HOH A 761      15.951  11.943  17.174  1.00 19.97           O  
HETATM 3982  O   HOH A 762      14.040  44.277  19.253  1.00 20.18           O  
HETATM 3983  O   HOH A 763      59.165  -3.929   8.409  1.00 56.38           O  
HETATM 3984  O   HOH A 764      50.996  29.354   9.405  1.00 14.62           O  
HETATM 3985  O   HOH A 765      13.476  39.030   8.563  1.00 14.86           O  
HETATM 3986  O   HOH A 766      29.177  10.686  28.858  1.00 29.34           O  
HETATM 3987  O   HOH A 767      41.251  41.507  22.238  1.00 22.12           O  
HETATM 3988  O   HOH A 768      45.330  20.978  36.281  1.00 41.41           O  
HETATM 3989  O   HOH A 769      10.682  23.396   5.880  1.00 15.26           O  
HETATM 3990  O   HOH A 770      34.510  34.289   7.238  1.00  6.22           O  
HETATM 3991  O   HOH A 771      60.303   9.279  20.393  1.00 33.23           O  
HETATM 3992  O   HOH A 772      44.012  -1.268   0.456  1.00  6.55           O  
HETATM 3993  O   HOH A 773      43.623  41.861  14.493  1.00 25.09           O  
HETATM 3994  O   HOH A 774      55.425  18.883  -6.938  1.00 13.25           O  
HETATM 3995  O   HOH A 775      42.941  18.314   3.175  1.00  3.73           O  
HETATM 3996  O   HOH A 776      42.718  47.593  20.188  1.00 23.89           O  
HETATM 3997  O   HOH A 777      31.715  23.165  -3.327  1.00 31.47           O  
HETATM 3998  O   HOH A 778      40.311  29.256  30.613  1.00  5.14           O  
HETATM 3999  O   HOH A 779      50.017 -13.823  24.712  1.00 25.55           O  
HETATM 4000  O   HOH A 780      14.180  21.822  17.728  1.00 22.24           O  
HETATM 4001  O   HOH A 781      55.598   1.504  26.706  1.00 21.76           O  
HETATM 4002  O   HOH A 782      49.698   3.681  28.353  1.00 21.58           O  
HETATM 4003  O   HOH A 783      50.459  14.767  11.983  1.00  3.48           O  
HETATM 4004  O   HOH A 784      57.520  21.632  21.057  1.00 27.59           O  
HETATM 4005  O   HOH A 785      42.556   8.959   3.412  1.00  3.81           O  
HETATM 4006  O   HOH A 786      38.043  46.002   4.826  1.00 11.33           O  
HETATM 4007  O   HOH A 787      17.930  32.710  -8.674  1.00 19.56           O  
HETATM 4008  O   HOH A 788      52.922  -7.203   2.448  1.00 22.58           O  
HETATM 4009  O   HOH A 789      40.279  21.617  35.040  1.00 18.35           O  
HETATM 4010  O   HOH A 790      26.629  44.133  29.331  1.00 43.46           O  
HETATM 4011  O   HOH A 791      44.637  -1.768   3.938  1.00  7.40           O  
HETATM 4012  O   HOH A 792      31.004  13.325  27.567  1.00 28.22           O  
HETATM 4013  O   HOH A 793      15.211  45.105   2.391  1.00 10.28           O  
HETATM 4014  O   HOH A 794      64.465   3.108  21.429  1.00 20.50           O  
HETATM 4015  O   HOH A 795      59.808   3.541   7.975  1.00 31.91           O  
HETATM 4016  O   HOH A 796      50.749   7.076  28.402  1.00 20.41           O  
HETATM 4017  O   HOH A 797      52.180  21.007   9.465  1.00 13.56           O  
HETATM 4018  O   HOH A 798      28.825  32.163  -2.904  1.00 26.24           O  
HETATM 4019  O   HOH A 799      41.145  27.284  22.650  1.00  5.51           O  
HETATM 4020  O   HOH A 800      16.279  26.173   3.385  1.00 10.41           O  
HETATM 4021  O   HOH A 801      55.538   5.630  17.145  1.00  4.95           O  
HETATM 4022  O   HOH A 802       9.806  29.405  -1.355  1.00 48.39           O  
HETATM 4023  O   HOH A 803      57.619 -12.711  12.640  1.00 33.92           O  
HETATM 4024  O   HOH A 804      32.219   4.044   8.610  1.00  9.75           O  
HETATM 4025  O   HOH A 805      45.587  25.304   0.175  1.00 15.96           O  
HETATM 4026  O   HOH A 806      35.366  30.000  -0.764  1.00 26.94           O  
HETATM 4027  O   HOH A 807      18.672  20.073   8.723  1.00 31.39           O  
HETATM 4028  O   HOH A 808      51.271  33.211  23.461  1.00 37.00           O  
HETATM 4029  O   HOH A 809      44.636  12.704  44.001  1.00 21.11           O  
HETATM 4030  O   HOH A 810      20.028  26.723  -4.666  1.00 24.11           O  
HETATM 4031  O   HOH A 811      34.871  16.840 -13.188  1.00 31.91           O  
HETATM 4032  O   HOH A 812      37.278  51.453  13.447  1.00 27.90           O  
HETATM 4033  O   HOH A 813      34.943  10.935 -16.651  1.00 13.49           O  
HETATM 4034  O   HOH A 814      45.217  23.302  -2.199  1.00 23.09           O  
HETATM 4035  O   HOH A 815      16.955  21.983  12.112  1.00  8.83           O  
HETATM 4036  O   HOH A 816      36.182   7.148   5.536  1.00  6.25           O  
HETATM 4037  O   HOH A 817      21.872   1.331  13.308  1.00 22.24           O  
HETATM 4038  O   HOH A 818      40.784  13.630 -14.682  1.00 19.23           O  
HETATM 4039  O   HOH A 819      48.523  25.966  -0.954  1.00 17.87           O  
HETATM 4040  O   HOH A 820      44.171  47.574  16.564  1.00 22.33           O  
HETATM 4041  O   HOH A 821      47.709  28.939  18.078  1.00 20.31           O  
HETATM 4042  O   HOH A 822      32.331  -4.481  17.097  1.00 12.75           O  
HETATM 4043  O   HOH A 823      31.798  31.986  -5.528  1.00 39.18           O  
HETATM 4044  O   HOH A 824       9.040  31.293  14.255  1.00 36.80           O  
HETATM 4045  O   HOH A 825      63.175  -3.261  17.429  1.00 18.20           O  
HETATM 4046  O   HOH A 826      39.404  31.050   2.278  1.00 10.98           O  
HETATM 4047  O   HOH A 827      19.233  41.878  12.519  1.00 11.07           O  
HETATM 4048  O   HOH A 828      58.719   1.078  20.171  1.00  7.24           O  
HETATM 4049  O   HOH A 829      29.890   7.089   6.833  1.00  5.65           O  
HETATM 4050  O   HOH A 830      20.901  24.061  26.488  1.00 14.93           O  
HETATM 4051  O   HOH A 831      24.153  11.307  31.798  1.00 23.14           O  
HETATM 4052  O   HOH A 832      48.165  10.550  25.633  1.00 14.90           O  
HETATM 4053  O   HOH A 833      50.973   9.462  -7.219  1.00 23.79           O  
HETATM 4054  O   HOH A 834      32.011  55.182  22.856  1.00 40.54           O  
HETATM 4055  O   HOH A 835      28.016  51.973  15.893  1.00 21.35           O  
HETATM 4056  O   HOH A 836      38.478  23.637  31.258  1.00  8.28           O  
HETATM 4057  O   HOH A 837      33.600  25.450  17.724  1.00  5.83           O  
HETATM 4058  O   HOH A 838      14.628  24.040  13.915  1.00  8.74           O  
HETATM 4059  O   HOH A 839      36.708  22.968  -0.859  1.00 13.16           O  
HETATM 4060  O   HOH A 840      32.479  28.744 -11.227  1.00 39.63           O  
HETATM 4061  O   HOH A 841      33.588  30.233  29.129  1.00  8.61           O  
HETATM 4062  O   HOH A 842      23.249  37.924   0.959  1.00 22.79           O  
HETATM 4063  O   HOH A 843      35.757  28.824  30.310  1.00 10.52           O  
HETATM 4064  O   HOH A 844      26.961  46.416   4.130  1.00 21.70           O  
HETATM 4065  O   HOH A 845      21.596   3.995  13.498  1.00 15.90           O  
HETATM 4066  O   HOH A 846      13.002  25.409  17.610  1.00 18.67           O  
HETATM 4067  O   HOH A 847      30.547  25.030  -0.014  1.00 45.66           O  
HETATM 4068  O   HOH A 848      17.701  38.246   8.099  1.00  6.66           O  
HETATM 4069  O   HOH A 849      38.850  37.559  28.637  1.00 52.47           O  
HETATM 4070  O   HOH A 850      58.506   3.766   5.706  1.00 10.69           O  
HETATM 4071  O   HOH A 851      60.011  11.216  22.659  1.00 27.43           O  
HETATM 4072  O   HOH A 852      42.599 -10.505  15.424  1.00 23.32           O  
HETATM 4073  O   HOH A 853      35.092  -8.832  22.209  1.00 15.95           O  
HETATM 4074  O   HOH A 854      37.159  -9.921  27.345  1.00 28.35           O  
HETATM 4075  O   HOH A 855      27.304  19.734   4.602  1.00 15.07           O  
HETATM 4076  O   HOH A 856      44.432  38.986  13.851  1.00 24.07           O  
HETATM 4077  O   HOH A 857      48.219  31.389  21.846  1.00 24.01           O  
HETATM 4078  O   HOH A 858      16.966  32.770  -6.041  1.00 21.52           O  
HETATM 4079  O   HOH A 859      34.363  18.439  32.407  1.00 18.21           O  
HETATM 4080  O   HOH A 860      45.142  28.850   5.878  1.00  5.40           O  
HETATM 4081  O   HOH A 861      56.045  15.690   8.777  1.00 12.04           O  
HETATM 4082  O   HOH A 862      19.524   9.829  10.165  1.00 47.53           O  
HETATM 4083  O   HOH A 863      24.150  25.250  36.080  1.00 19.01           O  
HETATM 4084  O   HOH A 864      51.393   1.598  -5.249  1.00 17.22           O  
HETATM 4085  O   HOH A 865      41.914  41.733  12.441  1.00  9.79           O  
HETATM 4086  O   HOH A 866      65.975   5.348  17.752  1.00 29.26           O  
HETATM 4087  O   HOH A 867      44.367  15.878  28.904  1.00 22.48           O  
HETATM 4088  O   HOH A 868      43.641  42.427   6.200  1.00 25.96           O  
HETATM 4089  O   HOH A 869      30.335  31.353  36.456  1.00 18.94           O  
HETATM 4090  O   HOH A 870      54.817   5.639  26.572  1.00 20.43           O  
HETATM 4091  O   HOH A 871      43.759  20.202  38.373  1.00 33.26           O  
HETATM 4092  O   HOH A 872      55.556  11.401   8.518  1.00  5.76           O  
HETATM 4093  O   HOH A 873      38.201  30.442 -10.509  1.00 47.61           O  
HETATM 4094  O   HOH A 874      45.061 -10.835  14.852  1.00 17.56           O  
HETATM 4095  O   HOH A 875      40.415 -10.247  25.924  1.00 40.94           O  
HETATM 4096  O   HOH A 876      37.757   4.931  -4.359  1.00 26.02           O  
HETATM 4097  O   HOH A 877      29.791   6.184  16.850  1.00  3.64           O  
HETATM 4098  O   HOH A 878      45.788 -15.450  26.692  1.00 40.22           O  
HETATM 4099  O   HOH A 879      42.896  17.304  43.285  1.00 41.63           O  
HETATM 4100  O   HOH A 880      40.363  30.781  11.379  1.00  3.06           O  
HETATM 4101  O   HOH A 881      65.476  18.780  16.473  1.00 24.89           O  
HETATM 4102  O   HOH A 882      10.958  17.891  -3.180  1.00 18.73           O  
HETATM 4103  O   HOH A 883      33.925  -5.802  28.377  1.00 32.78           O  
HETATM 4104  O   HOH A 884      50.238  20.376   7.957  1.00  3.60           O  
HETATM 4105  O   HOH A 885      49.533  43.021   7.399  1.00 37.88           O  
HETATM 4106  O   HOH A 886      32.500  -4.478  20.692  1.00 16.20           O  
HETATM 4107  O   HOH A 887      17.230  45.741   5.826  1.00 24.87           O  
HETATM 4108  O   HOH A 888      30.838  38.640   0.204  1.00 23.39           O  
HETATM 4109  O   HOH A 889      35.698  29.600  37.852  1.00 27.94           O  
HETATM 4110  O   HOH A 890      19.836  31.471 -10.909  1.00 20.18           O  
HETATM 4111  O   HOH A 891      46.134  11.376   2.733  1.00  5.21           O  
HETATM 4112  O   HOH A 892      59.655   8.136   6.069  1.00 27.34           O  
HETATM 4113  O   HOH A 893      29.469   1.149   8.770  1.00 12.15           O  
HETATM 4114  O   HOH A 894      36.757   3.968   3.502  1.00  5.75           O  
HETATM 4115  O   HOH A 895      20.503  46.417  27.345  1.00 36.03           O  
HETATM 4116  O   HOH A 896      32.245  27.665   5.050  1.00 14.24           O  
HETATM 4117  O   HOH A 897      40.748  35.659  28.508  1.00  9.98           O  
HETATM 4118  O   HOH A 898      30.382  13.543   0.092  1.00 24.96           O  
HETATM 4119  O   HOH A 899      50.539   6.771  -1.422  1.00  7.65           O  
HETATM 4120  O   HOH A 900      11.384  45.840   7.034  1.00 15.86           O  
HETATM 4121  O   HOH A 901      40.877  10.549  -5.869  1.00  9.73           O  
HETATM 4122  O   HOH A 902       8.666  42.043  15.084  1.00 22.97           O  
HETATM 4123  O   HOH A 903      36.221  24.931  32.207  1.00  9.23           O  
HETATM 4124  O   HOH A 904      45.820  11.109 -11.246  1.00 11.22           O  
HETATM 4125  O   HOH A 905      55.930 -11.765  22.041  1.00 20.74           O  
HETATM 4126  O   HOH A 906      45.466  -8.136  13.712  1.00 12.21           O  
HETATM 4127  O   HOH A 907      26.083  54.504  24.225  1.00 20.40           O  
HETATM 4128  O   HOH A 908      27.571   1.008  23.407  1.00 14.62           O  
HETATM 4129  O   HOH A 909      31.375  16.767   4.291  1.00 18.03           O  
HETATM 4130  O   HOH A 910      48.794   6.216  -6.341  1.00 19.12           O  
HETATM 4131  O   HOH A 911      57.342   1.504   4.794  1.00  6.78           O  
HETATM 4132  O   HOH A 912      32.495  38.587  26.593  1.00 23.04           O  
HETATM 4133  O   HOH A 913      40.255   5.805  -2.710  1.00  9.41           O  
HETATM 4134  O   HOH A 914      46.149  28.582  25.819  1.00 18.61           O  
HETATM 4135  O   HOH A 915      33.586  37.307  34.564  1.00 21.95           O  
HETATM 4136  O   HOH A 916      55.027  30.313   9.720  1.00 31.88           O  
HETATM 4137  O   HOH A 917      38.846  25.555   2.186  1.00 11.89           O  
HETATM 4138  O   HOH A 918       7.734  45.028  13.422  1.00 17.98           O  
HETATM 4139  O   HOH A 919      35.264  52.186   9.896  1.00 27.27           O  
HETATM 4140  O   HOH A 920      31.084  22.021   1.857  1.00 18.07           O  
HETATM 4141  O   HOH A 921      47.325   9.939  44.902  1.00 36.77           O  
HETATM 4142  O   HOH A 922      49.953 -14.334  13.421  1.00 19.33           O  
HETATM 4143  O   HOH A 923      42.819   8.600  -5.102  1.00 11.73           O  
HETATM 4144  O   HOH A 924      50.112  34.252  10.012  1.00 21.33           O  
HETATM 4145  O   HOH A 925      46.888 -10.697  27.912  1.00 26.92           O  
HETATM 4146  O   HOH A 926      55.414  -6.328   6.025  1.00 17.50           O  
HETATM 4147  O   HOH A 927      21.561  28.121  37.154  1.00 41.23           O  
HETATM 4148  O   HOH A 928      14.536  18.032   7.243  1.00 24.95           O  
HETATM 4149  O   HOH A 929      23.385  24.819  -1.562  1.00 19.21           O  
HETATM 4150  O   HOH A 930      36.998  41.706   2.314  1.00 20.00           O  
HETATM 4151  O   HOH A 931      62.010   2.938  14.224  1.00 23.59           O  
HETATM 4152  O   HOH A 932      35.678  36.786  31.164  1.00 21.46           O  
HETATM 4153  O   HOH A 933      24.383  14.791   5.357  1.00 12.82           O  
HETATM 4154  O   HOH A 934      47.845  -0.995  -2.650  1.00 22.03           O  
HETATM 4155  O   HOH A 935      42.574  -7.505   6.576  1.00 33.93           O  
HETATM 4156  O   HOH A 936      35.966  19.797  28.696  1.00  9.36           O  
HETATM 4157  O   HOH A 937      35.304  17.592  -5.274  1.00 18.53           O  
HETATM 4158  O   HOH A 938      27.580   4.366   5.859  1.00 19.52           O  
HETATM 4159  O   HOH A 939       5.687  23.485   2.321  1.00 26.14           O  
HETATM 4160  O   HOH A 940      24.927  46.348   6.377  1.00 15.25           O  
HETATM 4161  O   HOH A 941      57.507  -5.488   2.434  1.00 14.36           O  
HETATM 4162  O   HOH A 942      49.265  20.078  -5.524  1.00 15.46           O  
HETATM 4163  O   HOH A 943      33.476  23.029   0.243  1.00 10.61           O  
HETATM 4164  O   HOH A 944      65.845   0.064  19.455  1.00 25.10           O  
HETATM 4165  O   HOH A 945       7.467  26.649  -5.745  1.00 34.12           O  
HETATM 4166  O   HOH A 946      44.469  30.312  29.850  1.00  8.77           O  
HETATM 4167  O   HOH A 947      32.726  -0.663   7.595  1.00 17.52           O  
HETATM 4168  O   HOH A 948      52.938  -1.522   0.314  1.00 15.64           O  
HETATM 4169  O   HOH A 949      60.423   5.705  25.196  1.00 26.28           O  
HETATM 4170  O   HOH A 950      17.480  18.580  21.065  1.00 32.77           O  
HETATM 4171  O   HOH A 951      26.266  26.879  38.173  1.00 26.73           O  
HETATM 4172  O   HOH A 952      21.963  45.457   6.599  1.00 10.35           O  
HETATM 4173  O   HOH A 953      45.815  -8.892  31.659  1.00 21.73           O  
HETATM 4174  O   HOH A 954      49.154  -7.130   4.551  1.00 17.92           O  
HETATM 4175  O   HOH A 955      59.393   7.841  23.294  1.00 22.76           O  
HETATM 4176  O   HOH A 956      38.215  24.354   6.563  1.00  6.16           O  
HETATM 4177  O   HOH A 957      60.091  15.946  17.858  1.00 17.39           O  
HETATM 4178  O   HOH A 958      53.788  20.055  26.101  1.00 46.04           O  
HETATM 4179  O   HOH A 959      18.695  45.101   1.396  1.00 10.89           O  
HETATM 4180  O   HOH A 960      20.857   4.597   7.290  1.00 29.00           O  
HETATM 4181  O   HOH A 961      43.167  25.445  -3.639  1.00 30.97           O  
HETATM 4182  O   HOH A 962      29.489  36.861  -1.413  1.00 30.58           O  
HETATM 4183  O   HOH A 963      31.913  11.213   5.485  1.00  3.59           O  
HETATM 4184  O   HOH A 964      39.512   2.274  26.341  1.00  8.38           O  
HETATM 4185  O   HOH A 965      46.297  -2.075  29.666  1.00 17.44           O  
HETATM 4186  O   HOH A 966       1.777  23.295  -2.782  1.00 21.13           O  
HETATM 4187  O   HOH A 967      48.992  30.206  11.141  1.00 18.15           O  
HETATM 4188  O   HOH A 968      15.156  32.784  21.469  1.00 19.31           O  
HETATM 4189  O   HOH A 969      53.742  25.590  21.055  1.00 14.75           O  
HETATM 4190  O   HOH A 970       7.244  28.639   9.735  1.00 24.38           O  
HETATM 4191  O   HOH A 971      57.768  16.114   2.341  1.00 34.28           O  
HETATM 4192  O   HOH A 972      15.115  25.454  11.425  1.00  4.18           O  
HETATM 4193  O   HOH A 973      46.478  19.379  29.121  1.00 24.06           O  
HETATM 4194  O   HOH A 974      39.186  14.060 -21.640  1.00 40.38           O  
HETATM 4195  O   HOH A 975       6.284  21.335  -7.084  1.00 42.26           O  
HETATM 4196  O   HOH A 976      16.465  27.612  28.781  1.00 42.21           O  
HETATM 4197  O   HOH A 977      32.361  44.793  11.271  1.00  8.54           O  
HETATM 4198  O   HOH A 978      42.683   5.588  28.940  1.00 13.73           O  
HETATM 4199  O   HOH A 979      46.843   4.749  27.369  1.00 56.88           O  
HETATM 4200  O   HOH A 980      45.274  -9.377  10.038  1.00 17.12           O  
HETATM 4201  O   HOH A 981      32.642   7.204   7.659  1.00  4.65           O  
HETATM 4202  O   HOH A 982      22.423  52.007  13.135  1.00 24.93           O  
HETATM 4203  O   HOH A 983      47.537  24.125  28.526  1.00 36.08           O  
HETATM 4204  O   HOH A 984      55.807   2.292   2.613  1.00 14.30           O  
HETATM 4205  O   HOH A 985      39.230  37.841   2.124  1.00 29.99           O  
HETATM 4206  O   HOH A 986      27.883  27.714   3.815  1.00  5.10           O  
HETATM 4207  O   HOH A 987      18.223   5.602  17.189  1.00 39.53           O  
HETATM 4208  O   HOH A 988      35.797  20.603  33.095  1.00 14.16           O  
HETATM 4209  O   HOH A 989      33.141  -3.786  31.670  1.00 39.33           O  
HETATM 4210  O   HOH A 990      18.175  25.736  23.836  1.00 17.05           O  
HETATM 4211  O   HOH A 991      20.768   8.285  25.073  1.00 31.78           O  
HETATM 4212  O   HOH A 992      49.515  29.332  -0.266  1.00 19.09           O  
HETATM 4213  O   HOH A 993      49.462  -8.464  28.522  1.00 18.54           O  
HETATM 4214  O   HOH A 994      43.240  41.386   1.326  1.00 39.35           O  
HETATM 4215  O   HOH A 995      63.657  15.938  25.848  1.00 51.56           O  
HETATM 4216  O   HOH A 996      20.566  16.969  26.814  1.00 12.97           O  
HETATM 4217  O   HOH A 997      25.784  17.709   2.650  1.00 38.01           O  
HETATM 4218  O   HOH A 998      18.855  17.184   8.133  1.00 17.96           O  
HETATM 4219  O   HOH A 999      44.130  27.548  -0.606  1.00  9.68           O  
HETATM 4220  O   HOH A1000      21.549  -3.255  15.890  1.00 36.68           O  
HETATM 4221  O   HOH A1001      23.180  48.107  24.525  1.00 13.59           O  
HETATM 4222  O   HOH A1002      40.132   0.294   9.046  1.00  6.17           O  
HETATM 4223  O   HOH A1003      39.915  33.276   0.588  1.00 17.03           O  
HETATM 4224  O   HOH A1004      46.553   8.496 -11.302  1.00 22.04           O  
HETATM 4225  O   HOH A1005      35.785  33.084  -0.992  1.00 10.17           O  
HETATM 4226  O   HOH A1006      34.418  40.702  -0.854  1.00 30.63           O  
HETATM 4227  O   HOH A1007      26.311  35.391   1.355  1.00 10.08           O  
HETATM 4228  O   HOH A1008      44.323  21.655  31.749  1.00 20.03           O  
HETATM 4229  O   HOH A1009      13.325  16.167  10.390  1.00 14.52           O  
HETATM 4230  O   HOH A1010      29.828  26.075   4.709  1.00  6.51           O  
HETATM 4231  O   HOH A1011      24.172  51.798  10.187  1.00 25.43           O  
HETATM 4232  O   HOH A1012      28.447  40.002   1.840  1.00 19.63           O  
HETATM 4233  O   HOH A1013      34.548  -7.920  18.702  1.00 27.91           O  
HETATM 4234  O   HOH A1014      14.248  26.566  -7.832  1.00 19.25           O  
HETATM 4235  O   HOH A1015      31.342   9.459  27.354  1.00 23.82           O  
HETATM 4236  O   HOH A1016      46.768  44.527  11.376  1.00 44.59           O  
HETATM 4237  O   HOH A1017      62.095  -1.934  20.731  1.00 15.08           O  
HETATM 4238  O   HOH A1018      38.019  21.726   6.565  1.00  3.60           O  
HETATM 4239  O   HOH A1019      54.128  23.169   8.819  1.00 15.83           O  
HETATM 4240  O   HOH A1020      50.408  39.277   9.805  1.00 31.53           O  
HETATM 4241  O   HOH A1021      29.326  15.772 -15.573  1.00 28.31           O  
HETATM 4242  O   HOH A1022      44.878  17.776 -10.314  1.00 14.38           O  
HETATM 4243  O   HOH A1023      32.812  -6.099  14.761  1.00 19.08           O  
HETATM 4244  O   HOH A1024      21.809  22.522  12.436  1.00  8.46           O  
HETATM 4245  O   HOH A1025      31.895  14.918  29.795  1.00 20.17           O  
HETATM 4246  O   HOH A1026      14.683  45.770   6.046  1.00 12.50           O  
HETATM 4247  O   HOH A1027      54.770  -6.240  27.098  1.00  7.19           O  
HETATM 4248  O   HOH A1028      61.560  -2.251  10.953  1.00 10.97           O  
HETATM 4249  O   HOH A1029      38.785  16.648  -7.998  1.00 15.90           O  
HETATM 4250  O   HOH A1030      26.677  19.993  29.481  1.00  8.96           O  
HETATM 4251  O   HOH A1031      56.604  -7.009  10.256  1.00 18.54           O  
HETATM 4252  O   HOH A1032      31.821  23.204  33.992  1.00 12.34           O  
HETATM 4253  O   HOH A1033      30.358  13.286  25.104  1.00  9.85           O  
HETATM 4254  O   HOH A1034      38.173  17.540  33.754  1.00 17.72           O  
HETATM 4255  O   HOH A1035      45.486   9.035   3.575  1.00 12.93           O  
HETATM 4256  O   HOH A1036      47.443   5.173  -1.725  1.00  5.41           O  
HETATM 4257  O   HOH A1037      37.097  52.255  18.130  1.00 23.26           O  
HETATM 4258  O   HOH A1038      24.659  14.039  32.389  1.00 21.58           O  
HETATM 4259  O   HOH A1039      58.984  -4.654  12.060  1.00 20.63           O  
HETATM 4260  O   HOH A1040      28.245   5.491   8.415  1.00  8.74           O  
HETATM 4261  O   HOH A1041      57.759  15.769  13.715  1.00 12.76           O  
HETATM 4262  O   HOH A1042      34.098  38.143  28.375  1.00 15.30           O  
HETATM 4263  O   HOH A1043      17.360  46.222  25.444  1.00 39.79           O  
HETATM 4264  O   HOH A1044      59.903  12.145  19.234  1.00 23.71           O  
HETATM 4265  O   HOH A1045      53.822  31.265   4.492  1.00 47.43           O  
HETATM 4266  O   HOH A1046      18.796  28.687  22.880  1.00 15.25           O  
HETATM 4267  O   HOH A1047      32.703  -6.745  24.733  1.00 24.76           O  
HETATM 4268  O   HOH A1048      57.927  18.561  10.564  1.00 34.33           O  
HETATM 4269  O   HOH A1049      22.011  -3.531   9.695  1.00 38.86           O  
HETATM 4270  O   HOH A1050      25.210  17.171  31.947  1.00 21.10           O  
HETATM 4271  O   HOH A1051      37.938  52.487   6.781  1.00 30.28           O  
HETATM 4272  O   HOH A1052      15.825  44.501  21.474  1.00 11.71           O  
HETATM 4273  O   HOH A1053      51.190  34.253   6.136  1.00 26.92           O  
HETATM 4274  O   HOH A1054       8.693  25.094   4.655  1.00 12.27           O  
HETATM 4275  O   HOH A1055      52.305  -8.605   7.063  1.00 28.19           O  
HETATM 4276  O   HOH A1056      22.789  40.570   0.029  1.00 37.43           O  
HETATM 4277  O   HOH A1057      25.919  38.145   1.180  1.00 21.79           O  
HETATM 4278  O   HOH A1058      15.655  37.773  27.853  1.00 26.71           O  
HETATM 4279  O   HOH A1059      31.165  53.734  17.089  1.00 30.53           O  
HETATM 4280  O   HOH A1060      30.620  -2.275   8.872  1.00 15.58           O  
HETATM 4281  O   HOH A1061      46.936   2.447  29.145  1.00 14.02           O  
HETATM 4282  O   HOH A1062      40.163  16.417   5.082  1.00  4.87           O  
HETATM 4283  O   HOH A1063       8.851  31.057   0.307  1.00 20.11           O  
HETATM 4284  O   HOH A1064      24.312  -3.576   6.901  1.00 38.46           O  
HETATM 4285  O   HOH A1065      34.544   6.500  27.775  1.00 27.00           O  
HETATM 4286  O   HOH A1066      61.255   5.498   8.714  1.00 16.11           O  
HETATM 4287  O   HOH A1067      16.849  13.962   9.881  1.00 16.63           O  
HETATM 4288  O   HOH A1068      56.746  -4.794   8.424  1.00 17.12           O  
HETATM 4289  O   HOH A1069      31.381  -1.523  29.811  1.00 40.65           O  
HETATM 4290  O   HOH A1070      16.513  20.382  -3.588  1.00 20.13           O  
HETATM 4291  O   HOH A1071      43.274  11.718  30.257  1.00 35.32           O  
HETATM 4292  O   HOH A1072      37.941  40.232   4.387  1.00 13.39           O  
HETATM 4293  O   HOH A1073      34.536  44.746  12.806  1.00  6.56           O  
HETATM 4294  O   HOH A1074      58.258 -10.527  18.175  1.00 11.64           O  
HETATM 4295  O   HOH A1075      17.622  42.343  14.731  1.00  7.25           O  
HETATM 4296  O   HOH A1076      11.420  35.115   8.823  1.00 23.46           O  
HETATM 4297  O   HOH A1077      57.192  22.396  16.332  1.00 21.87           O  
HETATM 4298  O   HOH A1078      42.349  22.028  -4.555  1.00 21.34           O  
HETATM 4299  O   HOH A1079      36.414  24.342  -4.886  1.00 34.58           O  
HETATM 4300  O   HOH A1080      45.629  40.299   1.077  1.00 33.88           O  
HETATM 4301  O   HOH A1081      30.891  14.133   4.622  1.00 26.44           O  
HETATM 4302  O   HOH A1082      28.657  14.561   4.738  1.00 14.00           O  
HETATM 4303  O   HOH A1083      18.205   8.916  18.549  1.00 25.11           O  
HETATM 4304  O   HOH A1084      25.265   3.701  26.511  1.00 43.98           O  
HETATM 4305  O   HOH A1085      37.183 -10.571  24.739  1.00 25.49           O  
HETATM 4306  O   HOH A1086      23.424   9.885   5.127  1.00 20.94           O  
HETATM 4307  O   HOH A1087      34.964  45.828   9.299  1.00  9.83           O  
HETATM 4308  O   HOH A1088      17.170  18.747  15.009  1.00  5.26           O  
HETATM 4309  O   HOH A1089      53.678   9.953   4.763  1.00  5.43           O  
HETATM 4310  O   HOH A1090      25.236  52.768  13.681  1.00 26.71           O  
HETATM 4311  O   HOH A1091      60.186   2.067  26.945  1.00 26.63           O  
HETATM 4312  O   HOH A1092      37.466   7.358  -4.121  1.00 12.60           O  
HETATM 4313  O   HOH A1093      42.113 -10.110  33.206  1.00 35.12           O  
HETATM 4314  O   HOH A1094      25.600  -0.821   9.308  1.00 20.06           O  
HETATM 4315  O   HOH A1095      15.910  19.766  24.137  1.00 41.56           O  
HETATM 4316  O   HOH A1096      24.985  28.054 -10.639  1.00 32.75           O  
HETATM 4317  O   HOH A1097      54.156   8.436  -4.398  1.00 29.32           O  
HETATM 4318  O   HOH A1098      24.924  45.467   2.830  1.00 45.93           O  
HETATM 4319  O   HOH A1099      49.746  13.033  24.797  1.00 10.27           O  
HETATM 4320  O   HOH A1100      42.676  36.186  25.433  1.00 37.96           O  
HETATM 4321  O   HOH A1101      24.121  24.297  32.339  1.00 10.72           O  
HETATM 4322  O   HOH A1102      19.999  21.958   8.093  1.00 12.27           O  
HETATM 4323  O   HOH A1103      13.177  14.301   7.351  1.00 30.36           O  
HETATM 4324  O   HOH A1104      19.619  19.643  27.197  1.00 16.09           O  
HETATM 4325  O   HOH A1105      20.236  22.928  -1.792  1.00 24.62           O  
HETATM 4326  O   HOH A1106      20.568  26.161  -0.910  1.00 14.04           O  
HETATM 4327  O   HOH A1107      48.108  16.691  19.056  1.00  7.98           O  
HETATM 4328  O   HOH A1108      18.023  25.461  28.041  1.00 23.23           O  
HETATM 4329  O   HOH A1109      24.361  40.072  34.394  1.00 29.34           O  
HETATM 4330  O   HOH A1110      21.765   3.381  10.184  1.00 27.58           O  
HETATM 4331  O   HOH A1111      44.279  13.522  28.889  1.00 30.29           O  
HETATM 4332  O   HOH A1112      34.645  43.121  14.979  1.00 10.36           O  
HETATM 4333  O   HOH A1113      41.619  -9.795  18.906  1.00 21.03           O  
HETATM 4334  O   HOH A1114      31.426  50.250   3.706  1.00 30.98           O  
HETATM 4335  O   HOH A1115      10.388  37.840  17.704  1.00 24.03           O  
HETATM 4336  O   HOH A1116      56.363  12.763   2.610  1.00 23.09           O  
HETATM 4337  O   HOH A1117      26.519  19.378  33.413  1.00 26.55           O  
HETATM 4338  O   HOH A1118      49.643   4.831  -3.267  1.00 26.83           O  
HETATM 4339  O   HOH A1119      60.515  -4.283  14.582  1.00 16.57           O  
HETATM 4340  O   HOH A1120      40.705  43.033   2.987  1.00 30.69           O  
HETATM 4341  O   HOH A1121      32.305  16.749 -13.760  1.00 40.16           O  
HETATM 4342  O   HOH A1122      57.573  27.786  -1.714  1.00 31.45           O  
HETATM 4343  O   HOH A1123      36.949  39.337   0.631  1.00 27.64           O  
HETATM 4344  O   HOH A1124      64.736   2.952  17.153  1.00 29.34           O  
HETATM 4345  O   HOH A1125      40.192   8.722  28.619  1.00 10.99           O  
HETATM 4346  O   HOH A1126      20.094   8.310  22.080  1.00 20.12           O  
HETATM 4347  O   HOH A1127      34.144   9.764  25.644  1.00 16.84           O  
HETATM 4348  O   HOH A1128      52.725   7.583   0.955  1.00 19.75           O  
HETATM 4349  O   HOH A1129      20.041  24.823  34.181  1.00 34.50           O  
HETATM 4350  O   HOH A1130      12.385  39.571  19.696  1.00 22.02           O  
HETATM 4351  O   HOH A1131      55.478 -10.560  10.124  1.00 12.23           O  
HETATM 4352  O   HOH A1132      33.753  35.427  -6.621  1.00 40.27           O  
HETATM 4353  O   HOH A1133      37.576  12.206  28.677  1.00 10.96           O  
HETATM 4354  O   HOH A1134      19.738   5.678   0.372  1.00 22.62           O  
HETATM 4355  O   HOH A1135      47.303 -19.555  17.579  1.00 48.65           O  
HETATM 4356  O   HOH A1136      22.991   5.382  25.415  1.00 19.52           O  
HETATM 4357  O   HOH A1137      11.610  30.919  -2.568  1.00 19.34           O  
HETATM 4358  O   HOH A1138      30.483  29.820  -4.045  1.00 20.59           O  
HETATM 4359  O   HOH A1139      42.963  37.321   1.118  1.00 26.12           O  
HETATM 4360  O   HOH A1140      26.622   9.186  11.000  1.00  5.88           O  
HETATM 4361  O   HOH A1141      22.977  37.574  39.965  1.00 22.94           O  
HETATM 4362  O   HOH A1142      51.534  26.880  18.098  1.00  6.11           O  
HETATM 4363  O   HOH A1143      50.565  -1.985  -3.858  1.00 25.03           O  
HETATM 4364  O   HOH A1144      44.453   6.966 -11.453  1.00 24.09           O  
HETATM 4365  O   HOH A1145      26.545  -0.175  21.045  1.00 31.05           O  
HETATM 4366  O   HOH A1146      38.556   1.422  29.010  1.00 25.19           O  
HETATM 4367  O   HOH A1147      26.750  18.693  -1.600  1.00 33.46           O  
HETATM 4368  O   HOH A1148      58.366  23.495  23.652  1.00 40.98           O  
HETATM 4369  O   HOH A1149      11.596  13.407   9.752  1.00 56.43           O  
HETATM 4370  O   HOH A1150      58.360  15.451  24.123  1.00 36.82           O  
HETATM 4371  O   HOH A1151      16.291  13.309  24.413  1.00 36.90           O  
HETATM 4372  O   HOH A1152      45.158  -5.339   1.766  1.00 25.09           O  
HETATM 4373  O   HOH A1153      17.417  27.408  35.841  1.00 42.03           O  
HETATM 4374  O   HOH A1154      24.930  53.671  26.905  1.00 21.55           O  
HETATM 4375  O   HOH A1155      49.655  27.161  28.739  1.00 29.64           O  
HETATM 4376  O   HOH A1156      35.886  10.566  -2.788  1.00 21.07           O  
HETATM 4377  O   HOH A1157      46.480   2.255  -5.427  1.00 17.62           O  
HETATM 4378  O   HOH A1158      24.302  12.586   3.847  1.00 37.88           O  
HETATM 4379  O   HOH A1159      59.498  17.790  -1.533  1.00 32.89           O  
HETATM 4380  O   HOH A1160      46.458  37.802  -0.443  1.00 19.75           O  
HETATM 4381  O   HOH A1161       6.438  24.006  -7.420  1.00 37.84           O  
HETATM 4382  O   HOH A1162      30.210  21.810  -0.740  1.00 27.74           O  
HETATM 4383  O   HOH A1163      29.588   3.635   9.723  1.00  6.56           O  
HETATM 4384  O   HOH A1164      23.695  38.620  -5.330  1.00 39.84           O  
HETATM 4385  O   HOH A1165      11.434  18.652   9.319  1.00 30.92           O  
HETATM 4386  O   HOH A1166      49.456  23.096  -1.117  1.00 18.84           O  
HETATM 4387  O   HOH A1167      16.465  37.299  -2.239  1.00 32.95           O  
HETATM 4388  O   HOH A1168      57.425  -9.666  26.253  1.00  7.92           O  
HETATM 4389  O   HOH A1169      47.540 -15.142  14.450  1.00 33.85           O  
HETATM 4390  O   HOH A1170      32.818  13.418   3.049  1.00 29.31           O  
HETATM 4391  O   HOH A1171      55.353  16.011  27.245  1.00 47.86           O  
HETATM 4392  O   HOH A1172      19.171  46.825   7.652  1.00 39.91           O  
HETATM 4393  O   HOH A1173      59.598 -10.231  22.439  1.00 34.62           O  
HETATM 4394  O   HOH A1174      47.853  44.696   6.736  1.00 41.30           O  
HETATM 4395  O   HOH A1175       8.653  29.970  16.552  1.00 47.23           O  
HETATM 4396  O   HOH A1176      22.984  52.912  18.819  1.00 25.40           O  
HETATM 4397  O   HOH A1177      19.494  21.675  11.019  1.00  9.26           O  
HETATM 4398  O   HOH A1178      28.876   4.895   2.294  1.00 25.04           O  
HETATM 4399  O   HOH A1179      15.077  43.132  14.972  1.00 13.08           O  
HETATM 4400  O   HOH A1180      45.803  11.059  29.512  1.00 36.86           O  
HETATM 4401  O   HOH A1181      60.271  14.444  20.193  1.00 35.67           O  
HETATM 4402  O   HOH A1182      28.997  53.091  18.089  1.00 32.36           O  
HETATM 4403  O   HOH A1183      37.767  34.975   0.227  1.00 17.21           O  
HETATM 4404  O   HOH A1184      41.253  51.937  20.405  1.00 27.69           O  
HETATM 4405  O   HOH A1185      53.145 -13.532  19.275  1.00 26.06           O  
HETATM 4406  O   HOH A1186      21.832   8.866   7.303  1.00 28.01           O  
HETATM 4407  O   HOH A1187      42.874   1.353  -9.446  1.00 22.98           O  
HETATM 4408  O   HOH A1188      47.793  -5.380   2.962  1.00 28.26           O  
HETATM 4409  O   HOH A1189      27.728  -7.287  12.206  1.00 29.86           O  
HETATM 4410  O   HOH A1190      36.490  28.148   2.547  1.00 28.20           O  
HETATM 4411  O   HOH A1191      16.405  23.671  24.242  1.00 26.29           O  
HETATM 4412  O   HOH A1192      14.737  45.502  16.778  1.00 15.39           O  
HETATM 4413  O   HOH A1193      21.923  45.841  23.169  1.00  3.28           O  
HETATM 4414  O   HOH A1194      47.253  35.915  16.650  1.00 25.99           O  
HETATM 4415  O   HOH A1195      52.191  30.919   7.148  1.00 36.74           O  
HETATM 4416  O   HOH A1196      17.808  55.491  23.941  1.00 34.13           O  
HETATM 4417  O   HOH A1197      16.288  28.613  22.319  1.00 34.44           O  
HETATM 4418  O   HOH A1198      27.658  -0.228  25.743  1.00 33.87           O  
HETATM 4419  O   HOH A1199      20.761  51.140  10.085  1.00 26.26           O  
HETATM 4420  O   HOH A1200      37.630  26.985  -2.049  1.00 33.64           O  
HETATM 4421  O   HOH A1201       8.816  39.593  18.633  1.00 37.05           O  
HETATM 4422  O   HOH A1202      18.358  39.795  24.727  1.00 32.19           O  
HETATM 4423  O   HOH A1203      62.089  -6.639  14.248  1.00 35.19           O  
HETATM 4424  O   HOH A1204      58.225  19.555   7.446  1.00 26.60           O  
HETATM 4425  O   HOH A1205      16.990  17.290   5.994  1.00 31.94           O  
HETATM 4426  O   HOH A1206      27.190  -4.369   5.865  1.00 19.57           O  
HETATM 4427  O   HOH A1207      21.263  27.904 -10.446  1.00 34.60           O  
HETATM 4428  O   HOH A1208      51.752  35.273  26.783  1.00 36.66           O  
HETATM 4429  O   HOH A1209      13.159  19.831   3.741  1.00 24.89           O  
HETATM 4430  O   HOH A1210      18.223  11.867  10.943  1.00 35.08           O  
HETATM 4431  O   HOH A1211      37.272   5.739  25.785  1.00 32.18           O  
HETATM 4432  O   HOH A1212      44.106  -1.970  34.260  1.00 35.94           O  
HETATM 4433  O   HOH A1213      23.324  33.121  -2.905  1.00 25.29           O  
HETATM 4434  O   HOH A1214      47.747  14.952  28.486  1.00 53.85           O  
HETATM 4435  O   HOH A1215      37.436  26.835  33.853  1.00 16.41           O  
HETATM 4436  O   HOH A1216      56.020  10.842   5.774  1.00 11.01           O  
HETATM 4437  O   HOH A1217      16.843  48.628  19.119  1.00 19.22           O  
HETATM 4438  O   HOH A1218       0.408  20.897  -7.447  1.00 31.58           O  
HETATM 4439  O   HOH A1219      39.199  29.529  -1.618  1.00 22.49           O  
HETATM 4440  O   HOH A1220      32.672  28.243  -2.911  1.00 31.42           O  
HETATM 4441  O   HOH A1221      54.990   8.511  -1.999  1.00 39.36           O  
HETATM 4442  O   HOH A1222      34.282  13.514   0.725  1.00 13.86           O  
HETATM 4443  O   HOH A1223      44.768  50.891  13.914  1.00 33.38           O  
HETATM 4444  O   HOH A1224      40.241 -12.429  18.439  1.00 28.73           O  
HETATM 4445  O   HOH A1225      42.513  22.831  33.313  1.00 32.47           O  
HETATM 4446  O   HOH A1226      13.886  37.394  20.073  1.00 18.51           O  
HETATM 4447  O   HOH A1227      28.495  -6.774  15.897  1.00 26.10           O  
HETATM 4448  O   HOH A1228      19.071  33.401  28.412  1.00 35.79           O  
HETATM 4449  O   HOH A1229      26.392  43.702   0.082  1.00 27.52           O  
HETATM 4450  O   HOH A1230      39.084  47.532  27.854  1.00 40.14           O  
HETATM 4451  O   HOH A1231      56.204  12.030  -4.174  1.00 28.94           O  
HETATM 4452  O   HOH A1232      56.587   8.535   0.947  1.00 34.09           O  
HETATM 4453  O   HOH A1233      53.121 -10.879   8.086  1.00 37.43           O  
HETATM 4454  O   HOH A1234      39.130  52.678  11.629  1.00 42.30           O  
HETATM 4455  O   HOH A1235      59.744  11.832  -0.896  1.00 37.54           O  
HETATM 4456  O   HOH A1236      11.045  15.340   1.295  1.00 40.26           O  
HETATM 4457  O   HOH A1237      15.978  15.234  21.206  1.00 38.31           O  
HETATM 4458  O   HOH A1238      29.534  -4.106  17.291  1.00 37.05           O  
HETATM 4459  O   HOH A1239      57.312  23.060   4.536  1.00 18.14           O  
HETATM 4460  O   HOH A1240      36.575  -4.896   6.444  1.00 49.22           O  
HETATM 4461  O   HOH A1241      49.837   8.797  -9.531  1.00 33.16           O  
HETATM 4462  O   HOH A1242      17.227  28.403 -10.714  1.00 43.78           O  
HETATM 4463  O   HOH A1243      10.043  29.200  19.063  1.00 42.91           O  
HETATM 4464  O   HOH A1244      54.629 -15.641  10.816  1.00 46.78           O  
HETATM 4465  O   HOH A1245      44.773 -11.411  33.168  1.00 49.64           O  
HETATM 4466  O   HOH A1246      46.688  30.105  28.136  1.00 30.96           O  
HETATM 4467  O   HOH A1247      38.741  25.052  -3.364  1.00 35.91           O  
HETATM 4468  O   HOH A1248      33.979  11.226  -7.566  1.00 38.48           O  
HETATM 4469  O   HOH A1249      42.669  -3.637   3.715  1.00 23.73           O  
HETATM 4470  O   HOH A1250       9.011  22.117   9.197  1.00 44.57           O  
HETATM 4471  O   HOH A1251      25.747   8.863  28.870  1.00 37.10           O  
HETATM 4472  O   HOH A1252      14.622  43.725  23.655  1.00 43.75           O  
HETATM 4473  O   HOH A1253       1.270  25.369  -3.963  1.00 33.80           O  
HETATM 4474  O   HOH A1254      57.619   2.097  28.079  1.00 25.38           O  
HETATM 4475  O   HOH A1255      26.488  12.865   2.580  1.00 41.15           O  
HETATM 4476  O   HOH A1256      40.796   6.877  -5.806  1.00 31.19           O  
HETATM 4477  O   HOH A1257      53.104 -15.362  15.235  1.00 33.68           O  
HETATM 4478  O   HOH A1258      17.336  31.552  23.025  1.00 37.03           O  
HETATM 4479  O   HOH A1259      40.624  21.100  -8.791  1.00 29.84           O  
HETATM 4480  O   HOH A1260      58.245  15.985  -6.079  1.00 18.57           O  
HETATM 4481  O   HOH A1261      37.013  14.042  30.917  1.00 41.27           O  
HETATM 4482  O   HOH A1262      48.898   8.525  27.530  1.00 30.51           O  
HETATM 4483  O   HOH A1263      36.854  20.154  35.731  1.00 36.80           O  
HETATM 4484  O   HOH A1264      24.055   2.346  20.520  1.00 40.26           O  
HETATM 4485  O   HOH A1265      12.035  25.469  -8.743  1.00 39.95           O  
HETATM 4486  O   HOH A1266      27.501  35.241  -1.075  1.00 24.80           O  
HETATM 4487  O   HOH A1267      48.745  14.589 -11.345  1.00 15.20           O  
HETATM 4488  O   HOH A1268      42.749  17.788 -11.731  1.00 20.54           O  
HETATM 4489  O   HOH A1269      36.820  25.539  -0.034  1.00 15.02           O  
HETATM 4490  O   HOH A1270      52.514  11.705  -7.375  1.00 16.26           O  
HETATM 4491  O   HOH A1271      46.981  46.899  12.917  1.00 41.97           O  
HETATM 4492  O   HOH A1272      33.581  27.489   0.034  1.00 40.76           O  
HETATM 4493  O   HOH A1273      46.867  12.593  27.844  1.00 21.85           O  
HETATM 4494  O   HOH A1274      46.305  43.351  -0.123  1.00 38.70           O  
HETATM 4495  O   HOH A1275      61.922  20.512  18.620  1.00 39.03           O  
HETATM 4496  O   HOH A1276      36.676   1.455   2.500  1.00 15.01           O  
HETATM 4497  O   HOH A1277      18.936   4.723  13.390  1.00 30.19           O  
HETATM 4498  O   HOH A1278      11.861  37.436  10.216  1.00 23.78           O  
HETATM 4499  O   HOH A1279       9.205  33.372  -0.965  1.00 30.42           O  
HETATM 4500  O   HOH A1280      41.536   7.511  30.583  1.00 27.62           O  
HETATM 4501  O   HOH A1281      34.000  28.596   2.633  1.00 16.90           O  
HETATM 4502  O   HOH A1282      23.937   9.233  -0.545  1.00 40.27           O  
HETATM 4503  O   HOH A1283      31.704   1.841   7.170  1.00 12.26           O  
HETATM 4504  O   HOH A1284       7.767  26.425   7.869  1.00 24.16           O  
HETATM 4505  O   HOH A1285      49.763  14.929  26.882  1.00 29.84           O  
HETATM 4506  O   HOH A1286      43.231  24.343  31.224  1.00 30.93           O  
HETATM 4507  O   HOH A1287      58.504  13.222   4.769  1.00 40.82           O  
HETATM 4508  O   HOH A1288      59.291 -11.139  15.977  1.00 33.99           O  
HETATM 4509  O   HOH A1289      64.476  -1.082  21.749  1.00 28.71           O  
HETATM 4510  O   HOH A1290      45.329  44.797  17.160  1.00 38.49           O  
HETATM 4511  O   HOH A1291      53.770  20.649 -10.410  1.00 51.58           O  
HETATM 4512  O   HOH A1292      26.936  15.429  33.272  1.00 40.81           O  
HETATM 4513  O   HOH A1293       1.184  25.746  -6.717  1.00 32.63           O  
HETATM 4514  O   HOH A1294      24.640  48.850   5.700  1.00 31.40           O  
HETATM 4515  O   HOH A1295      46.058  40.875  11.772  1.00 35.11           O  
HETATM 4516  O   HOH A1296      31.759  21.102  35.579  1.00 33.75           O  
HETATM 4517  O   HOH A1297      30.942  54.760  14.424  1.00 35.58           O  
HETATM 4518  O   HOH A1298      50.387  31.960  13.347  1.00 28.29           O  
HETATM 4519  O   HOH A1299      28.423  -2.782   7.316  1.00 16.74           O  
HETATM 4520  O   HOH A1300      32.080  39.389  34.792  1.00 22.08           O  
HETATM 4521  O   HOH A1301      36.997  -2.114   5.938  1.00 20.08           O  
HETATM 4522  O   HOH A1302      33.138  34.386  -4.197  1.00 28.29           O  
HETATM 4523  O   HOH A1303      28.704  -1.257  19.664  1.00 35.18           O  
HETATM 4524  O   HOH A1304      31.058  12.909  31.598  1.00 27.40           O  
HETATM 4525  O   HOH A1305      38.147  16.524  31.362  1.00 17.98           O  
HETATM 4526  O   HOH A1306      43.605  10.563 -13.452  1.00 20.71           O  
HETATM 4527  O   HOH A1307       9.834  36.669  15.409  1.00 35.33           O  
HETATM 4528  O   HOH A1308      53.062  18.993  -8.479  1.00 13.94           O  
HETATM 4529  O   HOH A1309      23.647  23.108  34.589  1.00 20.48           O  
HETATM 4530  O   HOH A1310       8.706  11.111   6.236  1.00 39.72           O  
HETATM 4531  O   HOH A1311      11.903   7.094   6.154  1.00 44.10           O  
HETATM 4532  O   HOH A1312      17.185  47.051  21.184  1.00 22.56           O  
HETATM 4533  O   HOH A1313      35.840  -7.942   8.468  1.00 27.07           O  
HETATM 4534  O   HOH A1314      40.743  24.707  32.272  1.00 10.50           O  
HETATM 4535  O   HOH A1315      42.387  11.946 -16.004  1.00 29.19           O  
HETATM 4536  O   HOH A1316      59.509  -3.636   1.212  1.00 27.06           O  
HETATM 4537  O   HOH A1317      40.798  24.109  -4.633  1.00 27.91           O  
HETATM 4538  O   HOH A1318      46.507  40.931   8.668  1.00 31.56           O  
HETATM 4539  O   HOH A1319      34.286  -8.427  16.130  1.00 29.98           O  
HETATM 4540  O   HOH A1320      40.457  20.459  37.513  1.00 38.79           O  
HETATM 4541  O   HOH A1321      37.379  29.550   0.777  1.00 34.58           O  
HETATM 4542  O   HOH A1322       8.107  35.291  11.999  1.00 30.12           O  
HETATM 4543  O   HOH A1323      30.658  -7.216  13.526  1.00 33.90           O  
HETATM 4544  O   HOH A1324      30.610  35.518  -3.919  1.00 35.89           O  
HETATM 4545  O   HOH A1325      42.086  -7.330   3.529  1.00 31.10           O  
HETATM 4546  O   HOH A1326      43.068  50.287   5.577  1.00 34.09           O  
HETATM 4547  O   HOH A1327      22.490  25.753  -4.055  1.00 31.12           O  
HETATM 4548  O   HOH A1328      61.668   0.938   6.225  1.00 31.99           O  
HETATM 4549  O   HOH A1329      54.271  28.247  22.305  1.00 31.16           O  
HETATM 4550  O   HOH A1330      57.169  23.414   7.797  1.00 33.50           O  
HETATM 4551  O   HOH A1331      29.471  57.410  31.116  1.00 28.59           O  
HETATM 4552  O   HOH A1332      34.646  32.171  36.975  1.00 30.27           O  
HETATM 4553  O   HOH A1333      33.072  40.396  -3.188  1.00 41.96           O  
HETATM 4554  O   HOH A1334      27.268  54.997  18.670  1.00 28.41           O  
HETATM 4555  O   HOH A1335      -1.119  21.964  -3.454  1.00 24.85           O  
HETATM 4556  O   HOH A1336      56.476 -12.526  19.729  1.00 35.67           O  
HETATM 4557  O   HOH A1337      49.449  30.429  19.926  1.00 43.55           O  
HETATM 4558  O   HOH A1338      59.531  18.785   3.469  1.00 23.59           O  
HETATM 4559  O   HOH A1339      19.418  26.103  26.090  1.00 28.27           O  
HETATM 4560  O   HOH A1340      11.001  20.875   5.391  1.00 21.93           O  
HETATM 4561  O   HOH A1341      55.051   1.001  30.788  1.00 36.17           O  
HETATM 4562  O   HOH A1342      38.417  10.438  30.384  1.00 35.60           O  
HETATM 4563  O   HOH A1343      25.410  40.160  37.001  1.00 37.21           O  
HETATM 4564  O   HOH A1344      55.758  -8.830   6.967  1.00 37.71           O  
HETATM 4565  O   HOH A1345      47.503  33.980  22.094  1.00 42.95           O  
HETATM 4566  O   HOH A1346      37.544  53.668   9.276  1.00 30.98           O  
HETATM 4567  O   HOH A1347      51.595  -8.245   4.565  1.00 27.26           O  
HETATM 4568  O   HOH A1348      35.765  33.552  -3.608  1.00 28.09           O  
HETATM 4569  O   HOH A1349      33.044   8.232  29.088  1.00 55.61           O  
HETATM 4570  O   HOH A1350      41.987  45.054  20.337  1.00 26.06           O  
HETATM 4571  O   HOH A1351      52.481  12.378 -10.056  1.00 21.56           O  
HETATM 4572  O   HOH A1352      23.644   6.520  28.174  1.00 20.76           O  
HETATM 4573  O   HOH A1353      40.664  11.581  31.958  1.00 38.28           O  
HETATM 4574  O   HOH A1354      26.664  42.621  36.096  1.00 46.42           O  
HETATM 4575  O   HOH A1355      31.250  33.636  37.241  1.00 30.97           O  
HETATM 4576  O   HOH A1356      30.341  21.515  -5.073  1.00 27.17           O  
HETATM 4577  O   HOH A1357      53.136 -13.844  23.691  1.00 30.09           O  
HETATM 4578  O   HOH A1358       6.044  21.028 -10.242  1.00 35.72           O  
HETATM 4579  O   HOH A1359      15.298  15.461   8.123  1.00 26.39           O  
HETATM 4580  O   HOH A1360      42.062  13.853  31.266  1.00 26.56           O  
HETATM 4581  O   HOH A1361      59.933  22.533  17.416  1.00 30.10           O  
HETATM 4582  O   HOH A1362      57.527  16.826   6.864  1.00 23.08           O  
HETATM 4583  O   HOH A1363      58.201  11.647   8.925  1.00 14.61           O  
HETATM 4584  O   HOH A1364      57.114  17.258  -8.392  1.00 18.29           O  
HETATM 4585  O   HOH A1365      45.617  37.983  16.563  1.00 25.30           O  
HETATM 4586  O   HOH A1366      44.407  53.361  12.752  1.00 39.35           O  
HETATM 4587  O   HOH A1367      11.888  23.491  14.185  1.00 20.85           O  
HETATM 4588  O   HOH A1368      48.664  42.730  12.013  1.00 55.14           O  
HETATM 4589  O   HOH A1369      55.535  25.554  18.686  1.00 40.12           O  
HETATM 4590  O   HOH A1370      52.483  30.058  21.596  1.00 51.21           O  
HETATM 4591  O   HOH A1371      43.658  14.255  33.487  1.00 46.57           O  
HETATM 4592  O   HOH A1372      43.004  -3.564  -0.852  1.00 16.53           O  
HETATM 4593  O   HOH A1373      51.256  40.239  12.292  1.00 49.36           O  
HETATM 4594  O   HOH A1374      56.547  11.353  -1.852  1.00 36.27           O  
HETATM 4595  O   HOH A1375      32.457  -7.526  20.953  1.00 35.62           O  
HETATM 4596  O   HOH A1376      60.263  21.945  12.917  1.00 40.94           O  
HETATM 4597  O   HOH A1377      19.835  53.334  11.388  1.00 40.20           O  
HETATM 4598  O   HOH A1378      36.209  23.989  -7.533  1.00 39.34           O  
HETATM 4599  O   HOH A1379      32.069  29.395  38.038  1.00 39.35           O  
HETATM 4600  O   HOH A1380      59.587  21.300  22.688  1.00 35.97           O  
HETATM 4601  O   HOH A1381      35.687  17.377  30.079  1.00 15.56           O  
HETATM 4602  O   HOH A1382      42.433  44.804   2.295  1.00 44.82           O  
HETATM 4603  O   HOH A1383      46.983  20.507  -6.778  1.00 22.37           O  
HETATM 4604  O   HOH A1384      55.142  11.585   0.799  1.00 36.09           O  
HETATM 4605  O   HOH A1385      65.547  -2.124  17.048  1.00 31.02           O  
HETATM 4606  O   HOH A1386      27.268   0.450   7.543  1.00 39.27           O  
HETATM 4607  O   HOH A1387      41.979  16.342 -15.674  1.00 36.35           O  
HETATM 4608  O   HOH A1388      27.573  40.346  40.452  1.00 30.79           O  
HETATM 4609  O   HOH A1389      59.640  14.512  15.069  1.00 23.00           O  
HETATM 4610  O   HOH A1390      27.825  31.090  37.656  1.00 27.17           O  
HETATM 4611  O   HOH A1391      20.704   2.406  16.325  1.00 30.53           O  
HETATM 4612  O   HOH A1392      64.195   1.938  14.880  1.00 39.25           O  
HETATM 4613  O   HOH A1393      18.242  47.015   3.177  1.00 24.89           O  
HETATM 4614  O   HOH A1394      49.148  16.946  48.721  1.00 13.24           O  
HETATM 4615  O   HOH A1395      30.753  40.363  -2.038  1.00 31.68           O  
HETATM 4616  O   HOH A1396      16.720  35.484  -5.029  1.00 25.43           O  
HETATM 4617  O   HOH A1397      12.642  11.056  -0.809  1.00 32.01           O  
HETATM 4618  O   HOH A1398       4.389  23.675 -11.309  1.00 42.77           O  
HETATM 4619  O   HOH A1399      31.784 -10.375  35.306  1.00 38.89           O  
HETATM 4620  O   HOH A1400      40.561  46.752   4.457  1.00 24.26           O  
HETATM 4621  O   HOH A1401      25.851  34.118  -3.122  1.00 33.37           O  
HETATM 4622  O   HOH A1402      37.378  45.414   1.980  1.00 32.92           O  
HETATM 4623  O   HOH A1403      57.766 -12.964  23.831  1.00 27.34           O  
HETATM 4624  O   HOH A1404      36.795   7.645  27.789  1.00 28.12           O  
HETATM 4625  O   HOH A1405      19.604   0.234  13.293  1.00 33.26           O  
HETATM 4626  O   HOH A1406      10.527  16.558   4.523  1.00 44.83           O  
HETATM 4627  O   HOH A1407      34.554  15.268  29.548  1.00 28.80           O  
HETATM 4628  O   HOH A1408      44.304   7.757  45.498  1.00 46.65           O  
HETATM 4629  O   HOH A1409      57.554   6.195  26.785  1.00 35.71           O  
HETATM 4630  O   HOH A1410      12.060  15.407  -2.516  1.00 33.57           O  
HETATM 4631  O   HOH A1411      46.191  18.052 -12.527  1.00 24.81           O  
HETATM 4632  O   HOH A1412      45.142  22.236  -5.518  1.00 36.07           O  
HETATM 4633  O   HOH A1413      54.977 -16.058  13.297  1.00 51.83           O  
HETATM 4634  O   HOH A1414      60.796  18.487   1.229  1.00 26.67           O  
HETATM 4635  O   HOH A1415      35.307  16.897  34.251  1.00 26.85           O  
HETATM 4636  O   HOH A1416      10.049  36.784  20.002  1.00 40.77           O  
HETATM 4637  O   HOH A1417      57.821  15.654  11.183  1.00 24.78           O  
HETATM 4638  O   HOH A1418      52.403  36.695   7.394  1.00 44.83           O  
HETATM 4639  O   HOH A1419      59.435  11.744  16.936  1.00 19.96           O  
HETATM 4640  O   HOH A1420      16.025  24.579  -8.852  1.00 41.01           O  
HETATM 4641  O   HOH A1421      40.320  53.987  17.544  1.00 43.47           O  
HETATM 4642  O   HOH A1422      43.525  21.679 -13.387  1.00 42.52           O  
HETATM 4643  O   HOH A1423      34.554  23.253  33.424  1.00 13.72           O  
HETATM 4644  O   HOH A1424      50.415 -13.717  27.834  1.00 40.74           O  
HETATM 4645  O   HOH A1425      63.370  -5.845  16.387  1.00 38.35           O  
HETATM 4646  O   HOH A1426      45.211  26.813  -4.295  1.00 25.12           O  
HETATM 4647  O   HOH A1427      37.520 -13.289  17.376  1.00 39.11           O  
HETATM 4648  O   HOH A1428      62.422   2.983  28.636  1.00 29.14           O  
HETATM 4649  O   HOH A1429      44.371  12.220  46.672  1.00 14.17           O  
HETATM 4650  O   HOH A1430      35.238  12.704  29.700  1.00 58.65           O  
HETATM 4651  O   HOH A1431      62.025  -2.150   8.174  1.00 35.27           O  
HETATM 4652  O   HOH A1432      59.514  -2.756   6.086  1.00 24.49           O  
HETATM 4653  O   HOH A1433      16.407  23.086  27.015  1.00 27.40           O  
HETATM 4654  O   HOH A1434      57.949  23.584  13.669  1.00 39.65           O  
HETATM 4655  O   HOH A1435      63.685  -4.123  19.700  1.00 36.76           O  
HETATM 4656  O   HOH A1436      49.607   5.644  30.372  1.00 32.94           O  
HETATM 4657  O   HOH A1437      32.091  25.354  35.835  1.00 24.39           O  
HETATM 4658  O   HOH A1438       6.364  29.733  11.904  1.00 45.08           O  
HETATM 4659  O   HOH A1439      45.265  20.005  -8.737  1.00 21.25           O  
HETATM 4660  O   HOH A1440      46.322  10.669  47.368  1.00 18.46           O  
HETATM 4661  O   HOH A1441      51.788  11.928  46.562  1.00 42.06           O  
HETATM 4662  O   HOH A1442      42.937  -9.292   8.613  1.00 35.20           O  
HETATM 4663  O   HOH A1443      49.477  26.237  -3.319  1.00 19.04           O  
HETATM 4664  O   HOH A1444      60.751  17.291  -5.666  1.00 27.52           O  
HETATM 4665  O   HOH A1445      55.821  27.530  -3.721  1.00 38.69           O  
HETATM 4666  O   HOH A1446      24.899  20.434  35.143  1.00 33.07           O  
HETATM 4667  O   HOH A1447      58.010  -5.628   4.927  1.00 45.69           O  
HETATM 4668  O   HOH A1448      10.472  27.543  -9.413  1.00 34.40           O  
HETATM 4669  O   HOH A1449      26.004  37.647  -4.263  1.00 39.27           O  
HETATM 4670  O   HOH A1450      42.975  45.855   5.573  1.00 24.19           O  
HETATM 4671  O   HOH A1451      10.698  24.775  16.219  1.00 23.95           O  
HETATM 4672  O   HOH A1452      54.758  -8.895   2.188  1.00 30.98           O  
HETATM 4673  O   HOH A1453      59.384  -0.191   4.859  1.00 16.59           O  
HETATM 4674  O   HOH A1454      55.247  24.471  16.022  1.00 31.41           O  
HETATM 4675  O   HOH A1455      20.903  22.082  -5.683  1.00 29.96           O  
HETATM 4676  O   HOH A1456       8.862  13.999  10.040  1.00 28.42           O  
HETATM 4677  O   HOH A1457      49.550  27.903  16.349  1.00 12.84           O  
HETATM 4678  O   HOH A1458      54.817  11.028  -6.355  1.00 26.56           O  
HETATM 4679  O   HOH A1459      43.331  36.703  22.931  1.00 45.05           O  
HETATM 4680  O   HOH A1460      57.951   3.841   1.223  1.00 35.70           O  
HETATM 4681  O   HOH A1461      14.776  16.061  -5.038  1.00 42.02           O  
HETATM 4682  O   HOH A1462      51.263   9.880  28.778  1.00 32.68           O  
HETATM 4683  O   HOH A1463      44.815  47.218   8.624  1.00 36.70           O  
HETATM 4684  O   HOH A1464      51.176  39.361   7.459  1.00 30.90           O  
HETATM 4685  O   HOH A1465      38.915   6.688  27.281  1.00 14.67           O  
HETATM 4686  O   HOH A1466      47.757   3.974  -7.117  1.00 39.55           O  
HETATM 4687  O   HOH A1467      39.031  53.081  19.811  1.00 39.26           O  
HETATM 4688  O   HOH A1468      34.785  23.966  36.219  1.00 38.62           O  
HETATM 4689  O   HOH A1469      34.123  19.314  36.736  1.00 38.91           O  
HETATM 4690  O   HOH A1470      35.711  10.309  27.484  1.00 36.12           O  
HETATM 4691  O   HOH A1471      44.529   3.910  30.583  1.00 42.03           O  
HETATM 4692  O   HOH A1472      17.698  32.461  25.541  1.00 56.11           O  
HETATM 4693  O   HOH A1473      38.316  36.359  -2.051  1.00 24.40           O  
HETATM 4694  O   HOH A1474      45.865  50.090  10.020  1.00 27.18           O  
HETATM 4695  O   HOH A1475      41.195 -11.068  12.351  1.00 32.88           O  
HETATM 4696  O   HOH A1476      23.036  24.733  38.518  1.00 41.78           O  
HETATM 4697  O   HOH A1477      44.181   4.251 -11.537  1.00 31.02           O  
HETATM 4698  O   HOH A1478      52.335  29.208  19.170  1.00 34.51           O  
HETATM 4699  O   HOH A1479      57.719   8.670  25.556  1.00 54.35           O  
HETATM 4700  O   HOH A1480      18.830  29.302  25.564  1.00 42.36           O  
HETATM 4701  O   HOH A1481      40.356   4.385  27.780  1.00 18.67           O  
HETATM 4702  O   HOH A1482      44.209  18.112 -14.611  1.00 34.73           O  
HETATM 4703  O   HOH A1483      33.707  12.896  27.652  1.00 33.20           O  
HETATM 4704  O   HOH A1484      51.659  16.076  48.562  1.00 21.47           O  
HETATM 4705  O   HOH A1485      44.958   0.657  32.794  1.00 33.90           O  
HETATM 4706  O   HOH A1486      47.735  31.980  18.359  1.00 55.84           O  
HETATM 4707  O   HOH A1487      58.900  20.654   4.925  1.00 18.86           O  
HETATM 4708  O   HOH A1488      42.643  21.673  -7.166  1.00 37.40           O  
HETATM 4709  O   HOH A1489      60.061  -1.095   2.170  1.00 28.87           O  
HETATM 4710  O   HOH A1490       9.362  38.023  11.535  1.00 34.40           O  
HETATM 4711  O   HOH A1491      40.219  44.622  22.279  1.00 40.39           O  
HETATM 4712  O   HOH A1492      33.331  10.915  29.964  1.00 45.64           O  
HETATM 4713  O   HOH A1493       9.686  16.812   8.298  1.00 42.68           O  
HETATM 4714  O   HOH A1494      56.158  29.438  20.696  1.00 41.19           O  
HETATM 4715  O   HOH A1495      53.035  26.723  15.446  1.00 33.37           O  
HETATM 4716  O   HOH A1496       8.262  18.677  -9.608  1.00 30.40           O  
HETATM 4717  O   HOH A1497      51.082  30.137  15.698  1.00 17.11           O  
HETATM 4718  O   HOH A1498      38.992  31.060  -4.350  1.00 41.75           O  
HETATM 4719  O   HOH A1499      61.212  -3.724   3.885  1.00 39.71           O  
HETATM 4720  O   HOH A1500       6.644  28.515  13.995  1.00 33.37           O  
HETATM 4721  O   HOH A1501      44.268  24.174  -7.435  1.00 46.82           O  
HETATM 4722  O   HOH A1502      39.161   6.356  31.886  1.00 38.46           O  
HETATM 4723  O   HOH A1503      36.452   8.957  31.245  1.00 48.24           O  
HETATM 4724  O   HOH A1504      53.616  29.223  14.908  1.00 40.85           O  
HETATM 4725  O   HOH A1505      38.562  55.627  20.704  1.00 55.61           O  
HETATM 4726  O   HOH A1506       6.590  26.044  14.761  1.00 45.98           O  
CONECT    1    2    5                                                           
CONECT    2    1    3    7                                                      
CONECT    3    2    4                                                           
CONECT    4    3    5                                                           
CONECT    5    1    4    6                                                      
CONECT    6    5                                                                
CONECT    7    2    8    9                                                      
CONECT    8    7                                                                
CONECT    9    7                                                                
CONECT 1603 3786                                                                
CONECT 3786 1603 3787 3795                                                      
CONECT 3787 3786 3788 3792                                                      
CONECT 3788 3787 3789 3793                                                      
CONECT 3789 3788 3790 3794                                                      
CONECT 3790 3789 3791 3795                                                      
CONECT 3791 3790 3796                                                           
CONECT 3792 3787 3797                                                           
CONECT 3793 3788                                                                
CONECT 3794 3789 3851                                                           
CONECT 3795 3786 3790                                                           
CONECT 3796 3791                                                                
CONECT 3797 3792 3798 3806                                                      
CONECT 3798 3797 3799 3803                                                      
CONECT 3799 3798 3800 3804                                                      
CONECT 3800 3799 3801 3805                                                      
CONECT 3801 3800 3802 3806                                                      
CONECT 3802 3801 3807 3808                                                      
CONECT 3803 3798                                                                
CONECT 3804 3799                                                                
CONECT 3805 3800 3809                                                           
CONECT 3806 3797 3801                                                           
CONECT 3807 3802                                                                
CONECT 3808 3802                                                                
CONECT 3809 3805 3810 3817                                                      
CONECT 3810 3809 3811 3814                                                      
CONECT 3811 3810 3812 3815                                                      
CONECT 3812 3811 3813 3816                                                      
CONECT 3813 3812 3817                                                           
CONECT 3814 3810                                                                
CONECT 3815 3811                                                                
CONECT 3816 3812 3818                                                           
CONECT 3817 3809 3813                                                           
CONECT 3818 3816 3819 3826                                                      
CONECT 3819 3818 3820 3823                                                      
CONECT 3820 3819 3821 3824                                                      
CONECT 3821 3820 3822 3825                                                      
CONECT 3822 3821 3826 3828                                                      
CONECT 3823 3819 3827                                                           
CONECT 3824 3820 3829                                                           
CONECT 3825 3821 3845                                                           
CONECT 3826 3818 3822                                                           
CONECT 3827 3823                                                                
CONECT 3828 3822                                                                
CONECT 3829 3824 3830 3838                                                      
CONECT 3830 3829 3831 3835                                                      
CONECT 3831 3830 3832 3836                                                      
CONECT 3832 3831 3833 3837                                                      
CONECT 3833 3832 3834 3838                                                      
CONECT 3834 3833 3839                                                           
CONECT 3835 3830                                                                
CONECT 3836 3831                                                                
CONECT 3837 3832                                                                
CONECT 3838 3829 3833                                                           
CONECT 3839 3834                                                                
CONECT 3840 3841 3845 3846                                                      
CONECT 3841 3840 3842 3847                                                      
CONECT 3842 3841 3843 3848                                                      
CONECT 3843 3842 3844 3849                                                      
CONECT 3844 3843 3850                                                           
CONECT 3845 3825 3840 3849                                                      
CONECT 3846 3840                                                                
CONECT 3847 3841                                                                
CONECT 3848 3842                                                                
CONECT 3849 3843 3845                                                           
CONECT 3850 3844                                                                
CONECT 3851 3794 3852 3860                                                      
CONECT 3852 3851 3853 3857                                                      
CONECT 3853 3852 3854 3858                                                      
CONECT 3854 3853 3855 3859                                                      
CONECT 3855 3854 3856 3860                                                      
CONECT 3856 3855                                                                
CONECT 3857 3852                                                                
CONECT 3858 3853                                                                
CONECT 3859 3854                                                                
CONECT 3860 3851 3855                                                           
CONECT 3861 3862 3869 3873                                                      
CONECT 3862 3861 3863 3870                                                      
CONECT 3863 3862 3864 3871                                                      
CONECT 3864 3863 3865 3872                                                      
CONECT 3865 3864 3866 3873                                                      
CONECT 3866 3865 3874                                                           
CONECT 3867 3868 3870 3875                                                      
CONECT 3868 3867                                                                
CONECT 3869 3861                                                                
CONECT 3870 3862 3867                                                           
CONECT 3871 3863 3880                                                           
CONECT 3872 3864 3879                                                           
CONECT 3873 3861 3865                                                           
CONECT 3874 3866                                                                
CONECT 3875 3867                                                                
CONECT 3876 3879                                                                
CONECT 3877 3879                                                                
CONECT 3878 3879                                                                
CONECT 3879 3872 3876 3877 3878                                                 
CONECT 3880 3871 3881 3889                                                      
CONECT 3881 3880 3882 3886                                                      
CONECT 3882 3881 3883 3887                                                      
CONECT 3883 3882 3884 3888                                                      
CONECT 3884 3883 3885 3889                                                      
CONECT 3885 3884 3890 3891                                                      
CONECT 3886 3881                                                                
CONECT 3887 3882                                                                
CONECT 3888 3883 3892                                                           
CONECT 3889 3880 3884                                                           
CONECT 3890 3885                                                                
CONECT 3891 3885                                                                
CONECT 3892 3888 3893 3903                                                      
CONECT 3893 3892 3894 3900                                                      
CONECT 3894 3893 3895 3901                                                      
CONECT 3895 3894 3896 3902                                                      
CONECT 3896 3895 3897 3903                                                      
CONECT 3897 3896 3904                                                           
CONECT 3898 3899 3900 3905                                                      
CONECT 3899 3898                                                                
CONECT 3900 3893 3898                                                           
CONECT 3901 3894 3910                                                           
CONECT 3902 3895 3909                                                           
CONECT 3903 3892 3896                                                           
CONECT 3904 3897                                                                
CONECT 3905 3898                                                                
CONECT 3906 3909                                                                
CONECT 3907 3909                                                                
CONECT 3908 3909                                                                
CONECT 3909 3902 3906 3907 3908                                                 
CONECT 3910 3901 3911 3918                                                      
CONECT 3911 3910 3912 3916                                                      
CONECT 3912 3911 3913 3917                                                      
CONECT 3913 3912 3914                                                           
CONECT 3914 3913 3915 3918                                                      
CONECT 3915 3914 3919 3920                                                      
CONECT 3916 3911                                                                
CONECT 3917 3912                                                                
CONECT 3918 3910 3914                                                           
CONECT 3919 3915                                                                
CONECT 3920 3915                                                                
MASTER      297    0   12    6   39    0    0    6 4725    1  145   37          
END                                                                             
