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HEADER    METAL BINDING PROTEIN                   12-JUN-09   3HTN              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE DNA BINDING PROTEIN (BT_1116) FROM    
TITLE    2 BACTEROIDES THETAIOTAOMICRON VPI-5482 AT 1.50 A RESOLUTION           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE DNA BINDING PROTEIN;                              
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: RESIDUES 38-185;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON VPI-5482;          
SOURCE   3 ORGANISM_TAXID: 226186;                                              
SOURCE   4 GENE: BT_1116, NP_810029.1;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: HK100;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    DUF269 FAMILY PROTEIN, STRUCTURAL GENOMICS, JOINT CENTER FOR          
KEYWDS   2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2,      
KEYWDS   3 METAL BINDING PROTEIN                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   6   24-JUL-19 3HTN    1       REMARK LINK                              
REVDAT   5   25-OCT-17 3HTN    1       REMARK                                   
REVDAT   4   13-JUL-11 3HTN    1       VERSN                                    
REVDAT   3   23-MAR-11 3HTN    1       HEADER TITLE  KEYWDS                     
REVDAT   2   24-NOV-09 3HTN    1       JRNL   TITLE  SOURCE                     
REVDAT   1   30-JUN-09 3HTN    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF PUTATIVE DNA BINDING PROTEIN            
JRNL        TITL 2 (NP_810029.1) FROM BACTEROIDES THETAIOTAOMICRON VPI-5482 AT  
JRNL        TITL 3 1.50 A RESOLUTION                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 79234                          
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 + TEST SET) : 0.145                           
REMARK   3   R VALUE            (WORKING SET) : 0.143                           
REMARK   3   FREE R VALUE                     : 0.167                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3974                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5515                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 309                          
REMARK   3   BIN FREE R VALUE                    : 0.2350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3342                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 553                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 16.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.04000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.059         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.061         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.266         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.977                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.969                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3811 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2544 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5176 ; 1.584 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6236 ; 1.134 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   493 ; 5.308 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   177 ;40.897 ;24.463       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   659 ; 9.688 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;13.132 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   554 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4383 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   789 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   643 ; 0.200 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2827 ; 0.177 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1869 ; 0.175 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2230 ; 0.088 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   867 ; 0.170 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.153 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    11 ; 0.211 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    61 ; 0.240 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    55 ; 0.164 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2491 ; 1.702 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   951 ; 0.418 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3766 ; 2.354 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1618 ; 3.678 ; 7.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1410 ; 5.051 ; 9.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    43        A   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8005  29.9020   1.0218              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0142 T22:  -0.0051                                     
REMARK   3      T33:  -0.0228 T12:   0.0464                                     
REMARK   3      T13:   0.0115 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6651 L22:   0.4066                                     
REMARK   3      L33:   0.6363 L12:  -0.1160                                     
REMARK   3      L13:   0.3944 L23:  -0.3913                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0630 S12:   0.1431 S13:  -0.0207                       
REMARK   3      S21:  -0.0942 S22:  -0.1062 S23:  -0.1167                       
REMARK   3      S31:   0.1455 S32:   0.1821 S33:   0.0432                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    43        B   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9268  22.2079  21.8894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0255 T22:  -0.0366                                     
REMARK   3      T33:  -0.0177 T12:   0.0116                                     
REMARK   3      T13:  -0.0189 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9358 L22:   0.6127                                     
REMARK   3      L33:   0.2298 L12:  -0.5208                                     
REMARK   3      L13:   0.0602 L23:  -0.2007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0109 S12:  -0.0879 S13:  -0.0706                       
REMARK   3      S21:   0.0992 S22:  -0.0283 S23:  -0.0347                       
REMARK   3      S31:   0.0671 S32:   0.0257 S33:   0.0174                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    43        C   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7822  26.9582   9.4922              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0029 T22:  -0.0314                                     
REMARK   3      T33:  -0.0072 T12:  -0.0204                                     
REMARK   3      T13:  -0.0064 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3396 L22:   0.5234                                     
REMARK   3      L33:   0.4251 L12:  -0.0970                                     
REMARK   3      L13:  -0.0165 L23:  -0.4114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:   0.0351 S13:  -0.0545                       
REMARK   3      S21:  -0.0567 S22:  -0.0024 S23:   0.1057                       
REMARK   3      S31:   0.0601 S32:  -0.0813 S33:  -0.0289                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1.HYDROGENS HAVE BEEN ADDED IN THE        
REMARK   3  RIDING POSITIONS. 2.ATOM RECORD CONTAINS RESIDUAL B FACTORS         
REMARK   3  ONLY. 3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE     
REMARK   3  INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE    
REMARK   3  ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 TO ACCOUNT FOR THE    
REMARK   3  REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION.        
REMARK   3  4.SULPHATE ANIONS AND PEG MOLECULES FROM CRYSTALLIZATION ARE        
REMARK   3  MODELED IN THE STRUCTURE, RESPECTIVELY. 5.NI AND FE METAL IONS      
REMARK   3  FROM PROTEIN EXPRESSION AND PURIFICATION ARE MODELED IN THE         
REMARK   3  STRUCTURE. THE PRESENCE OF NI AND FE ARE SUPPORTED BY X-RAY         
REMARK   3  FLUORESCENCE, BINDING GEOMETRY AND ANOMALOUS DIFFERENCE FOURIERS    
REMARK   3  ABOVE AND BELOW THE NI AND FE ABSORPTION EDGE, RESPECTIVELY.        
REMARK   4                                                                      
REMARK   4 3HTN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053568.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91837,0.97908,0.97840            
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   MONOCHROMATOR (HORIZONTAL          
REMARK 200                                   FOCUSING)                          
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL FOCUSING)    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79258                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.683                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 3.770                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELX, SHELXD, AUTOSHARP                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 34.0000% POLYETHYLENE GLYCOL 400,        
REMARK 280  0.2000M LITHIUM SULFATE, 0.1M TRIS PH 8.0, NANODROP, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.92533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       17.96267            
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 300 REMARK: THE RESULTS FROM SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS      
REMARK 300 THE ASSIGNMENT OF A TRIMER AS A SIGNIFICANT OLIGOMERIZATION          
REMARK 300 STATE.                                                               
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11030 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 16900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -200.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     ASN A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     LYS A    42                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     GLN B    39                                                      
REMARK 465     ASN B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     LYS B    42                                                      
REMARK 465     THR B   100                                                      
REMARK 465     LYS B   101                                                      
REMARK 465     ALA B   102                                                      
REMARK 465     TYR B   103                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     ALA C    38                                                      
REMARK 465     GLN C    39                                                      
REMARK 465     ASN C    40                                                      
REMARK 465     GLU C    41                                                      
REMARK 465     LYS C    42                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  99    CD   CE   NZ                                        
REMARK 470     ASN A 125    CG   OD1  ND2                                       
REMARK 470     GLU A 126    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 127    CD   OE1  NE2                                       
REMARK 470     LYS B  99    CG   CD   CE   NZ                                   
REMARK 470     ASP B 104    CG   OD1  OD2                                       
REMARK 470     LYS C  75    NZ                                                  
REMARK 470     LYS C  99    CG   CD   CE   NZ                                   
REMARK 470     GLU C 184    OE1  OE2                                            
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   OH   TYR B    45     OE2  GLU B    74              2.11            
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    TYR B 141       -2.73     72.61                                   
REMARK 500    TYR C 141       -0.87     71.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1PE A  206                                                       
REMARK 610     1PE B  212                                                       
REMARK 610     1PE C  216                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 201  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 131   NE2                                                    
REMARK 620 2 HIS A 133   NE2  93.9                                              
REMARK 620 3 HIS A 147   ND1 108.7  97.7                                        
REMARK 620 4 HOH A 410   O   102.8 161.7  84.2                                  
REMARK 620 5 HOH A 410   O   152.2 102.7  91.3  59.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 207  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 131   NE2                                                    
REMARK 620 2 HIS B 133   NE2  97.2                                              
REMARK 620 3 HIS B 147   ND1 106.0  97.8                                        
REMARK 620 4 HOH B 528   O    86.2 172.8  87.4                                  
REMARK 620 5 HOH B 519   O   155.4 103.9  83.8  71.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 212                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 213                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 214                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE C 215                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE C 216                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 393032   RELATED DB: TARGETDB                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG                  
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING   
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. THE CLONED       
REMARK 999 CONSTRUCT CONTAINS RESIDUES 38-185 OF THE FULL LENGTH PROTEIN.       
DBREF  3HTN A   38   185  UNP    Q8A8Q1   Q8A8Q1_BACTN    38    185             
DBREF  3HTN B   38   185  UNP    Q8A8Q1   Q8A8Q1_BACTN    38    185             
DBREF  3HTN C   38   185  UNP    Q8A8Q1   Q8A8Q1_BACTN    38    185             
SEQADV 3HTN GLY A    0  UNP  Q8A8Q1              LEADER SEQUENCE                
SEQADV 3HTN GLY B    0  UNP  Q8A8Q1              LEADER SEQUENCE                
SEQADV 3HTN GLY C    0  UNP  Q8A8Q1              LEADER SEQUENCE                
SEQRES   1 A  149  GLY ALA GLN ASN GLU LYS ASN MSE TYR SER TYR LYS LYS          
SEQRES   2 A  149  ILE GLY ASN LYS TYR ILE VAL SER ILE ASN ASN HIS THR          
SEQRES   3 A  149  GLU ILE VAL LYS ALA LEU ASN ALA PHE CYS LYS GLU LYS          
SEQRES   4 A  149  GLY ILE LEU SER GLY SER ILE ASN GLY ILE GLY ALA ILE          
SEQRES   5 A  149  GLY GLU LEU THR LEU ARG PHE PHE ASN PRO LYS THR LYS          
SEQRES   6 A  149  ALA TYR ASP ASP LYS THR PHE ARG GLU GLN MSE GLU ILE          
SEQRES   7 A  149  SER ASN LEU THR GLY ASN ILE SER SER MSE ASN GLU GLN          
SEQRES   8 A  149  VAL TYR LEU HIS LEU HIS ILE THR VAL GLY ARG SER ASP          
SEQRES   9 A  149  TYR SER ALA LEU ALA GLY HIS LEU LEU SER ALA ILE GLN          
SEQRES  10 A  149  ASN GLY ALA GLY GLU PHE VAL VAL GLU ASP TYR SER GLU          
SEQRES  11 A  149  ARG ILE SER ARG THR TYR ASN PRO ASP LEU GLY LEU ASN          
SEQRES  12 A  149  ILE TYR ASP PHE GLU ARG                                      
SEQRES   1 B  149  GLY ALA GLN ASN GLU LYS ASN MSE TYR SER TYR LYS LYS          
SEQRES   2 B  149  ILE GLY ASN LYS TYR ILE VAL SER ILE ASN ASN HIS THR          
SEQRES   3 B  149  GLU ILE VAL LYS ALA LEU ASN ALA PHE CYS LYS GLU LYS          
SEQRES   4 B  149  GLY ILE LEU SER GLY SER ILE ASN GLY ILE GLY ALA ILE          
SEQRES   5 B  149  GLY GLU LEU THR LEU ARG PHE PHE ASN PRO LYS THR LYS          
SEQRES   6 B  149  ALA TYR ASP ASP LYS THR PHE ARG GLU GLN MSE GLU ILE          
SEQRES   7 B  149  SER ASN LEU THR GLY ASN ILE SER SER MSE ASN GLU GLN          
SEQRES   8 B  149  VAL TYR LEU HIS LEU HIS ILE THR VAL GLY ARG SER ASP          
SEQRES   9 B  149  TYR SER ALA LEU ALA GLY HIS LEU LEU SER ALA ILE GLN          
SEQRES  10 B  149  ASN GLY ALA GLY GLU PHE VAL VAL GLU ASP TYR SER GLU          
SEQRES  11 B  149  ARG ILE SER ARG THR TYR ASN PRO ASP LEU GLY LEU ASN          
SEQRES  12 B  149  ILE TYR ASP PHE GLU ARG                                      
SEQRES   1 C  149  GLY ALA GLN ASN GLU LYS ASN MSE TYR SER TYR LYS LYS          
SEQRES   2 C  149  ILE GLY ASN LYS TYR ILE VAL SER ILE ASN ASN HIS THR          
SEQRES   3 C  149  GLU ILE VAL LYS ALA LEU ASN ALA PHE CYS LYS GLU LYS          
SEQRES   4 C  149  GLY ILE LEU SER GLY SER ILE ASN GLY ILE GLY ALA ILE          
SEQRES   5 C  149  GLY GLU LEU THR LEU ARG PHE PHE ASN PRO LYS THR LYS          
SEQRES   6 C  149  ALA TYR ASP ASP LYS THR PHE ARG GLU GLN MSE GLU ILE          
SEQRES   7 C  149  SER ASN LEU THR GLY ASN ILE SER SER MSE ASN GLU GLN          
SEQRES   8 C  149  VAL TYR LEU HIS LEU HIS ILE THR VAL GLY ARG SER ASP          
SEQRES   9 C  149  TYR SER ALA LEU ALA GLY HIS LEU LEU SER ALA ILE GLN          
SEQRES  10 C  149  ASN GLY ALA GLY GLU PHE VAL VAL GLU ASP TYR SER GLU          
SEQRES  11 C  149  ARG ILE SER ARG THR TYR ASN PRO ASP LEU GLY LEU ASN          
SEQRES  12 C  149  ILE TYR ASP PHE GLU ARG                                      
MODRES 3HTN MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE A  112  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE A  124  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE B   44  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE B  112  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE B  124  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE C   44  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE C  112  MET  SELENOMETHIONINE                                   
MODRES 3HTN MSE C  124  MET  SELENOMETHIONINE                                   
HET    MSE  A  44      16                                                       
HET    MSE  A 112       8                                                       
HET    MSE  A 124       8                                                       
HET    MSE  B  44      16                                                       
HET    MSE  B 112       8                                                       
HET    MSE  B 124       8                                                       
HET    MSE  C  44      16                                                       
HET    MSE  C 112       8                                                       
HET    MSE  C 124       8                                                       
HET     NI  A 201       1                                                       
HET    SO4  A 202       5                                                       
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HET    1PE  A 205      16                                                       
HET    1PE  A 206       7                                                       
HET     FE  B 207       1                                                       
HET     NI  B 208       1                                                       
HET    SO4  B 209       5                                                       
HET    SO4  B 210       5                                                       
HET    SO4  B 211       5                                                       
HET    1PE  B 212       7                                                       
HET    SO4  C 213       5                                                       
HET    SO4  C 214       5                                                       
HET    1PE  C 215      16                                                       
HET    1PE  C 216       7                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM      FE FE (III) ION                                                     
HETSYN     1PE PEG400                                                           
FORMUL   1  MSE    9(C5 H11 N O2 SE)                                            
FORMUL   4   NI    2(NI 2+)                                                     
FORMUL   5  SO4    8(O4 S 2-)                                                   
FORMUL   8  1PE    5(C10 H22 O6)                                                
FORMUL  10   FE    FE 3+                                                        
FORMUL  20  HOH   *553(H2 O)                                                    
HELIX    1   1 GLU A   63  GLY A   76  1                                  14    
HELIX    2   2 GLU B   63  LYS B   75  1                                  13    
HELIX    3   3 GLU C   63  GLY C   76  1                                  14    
SHEET    1   A 5 TYR A  45  ILE A  50  0                                        
SHEET    2   A 5 LYS A  53  ILE A  58 -1  O  SER A  57   N  SER A  46           
SHEET    3   A 5 ALA A 143  ASP A 163 -1  O  PHE A 159   N  VAL A  56           
SHEET    4   A 5 GLY A  80  PHE A  96 -1  N  ASN A  83   O  VAL A 160           
SHEET    5   A 5 TYR A 103  PHE A 108 -1  O  PHE A 108   N  LEU A  91           
SHEET    1   B 7 TYR A  45  ILE A  50  0                                        
SHEET    2   B 7 LYS A  53  ILE A  58 -1  O  SER A  57   N  SER A  46           
SHEET    3   B 7 ALA A 143  ASP A 163 -1  O  PHE A 159   N  VAL A  56           
SHEET    4   B 7 GLN A 127  GLY A 137 -1  N  VAL A 136   O  LEU A 144           
SHEET    5   B 7 MSE A 112  MSE A 124 -1  N  THR A 118   O  HIS A 133           
SHEET    6   B 7 GLY A  80  PHE A  96 -1  N  GLY A  86   O  ILE A 114           
SHEET    7   B 7 TYR A 103  PHE A 108 -1  O  PHE A 108   N  LEU A  91           
SHEET    1   C 2 SER A 169  ASN A 173  0                                        
SHEET    2   C 2 LEU A 178  ASP A 182 -1  O  LEU A 178   N  ASN A 173           
SHEET    1   D 5 TYR B  45  ILE B  50  0                                        
SHEET    2   D 5 LYS B  53  ILE B  58 -1  O  SER B  57   N  SER B  46           
SHEET    3   D 5 ALA B 143  ASP B 163 -1  O  PHE B 159   N  VAL B  56           
SHEET    4   D 5 GLY B  80  ARG B  94 -1  N  ASN B  83   O  VAL B 160           
SHEET    5   D 5 ASP B 105  PHE B 108 -1  O  PHE B 108   N  LEU B  91           
SHEET    1   E 7 TYR B  45  ILE B  50  0                                        
SHEET    2   E 7 LYS B  53  ILE B  58 -1  O  SER B  57   N  SER B  46           
SHEET    3   E 7 ALA B 143  ASP B 163 -1  O  PHE B 159   N  VAL B  56           
SHEET    4   E 7 GLN B 127  GLY B 137 -1  N  LEU B 132   O  LEU B 148           
SHEET    5   E 7 MSE B 112  MSE B 124 -1  N  THR B 118   O  HIS B 133           
SHEET    6   E 7 GLY B  80  ARG B  94 -1  N  GLY B  86   O  ILE B 114           
SHEET    7   E 7 ASP B 105  PHE B 108 -1  O  PHE B 108   N  LEU B  91           
SHEET    1   F 2 SER B 169  ASN B 173  0                                        
SHEET    2   F 2 LEU B 178  ASP B 182 -1  O  LEU B 178   N  ASN B 173           
SHEET    1   G 5 TYR C  45  ILE C  50  0                                        
SHEET    2   G 5 LYS C  53  ILE C  58 -1  O  LYS C  53   N  ILE C  50           
SHEET    3   G 5 ALA C 143  ASP C 163 -1  O  PHE C 159   N  VAL C  56           
SHEET    4   G 5 GLY C  80  PHE C  96 -1  N  THR C  92   O  SER C 150           
SHEET    5   G 5 TYR C 103  PHE C 108 -1  O  PHE C 108   N  LEU C  91           
SHEET    1   H 7 TYR C  45  ILE C  50  0                                        
SHEET    2   H 7 LYS C  53  ILE C  58 -1  O  LYS C  53   N  ILE C  50           
SHEET    3   H 7 ALA C 143  ASP C 163 -1  O  PHE C 159   N  VAL C  56           
SHEET    4   H 7 GLN C 127  GLY C 137 -1  N  VAL C 136   O  LEU C 144           
SHEET    5   H 7 MSE C 112  MSE C 124 -1  N  THR C 118   O  HIS C 133           
SHEET    6   H 7 GLY C  80  PHE C  96 -1  N  GLY C  86   O  ILE C 114           
SHEET    7   H 7 TYR C 103  PHE C 108 -1  O  PHE C 108   N  LEU C  91           
SHEET    1   I 2 SER C 169  ASN C 173  0                                        
SHEET    2   I 2 LEU C 178  ASP C 182 -1  O  LEU C 178   N  ASN C 173           
LINK         C   ASN A  43                 N  AMSE A  44     1555   1555  1.33  
LINK         C   ASN A  43                 N  BMSE A  44     1555   1555  1.33  
LINK         C  AMSE A  44                 N   TYR A  45     1555   1555  1.33  
LINK         C  BMSE A  44                 N   TYR A  45     1555   1555  1.33  
LINK         C   GLN A 111                 N   MSE A 112     1555   1555  1.32  
LINK         C   MSE A 112                 N   GLU A 113     1555   1555  1.33  
LINK         C   SER A 123                 N   MSE A 124     1555   1555  1.33  
LINK         C   MSE A 124                 N   ASN A 125     1555   1555  1.33  
LINK         C   ASN B  43                 N  AMSE B  44     1555   1555  1.33  
LINK         C   ASN B  43                 N  BMSE B  44     1555   1555  1.33  
LINK         C  AMSE B  44                 N   TYR B  45     1555   1555  1.33  
LINK         C  BMSE B  44                 N   TYR B  45     1555   1555  1.33  
LINK         C   GLN B 111                 N   MSE B 112     1555   1555  1.33  
LINK         C   MSE B 112                 N   GLU B 113     1555   1555  1.32  
LINK         C   SER B 123                 N   MSE B 124     1555   1555  1.32  
LINK         C   MSE B 124                 N   ASN B 125     1555   1555  1.34  
LINK         C   ASN C  43                 N  AMSE C  44     1555   1555  1.33  
LINK         C   ASN C  43                 N  BMSE C  44     1555   1555  1.33  
LINK         C  AMSE C  44                 N   TYR C  45     1555   1555  1.33  
LINK         C  BMSE C  44                 N   TYR C  45     1555   1555  1.33  
LINK         C   GLN C 111                 N   MSE C 112     1555   1555  1.33  
LINK         C   MSE C 112                 N   GLU C 113     1555   1555  1.32  
LINK         C   SER C 123                 N   MSE C 124     1555   1555  1.32  
LINK         C   MSE C 124                 N   ASN C 125     1555   1555  1.33  
LINK         NE2 HIS A 131                NI    NI A 201     1555   1555  2.18  
LINK         NE2 HIS A 133                NI    NI A 201     1555   1555  2.26  
LINK         ND1BHIS A 147                NI    NI A 201     1555   1555  2.23  
LINK         NE2 HIS B  61                NI    NI B 208     1555   1555  2.18  
LINK         NE2 HIS B 131                FE    FE B 207     1555   1555  2.10  
LINK         NE2 HIS B 133                FE    FE B 207     1555   1555  2.19  
LINK         ND1AHIS B 147                FE    FE B 207     1555   1555  2.36  
LINK        NI    NI A 201                 O  AHOH A 410     1555   1555  1.71  
LINK        NI    NI A 201                 O  BHOH A 410     1555   1555  1.83  
LINK        FE    FE B 207                 O   HOH B 528     1555   1555  2.06  
LINK        FE    FE B 207                 O   HOH B 519     1555   1555  1.87  
SITE     1 AC1  5 HIS A 131  HIS A 133  HIS A 147  HOH A 410                    
SITE     2 AC1  5 HOH C 619                                                     
SITE     1 AC2 11 LYS A 106  PHE A 108  ARG A 138  HOH A 294                    
SITE     2 AC2 11 HOH A 304  HOH A 398  HOH B 524  ASN C  97                    
SITE     3 AC2 11 THR C 100  ALA C 102  HOH C 737                               
SITE     1 AC3  7 ASN A  52  LYS A  53  GLU A 162  ASN B  52                    
SITE     2 AC3  7 LYS B  53  ASN C  52  LYS C  53                               
SITE     1 AC4  8 SER A 123  MSE A 124  ASN A 125  GLU A 126                    
SITE     2 AC4  8 ARG A 167  SER A 169  HOH A 271  HOH A 335                    
SITE     1 AC5  5 ARG A  94  TYR A 103  TYR A 129  HIS A 147                    
SITE     2 AC5  5 HOH A 287                                                     
SITE     1 AC6  4 ASN A  60  HIS A  61  HOH A 352  LEU B 176                    
SITE     1 AC7  6 HOH A 269  HIS B 131  HIS B 133  HIS B 147                    
SITE     2 AC7  6 HOH B 519  HOH B 528                                          
SITE     1 AC8  2 HIS B  61  HOH B 500                                          
SITE     1 AC9  6 LYS B 106  PHE B 108  ARG B 138  1PE B 212                    
SITE     2 AC9  6 HOH B 531  HOH B 567                                          
SITE     1 BC1  7 ASN B 125  ARG B 167  SER B 169  ARG B 185                    
SITE     2 BC1  7 HOH B 473  HOH B 494  HOH B 571                               
SITE     1 BC2  4 LYS B  49  TYR B  54  LYS B  75  HOH B 573                    
SITE     1 BC3  6 GLU B 110  ARG B 138  SER B 139  ASP B 140                    
SITE     2 BC3  6 SO4 B 209  HOH B 584                                          
SITE     1 BC4  7 MSE C 124  ASN C 125  ARG C 167  SER C 169                    
SITE     2 BC4  7 ARG C 185  HOH C 622  HOH C 673                               
SITE     1 BC5 11 ASN A  97  THR A 100  ALA A 102  HOH A 353                    
SITE     2 BC5 11 LYS C 106  ARG C 138  HOH C 655  HOH C 671                    
SITE     3 BC5 11 HOH C 697  HOH C 743  HOH C 758                               
SITE     1 BC6  6 ARG A 109  ARG C  94  PHE C  96  TYR C 103                    
SITE     2 BC6  6 TYR C 129  HIS C 147                                          
SITE     1 BC7  5 TYR C  47  LYS C  49  TYR C  54  LYS C  75                    
SITE     2 BC7  5 HOH C 677                                                     
CRYST1   90.688   90.688   53.888  90.00  90.00 120.00 P 32          9          
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      0.011027  0.006366  0.000000        0.00000                         
SCALE2      0.000000  0.012733  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018557        0.00000                         
ATOM      1  N   ASN A  43      33.214  24.542   0.024  1.00 42.24           N  
ATOM      2  CA  ASN A  43      32.335  23.730   0.916  1.00 39.35           C  
ATOM      3  C   ASN A  43      31.423  24.664   1.708  1.00 33.60           C  
ATOM      4  O   ASN A  43      31.909  25.592   2.367  1.00 37.53           O  
ATOM      5  CB  ASN A  43      33.151  22.863   1.871  1.00 42.41           C  
ATOM      6  CG  ASN A  43      32.305  21.780   2.551  1.00 46.71           C  
ATOM      7  OD1 ASN A  43      31.613  21.008   1.879  1.00 55.82           O  
ATOM      8  ND2 ASN A  43      32.373  21.710   3.885  1.00 53.84           N  
HETATM    9  N  AMSE A  44      30.113  24.433   1.633  0.50 27.70           N  
HETATM   10  N  BMSE A  44      30.116  24.415   1.631  0.50 27.82           N  
HETATM   11  CA AMSE A  44      29.138  25.284   2.317  0.50 22.82           C  
HETATM   12  CA BMSE A  44      29.112  25.269   2.259  0.50 23.09           C  
HETATM   13  C  AMSE A  44      28.268  24.581   3.360  0.50 20.80           C  
HETATM   14  C  BMSE A  44      28.268  24.581   3.340  0.50 20.92           C  
HETATM   15  O  AMSE A  44      27.575  25.251   4.118  0.50 18.80           O  
HETATM   16  O  BMSE A  44      27.590  25.264   4.100  0.50 18.86           O  
HETATM   17  CB AMSE A  44      28.260  25.969   1.270  0.50 23.14           C  
HETATM   18  CB BMSE A  44      28.200  25.826   1.164  0.50 23.05           C  
HETATM   19  CG AMSE A  44      28.983  27.087   0.547  0.50 21.03           C  
HETATM   20  CG BMSE A  44      28.955  26.568   0.065  0.50 21.47           C  
HETATM   21 SE  AMSE A  44      27.806  28.022  -0.640  0.38 19.08          SE  
HETATM   22 SE  BMSE A  44      27.777  27.306  -1.240  0.37 20.86          SE  
HETATM   23  CE AMSE A  44      27.692  26.660  -2.041  0.50 26.50           C  
HETATM   24  CE BMSE A  44      27.000  28.730  -0.109  0.50 30.68           C  
ATOM     25  N   TYR A  45      28.310  23.252   3.427  1.00 18.51           N  
ATOM     26  CA  TYR A  45      27.440  22.526   4.340  1.00 19.49           C  
ATOM     27  C   TYR A  45      27.897  21.095   4.516  1.00 18.48           C  
ATOM     28  O   TYR A  45      28.710  20.582   3.728  1.00 18.04           O  
ATOM     29  CB  TYR A  45      25.997  22.502   3.778  1.00 18.51           C  
ATOM     30  CG  TYR A  45      25.935  22.050   2.347  1.00 16.97           C  
ATOM     31  CD1 TYR A  45      26.057  20.697   2.002  1.00 17.25           C  
ATOM     32  CD2 TYR A  45      25.819  22.981   1.315  1.00 17.98           C  
ATOM     33  CE1 TYR A  45      26.070  20.301   0.674  1.00 21.58           C  
ATOM     34  CE2 TYR A  45      25.820  22.588  -0.014  1.00 20.44           C  
ATOM     35  CZ  TYR A  45      25.931  21.252  -0.324  1.00 17.76           C  
ATOM     36  OH  TYR A  45      25.935  20.880  -1.651  1.00 24.06           O  
ATOM     37  N  ASER A  46      27.385  20.463   5.570  0.50 18.60           N  
ATOM     38  N  BSER A  46      27.358  20.483   5.569  0.50 18.55           N  
ATOM     39  CA ASER A  46      27.505  19.024   5.792  0.50 17.90           C  
ATOM     40  CA BSER A  46      27.456  19.062   5.854  0.50 18.06           C  
ATOM     41  C  ASER A  46      26.072  18.535   5.975  0.50 17.41           C  
ATOM     42  C  BSER A  46      26.019  18.571   5.828  0.50 17.46           C  
ATOM     43  O  ASER A  46      25.198  19.297   6.413  0.50 16.06           O  
ATOM     44  O  BSER A  46      25.076  19.372   5.948  0.50 17.34           O  
ATOM     45  CB ASER A  46      28.375  18.700   7.005  0.50 19.77           C  
ATOM     46  CB BSER A  46      28.062  18.824   7.230  0.50 18.72           C  
ATOM     47  OG ASER A  46      27.838  19.229   8.201  0.50 20.70           O  
ATOM     48  OG BSER A  46      29.320  19.462   7.336  0.50 24.48           O  
ATOM     49  N   TYR A  47      25.823  17.270   5.660  1.00 18.46           N  
ATOM     50  CA  TYR A  47      24.475  16.734   5.692  1.00 16.87           C  
ATOM     51  C   TYR A  47      24.415  15.260   6.067  1.00 16.83           C  
ATOM     52  O   TYR A  47      25.424  14.564   6.031  1.00 17.56           O  
ATOM     53  CB  TYR A  47      23.791  16.948   4.341  1.00 19.13           C  
ATOM     54  CG  TYR A  47      24.418  16.139   3.256  1.00 21.43           C  
ATOM     55  CD1 TYR A  47      25.497  16.637   2.543  1.00 18.71           C  
ATOM     56  CD2 TYR A  47      23.936  14.877   2.937  1.00 20.25           C  
ATOM     57  CE1 TYR A  47      26.097  15.900   1.555  1.00 24.58           C  
ATOM     58  CE2 TYR A  47      24.535  14.122   1.944  1.00 26.07           C  
ATOM     59  CZ  TYR A  47      25.617  14.648   1.260  1.00 24.83           C  
ATOM     60  OH  TYR A  47      26.214  13.926   0.263  1.00 30.28           O  
ATOM     61  N   LYS A  48      23.210  14.816   6.423  1.00 17.09           N  
ATOM     62  CA  LYS A  48      22.918  13.417   6.670  1.00 16.23           C  
ATOM     63  C   LYS A  48      21.617  13.049   5.979  1.00 16.18           C  
ATOM     64  O   LYS A  48      20.601  13.673   6.206  1.00 19.56           O  
ATOM     65  CB  LYS A  48      22.805  13.136   8.170  1.00 16.94           C  
ATOM     66  CG  LYS A  48      22.543  11.687   8.525  1.00 20.50           C  
ATOM     67  CD  LYS A  48      22.481  11.541  10.035  1.00 22.62           C  
ATOM     68  CE  LYS A  48      22.219  10.105  10.427  1.00 23.99           C  
ATOM     69  NZ  LYS A  48      23.297   9.193   9.941  1.00 26.77           N  
ATOM     70  N  ALYS A  49      21.653  12.016   5.150  0.70 15.80           N  
ATOM     71  N  BLYS A  49      21.669  12.024   5.136  0.30 16.72           N  
ATOM     72  CA ALYS A  49      20.454  11.548   4.479  0.70 18.42           C  
ATOM     73  CA BLYS A  49      20.479  11.506   4.484  0.30 17.94           C  
ATOM     74  C  ALYS A  49      19.695  10.584   5.364  0.70 19.38           C  
ATOM     75  C  BLYS A  49      19.714  10.639   5.464  0.30 19.01           C  
ATOM     76  O  ALYS A  49      20.271   9.605   5.852  0.70 18.93           O  
ATOM     77  O  BLYS A  49      20.312   9.831   6.177  0.30 19.37           O  
ATOM     78  CB ALYS A  49      20.808  10.841   3.174  0.70 18.49           C  
ATOM     79  CB BLYS A  49      20.850  10.672   3.255  0.30 17.94           C  
ATOM     80  CG ALYS A  49      19.608  10.501   2.311  0.70 19.27           C  
ATOM     81  CG BLYS A  49      19.662  10.027   2.547  0.30 18.86           C  
ATOM     82  CD ALYS A  49      20.071   9.935   0.970  0.70 22.07           C  
ATOM     83  CD BLYS A  49      20.083   9.417   1.226  0.30 18.41           C  
ATOM     84  CE ALYS A  49      18.890   9.574   0.078  0.70 23.75           C  
ATOM     85  CE BLYS A  49      18.913   8.731   0.544  0.30 20.22           C  
ATOM     86  NZ ALYS A  49      18.074   8.467   0.671  0.70 26.87           N  
ATOM     87  NZ BLYS A  49      19.171   8.509  -0.902  0.30 20.43           N  
ATOM     88  N   ILE A  50      18.400  10.831   5.533  1.00 19.26           N  
ATOM     89  CA  ILE A  50      17.526   9.953   6.328  1.00 22.23           C  
ATOM     90  C   ILE A  50      16.247   9.744   5.533  1.00 20.15           C  
ATOM     91  O   ILE A  50      15.350  10.574   5.571  1.00 20.71           O  
ATOM     92  CB  ILE A  50      17.169  10.499   7.708  1.00 21.93           C  
ATOM     93  CG1 ILE A  50      18.426  10.838   8.519  1.00 27.04           C  
ATOM     94  CG2 ILE A  50      16.346   9.418   8.455  1.00 25.49           C  
ATOM     95  CD1 ILE A  50      18.141  11.441   9.869  1.00 26.24           C  
ATOM     96  N   GLY A  51      16.191   8.640   4.801  1.00 21.29           N  
ATOM     97  CA  GLY A  51      15.052   8.347   3.962  1.00 22.14           C  
ATOM     98  C   GLY A  51      14.876   9.411   2.895  1.00 22.04           C  
ATOM     99  O   GLY A  51      15.823   9.718   2.176  1.00 22.56           O  
ATOM    100  N   ASN A  52      13.687  10.015   2.867  1.00 23.49           N  
ATOM    101  CA  ASN A  52      13.332  11.042   1.888  1.00 23.02           C  
ATOM    102  C   ASN A  52      13.752  12.455   2.315  1.00 22.14           C  
ATOM    103  O   ASN A  52      13.433  13.417   1.619  1.00 22.45           O  
ATOM    104  CB  ASN A  52      11.811  11.001   1.600  1.00 25.92           C  
ATOM    105  CG  ASN A  52      10.941  11.338   2.840  1.00 32.72           C  
ATOM    106  OD1 ASN A  52      11.393  11.253   3.982  1.00 42.51           O  
ATOM    107  ND2 ASN A  52       9.684  11.705   2.600  1.00 39.67           N  
ATOM    108  N   LYS A  53      14.463  12.566   3.440  1.00 19.48           N  
ATOM    109  CA  LYS A  53      14.902  13.838   3.966  1.00 19.68           C  
ATOM    110  C   LYS A  53      16.408  13.903   4.110  1.00 16.98           C  
ATOM    111  O   LYS A  53      17.103  12.881   4.122  1.00 17.82           O  
ATOM    112  CB  LYS A  53      14.263  14.063   5.336  1.00 20.76           C  
ATOM    113  CG  LYS A  53      12.763  14.221   5.241  1.00 25.68           C  
ATOM    114  CD  LYS A  53      12.129  14.523   6.573  1.00 27.87           C  
ATOM    115  CE  LYS A  53      10.626  14.333   6.495  1.00 35.31           C  
ATOM    116  NZ  LYS A  53      10.310  12.875   6.561  1.00 37.15           N  
ATOM    117  N   TYR A  54      16.893  15.129   4.225  1.00 16.74           N  
ATOM    118  CA  TYR A  54      18.272  15.405   4.524  1.00 16.09           C  
ATOM    119  C   TYR A  54      18.314  16.400   5.662  1.00 16.69           C  
ATOM    120  O   TYR A  54      17.581  17.368   5.661  1.00 16.98           O  
ATOM    121  CB  TYR A  54      18.998  16.018   3.342  1.00 18.15           C  
ATOM    122  CG  TYR A  54      19.057  15.178   2.101  1.00 19.02           C  
ATOM    123  CD1 TYR A  54      20.120  14.330   1.882  1.00 19.13           C  
ATOM    124  CD2 TYR A  54      18.077  15.280   1.108  1.00 19.60           C  
ATOM    125  CE1 TYR A  54      20.194  13.574   0.719  1.00 17.84           C  
ATOM    126  CE2 TYR A  54      18.151  14.538  -0.044  1.00 21.51           C  
ATOM    127  CZ  TYR A  54      19.207  13.692  -0.233  1.00 17.65           C  
ATOM    128  OH  TYR A  54      19.270  12.934  -1.384  1.00 20.42           O  
ATOM    129  N   ILE A  55      19.177  16.146   6.628  1.00 16.49           N  
ATOM    130  CA  ILE A  55      19.447  17.099   7.680  1.00 15.86           C  
ATOM    131  C   ILE A  55      20.670  17.847   7.193  1.00 16.35           C  
ATOM    132  O   ILE A  55      21.727  17.234   7.007  1.00 17.96           O  
ATOM    133  CB  ILE A  55      19.729  16.420   9.043  1.00 17.28           C  
ATOM    134  CG1 ILE A  55      18.589  15.463   9.409  1.00 21.88           C  
ATOM    135  CG2 ILE A  55      19.953  17.441  10.113  1.00 20.00           C  
ATOM    136  CD1 ILE A  55      17.197  15.970   9.174  1.00 26.59           C  
ATOM    137  N   VAL A  56      20.525  19.155   6.997  1.00 17.05           N  
ATOM    138  CA  VAL A  56      21.598  19.975   6.455  1.00 16.23           C  
ATOM    139  C   VAL A  56      22.087  20.945   7.509  1.00 16.33           C  
ATOM    140  O   VAL A  56      21.292  21.686   8.082  1.00 20.65           O  
ATOM    141  CB  VAL A  56      21.139  20.726   5.215  1.00 17.58           C  
ATOM    142  CG1 VAL A  56      22.270  21.558   4.620  1.00 21.21           C  
ATOM    143  CG2 VAL A  56      20.580  19.727   4.208  1.00 18.96           C  
ATOM    144  N   SER A  57      23.392  20.890   7.776  1.00 16.01           N  
ATOM    145  CA  SER A  57      24.069  21.788   8.683  1.00 16.63           C  
ATOM    146  C   SER A  57      24.929  22.726   7.864  1.00 17.46           C  
ATOM    147  O   SER A  57      25.945  22.326   7.315  1.00 17.12           O  
ATOM    148  CB  SER A  57      24.882  20.998   9.694  1.00 17.11           C  
ATOM    149  OG  SER A  57      25.491  21.875  10.601  1.00 18.02           O  
ATOM    150  N   ILE A  58      24.502  23.974   7.760  1.00 16.82           N  
ATOM    151  CA  ILE A  58      25.206  24.933   6.926  1.00 18.13           C  
ATOM    152  C   ILE A  58      26.442  25.413   7.686  1.00 17.09           C  
ATOM    153  O   ILE A  58      26.431  25.508   8.925  1.00 17.09           O  
ATOM    154  CB  ILE A  58      24.249  26.091   6.520  1.00 18.29           C  
ATOM    155  CG1 ILE A  58      23.070  25.528   5.693  1.00 20.28           C  
ATOM    156  CG2 ILE A  58      25.012  27.152   5.751  1.00 16.47           C  
ATOM    157  CD1 ILE A  58      22.145  26.525   5.117  1.00 23.06           C  
ATOM    158  N   ASN A  59      27.540  25.651   6.951  1.00 16.70           N  
ATOM    159  CA  ASN A  59      28.777  26.128   7.548  1.00 18.64           C  
ATOM    160  C   ASN A  59      28.579  27.517   8.116  1.00 16.54           C  
ATOM    161  O   ASN A  59      27.811  28.317   7.581  1.00 16.23           O  
ATOM    162  CB  ASN A  59      29.926  26.184   6.518  1.00 18.53           C  
ATOM    163  CG  ASN A  59      30.374  24.820   6.044  1.00 23.38           C  
ATOM    164  OD1 ASN A  59      29.910  23.799   6.521  1.00 22.75           O  
ATOM    165  ND2 ASN A  59      31.265  24.810   5.049  1.00 23.92           N  
ATOM    166  N   ASN A  60      29.302  27.840   9.171  1.00 15.84           N  
ATOM    167  CA  ASN A  60      29.205  29.155   9.743  1.00 16.08           C  
ATOM    168  C   ASN A  60      29.717  30.191   8.738  1.00 16.65           C  
ATOM    169  O   ASN A  60      30.517  29.882   7.831  1.00 18.07           O  
ATOM    170  CB  ASN A  60      30.026  29.229  11.020  1.00 17.22           C  
ATOM    171  CG  ASN A  60      29.593  30.350  11.938  1.00 18.18           C  
ATOM    172  OD1 ASN A  60      28.587  31.017  11.693  1.00 18.97           O  
ATOM    173  ND2 ASN A  60      30.366  30.576  13.007  1.00 17.44           N  
ATOM    174  N   HIS A  61      29.242  31.421   8.881  1.00 17.09           N  
ATOM    175  CA  HIS A  61      29.664  32.546   8.043  1.00 17.18           C  
ATOM    176  C   HIS A  61      29.355  32.363   6.565  1.00 18.35           C  
ATOM    177  O   HIS A  61      30.011  32.958   5.706  1.00 22.68           O  
ATOM    178  CB  HIS A  61      31.167  32.826   8.218  1.00 19.36           C  
ATOM    179  CG  HIS A  61      31.593  32.896   9.640  1.00 20.99           C  
ATOM    180  ND1 HIS A  61      31.030  33.776  10.534  1.00 24.01           N  
ATOM    181  CD2 HIS A  61      32.530  32.205  10.324  1.00 27.66           C  
ATOM    182  CE1 HIS A  61      31.610  33.633  11.710  1.00 27.45           C  
ATOM    183  NE2 HIS A  61      32.511  32.672  11.613  1.00 25.80           N  
ATOM    184  N   THR A  62      28.344  31.559   6.270  1.00 16.79           N  
ATOM    185  CA  THR A  62      27.961  31.228   4.919  1.00 16.51           C  
ATOM    186  C   THR A  62      26.578  31.783   4.647  1.00 16.22           C  
ATOM    187  O   THR A  62      25.744  31.810   5.558  1.00 15.50           O  
ATOM    188  CB  THR A  62      27.964  29.707   4.790  1.00 18.11           C  
ATOM    189  OG1 THR A  62      29.286  29.234   5.114  1.00 19.12           O  
ATOM    190  CG2 THR A  62      27.611  29.242   3.404  1.00 18.03           C  
ATOM    191  N   GLU A  63      26.339  32.234   3.417  1.00 15.75           N  
ATOM    192  CA  GLU A  63      25.045  32.754   3.019  1.00 15.98           C  
ATOM    193  C   GLU A  63      24.122  31.546   2.804  1.00 16.48           C  
ATOM    194  O   GLU A  63      24.369  30.693   1.939  1.00 15.80           O  
ATOM    195  CB  GLU A  63      25.159  33.675   1.795  1.00 16.04           C  
ATOM    196  CG  GLU A  63      23.964  34.609   1.673  1.00 18.27           C  
ATOM    197  CD  GLU A  63      22.763  33.916   1.130  1.00 16.48           C  
ATOM    198  OE1 GLU A  63      22.834  33.483  -0.037  1.00 18.32           O  
ATOM    199  OE2 GLU A  63      21.792  33.780   1.874  1.00 17.67           O  
ATOM    200  N  AILE A  64      23.059  31.513   3.596  0.70 15.01           N  
ATOM    201  N  BILE A  64      23.077  31.449   3.627  0.30 14.59           N  
ATOM    202  CA AILE A  64      22.195  30.323   3.716  0.70 17.55           C  
ATOM    203  CA BILE A  64      22.246  30.222   3.657  0.30 14.58           C  
ATOM    204  C  AILE A  64      21.406  29.975   2.452  0.70 16.34           C  
ATOM    205  C  BILE A  64      21.412  29.950   2.413  0.30 14.89           C  
ATOM    206  O  AILE A  64      21.218  28.794   2.121  0.70 16.76           O  
ATOM    207  O  BILE A  64      21.180  28.785   2.074  0.30 15.19           O  
ATOM    208  CB AILE A  64      21.257  30.506   4.924  0.70 17.25           C  
ATOM    209  CB BILE A  64      21.308  30.150   4.898  0.30 13.33           C  
ATOM    210  CG1AILE A  64      22.075  30.487   6.218  0.70 16.75           C  
ATOM    211  CG1BILE A  64      20.237  31.261   4.907  0.30 11.14           C  
ATOM    212  CG2AILE A  64      20.157  29.432   4.974  0.70 22.67           C  
ATOM    213  CG2BILE A  64      22.126  30.181   6.165  0.30 11.07           C  
ATOM    214  CD1AILE A  64      21.304  30.947   7.455  0.70 18.75           C  
ATOM    215  CD1BILE A  64      19.302  31.207   6.104  0.30 14.79           C  
ATOM    216  N   VAL A  65      20.937  30.998   1.743  1.00 15.54           N  
ATOM    217  CA  VAL A  65      20.118  30.779   0.557  1.00 15.42           C  
ATOM    218  C   VAL A  65      20.966  30.183  -0.565  1.00 15.67           C  
ATOM    219  O   VAL A  65      20.578  29.185  -1.169  1.00 17.64           O  
ATOM    220  CB  VAL A  65      19.374  32.065   0.131  1.00 16.32           C  
ATOM    221  CG1 VAL A  65      18.611  31.814  -1.168  1.00 16.47           C  
ATOM    222  CG2 VAL A  65      18.455  32.549   1.245  1.00 17.03           C  
ATOM    223  N   LYS A  66      22.158  30.744  -0.774  1.00 15.10           N  
ATOM    224  CA  LYS A  66      23.129  30.213  -1.718  1.00 17.66           C  
ATOM    225  C   LYS A  66      23.456  28.752  -1.377  1.00 15.01           C  
ATOM    226  O   LYS A  66      23.503  27.897  -2.254  1.00 17.56           O  
ATOM    227  CB  LYS A  66      24.409  31.049  -1.667  1.00 18.42           C  
ATOM    228  CG  LYS A  66      25.508  30.681  -2.687  1.00 22.46           C  
ATOM    229  CD  LYS A  66      26.773  31.479  -2.436  1.00 25.47           C  
ATOM    230  CE  LYS A  66      27.943  30.958  -3.281  1.00 30.53           C  
ATOM    231  NZ  LYS A  66      29.226  31.686  -2.981  1.00 35.55           N  
ATOM    232  N   ALA A  67      23.697  28.483  -0.101  1.00 15.34           N  
ATOM    233  CA  ALA A  67      24.033  27.139   0.336  1.00 14.05           C  
ATOM    234  C   ALA A  67      22.894  26.159   0.097  1.00 16.55           C  
ATOM    235  O   ALA A  67      23.103  25.047  -0.387  1.00 15.77           O  
ATOM    236  CB  ALA A  67      24.460  27.127   1.807  1.00 16.88           C  
ATOM    237  N   LEU A  68      21.684  26.555   0.448  1.00 15.88           N  
ATOM    238  CA  LEU A  68      20.533  25.663   0.223  1.00 15.76           C  
ATOM    239  C   LEU A  68      20.307  25.401  -1.247  1.00 16.09           C  
ATOM    240  O   LEU A  68      19.975  24.267  -1.631  1.00 16.92           O  
ATOM    241  CB  LEU A  68      19.273  26.203   0.888  1.00 15.37           C  
ATOM    242  CG  LEU A  68      19.283  26.184   2.414  1.00 17.05           C  
ATOM    243  CD1 LEU A  68      18.178  27.071   2.983  1.00 18.57           C  
ATOM    244  CD2 LEU A  68      19.147  24.762   3.008  1.00 17.65           C  
ATOM    245  N  AASN A  69      20.465  26.427  -2.080  0.50 16.84           N  
ATOM    246  N  BASN A  69      20.507  26.414  -2.075  0.50 17.26           N  
ATOM    247  CA AASN A  69      20.359  26.246  -3.530  0.50 16.88           C  
ATOM    248  CA BASN A  69      20.333  26.252  -3.508  0.50 17.92           C  
ATOM    249  C  AASN A  69      21.366  25.212  -3.994  0.50 15.54           C  
ATOM    250  C  BASN A  69      21.387  25.290  -4.073  0.50 17.20           C  
ATOM    251  O  AASN A  69      21.011  24.241  -4.669  0.50 13.86           O  
ATOM    252  O  BASN A  69      21.090  24.473  -4.944  0.50 19.34           O  
ATOM    253  CB AASN A  69      20.582  27.569  -4.288  0.50 18.02           C  
ATOM    254  CB BASN A  69      20.376  27.625  -4.192  0.50 18.41           C  
ATOM    255  CG AASN A  69      19.325  28.409  -4.389  0.50 18.57           C  
ATOM    256  CG BASN A  69      19.882  27.580  -5.613  0.50 20.46           C  
ATOM    257  OD1AASN A  69      18.428  28.110  -5.174  0.50 22.97           O  
ATOM    258  OD1BASN A  69      18.781  28.042  -5.913  0.50 25.21           O  
ATOM    259  ND2AASN A  69      19.267  29.477  -3.618  0.50 21.60           N  
ATOM    260  ND2BASN A  69      20.676  27.001  -6.496  0.50 23.45           N  
ATOM    261  N   ALA A  70      22.611  25.395  -3.566  1.00 15.36           N  
ATOM    262  CA  ALA A  70      23.712  24.508  -3.950  1.00 15.35           C  
ATOM    263  C   ALA A  70      23.462  23.061  -3.500  1.00 17.53           C  
ATOM    264  O   ALA A  70      23.746  22.111  -4.250  1.00 17.04           O  
ATOM    265  CB  ALA A  70      25.016  25.028  -3.368  1.00 17.41           C  
ATOM    266  N   PHE A  71      22.910  22.902  -2.297  1.00 15.37           N  
ATOM    267  CA  PHE A  71      22.563  21.593  -1.799  1.00 14.74           C  
ATOM    268  C   PHE A  71      21.537  20.887  -2.680  1.00 14.01           C  
ATOM    269  O   PHE A  71      21.714  19.748  -3.055  1.00 16.39           O  
ATOM    270  CB  PHE A  71      22.006  21.692  -0.383  1.00 16.84           C  
ATOM    271  CG  PHE A  71      21.654  20.371   0.160  1.00 16.97           C  
ATOM    272  CD1 PHE A  71      22.645  19.548   0.607  1.00 18.35           C  
ATOM    273  CD2 PHE A  71      20.345  19.908   0.138  1.00 15.92           C  
ATOM    274  CE1 PHE A  71      22.357  18.283   1.053  1.00 19.39           C  
ATOM    275  CE2 PHE A  71      20.059  18.649   0.557  1.00 17.40           C  
ATOM    276  CZ  PHE A  71      21.061  17.842   1.037  1.00 16.50           C  
ATOM    277  N   CYS A  72      20.449  21.581  -2.976  1.00 15.03           N  
ATOM    278  CA  CYS A  72      19.390  21.028  -3.797  1.00 16.30           C  
ATOM    279  C   CYS A  72      19.899  20.693  -5.189  1.00 16.11           C  
ATOM    280  O   CYS A  72      19.514  19.677  -5.770  1.00 16.78           O  
ATOM    281  CB  CYS A  72      18.209  21.993  -3.895  1.00 17.27           C  
ATOM    282  SG  CYS A  72      17.348  22.253  -2.340  1.00 19.27           S  
ATOM    283  N   LYS A  73      20.748  21.560  -5.724  1.00 18.26           N  
ATOM    284  CA  LYS A  73      21.346  21.306  -7.026  1.00 19.53           C  
ATOM    285  C   LYS A  73      22.215  20.046  -6.962  1.00 20.80           C  
ATOM    286  O   LYS A  73      22.095  19.154  -7.810  1.00 21.26           O  
ATOM    287  CB  LYS A  73      22.167  22.510  -7.481  1.00 19.96           C  
ATOM    288  CG  LYS A  73      22.820  22.314  -8.848  1.00 23.25           C  
ATOM    289  CD  LYS A  73      23.472  23.577  -9.376  1.00 24.35           C  
ATOM    290  CE  LYS A  73      24.269  23.268 -10.653  1.00 31.78           C  
ATOM    291  NZ  LYS A  73      24.857  24.504 -11.241  1.00 38.09           N  
ATOM    292  N   GLU A  74      23.085  19.962  -5.955  1.00 19.88           N  
ATOM    293  CA  GLU A  74      23.964  18.799  -5.791  1.00 18.54           C  
ATOM    294  C   GLU A  74      23.170  17.493  -5.721  1.00 19.43           C  
ATOM    295  O   GLU A  74      23.573  16.479  -6.313  1.00 20.52           O  
ATOM    296  CB  GLU A  74      24.816  18.919  -4.516  1.00 19.33           C  
ATOM    297  CG  GLU A  74      25.725  17.700  -4.291  1.00 20.25           C  
ATOM    298  CD  GLU A  74      26.488  17.659  -2.951  1.00 25.87           C  
ATOM    299  OE1 GLU A  74      26.414  18.607  -2.140  1.00 34.74           O  
ATOM    300  OE2 GLU A  74      27.196  16.637  -2.733  1.00 35.66           O  
ATOM    301  N   LYS A  75      22.060  17.514  -4.994  1.00 18.33           N  
ATOM    302  CA  LYS A  75      21.249  16.319  -4.778  1.00 16.82           C  
ATOM    303  C   LYS A  75      20.158  16.124  -5.823  1.00 18.43           C  
ATOM    304  O   LYS A  75      19.435  15.131  -5.765  1.00 20.90           O  
ATOM    305  CB  LYS A  75      20.668  16.309  -3.361  1.00 16.73           C  
ATOM    306  CG  LYS A  75      21.731  16.281  -2.261  1.00 19.09           C  
ATOM    307  CD  LYS A  75      22.582  15.011  -2.362  1.00 23.55           C  
ATOM    308  CE  LYS A  75      23.585  14.866  -1.279  1.00 24.41           C  
ATOM    309  NZ  LYS A  75      24.377  13.604  -1.491  1.00 25.17           N  
ATOM    310  N   GLY A  76      20.091  17.006  -6.814  1.00 17.44           N  
ATOM    311  CA  GLY A  76      19.120  16.884  -7.897  1.00 18.94           C  
ATOM    312  C   GLY A  76      17.684  16.936  -7.422  1.00 20.05           C  
ATOM    313  O   GLY A  76      16.829  16.252  -7.978  1.00 20.22           O  
ATOM    314  N   ILE A  77      17.409  17.758  -6.406  1.00 17.31           N  
ATOM    315  CA  ILE A  77      16.076  17.799  -5.819  1.00 17.56           C  
ATOM    316  C   ILE A  77      15.185  18.642  -6.725  1.00 18.93           C  
ATOM    317  O   ILE A  77      15.463  19.804  -6.975  1.00 19.72           O  
ATOM    318  CB  ILE A  77      16.087  18.358  -4.412  1.00 16.60           C  
ATOM    319  CG1 ILE A  77      16.928  17.455  -3.510  1.00 17.95           C  
ATOM    320  CG2 ILE A  77      14.675  18.429  -3.896  1.00 18.12           C  
ATOM    321  CD1 ILE A  77      17.089  17.944  -2.091  1.00 18.96           C  
ATOM    322  N   LEU A  78      14.130  18.020  -7.226  1.00 19.66           N  
ATOM    323  CA  LEU A  78      13.230  18.666  -8.177  1.00 18.22           C  
ATOM    324  C   LEU A  78      12.146  19.480  -7.490  1.00 16.61           C  
ATOM    325  O   LEU A  78      11.713  20.508  -8.012  1.00 16.88           O  
ATOM    326  CB  LEU A  78      12.594  17.587  -9.059  1.00 18.76           C  
ATOM    327  CG  LEU A  78      13.551  16.673  -9.826  1.00 18.90           C  
ATOM    328  CD1 LEU A  78      12.762  15.614 -10.556  1.00 19.50           C  
ATOM    329  CD2 LEU A  78      14.381  17.519 -10.775  1.00 20.90           C  
ATOM    330  N   SER A  79      11.675  18.967  -6.355  1.00 16.89           N  
ATOM    331  CA  SER A  79      10.702  19.648  -5.525  1.00 18.11           C  
ATOM    332  C   SER A  79      10.813  19.097  -4.120  1.00 18.45           C  
ATOM    333  O   SER A  79      11.403  18.024  -3.898  1.00 16.56           O  
ATOM    334  CB  SER A  79       9.274  19.504  -6.061  1.00 16.20           C  
ATOM    335  OG  SER A  79       8.802  18.180  -5.913  1.00 18.59           O  
ATOM    336  N   GLY A  80      10.272  19.855  -3.169  1.00 17.31           N  
ATOM    337  CA  GLY A  80      10.426  19.489  -1.779  1.00 16.63           C  
ATOM    338  C   GLY A  80      10.148  20.640  -0.859  1.00 16.01           C  
ATOM    339  O   GLY A  80       9.610  21.654  -1.263  1.00 15.19           O  
ATOM    340  N   SER A  81      10.568  20.491   0.388  1.00 15.07           N  
ATOM    341  CA  SER A  81      10.360  21.512   1.397  1.00 16.47           C  
ATOM    342  C   SER A  81      11.623  21.727   2.176  1.00 18.00           C  
ATOM    343  O   SER A  81      12.495  20.863   2.216  1.00 16.77           O  
ATOM    344  CB  SER A  81       9.251  21.085   2.338  1.00 19.18           C  
ATOM    345  OG  SER A  81       9.672  19.963   3.076  1.00 24.65           O  
ATOM    346  N   ILE A  82      11.731  22.910   2.780  1.00 16.48           N  
ATOM    347  CA  ILE A  82      12.870  23.255   3.611  1.00 15.34           C  
ATOM    348  C   ILE A  82      12.317  23.931   4.847  1.00 17.15           C  
ATOM    349  O   ILE A  82      11.450  24.785   4.738  1.00 16.94           O  
ATOM    350  CB  ILE A  82      13.850  24.223   2.886  1.00 16.35           C  
ATOM    351  CG1 ILE A  82      14.379  23.635   1.579  1.00 16.98           C  
ATOM    352  CG2 ILE A  82      15.013  24.630   3.844  1.00 17.23           C  
ATOM    353  CD1 ILE A  82      15.318  24.548   0.769  1.00 16.73           C  
ATOM    354  N   ASN A  83      12.828  23.545   6.006  1.00 16.81           N  
ATOM    355  CA  ASN A  83      12.414  24.085   7.284  1.00 17.31           C  
ATOM    356  C   ASN A  83      13.596  24.050   8.215  1.00 17.58           C  
ATOM    357  O   ASN A  83      14.332  23.085   8.232  1.00 21.12           O  
ATOM    358  CB  ASN A  83      11.332  23.227   7.877  1.00 20.86           C  
ATOM    359  CG  ASN A  83      10.059  23.314   7.114  1.00 27.21           C  
ATOM    360  OD1 ASN A  83       9.319  24.300   7.257  1.00 28.39           O  
ATOM    361  ND2 ASN A  83       9.768  22.295   6.278  1.00 27.73           N  
ATOM    362  N   GLY A  84      13.791  25.092   9.005  1.00 17.09           N  
ATOM    363  CA  GLY A  84      14.794  25.034  10.031  1.00 17.23           C  
ATOM    364  C   GLY A  84      15.006  26.264  10.864  1.00 17.43           C  
ATOM    365  O   GLY A  84      14.173  27.185  10.864  1.00 16.11           O  
ATOM    366  N   ILE A  85      16.116  26.241  11.602  1.00 15.94           N  
ATOM    367  CA  ILE A  85      16.442  27.239  12.613  1.00 16.31           C  
ATOM    368  C   ILE A  85      17.943  27.471  12.606  1.00 15.97           C  
ATOM    369  O   ILE A  85      18.727  26.694  12.023  1.00 17.03           O  
ATOM    370  CB  ILE A  85      15.938  26.798  14.036  1.00 14.33           C  
ATOM    371  CG1 ILE A  85      16.548  25.449  14.469  1.00 15.13           C  
ATOM    372  CG2 ILE A  85      14.425  26.729  14.083  1.00 15.94           C  
ATOM    373  CD1 ILE A  85      16.318  25.109  15.948  1.00 17.42           C  
ATOM    374  N   GLY A  86      18.375  28.537  13.278  1.00 14.98           N  
ATOM    375  CA  GLY A  86      19.770  28.880  13.324  1.00 17.29           C  
ATOM    376  C   GLY A  86      19.909  30.327  13.769  1.00 15.98           C  
ATOM    377  O   GLY A  86      18.954  30.914  14.274  1.00 17.95           O  
ATOM    378  N   ALA A  87      21.111  30.859  13.619  1.00 15.32           N  
ATOM    379  CA  ALA A  87      21.428  32.235  13.980  1.00 15.47           C  
ATOM    380  C   ALA A  87      22.243  32.860  12.870  1.00 15.22           C  
ATOM    381  O   ALA A  87      22.997  32.177  12.145  1.00 15.75           O  
ATOM    382  CB  ALA A  87      22.164  32.294  15.312  1.00 17.92           C  
ATOM    383  N   ILE A  88      22.032  34.166  12.707  1.00 14.90           N  
ATOM    384  CA  ILE A  88      22.566  34.929  11.589  1.00 14.26           C  
ATOM    385  C   ILE A  88      23.057  36.299  12.038  1.00 14.65           C  
ATOM    386  O   ILE A  88      22.672  36.810  13.080  1.00 15.88           O  
ATOM    387  CB  ILE A  88      21.528  35.118  10.465  1.00 14.70           C  
ATOM    388  CG1 ILE A  88      20.300  35.874  10.965  1.00 15.15           C  
ATOM    389  CG2 ILE A  88      21.112  33.768   9.880  1.00 15.49           C  
ATOM    390  CD1 ILE A  88      19.276  36.175   9.910  1.00 14.67           C  
ATOM    391  N   GLY A  89      23.951  36.857  11.234  1.00 13.72           N  
ATOM    392  CA  GLY A  89      24.496  38.203  11.428  1.00 15.55           C  
ATOM    393  C   GLY A  89      24.120  39.228  10.386  1.00 14.70           C  
ATOM    394  O   GLY A  89      24.479  40.417  10.516  1.00 16.70           O  
ATOM    395  N  AGLU A  90      23.375  38.789   9.370  0.70 16.88           N  
ATOM    396  N  BGLU A  90      23.430  38.778   9.334  0.30 15.15           N  
ATOM    397  CA AGLU A  90      22.900  39.670   8.312  0.70 17.31           C  
ATOM    398  CA BGLU A  90      22.925  39.644   8.271  0.30 14.80           C  
ATOM    399  C  AGLU A  90      21.694  38.999   7.669  0.70 15.81           C  
ATOM    400  C  BGLU A  90      21.665  38.982   7.714  0.30 14.40           C  
ATOM    401  O  AGLU A  90      21.671  37.782   7.520  0.70 15.99           O  
ATOM    402  O  BGLU A  90      21.576  37.753   7.674  0.30 14.55           O  
ATOM    403  CB AGLU A  90      24.004  39.953   7.291  0.70 17.65           C  
ATOM    404  CB BGLU A  90      23.969  39.851   7.165  0.30 14.76           C  
ATOM    405  CG AGLU A  90      23.669  41.079   6.329  0.70 17.19           C  
ATOM    406  CG BGLU A  90      23.568  40.875   6.096  0.30 13.89           C  
ATOM    407  CD AGLU A  90      24.897  41.684   5.678  0.70 19.58           C  
ATOM    408  CD BGLU A  90      24.501  40.876   4.900  0.30 14.45           C  
ATOM    409  OE1AGLU A  90      25.893  41.958   6.400  0.70 26.63           O  
ATOM    410  OE1BGLU A  90      25.595  41.491   4.976  0.30 17.53           O  
ATOM    411  OE2AGLU A  90      24.858  41.902   4.445  0.70 27.20           O  
ATOM    412  OE2BGLU A  90      24.128  40.281   3.867  0.30 15.14           O  
ATOM    413  N   LEU A  91      20.689  39.796   7.315  1.00 13.74           N  
ATOM    414  CA  LEU A  91      19.454  39.310   6.719  1.00 13.89           C  
ATOM    415  C   LEU A  91      18.968  40.267   5.677  1.00 15.62           C  
ATOM    416  O   LEU A  91      18.971  41.465   5.929  1.00 15.67           O  
ATOM    417  CB  LEU A  91      18.368  39.266   7.793  1.00 15.07           C  
ATOM    418  CG  LEU A  91      16.961  38.841   7.378  1.00 14.74           C  
ATOM    419  CD1 LEU A  91      16.920  37.385   6.884  1.00 15.65           C  
ATOM    420  CD2 LEU A  91      15.974  39.069   8.505  1.00 15.59           C  
ATOM    421  N   THR A  92      18.522  39.747   4.540  1.00 13.57           N  
ATOM    422  CA  THR A  92      17.866  40.584   3.547  1.00 12.67           C  
ATOM    423  C   THR A  92      16.484  39.996   3.276  1.00 13.89           C  
ATOM    424  O   THR A  92      16.360  38.828   2.885  1.00 14.88           O  
ATOM    425  CB  THR A  92      18.635  40.705   2.244  1.00 13.80           C  
ATOM    426  OG1 THR A  92      19.959  41.166   2.534  1.00 15.75           O  
ATOM    427  CG2 THR A  92      17.942  41.715   1.306  1.00 13.90           C  
ATOM    428  N   LEU A  93      15.464  40.839   3.455  1.00 15.47           N  
ATOM    429  CA  LEU A  93      14.071  40.525   3.151  1.00 14.90           C  
ATOM    430  C   LEU A  93      13.582  41.377   2.019  1.00 15.85           C  
ATOM    431  O   LEU A  93      14.086  42.481   1.823  1.00 15.77           O  
ATOM    432  CB  LEU A  93      13.188  40.769   4.371  1.00 14.90           C  
ATOM    433  CG  LEU A  93      13.556  40.041   5.661  1.00 14.87           C  
ATOM    434  CD1 LEU A  93      12.661  40.512   6.819  1.00 14.47           C  
ATOM    435  CD2 LEU A  93      13.529  38.499   5.474  1.00 16.12           C  
ATOM    436  N   ARG A  94      12.609  40.875   1.264  1.00 13.95           N  
ATOM    437  CA  ARG A  94      11.953  41.633   0.203  1.00 14.90           C  
ATOM    438  C   ARG A  94      10.493  41.841   0.523  1.00 14.58           C  
ATOM    439  O   ARG A  94       9.796  40.883   0.873  1.00 15.79           O  
ATOM    440  CB  ARG A  94      12.046  40.908  -1.127  1.00 15.10           C  
ATOM    441  CG  ARG A  94      11.334  41.634  -2.259  1.00 15.41           C  
ATOM    442  CD  ARG A  94      11.703  41.131  -3.607  1.00 15.53           C  
ATOM    443  NE  ARG A  94      13.074  41.469  -3.942  1.00 14.99           N  
ATOM    444  CZ  ARG A  94      13.731  41.071  -5.034  1.00 17.75           C  
ATOM    445  NH1 ARG A  94      13.193  40.230  -5.880  1.00 21.06           N  
ATOM    446  NH2 ARG A  94      14.961  41.468  -5.243  1.00 18.64           N  
ATOM    447  N   PHE A  95      10.021  43.071   0.329  1.00 14.92           N  
ATOM    448  CA  PHE A  95       8.587  43.374   0.397  1.00 15.37           C  
ATOM    449  C   PHE A  95       8.143  43.870  -0.977  1.00 14.31           C  
ATOM    450  O   PHE A  95       8.615  44.857  -1.478  1.00 16.17           O  
ATOM    451  CB  PHE A  95       8.237  44.383   1.483  1.00 15.44           C  
ATOM    452  CG  PHE A  95       6.777  44.414   1.804  1.00 14.75           C  
ATOM    453  CD1 PHE A  95       6.255  43.511   2.702  1.00 18.27           C  
ATOM    454  CD2 PHE A  95       5.929  45.339   1.206  1.00 18.27           C  
ATOM    455  CE1 PHE A  95       4.889  43.517   3.006  1.00 19.01           C  
ATOM    456  CE2 PHE A  95       4.573  45.312   1.509  1.00 20.63           C  
ATOM    457  CZ  PHE A  95       4.088  44.407   2.395  1.00 20.01           C  
ATOM    458  N   PHE A  96       7.216  43.126  -1.572  1.00 15.76           N  
ATOM    459  CA  PHE A  96       6.664  43.425  -2.889  1.00 15.80           C  
ATOM    460  C   PHE A  96       5.314  44.115  -2.771  1.00 19.49           C  
ATOM    461  O   PHE A  96       4.455  43.642  -2.046  1.00 18.80           O  
ATOM    462  CB  PHE A  96       6.553  42.125  -3.646  1.00 16.62           C  
ATOM    463  CG  PHE A  96       5.906  42.238  -4.970  1.00 19.09           C  
ATOM    464  CD1 PHE A  96       6.541  42.847  -6.008  1.00 20.36           C  
ATOM    465  CD2 PHE A  96       4.641  41.716  -5.172  1.00 19.97           C  
ATOM    466  CE1 PHE A  96       5.927  42.941  -7.274  1.00 21.32           C  
ATOM    467  CE2 PHE A  96       4.038  41.785  -6.421  1.00 20.42           C  
ATOM    468  CZ  PHE A  96       4.693  42.394  -7.470  1.00 19.37           C  
ATOM    469  N   ASN A  97       5.155  45.241  -3.477  1.00 17.08           N  
ATOM    470  CA  ASN A  97       3.910  45.977  -3.488  1.00 18.45           C  
ATOM    471  C   ASN A  97       3.156  45.571  -4.734  1.00 19.03           C  
ATOM    472  O   ASN A  97       3.537  45.970  -5.835  1.00 18.91           O  
ATOM    473  CB  ASN A  97       4.221  47.466  -3.505  1.00 18.70           C  
ATOM    474  CG  ASN A  97       2.984  48.326  -3.427  1.00 24.30           C  
ATOM    475  OD1 ASN A  97       1.917  47.966  -3.948  1.00 24.81           O  
ATOM    476  ND2 ASN A  97       3.124  49.492  -2.800  1.00 25.61           N  
ATOM    477  N   PRO A  98       2.080  44.788  -4.591  1.00 17.60           N  
ATOM    478  CA  PRO A  98       1.330  44.331  -5.770  1.00 19.66           C  
ATOM    479  C   PRO A  98       0.625  45.414  -6.533  1.00 21.49           C  
ATOM    480  O   PRO A  98       0.340  45.209  -7.699  1.00 25.14           O  
ATOM    481  CB  PRO A  98       0.277  43.381  -5.191  1.00 21.35           C  
ATOM    482  CG  PRO A  98       0.196  43.708  -3.735  1.00 21.76           C  
ATOM    483  CD  PRO A  98       1.504  44.286  -3.331  1.00 20.73           C  
ATOM    484  N   LYS A  99       0.313  46.521  -5.888  1.00 20.61           N  
ATOM    485  CA  LYS A  99      -0.416  47.595  -6.539  1.00 24.02           C  
ATOM    486  C   LYS A  99       0.483  48.357  -7.502  1.00 24.15           C  
ATOM    487  O   LYS A  99       0.126  48.541  -8.662  1.00 26.26           O  
ATOM    488  CB  LYS A  99      -1.003  48.524  -5.489  1.00 24.60           C  
ATOM    489  CG  LYS A  99      -1.938  49.592  -6.053  1.00 34.86           C  
ATOM    490  N   THR A 100       1.670  48.739  -7.054  1.00 21.15           N  
ATOM    491  CA  THR A 100       2.568  49.541  -7.903  1.00 19.46           C  
ATOM    492  C   THR A 100       3.698  48.753  -8.574  1.00 17.93           C  
ATOM    493  O   THR A 100       4.407  49.289  -9.430  1.00 18.89           O  
ATOM    494  CB  THR A 100       3.255  50.613  -7.053  1.00 19.22           C  
ATOM    495  OG1 THR A 100       4.044  49.989  -6.050  1.00 19.16           O  
ATOM    496  CG2 THR A 100       2.196  51.543  -6.395  1.00 23.69           C  
ATOM    497  N  ALYS A 101       3.848  47.498  -8.174  0.50 19.22           N  
ATOM    498  N  BLYS A 101       3.862  47.495  -8.167  0.50 18.60           N  
ATOM    499  CA ALYS A 101       4.936  46.653  -8.616  0.50 19.92           C  
ATOM    500  CA BLYS A 101       4.967  46.625  -8.583  0.50 18.81           C  
ATOM    501  C  ALYS A 101       6.303  47.180  -8.182  0.50 17.47           C  
ATOM    502  C  BLYS A 101       6.324  47.065  -8.045  0.50 15.80           C  
ATOM    503  O  ALYS A 101       7.290  46.789  -8.763  0.50 16.66           O  
ATOM    504  O  BLYS A 101       7.340  46.451  -8.344  0.50 11.73           O  
ATOM    505  CB ALYS A 101       4.905  46.435 -10.146  0.50 21.39           C  
ATOM    506  CB BLYS A 101       5.031  46.451 -10.114  0.50 20.35           C  
ATOM    507  CG ALYS A 101       3.517  46.113 -10.715  0.50 24.70           C  
ATOM    508  CG BLYS A 101       3.711  46.016 -10.741  0.50 24.62           C  
ATOM    509  CD ALYS A 101       2.880  44.894 -10.045  0.50 23.37           C  
ATOM    510  CD BLYS A 101       3.267  44.624 -10.276  0.50 24.43           C  
ATOM    511  CE ALYS A 101       1.540  44.531 -10.689  0.50 26.65           C  
ATOM    512  CE BLYS A 101       1.895  44.257 -10.808  0.50 27.82           C  
ATOM    513  NZ ALYS A 101       0.548  45.635 -10.660  0.50 28.31           N  
ATOM    514  NZ BLYS A 101       1.807  44.401 -12.277  0.50 27.79           N  
ATOM    515  N   ALA A 102       6.351  48.094  -7.206  1.00 16.10           N  
ATOM    516  CA  ALA A 102       7.586  48.440  -6.518  1.00 14.38           C  
ATOM    517  C   ALA A 102       7.942  47.293  -5.581  1.00 15.59           C  
ATOM    518  O   ALA A 102       7.066  46.528  -5.153  1.00 16.21           O  
ATOM    519  CB  ALA A 102       7.423  49.724  -5.717  1.00 15.48           C  
ATOM    520  N   TYR A 103       9.222  47.152  -5.278  1.00 14.37           N  
ATOM    521  CA  TYR A 103       9.654  46.200  -4.285  1.00 14.66           C  
ATOM    522  C   TYR A 103      10.801  46.797  -3.525  1.00 14.87           C  
ATOM    523  O   TYR A 103      11.534  47.621  -4.051  1.00 15.55           O  
ATOM    524  CB  TYR A 103      10.053  44.864  -4.903  1.00 14.07           C  
ATOM    525  CG  TYR A 103      11.191  44.897  -5.860  1.00 14.55           C  
ATOM    526  CD1 TYR A 103      10.985  45.214  -7.189  1.00 14.92           C  
ATOM    527  CD2 TYR A 103      12.492  44.676  -5.443  1.00 14.91           C  
ATOM    528  CE1 TYR A 103      12.055  45.264  -8.101  1.00 15.05           C  
ATOM    529  CE2 TYR A 103      13.555  44.713  -6.339  1.00 14.80           C  
ATOM    530  CZ  TYR A 103      13.325  45.004  -7.663  1.00 15.71           C  
ATOM    531  OH  TYR A 103      14.377  45.046  -8.567  1.00 18.49           O  
ATOM    532  N   ASP A 104      10.959  46.410  -2.272  1.00 14.23           N  
ATOM    533  CA  ASP A 104      12.113  46.861  -1.540  1.00 14.91           C  
ATOM    534  C   ASP A 104      12.772  45.725  -0.832  1.00 14.05           C  
ATOM    535  O   ASP A 104      12.118  44.805  -0.342  1.00 15.24           O  
ATOM    536  CB  ASP A 104      11.810  47.986  -0.585  1.00 16.89           C  
ATOM    537  CG  ASP A 104      11.068  47.555   0.604  1.00 17.53           C  
ATOM    538  OD1 ASP A 104      11.692  47.396   1.707  1.00 19.96           O  
ATOM    539  OD2 ASP A 104       9.851  47.353   0.441  1.00 19.79           O  
ATOM    540  N   ASP A 105      14.089  45.830  -0.792  1.00 12.95           N  
ATOM    541  CA  ASP A 105      14.938  44.856  -0.174  1.00 13.54           C  
ATOM    542  C   ASP A 105      15.607  45.501   1.021  1.00 14.08           C  
ATOM    543  O   ASP A 105      16.394  46.442   0.866  1.00 14.66           O  
ATOM    544  CB  ASP A 105      15.989  44.385  -1.172  1.00 13.19           C  
ATOM    545  CG  ASP A 105      15.397  43.636  -2.357  1.00 15.46           C  
ATOM    546  OD1 ASP A 105      14.202  43.339  -2.356  1.00 16.20           O  
ATOM    547  OD2 ASP A 105      16.208  43.327  -3.279  1.00 16.62           O  
ATOM    548  N   LYS A 106      15.284  45.003   2.213  1.00 14.61           N  
ATOM    549  CA  LYS A 106      15.861  45.567   3.426  1.00 14.68           C  
ATOM    550  C   LYS A 106      16.869  44.613   4.053  1.00 13.46           C  
ATOM    551  O   LYS A 106      16.546  43.448   4.310  1.00 14.26           O  
ATOM    552  CB  LYS A 106      14.786  45.930   4.451  1.00 15.50           C  
ATOM    553  CG  LYS A 106      15.362  46.763   5.617  1.00 17.21           C  
ATOM    554  CD  LYS A 106      14.289  47.436   6.424  1.00 17.61           C  
ATOM    555  CE  LYS A 106      14.900  48.261   7.535  1.00 18.68           C  
ATOM    556  NZ  LYS A 106      13.899  49.080   8.237  1.00 17.56           N  
ATOM    557  N   THR A 107      18.065  45.133   4.305  1.00 13.84           N  
ATOM    558  CA  THR A 107      19.156  44.374   4.877  1.00 14.36           C  
ATOM    559  C   THR A 107      19.374  44.835   6.293  1.00 16.58           C  
ATOM    560  O   THR A 107      19.611  45.999   6.550  1.00 16.10           O  
ATOM    561  CB  THR A 107      20.441  44.517   4.067  1.00 15.58           C  
ATOM    562  OG1 THR A 107      20.217  43.989   2.754  1.00 15.40           O  
ATOM    563  CG2 THR A 107      21.630  43.782   4.745  1.00 14.84           C  
ATOM    564  N   PHE A 108      19.280  43.883   7.216  1.00 15.77           N  
ATOM    565  CA  PHE A 108      19.568  44.103   8.629  1.00 16.52           C  
ATOM    566  C   PHE A 108      20.941  43.577   8.927  1.00 17.25           C  
ATOM    567  O   PHE A 108      21.295  42.502   8.469  1.00 17.07           O  
ATOM    568  CB  PHE A 108      18.522  43.372   9.466  1.00 15.77           C  
ATOM    569  CG  PHE A 108      17.122  43.822   9.202  1.00 16.33           C  
ATOM    570  CD1 PHE A 108      16.381  43.250   8.157  1.00 18.16           C  
ATOM    571  CD2 PHE A 108      16.537  44.793   9.991  1.00 17.77           C  
ATOM    572  CE1 PHE A 108      15.101  43.662   7.880  1.00 18.58           C  
ATOM    573  CE2 PHE A 108      15.226  45.217   9.721  1.00 18.53           C  
ATOM    574  CZ  PHE A 108      14.525  44.629   8.652  1.00 17.89           C  
ATOM    575  N   ARG A 109      21.732  44.343   9.675  1.00 14.37           N  
ATOM    576  CA  ARG A 109      23.101  44.004   9.998  1.00 15.72           C  
ATOM    577  C   ARG A 109      23.267  44.010  11.502  1.00 15.87           C  
ATOM    578  O   ARG A 109      23.637  45.003  12.111  1.00 16.50           O  
ATOM    579  CB  ARG A 109      24.019  45.004   9.319  1.00 16.76           C  
ATOM    580  CG  ARG A 109      23.916  44.860   7.809  1.00 17.90           C  
ATOM    581  CD  ARG A 109      24.947  45.674   7.116  1.00 16.70           C  
ATOM    582  NE  ARG A 109      24.609  47.091   7.179  1.00 17.12           N  
ATOM    583  CZ  ARG A 109      25.400  48.066   6.743  1.00 16.69           C  
ATOM    584  NH1 ARG A 109      26.555  47.801   6.157  1.00 17.38           N  
ATOM    585  NH2 ARG A 109      25.022  49.320   6.863  1.00 16.00           N  
ATOM    586  N   GLU A 110      22.930  42.868  12.081  1.00 16.10           N  
ATOM    587  CA  GLU A 110      22.874  42.657  13.519  1.00 14.18           C  
ATOM    588  C   GLU A 110      22.728  41.170  13.781  1.00 15.12           C  
ATOM    589  O   GLU A 110      22.391  40.413  12.868  1.00 15.36           O  
ATOM    590  CB  GLU A 110      21.661  43.412  14.086  1.00 16.04           C  
ATOM    591  CG  GLU A 110      20.329  42.909  13.579  1.00 15.47           C  
ATOM    592  CD  GLU A 110      19.214  43.807  13.945  1.00 18.09           C  
ATOM    593  OE1 GLU A 110      19.020  44.803  13.232  1.00 18.67           O  
ATOM    594  OE2 GLU A 110      18.519  43.545  14.944  1.00 19.39           O  
ATOM    595  N   GLN A 111      22.894  40.764  15.024  1.00 15.84           N  
ATOM    596  CA  GLN A 111      22.746  39.372  15.384  1.00 14.56           C  
ATOM    597  C   GLN A 111      21.251  39.065  15.507  1.00 14.06           C  
ATOM    598  O   GLN A 111      20.492  39.838  16.110  1.00 16.22           O  
ATOM    599  CB  GLN A 111      23.471  39.050  16.689  1.00 16.04           C  
ATOM    600  CG  GLN A 111      23.485  37.606  17.036  1.00 14.72           C  
ATOM    601  CD  GLN A 111      24.290  36.749  16.070  1.00 15.06           C  
ATOM    602  OE1 GLN A 111      25.131  37.259  15.328  1.00 17.22           O  
ATOM    603  NE2 GLN A 111      24.094  35.440  16.124  1.00 15.97           N  
HETATM  604  N   MSE A 112      20.815  37.979  14.892  1.00 15.03           N  
HETATM  605  CA  MSE A 112      19.425  37.571  14.956  1.00 14.77           C  
HETATM  606  C   MSE A 112      19.331  36.065  15.077  1.00 15.59           C  
HETATM  607  O   MSE A 112      20.171  35.345  14.536  1.00 16.38           O  
HETATM  608  CB  MSE A 112      18.659  37.994  13.670  1.00 16.08           C  
HETATM  609  CG  MSE A 112      18.530  39.493  13.523  1.00 14.22           C  
HETATM  610 SE   MSE A 112      18.073  40.089  11.756  0.75 13.94          SE  
HETATM  611  CE  MSE A 112      19.907  39.918  10.979  1.00 18.92           C  
ATOM    612  N   GLU A 113      18.271  35.597  15.724  1.00 15.47           N  
ATOM    613  CA  GLU A 113      17.936  34.179  15.767  1.00 16.67           C  
ATOM    614  C   GLU A 113      16.886  33.884  14.722  1.00 16.78           C  
ATOM    615  O   GLU A 113      15.908  34.639  14.626  1.00 17.61           O  
ATOM    616  CB  GLU A 113      17.368  33.826  17.128  1.00 17.85           C  
ATOM    617  CG  GLU A 113      18.439  33.803  18.252  1.00 22.75           C  
ATOM    618  CD  GLU A 113      19.511  32.707  18.119  1.00 30.83           C  
ATOM    619  OE1 GLU A 113      19.411  31.798  17.248  1.00 26.99           O  
ATOM    620  OE2 GLU A 113      20.504  32.764  18.892  1.00 28.71           O  
ATOM    621  N   ILE A 114      17.064  32.850  13.914  1.00 15.27           N  
ATOM    622  CA  ILE A 114      16.029  32.414  13.013  1.00 15.55           C  
ATOM    623  C   ILE A 114      15.050  31.565  13.813  1.00 14.99           C  
ATOM    624  O   ILE A 114      15.376  30.414  14.197  1.00 14.63           O  
ATOM    625  CB  ILE A 114      16.580  31.557  11.863  1.00 15.60           C  
ATOM    626  CG1 ILE A 114      17.657  32.298  11.056  1.00 15.08           C  
ATOM    627  CG2 ILE A 114      15.411  31.108  10.956  1.00 16.48           C  
ATOM    628  CD1 ILE A 114      18.346  31.458   9.991  1.00 16.82           C  
ATOM    629  N   SER A 115      13.861  32.079  14.111  1.00 16.10           N  
ATOM    630  CA  SER A 115      12.890  31.272  14.858  1.00 14.58           C  
ATOM    631  C   SER A 115      12.208  30.275  13.944  1.00 14.22           C  
ATOM    632  O   SER A 115      11.843  29.182  14.395  1.00 15.48           O  
ATOM    633  CB  SER A 115      11.878  32.124  15.592  1.00 15.98           C  
ATOM    634  OG  SER A 115      11.085  32.886  14.695  1.00 14.80           O  
ATOM    635  N   ASN A 116      12.133  30.579  12.653  1.00 14.56           N  
ATOM    636  CA  ASN A 116      11.591  29.659  11.687  1.00 13.88           C  
ATOM    637  C   ASN A 116      11.981  30.104  10.306  1.00 14.67           C  
ATOM    638  O   ASN A 116      11.833  31.267   9.978  1.00 16.39           O  
ATOM    639  CB  ASN A 116      10.062  29.600  11.773  1.00 16.33           C  
ATOM    640  CG  ASN A 116       9.476  28.752  10.734  1.00 20.04           C  
ATOM    641  OD1 ASN A 116       9.290  29.191   9.614  1.00 20.97           O  
ATOM    642  ND2 ASN A 116       9.257  27.481  11.048  1.00 23.19           N  
ATOM    643  N   LEU A 117      12.513  29.190   9.525  1.00 15.92           N  
ATOM    644  CA  LEU A 117      12.695  29.391   8.096  1.00 15.31           C  
ATOM    645  C   LEU A 117      11.802  28.321   7.487  1.00 17.25           C  
ATOM    646  O   LEU A 117      11.895  27.139   7.870  1.00 18.47           O  
ATOM    647  CB  LEU A 117      14.146  29.223   7.678  1.00 17.20           C  
ATOM    648  CG  LEU A 117      14.479  29.357   6.171  1.00 19.00           C  
ATOM    649  CD1 LEU A 117      15.896  29.843   6.011  1.00 19.54           C  
ATOM    650  CD2 LEU A 117      14.222  28.046   5.432  1.00 21.62           C  
ATOM    651  N  ATHR A 118      10.879  28.731   6.602  0.34 16.62           N  
ATOM    652  N  BTHR A 118      10.903  28.725   6.585  0.33 18.94           N  
ATOM    653  N  CTHR A 118      11.032  28.681   6.485  0.33 14.67           N  
ATOM    654  CA ATHR A 118       9.894  27.864   5.930  0.34 16.45           C  
ATOM    655  CA BTHR A 118       9.955  27.835   5.909  0.33 20.30           C  
ATOM    656  CA CTHR A 118      10.215  27.689   5.872  0.33 13.36           C  
ATOM    657  C  ATHR A 118       9.963  28.093   4.425  0.34 15.82           C  
ATOM    658  C  BTHR A 118       9.972  28.091   4.420  0.33 17.82           C  
ATOM    659  C  CTHR A 118       9.912  28.059   4.442  0.33 13.54           C  
ATOM    660  O  ATHR A 118      10.029  29.236   3.981  0.34 18.19           O  
ATOM    661  O  BTHR A 118      10.001  29.240   3.984  0.33 19.57           O  
ATOM    662  O  CTHR A 118       9.660  29.212   4.086  0.33 14.25           O  
ATOM    663  CB ATHR A 118       8.411  28.224   6.294  0.34 17.28           C  
ATOM    664  CB BTHR A 118       8.484  28.089   6.328  0.33 21.75           C  
ATOM    665  CB CTHR A 118       8.934  27.453   6.663  0.33 12.08           C  
ATOM    666  OG1ATHR A 118       8.221  28.262   7.706  0.34 14.40           O  
ATOM    667  OG1BTHR A 118       8.294  29.479   6.603  0.33 28.02           O  
ATOM    668  OG1CTHR A 118       8.304  26.267   6.173  0.33 11.10           O  
ATOM    669  CG2ATHR A 118       7.436  27.219   5.709  0.34 14.53           C  
ATOM    670  CG2BTHR A 118       8.130  27.327   7.543  0.33 24.41           C  
ATOM    671  CG2CTHR A 118       7.978  28.648   6.539  0.33  8.73           C  
ATOM    672  N   GLY A 119       9.909  27.032   3.629  1.00 15.46           N  
ATOM    673  CA  GLY A 119       9.825  27.228   2.231  1.00 18.29           C  
ATOM    674  C   GLY A 119       9.735  25.980   1.439  1.00 16.42           C  
ATOM    675  O   GLY A 119       9.613  24.878   1.971  1.00 16.91           O  
ATOM    676  N   ASN A 120       9.784  26.196   0.135  1.00 16.03           N  
ATOM    677  CA  ASN A 120       9.602  25.101  -0.785  1.00 15.30           C  
ATOM    678  C   ASN A 120      10.598  25.115  -1.932  1.00 17.32           C  
ATOM    679  O   ASN A 120      11.261  26.117  -2.177  1.00 16.26           O  
ATOM    680  CB  ASN A 120       8.131  25.040  -1.223  1.00 16.40           C  
ATOM    681  CG  ASN A 120       7.661  26.301  -1.877  1.00 18.12           C  
ATOM    682  OD1 ASN A 120       8.288  26.750  -2.807  1.00 16.65           O  
ATOM    683  ND2 ASN A 120       6.545  26.880  -1.394  1.00 16.02           N  
ATOM    684  N   ILE A 121      10.693  23.971  -2.609  1.00 15.59           N  
ATOM    685  CA  ILE A 121      11.625  23.746  -3.674  1.00 15.62           C  
ATOM    686  C   ILE A 121      10.796  23.364  -4.869  1.00 15.57           C  
ATOM    687  O   ILE A 121       9.819  22.603  -4.761  1.00 16.86           O  
ATOM    688  CB  ILE A 121      12.570  22.542  -3.374  1.00 14.66           C  
ATOM    689  CG1 ILE A 121      13.310  22.735  -2.036  1.00 17.82           C  
ATOM    690  CG2 ILE A 121      13.542  22.308  -4.528  1.00 16.78           C  
ATOM    691  CD1 ILE A 121      13.840  21.439  -1.435  1.00 15.89           C  
ATOM    692  N   SER A 122      11.200  23.888  -6.022  1.00 14.18           N  
ATOM    693  CA  SER A 122      10.573  23.576  -7.297  1.00 17.01           C  
ATOM    694  C   SER A 122      11.645  23.814  -8.350  1.00 16.54           C  
ATOM    695  O   SER A 122      12.820  23.977  -8.000  1.00 17.39           O  
ATOM    696  CB  SER A 122       9.308  24.444  -7.488  1.00 18.09           C  
ATOM    697  OG  SER A 122       9.568  25.827  -7.339  1.00 16.53           O  
ATOM    698  N   SER A 123      11.275  23.827  -9.630  1.00 19.57           N  
ATOM    699  CA  SER A 123      12.225  24.193 -10.676  1.00 18.45           C  
ATOM    700  C   SER A 123      11.666  25.318 -11.536  1.00 20.49           C  
ATOM    701  O   SER A 123      10.450  25.484 -11.668  1.00 19.51           O  
ATOM    702  CB  SER A 123      12.585  23.005 -11.578  1.00 19.35           C  
ATOM    703  OG  SER A 123      11.421  22.481 -12.185  1.00 18.32           O  
HETATM  704  N   MSE A 124      12.585  26.110 -12.076  1.00 18.65           N  
HETATM  705  CA  MSE A 124      12.255  27.147 -13.034  1.00 22.95           C  
HETATM  706  C   MSE A 124      13.452  27.389 -13.948  1.00 26.21           C  
HETATM  707  O   MSE A 124      14.588  27.446 -13.478  1.00 26.29           O  
HETATM  708  CB  MSE A 124      11.872  28.413 -12.280  1.00 25.54           C  
HETATM  709  CG  MSE A 124      11.338  29.506 -13.116  1.00 27.19           C  
HETATM  710 SE   MSE A 124      10.382  30.819 -12.039  0.75 22.09          SE  
HETATM  711  CE  MSE A 124       9.278  31.199 -13.502  1.00 23.42           C  
ATOM    712  N   ASN A 125      13.190  27.532 -15.248  1.00 30.91           N  
ATOM    713  CA  ASN A 125      14.237  27.847 -16.241  1.00 33.86           C  
ATOM    714  C   ASN A 125      15.496  26.995 -16.075  1.00 34.60           C  
ATOM    715  O   ASN A 125      16.608  27.531 -15.953  1.00 36.48           O  
ATOM    716  CB  ASN A 125      14.595  29.339 -16.159  1.00 35.64           C  
ATOM    717  N   GLU A 126      15.288  25.676 -16.009  1.00 31.58           N  
ATOM    718  CA  GLU A 126      16.347  24.688 -15.860  1.00 31.40           C  
ATOM    719  C   GLU A 126      17.197  24.804 -14.565  1.00 30.20           C  
ATOM    720  O   GLU A 126      18.330  24.314 -14.521  1.00 31.08           O  
ATOM    721  CB  GLU A 126      17.261  24.730 -17.100  1.00 32.51           C  
ATOM    722  N   GLN A 127      16.663  25.424 -13.511  1.00 26.08           N  
ATOM    723  CA  GLN A 127      17.437  25.621 -12.307  1.00 22.64           C  
ATOM    724  C   GLN A 127      16.548  25.345 -11.106  1.00 22.37           C  
ATOM    725  O   GLN A 127      15.314  25.359 -11.223  1.00 19.49           O  
ATOM    726  CB  GLN A 127      17.978  27.052 -12.250  1.00 26.26           C  
ATOM    727  CG  GLN A 127      18.885  27.439 -13.450  1.00 28.22           C  
ATOM    728  N   VAL A 128      17.189  25.051  -9.981  1.00 20.73           N  
ATOM    729  CA  VAL A 128      16.481  24.951  -8.713  1.00 19.33           C  
ATOM    730  C   VAL A 128      15.816  26.302  -8.454  1.00 20.72           C  
ATOM    731  O   VAL A 128      16.422  27.352  -8.681  1.00 21.00           O  
ATOM    732  CB  VAL A 128      17.450  24.590  -7.543  1.00 19.16           C  
ATOM    733  CG1 VAL A 128      16.782  24.804  -6.171  1.00 21.82           C  
ATOM    734  CG2 VAL A 128      17.957  23.161  -7.684  1.00 19.39           C  
ATOM    735  N   TYR A 129      14.576  26.280  -7.948  1.00 18.44           N  
ATOM    736  CA  TYR A 129      13.871  27.487  -7.546  1.00 17.66           C  
ATOM    737  C   TYR A 129      13.465  27.311  -6.090  1.00 16.73           C  
ATOM    738  O   TYR A 129      12.733  26.385  -5.765  1.00 16.21           O  
ATOM    739  CB  TYR A 129      12.637  27.713  -8.408  1.00 16.87           C  
ATOM    740  CG  TYR A 129      12.025  29.061  -8.142  1.00 17.90           C  
ATOM    741  CD1 TYR A 129      11.042  29.236  -7.186  1.00 19.56           C  
ATOM    742  CD2 TYR A 129      12.435  30.170  -8.847  1.00 19.94           C  
ATOM    743  CE1 TYR A 129      10.473  30.465  -6.948  1.00 18.19           C  
ATOM    744  CE2 TYR A 129      11.869  31.430  -8.608  1.00 22.17           C  
ATOM    745  CZ  TYR A 129      10.888  31.567  -7.655  1.00 18.63           C  
ATOM    746  OH  TYR A 129      10.326  32.800  -7.403  1.00 21.52           O  
ATOM    747  N   LEU A 130      14.000  28.163  -5.220  1.00 17.87           N  
ATOM    748  CA  LEU A 130      13.645  28.157  -3.819  1.00 17.79           C  
ATOM    749  C   LEU A 130      12.733  29.333  -3.516  1.00 16.25           C  
ATOM    750  O   LEU A 130      12.976  30.430  -3.971  1.00 17.92           O  
ATOM    751  CB  LEU A 130      14.881  28.286  -2.944  1.00 19.95           C  
ATOM    752  CG  LEU A 130      15.902  27.180  -3.067  1.00 20.21           C  
ATOM    753  CD1 LEU A 130      16.990  27.374  -2.004  1.00 23.04           C  
ATOM    754  CD2 LEU A 130      15.228  25.851  -2.930  1.00 18.55           C  
ATOM    755  N   HIS A 131      11.667  29.093  -2.752  1.00 17.16           N  
ATOM    756  CA  HIS A 131      10.799  30.130  -2.245  1.00 16.67           C  
ATOM    757  C   HIS A 131      10.795  29.969  -0.736  1.00 15.63           C  
ATOM    758  O   HIS A 131      10.234  29.016  -0.234  1.00 16.66           O  
ATOM    759  CB  HIS A 131       9.404  29.999  -2.848  1.00 15.70           C  
ATOM    760  CG  HIS A 131       8.485  31.119  -2.505  1.00 16.03           C  
ATOM    761  ND1 HIS A 131       7.119  31.000  -2.597  1.00 17.10           N  
ATOM    762  CD2 HIS A 131       8.727  32.358  -2.001  1.00 17.16           C  
ATOM    763  CE1 HIS A 131       6.559  32.136  -2.202  1.00 20.50           C  
ATOM    764  NE2 HIS A 131       7.515  32.984  -1.857  1.00 17.92           N  
ATOM    765  N   LEU A 132      11.470  30.891  -0.059  1.00 14.80           N  
ATOM    766  CA  LEU A 132      11.733  30.798   1.362  1.00 16.46           C  
ATOM    767  C   LEU A 132      11.261  32.046   2.055  1.00 15.42           C  
ATOM    768  O   LEU A 132      11.549  33.151   1.614  1.00 14.37           O  
ATOM    769  CB  LEU A 132      13.250  30.652   1.602  1.00 15.93           C  
ATOM    770  CG  LEU A 132      13.976  29.529   0.856  1.00 17.90           C  
ATOM    771  CD1 LEU A 132      15.475  29.547   1.180  1.00 18.45           C  
ATOM    772  CD2 LEU A 132      13.330  28.171   1.172  1.00 21.68           C  
ATOM    773  N   HIS A 133      10.511  31.867   3.132  1.00 15.55           N  
ATOM    774  CA  HIS A 133      10.166  32.932   4.032  1.00 14.96           C  
ATOM    775  C   HIS A 133      10.812  32.670   5.392  1.00 15.19           C  
ATOM    776  O   HIS A 133      11.295  31.568   5.671  1.00 14.96           O  
ATOM    777  CB  HIS A 133       8.647  33.050   4.166  1.00 15.65           C  
ATOM    778  CG  HIS A 133       7.959  33.624   2.968  1.00 15.17           C  
ATOM    779  ND1 HIS A 133       6.677  34.122   3.027  1.00 16.35           N  
ATOM    780  CD2 HIS A 133       8.383  33.824   1.697  1.00 14.94           C  
ATOM    781  CE1 HIS A 133       6.339  34.576   1.826  1.00 15.72           C  
ATOM    782  NE2 HIS A 133       7.380  34.466   1.022  1.00 15.06           N  
ATOM    783  N   ILE A 134      10.845  33.677   6.245  1.00 14.46           N  
ATOM    784  CA  ILE A 134      11.577  33.557   7.474  1.00 13.96           C  
ATOM    785  C   ILE A 134      10.982  34.457   8.527  1.00 14.46           C  
ATOM    786  O   ILE A 134      10.392  35.494   8.211  1.00 14.75           O  
ATOM    787  CB  ILE A 134      13.071  33.910   7.217  1.00 14.10           C  
ATOM    788  CG1 ILE A 134      14.031  33.413   8.302  1.00 12.54           C  
ATOM    789  CG2 ILE A 134      13.278  35.449   6.954  1.00 16.39           C  
ATOM    790  CD1 ILE A 134      15.499  33.608   7.960  1.00 14.17           C  
ATOM    791  N   THR A 135      11.193  34.049   9.785  1.00 14.27           N  
ATOM    792  CA  THR A 135      10.863  34.777  10.965  1.00 13.95           C  
ATOM    793  C   THR A 135      12.114  34.787  11.802  1.00 14.50           C  
ATOM    794  O   THR A 135      12.732  33.716  12.023  1.00 14.47           O  
ATOM    795  CB  THR A 135       9.720  34.152  11.756  1.00 13.11           C  
ATOM    796  OG1 THR A 135       8.644  33.831  10.860  1.00 15.37           O  
ATOM    797  CG2 THR A 135       9.275  35.077  12.883  1.00 16.13           C  
ATOM    798  N   VAL A 136      12.516  35.972  12.221  1.00 14.88           N  
ATOM    799  CA  VAL A 136      13.691  36.144  13.049  1.00 14.12           C  
ATOM    800  C   VAL A 136      13.388  36.936  14.320  1.00 13.47           C  
ATOM    801  O   VAL A 136      12.452  37.716  14.352  1.00 14.36           O  
ATOM    802  CB  VAL A 136      14.856  36.823  12.291  1.00 16.11           C  
ATOM    803  CG1 VAL A 136      15.215  36.010  11.031  1.00 15.96           C  
ATOM    804  CG2 VAL A 136      14.518  38.285  11.964  1.00 16.42           C  
ATOM    805  N   GLY A 137      14.180  36.682  15.366  1.00 14.25           N  
ATOM    806  CA  GLY A 137      14.196  37.454  16.600  1.00 14.38           C  
ATOM    807  C   GLY A 137      15.411  38.325  16.685  1.00 14.03           C  
ATOM    808  O   GLY A 137      16.531  37.894  16.389  1.00 15.02           O  
ATOM    809  N   ARG A 138      15.195  39.552  17.123  1.00 14.62           N  
ATOM    810  CA  ARG A 138      16.284  40.505  17.356  1.00 14.72           C  
ATOM    811  C   ARG A 138      16.738  40.395  18.796  1.00 14.90           C  
ATOM    812  O   ARG A 138      16.188  39.613  19.574  1.00 15.50           O  
ATOM    813  CB  ARG A 138      15.826  41.923  17.019  1.00 15.51           C  
ATOM    814  CG  ARG A 138      15.193  42.007  15.646  1.00 17.63           C  
ATOM    815  CD  ARG A 138      14.679  43.434  15.354  1.00 15.29           C  
ATOM    816  NE  ARG A 138      15.702  44.288  14.742  1.00 15.23           N  
ATOM    817  CZ  ARG A 138      15.455  45.416  14.091  1.00 17.59           C  
ATOM    818  NH1 ARG A 138      14.250  45.920  14.041  1.00 16.95           N  
ATOM    819  NH2 ARG A 138      16.427  46.060  13.507  1.00 17.02           N  
ATOM    820  N   SER A 139      17.750  41.173  19.170  1.00 14.54           N  
ATOM    821  CA  SER A 139      18.303  41.092  20.520  1.00 15.54           C  
ATOM    822  C   SER A 139      17.318  41.538  21.596  1.00 16.07           C  
ATOM    823  O   SER A 139      17.509  41.217  22.762  1.00 17.71           O  
ATOM    824  CB  SER A 139      19.593  41.904  20.636  1.00 17.89           C  
ATOM    825  OG  SER A 139      19.319  43.263  20.475  1.00 17.18           O  
ATOM    826  N   ASP A 140      16.271  42.265  21.209  1.00 16.33           N  
ATOM    827  CA  ASP A 140      15.204  42.661  22.143  1.00 15.80           C  
ATOM    828  C   ASP A 140      14.000  41.729  22.090  1.00 15.60           C  
ATOM    829  O   ASP A 140      12.952  42.034  22.659  1.00 17.85           O  
ATOM    830  CB  ASP A 140      14.763  44.114  21.901  1.00 17.14           C  
ATOM    831  CG  ASP A 140      14.093  44.337  20.570  1.00 20.35           C  
ATOM    832  OD1 ASP A 140      14.018  43.404  19.740  1.00 16.43           O  
ATOM    833  OD2 ASP A 140      13.638  45.482  20.336  1.00 21.85           O  
ATOM    834  N   TYR A 141      14.165  40.626  21.354  1.00 14.89           N  
ATOM    835  CA  TYR A 141      13.182  39.533  21.207  1.00 16.15           C  
ATOM    836  C   TYR A 141      12.038  39.919  20.288  1.00 15.81           C  
ATOM    837  O   TYR A 141      11.194  39.071  19.988  1.00 15.71           O  
ATOM    838  CB  TYR A 141      12.660  38.979  22.555  1.00 16.80           C  
ATOM    839  CG  TYR A 141      13.800  38.634  23.475  1.00 17.59           C  
ATOM    840  CD1 TYR A 141      14.523  37.472  23.301  1.00 20.29           C  
ATOM    841  CD2 TYR A 141      14.203  39.528  24.461  1.00 18.54           C  
ATOM    842  CE1 TYR A 141      15.604  37.172  24.138  1.00 18.45           C  
ATOM    843  CE2 TYR A 141      15.291  39.256  25.264  1.00 21.75           C  
ATOM    844  CZ  TYR A 141      15.967  38.065  25.103  1.00 20.20           C  
ATOM    845  OH  TYR A 141      17.042  37.812  25.936  1.00 23.13           O  
ATOM    846  N   SER A 142      12.057  41.132  19.731  1.00 16.28           N  
ATOM    847  CA  SER A 142      11.058  41.495  18.746  1.00 14.76           C  
ATOM    848  C   SER A 142      11.289  40.678  17.488  1.00 14.99           C  
ATOM    849  O   SER A 142      12.418  40.275  17.210  1.00 15.12           O  
ATOM    850  CB  SER A 142      11.070  42.988  18.438  1.00 15.52           C  
ATOM    851  OG  SER A 142      12.274  43.392  17.789  1.00 17.04           O  
ATOM    852  N   ALA A 143      10.215  40.382  16.764  1.00 15.14           N  
ATOM    853  CA  ALA A 143      10.289  39.570  15.593  1.00 14.64           C  
ATOM    854  C   ALA A 143      10.155  40.365  14.305  1.00 16.58           C  
ATOM    855  O   ALA A 143       9.329  41.278  14.231  1.00 16.29           O  
ATOM    856  CB  ALA A 143       9.225  38.471  15.639  1.00 16.25           C  
ATOM    857  N   LEU A 144      10.930  39.958  13.299  1.00 15.36           N  
ATOM    858  CA  LEU A 144      10.796  40.433  11.922  1.00 14.94           C  
ATOM    859  C   LEU A 144      10.394  39.234  11.068  1.00 15.20           C  
ATOM    860  O   LEU A 144      10.746  38.085  11.380  1.00 15.37           O  
ATOM    861  CB  LEU A 144      12.094  41.023  11.405  1.00 15.66           C  
ATOM    862  CG  LEU A 144      12.720  42.145  12.227  1.00 15.52           C  
ATOM    863  CD1 LEU A 144      14.151  42.354  11.704  1.00 16.63           C  
ATOM    864  CD2 LEU A 144      11.921  43.423  12.165  1.00 17.82           C  
ATOM    865  N   ALA A 145       9.704  39.478   9.976  1.00 13.77           N  
ATOM    866  CA  ALA A 145       9.205  38.402   9.145  1.00 14.88           C  
ATOM    867  C   ALA A 145       9.041  38.861   7.719  1.00 13.70           C  
ATOM    868  O   ALA A 145       8.673  40.014   7.456  1.00 15.65           O  
ATOM    869  CB  ALA A 145       7.853  37.910   9.667  1.00 15.06           C  
ATOM    870  N   GLY A 146       9.261  37.928   6.796  1.00 14.32           N  
ATOM    871  CA  GLY A 146       9.048  38.207   5.408  1.00 14.28           C  
ATOM    872  C   GLY A 146       9.653  37.226   4.447  1.00 15.89           C  
ATOM    873  O   GLY A 146      10.087  36.161   4.824  1.00 16.02           O  
ATOM    874  N  AHIS A 147       9.696  37.633   3.181  0.50 14.27           N  
ATOM    875  N  BHIS A 147       9.683  37.637   3.186  0.50 14.53           N  
ATOM    876  CA AHIS A 147      10.267  36.845   2.098  0.50 13.76           C  
ATOM    877  CA BHIS A 147      10.246  36.862   2.106  0.50 14.07           C  
ATOM    878  C  AHIS A 147      11.775  36.980   2.140  0.50 14.49           C  
ATOM    879  C  BHIS A 147      11.765  36.982   2.164  0.50 14.69           C  
ATOM    880  O  AHIS A 147      12.304  38.072   2.075  0.50 15.86           O  
ATOM    881  O  BHIS A 147      12.292  38.075   2.126  0.50 15.48           O  
ATOM    882  CB AHIS A 147       9.702  37.333   0.778  0.50 14.15           C  
ATOM    883  CB BHIS A 147       9.716  37.408   0.797  0.50 14.91           C  
ATOM    884  CG AHIS A 147      10.413  36.848  -0.445  0.50 13.74           C  
ATOM    885  CG BHIS A 147      10.279  36.751  -0.413  0.50 14.82           C  
ATOM    886  ND1AHIS A 147      10.999  35.607  -0.561  0.50 14.97           N  
ATOM    887  ND1BHIS A 147       9.584  35.817  -1.149  0.50 17.81           N  
ATOM    888  CD2AHIS A 147      10.534  37.433  -1.657  0.50 12.69           C  
ATOM    889  CD2BHIS A 147      11.463  36.919  -1.036  0.50 14.14           C  
ATOM    890  CE1AHIS A 147      11.478  35.471  -1.790  0.50 13.12           C  
ATOM    891  CE1BHIS A 147      10.331  35.424  -2.165  0.50 19.11           C  
ATOM    892  NE2AHIS A 147      11.223  36.573  -2.462  0.50 16.38           N  
ATOM    893  NE2BHIS A 147      11.473  36.079  -2.121  0.50 14.83           N  
ATOM    894  N   LEU A 148      12.452  35.845   2.290  1.00 14.36           N  
ATOM    895  CA  LEU A 148      13.887  35.797   2.441  1.00 15.35           C  
ATOM    896  C   LEU A 148      14.637  35.853   1.128  1.00 14.42           C  
ATOM    897  O   LEU A 148      14.395  35.031   0.237  1.00 15.13           O  
ATOM    898  CB  LEU A 148      14.271  34.488   3.141  1.00 15.41           C  
ATOM    899  CG  LEU A 148      15.749  34.194   3.313  1.00 14.07           C  
ATOM    900  CD1 LEU A 148      16.443  35.234   4.234  1.00 16.83           C  
ATOM    901  CD2 LEU A 148      15.928  32.764   3.834  1.00 14.72           C  
ATOM    902  N   LEU A 149      15.561  36.802   1.007  1.00 13.11           N  
ATOM    903  CA  LEU A 149      16.510  36.836  -0.120  1.00 14.15           C  
ATOM    904  C   LEU A 149      17.870  36.265   0.221  1.00 15.37           C  
ATOM    905  O   LEU A 149      18.474  35.570  -0.591  1.00 16.30           O  
ATOM    906  CB  LEU A 149      16.717  38.263  -0.635  1.00 15.32           C  
ATOM    907  CG  LEU A 149      15.486  38.959  -1.230  1.00 17.83           C  
ATOM    908  CD1 LEU A 149      15.934  40.277  -1.854  1.00 16.51           C  
ATOM    909  CD2 LEU A 149      14.768  38.059  -2.270  1.00 16.39           C  
ATOM    910  N  ASER A 150      18.350  36.572   1.415  0.50 14.75           N  
ATOM    911  N  BSER A 150      18.357  36.569   1.419  0.50 14.27           N  
ATOM    912  CA ASER A 150      19.646  36.095   1.854  0.50 15.13           C  
ATOM    913  CA BSER A 150      19.730  36.260   1.808  0.50 14.42           C  
ATOM    914  C  ASER A 150      19.805  36.256   3.343  0.50 15.66           C  
ATOM    915  C  BSER A 150      19.898  36.353   3.314  0.50 14.98           C  
ATOM    916  O  ASER A 150      19.095  37.032   3.976  0.50 15.76           O  
ATOM    917  O  BSER A 150      19.266  37.194   3.939  0.50 14.45           O  
ATOM    918  CB ASER A 150      20.754  36.876   1.159  0.50 15.82           C  
ATOM    919  CB BSER A 150      20.651  37.278   1.124  0.50 14.10           C  
ATOM    920  OG ASER A 150      20.724  38.245   1.514  0.50 17.44           O  
ATOM    921  OG BSER A 150      22.030  37.108   1.444  0.50 16.50           O  
ATOM    922  N   ALA A 151      20.733  35.493   3.901  1.00 15.47           N  
ATOM    923  CA  ALA A 151      21.056  35.582   5.313  1.00 15.25           C  
ATOM    924  C   ALA A 151      22.422  34.960   5.520  1.00 15.89           C  
ATOM    925  O   ALA A 151      22.664  33.882   5.008  1.00 17.66           O  
ATOM    926  CB  ALA A 151      20.032  34.888   6.175  1.00 17.13           C  
ATOM    927  N   ILE A 152      23.284  35.620   6.283  1.00 17.75           N  
ATOM    928  CA  ILE A 152      24.629  35.115   6.568  1.00 16.60           C  
ATOM    929  C   ILE A 152      24.649  34.503   7.959  1.00 15.59           C  
ATOM    930  O   ILE A 152      24.431  35.203   8.952  1.00 14.60           O  
ATOM    931  CB  ILE A 152      25.691  36.228   6.475  1.00 15.24           C  
ATOM    932  CG1 ILE A 152      25.683  36.850   5.067  1.00 18.50           C  
ATOM    933  CG2 ILE A 152      27.087  35.670   6.828  1.00 16.56           C  
ATOM    934  CD1 ILE A 152      26.600  38.096   4.925  1.00 20.80           C  
ATOM    935  N   GLN A 153      24.917  33.201   8.027  1.00 14.68           N  
ATOM    936  CA  GLN A 153      24.981  32.509   9.289  1.00 15.06           C  
ATOM    937  C   GLN A 153      26.061  33.050  10.215  1.00 16.02           C  
ATOM    938  O   GLN A 153      27.154  33.402   9.789  1.00 15.35           O  
ATOM    939  CB  GLN A 153      25.180  31.031   9.023  1.00 14.81           C  
ATOM    940  CG  GLN A 153      25.114  30.123  10.240  1.00 15.57           C  
ATOM    941  CD  GLN A 153      25.027  28.711   9.849  1.00 19.70           C  
ATOM    942  OE1 GLN A 153      24.276  28.364   8.940  1.00 18.70           O  
ATOM    943  NE2 GLN A 153      25.771  27.868  10.531  1.00 19.54           N  
ATOM    944  N   ASN A 154      25.720  33.105  11.489  1.00 16.99           N  
ATOM    945  CA  ASN A 154      26.650  33.470  12.552  1.00 15.01           C  
ATOM    946  C   ASN A 154      26.245  32.674  13.790  1.00 15.43           C  
ATOM    947  O   ASN A 154      25.571  33.170  14.699  1.00 16.91           O  
ATOM    948  CB  ASN A 154      26.653  34.976  12.800  1.00 15.73           C  
ATOM    949  CG  ASN A 154      27.852  35.399  13.600  1.00 20.62           C  
ATOM    950  OD1 ASN A 154      28.941  34.860  13.398  1.00 20.61           O  
ATOM    951  ND2 ASN A 154      27.668  36.325  14.532  1.00 19.57           N  
ATOM    952  N   GLY A 155      26.673  31.414  13.799  1.00 16.05           N  
ATOM    953  CA  GLY A 155      26.267  30.426  14.801  1.00 16.41           C  
ATOM    954  C   GLY A 155      25.950  29.146  14.046  1.00 16.88           C  
ATOM    955  O   GLY A 155      26.705  28.751  13.148  1.00 18.49           O  
ATOM    956  N   ALA A 156      24.825  28.521  14.382  1.00 16.48           N  
ATOM    957  CA  ALA A 156      24.374  27.266  13.804  1.00 17.78           C  
ATOM    958  C   ALA A 156      23.386  27.506  12.701  1.00 16.68           C  
ATOM    959  O   ALA A 156      22.774  28.585  12.609  1.00 17.70           O  
ATOM    960  CB  ALA A 156      23.719  26.415  14.901  1.00 18.84           C  
ATOM    961  N   GLY A 157      23.191  26.486  11.880  1.00 16.69           N  
ATOM    962  CA  GLY A 157      22.237  26.523  10.784  1.00 15.51           C  
ATOM    963  C   GLY A 157      21.767  25.115  10.497  1.00 16.14           C  
ATOM    964  O   GLY A 157      22.505  24.325   9.894  1.00 16.29           O  
ATOM    965  N   GLU A 158      20.563  24.796  10.958  1.00 16.07           N  
ATOM    966  CA  GLU A 158      20.076  23.411  11.067  1.00 16.24           C  
ATOM    967  C   GLU A 158      18.776  23.299  10.319  1.00 14.33           C  
ATOM    968  O   GLU A 158      17.769  23.824  10.763  1.00 14.56           O  
ATOM    969  CB  GLU A 158      19.899  23.083  12.546  1.00 16.11           C  
ATOM    970  CG  GLU A 158      21.222  23.160  13.310  1.00 16.21           C  
ATOM    971  CD  GLU A 158      21.101  23.013  14.809  1.00 17.28           C  
ATOM    972  OE1 GLU A 158      20.024  22.606  15.296  1.00 18.18           O  
ATOM    973  OE2 GLU A 158      22.119  23.282  15.488  1.00 16.95           O  
ATOM    974  N   PHE A 159      18.809  22.656   9.155  1.00 16.80           N  
ATOM    975  CA  PHE A 159      17.682  22.633   8.238  1.00 16.41           C  
ATOM    976  C   PHE A 159      17.320  21.230   7.837  1.00 20.02           C  
ATOM    977  O   PHE A 159      18.196  20.366   7.773  1.00 23.54           O  
ATOM    978  CB  PHE A 159      17.997  23.487   6.999  1.00 17.74           C  
ATOM    979  CG  PHE A 159      18.318  24.889   7.362  1.00 16.48           C  
ATOM    980  CD1 PHE A 159      17.294  25.779   7.630  1.00 19.61           C  
ATOM    981  CD2 PHE A 159      19.615  25.306   7.536  1.00 19.39           C  
ATOM    982  CE1 PHE A 159      17.567  27.056   8.042  1.00 20.24           C  
ATOM    983  CE2 PHE A 159      19.889  26.590   7.935  1.00 19.56           C  
ATOM    984  CZ  PHE A 159      18.872  27.461   8.208  1.00 18.10           C  
ATOM    985  N   VAL A 160      16.030  20.988   7.659  1.00 15.74           N  
ATOM    986  CA  VAL A 160      15.533  19.711   7.174  1.00 17.18           C  
ATOM    987  C   VAL A 160      15.037  19.956   5.748  1.00 17.15           C  
ATOM    988  O   VAL A 160      14.176  20.831   5.523  1.00 16.62           O  
ATOM    989  CB  VAL A 160      14.408  19.145   8.046  1.00 16.47           C  
ATOM    990  CG1 VAL A 160      13.931  17.794   7.487  1.00 18.19           C  
ATOM    991  CG2 VAL A 160      14.896  18.977   9.502  1.00 19.65           C  
ATOM    992  N   VAL A 161      15.595  19.217   4.798  1.00 15.66           N  
ATOM    993  CA  VAL A 161      15.218  19.329   3.374  1.00 15.95           C  
ATOM    994  C   VAL A 161      14.545  18.029   2.990  1.00 16.56           C  
ATOM    995  O   VAL A 161      15.184  16.976   3.093  1.00 17.61           O  
ATOM    996  CB  VAL A 161      16.411  19.566   2.477  1.00 15.51           C  
ATOM    997  CG1 VAL A 161      15.982  19.631   0.982  1.00 20.06           C  
ATOM    998  CG2 VAL A 161      17.148  20.820   2.879  1.00 16.31           C  
ATOM    999  N   GLU A 162      13.267  18.083   2.632  1.00 16.70           N  
ATOM   1000  CA  GLU A 162      12.549  16.911   2.164  1.00 18.22           C  
ATOM   1001  C   GLU A 162      12.557  16.920   0.650  1.00 18.22           C  
ATOM   1002  O   GLU A 162      12.278  17.941   0.038  1.00 16.81           O  
ATOM   1003  CB  GLU A 162      11.111  16.879   2.637  1.00 18.93           C  
ATOM   1004  CG  GLU A 162      10.403  15.587   2.225  1.00 26.03           C  
ATOM   1005  CD  GLU A 162       9.004  15.447   2.780  1.00 30.38           C  
ATOM   1006  OE1 GLU A 162       8.603  16.272   3.633  1.00 38.91           O  
ATOM   1007  OE2 GLU A 162       8.302  14.506   2.347  1.00 37.54           O  
ATOM   1008  N   ASP A 163      12.839  15.761   0.080  1.00 16.86           N  
ATOM   1009  CA  ASP A 163      12.871  15.550  -1.360  1.00 16.61           C  
ATOM   1010  C   ASP A 163      11.593  14.809  -1.762  1.00 16.96           C  
ATOM   1011  O   ASP A 163      11.354  13.694  -1.308  1.00 18.80           O  
ATOM   1012  CB  ASP A 163      14.099  14.725  -1.697  1.00 16.26           C  
ATOM   1013  CG  ASP A 163      14.256  14.460  -3.164  1.00 16.24           C  
ATOM   1014  OD1 ASP A 163      13.484  14.940  -4.009  1.00 17.83           O  
ATOM   1015  OD2 ASP A 163      15.205  13.699  -3.479  1.00 18.84           O  
ATOM   1016  N   TYR A 164      10.755  15.462  -2.569  1.00 16.23           N  
ATOM   1017  CA  TYR A 164       9.530  14.846  -3.060  1.00 16.42           C  
ATOM   1018  C   TYR A 164       9.743  13.888  -4.224  1.00 18.31           C  
ATOM   1019  O   TYR A 164       8.834  13.144  -4.535  1.00 19.75           O  
ATOM   1020  CB  TYR A 164       8.513  15.890  -3.496  1.00 17.80           C  
ATOM   1021  CG  TYR A 164       8.042  16.849  -2.427  1.00 15.75           C  
ATOM   1022  CD1 TYR A 164       8.031  16.517  -1.079  1.00 17.41           C  
ATOM   1023  CD2 TYR A 164       7.516  18.087  -2.785  1.00 20.58           C  
ATOM   1024  CE1 TYR A 164       7.567  17.413  -0.123  1.00 17.74           C  
ATOM   1025  CE2 TYR A 164       7.053  18.967  -1.847  1.00 19.36           C  
ATOM   1026  CZ  TYR A 164       7.081  18.628  -0.526  1.00 18.13           C  
ATOM   1027  OH  TYR A 164       6.613  19.510   0.401  1.00 18.75           O  
ATOM   1028  N   SER A 165      10.907  13.922  -4.871  1.00 19.14           N  
ATOM   1029  CA  SER A 165      11.182  13.060  -6.023  1.00 18.13           C  
ATOM   1030  C   SER A 165      10.168  13.226  -7.154  1.00 19.42           C  
ATOM   1031  O   SER A 165       9.860  12.262  -7.859  1.00 20.41           O  
ATOM   1032  CB  SER A 165      11.266  11.573  -5.591  1.00 18.34           C  
ATOM   1033  OG  SER A 165      12.290  11.381  -4.654  1.00 24.25           O  
ATOM   1034  N  AGLU A 166       9.652  14.433  -7.328  0.80 20.37           N  
ATOM   1035  N  BGLU A 166       9.677  14.448  -7.336  0.20 19.88           N  
ATOM   1036  CA AGLU A 166       8.672  14.733  -8.374  0.80 21.91           C  
ATOM   1037  CA BGLU A 166       8.660  14.767  -8.334  0.20 20.46           C  
ATOM   1038  C  AGLU A 166       8.924  16.137  -8.895  0.80 21.83           C  
ATOM   1039  C  BGLU A 166       8.909  16.162  -8.885  0.20 20.31           C  
ATOM   1040  O  AGLU A 166       9.360  17.006  -8.157  0.80 21.19           O  
ATOM   1041  O  BGLU A 166       9.370  17.041  -8.160  0.20 20.18           O  
ATOM   1042  CB AGLU A 166       7.254  14.725  -7.822  0.80 24.92           C  
ATOM   1043  CB BGLU A 166       7.271  14.718  -7.700  0.20 21.52           C  
ATOM   1044  CG AGLU A 166       6.751  13.430  -7.257  0.80 31.65           C  
ATOM   1045  CG BGLU A 166       6.583  13.369  -7.767  0.20 23.68           C  
ATOM   1046  CD AGLU A 166       6.315  12.438  -8.296  0.80 39.86           C  
ATOM   1047  CD BGLU A 166       5.902  13.120  -9.099  0.20 26.79           C  
ATOM   1048  OE1AGLU A 166       6.480  12.709  -9.506  0.80 49.68           O  
ATOM   1049  OE1BGLU A 166       6.211  12.092  -9.744  0.20 31.50           O  
ATOM   1050  OE2AGLU A 166       5.793  11.377  -7.889  0.80 44.50           O  
ATOM   1051  OE2BGLU A 166       5.062  13.951  -9.503  0.20 27.78           O  
ATOM   1052  N   ARG A 167       8.596  16.366 -10.161  1.00 19.35           N  
ATOM   1053  CA  ARG A 167       8.750  17.685 -10.778  1.00 19.21           C  
ATOM   1054  C   ARG A 167       7.633  18.619 -10.338  1.00 19.72           C  
ATOM   1055  O   ARG A 167       6.482  18.214 -10.297  1.00 19.63           O  
ATOM   1056  CB  ARG A 167       8.717  17.564 -12.305  1.00 18.33           C  
ATOM   1057  CG  ARG A 167       8.593  18.875 -13.096  1.00 18.95           C  
ATOM   1058  CD  ARG A 167       8.604  18.595 -14.581  1.00 19.28           C  
ATOM   1059  NE  ARG A 167       8.435  19.819 -15.368  1.00 20.51           N  
ATOM   1060  CZ  ARG A 167       9.402  20.699 -15.625  1.00 26.35           C  
ATOM   1061  NH1 ARG A 167      10.624  20.514 -15.137  1.00 26.20           N  
ATOM   1062  NH2 ARG A 167       9.151  21.770 -16.380  1.00 21.49           N  
ATOM   1063  N   ILE A 168       7.987  19.849  -9.971  1.00 19.54           N  
ATOM   1064  CA  ILE A 168       7.008  20.940  -9.768  1.00 18.72           C  
ATOM   1065  C   ILE A 168       7.681  22.166 -10.343  1.00 19.17           C  
ATOM   1066  O   ILE A 168       8.767  22.537  -9.909  1.00 17.83           O  
ATOM   1067  CB  ILE A 168       6.625  21.221  -8.310  1.00 20.37           C  
ATOM   1068  CG1 ILE A 168       6.009  19.982  -7.654  1.00 20.51           C  
ATOM   1069  CG2 ILE A 168       5.631  22.382  -8.252  1.00 20.67           C  
ATOM   1070  CD1 ILE A 168       5.661  20.189  -6.177  1.00 18.70           C  
ATOM   1071  N   SER A 169       7.066  22.765 -11.353  1.00 18.92           N  
ATOM   1072  CA  SER A 169       7.611  23.932 -12.029  1.00 19.92           C  
ATOM   1073  C   SER A 169       6.811  25.164 -11.659  1.00 20.00           C  
ATOM   1074  O   SER A 169       5.953  25.146 -10.759  1.00 20.70           O  
ATOM   1075  CB  SER A 169       7.613  23.720 -13.552  1.00 19.38           C  
ATOM   1076  OG  SER A 169       8.308  24.756 -14.267  1.00 20.66           O  
ATOM   1077  N   ARG A 170       7.152  26.256 -12.326  1.00 19.86           N  
ATOM   1078  CA  ARG A 170       6.529  27.530 -12.104  1.00 21.62           C  
ATOM   1079  C   ARG A 170       6.460  28.315 -13.373  1.00 19.90           C  
ATOM   1080  O   ARG A 170       7.261  28.123 -14.284  1.00 18.98           O  
ATOM   1081  CB  ARG A 170       7.354  28.324 -11.126  1.00 23.16           C  
ATOM   1082  CG  ARG A 170       7.183  27.817  -9.740  1.00 25.98           C  
ATOM   1083  CD  ARG A 170       7.783  28.742  -8.832  1.00 19.83           C  
ATOM   1084  NE  ARG A 170       7.862  28.201  -7.498  1.00 17.88           N  
ATOM   1085  CZ  ARG A 170       7.061  28.508  -6.495  1.00 18.10           C  
ATOM   1086  NH1 ARG A 170       6.061  29.312  -6.663  1.00 17.32           N  
ATOM   1087  NH2 ARG A 170       7.298  27.988  -5.301  1.00 18.12           N  
ATOM   1088  N   THR A 171       5.520  29.249 -13.395  1.00 18.43           N  
ATOM   1089  CA  THR A 171       5.336  30.127 -14.531  1.00 17.60           C  
ATOM   1090  C   THR A 171       5.178  31.530 -14.016  1.00 16.42           C  
ATOM   1091  O   THR A 171       4.371  31.779 -13.099  1.00 17.75           O  
ATOM   1092  CB  THR A 171       4.095  29.729 -15.316  1.00 17.37           C  
ATOM   1093  OG1 THR A 171       4.336  28.449 -15.878  1.00 20.26           O  
ATOM   1094  CG2 THR A 171       3.763  30.734 -16.439  1.00 20.01           C  
ATOM   1095  N   TYR A 172       5.938  32.456 -14.583  1.00 15.98           N  
ATOM   1096  CA  TYR A 172       5.832  33.863 -14.220  1.00 15.90           C  
ATOM   1097  C   TYR A 172       4.514  34.395 -14.762  1.00 17.77           C  
ATOM   1098  O   TYR A 172       4.227  34.284 -15.948  1.00 18.38           O  
ATOM   1099  CB  TYR A 172       7.018  34.648 -14.776  1.00 17.85           C  
ATOM   1100  CG  TYR A 172       7.011  36.133 -14.500  1.00 18.73           C  
ATOM   1101  CD1 TYR A 172       7.482  36.650 -13.303  1.00 20.70           C  
ATOM   1102  CD2 TYR A 172       6.554  37.018 -15.436  1.00 23.60           C  
ATOM   1103  CE1 TYR A 172       7.479  38.024 -13.057  1.00 22.97           C  
ATOM   1104  CE2 TYR A 172       6.568  38.377 -15.212  1.00 20.62           C  
ATOM   1105  CZ  TYR A 172       7.036  38.868 -14.006  1.00 23.44           C  
ATOM   1106  OH  TYR A 172       7.057  40.226 -13.776  1.00 26.85           O  
ATOM   1107  N   ASN A 173       3.699  34.928 -13.872  1.00 18.08           N  
ATOM   1108  CA  ASN A 173       2.439  35.568 -14.195  1.00 19.54           C  
ATOM   1109  C   ASN A 173       2.742  37.044 -14.406  1.00 20.03           C  
ATOM   1110  O   ASN A 173       3.010  37.748 -13.438  1.00 19.80           O  
ATOM   1111  CB  ASN A 173       1.439  35.352 -13.073  1.00 18.37           C  
ATOM   1112  CG  ASN A 173       0.116  35.992 -13.359  1.00 20.53           C  
ATOM   1113  OD1 ASN A 173       0.052  37.031 -13.992  1.00 24.84           O  
ATOM   1114  ND2 ASN A 173      -0.960  35.354 -12.923  1.00 23.55           N  
ATOM   1115  N   PRO A 174       2.710  37.536 -15.659  1.00 20.12           N  
ATOM   1116  CA  PRO A 174       3.109  38.907 -15.902  1.00 22.21           C  
ATOM   1117  C   PRO A 174       2.143  39.937 -15.346  1.00 23.91           C  
ATOM   1118  O   PRO A 174       2.552  41.081 -15.110  1.00 28.78           O  
ATOM   1119  CB  PRO A 174       3.191  38.985 -17.429  1.00 21.95           C  
ATOM   1120  CG  PRO A 174       2.303  37.975 -17.912  1.00 20.09           C  
ATOM   1121  CD  PRO A 174       2.320  36.859 -16.904  1.00 18.53           C  
ATOM   1122  N   ASP A 175       0.903  39.542 -15.107  1.00 22.03           N  
ATOM   1123  CA  ASP A 175      -0.067  40.456 -14.498  1.00 25.63           C  
ATOM   1124  C   ASP A 175       0.223  40.684 -13.020  1.00 25.58           C  
ATOM   1125  O   ASP A 175       0.063  41.791 -12.547  1.00 27.40           O  
ATOM   1126  CB  ASP A 175      -1.480  39.923 -14.634  1.00 27.91           C  
ATOM   1127  CG  ASP A 175      -1.893  39.732 -16.092  1.00 39.23           C  
ATOM   1128  OD1 ASP A 175      -1.511  40.577 -16.939  1.00 43.53           O  
ATOM   1129  OD2 ASP A 175      -2.575  38.723 -16.377  1.00 48.35           O  
ATOM   1130  N   LEU A 176       0.635  39.646 -12.300  1.00 21.87           N  
ATOM   1131  CA  LEU A 176       1.017  39.793 -10.904  1.00 20.94           C  
ATOM   1132  C   LEU A 176       2.477  40.179 -10.699  1.00 21.96           C  
ATOM   1133  O   LEU A 176       2.820  40.828  -9.710  1.00 22.60           O  
ATOM   1134  CB  LEU A 176       0.793  38.487 -10.148  1.00 21.27           C  
ATOM   1135  CG  LEU A 176      -0.623  37.946 -10.123  1.00 24.44           C  
ATOM   1136  CD1 LEU A 176      -0.640  36.684  -9.246  1.00 23.69           C  
ATOM   1137  CD2 LEU A 176      -1.600  39.009  -9.616  1.00 25.19           C  
ATOM   1138  N   GLY A 177       3.350  39.735 -11.580  1.00 19.53           N  
ATOM   1139  CA  GLY A 177       4.778  39.908 -11.386  1.00 19.91           C  
ATOM   1140  C   GLY A 177       5.386  38.887 -10.453  1.00 19.94           C  
ATOM   1141  O   GLY A 177       6.390  39.183  -9.801  1.00 21.72           O  
ATOM   1142  N   LEU A 178       4.761  37.704 -10.364  1.00 17.23           N  
ATOM   1143  CA  LEU A 178       5.180  36.637  -9.471  1.00 17.70           C  
ATOM   1144  C   LEU A 178       5.310  35.297 -10.188  1.00 17.38           C  
ATOM   1145  O   LEU A 178       4.615  35.020 -11.164  1.00 16.99           O  
ATOM   1146  CB  LEU A 178       4.162  36.481  -8.364  1.00 18.17           C  
ATOM   1147  CG  LEU A 178       3.949  37.711  -7.482  1.00 18.92           C  
ATOM   1148  CD1 LEU A 178       2.842  37.443  -6.471  1.00 21.23           C  
ATOM   1149  CD2 LEU A 178       5.247  38.122  -6.793  1.00 21.84           C  
ATOM   1150  N   ASN A 179       6.200  34.467  -9.671  1.00 17.31           N  
ATOM   1151  CA  ASN A 179       6.408  33.123 -10.169  1.00 16.55           C  
ATOM   1152  C   ASN A 179       5.482  32.175  -9.414  1.00 17.93           C  
ATOM   1153  O   ASN A 179       5.711  31.854  -8.258  1.00 17.99           O  
ATOM   1154  CB  ASN A 179       7.856  32.728  -9.948  1.00 16.18           C  
ATOM   1155  CG  ASN A 179       8.803  33.619 -10.692  1.00 19.90           C  
ATOM   1156  OD1 ASN A 179       8.602  33.880 -11.867  1.00 21.73           O  
ATOM   1157  ND2 ASN A 179       9.850  34.054 -10.027  1.00 20.86           N  
ATOM   1158  N   ILE A 180       4.456  31.701 -10.102  1.00 15.50           N  
ATOM   1159  CA  ILE A 180       3.380  30.921  -9.488  1.00 17.44           C  
ATOM   1160  C   ILE A 180       3.513  29.445  -9.820  1.00 17.38           C  
ATOM   1161  O   ILE A 180       3.884  29.085 -10.933  1.00 17.86           O  
ATOM   1162  CB  ILE A 180       1.990  31.479  -9.980  1.00 19.39           C  
ATOM   1163  CG1 ILE A 180       1.810  32.953  -9.579  1.00 21.48           C  
ATOM   1164  CG2 ILE A 180       0.792  30.673  -9.468  1.00 19.75           C  
ATOM   1165  CD1 ILE A 180       1.897  33.237  -8.104  1.00 20.52           C  
ATOM   1166  N   TYR A 181       3.254  28.576  -8.852  1.00 16.46           N  
ATOM   1167  CA  TYR A 181       3.273  27.150  -9.100  1.00 18.37           C  
ATOM   1168  C   TYR A 181       2.540  26.811 -10.401  1.00 18.58           C  
ATOM   1169  O   TYR A 181       1.446  27.315 -10.663  1.00 16.74           O  
ATOM   1170  CB  TYR A 181       2.609  26.400  -7.952  1.00 16.85           C  
ATOM   1171  CG  TYR A 181       3.442  26.014  -6.769  1.00 16.74           C  
ATOM   1172  CD1 TYR A 181       4.759  25.557  -6.904  1.00 18.47           C  
ATOM   1173  CD2 TYR A 181       2.843  25.931  -5.521  1.00 17.63           C  
ATOM   1174  CE1 TYR A 181       5.475  25.118  -5.801  1.00 17.84           C  
ATOM   1175  CE2 TYR A 181       3.536  25.476  -4.433  1.00 16.40           C  
ATOM   1176  CZ  TYR A 181       4.853  25.062  -4.590  1.00 17.04           C  
ATOM   1177  OH  TYR A 181       5.575  24.553  -3.546  1.00 17.74           O  
ATOM   1178  N   ASP A 182       3.149  25.939 -11.195  1.00 19.09           N  
ATOM   1179  CA  ASP A 182       2.552  25.446 -12.430  1.00 21.01           C  
ATOM   1180  C   ASP A 182       2.706  23.933 -12.402  1.00 21.86           C  
ATOM   1181  O   ASP A 182       3.825  23.416 -12.559  1.00 23.54           O  
ATOM   1182  CB  ASP A 182       3.244  26.076 -13.621  1.00 18.93           C  
ATOM   1183  CG  ASP A 182       2.559  25.755 -14.922  1.00 22.67           C  
ATOM   1184  OD1 ASP A 182       2.021  24.642 -15.043  1.00 26.07           O  
ATOM   1185  OD2 ASP A 182       2.545  26.617 -15.820  1.00 21.79           O  
ATOM   1186  N   PHE A 183       1.601  23.238 -12.137  1.00 20.57           N  
ATOM   1187  CA  PHE A 183       1.626  21.792 -12.000  1.00 20.93           C  
ATOM   1188  C   PHE A 183       1.516  21.089 -13.361  1.00 20.48           C  
ATOM   1189  O   PHE A 183       1.614  19.875 -13.428  1.00 21.18           O  
ATOM   1190  CB  PHE A 183       0.497  21.314 -11.072  1.00 20.53           C  
ATOM   1191  CG  PHE A 183       0.534  21.926  -9.663  1.00 18.66           C  
ATOM   1192  CD1 PHE A 183       1.697  21.915  -8.895  1.00 20.84           C  
ATOM   1193  CD2 PHE A 183      -0.603  22.503  -9.124  1.00 22.38           C  
ATOM   1194  CE1 PHE A 183       1.715  22.472  -7.610  1.00 20.85           C  
ATOM   1195  CE2 PHE A 183      -0.602  23.048  -7.851  1.00 21.52           C  
ATOM   1196  CZ  PHE A 183       0.560  23.040  -7.085  1.00 19.21           C  
ATOM   1197  N   GLU A 184       1.342  21.844 -14.441  1.00 20.44           N  
ATOM   1198  CA  GLU A 184       1.231  21.285 -15.793  1.00 19.71           C  
ATOM   1199  C   GLU A 184       2.520  21.244 -16.587  1.00 23.26           C  
ATOM   1200  O   GLU A 184       2.745  20.290 -17.351  1.00 23.92           O  
ATOM   1201  CB  GLU A 184       0.245  22.106 -16.600  1.00 22.14           C  
ATOM   1202  CG  GLU A 184      -1.127  22.275 -15.986  1.00 27.94           C  
ATOM   1203  CD  GLU A 184      -1.856  20.983 -15.820  1.00 35.84           C  
ATOM   1204  OE1 GLU A 184      -1.807  20.144 -16.754  1.00 43.61           O  
ATOM   1205  OE2 GLU A 184      -2.479  20.801 -14.753  1.00 47.52           O  
ATOM   1206  N   ARG A 185       3.349  22.276 -16.470  1.00 21.79           N  
ATOM   1207  CA  ARG A 185       4.506  22.374 -17.351  1.00 24.30           C  
ATOM   1208  C   ARG A 185       5.650  21.456 -16.906  1.00 24.90           C  
ATOM   1209  O   ARG A 185       5.729  20.937 -15.787  1.00 25.76           O  
ATOM   1210  CB  ARG A 185       4.974  23.835 -17.532  1.00 26.61           C  
ATOM   1211  CG  ARG A 185       5.748  24.408 -16.399  1.00 22.73           C  
ATOM   1212  CD  ARG A 185       6.038  25.892 -16.607  1.00 22.89           C  
ATOM   1213  NE  ARG A 185       7.136  26.182 -17.545  1.00 17.67           N  
ATOM   1214  CZ  ARG A 185       7.362  27.395 -18.069  1.00 24.11           C  
ATOM   1215  NH1 ARG A 185       6.569  28.413 -17.812  1.00 19.44           N  
ATOM   1216  NH2 ARG A 185       8.370  27.582 -18.915  1.00 23.93           N  
ATOM   1217  OXT ARG A 185       6.540  21.240 -17.725  1.00 25.26           O  
TER    1218      ARG A 185                                                      
ATOM   1219  N   ASN B  43       2.782  12.515  34.985  1.00 40.49           N  
ATOM   1220  CA  ASN B  43       2.078  12.657  33.671  1.00 38.72           C  
ATOM   1221  C   ASN B  43       2.102  14.094  33.133  1.00 33.44           C  
ATOM   1222  O   ASN B  43       1.606  15.019  33.790  1.00 36.87           O  
ATOM   1223  CB  ASN B  43       0.624  12.210  33.754  1.00 41.36           C  
ATOM   1224  CG  ASN B  43      -0.046  12.202  32.384  1.00 44.02           C  
ATOM   1225  OD1 ASN B  43      -0.916  13.023  32.101  1.00 42.27           O  
ATOM   1226  ND2 ASN B  43       0.393  11.290  31.514  1.00 50.67           N  
HETATM 1227  N  AMSE B  44       2.692  14.287  31.955  0.50 28.47           N  
HETATM 1228  N  BMSE B  44       2.671  14.256  31.943  0.50 28.70           N  
HETATM 1229  CA AMSE B  44       2.772  15.615  31.336  0.50 23.15           C  
HETATM 1230  CA BMSE B  44       2.836  15.563  31.326  0.50 23.53           C  
HETATM 1231  C  AMSE B  44       2.157  15.712  29.940  0.50 20.18           C  
HETATM 1232  C  BMSE B  44       2.179  15.699  29.950  0.50 20.34           C  
HETATM 1233  O  AMSE B  44       2.060  16.815  29.409  0.50 18.69           O  
HETATM 1234  O  BMSE B  44       2.077  16.813  29.448  0.50 18.55           O  
HETATM 1235  CB AMSE B  44       4.235  16.077  31.287  0.50 22.50           C  
HETATM 1236  CB BMSE B  44       4.335  15.858  31.206  0.50 23.39           C  
HETATM 1237  CG AMSE B  44       4.757  16.567  32.632  0.50 19.36           C  
HETATM 1238  CG BMSE B  44       5.120  15.594  32.511  0.50 22.09           C  
HETATM 1239 SE  AMSE B  44       6.632  17.052  32.513  0.38 22.56          SE  
HETATM 1240 SE  BMSE B  44       6.975  16.039  32.341  0.37 21.93          SE  
HETATM 1241  CE AMSE B  44       7.323  15.168  32.346  0.50 28.38           C  
HETATM 1242  CE BMSE B  44       6.674  17.935  32.209  0.50 19.21           C  
ATOM   1243  N   TYR B  45       1.704  14.598  29.366  1.00 16.95           N  
ATOM   1244  CA  TYR B  45       1.167  14.615  28.016  1.00 16.60           C  
ATOM   1245  C   TYR B  45       0.389  13.362  27.685  1.00 16.80           C  
ATOM   1246  O   TYR B  45       0.409  12.371  28.434  1.00 16.58           O  
ATOM   1247  CB  TYR B  45       2.325  14.731  26.987  1.00 18.19           C  
ATOM   1248  CG  TYR B  45       3.443  13.743  27.256  1.00 19.13           C  
ATOM   1249  CD1 TYR B  45       3.330  12.394  26.904  1.00 20.02           C  
ATOM   1250  CD2 TYR B  45       4.595  14.151  27.908  1.00 19.28           C  
ATOM   1251  CE1 TYR B  45       4.329  11.503  27.209  1.00 21.00           C  
ATOM   1252  CE2 TYR B  45       5.598  13.261  28.203  1.00 21.37           C  
ATOM   1253  CZ  TYR B  45       5.460  11.961  27.858  1.00 20.52           C  
ATOM   1254  OH  TYR B  45       6.469  11.080  28.174  1.00 24.83           O  
ATOM   1255  N  ASER B  46      -0.307  13.421  26.555  0.50 16.87           N  
ATOM   1256  N  BSER B  46      -0.287  13.441  26.543  0.50 17.36           N  
ATOM   1257  CA ASER B  46      -0.942  12.265  25.932  0.50 17.61           C  
ATOM   1258  CA BSER B  46      -0.949  12.325  25.893  0.50 18.54           C  
ATOM   1259  C  ASER B  46      -0.507  12.318  24.475  0.50 17.44           C  
ATOM   1260  C  BSER B  46      -0.385  12.304  24.481  0.50 17.66           C  
ATOM   1261  O  ASER B  46      -0.177  13.386  23.957  0.50 16.66           O  
ATOM   1262  O  BSER B  46       0.183  13.301  23.993  0.50 16.26           O  
ATOM   1263  CB ASER B  46      -2.466  12.302  26.055  0.50 18.56           C  
ATOM   1264  CB BSER B  46      -2.463  12.521  25.836  0.50 20.14           C  
ATOM   1265  OG ASER B  46      -3.018  13.449  25.420  0.50 19.09           O  
ATOM   1266  OG BSER B  46      -2.975  12.991  27.069  0.50 23.32           O  
ATOM   1267  N   TYR B  47      -0.525  11.172  23.807  1.00 17.00           N  
ATOM   1268  CA  TYR B  47      -0.030  11.078  22.443  1.00 16.51           C  
ATOM   1269  C   TYR B  47      -0.715   9.996  21.635  1.00 19.65           C  
ATOM   1270  O   TYR B  47      -1.401   9.097  22.163  1.00 19.00           O  
ATOM   1271  CB  TYR B  47       1.487  10.859  22.433  1.00 16.80           C  
ATOM   1272  CG  TYR B  47       1.900   9.509  22.955  1.00 21.77           C  
ATOM   1273  CD1 TYR B  47       2.072   9.303  24.310  1.00 25.46           C  
ATOM   1274  CD2 TYR B  47       2.133   8.443  22.080  1.00 23.05           C  
ATOM   1275  CE1 TYR B  47       2.437   8.066  24.798  1.00 24.93           C  
ATOM   1276  CE2 TYR B  47       2.488   7.189  22.558  1.00 22.89           C  
ATOM   1277  CZ  TYR B  47       2.638   7.019  23.913  1.00 26.07           C  
ATOM   1278  OH  TYR B  47       3.017   5.787  24.392  1.00 29.16           O  
ATOM   1279  N   LYS B  48      -0.502  10.106  20.332  1.00 19.56           N  
ATOM   1280  CA  LYS B  48      -0.994   9.160  19.369  1.00 17.25           C  
ATOM   1281  C   LYS B  48       0.121   8.952  18.359  1.00 17.08           C  
ATOM   1282  O   LYS B  48       0.636   9.906  17.784  1.00 17.99           O  
ATOM   1283  CB  LYS B  48      -2.227   9.689  18.677  1.00 18.17           C  
ATOM   1284  CG  LYS B  48      -2.757   8.710  17.625  1.00 20.00           C  
ATOM   1285  CD  LYS B  48      -3.976   9.237  16.943  1.00 22.64           C  
ATOM   1286  CE  LYS B  48      -4.466   8.271  15.907  1.00 26.76           C  
ATOM   1287  NZ  LYS B  48      -4.963   7.026  16.548  1.00 24.88           N  
ATOM   1288  N   LYS B  49       0.491   7.698  18.165  1.00 16.73           N  
ATOM   1289  CA  LYS B  49       1.517   7.324  17.203  1.00 17.98           C  
ATOM   1290  C   LYS B  49       0.879   7.130  15.837  1.00 19.52           C  
ATOM   1291  O   LYS B  49      -0.108   6.377  15.708  1.00 21.15           O  
ATOM   1292  CB  LYS B  49       2.191   6.027  17.641  1.00 20.02           C  
ATOM   1293  CG  LYS B  49       3.423   5.646  16.806  1.00 21.66           C  
ATOM   1294  CD  LYS B  49       3.923   4.272  17.182  1.00 23.74           C  
ATOM   1295  CE  LYS B  49       5.179   3.869  16.395  1.00 28.81           C  
ATOM   1296  NZ  LYS B  49       4.856   3.569  14.969  1.00 33.75           N  
ATOM   1297  N   ILE B  50       1.417   7.799  14.826  1.00 19.01           N  
ATOM   1298  CA  ILE B  50       0.988   7.607  13.451  1.00 20.82           C  
ATOM   1299  C   ILE B  50       2.236   7.379  12.614  1.00 19.48           C  
ATOM   1300  O   ILE B  50       2.910   8.320  12.216  1.00 20.48           O  
ATOM   1301  CB  ILE B  50       0.183   8.776  12.910  1.00 22.14           C  
ATOM   1302  CG1 ILE B  50      -1.029   9.043  13.805  1.00 26.34           C  
ATOM   1303  CG2 ILE B  50      -0.267   8.453  11.463  1.00 25.87           C  
ATOM   1304  CD1 ILE B  50      -1.838  10.223  13.368  1.00 25.77           C  
ATOM   1305  N   GLY B  51       2.535   6.114  12.352  1.00 21.42           N  
ATOM   1306  CA  GLY B  51       3.708   5.761  11.588  1.00 21.47           C  
ATOM   1307  C   GLY B  51       4.949   6.268  12.288  1.00 21.08           C  
ATOM   1308  O   GLY B  51       5.148   5.970  13.462  1.00 22.03           O  
ATOM   1309  N   ASN B  52       5.743   7.058  11.566  1.00 22.58           N  
ATOM   1310  CA  ASN B  52       6.993   7.640  12.072  1.00 24.09           C  
ATOM   1311  C   ASN B  52       6.807   8.927  12.869  1.00 22.83           C  
ATOM   1312  O   ASN B  52       7.786   9.549  13.240  1.00 22.09           O  
ATOM   1313  CB  ASN B  52       7.968   7.919  10.901  1.00 26.73           C  
ATOM   1314  CG  ASN B  52       7.442   8.989   9.899  1.00 32.16           C  
ATOM   1315  OD1 ASN B  52       6.276   9.380   9.930  1.00 37.76           O  
ATOM   1316  ND2 ASN B  52       8.312   9.430   8.991  1.00 39.97           N  
ATOM   1317  N   LYS B  53       5.567   9.319  13.126  1.00 19.33           N  
ATOM   1318  CA  LYS B  53       5.271  10.553  13.831  1.00 20.45           C  
ATOM   1319  C   LYS B  53       4.488  10.269  15.091  1.00 19.77           C  
ATOM   1320  O   LYS B  53       3.841   9.231  15.218  1.00 18.86           O  
ATOM   1321  CB  LYS B  53       4.442  11.471  12.943  1.00 20.92           C  
ATOM   1322  CG  LYS B  53       5.203  11.993  11.774  1.00 26.23           C  
ATOM   1323  CD  LYS B  53       4.337  12.933  10.947  1.00 28.81           C  
ATOM   1324  CE  LYS B  53       4.999  13.233   9.625  1.00 35.87           C  
ATOM   1325  NZ  LYS B  53       4.950  12.030   8.740  1.00 36.95           N  
ATOM   1326  N   TYR B  54       4.577  11.194  16.031  1.00 15.55           N  
ATOM   1327  CA  TYR B  54       3.749  11.197  17.220  1.00 16.12           C  
ATOM   1328  C   TYR B  54       3.034  12.530  17.296  1.00 16.51           C  
ATOM   1329  O   TYR B  54       3.660  13.578  17.143  1.00 18.40           O  
ATOM   1330  CB  TYR B  54       4.554  11.017  18.490  1.00 17.51           C  
ATOM   1331  CG  TYR B  54       5.273   9.689  18.644  1.00 17.24           C  
ATOM   1332  CD1 TYR B  54       4.621   8.584  19.170  1.00 17.38           C  
ATOM   1333  CD2 TYR B  54       6.622   9.570  18.309  1.00 19.17           C  
ATOM   1334  CE1 TYR B  54       5.287   7.399  19.345  1.00 18.81           C  
ATOM   1335  CE2 TYR B  54       7.289   8.383  18.473  1.00 19.44           C  
ATOM   1336  CZ  TYR B  54       6.629   7.312  18.998  1.00 20.35           C  
ATOM   1337  OH  TYR B  54       7.331   6.121  19.162  1.00 22.79           O  
ATOM   1338  N   ILE B  55       1.736  12.489  17.530  1.00 16.56           N  
ATOM   1339  CA  ILE B  55       0.974  13.686  17.776  1.00 16.24           C  
ATOM   1340  C   ILE B  55       0.935  13.778  19.306  1.00 16.92           C  
ATOM   1341  O   ILE B  55       0.429  12.863  19.969  1.00 18.12           O  
ATOM   1342  CB  ILE B  55      -0.437  13.601  17.166  1.00 18.53           C  
ATOM   1343  CG1 ILE B  55      -0.388  13.188  15.680  1.00 21.86           C  
ATOM   1344  CG2 ILE B  55      -1.144  14.902  17.343  1.00 21.10           C  
ATOM   1345  CD1 ILE B  55       0.612  13.927  14.814  1.00 25.95           C  
ATOM   1346  N   VAL B  56       1.500  14.856  19.855  1.00 17.55           N  
ATOM   1347  CA  VAL B  56       1.662  15.010  21.290  1.00 16.27           C  
ATOM   1348  C   VAL B  56       0.825  16.170  21.791  1.00 16.24           C  
ATOM   1349  O   VAL B  56       0.979  17.289  21.311  1.00 18.18           O  
ATOM   1350  CB  VAL B  56       3.154  15.236  21.636  1.00 17.36           C  
ATOM   1351  CG1 VAL B  56       3.391  15.342  23.164  1.00 17.10           C  
ATOM   1352  CG2 VAL B  56       4.049  14.115  21.051  1.00 18.72           C  
ATOM   1353  N   SER B  57      -0.042  15.905  22.752  1.00 14.89           N  
ATOM   1354  CA  SER B  57      -0.873  16.892  23.360  1.00 16.02           C  
ATOM   1355  C   SER B  57      -0.362  17.074  24.770  1.00 15.92           C  
ATOM   1356  O   SER B  57      -0.493  16.214  25.616  1.00 16.40           O  
ATOM   1357  CB  SER B  57      -2.289  16.404  23.361  1.00 16.27           C  
ATOM   1358  OG  SER B  57      -3.118  17.396  23.913  1.00 19.93           O  
ATOM   1359  N   ILE B  58       0.280  18.200  25.016  1.00 14.81           N  
ATOM   1360  CA  ILE B  58       0.880  18.447  26.322  1.00 16.70           C  
ATOM   1361  C   ILE B  58      -0.213  18.860  27.280  1.00 15.02           C  
ATOM   1362  O   ILE B  58      -1.192  19.503  26.862  1.00 15.89           O  
ATOM   1363  CB  ILE B  58       1.993  19.510  26.178  1.00 15.87           C  
ATOM   1364  CG1 ILE B  58       3.095  18.971  25.243  1.00 16.75           C  
ATOM   1365  CG2 ILE B  58       2.562  19.909  27.551  1.00 15.25           C  
ATOM   1366  CD1 ILE B  58       4.263  19.845  25.013  1.00 19.57           C  
ATOM   1367  N   ASN B  59      -0.107  18.421  28.536  1.00 15.97           N  
ATOM   1368  CA  ASN B  59      -1.093  18.773  29.537  1.00 16.33           C  
ATOM   1369  C   ASN B  59      -1.092  20.240  29.808  1.00 16.11           C  
ATOM   1370  O   ASN B  59      -0.058  20.886  29.759  1.00 14.71           O  
ATOM   1371  CB  ASN B  59      -0.790  18.073  30.865  1.00 17.64           C  
ATOM   1372  CG  ASN B  59      -1.018  16.565  30.819  1.00 20.45           C  
ATOM   1373  OD1 ASN B  59      -1.450  16.015  29.811  1.00 19.94           O  
ATOM   1374  ND2 ASN B  59      -0.721  15.895  31.920  1.00 21.45           N  
ATOM   1375  N   ASN B  60      -2.246  20.792  30.149  1.00 15.36           N  
ATOM   1376  CA  ASN B  60      -2.300  22.189  30.511  1.00 15.02           C  
ATOM   1377  C   ASN B  60      -1.453  22.447  31.753  1.00 14.17           C  
ATOM   1378  O   ASN B  60      -1.192  21.545  32.551  1.00 15.58           O  
ATOM   1379  CB  ASN B  60      -3.745  22.623  30.740  1.00 14.31           C  
ATOM   1380  CG  ASN B  60      -3.949  24.081  30.585  1.00 15.33           C  
ATOM   1381  OD1 ASN B  60      -3.046  24.803  30.175  1.00 17.24           O  
ATOM   1382  ND2 ASN B  60      -5.144  24.538  30.903  1.00 18.33           N  
ATOM   1383  N   HIS B  61      -0.976  23.690  31.866  1.00 15.49           N  
ATOM   1384  CA  HIS B  61      -0.205  24.163  33.028  1.00 14.26           C  
ATOM   1385  C   HIS B  61       1.159  23.509  33.215  1.00 17.31           C  
ATOM   1386  O   HIS B  61       1.754  23.597  34.270  1.00 19.96           O  
ATOM   1387  CB  HIS B  61      -1.020  23.985  34.319  1.00 16.58           C  
ATOM   1388  CG  HIS B  61      -2.436  24.436  34.211  1.00 16.68           C  
ATOM   1389  ND1 HIS B  61      -2.777  25.735  33.929  1.00 23.09           N  
ATOM   1390  CD2 HIS B  61      -3.596  23.775  34.422  1.00 20.74           C  
ATOM   1391  CE1 HIS B  61      -4.094  25.848  33.916  1.00 25.59           C  
ATOM   1392  NE2 HIS B  61      -4.613  24.671  34.212  1.00 22.96           N  
ATOM   1393  N   THR B  62       1.664  22.894  32.167  1.00 15.27           N  
ATOM   1394  CA  THR B  62       2.908  22.161  32.147  1.00 15.23           C  
ATOM   1395  C   THR B  62       3.963  22.958  31.417  1.00 14.79           C  
ATOM   1396  O   THR B  62       3.645  23.691  30.491  1.00 16.07           O  
ATOM   1397  CB  THR B  62       2.634  20.815  31.390  1.00 17.31           C  
ATOM   1398  OG1 THR B  62       1.663  20.107  32.167  1.00 22.59           O  
ATOM   1399  CG2 THR B  62       3.858  19.950  31.215  1.00 21.58           C  
ATOM   1400  N   GLU B  63       5.222  22.749  31.796  1.00 14.49           N  
ATOM   1401  CA  GLU B  63       6.328  23.386  31.129  1.00 16.05           C  
ATOM   1402  C   GLU B  63       6.633  22.527  29.907  1.00 15.86           C  
ATOM   1403  O   GLU B  63       7.020  21.362  30.009  1.00 17.19           O  
ATOM   1404  CB  GLU B  63       7.511  23.587  32.074  1.00 16.60           C  
ATOM   1405  CG  GLU B  63       8.445  24.690  31.622  1.00 17.94           C  
ATOM   1406  CD  GLU B  63       9.326  24.207  30.514  1.00 16.55           C  
ATOM   1407  OE1 GLU B  63      10.152  23.304  30.780  1.00 18.07           O  
ATOM   1408  OE2 GLU B  63       9.171  24.682  29.368  1.00 15.53           O  
ATOM   1409  N  AILE B  64       6.487  23.143  28.748  0.70 15.13           N  
ATOM   1410  N  BILE B  64       6.457  23.117  28.730  0.30 14.58           N  
ATOM   1411  CA AILE B  64       6.537  22.456  27.470  0.70 15.44           C  
ATOM   1412  CA BILE B  64       6.521  22.352  27.480  0.30 13.63           C  
ATOM   1413  C  AILE B  64       7.886  21.860  27.112  0.70 15.84           C  
ATOM   1414  C  BILE B  64       7.903  21.825  27.105  0.30 14.87           C  
ATOM   1415  O  AILE B  64       7.935  20.781  26.536  0.70 16.14           O  
ATOM   1416  O  BILE B  64       7.987  20.762  26.500  0.30 15.16           O  
ATOM   1417  CB AILE B  64       6.070  23.438  26.348  0.70 16.48           C  
ATOM   1418  CB BILE B  64       5.927  23.137  26.264  0.30 13.60           C  
ATOM   1419  CG1AILE B  64       4.568  23.705  26.494  0.70 18.06           C  
ATOM   1420  CG1BILE B  64       6.827  24.319  25.860  0.30 13.17           C  
ATOM   1421  CG2AILE B  64       6.389  22.915  24.946  0.70 17.96           C  
ATOM   1422  CG2BILE B  64       4.497  23.578  26.569  0.30 14.41           C  
ATOM   1423  CD1AILE B  64       4.090  24.926  25.720  0.70 19.18           C  
ATOM   1424  CD1BILE B  64       6.272  25.197  24.780  0.30 11.77           C  
ATOM   1425  N   VAL B  65       8.972  22.564  27.409  1.00 15.79           N  
ATOM   1426  CA  VAL B  65      10.331  22.052  27.099  1.00 15.20           C  
ATOM   1427  C   VAL B  65      10.625  20.812  27.945  1.00 16.32           C  
ATOM   1428  O   VAL B  65      11.037  19.801  27.417  1.00 15.76           O  
ATOM   1429  CB  VAL B  65      11.389  23.126  27.280  1.00 16.72           C  
ATOM   1430  CG1 VAL B  65      12.793  22.549  27.027  1.00 16.27           C  
ATOM   1431  CG2 VAL B  65      11.092  24.283  26.313  1.00 17.82           C  
ATOM   1432  N   LYS B  66      10.340  20.891  29.237  1.00 14.81           N  
ATOM   1433  CA  LYS B  66      10.478  19.727  30.102  1.00 15.20           C  
ATOM   1434  C   LYS B  66       9.606  18.560  29.591  1.00 16.32           C  
ATOM   1435  O   LYS B  66      10.043  17.423  29.570  1.00 16.20           O  
ATOM   1436  CB  LYS B  66      10.083  20.098  31.535  1.00 16.39           C  
ATOM   1437  CG  LYS B  66      10.273  19.008  32.546  1.00 19.60           C  
ATOM   1438  CD  LYS B  66       9.813  19.468  33.927  1.00 23.55           C  
ATOM   1439  CE  LYS B  66      10.036  18.363  34.964  1.00 32.56           C  
ATOM   1440  NZ  LYS B  66       8.967  18.323  35.978  1.00 42.10           N  
ATOM   1441  N   ALA B  67       8.357  18.838  29.201  1.00 14.90           N  
ATOM   1442  CA  ALA B  67       7.474  17.803  28.679  1.00 14.38           C  
ATOM   1443  C   ALA B  67       8.007  17.150  27.394  1.00 15.06           C  
ATOM   1444  O   ALA B  67       7.943  15.937  27.249  1.00 15.81           O  
ATOM   1445  CB  ALA B  67       6.094  18.375  28.413  1.00 16.76           C  
ATOM   1446  N   LEU B  68       8.458  17.971  26.457  1.00 14.50           N  
ATOM   1447  CA  LEU B  68       8.994  17.464  25.202  1.00 13.97           C  
ATOM   1448  C   LEU B  68      10.257  16.626  25.433  1.00 17.20           C  
ATOM   1449  O   LEU B  68      10.397  15.565  24.845  1.00 16.15           O  
ATOM   1450  CB  LEU B  68       9.229  18.600  24.190  1.00 15.75           C  
ATOM   1451  CG  LEU B  68       7.950  19.251  23.634  1.00 16.02           C  
ATOM   1452  CD1 LEU B  68       8.291  20.525  22.887  1.00 17.06           C  
ATOM   1453  CD2 LEU B  68       7.152  18.310  22.722  1.00 16.47           C  
ATOM   1454  N   ASN B  69      11.140  17.084  26.319  1.00 16.29           N  
ATOM   1455  CA  ASN B  69      12.318  16.305  26.685  1.00 18.66           C  
ATOM   1456  C   ASN B  69      11.877  14.983  27.295  1.00 16.88           C  
ATOM   1457  O   ASN B  69      12.395  13.932  26.947  1.00 17.12           O  
ATOM   1458  CB  ASN B  69      13.200  17.099  27.656  1.00 16.93           C  
ATOM   1459  CG  ASN B  69      14.194  17.991  26.951  1.00 26.54           C  
ATOM   1460  OD1 ASN B  69      15.277  17.535  26.574  1.00 25.88           O  
ATOM   1461  ND2 ASN B  69      13.849  19.276  26.781  1.00 23.70           N  
ATOM   1462  N   ALA B  70      10.870  15.015  28.171  1.00 16.78           N  
ATOM   1463  CA  ALA B  70      10.393  13.793  28.833  1.00 15.56           C  
ATOM   1464  C   ALA B  70       9.809  12.831  27.802  1.00 16.42           C  
ATOM   1465  O   ALA B  70      10.026  11.623  27.871  1.00 17.14           O  
ATOM   1466  CB  ALA B  70       9.353  14.120  29.911  1.00 16.85           C  
ATOM   1467  N   PHE B  71       9.039  13.358  26.856  1.00 15.65           N  
ATOM   1468  CA  PHE B  71       8.472  12.540  25.793  1.00 15.57           C  
ATOM   1469  C   PHE B  71       9.555  11.837  24.994  1.00 15.06           C  
ATOM   1470  O   PHE B  71       9.465  10.634  24.756  1.00 15.66           O  
ATOM   1471  CB  PHE B  71       7.630  13.373  24.823  1.00 15.09           C  
ATOM   1472  CG  PHE B  71       7.028  12.549  23.739  1.00 17.02           C  
ATOM   1473  CD1 PHE B  71       5.896  11.814  23.991  1.00 17.21           C  
ATOM   1474  CD2 PHE B  71       7.588  12.480  22.471  1.00 17.65           C  
ATOM   1475  CE1 PHE B  71       5.341  11.003  23.029  1.00 18.52           C  
ATOM   1476  CE2 PHE B  71       7.019  11.681  21.500  1.00 18.57           C  
ATOM   1477  CZ  PHE B  71       5.910  10.930  21.798  1.00 17.59           C  
ATOM   1478  N   CYS B  72      10.562  12.589  24.581  1.00 16.28           N  
ATOM   1479  CA  CYS B  72      11.655  12.021  23.781  1.00 17.56           C  
ATOM   1480  C   CYS B  72      12.452  10.963  24.547  1.00 18.26           C  
ATOM   1481  O   CYS B  72      12.855   9.946  23.973  1.00 19.91           O  
ATOM   1482  CB  CYS B  72      12.585  13.114  23.249  1.00 18.68           C  
ATOM   1483  SG  CYS B  72      11.764  14.156  22.033  1.00 19.48           S  
ATOM   1484  N   LYS B  73      12.682  11.190  25.831  1.00 17.14           N  
ATOM   1485  CA  LYS B  73      13.321  10.172  26.664  1.00 17.23           C  
ATOM   1486  C   LYS B  73      12.420   8.941  26.816  1.00 18.34           C  
ATOM   1487  O   LYS B  73      12.914   7.798  26.794  1.00 18.74           O  
ATOM   1488  CB  LYS B  73      13.616  10.718  28.045  1.00 18.97           C  
ATOM   1489  CG  LYS B  73      14.665  11.744  28.128  1.00 20.00           C  
ATOM   1490  CD  LYS B  73      14.907  12.074  29.595  1.00 29.60           C  
ATOM   1491  CE  LYS B  73      15.485  13.439  29.779  1.00 37.78           C  
ATOM   1492  NZ  LYS B  73      15.689  13.717  31.237  1.00 43.04           N  
ATOM   1493  N   GLU B  74      11.120   9.119  27.079  1.00 17.29           N  
ATOM   1494  CA  GLU B  74      10.215   7.969  27.269  1.00 17.42           C  
ATOM   1495  C   GLU B  74      10.121   7.074  26.041  1.00 15.24           C  
ATOM   1496  O   GLU B  74       9.966   5.837  26.172  1.00 15.99           O  
ATOM   1497  CB  GLU B  74       8.799   8.446  27.660  1.00 20.43           C  
ATOM   1498  CG  GLU B  74       7.678   7.366  27.732  1.00 23.54           C  
ATOM   1499  CD  GLU B  74       6.246   7.949  27.898  1.00 28.43           C  
ATOM   1500  OE1 GLU B  74       5.276   7.315  27.431  1.00 40.63           O  
ATOM   1501  OE2 GLU B  74       6.106   9.026  28.505  1.00 35.54           O  
ATOM   1502  N   LYS B  75      10.133   7.704  24.869  1.00 14.98           N  
ATOM   1503  CA  LYS B  75       9.987   7.002  23.593  1.00 16.56           C  
ATOM   1504  C   LYS B  75      11.320   6.634  22.988  1.00 18.65           C  
ATOM   1505  O   LYS B  75      11.368   6.006  21.938  1.00 20.56           O  
ATOM   1506  CB  LYS B  75       9.153   7.828  22.615  1.00 16.23           C  
ATOM   1507  CG  LYS B  75       7.703   7.986  23.022  1.00 20.30           C  
ATOM   1508  CD  LYS B  75       7.096   6.626  23.200  1.00 23.01           C  
ATOM   1509  CE  LYS B  75       5.672   6.626  23.301  1.00 33.24           C  
ATOM   1510  NZ  LYS B  75       5.260   5.194  23.472  1.00 30.83           N  
ATOM   1511  N   GLY B  76      12.397   6.991  23.662  1.00 16.95           N  
ATOM   1512  CA  GLY B  76      13.725   6.660  23.164  1.00 18.37           C  
ATOM   1513  C   GLY B  76      14.025   7.223  21.802  1.00 17.88           C  
ATOM   1514  O   GLY B  76      14.647   6.572  20.989  1.00 18.30           O  
ATOM   1515  N   ILE B  77      13.622   8.462  21.543  1.00 15.89           N  
ATOM   1516  CA  ILE B  77      13.808   9.043  20.222  1.00 16.72           C  
ATOM   1517  C   ILE B  77      15.250   9.502  20.080  1.00 17.57           C  
ATOM   1518  O   ILE B  77      15.732  10.286  20.885  1.00 19.82           O  
ATOM   1519  CB  ILE B  77      12.851  10.190  19.965  1.00 16.19           C  
ATOM   1520  CG1 ILE B  77      11.425   9.646  20.021  1.00 19.29           C  
ATOM   1521  CG2 ILE B  77      13.146  10.835  18.613  1.00 15.60           C  
ATOM   1522  CD1 ILE B  77      10.310  10.669  19.802  1.00 18.83           C  
ATOM   1523  N   LEU B  78      15.928   9.002  19.044  1.00 16.45           N  
ATOM   1524  CA  LEU B  78      17.311   9.335  18.776  1.00 15.58           C  
ATOM   1525  C   LEU B  78      17.490  10.700  18.113  1.00 16.73           C  
ATOM   1526  O   LEU B  78      18.371  11.503  18.497  1.00 15.81           O  
ATOM   1527  CB  LEU B  78      17.901   8.240  17.874  1.00 17.28           C  
ATOM   1528  CG  LEU B  78      17.964   6.847  18.503  1.00 19.63           C  
ATOM   1529  CD1 LEU B  78      18.173   5.802  17.431  1.00 17.67           C  
ATOM   1530  CD2 LEU B  78      19.058   6.790  19.541  1.00 21.13           C  
ATOM   1531  N   SER B  79      16.642  10.955  17.121  1.00 15.18           N  
ATOM   1532  CA  SER B  79      16.637  12.206  16.407  1.00 15.58           C  
ATOM   1533  C   SER B  79      15.304  12.373  15.728  1.00 15.26           C  
ATOM   1534  O   SER B  79      14.512  11.428  15.609  1.00 15.27           O  
ATOM   1535  CB  SER B  79      17.762  12.274  15.370  1.00 16.05           C  
ATOM   1536  OG  SER B  79      17.547  11.349  14.341  1.00 17.16           O  
ATOM   1537  N   GLY B  80      15.060  13.590  15.298  1.00 14.93           N  
ATOM   1538  CA  GLY B  80      13.768  13.946  14.764  1.00 15.29           C  
ATOM   1539  C   GLY B  80      13.514  15.430  14.775  1.00 15.86           C  
ATOM   1540  O   GLY B  80      14.418  16.233  15.000  1.00 15.33           O  
ATOM   1541  N   SER B  81      12.257  15.755  14.515  1.00 17.10           N  
ATOM   1542  CA  SER B  81      11.817  17.130  14.476  1.00 15.37           C  
ATOM   1543  C   SER B  81      10.620  17.323  15.370  1.00 16.64           C  
ATOM   1544  O   SER B  81       9.888  16.380  15.651  1.00 15.73           O  
ATOM   1545  CB  SER B  81      11.442  17.520  13.050  1.00 18.70           C  
ATOM   1546  OG  SER B  81      10.331  16.761  12.642  1.00 21.15           O  
ATOM   1547  N   ILE B  82      10.452  18.551  15.834  1.00 15.86           N  
ATOM   1548  CA  ILE B  82       9.314  18.921  16.650  1.00 15.21           C  
ATOM   1549  C   ILE B  82       8.733  20.193  16.054  1.00 16.33           C  
ATOM   1550  O   ILE B  82       9.454  21.147  15.785  1.00 16.62           O  
ATOM   1551  CB  ILE B  82       9.700  19.177  18.112  1.00 16.52           C  
ATOM   1552  CG1 ILE B  82      10.386  17.928  18.717  1.00 16.44           C  
ATOM   1553  CG2 ILE B  82       8.444  19.580  18.924  1.00 18.15           C  
ATOM   1554  CD1 ILE B  82      10.874  18.074  20.168  1.00 16.50           C  
ATOM   1555  N   ASN B  83       7.422  20.196  15.855  1.00 17.27           N  
ATOM   1556  CA  ASN B  83       6.724  21.375  15.342  1.00 16.47           C  
ATOM   1557  C   ASN B  83       5.371  21.463  15.984  1.00 19.04           C  
ATOM   1558  O   ASN B  83       4.697  20.469  16.109  1.00 21.51           O  
ATOM   1559  CB  ASN B  83       6.556  21.271  13.833  1.00 17.95           C  
ATOM   1560  CG  ASN B  83       7.842  21.363  13.129  1.00 20.72           C  
ATOM   1561  OD1 ASN B  83       8.334  22.469  12.907  1.00 25.28           O  
ATOM   1562  ND2 ASN B  83       8.445  20.215  12.784  1.00 23.02           N  
ATOM   1563  N   GLY B  84       4.941  22.650  16.371  1.00 15.83           N  
ATOM   1564  CA  GLY B  84       3.553  22.770  16.814  1.00 16.76           C  
ATOM   1565  C   GLY B  84       3.124  24.127  17.244  1.00 16.73           C  
ATOM   1566  O   GLY B  84       3.829  25.106  17.044  1.00 16.71           O  
ATOM   1567  N   ILE B  85       1.965  24.160  17.889  1.00 15.83           N  
ATOM   1568  CA  ILE B  85       1.264  25.389  18.241  1.00 16.43           C  
ATOM   1569  C   ILE B  85       0.575  25.176  19.598  1.00 16.69           C  
ATOM   1570  O   ILE B  85       0.440  24.033  20.080  1.00 16.08           O  
ATOM   1571  CB  ILE B  85       0.220  25.765  17.159  1.00 15.71           C  
ATOM   1572  CG1 ILE B  85      -0.823  24.655  16.926  1.00 15.42           C  
ATOM   1573  CG2 ILE B  85       0.882  26.070  15.819  1.00 15.60           C  
ATOM   1574  CD1 ILE B  85      -2.009  25.104  16.032  1.00 16.71           C  
ATOM   1575  N   GLY B  86       0.100  26.252  20.201  1.00 15.00           N  
ATOM   1576  CA  GLY B  86      -0.573  26.187  21.492  1.00 15.44           C  
ATOM   1577  C   GLY B  86      -0.592  27.550  22.119  1.00 15.76           C  
ATOM   1578  O   GLY B  86      -0.252  28.506  21.460  1.00 16.95           O  
ATOM   1579  N   ALA B  87      -1.001  27.618  23.376  1.00 14.27           N  
ATOM   1580  CA  ALA B  87      -1.113  28.857  24.108  1.00 14.27           C  
ATOM   1581  C   ALA B  87      -0.392  28.699  25.422  1.00 15.07           C  
ATOM   1582  O   ALA B  87      -0.380  27.609  26.021  1.00 14.69           O  
ATOM   1583  CB  ALA B  87      -2.593  29.206  24.361  1.00 16.71           C  
ATOM   1584  N   ILE B  88       0.231  29.799  25.860  1.00 14.36           N  
ATOM   1585  CA  ILE B  88       1.092  29.824  27.024  1.00 13.46           C  
ATOM   1586  C   ILE B  88       0.864  31.035  27.898  1.00 14.66           C  
ATOM   1587  O   ILE B  88       0.288  32.028  27.440  1.00 15.43           O  
ATOM   1588  CB  ILE B  88       2.589  29.758  26.656  1.00 14.68           C  
ATOM   1589  CG1 ILE B  88       2.985  30.952  25.761  1.00 15.26           C  
ATOM   1590  CG2 ILE B  88       2.903  28.436  25.969  1.00 14.60           C  
ATOM   1591  CD1 ILE B  88       4.472  31.005  25.407  1.00 14.18           C  
ATOM   1592  N   GLY B  89       1.302  30.941  29.166  1.00 14.80           N  
ATOM   1593  CA  GLY B  89       1.213  32.041  30.137  1.00 14.46           C  
ATOM   1594  C   GLY B  89       2.538  32.574  30.663  1.00 15.69           C  
ATOM   1595  O   GLY B  89       2.564  33.528  31.443  1.00 14.64           O  
ATOM   1596  N   GLU B  90       3.630  31.949  30.221  1.00 14.08           N  
ATOM   1597  CA  GLU B  90       4.998  32.303  30.607  1.00 14.89           C  
ATOM   1598  C   GLU B  90       5.920  31.780  29.509  1.00 15.13           C  
ATOM   1599  O   GLU B  90       5.688  30.695  28.971  1.00 14.67           O  
ATOM   1600  CB  GLU B  90       5.362  31.693  31.963  1.00 16.33           C  
ATOM   1601  CG  GLU B  90       6.665  32.215  32.585  1.00 15.61           C  
ATOM   1602  CD  GLU B  90       7.104  31.350  33.729  1.00 18.84           C  
ATOM   1603  OE1 GLU B  90       6.505  31.504  34.804  1.00 20.98           O  
ATOM   1604  OE2 GLU B  90       8.019  30.511  33.562  1.00 17.45           O  
ATOM   1605  N   LEU B  91       6.949  32.559  29.182  1.00 13.79           N  
ATOM   1606  CA  LEU B  91       7.903  32.233  28.142  1.00 14.82           C  
ATOM   1607  C   LEU B  91       9.253  32.754  28.543  1.00 13.61           C  
ATOM   1608  O   LEU B  91       9.382  33.917  28.937  1.00 14.22           O  
ATOM   1609  CB  LEU B  91       7.522  32.937  26.851  1.00 15.77           C  
ATOM   1610  CG  LEU B  91       8.465  32.760  25.652  1.00 15.42           C  
ATOM   1611  CD1 LEU B  91       8.475  31.329  25.162  1.00 16.93           C  
ATOM   1612  CD2 LEU B  91       8.058  33.742  24.523  1.00 15.80           C  
ATOM   1613  N   THR B  92      10.284  31.920  28.430  1.00 14.75           N  
ATOM   1614  CA  THR B  92      11.674  32.351  28.614  1.00 13.84           C  
ATOM   1615  C   THR B  92      12.437  32.114  27.316  1.00 15.22           C  
ATOM   1616  O   THR B  92      12.477  30.991  26.799  1.00 14.54           O  
ATOM   1617  CB  THR B  92      12.332  31.627  29.766  1.00 16.22           C  
ATOM   1618  OG1 THR B  92      11.522  31.841  30.941  1.00 16.96           O  
ATOM   1619  CG2 THR B  92      13.716  32.214  30.003  1.00 14.97           C  
ATOM   1620  N   LEU B  93      12.986  33.205  26.784  1.00 15.99           N  
ATOM   1621  CA  LEU B  93      13.783  33.202  25.552  1.00 16.31           C  
ATOM   1622  C   LEU B  93      15.218  33.529  25.890  1.00 17.86           C  
ATOM   1623  O   LEU B  93      15.469  34.245  26.845  1.00 17.11           O  
ATOM   1624  CB  LEU B  93      13.275  34.279  24.585  1.00 16.50           C  
ATOM   1625  CG  LEU B  93      11.847  34.147  24.019  1.00 17.18           C  
ATOM   1626  CD1 LEU B  93      11.393  35.326  23.104  1.00 15.61           C  
ATOM   1627  CD2 LEU B  93      11.694  32.749  23.303  1.00 17.67           C  
ATOM   1628  N   ARG B  94      16.155  33.019  25.083  1.00 19.25           N  
ATOM   1629  CA  ARG B  94      17.572  33.300  25.251  1.00 21.20           C  
ATOM   1630  C   ARG B  94      18.107  33.961  23.994  1.00 20.70           C  
ATOM   1631  O   ARG B  94      17.712  33.611  22.915  1.00 23.25           O  
ATOM   1632  CB  ARG B  94      18.388  32.025  25.537  1.00 21.35           C  
ATOM   1633  CG  ARG B  94      19.932  32.272  25.611  1.00 25.38           C  
ATOM   1634  CD  ARG B  94      20.685  31.072  26.155  1.00 28.87           C  
ATOM   1635  NE  ARG B  94      20.485  30.971  27.595  1.00 33.06           N  
ATOM   1636  CZ  ARG B  94      20.602  29.860  28.322  1.00 31.47           C  
ATOM   1637  NH1 ARG B  94      20.898  28.678  27.792  1.00 34.74           N  
ATOM   1638  NH2 ARG B  94      20.402  29.948  29.614  1.00 27.76           N  
ATOM   1639  N   PHE B  95      18.963  34.954  24.191  1.00 21.39           N  
ATOM   1640  CA  PHE B  95      19.658  35.592  23.089  1.00 22.37           C  
ATOM   1641  C   PHE B  95      21.154  35.472  23.339  1.00 17.54           C  
ATOM   1642  O   PHE B  95      21.692  36.057  24.291  1.00 25.48           O  
ATOM   1643  CB  PHE B  95      19.244  37.039  22.889  1.00 21.03           C  
ATOM   1644  CG  PHE B  95      19.691  37.597  21.570  1.00 18.67           C  
ATOM   1645  CD1 PHE B  95      18.930  37.417  20.423  1.00 17.91           C  
ATOM   1646  CD2 PHE B  95      20.900  38.271  21.477  1.00 17.29           C  
ATOM   1647  CE1 PHE B  95      19.343  37.935  19.237  1.00 18.75           C  
ATOM   1648  CE2 PHE B  95      21.330  38.790  20.268  1.00 18.68           C  
ATOM   1649  CZ  PHE B  95      20.540  38.615  19.152  1.00 19.37           C  
ATOM   1650  N   PHE B  96      21.782  34.735  22.442  1.00 25.12           N  
ATOM   1651  CA  PHE B  96      23.201  34.427  22.500  1.00 25.95           C  
ATOM   1652  C   PHE B  96      23.956  35.453  21.712  1.00 23.41           C  
ATOM   1653  O   PHE B  96      23.677  35.653  20.513  1.00 21.87           O  
ATOM   1654  CB  PHE B  96      23.450  33.058  21.889  1.00 26.85           C  
ATOM   1655  CG  PHE B  96      24.872  32.584  21.996  1.00 27.44           C  
ATOM   1656  CD1 PHE B  96      25.380  32.152  23.211  1.00 34.79           C  
ATOM   1657  CD2 PHE B  96      25.689  32.553  20.882  1.00 23.05           C  
ATOM   1658  CE1 PHE B  96      26.688  31.698  23.306  1.00 32.77           C  
ATOM   1659  CE2 PHE B  96      26.993  32.093  20.971  1.00 25.34           C  
ATOM   1660  CZ  PHE B  96      27.487  31.668  22.186  1.00 30.08           C  
ATOM   1661  N   ASN B  97      24.872  36.112  22.408  1.00 27.17           N  
ATOM   1662  CA  ASN B  97      25.792  37.078  21.858  1.00 30.70           C  
ATOM   1663  C   ASN B  97      27.082  36.328  21.476  1.00 30.10           C  
ATOM   1664  O   ASN B  97      27.785  35.822  22.353  1.00 29.62           O  
ATOM   1665  CB  ASN B  97      26.066  38.166  22.907  1.00 35.45           C  
ATOM   1666  CG  ASN B  97      26.955  39.284  22.393  1.00 42.53           C  
ATOM   1667  OD1 ASN B  97      27.563  39.197  21.317  1.00 58.66           O  
ATOM   1668  ND2 ASN B  97      27.041  40.359  23.178  1.00 56.37           N  
ATOM   1669  N   PRO B  98      27.383  36.207  20.173  1.00 29.88           N  
ATOM   1670  CA  PRO B  98      28.613  35.517  19.790  1.00 33.47           C  
ATOM   1671  C   PRO B  98      29.912  36.227  20.212  1.00 36.45           C  
ATOM   1672  O   PRO B  98      30.953  35.584  20.220  1.00 38.23           O  
ATOM   1673  CB  PRO B  98      28.528  35.460  18.262  1.00 33.69           C  
ATOM   1674  CG  PRO B  98      27.111  35.726  17.947  1.00 33.27           C  
ATOM   1675  CD  PRO B  98      26.620  36.631  18.990  1.00 29.78           C  
ATOM   1676  N   LYS B  99      29.844  37.521  20.524  1.00 38.34           N  
ATOM   1677  CA  LYS B  99      30.982  38.271  21.080  1.00 38.77           C  
ATOM   1678  C   LYS B  99      30.757  38.517  22.576  1.00 39.58           C  
ATOM   1679  O   LYS B  99      31.150  37.703  23.424  1.00 39.92           O  
ATOM   1680  CB  LYS B  99      31.144  39.594  20.343  1.00 39.44           C  
ATOM   1681  N   ASP B 104      21.772  36.406  27.090  1.00 31.31           N  
ATOM   1682  CA  ASP B 104      20.797  37.066  27.910  1.00 29.76           C  
ATOM   1683  C   ASP B 104      19.476  36.323  27.759  1.00 25.72           C  
ATOM   1684  O   ASP B 104      19.052  36.026  26.643  1.00 26.43           O  
ATOM   1685  CB  ASP B 104      20.614  38.524  27.488  1.00 31.90           C  
ATOM   1686  N   ASP B 105      18.849  36.066  28.899  1.00 24.38           N  
ATOM   1687  CA  ASP B 105      17.542  35.445  28.978  1.00 23.32           C  
ATOM   1688  C   ASP B 105      16.534  36.484  29.387  1.00 23.18           C  
ATOM   1689  O   ASP B 105      16.860  37.438  30.097  1.00 24.27           O  
ATOM   1690  CB  ASP B 105      17.546  34.334  30.008  1.00 22.40           C  
ATOM   1691  CG  ASP B 105      18.486  33.192  29.648  1.00 23.15           C  
ATOM   1692  OD1 ASP B 105      18.741  32.343  30.524  1.00 26.51           O  
ATOM   1693  OD2 ASP B 105      18.915  33.119  28.488  1.00 27.57           O  
ATOM   1694  N   LYS B 106      15.307  36.324  28.915  1.00 18.65           N  
ATOM   1695  CA  LYS B 106      14.222  37.174  29.337  1.00 17.07           C  
ATOM   1696  C   LYS B 106      12.968  36.344  29.456  1.00 16.24           C  
ATOM   1697  O   LYS B 106      12.665  35.540  28.561  1.00 15.48           O  
ATOM   1698  CB  LYS B 106      13.968  38.324  28.354  1.00 18.94           C  
ATOM   1699  CG  LYS B 106      12.851  39.241  28.809  1.00 19.23           C  
ATOM   1700  CD  LYS B 106      12.832  40.567  28.060  1.00 21.72           C  
ATOM   1701  CE  LYS B 106      11.637  41.415  28.470  1.00 26.45           C  
ATOM   1702  NZ  LYS B 106      11.626  42.699  27.727  1.00 30.95           N  
ATOM   1703  N   THR B 107      12.223  36.595  30.529  1.00 16.58           N  
ATOM   1704  CA  THR B 107      10.978  35.921  30.774  1.00 14.68           C  
ATOM   1705  C   THR B 107       9.810  36.893  30.609  1.00 16.93           C  
ATOM   1706  O   THR B 107       9.813  37.989  31.184  1.00 19.25           O  
ATOM   1707  CB  THR B 107      10.972  35.242  32.166  1.00 16.39           C  
ATOM   1708  OG1 THR B 107      12.031  34.279  32.229  1.00 17.84           O  
ATOM   1709  CG2 THR B 107       9.650  34.511  32.440  1.00 16.76           C  
ATOM   1710  N   PHE B 108       8.840  36.469  29.814  1.00 14.79           N  
ATOM   1711  CA  PHE B 108       7.593  37.185  29.560  1.00 14.75           C  
ATOM   1712  C   PHE B 108       6.498  36.453  30.343  1.00 15.88           C  
ATOM   1713  O   PHE B 108       6.414  35.229  30.314  1.00 16.11           O  
ATOM   1714  CB  PHE B 108       7.280  37.202  28.071  1.00 16.26           C  
ATOM   1715  CG  PHE B 108       8.297  37.936  27.282  1.00 16.40           C  
ATOM   1716  CD1 PHE B 108       9.433  37.294  26.828  1.00 16.14           C  
ATOM   1717  CD2 PHE B 108       8.137  39.294  27.027  1.00 15.95           C  
ATOM   1718  CE1 PHE B 108      10.387  38.013  26.103  1.00 18.54           C  
ATOM   1719  CE2 PHE B 108       9.082  39.996  26.293  1.00 17.62           C  
ATOM   1720  CZ  PHE B 108      10.206  39.357  25.857  1.00 17.40           C  
ATOM   1721  N  AARG B 109       5.660  37.239  31.019  0.50 17.53           N  
ATOM   1722  N  BARG B 109       5.685  37.209  31.076  0.50 17.47           N  
ATOM   1723  CA AARG B 109       4.696  36.749  31.996  0.50 17.22           C  
ATOM   1724  CA BARG B 109       4.660  36.640  31.954  0.50 16.91           C  
ATOM   1725  C  AARG B 109       3.313  37.320  31.633  0.50 16.97           C  
ATOM   1726  C  BARG B 109       3.332  37.300  31.618  0.50 17.03           C  
ATOM   1727  O  AARG B 109       2.880  38.342  32.169  0.50 17.33           O  
ATOM   1728  O  BARG B 109       2.971  38.356  32.138  0.50 17.53           O  
ATOM   1729  CB AARG B 109       5.195  37.176  33.393  0.50 18.71           C  
ATOM   1730  CB BARG B 109       5.067  36.848  33.402  0.50 18.76           C  
ATOM   1731  CG AARG B 109       6.732  36.898  33.628  0.50 17.50           C  
ATOM   1732  CG BARG B 109       6.417  36.193  33.721  0.50 17.62           C  
ATOM   1733  CD AARG B 109       7.242  37.215  35.036  0.50 19.53           C  
ATOM   1734  CD BARG B 109       6.831  36.387  35.154  0.50 18.64           C  
ATOM   1735  NE AARG B 109       8.543  36.602  35.385  0.50 20.47           N  
ATOM   1736  NE BARG B 109       8.244  36.087  35.414  0.50 25.23           N  
ATOM   1737  CZ AARG B 109       8.734  35.311  35.676  0.50 18.01           C  
ATOM   1738  CZ BARG B 109       9.262  36.952  35.336  0.50 23.37           C  
ATOM   1739  NH1AARG B 109       7.733  34.460  35.617  0.50 19.06           N  
ATOM   1740  NH1BARG B 109       9.089  38.230  34.979  0.50 30.68           N  
ATOM   1741  NH2AARG B 109       9.934  34.846  35.985  0.50 24.92           N  
ATOM   1742  NH2BARG B 109      10.490  36.528  35.603  0.50 23.04           N  
ATOM   1743  N   GLU B 110       2.637  36.651  30.690  1.00 17.25           N  
ATOM   1744  CA  GLU B 110       1.422  37.157  30.086  1.00 16.58           C  
ATOM   1745  C   GLU B 110       0.863  36.079  29.183  1.00 14.81           C  
ATOM   1746  O   GLU B 110       1.545  35.113  28.873  1.00 16.17           O  
ATOM   1747  CB  GLU B 110       1.747  38.384  29.234  1.00 17.31           C  
ATOM   1748  CG  GLU B 110       2.756  38.092  28.113  1.00 16.35           C  
ATOM   1749  CD  GLU B 110       3.249  39.353  27.445  1.00 19.99           C  
ATOM   1750  OE1 GLU B 110       4.143  39.990  28.030  1.00 19.89           O  
ATOM   1751  OE2 GLU B 110       2.717  39.702  26.367  1.00 18.81           O  
ATOM   1752  N   GLN B 111      -0.365  36.234  28.741  1.00 16.35           N  
ATOM   1753  CA  GLN B 111      -0.937  35.244  27.859  1.00 14.59           C  
ATOM   1754  C   GLN B 111      -0.384  35.445  26.443  1.00 15.39           C  
ATOM   1755  O   GLN B 111      -0.355  36.564  25.938  1.00 14.41           O  
ATOM   1756  CB  GLN B 111      -2.471  35.359  27.845  1.00 14.15           C  
ATOM   1757  CG  GLN B 111      -3.193  34.277  27.070  1.00 15.64           C  
ATOM   1758  CD  GLN B 111      -3.068  32.920  27.686  1.00 16.78           C  
ATOM   1759  OE1 GLN B 111      -2.683  32.786  28.857  1.00 16.38           O  
ATOM   1760  NE2 GLN B 111      -3.378  31.891  26.895  1.00 17.23           N  
HETATM 1761  N   MSE B 112       0.071  34.357  25.821  1.00 12.96           N  
HETATM 1762  CA  MSE B 112       0.612  34.392  24.456  1.00 13.21           C  
HETATM 1763  C   MSE B 112       0.153  33.166  23.671  1.00 14.27           C  
HETATM 1764  O   MSE B 112      -0.101  32.100  24.242  1.00 15.68           O  
HETATM 1765  CB  MSE B 112       2.133  34.413  24.460  1.00 14.62           C  
HETATM 1766  CG  MSE B 112       2.686  35.616  25.134  1.00 14.69           C  
HETATM 1767 SE   MSE B 112       4.581  35.525  25.652  0.75 13.45          SE  
HETATM 1768  CE  MSE B 112       4.357  34.498  27.327  1.00 15.62           C  
ATOM   1769  N   GLU B 113       0.055  33.353  22.364  1.00 15.59           N  
ATOM   1770  CA  GLU B 113      -0.191  32.235  21.457  1.00 15.25           C  
ATOM   1771  C   GLU B 113       1.101  31.817  20.791  1.00 14.44           C  
ATOM   1772  O   GLU B 113       1.827  32.672  20.244  1.00 16.47           O  
ATOM   1773  CB  GLU B 113      -1.213  32.598  20.385  1.00 16.36           C  
ATOM   1774  CG  GLU B 113      -2.636  32.735  20.939  1.00 20.16           C  
ATOM   1775  CD  GLU B 113      -3.271  31.409  21.360  1.00 20.21           C  
ATOM   1776  OE1 GLU B 113      -2.684  30.317  21.153  1.00 18.91           O  
ATOM   1777  OE2 GLU B 113      -4.385  31.460  21.963  1.00 22.44           O  
ATOM   1778  N   ILE B 114       1.408  30.534  20.799  1.00 14.91           N  
ATOM   1779  CA  ILE B 114       2.579  30.043  20.098  1.00 13.56           C  
ATOM   1780  C   ILE B 114       2.193  29.932  18.629  1.00 13.64           C  
ATOM   1781  O   ILE B 114       1.410  29.052  18.257  1.00 15.20           O  
ATOM   1782  CB  ILE B 114       3.017  28.662  20.560  1.00 13.55           C  
ATOM   1783  CG1 ILE B 114       3.390  28.665  22.049  1.00 17.32           C  
ATOM   1784  CG2 ILE B 114       4.210  28.180  19.698  1.00 16.41           C  
ATOM   1785  CD1 ILE B 114       3.662  27.225  22.616  1.00 16.88           C  
ATOM   1786  N   SER B 115       2.686  30.828  17.787  1.00 13.97           N  
ATOM   1787  CA  SER B 115       2.352  30.745  16.373  1.00 13.89           C  
ATOM   1788  C   SER B 115       3.151  29.667  15.664  1.00 14.97           C  
ATOM   1789  O   SER B 115       2.686  29.077  14.694  1.00 15.11           O  
ATOM   1790  CB  SER B 115       2.516  32.109  15.675  1.00 16.39           C  
ATOM   1791  OG  SER B 115       3.852  32.568  15.657  1.00 15.96           O  
ATOM   1792  N   ASN B 116       4.346  29.395  16.149  1.00 13.47           N  
ATOM   1793  CA  ASN B 116       5.138  28.313  15.684  1.00 15.09           C  
ATOM   1794  C   ASN B 116       6.203  27.962  16.705  1.00 15.25           C  
ATOM   1795  O   ASN B 116       6.887  28.843  17.225  1.00 15.45           O  
ATOM   1796  CB  ASN B 116       5.796  28.669  14.364  1.00 16.05           C  
ATOM   1797  CG  ASN B 116       6.656  27.590  13.863  1.00 22.30           C  
ATOM   1798  OD1 ASN B 116       6.193  26.713  13.117  1.00 29.40           O  
ATOM   1799  ND2 ASN B 116       7.929  27.613  14.243  1.00 20.64           N  
ATOM   1800  N   LEU B 117       6.381  26.670  16.931  1.00 16.58           N  
ATOM   1801  CA  LEU B 117       7.506  26.131  17.697  1.00 16.74           C  
ATOM   1802  C   LEU B 117       8.168  25.193  16.753  1.00 17.83           C  
ATOM   1803  O   LEU B 117       7.491  24.311  16.218  1.00 19.02           O  
ATOM   1804  CB  LEU B 117       7.056  25.422  18.972  1.00 16.48           C  
ATOM   1805  CG  LEU B 117       8.165  24.834  19.874  1.00 20.36           C  
ATOM   1806  CD1 LEU B 117       7.701  24.760  21.344  1.00 21.35           C  
ATOM   1807  CD2 LEU B 117       8.629  23.478  19.338  1.00 24.81           C  
ATOM   1808  N  ATHR B 118       9.458  25.430  16.443  0.50 15.80           N  
ATOM   1809  N  BTHR B 118       9.460  25.348  16.532  0.50 19.22           N  
ATOM   1810  CA ATHR B 118      10.259  24.660  15.457  0.50 14.32           C  
ATOM   1811  CA BTHR B 118      10.116  24.437  15.631  0.50 19.57           C  
ATOM   1812  C  ATHR B 118      11.519  24.143  16.153  0.50 15.29           C  
ATOM   1813  C  BTHR B 118      11.510  24.129  16.128  0.50 18.25           C  
ATOM   1814  O  ATHR B 118      12.205  24.917  16.799  0.50 14.59           O  
ATOM   1815  O  BTHR B 118      12.255  24.997  16.586  0.50 17.69           O  
ATOM   1816  CB ATHR B 118      10.730  25.551  14.274  0.50 13.58           C  
ATOM   1817  CB BTHR B 118      10.102  24.935  14.190  0.50 22.21           C  
ATOM   1818  OG1ATHR B 118       9.623  26.241  13.696  0.50 15.93           O  
ATOM   1819  OG1BTHR B 118      10.430  23.829  13.337  0.50 21.25           O  
ATOM   1820  CG2ATHR B 118      11.452  24.724  13.166  0.50 13.21           C  
ATOM   1821  CG2BTHR B 118      11.062  26.093  13.972  0.50 20.82           C  
ATOM   1822  N   GLY B 119      11.836  22.866  16.036  1.00 15.76           N  
ATOM   1823  CA  GLY B 119      13.068  22.411  16.558  1.00 18.13           C  
ATOM   1824  C   GLY B 119      13.433  21.029  16.129  1.00 15.25           C  
ATOM   1825  O   GLY B 119      12.762  20.397  15.311  1.00 15.74           O  
ATOM   1826  N   ASN B 120      14.534  20.588  16.688  1.00 15.80           N  
ATOM   1827  CA  ASN B 120      15.028  19.287  16.345  1.00 15.58           C  
ATOM   1828  C   ASN B 120      15.498  18.542  17.562  1.00 15.84           C  
ATOM   1829  O   ASN B 120      15.664  19.083  18.652  1.00 16.19           O  
ATOM   1830  CB  ASN B 120      16.121  19.413  15.286  1.00 15.04           C  
ATOM   1831  CG  ASN B 120      17.223  20.351  15.679  1.00 15.75           C  
ATOM   1832  OD1 ASN B 120      17.864  20.170  16.711  1.00 16.13           O  
ATOM   1833  ND2 ASN B 120      17.480  21.362  14.838  1.00 16.18           N  
ATOM   1834  N   ILE B 121      15.673  17.234  17.363  1.00 13.87           N  
ATOM   1835  CA  ILE B 121      16.077  16.285  18.394  1.00 14.10           C  
ATOM   1836  C   ILE B 121      17.353  15.605  17.905  1.00 14.66           C  
ATOM   1837  O   ILE B 121      17.442  15.218  16.736  1.00 15.44           O  
ATOM   1838  CB  ILE B 121      15.015  15.188  18.591  1.00 14.04           C  
ATOM   1839  CG1 ILE B 121      13.638  15.801  18.866  1.00 15.77           C  
ATOM   1840  CG2 ILE B 121      15.422  14.195  19.727  1.00 13.87           C  
ATOM   1841  CD1 ILE B 121      12.501  14.816  18.555  1.00 15.78           C  
ATOM   1842  N   SER B 122      18.304  15.432  18.814  1.00 14.67           N  
ATOM   1843  CA  SER B 122      19.578  14.753  18.568  1.00 14.96           C  
ATOM   1844  C   SER B 122      20.055  14.231  19.921  1.00 13.54           C  
ATOM   1845  O   SER B 122      19.260  14.107  20.843  1.00 16.24           O  
ATOM   1846  CB  SER B 122      20.556  15.703  17.903  1.00 14.92           C  
ATOM   1847  OG  SER B 122      20.739  16.885  18.676  1.00 16.31           O  
ATOM   1848  N   SER B 123      21.327  13.879  20.050  1.00 15.30           N  
ATOM   1849  CA  SER B 123      21.842  13.424  21.330  1.00 14.26           C  
ATOM   1850  C   SER B 123      23.256  13.882  21.511  1.00 15.00           C  
ATOM   1851  O   SER B 123      23.950  14.199  20.528  1.00 17.21           O  
ATOM   1852  CB  SER B 123      21.781  11.897  21.438  1.00 17.62           C  
ATOM   1853  OG  SER B 123      22.630  11.313  20.445  1.00 18.85           O  
HETATM 1854  N   MSE B 124      23.681  13.945  22.759  1.00 15.75           N  
HETATM 1855  CA  MSE B 124      25.108  14.097  23.074  1.00 17.02           C  
HETATM 1856  C   MSE B 124      25.389  13.108  24.190  1.00 16.77           C  
HETATM 1857  O   MSE B 124      24.733  13.145  25.222  1.00 17.19           O  
HETATM 1858  CB  MSE B 124      25.448  15.510  23.534  1.00 19.63           C  
HETATM 1859  CG  MSE B 124      25.211  16.538  22.481  1.00 16.21           C  
HETATM 1860 SE   MSE B 124      25.857  18.317  22.991  0.75 18.08          SE  
HETATM 1861  CE  MSE B 124      27.728  18.024  22.774  1.00 20.40           C  
ATOM   1862  N   ASN B 125      26.351  12.202  23.995  1.00 18.15           N  
ATOM   1863  CA  ASN B 125      26.645  11.171  24.987  1.00 19.40           C  
ATOM   1864  C   ASN B 125      25.380  10.368  25.350  1.00 18.60           C  
ATOM   1865  O   ASN B 125      25.134  10.045  26.525  1.00 18.94           O  
ATOM   1866  CB  ASN B 125      27.282  11.782  26.236  1.00 21.70           C  
ATOM   1867  CG  ASN B 125      28.400  12.748  25.909  1.00 31.05           C  
ATOM   1868  OD1 ASN B 125      28.301  13.947  26.209  1.00 45.15           O  
ATOM   1869  ND2 ASN B 125      29.449  12.249  25.250  1.00 34.64           N  
ATOM   1870  N   GLU B 126      24.607  10.063  24.313  1.00 17.12           N  
ATOM   1871  CA  GLU B 126      23.328   9.330  24.383  1.00 17.94           C  
ATOM   1872  C   GLU B 126      22.164  10.051  25.053  1.00 19.48           C  
ATOM   1873  O   GLU B 126      21.057   9.488  25.129  1.00 19.24           O  
ATOM   1874  CB  GLU B 126      23.493   7.965  25.055  1.00 19.66           C  
ATOM   1875  CG  GLU B 126      24.518   7.058  24.423  1.00 20.10           C  
ATOM   1876  CD  GLU B 126      24.600   5.735  25.127  1.00 18.97           C  
ATOM   1877  OE1 GLU B 126      23.585   5.002  25.144  1.00 16.09           O  
ATOM   1878  OE2 GLU B 126      25.664   5.411  25.684  1.00 19.06           O  
ATOM   1879  N   GLN B 127      22.377  11.278  25.511  1.00 17.20           N  
ATOM   1880  CA  GLN B 127      21.347  12.036  26.199  1.00 16.26           C  
ATOM   1881  C   GLN B 127      20.579  12.872  25.211  1.00 14.90           C  
ATOM   1882  O   GLN B 127      21.173  13.549  24.400  1.00 15.83           O  
ATOM   1883  CB  GLN B 127      21.972  12.911  27.264  1.00 18.20           C  
ATOM   1884  CG  GLN B 127      22.730  12.059  28.266  1.00 21.61           C  
ATOM   1885  CD  GLN B 127      23.162  12.825  29.442  1.00 32.10           C  
ATOM   1886  OE1 GLN B 127      23.768  13.873  29.309  1.00 32.48           O  
ATOM   1887  NE2 GLN B 127      22.881  12.301  30.622  1.00 39.00           N  
ATOM   1888  N   VAL B 128      19.253  12.816  25.317  1.00 15.21           N  
ATOM   1889  CA  VAL B 128      18.379  13.595  24.463  1.00 16.39           C  
ATOM   1890  C   VAL B 128      18.806  15.064  24.455  1.00 14.96           C  
ATOM   1891  O   VAL B 128      19.095  15.636  25.519  1.00 18.43           O  
ATOM   1892  CB  VAL B 128      16.893  13.492  24.944  1.00 15.99           C  
ATOM   1893  CG1 VAL B 128      16.035  14.561  24.270  1.00 23.80           C  
ATOM   1894  CG2 VAL B 128      16.364  12.122  24.681  1.00 19.64           C  
ATOM   1895  N   TYR B 129      18.879  15.646  23.256  1.00 14.93           N  
ATOM   1896  CA  TYR B 129      19.247  17.050  23.077  1.00 15.54           C  
ATOM   1897  C   TYR B 129      18.216  17.704  22.207  1.00 16.32           C  
ATOM   1898  O   TYR B 129      18.090  17.347  21.059  1.00 16.47           O  
ATOM   1899  CB  TYR B 129      20.647  17.172  22.469  1.00 16.61           C  
ATOM   1900  CG  TYR B 129      21.215  18.571  22.468  1.00 16.72           C  
ATOM   1901  CD1 TYR B 129      20.832  19.510  21.523  1.00 20.07           C  
ATOM   1902  CD2 TYR B 129      22.149  18.946  23.415  1.00 20.25           C  
ATOM   1903  CE1 TYR B 129      21.377  20.785  21.533  1.00 20.02           C  
ATOM   1904  CE2 TYR B 129      22.685  20.209  23.439  1.00 22.48           C  
ATOM   1905  CZ  TYR B 129      22.304  21.128  22.487  1.00 21.82           C  
ATOM   1906  OH  TYR B 129      22.859  22.400  22.496  1.00 21.61           O  
ATOM   1907  N  ALEU B 130      17.442  18.640  22.765  0.60 17.28           N  
ATOM   1908  N  BLEU B 130      17.495  18.665  22.783  0.40 15.48           N  
ATOM   1909  CA ALEU B 130      16.388  19.333  22.015  0.60 16.91           C  
ATOM   1910  CA BLEU B 130      16.525  19.429  22.038  0.40 14.15           C  
ATOM   1911  C  ALEU B 130      16.821  20.775  21.769  0.60 17.12           C  
ATOM   1912  C  BLEU B 130      17.114  20.774  21.715  0.40 14.41           C  
ATOM   1913  O  ALEU B 130      17.128  21.480  22.716  0.60 20.32           O  
ATOM   1914  O  BLEU B 130      17.858  21.385  22.497  0.40 12.74           O  
ATOM   1915  CB ALEU B 130      15.042  19.293  22.770  0.60 18.19           C  
ATOM   1916  CB BLEU B 130      15.228  19.621  22.821  0.40 15.30           C  
ATOM   1917  CG ALEU B 130      14.077  18.123  22.498  0.60 18.93           C  
ATOM   1918  CG BLEU B 130      14.509  18.342  23.233  0.40 12.59           C  
ATOM   1919  CD1ALEU B 130      14.690  16.795  22.820  0.60 21.39           C  
ATOM   1920  CD1BLEU B 130      13.171  18.690  23.833  0.40 16.53           C  
ATOM   1921  CD2ALEU B 130      12.765  18.293  23.273  0.60 18.40           C  
ATOM   1922  CD2BLEU B 130      14.349  17.400  22.051  0.40 12.62           C  
ATOM   1923  N   HIS B 131      16.837  21.195  20.499  1.00 15.67           N  
ATOM   1924  CA  HIS B 131      17.130  22.554  20.100  1.00 16.11           C  
ATOM   1925  C   HIS B 131      15.822  23.134  19.557  1.00 15.33           C  
ATOM   1926  O   HIS B 131      15.372  22.718  18.498  1.00 15.12           O  
ATOM   1927  CB  HIS B 131      18.233  22.579  19.053  1.00 16.22           C  
ATOM   1928  CG  HIS B 131      18.696  23.952  18.703  1.00 17.21           C  
ATOM   1929  ND1 HIS B 131      19.432  24.211  17.573  1.00 18.32           N  
ATOM   1930  CD2 HIS B 131      18.529  25.143  19.328  1.00 20.66           C  
ATOM   1931  CE1 HIS B 131      19.702  25.506  17.516  1.00 23.39           C  
ATOM   1932  NE2 HIS B 131      19.157  26.092  18.564  1.00 20.61           N  
ATOM   1933  N   LEU B 132      15.199  24.031  20.307  1.00 15.56           N  
ATOM   1934  CA  LEU B 132      13.878  24.542  20.003  1.00 14.94           C  
ATOM   1935  C   LEU B 132      13.876  26.060  19.928  1.00 13.48           C  
ATOM   1936  O   LEU B 132      14.426  26.749  20.800  1.00 14.38           O  
ATOM   1937  CB  LEU B 132      12.910  24.131  21.110  1.00 15.07           C  
ATOM   1938  CG  LEU B 132      12.880  22.656  21.517  1.00 16.41           C  
ATOM   1939  CD1 LEU B 132      11.989  22.477  22.758  1.00 16.40           C  
ATOM   1940  CD2 LEU B 132      12.424  21.840  20.356  1.00 18.40           C  
ATOM   1941  N   HIS B 133      13.298  26.572  18.855  1.00 13.70           N  
ATOM   1942  CA  HIS B 133      13.039  28.010  18.683  1.00 15.03           C  
ATOM   1943  C   HIS B 133      11.525  28.191  18.646  1.00 14.87           C  
ATOM   1944  O   HIS B 133      10.767  27.233  18.481  1.00 14.59           O  
ATOM   1945  CB  HIS B 133      13.703  28.551  17.431  1.00 14.39           C  
ATOM   1946  CG  HIS B 133      15.186  28.700  17.521  1.00 14.82           C  
ATOM   1947  ND1 HIS B 133      15.891  29.480  16.638  1.00 15.95           N  
ATOM   1948  CD2 HIS B 133      16.096  28.202  18.389  1.00 14.44           C  
ATOM   1949  CE1 HIS B 133      17.178  29.438  16.941  1.00 16.75           C  
ATOM   1950  NE2 HIS B 133      17.332  28.689  18.014  1.00 16.11           N  
ATOM   1951  N   ILE B 134      11.084  29.427  18.805  1.00 13.11           N  
ATOM   1952  CA  ILE B 134       9.679  29.716  18.947  1.00 13.46           C  
ATOM   1953  C   ILE B 134       9.353  31.104  18.464  1.00 14.10           C  
ATOM   1954  O   ILE B 134      10.189  32.016  18.536  1.00 13.43           O  
ATOM   1955  CB  ILE B 134       9.258  29.534  20.431  1.00 14.06           C  
ATOM   1956  CG1 ILE B 134       7.741  29.370  20.575  1.00 14.41           C  
ATOM   1957  CG2 ILE B 134       9.836  30.631  21.306  1.00 14.26           C  
ATOM   1958  CD1 ILE B 134       7.277  28.945  21.972  1.00 15.57           C  
ATOM   1959  N   THR B 135       8.128  31.250  17.986  1.00 14.56           N  
ATOM   1960  CA  THR B 135       7.538  32.539  17.649  1.00 12.85           C  
ATOM   1961  C   THR B 135       6.195  32.589  18.375  1.00 13.84           C  
ATOM   1962  O   THR B 135       5.423  31.646  18.313  1.00 13.18           O  
ATOM   1963  CB  THR B 135       7.291  32.689  16.145  1.00 13.47           C  
ATOM   1964  OG1 THR B 135       8.478  32.333  15.425  1.00 15.64           O  
ATOM   1965  CG2 THR B 135       6.824  34.109  15.768  1.00 13.68           C  
ATOM   1966  N   VAL B 136       5.941  33.663  19.108  1.00 13.63           N  
ATOM   1967  CA  VAL B 136       4.705  33.829  19.827  1.00 12.55           C  
ATOM   1968  C   VAL B 136       4.040  35.161  19.472  1.00 13.87           C  
ATOM   1969  O   VAL B 136       4.727  36.114  19.053  1.00 15.05           O  
ATOM   1970  CB  VAL B 136       4.894  33.768  21.365  1.00 14.15           C  
ATOM   1971  CG1 VAL B 136       5.532  32.411  21.816  1.00 15.17           C  
ATOM   1972  CG2 VAL B 136       5.702  34.931  21.877  1.00 14.82           C  
ATOM   1973  N   GLY B 137       2.721  35.220  19.672  1.00 14.07           N  
ATOM   1974  CA  GLY B 137       1.946  36.449  19.557  1.00 14.01           C  
ATOM   1975  C   GLY B 137       1.432  36.876  20.917  1.00 14.48           C  
ATOM   1976  O   GLY B 137       1.015  36.062  21.731  1.00 15.21           O  
ATOM   1977  N   ARG B 138       1.499  38.179  21.159  1.00 14.24           N  
ATOM   1978  CA  ARG B 138       1.052  38.793  22.394  1.00 13.66           C  
ATOM   1979  C   ARG B 138      -0.389  39.249  22.241  1.00 14.88           C  
ATOM   1980  O   ARG B 138      -0.994  39.120  21.162  1.00 14.66           O  
ATOM   1981  CB  ARG B 138       1.969  39.979  22.730  1.00 14.80           C  
ATOM   1982  CG  ARG B 138       3.455  39.625  22.788  1.00 15.12           C  
ATOM   1983  CD  ARG B 138       4.321  40.830  23.089  1.00 14.35           C  
ATOM   1984  NE  ARG B 138       4.435  41.031  24.511  1.00 15.17           N  
ATOM   1985  CZ  ARG B 138       5.326  41.841  25.054  1.00 17.15           C  
ATOM   1986  NH1 ARG B 138       6.140  42.576  24.297  1.00 17.66           N  
ATOM   1987  NH2 ARG B 138       5.410  41.935  26.383  1.00 18.08           N  
ATOM   1988  N   SER B 139      -0.972  39.806  23.313  1.00 15.02           N  
ATOM   1989  CA  SER B 139      -2.337  40.257  23.269  1.00 14.81           C  
ATOM   1990  C   SER B 139      -2.559  41.424  22.320  1.00 14.53           C  
ATOM   1991  O   SER B 139      -3.720  41.688  21.973  1.00 17.29           O  
ATOM   1992  CB  SER B 139      -2.789  40.642  24.660  1.00 16.19           C  
ATOM   1993  OG  SER B 139      -2.067  41.771  25.117  1.00 17.11           O  
ATOM   1994  N   ASP B 140      -1.491  42.122  21.922  1.00 15.54           N  
ATOM   1995  CA  ASP B 140      -1.577  43.155  20.879  1.00 15.07           C  
ATOM   1996  C   ASP B 140      -1.176  42.645  19.500  1.00 15.13           C  
ATOM   1997  O   ASP B 140      -1.027  43.421  18.563  1.00 15.64           O  
ATOM   1998  CB  ASP B 140      -0.747  44.379  21.255  1.00 15.43           C  
ATOM   1999  CG  ASP B 140       0.768  44.126  21.212  1.00 16.73           C  
ATOM   2000  OD1 ASP B 140       1.198  42.974  21.029  1.00 15.15           O  
ATOM   2001  OD2 ASP B 140       1.558  45.101  21.376  1.00 20.69           O  
ATOM   2002  N   TYR B 141      -1.050  41.336  19.410  1.00 14.68           N  
ATOM   2003  CA  TYR B 141      -0.751  40.623  18.170  1.00 14.65           C  
ATOM   2004  C   TYR B 141       0.677  40.786  17.688  1.00 15.45           C  
ATOM   2005  O   TYR B 141       1.035  40.204  16.686  1.00 15.77           O  
ATOM   2006  CB  TYR B 141      -1.776  40.928  17.044  1.00 16.48           C  
ATOM   2007  CG  TYR B 141      -3.220  40.735  17.519  1.00 14.78           C  
ATOM   2008  CD1 TYR B 141      -3.814  39.466  17.507  1.00 18.28           C  
ATOM   2009  CD2 TYR B 141      -3.930  41.784  17.994  1.00 17.45           C  
ATOM   2010  CE1 TYR B 141      -5.089  39.304  17.970  1.00 18.43           C  
ATOM   2011  CE2 TYR B 141      -5.204  41.619  18.443  1.00 19.27           C  
ATOM   2012  CZ  TYR B 141      -5.772  40.392  18.421  1.00 19.67           C  
ATOM   2013  OH  TYR B 141      -7.082  40.343  18.891  1.00 22.91           O  
ATOM   2014  N   SER B 142       1.496  41.579  18.373  1.00 14.87           N  
ATOM   2015  CA  SER B 142       2.902  41.648  18.032  1.00 13.18           C  
ATOM   2016  C   SER B 142       3.574  40.334  18.337  1.00 14.94           C  
ATOM   2017  O   SER B 142       3.119  39.582  19.209  1.00 15.48           O  
ATOM   2018  CB  SER B 142       3.586  42.787  18.807  1.00 13.85           C  
ATOM   2019  OG  SER B 142       3.656  42.512  20.198  1.00 15.60           O  
ATOM   2020  N   ALA B 143       4.624  40.029  17.580  1.00 14.71           N  
ATOM   2021  CA  ALA B 143       5.332  38.772  17.707  1.00 13.69           C  
ATOM   2022  C   ALA B 143       6.653  38.939  18.420  1.00 14.69           C  
ATOM   2023  O   ALA B 143       7.376  39.941  18.202  1.00 16.29           O  
ATOM   2024  CB  ALA B 143       5.547  38.132  16.306  1.00 14.68           C  
ATOM   2025  N   LEU B 144       6.971  37.946  19.252  1.00 14.01           N  
ATOM   2026  CA  LEU B 144       8.283  37.760  19.847  1.00 13.84           C  
ATOM   2027  C   LEU B 144       8.865  36.478  19.284  1.00 13.49           C  
ATOM   2028  O   LEU B 144       8.140  35.569  18.929  1.00 14.59           O  
ATOM   2029  CB  LEU B 144       8.218  37.670  21.367  1.00 15.56           C  
ATOM   2030  CG  LEU B 144       7.542  38.820  22.095  1.00 15.59           C  
ATOM   2031  CD1 LEU B 144       7.268  38.450  23.568  1.00 17.11           C  
ATOM   2032  CD2 LEU B 144       8.358  40.139  21.947  1.00 15.86           C  
ATOM   2033  N   ALA B 145      10.178  36.397  19.168  1.00 13.63           N  
ATOM   2034  CA  ALA B 145      10.811  35.222  18.590  1.00 14.59           C  
ATOM   2035  C   ALA B 145      12.190  35.014  19.145  1.00 14.78           C  
ATOM   2036  O   ALA B 145      12.918  35.975  19.443  1.00 14.48           O  
ATOM   2037  CB  ALA B 145      10.895  35.342  17.055  1.00 15.26           C  
ATOM   2038  N   GLY B 146      12.580  33.762  19.250  1.00 14.13           N  
ATOM   2039  CA  GLY B 146      13.920  33.448  19.661  1.00 15.74           C  
ATOM   2040  C   GLY B 146      14.157  32.022  20.028  1.00 14.10           C  
ATOM   2041  O   GLY B 146      13.371  31.145  19.712  1.00 14.38           O  
ATOM   2042  N  AHIS B 147      15.295  31.793  20.665  0.50 14.20           N  
ATOM   2043  N  BHIS B 147      15.269  31.792  20.709  0.50 15.33           N  
ATOM   2044  CA AHIS B 147      15.654  30.485  21.188  0.50 13.97           C  
ATOM   2045  CA BHIS B 147      15.641  30.454  21.166  0.50 15.89           C  
ATOM   2046  C  AHIS B 147      14.788  30.250  22.416  0.50 12.01           C  
ATOM   2047  C  BHIS B 147      14.930  30.153  22.480  0.50 15.63           C  
ATOM   2048  O  AHIS B 147      14.723  31.112  23.304  0.50 11.73           O  
ATOM   2049  O  BHIS B 147      15.151  30.830  23.490  0.50 17.39           O  
ATOM   2050  CB AHIS B 147      17.140  30.490  21.515  0.50 15.84           C  
ATOM   2051  CB BHIS B 147      17.163  30.365  21.235  0.50 17.08           C  
ATOM   2052  CG AHIS B 147      17.682  29.186  22.006  0.50 17.02           C  
ATOM   2053  CG BHIS B 147      17.703  29.283  22.114  0.50 18.53           C  
ATOM   2054  ND1AHIS B 147      18.482  28.363  21.232  0.50 16.54           N  
ATOM   2055  ND1BHIS B 147      17.251  27.978  22.101  0.50 19.94           N  
ATOM   2056  CD2AHIS B 147      17.576  28.582  23.214  0.50 17.15           C  
ATOM   2057  CD2BHIS B 147      18.751  29.306  22.967  0.50 17.13           C  
ATOM   2058  CE1AHIS B 147      18.847  27.313  21.955  0.50 12.24           C  
ATOM   2059  CE1BHIS B 147      17.979  27.263  22.946  0.50 20.05           C  
ATOM   2060  NE2AHIS B 147      18.300  27.414  23.152  0.50 16.78           N  
ATOM   2061  NE2BHIS B 147      18.888  28.051  23.486  0.50 17.52           N  
ATOM   2062  N   LEU B 148      14.118  29.098  22.452  1.00 15.43           N  
ATOM   2063  CA  LEU B 148      13.243  28.719  23.576  1.00 14.69           C  
ATOM   2064  C   LEU B 148      13.953  28.000  24.695  1.00 15.48           C  
ATOM   2065  O   LEU B 148      14.580  26.968  24.466  1.00 16.11           O  
ATOM   2066  CB  LEU B 148      12.133  27.808  23.074  1.00 15.45           C  
ATOM   2067  CG  LEU B 148      11.129  27.264  24.105  1.00 13.83           C  
ATOM   2068  CD1 LEU B 148      10.317  28.388  24.726  1.00 16.90           C  
ATOM   2069  CD2 LEU B 148      10.219  26.195  23.459  1.00 14.75           C  
ATOM   2070  N  ALEU B 149      13.924  28.559  25.893  0.60 16.24           N  
ATOM   2071  N  BLEU B 149      13.767  28.539  25.909  0.40 13.52           N  
ATOM   2072  CA ALEU B 149      14.462  27.854  27.060  0.60 15.72           C  
ATOM   2073  CA BLEU B 149      14.206  27.897  27.159  0.40 11.88           C  
ATOM   2074  C  ALEU B 149      13.345  27.014  27.698  0.60 16.27           C  
ATOM   2075  C  BLEU B 149      13.029  27.311  27.958  0.40 13.28           C  
ATOM   2076  O  ALEU B 149      13.517  25.858  28.070  0.60 18.65           O  
ATOM   2077  O  BLEU B 149      13.165  26.206  28.473  0.40 10.75           O  
ATOM   2078  CB ALEU B 149      15.018  28.853  28.070  0.60 16.93           C  
ATOM   2079  CB BLEU B 149      14.994  28.846  28.065  0.40 13.08           C  
ATOM   2080  CG ALEU B 149      15.560  28.342  29.395  0.60 18.13           C  
ATOM   2081  CG BLEU B 149      16.262  29.525  27.553  0.40 11.02           C  
ATOM   2082  CD1ALEU B 149      16.636  27.278  29.161  0.60 19.94           C  
ATOM   2083  CD1BLEU B 149      16.917  30.218  28.757  0.40 11.84           C  
ATOM   2084  CD2ALEU B 149      16.101  29.535  30.157  0.60 19.10           C  
ATOM   2085  CD2BLEU B 149      17.241  28.583  26.862  0.40 11.64           C  
ATOM   2086  N  ASER B 150      12.191  27.691  27.888  0.50 14.72           N  
ATOM   2087  N  BSER B 150      11.912  28.028  28.127  0.50 13.88           N  
ATOM   2088  CA ASER B 150      10.984  27.181  28.591  0.50 15.11           C  
ATOM   2089  CA BSER B 150      10.855  27.476  28.915  0.50 13.36           C  
ATOM   2090  C  ASER B 150       9.679  27.980  28.315  0.50 14.38           C  
ATOM   2091  C  BSER B 150       9.596  28.107  28.450  0.50 13.13           C  
ATOM   2092  O  ASER B 150       9.730  29.131  27.918  0.50 15.26           O  
ATOM   2093  O  BSER B 150       9.590  29.245  27.985  0.50 13.63           O  
ATOM   2094  CB ASER B 150      11.217  27.168  30.109  0.50 16.64           C  
ATOM   2095  CB BSER B 150      11.104  27.802  30.378  0.50 14.33           C  
ATOM   2096  OG ASER B 150      11.300  28.474  30.674  0.50 18.28           O  
ATOM   2097  OG BSER B 150      10.001  27.438  31.162  0.50 16.92           O  
ATOM   2098  N   ALA B 151       8.516  27.357  28.541  1.00 15.54           N  
ATOM   2099  CA  ALA B 151       7.228  27.993  28.350  1.00 15.72           C  
ATOM   2100  C   ALA B 151       6.191  27.196  29.098  1.00 16.26           C  
ATOM   2101  O   ALA B 151       6.206  25.974  29.054  1.00 16.47           O  
ATOM   2102  CB  ALA B 151       6.884  28.096  26.864  1.00 15.04           C  
ATOM   2103  N   ILE B 152       5.267  27.877  29.757  1.00 15.90           N  
ATOM   2104  CA  ILE B 152       4.198  27.226  30.528  1.00 14.70           C  
ATOM   2105  C   ILE B 152       2.895  27.276  29.764  1.00 15.07           C  
ATOM   2106  O   ILE B 152       2.407  28.364  29.471  1.00 15.26           O  
ATOM   2107  CB  ILE B 152       3.999  27.865  31.906  1.00 16.87           C  
ATOM   2108  CG1 ILE B 152       5.281  27.748  32.729  1.00 16.26           C  
ATOM   2109  CG2 ILE B 152       2.844  27.155  32.623  1.00 18.61           C  
ATOM   2110  CD1 ILE B 152       5.514  26.347  33.262  1.00 22.22           C  
ATOM   2111  N   GLN B 153       2.326  26.108  29.450  1.00 14.63           N  
ATOM   2112  CA  GLN B 153       1.102  26.032  28.699  1.00 14.84           C  
ATOM   2113  C   GLN B 153      -0.061  26.596  29.503  1.00 14.21           C  
ATOM   2114  O   GLN B 153      -0.126  26.393  30.715  1.00 14.40           O  
ATOM   2115  CB  GLN B 153       0.828  24.588  28.358  1.00 15.58           C  
ATOM   2116  CG  GLN B 153      -0.375  24.383  27.478  1.00 14.73           C  
ATOM   2117  CD  GLN B 153      -0.372  22.991  26.876  1.00 16.42           C  
ATOM   2118  OE1 GLN B 153       0.675  22.523  26.395  1.00 16.62           O  
ATOM   2119  NE2 GLN B 153      -1.537  22.354  26.848  1.00 17.10           N  
ATOM   2120  N   ASN B 154      -0.937  27.336  28.826  1.00 13.95           N  
ATOM   2121  CA  ASN B 154      -2.184  27.882  29.374  1.00 14.53           C  
ATOM   2122  C   ASN B 154      -3.223  27.854  28.251  1.00 15.10           C  
ATOM   2123  O   ASN B 154      -3.542  28.855  27.635  1.00 16.07           O  
ATOM   2124  CB  ASN B 154      -2.016  29.278  29.959  1.00 15.62           C  
ATOM   2125  CG  ASN B 154      -3.167  29.660  30.840  1.00 16.05           C  
ATOM   2126  OD1 ASN B 154      -3.669  28.844  31.603  1.00 19.73           O  
ATOM   2127  ND2 ASN B 154      -3.541  30.906  30.794  1.00 18.20           N  
ATOM   2128  N   GLY B 155      -3.702  26.652  27.986  1.00 14.12           N  
ATOM   2129  CA  GLY B 155      -4.592  26.332  26.885  1.00 15.23           C  
ATOM   2130  C   GLY B 155      -4.171  24.997  26.309  1.00 16.30           C  
ATOM   2131  O   GLY B 155      -3.927  24.032  27.065  1.00 17.05           O  
ATOM   2132  N   ALA B 156      -4.099  24.929  24.985  1.00 17.00           N  
ATOM   2133  CA  ALA B 156      -3.720  23.718  24.272  1.00 15.22           C  
ATOM   2134  C   ALA B 156      -2.230  23.718  23.975  1.00 16.20           C  
ATOM   2135  O   ALA B 156      -1.537  24.740  24.045  1.00 16.52           O  
ATOM   2136  CB  ALA B 156      -4.502  23.591  22.953  1.00 19.86           C  
ATOM   2137  N   GLY B 157      -1.718  22.551  23.625  1.00 16.81           N  
ATOM   2138  CA  GLY B 157      -0.313  22.335  23.278  1.00 17.24           C  
ATOM   2139  C   GLY B 157      -0.302  21.149  22.365  1.00 16.97           C  
ATOM   2140  O   GLY B 157      -0.429  20.015  22.807  1.00 17.04           O  
ATOM   2141  N   GLU B 158      -0.159  21.426  21.080  1.00 14.77           N  
ATOM   2142  CA  GLU B 158      -0.371  20.451  20.014  1.00 14.88           C  
ATOM   2143  C   GLU B 158       0.875  20.387  19.176  1.00 14.85           C  
ATOM   2144  O   GLU B 158       1.154  21.295  18.392  1.00 15.65           O  
ATOM   2145  CB  GLU B 158      -1.581  20.893  19.187  1.00 14.99           C  
ATOM   2146  CG  GLU B 158      -2.860  20.878  20.028  1.00 15.85           C  
ATOM   2147  CD  GLU B 158      -4.082  21.469  19.378  1.00 16.55           C  
ATOM   2148  OE1 GLU B 158      -4.062  21.702  18.143  1.00 18.61           O  
ATOM   2149  OE2 GLU B 158      -5.082  21.671  20.115  1.00 16.75           O  
ATOM   2150  N   PHE B 159       1.632  19.305  19.328  1.00 16.66           N  
ATOM   2151  CA  PHE B 159       2.935  19.157  18.690  1.00 15.89           C  
ATOM   2152  C   PHE B 159       3.083  17.869  17.914  1.00 20.10           C  
ATOM   2153  O   PHE B 159       2.593  16.838  18.340  1.00 22.04           O  
ATOM   2154  CB  PHE B 159       4.052  19.261  19.751  1.00 19.09           C  
ATOM   2155  CG  PHE B 159       4.001  20.533  20.533  1.00 18.53           C  
ATOM   2156  CD1 PHE B 159       4.555  21.683  20.022  1.00 22.67           C  
ATOM   2157  CD2 PHE B 159       3.290  20.623  21.710  1.00 17.43           C  
ATOM   2158  CE1 PHE B 159       4.442  22.868  20.690  1.00 21.39           C  
ATOM   2159  CE2 PHE B 159       3.195  21.814  22.388  1.00 18.55           C  
ATOM   2160  CZ  PHE B 159       3.766  22.929  21.883  1.00 19.31           C  
ATOM   2161  N   VAL B 160       3.767  17.945  16.785  1.00 16.89           N  
ATOM   2162  CA  VAL B 160       4.069  16.788  15.969  1.00 16.46           C  
ATOM   2163  C   VAL B 160       5.548  16.499  16.138  1.00 16.66           C  
ATOM   2164  O   VAL B 160       6.369  17.376  15.928  1.00 16.18           O  
ATOM   2165  CB  VAL B 160       3.777  16.989  14.477  1.00 18.64           C  
ATOM   2166  CG1 VAL B 160       4.080  15.697  13.726  1.00 19.82           C  
ATOM   2167  CG2 VAL B 160       2.332  17.341  14.263  1.00 19.84           C  
ATOM   2168  N   VAL B 161       5.859  15.290  16.578  1.00 16.80           N  
ATOM   2169  CA  VAL B 161       7.228  14.860  16.784  1.00 17.25           C  
ATOM   2170  C   VAL B 161       7.500  13.780  15.753  1.00 18.90           C  
ATOM   2171  O   VAL B 161       6.865  12.708  15.789  1.00 22.06           O  
ATOM   2172  CB  VAL B 161       7.434  14.308  18.186  1.00 17.68           C  
ATOM   2173  CG1 VAL B 161       8.863  13.752  18.347  1.00 22.61           C  
ATOM   2174  CG2 VAL B 161       7.107  15.369  19.227  1.00 18.07           C  
ATOM   2175  N   GLU B 162       8.402  14.045  14.816  1.00 18.66           N  
ATOM   2176  CA  GLU B 162       8.805  13.046  13.835  1.00 19.69           C  
ATOM   2177  C   GLU B 162      10.024  12.338  14.369  1.00 16.38           C  
ATOM   2178  O   GLU B 162      10.962  12.986  14.768  1.00 18.57           O  
ATOM   2179  CB  GLU B 162       9.139  13.649  12.476  1.00 20.11           C  
ATOM   2180  CG  GLU B 162       9.511  12.560  11.453  1.00 23.04           C  
ATOM   2181  CD  GLU B 162       9.758  13.057  10.014  1.00 28.60           C  
ATOM   2182  OE1 GLU B 162       9.504  14.248   9.697  1.00 33.49           O  
ATOM   2183  OE2 GLU B 162      10.224  12.213   9.194  1.00 31.71           O  
ATOM   2184  N   ASP B 163       9.980  11.017  14.380  1.00 16.89           N  
ATOM   2185  CA  ASP B 163      11.081  10.162  14.826  1.00 16.75           C  
ATOM   2186  C   ASP B 163      11.838   9.682  13.606  1.00 16.81           C  
ATOM   2187  O   ASP B 163      11.261   8.977  12.769  1.00 18.28           O  
ATOM   2188  CB  ASP B 163      10.479   8.998  15.605  1.00 16.20           C  
ATOM   2189  CG  ASP B 163      11.499   8.036  16.156  1.00 17.53           C  
ATOM   2190  OD1 ASP B 163      12.728   8.217  15.989  1.00 16.63           O  
ATOM   2191  OD2 ASP B 163      11.035   7.033  16.764  1.00 18.46           O  
ATOM   2192  N   TYR B 164      13.112  10.059  13.502  1.00 15.83           N  
ATOM   2193  CA  TYR B 164      13.944   9.619  12.383  1.00 15.89           C  
ATOM   2194  C   TYR B 164      14.569   8.233  12.568  1.00 17.65           C  
ATOM   2195  O   TYR B 164      15.119   7.704  11.605  1.00 18.39           O  
ATOM   2196  CB  TYR B 164      15.098  10.587  12.141  1.00 16.41           C  
ATOM   2197  CG  TYR B 164      14.745  12.016  11.810  1.00 18.32           C  
ATOM   2198  CD1 TYR B 164      13.547  12.370  11.203  1.00 17.69           C  
ATOM   2199  CD2 TYR B 164      15.664  13.018  12.082  1.00 18.54           C  
ATOM   2200  CE1 TYR B 164      13.274  13.678  10.881  1.00 16.74           C  
ATOM   2201  CE2 TYR B 164      15.396  14.331  11.773  1.00 18.35           C  
ATOM   2202  CZ  TYR B 164      14.202  14.651  11.190  1.00 15.78           C  
ATOM   2203  OH  TYR B 164      13.915  15.961  10.873  1.00 20.67           O  
ATOM   2204  N   SER B 165      14.554   7.686  13.793  1.00 16.77           N  
ATOM   2205  CA  SER B 165      15.128   6.357  14.075  1.00 15.85           C  
ATOM   2206  C   SER B 165      16.617   6.251  13.699  1.00 17.67           C  
ATOM   2207  O   SER B 165      17.094   5.189  13.293  1.00 18.62           O  
ATOM   2208  CB  SER B 165      14.325   5.243  13.398  1.00 17.53           C  
ATOM   2209  OG  SER B 165      12.982   5.280  13.792  1.00 21.59           O  
ATOM   2210  N   GLU B 166      17.342   7.341  13.851  1.00 15.37           N  
ATOM   2211  CA  GLU B 166      18.761   7.434  13.520  1.00 19.37           C  
ATOM   2212  C   GLU B 166      19.498   8.242  14.557  1.00 16.55           C  
ATOM   2213  O   GLU B 166      19.064   9.322  14.950  1.00 16.97           O  
ATOM   2214  CB  GLU B 166      18.938   8.187  12.214  1.00 20.38           C  
ATOM   2215  CG  GLU B 166      18.509   7.422  11.002  1.00 29.95           C  
ATOM   2216  CD  GLU B 166      19.556   6.491  10.471  1.00 37.39           C  
ATOM   2217  OE1 GLU B 166      20.622   6.309  11.107  1.00 45.01           O  
ATOM   2218  OE2 GLU B 166      19.302   5.941   9.383  1.00 52.16           O  
ATOM   2219  N   ARG B 167      20.646   7.759  14.969  1.00 16.02           N  
ATOM   2220  CA  ARG B 167      21.519   8.502  15.841  1.00 20.01           C  
ATOM   2221  C   ARG B 167      22.098   9.725  15.102  1.00 21.76           C  
ATOM   2222  O   ARG B 167      22.606   9.607  13.964  1.00 22.32           O  
ATOM   2223  CB  ARG B 167      22.635   7.585  16.307  1.00 23.09           C  
ATOM   2224  CG  ARG B 167      23.486   8.145  17.381  1.00 27.29           C  
ATOM   2225  CD  ARG B 167      24.467   7.091  17.908  1.00 30.47           C  
ATOM   2226  NE  ARG B 167      25.657   7.801  18.348  1.00 42.42           N  
ATOM   2227  CZ  ARG B 167      26.609   8.249  17.534  1.00 41.05           C  
ATOM   2228  NH1 ARG B 167      26.547   8.069  16.209  1.00 46.29           N  
ATOM   2229  NH2 ARG B 167      27.613   8.915  18.067  1.00 39.30           N  
ATOM   2230  N   ILE B 168      21.997  10.898  15.735  1.00 18.85           N  
ATOM   2231  CA  ILE B 168      22.584  12.152  15.249  1.00 19.51           C  
ATOM   2232  C   ILE B 168      23.190  12.819  16.475  1.00 20.99           C  
ATOM   2233  O   ILE B 168      22.483  13.111  17.427  1.00 17.84           O  
ATOM   2234  CB  ILE B 168      21.583  13.117  14.621  1.00 19.14           C  
ATOM   2235  CG1 ILE B 168      20.954  12.504  13.372  1.00 21.34           C  
ATOM   2236  CG2 ILE B 168      22.304  14.436  14.245  1.00 18.95           C  
ATOM   2237  CD1 ILE B 168      20.003  13.453  12.639  1.00 21.71           C  
ATOM   2238  N  ASER B 169      24.502  13.021  16.460  0.50 19.85           N  
ATOM   2239  N  BSER B 169      24.506  13.002  16.460  0.50 21.58           N  
ATOM   2240  CA ASER B 169      25.211  13.603  17.582  0.50 18.96           C  
ATOM   2241  CA BSER B 169      25.235  13.584  17.575  0.50 22.38           C  
ATOM   2242  C  ASER B 169      25.636  15.024  17.274  0.50 18.30           C  
ATOM   2243  C  BSER B 169      25.681  14.999  17.265  0.50 20.14           C  
ATOM   2244  O  ASER B 169      25.461  15.529  16.153  0.50 18.60           O  
ATOM   2245  O  BSER B 169      25.580  15.467  16.127  0.50 21.39           O  
ATOM   2246  CB ASER B 169      26.443  12.762  17.927  0.50 18.32           C  
ATOM   2247  CB BSER B 169      26.458  12.730  17.922  0.50 22.61           C  
ATOM   2248  OG ASER B 169      27.041  13.148  19.160  0.50 15.65           O  
ATOM   2249  OG BSER B 169      26.073  11.475  18.458  0.50 31.13           O  
ATOM   2250  N   ARG B 170      26.138  15.675  18.315  1.00 19.51           N  
ATOM   2251  CA  ARG B 170      26.708  17.014  18.233  1.00 20.77           C  
ATOM   2252  C   ARG B 170      28.045  17.052  18.933  1.00 20.79           C  
ATOM   2253  O   ARG B 170      28.347  16.202  19.771  1.00 22.02           O  
ATOM   2254  CB  ARG B 170      25.799  18.024  18.926  1.00 20.96           C  
ATOM   2255  CG  ARG B 170      24.508  18.333  18.221  1.00 22.53           C  
ATOM   2256  CD  ARG B 170      23.588  19.112  19.126  1.00 20.60           C  
ATOM   2257  NE  ARG B 170      22.291  19.334  18.489  1.00 18.82           N  
ATOM   2258  CZ  ARG B 170      22.025  20.316  17.641  1.00 18.46           C  
ATOM   2259  NH1 ARG B 170      22.943  21.211  17.342  1.00 20.35           N  
ATOM   2260  NH2 ARG B 170      20.828  20.394  17.110  1.00 19.21           N  
ATOM   2261  N   THR B 171      28.854  18.034  18.587  1.00 20.92           N  
ATOM   2262  CA  THR B 171      30.157  18.241  19.224  1.00 22.18           C  
ATOM   2263  C   THR B 171      30.254  19.686  19.634  1.00 21.49           C  
ATOM   2264  O   THR B 171      29.967  20.579  18.821  1.00 20.43           O  
ATOM   2265  CB  THR B 171      31.288  17.928  18.276  1.00 24.53           C  
ATOM   2266  OG1 THR B 171      31.226  16.542  17.938  1.00 27.84           O  
ATOM   2267  CG2 THR B 171      32.648  18.232  18.907  1.00 25.73           C  
ATOM   2268  N   TYR B 172      30.638  19.905  20.887  1.00 21.81           N  
ATOM   2269  CA  TYR B 172      30.852  21.237  21.408  1.00 20.77           C  
ATOM   2270  C   TYR B 172      32.006  21.886  20.663  1.00 21.97           C  
ATOM   2271  O   TYR B 172      33.081  21.317  20.558  1.00 23.08           O  
ATOM   2272  CB  TYR B 172      31.167  21.180  22.902  1.00 22.48           C  
ATOM   2273  CG  TYR B 172      31.395  22.534  23.513  1.00 23.54           C  
ATOM   2274  CD1 TYR B 172      30.350  23.423  23.682  1.00 20.16           C  
ATOM   2275  CD2 TYR B 172      32.657  22.929  23.920  1.00 23.89           C  
ATOM   2276  CE1 TYR B 172      30.547  24.668  24.232  1.00 20.80           C  
ATOM   2277  CE2 TYR B 172      32.861  24.178  24.472  1.00 22.94           C  
ATOM   2278  CZ  TYR B 172      31.805  25.028  24.632  1.00 22.62           C  
ATOM   2279  OH  TYR B 172      32.007  26.262  25.191  1.00 26.46           O  
ATOM   2280  N   ASN B 173      31.755  23.059  20.105  1.00 20.90           N  
ATOM   2281  CA  ASN B 173      32.779  23.838  19.445  1.00 22.51           C  
ATOM   2282  C   ASN B 173      33.193  24.935  20.420  1.00 23.28           C  
ATOM   2283  O   ASN B 173      32.438  25.864  20.664  1.00 21.54           O  
ATOM   2284  CB  ASN B 173      32.238  24.403  18.135  1.00 21.76           C  
ATOM   2285  CG  ASN B 173      33.246  25.253  17.388  1.00 28.40           C  
ATOM   2286  OD1 ASN B 173      34.097  25.894  17.988  1.00 28.76           O  
ATOM   2287  ND2 ASN B 173      33.130  25.281  16.062  1.00 28.57           N  
ATOM   2288  N   PRO B 174      34.394  24.823  21.005  1.00 25.63           N  
ATOM   2289  CA  PRO B 174      34.796  25.810  22.006  1.00 26.18           C  
ATOM   2290  C   PRO B 174      35.087  27.196  21.452  1.00 25.77           C  
ATOM   2291  O   PRO B 174      35.004  28.153  22.209  1.00 28.70           O  
ATOM   2292  CB  PRO B 174      36.051  25.184  22.621  1.00 27.33           C  
ATOM   2293  CG  PRO B 174      36.601  24.335  21.555  1.00 27.89           C  
ATOM   2294  CD  PRO B 174      35.435  23.803  20.795  1.00 26.55           C  
ATOM   2295  N   ASP B 175      35.389  27.319  20.162  1.00 25.02           N  
ATOM   2296  CA  ASP B 175      35.538  28.637  19.542  1.00 27.19           C  
ATOM   2297  C   ASP B 175      34.214  29.404  19.526  1.00 25.96           C  
ATOM   2298  O   ASP B 175      34.198  30.619  19.701  1.00 26.14           O  
ATOM   2299  CB  ASP B 175      36.057  28.540  18.104  1.00 29.33           C  
ATOM   2300  CG  ASP B 175      37.422  27.896  18.012  1.00 39.69           C  
ATOM   2301  OD1 ASP B 175      38.103  27.746  19.055  1.00 45.53           O  
ATOM   2302  OD2 ASP B 175      37.813  27.539  16.877  1.00 52.12           O  
ATOM   2303  N   LEU B 176      33.108  28.700  19.303  1.00 22.72           N  
ATOM   2304  CA  LEU B 176      31.793  29.330  19.285  1.00 21.19           C  
ATOM   2305  C   LEU B 176      31.039  29.271  20.595  1.00 19.74           C  
ATOM   2306  O   LEU B 176      30.166  30.103  20.820  1.00 21.02           O  
ATOM   2307  CB  LEU B 176      30.920  28.680  18.218  1.00 23.23           C  
ATOM   2308  CG  LEU B 176      31.449  28.734  16.792  1.00 24.66           C  
ATOM   2309  CD1 LEU B 176      30.422  28.092  15.863  1.00 25.44           C  
ATOM   2310  CD2 LEU B 176      31.759  30.160  16.364  1.00 24.28           C  
ATOM   2311  N   GLY B 177      31.312  28.279  21.425  1.00 20.65           N  
ATOM   2312  CA  GLY B 177      30.519  28.063  22.632  1.00 20.88           C  
ATOM   2313  C   GLY B 177      29.167  27.420  22.344  1.00 20.04           C  
ATOM   2314  O   GLY B 177      28.235  27.565  23.125  1.00 21.49           O  
ATOM   2315  N   LEU B 178      29.099  26.658  21.249  1.00 20.14           N  
ATOM   2316  CA  LEU B 178      27.879  26.035  20.780  1.00 18.97           C  
ATOM   2317  C   LEU B 178      28.069  24.560  20.441  1.00 17.75           C  
ATOM   2318  O   LEU B 178      29.140  24.126  20.048  1.00 20.21           O  
ATOM   2319  CB  LEU B 178      27.401  26.750  19.519  1.00 19.75           C  
ATOM   2320  CG  LEU B 178      27.008  28.228  19.644  1.00 20.33           C  
ATOM   2321  CD1 LEU B 178      26.712  28.814  18.272  1.00 21.41           C  
ATOM   2322  CD2 LEU B 178      25.818  28.446  20.597  1.00 22.14           C  
ATOM   2323  N   ASN B 179      26.995  23.792  20.595  1.00 18.81           N  
ATOM   2324  CA  ASN B 179      26.977  22.365  20.269  1.00 18.12           C  
ATOM   2325  C   ASN B 179      26.468  22.239  18.852  1.00 19.66           C  
ATOM   2326  O   ASN B 179      25.303  22.511  18.572  1.00 20.30           O  
ATOM   2327  CB  ASN B 179      26.067  21.636  21.230  1.00 18.03           C  
ATOM   2328  CG  ASN B 179      26.536  21.773  22.632  1.00 19.14           C  
ATOM   2329  OD1 ASN B 179      27.684  21.493  22.914  1.00 20.95           O  
ATOM   2330  ND2 ASN B 179      25.668  22.247  23.516  1.00 18.05           N  
ATOM   2331  N   ILE B 180      27.357  21.841  17.964  1.00 19.35           N  
ATOM   2332  CA  ILE B 180      27.092  21.846  16.534  1.00 19.33           C  
ATOM   2333  C   ILE B 180      26.916  20.416  16.055  1.00 20.80           C  
ATOM   2334  O   ILE B 180      27.603  19.524  16.519  1.00 19.88           O  
ATOM   2335  CB  ILE B 180      28.277  22.539  15.783  1.00 19.64           C  
ATOM   2336  CG1 ILE B 180      28.436  24.013  16.216  1.00 20.87           C  
ATOM   2337  CG2 ILE B 180      28.152  22.447  14.237  1.00 19.92           C  
ATOM   2338  CD1 ILE B 180      27.279  24.931  15.928  1.00 22.24           C  
ATOM   2339  N   TYR B 181      25.990  20.193  15.128  1.00 18.79           N  
ATOM   2340  CA  TYR B 181      25.802  18.863  14.549  1.00 18.24           C  
ATOM   2341  C   TYR B 181      27.140  18.270  14.069  1.00 18.36           C  
ATOM   2342  O   TYR B 181      27.952  18.975  13.472  1.00 21.05           O  
ATOM   2343  CB  TYR B 181      24.896  18.927  13.341  1.00 19.08           C  
ATOM   2344  CG  TYR B 181      23.387  18.912  13.536  1.00 16.81           C  
ATOM   2345  CD1 TYR B 181      22.777  18.067  14.431  1.00 20.85           C  
ATOM   2346  CD2 TYR B 181      22.562  19.641  12.689  1.00 17.94           C  
ATOM   2347  CE1 TYR B 181      21.383  18.004  14.540  1.00 20.29           C  
ATOM   2348  CE2 TYR B 181      21.184  19.562  12.768  1.00 18.22           C  
ATOM   2349  CZ  TYR B 181      20.596  18.751  13.692  1.00 19.48           C  
ATOM   2350  OH  TYR B 181      19.236  18.619  13.779  1.00 18.58           O  
ATOM   2351  N   ASP B 182      27.355  16.997  14.358  1.00 19.11           N  
ATOM   2352  CA  ASP B 182      28.567  16.289  13.965  1.00 19.48           C  
ATOM   2353  C   ASP B 182      28.097  14.947  13.406  1.00 21.85           C  
ATOM   2354  O   ASP B 182      27.888  13.985  14.134  1.00 23.57           O  
ATOM   2355  CB  ASP B 182      29.491  16.123  15.158  1.00 20.69           C  
ATOM   2356  CG  ASP B 182      30.861  15.572  14.774  1.00 23.62           C  
ATOM   2357  OD1 ASP B 182      31.019  15.079  13.633  1.00 26.42           O  
ATOM   2358  OD2 ASP B 182      31.766  15.642  15.630  1.00 28.30           O  
ATOM   2359  N   PHE B 183      27.910  14.904  12.100  1.00 24.17           N  
ATOM   2360  CA  PHE B 183      27.341  13.723  11.470  1.00 25.02           C  
ATOM   2361  C   PHE B 183      28.325  12.565  11.341  1.00 27.85           C  
ATOM   2362  O   PHE B 183      27.894  11.446  11.085  1.00 29.83           O  
ATOM   2363  CB  PHE B 183      26.775  14.065  10.083  1.00 23.51           C  
ATOM   2364  CG  PHE B 183      25.695  15.118  10.102  1.00 21.28           C  
ATOM   2365  CD1 PHE B 183      24.584  15.004  10.938  1.00 23.43           C  
ATOM   2366  CD2 PHE B 183      25.781  16.223   9.279  1.00 23.17           C  
ATOM   2367  CE1 PHE B 183      23.602  15.963  10.950  1.00 21.71           C  
ATOM   2368  CE2 PHE B 183      24.804  17.189   9.294  1.00 23.24           C  
ATOM   2369  CZ  PHE B 183      23.715  17.064  10.130  1.00 21.91           C  
ATOM   2370  N   GLU B 184      29.616  12.819  11.543  1.00 30.62           N  
ATOM   2371  CA  GLU B 184      30.632  11.766  11.462  1.00 35.06           C  
ATOM   2372  C   GLU B 184      30.919  11.070  12.786  1.00 37.04           C  
ATOM   2373  O   GLU B 184      31.504   9.985  12.780  1.00 38.01           O  
ATOM   2374  CB  GLU B 184      31.932  12.342  10.881  1.00 36.24           C  
ATOM   2375  CG  GLU B 184      31.731  13.077   9.542  1.00 42.79           C  
ATOM   2376  CD  GLU B 184      30.964  12.240   8.516  1.00 50.89           C  
ATOM   2377  OE1 GLU B 184      31.263  11.031   8.396  1.00 61.18           O  
ATOM   2378  OE2 GLU B 184      30.059  12.775   7.838  1.00 59.23           O  
ATOM   2379  N   ARG B 185      30.522  11.644  13.917  1.00 37.22           N  
ATOM   2380  CA  ARG B 185      30.829  10.987  15.181  1.00 39.51           C  
ATOM   2381  C   ARG B 185      29.749   9.974  15.539  1.00 40.43           C  
ATOM   2382  O   ARG B 185      28.595  10.026  15.090  1.00 38.04           O  
ATOM   2383  CB  ARG B 185      31.043  11.997  16.305  1.00 40.40           C  
ATOM   2384  CG  ARG B 185      29.806  12.530  16.954  1.00 41.02           C  
ATOM   2385  CD  ARG B 185      30.172  13.495  18.058  1.00 38.66           C  
ATOM   2386  NE  ARG B 185      30.641  12.806  19.256  1.00 36.30           N  
ATOM   2387  CZ  ARG B 185      31.254  13.399  20.283  1.00 36.42           C  
ATOM   2388  NH1 ARG B 185      31.547  14.703  20.272  1.00 36.01           N  
ATOM   2389  NH2 ARG B 185      31.627  12.670  21.326  1.00 37.70           N  
ATOM   2390  OXT ARG B 185      30.048   9.070  16.322  1.00 41.29           O  
TER    2391      ARG B 185                                                      
ATOM   2392  N   ASN C  43     -14.200  26.777  -7.456  1.00 41.97           N  
ATOM   2393  CA  ASN C  43     -12.734  26.535  -7.582  1.00 38.50           C  
ATOM   2394  C   ASN C  43     -11.944  27.554  -6.770  1.00 32.92           C  
ATOM   2395  O   ASN C  43     -11.856  28.724  -7.139  1.00 36.80           O  
ATOM   2396  CB  ASN C  43     -12.284  26.599  -9.033  1.00 42.35           C  
ATOM   2397  CG  ASN C  43     -10.830  26.180  -9.204  1.00 46.46           C  
ATOM   2398  OD1 ASN C  43     -10.496  24.993  -9.059  1.00 56.29           O  
ATOM   2399  ND2 ASN C  43      -9.962  27.143  -9.529  1.00 48.47           N  
HETATM 2400  N  AMSE C  44     -11.394  27.111  -5.649  0.50 28.74           N  
HETATM 2401  N  BMSE C  44     -11.387  27.090  -5.661  0.50 27.73           N  
HETATM 2402  CA AMSE C  44     -10.609  27.976  -4.771  0.50 23.49           C  
HETATM 2403  CA BMSE C  44     -10.634  27.927  -4.742  0.50 21.39           C  
HETATM 2404  C  AMSE C  44      -9.118  27.654  -4.752  0.50 21.62           C  
HETATM 2405  C  BMSE C  44      -9.133  27.657  -4.761  0.50 20.42           C  
HETATM 2406  O  AMSE C  44      -8.345  28.406  -4.163  0.50 19.72           O  
HETATM 2407  O  BMSE C  44      -8.372  28.446  -4.210  0.50 17.71           O  
HETATM 2408  CB AMSE C  44     -11.168  27.901  -3.353  0.50 22.55           C  
HETATM 2409  CB BMSE C  44     -11.161  27.695  -3.332  0.50 20.09           C  
HETATM 2410  CG AMSE C  44     -12.373  28.793  -3.136  0.50 19.88           C  
HETATM 2411  CG BMSE C  44     -12.664  27.885  -3.220  0.50 18.48           C  
HETATM 2412 SE  AMSE C  44     -13.086  28.539  -1.354  0.38 22.89          SE  
HETATM 2413 SE  BMSE C  44     -13.297  27.772  -1.419  0.37 17.30          SE  
HETATM 2414  CE AMSE C  44     -13.912  26.800  -1.829  0.50 19.43           C  
HETATM 2415  CE BMSE C  44     -12.536  29.473  -0.739  0.50 23.75           C  
ATOM   2416  N   TYR C  45      -8.718  26.568  -5.404  1.00 18.92           N  
ATOM   2417  CA  TYR C  45      -7.334  26.134  -5.402  1.00 17.41           C  
ATOM   2418  C   TYR C  45      -7.034  25.154  -6.521  1.00 16.03           C  
ATOM   2419  O   TYR C  45      -7.949  24.626  -7.200  1.00 17.70           O  
ATOM   2420  CB  TYR C  45      -7.023  25.420  -4.060  1.00 17.58           C  
ATOM   2421  CG  TYR C  45      -8.049  24.347  -3.733  1.00 18.81           C  
ATOM   2422  CD1 TYR C  45      -8.052  23.120  -4.393  1.00 17.44           C  
ATOM   2423  CD2 TYR C  45      -9.062  24.590  -2.821  1.00 19.48           C  
ATOM   2424  CE1 TYR C  45      -9.038  22.157  -4.134  1.00 19.24           C  
ATOM   2425  CE2 TYR C  45     -10.040  23.648  -2.569  1.00 17.88           C  
ATOM   2426  CZ  TYR C  45     -10.018  22.447  -3.207  1.00 21.60           C  
ATOM   2427  OH  TYR C  45     -10.974  21.517  -2.951  1.00 25.48           O  
ATOM   2428  N  ASER C  46      -5.746  24.916  -6.732  0.50 16.20           N  
ATOM   2429  N  BSER C  46      -5.734  24.942  -6.725  0.50 16.98           N  
ATOM   2430  CA ASER C  46      -5.272  23.803  -7.554  0.50 14.87           C  
ATOM   2431  CA BSER C  46      -5.181  23.884  -7.573  0.50 16.86           C  
ATOM   2432  C  ASER C  46      -4.273  23.060  -6.683  0.50 14.23           C  
ATOM   2433  C  BSER C  46      -4.303  23.049  -6.652  0.50 15.29           C  
ATOM   2434  O  ASER C  46      -3.782  23.604  -5.679  0.50 15.64           O  
ATOM   2435  O  BSER C  46      -3.924  23.524  -5.567  0.50 16.53           O  
ATOM   2436  CB ASER C  46      -4.613  24.279  -8.840  0.50 16.66           C  
ATOM   2437  CB BSER C  46      -4.310  24.462  -8.683  0.50 18.09           C  
ATOM   2438  OG ASER C  46      -3.592  25.221  -8.574  0.50 16.29           O  
ATOM   2439  OG BSER C  46      -5.033  25.361  -9.503  0.50 24.73           O  
ATOM   2440  N   TYR C  47      -3.961  21.827  -7.047  1.00 15.68           N  
ATOM   2441  CA  TYR C  47      -3.113  21.018  -6.211  1.00 16.22           C  
ATOM   2442  C   TYR C  47      -2.455  19.899  -6.974  1.00 15.57           C  
ATOM   2443  O   TYR C  47      -2.860  19.577  -8.093  1.00 16.46           O  
ATOM   2444  CB  TYR C  47      -3.923  20.443  -5.035  1.00 16.24           C  
ATOM   2445  CG  TYR C  47      -4.897  19.366  -5.437  1.00 18.30           C  
ATOM   2446  CD1 TYR C  47      -6.180  19.670  -5.863  1.00 22.71           C  
ATOM   2447  CD2 TYR C  47      -4.517  18.027  -5.384  1.00 20.63           C  
ATOM   2448  CE1 TYR C  47      -7.071  18.650  -6.244  1.00 24.54           C  
ATOM   2449  CE2 TYR C  47      -5.394  17.030  -5.742  1.00 22.31           C  
ATOM   2450  CZ  TYR C  47      -6.656  17.345  -6.158  1.00 24.81           C  
ATOM   2451  OH  TYR C  47      -7.491  16.303  -6.493  1.00 28.59           O  
ATOM   2452  N   LYS C  48      -1.429  19.344  -6.343  1.00 17.84           N  
ATOM   2453  CA  LYS C  48      -0.710  18.178  -6.833  1.00 17.82           C  
ATOM   2454  C   LYS C  48      -0.535  17.227  -5.666  1.00 17.66           C  
ATOM   2455  O   LYS C  48      -0.057  17.611  -4.607  1.00 17.16           O  
ATOM   2456  CB  LYS C  48       0.653  18.574  -7.392  1.00 17.61           C  
ATOM   2457  CG  LYS C  48       1.472  17.399  -7.962  1.00 21.99           C  
ATOM   2458  CD  LYS C  48       2.813  17.893  -8.496  1.00 26.07           C  
ATOM   2459  CE  LYS C  48       3.678  16.756  -9.012  1.00 29.45           C  
ATOM   2460  NZ  LYS C  48       3.110  16.120 -10.233  1.00 30.80           N  
ATOM   2461  N   LYS C  49      -0.921  15.977  -5.865  1.00 18.12           N  
ATOM   2462  CA  LYS C  49      -0.775  14.939  -4.862  1.00 17.35           C  
ATOM   2463  C   LYS C  49       0.584  14.280  -5.033  1.00 19.24           C  
ATOM   2464  O   LYS C  49       0.901  13.835  -6.145  1.00 20.08           O  
ATOM   2465  CB  LYS C  49      -1.866  13.889  -5.039  1.00 19.00           C  
ATOM   2466  CG  LYS C  49      -1.886  12.809  -3.958  1.00 22.85           C  
ATOM   2467  CD  LYS C  49      -3.026  11.815  -4.209  1.00 22.98           C  
ATOM   2468  CE  LYS C  49      -3.095  10.786  -3.090  1.00 26.61           C  
ATOM   2469  NZ  LYS C  49      -1.849   9.934  -3.092  1.00 34.67           N  
ATOM   2470  N   ILE C  50       1.361  14.195  -3.953  1.00 19.49           N  
ATOM   2471  CA  ILE C  50       2.637  13.489  -3.968  1.00 21.12           C  
ATOM   2472  C   ILE C  50       2.640  12.594  -2.749  1.00 21.86           C  
ATOM   2473  O   ILE C  50       2.931  13.033  -1.642  1.00 20.43           O  
ATOM   2474  CB  ILE C  50       3.862  14.418  -3.952  1.00 23.29           C  
ATOM   2475  CG1 ILE C  50       3.815  15.389  -5.132  1.00 22.44           C  
ATOM   2476  CG2 ILE C  50       5.157  13.587  -4.018  1.00 24.89           C  
ATOM   2477  CD1 ILE C  50       4.897  16.432  -5.116  1.00 23.44           C  
ATOM   2478  N   GLY C  51       2.314  11.321  -2.970  1.00 23.61           N  
ATOM   2479  CA  GLY C  51       2.253  10.365  -1.892  1.00 23.34           C  
ATOM   2480  C   GLY C  51       1.211  10.797  -0.879  1.00 23.17           C  
ATOM   2481  O   GLY C  51       0.055  11.037  -1.240  1.00 25.07           O  
ATOM   2482  N   ASN C  52       1.658  10.976   0.366  1.00 21.97           N  
ATOM   2483  CA  ASN C  52       0.796  11.323   1.490  1.00 25.55           C  
ATOM   2484  C   ASN C  52       0.602  12.818   1.675  1.00 22.79           C  
ATOM   2485  O   ASN C  52       0.013  13.244   2.653  1.00 23.69           O  
ATOM   2486  CB  ASN C  52       1.342  10.702   2.796  1.00 26.38           C  
ATOM   2487  CG  ASN C  52       2.740  11.218   3.194  1.00 32.35           C  
ATOM   2488  OD1 ASN C  52       3.451  11.830   2.397  1.00 42.75           O  
ATOM   2489  ND2 ASN C  52       3.150  10.920   4.424  1.00 35.04           N  
ATOM   2490  N   LYS C  53       1.099  13.597   0.737  1.00 20.27           N  
ATOM   2491  CA  LYS C  53       1.009  15.043   0.803  1.00 19.84           C  
ATOM   2492  C   LYS C  53       0.321  15.595  -0.424  1.00 18.92           C  
ATOM   2493  O   LYS C  53       0.309  14.993  -1.501  1.00 18.47           O  
ATOM   2494  CB  LYS C  53       2.406  15.631   0.910  1.00 21.49           C  
ATOM   2495  CG  LYS C  53       3.107  15.224   2.167  1.00 26.82           C  
ATOM   2496  CD  LYS C  53       4.435  15.909   2.285  1.00 31.14           C  
ATOM   2497  CE  LYS C  53       5.154  15.484   3.559  1.00 33.48           C  
ATOM   2498  NZ  LYS C  53       5.655  14.072   3.409  1.00 34.73           N  
ATOM   2499  N   TYR C  54      -0.283  16.759  -0.220  1.00 16.35           N  
ATOM   2500  CA  TYR C  54      -0.841  17.556  -1.281  1.00 16.57           C  
ATOM   2501  C   TYR C  54      -0.148  18.906  -1.259  1.00 15.99           C  
ATOM   2502  O   TYR C  54      -0.096  19.544  -0.196  1.00 15.49           O  
ATOM   2503  CB  TYR C  54      -2.310  17.780  -1.049  1.00 16.67           C  
ATOM   2504  CG  TYR C  54      -3.152  16.536  -1.116  1.00 18.05           C  
ATOM   2505  CD1 TYR C  54      -3.612  16.061  -2.320  1.00 21.40           C  
ATOM   2506  CD2 TYR C  54      -3.527  15.873   0.039  1.00 18.35           C  
ATOM   2507  CE1 TYR C  54      -4.431  14.928  -2.379  1.00 21.70           C  
ATOM   2508  CE2 TYR C  54      -4.341  14.738  -0.005  1.00 21.84           C  
ATOM   2509  CZ  TYR C  54      -4.781  14.272  -1.215  1.00 19.26           C  
ATOM   2510  OH  TYR C  54      -5.583  13.149  -1.237  1.00 23.27           O  
ATOM   2511  N   ILE C  55       0.338  19.344  -2.425  1.00 14.88           N  
ATOM   2512  CA  ILE C  55       0.916  20.651  -2.590  1.00 15.31           C  
ATOM   2513  C   ILE C  55      -0.261  21.463  -3.115  1.00 15.94           C  
ATOM   2514  O   ILE C  55      -0.760  21.183  -4.230  1.00 16.80           O  
ATOM   2515  CB  ILE C  55       2.093  20.674  -3.562  1.00 15.97           C  
ATOM   2516  CG1 ILE C  55       3.155  19.647  -3.155  1.00 20.17           C  
ATOM   2517  CG2 ILE C  55       2.649  22.090  -3.659  1.00 16.92           C  
ATOM   2518  CD1 ILE C  55       3.543  19.662  -1.708  1.00 23.31           C  
ATOM   2519  N   VAL C  56      -0.703  22.434  -2.321  1.00 16.30           N  
ATOM   2520  CA  VAL C  56      -1.911  23.195  -2.597  1.00 14.46           C  
ATOM   2521  C   VAL C  56      -1.550  24.630  -2.917  1.00 15.10           C  
ATOM   2522  O   VAL C  56      -0.863  25.303  -2.125  1.00 16.34           O  
ATOM   2523  CB  VAL C  56      -2.877  23.142  -1.415  1.00 14.40           C  
ATOM   2524  CG1 VAL C  56      -4.152  23.893  -1.740  1.00 16.66           C  
ATOM   2525  CG2 VAL C  56      -3.182  21.679  -1.036  1.00 16.10           C  
ATOM   2526  N   SER C  57      -1.963  25.080  -4.094  1.00 14.68           N  
ATOM   2527  CA  SER C  57      -1.790  26.432  -4.555  1.00 16.25           C  
ATOM   2528  C   SER C  57      -3.169  27.108  -4.518  1.00 16.18           C  
ATOM   2529  O   SER C  57      -4.015  26.835  -5.354  1.00 16.25           O  
ATOM   2530  CB  SER C  57      -1.200  26.445  -5.950  1.00 16.63           C  
ATOM   2531  OG  SER C  57      -0.950  27.769  -6.363  1.00 18.09           O  
ATOM   2532  N   ILE C  58      -3.384  27.976  -3.533  1.00 14.36           N  
ATOM   2533  CA  ILE C  58      -4.685  28.615  -3.357  1.00 14.52           C  
ATOM   2534  C   ILE C  58      -4.819  29.708  -4.405  1.00 15.00           C  
ATOM   2535  O   ILE C  58      -3.833  30.314  -4.803  1.00 15.41           O  
ATOM   2536  CB  ILE C  58      -4.874  29.137  -1.902  1.00 13.87           C  
ATOM   2537  CG1 ILE C  58      -4.839  27.943  -0.929  1.00 16.96           C  
ATOM   2538  CG2 ILE C  58      -6.153  29.963  -1.786  1.00 15.38           C  
ATOM   2539  CD1 ILE C  58      -5.092  28.246   0.518  1.00 19.30           C  
ATOM   2540  N   ASN C  59      -6.027  29.916  -4.922  1.00 15.24           N  
ATOM   2541  CA  ASN C  59      -6.238  30.917  -5.947  1.00 15.96           C  
ATOM   2542  C   ASN C  59      -6.060  32.303  -5.335  1.00 15.35           C  
ATOM   2543  O   ASN C  59      -6.329  32.533  -4.146  1.00 16.62           O  
ATOM   2544  CB  ASN C  59      -7.655  30.851  -6.514  1.00 17.09           C  
ATOM   2545  CG  ASN C  59      -7.941  29.604  -7.332  1.00 18.45           C  
ATOM   2546  OD1 ASN C  59      -7.067  28.799  -7.622  1.00 21.55           O  
ATOM   2547  ND2 ASN C  59      -9.213  29.449  -7.708  1.00 21.61           N  
ATOM   2548  N   ASN C  60      -5.651  33.256  -6.154  1.00 15.73           N  
ATOM   2549  CA  ASN C  60      -5.517  34.599  -5.657  1.00 15.35           C  
ATOM   2550  C   ASN C  60      -6.880  35.172  -5.247  1.00 13.69           C  
ATOM   2551  O   ASN C  60      -7.938  34.720  -5.728  1.00 15.76           O  
ATOM   2552  CB  ASN C  60      -4.867  35.473  -6.720  1.00 15.66           C  
ATOM   2553  CG  ASN C  60      -4.213  36.713  -6.137  1.00 16.52           C  
ATOM   2554  OD1 ASN C  60      -4.079  36.867  -4.910  1.00 14.93           O  
ATOM   2555  ND2 ASN C  60      -3.790  37.599  -7.015  1.00 18.89           N  
ATOM   2556  N   HIS C  61      -6.851  36.159  -4.346  1.00 14.62           N  
ATOM   2557  CA  HIS C  61      -8.067  36.865  -3.887  1.00 15.86           C  
ATOM   2558  C   HIS C  61      -9.082  35.959  -3.179  1.00 16.88           C  
ATOM   2559  O   HIS C  61     -10.255  36.295  -3.073  1.00 21.15           O  
ATOM   2560  CB  HIS C  61      -8.745  37.618  -5.052  1.00 15.03           C  
ATOM   2561  CG  HIS C  61      -7.790  38.407  -5.892  1.00 19.38           C  
ATOM   2562  ND1 HIS C  61      -6.940  39.347  -5.359  1.00 21.28           N  
ATOM   2563  CD2 HIS C  61      -7.540  38.379  -7.223  1.00 22.26           C  
ATOM   2564  CE1 HIS C  61      -6.229  39.893  -6.330  1.00 24.16           C  
ATOM   2565  NE2 HIS C  61      -6.562  39.310  -7.468  1.00 22.80           N  
ATOM   2566  N   THR C  62      -8.606  34.842  -2.648  1.00 15.15           N  
ATOM   2567  CA  THR C  62      -9.421  33.842  -1.980  1.00 14.39           C  
ATOM   2568  C   THR C  62      -9.098  33.823  -0.494  1.00 15.13           C  
ATOM   2569  O   THR C  62      -7.936  34.034  -0.091  1.00 14.52           O  
ATOM   2570  CB  THR C  62      -9.131  32.469  -2.604  1.00 14.51           C  
ATOM   2571  OG1 THR C  62      -9.369  32.574  -4.023  1.00 16.59           O  
ATOM   2572  CG2 THR C  62      -9.983  31.379  -2.012  1.00 16.47           C  
ATOM   2573  N   GLU C  63     -10.131  33.574   0.306  1.00 14.06           N  
ATOM   2574  CA  GLU C  63      -9.959  33.481   1.745  1.00 14.42           C  
ATOM   2575  C   GLU C  63      -9.364  32.079   2.039  1.00 14.66           C  
ATOM   2576  O   GLU C  63      -9.982  31.029   1.762  1.00 13.81           O  
ATOM   2577  CB  GLU C  63     -11.264  33.760   2.477  1.00 14.28           C  
ATOM   2578  CG  GLU C  63     -11.103  34.192   3.926  1.00 16.22           C  
ATOM   2579  CD  GLU C  63     -10.747  33.007   4.805  1.00 14.82           C  
ATOM   2580  OE1 GLU C  63     -11.644  32.138   4.964  1.00 16.87           O  
ATOM   2581  OE2 GLU C  63      -9.591  32.921   5.261  1.00 14.67           O  
ATOM   2582  N  AILE C  64      -8.162  32.091   2.581  0.70 14.07           N  
ATOM   2583  N  BILE C  64      -8.153  32.073   2.583  0.30 12.85           N  
ATOM   2584  CA AILE C  64      -7.338  30.907   2.732  0.70 15.50           C  
ATOM   2585  CA BILE C  64      -7.354  30.849   2.671  0.30 12.28           C  
ATOM   2586  C  AILE C  64      -7.903  29.877   3.673  0.70 14.62           C  
ATOM   2587  C  BILE C  64      -7.850  29.853   3.708  0.30 13.34           C  
ATOM   2588  O  AILE C  64      -7.809  28.675   3.398  0.70 15.58           O  
ATOM   2589  O  BILE C  64      -7.626  28.653   3.552  0.30 13.48           O  
ATOM   2590  CB AILE C  64      -5.899  31.326   3.158  0.70 15.76           C  
ATOM   2591  CB BILE C  64      -5.828  31.161   2.880  0.30 10.90           C  
ATOM   2592  CG1AILE C  64      -5.176  31.955   1.965  0.70 17.36           C  
ATOM   2593  CG1BILE C  64      -5.527  31.622   4.315  0.30  6.86           C  
ATOM   2594  CG2AILE C  64      -5.107  30.144   3.701  0.70 17.56           C  
ATOM   2595  CG2BILE C  64      -5.352  32.190   1.843  0.30 10.54           C  
ATOM   2596  CD1AILE C  64      -3.981  32.766   2.367  0.70 19.48           C  
ATOM   2597  CD1BILE C  64      -4.059  31.953   4.542  0.30 13.05           C  
ATOM   2598  N   VAL C  65      -8.491  30.327   4.773  1.00 14.81           N  
ATOM   2599  CA  VAL C  65      -9.027  29.399   5.777  1.00 13.85           C  
ATOM   2600  C   VAL C  65     -10.232  28.636   5.187  1.00 13.63           C  
ATOM   2601  O   VAL C  65     -10.297  27.400   5.304  1.00 15.34           O  
ATOM   2602  CB  VAL C  65      -9.337  30.094   7.103  1.00 13.51           C  
ATOM   2603  CG1 VAL C  65      -9.986  29.085   8.070  1.00 15.33           C  
ATOM   2604  CG2 VAL C  65      -8.068  30.689   7.702  1.00 14.18           C  
ATOM   2605  N  ALYS C  66     -11.141  29.364   4.549  0.50 14.42           N  
ATOM   2606  N  BLYS C  66     -11.159  29.330   4.532  0.50 14.14           N  
ATOM   2607  CA ALYS C  66     -12.253  28.785   3.811  0.50 15.98           C  
ATOM   2608  CA BLYS C  66     -12.272  28.641   3.884  0.50 15.05           C  
ATOM   2609  C  ALYS C  66     -11.742  27.761   2.808  0.50 16.18           C  
ATOM   2610  C  BLYS C  66     -11.745  27.716   2.789  0.50 15.67           C  
ATOM   2611  O  ALYS C  66     -12.249  26.645   2.748  0.50 15.25           O  
ATOM   2612  O  BLYS C  66     -12.263  26.617   2.632  0.50 14.87           O  
ATOM   2613  CB ALYS C  66     -13.018  29.902   3.096  0.50 17.45           C  
ATOM   2614  CB BLYS C  66     -13.299  29.616   3.310  0.50 14.05           C  
ATOM   2615  CG ALYS C  66     -14.098  29.472   2.133  0.50 19.19           C  
ATOM   2616  CG BLYS C  66     -14.538  28.943   2.712  0.50 16.44           C  
ATOM   2617  CD ALYS C  66     -14.773  30.689   1.512  0.50 19.25           C  
ATOM   2618  CD BLYS C  66     -15.442  29.944   2.004  0.50 18.40           C  
ATOM   2619  CE ALYS C  66     -15.999  30.295   0.696  0.50 22.43           C  
ATOM   2620  CE BLYS C  66     -16.466  29.251   1.096  0.50 24.15           C  
ATOM   2621  NZ ALYS C  66     -17.108  29.720   1.546  0.50 27.33           N  
ATOM   2622  NZ BLYS C  66     -17.230  30.266   0.305  0.50 26.86           N  
ATOM   2623  N   ALA C  67     -10.732  28.145   2.033  1.00 14.86           N  
ATOM   2624  CA  ALA C  67     -10.159  27.281   0.989  1.00 14.59           C  
ATOM   2625  C   ALA C  67      -9.509  26.020   1.548  1.00 13.31           C  
ATOM   2626  O   ALA C  67      -9.743  24.943   1.012  1.00 14.34           O  
ATOM   2627  CB  ALA C  67      -9.167  28.063   0.121  1.00 16.66           C  
ATOM   2628  N   LEU C  68      -8.780  26.154   2.652  1.00 14.13           N  
ATOM   2629  CA  LEU C  68      -8.123  24.988   3.256  1.00 14.76           C  
ATOM   2630  C   LEU C  68      -9.162  24.047   3.840  1.00 15.89           C  
ATOM   2631  O   LEU C  68      -9.020  22.835   3.737  1.00 14.50           O  
ATOM   2632  CB  LEU C  68      -7.107  25.404   4.313  1.00 13.90           C  
ATOM   2633  CG  LEU C  68      -5.833  26.041   3.762  1.00 13.99           C  
ATOM   2634  CD1 LEU C  68      -5.015  26.786   4.858  1.00 13.60           C  
ATOM   2635  CD2 LEU C  68      -4.941  25.008   3.018  1.00 16.04           C  
ATOM   2636  N   ASN C  69     -10.199  24.597   4.456  1.00 14.77           N  
ATOM   2637  CA  ASN C  69     -11.295  23.777   4.947  1.00 14.90           C  
ATOM   2638  C   ASN C  69     -11.959  23.043   3.793  1.00 15.30           C  
ATOM   2639  O   ASN C  69     -12.207  21.833   3.883  1.00 16.23           O  
ATOM   2640  CB  ASN C  69     -12.340  24.588   5.685  1.00 13.26           C  
ATOM   2641  CG  ASN C  69     -12.020  24.761   7.137  1.00 19.86           C  
ATOM   2642  OD1 ASN C  69     -12.386  23.914   7.973  1.00 22.03           O  
ATOM   2643  ND2 ASN C  69     -11.361  25.883   7.477  1.00 20.94           N  
ATOM   2644  N   ALA C  70     -12.225  23.767   2.713  1.00 15.24           N  
ATOM   2645  CA  ALA C  70     -12.838  23.178   1.513  1.00 14.68           C  
ATOM   2646  C   ALA C  70     -11.970  22.062   0.976  1.00 15.66           C  
ATOM   2647  O   ALA C  70     -12.480  20.982   0.618  1.00 14.59           O  
ATOM   2648  CB  ALA C  70     -13.075  24.272   0.438  1.00 15.72           C  
ATOM   2649  N   PHE C  71     -10.668  22.287   0.916  1.00 15.68           N  
ATOM   2650  CA  PHE C  71      -9.759  21.284   0.402  1.00 14.53           C  
ATOM   2651  C   PHE C  71      -9.815  20.007   1.225  1.00 14.49           C  
ATOM   2652  O   PHE C  71      -9.929  18.919   0.670  1.00 13.87           O  
ATOM   2653  CB  PHE C  71      -8.322  21.814   0.382  1.00 15.06           C  
ATOM   2654  CG  PHE C  71      -7.355  20.845  -0.159  1.00 14.79           C  
ATOM   2655  CD1 PHE C  71      -7.200  20.721  -1.519  1.00 16.21           C  
ATOM   2656  CD2 PHE C  71      -6.645  19.988   0.667  1.00 17.08           C  
ATOM   2657  CE1 PHE C  71      -6.350  19.761  -2.058  1.00 18.87           C  
ATOM   2658  CE2 PHE C  71      -5.800  19.031   0.112  1.00 16.55           C  
ATOM   2659  CZ  PHE C  71      -5.663  18.940  -1.252  1.00 17.25           C  
ATOM   2660  N   CYS C  72      -9.755  20.145   2.540  1.00 15.76           N  
ATOM   2661  CA  CYS C  72      -9.823  18.995   3.414  1.00 15.32           C  
ATOM   2662  C   CYS C  72     -11.160  18.261   3.314  1.00 15.20           C  
ATOM   2663  O   CYS C  72     -11.201  17.014   3.355  1.00 14.97           O  
ATOM   2664  CB  CYS C  72      -9.557  19.381   4.860  1.00 14.36           C  
ATOM   2665  SG  CYS C  72      -7.858  19.944   5.124  1.00 17.49           S  
ATOM   2666  N   LYS C  73     -12.253  19.008   3.154  1.00 14.66           N  
ATOM   2667  CA  LYS C  73     -13.560  18.387   2.957  1.00 16.80           C  
ATOM   2668  C   LYS C  73     -13.630  17.656   1.602  1.00 15.33           C  
ATOM   2669  O   LYS C  73     -14.156  16.537   1.512  1.00 17.45           O  
ATOM   2670  CB  LYS C  73     -14.695  19.412   3.056  1.00 15.52           C  
ATOM   2671  CG  LYS C  73     -14.935  19.900   4.447  1.00 16.54           C  
ATOM   2672  CD  LYS C  73     -16.168  20.826   4.554  1.00 21.70           C  
ATOM   2673  CE  LYS C  73     -16.025  22.172   3.911  1.00 32.44           C  
ATOM   2674  NZ  LYS C  73     -17.392  22.818   3.900  1.00 37.88           N  
ATOM   2675  N  AGLU C  74     -13.106  18.277   0.550  0.50 14.88           N  
ATOM   2676  N  BGLU C  74     -13.113  18.301   0.546  0.50 15.94           N  
ATOM   2677  CA AGLU C  74     -13.182  17.674  -0.776  0.50 14.52           C  
ATOM   2678  CA BGLU C  74     -13.093  17.714  -0.808  0.50 16.27           C  
ATOM   2679  C  AGLU C  74     -12.256  16.452  -0.959  0.50 13.49           C  
ATOM   2680  C  BGLU C  74     -12.287  16.422  -0.892  0.50 14.34           C  
ATOM   2681  O  AGLU C  74     -12.567  15.583  -1.784  0.50 13.28           O  
ATOM   2682  O  BGLU C  74     -12.697  15.487  -1.584  0.50 14.32           O  
ATOM   2683  CB AGLU C  74     -12.961  18.736  -1.860  0.50 15.84           C  
ATOM   2684  CB BGLU C  74     -12.577  18.714  -1.872  0.50 18.14           C  
ATOM   2685  CG AGLU C  74     -14.036  19.845  -1.883  0.50 18.37           C  
ATOM   2686  CG BGLU C  74     -12.177  18.060  -3.236  0.50 16.68           C  
ATOM   2687  CD AGLU C  74     -15.412  19.402  -2.358  0.50 19.02           C  
ATOM   2688  CD BGLU C  74     -12.202  18.996  -4.426  0.50 21.49           C  
ATOM   2689  OE1AGLU C  74     -16.403  20.016  -1.918  0.50 28.31           O  
ATOM   2690  OE1BGLU C  74     -13.281  19.146  -5.046  0.50 32.63           O  
ATOM   2691  OE2AGLU C  74     -15.525  18.448  -3.147  0.50 15.89           O  
ATOM   2692  OE2BGLU C  74     -11.141  19.537  -4.783  0.50 20.84           O  
ATOM   2693  N   LYS C  75     -11.145  16.393  -0.217  1.00 15.39           N  
ATOM   2694  CA  LYS C  75     -10.256  15.231  -0.225  1.00 15.56           C  
ATOM   2695  C   LYS C  75     -10.550  14.261   0.911  1.00 17.72           C  
ATOM   2696  O   LYS C  75      -9.895  13.230   0.992  1.00 20.76           O  
ATOM   2697  CB  LYS C  75      -8.781  15.642  -0.181  1.00 16.93           C  
ATOM   2698  CG  LYS C  75      -8.344  16.559  -1.313  1.00 20.86           C  
ATOM   2699  CD  LYS C  75      -8.673  16.081  -2.746  1.00 26.16           C  
ATOM   2700  CE  LYS C  75      -7.845  14.902  -3.119  1.00 33.17           C  
ATOM   2701  N   GLY C  76     -11.515  14.573   1.773  1.00 16.23           N  
ATOM   2702  CA  GLY C  76     -11.872  13.684   2.873  1.00 17.24           C  
ATOM   2703  C   GLY C  76     -10.733  13.413   3.826  1.00 18.31           C  
ATOM   2704  O   GLY C  76     -10.520  12.268   4.244  1.00 19.80           O  
ATOM   2705  N   ILE C  77      -9.973  14.446   4.172  1.00 16.72           N  
ATOM   2706  CA  ILE C  77      -8.794  14.261   4.997  1.00 15.73           C  
ATOM   2707  C   ILE C  77      -9.251  14.183   6.437  1.00 18.07           C  
ATOM   2708  O   ILE C  77      -9.919  15.076   6.931  1.00 18.04           O  
ATOM   2709  CB  ILE C  77      -7.761  15.376   4.820  1.00 15.44           C  
ATOM   2710  CG1 ILE C  77      -7.237  15.383   3.373  1.00 17.92           C  
ATOM   2711  CG2 ILE C  77      -6.594  15.211   5.850  1.00 16.19           C  
ATOM   2712  CD1 ILE C  77      -6.275  16.474   3.068  1.00 18.35           C  
ATOM   2713  N   LEU C  78      -8.880  13.081   7.085  1.00 15.56           N  
ATOM   2714  CA  LEU C  78      -9.255  12.813   8.467  1.00 16.29           C  
ATOM   2715  C   LEU C  78      -8.446  13.641   9.481  1.00 17.03           C  
ATOM   2716  O   LEU C  78      -8.962  14.192  10.459  1.00 17.11           O  
ATOM   2717  CB  LEU C  78      -9.055  11.306   8.722  1.00 16.37           C  
ATOM   2718  CG  LEU C  78      -9.967  10.347   7.940  1.00 18.86           C  
ATOM   2719  CD1 LEU C  78      -9.456   8.904   7.974  1.00 18.58           C  
ATOM   2720  CD2 LEU C  78     -11.358  10.480   8.499  1.00 19.97           C  
ATOM   2721  N   SER C  79      -7.145  13.662   9.262  1.00 16.16           N  
ATOM   2722  CA  SER C  79      -6.202  14.339  10.128  1.00 16.21           C  
ATOM   2723  C   SER C  79      -4.943  14.554   9.346  1.00 16.37           C  
ATOM   2724  O   SER C  79      -4.724  13.933   8.323  1.00 15.26           O  
ATOM   2725  CB  SER C  79      -5.898  13.552  11.414  1.00 17.44           C  
ATOM   2726  OG  SER C  79      -5.152  12.371  11.138  1.00 18.84           O  
ATOM   2727  N   GLY C  80      -4.118  15.467   9.837  1.00 14.94           N  
ATOM   2728  CA  GLY C  80      -2.915  15.840   9.129  1.00 15.03           C  
ATOM   2729  C   GLY C  80      -2.397  17.170   9.597  1.00 13.83           C  
ATOM   2730  O   GLY C  80      -2.803  17.678  10.648  1.00 15.11           O  
ATOM   2731  N   SER C  81      -1.484  17.686   8.813  1.00 14.40           N  
ATOM   2732  CA  SER C  81      -0.845  18.978   9.092  1.00 15.01           C  
ATOM   2733  C   SER C  81      -0.961  19.880   7.876  1.00 15.94           C  
ATOM   2734  O   SER C  81      -1.104  19.422   6.740  1.00 15.40           O  
ATOM   2735  CB  SER C  81       0.623  18.779   9.397  1.00 17.85           C  
ATOM   2736  OG  SER C  81       1.322  18.305   8.273  1.00 21.85           O  
ATOM   2737  N   ILE C  82      -0.855  21.180   8.140  1.00 14.90           N  
ATOM   2738  CA  ILE C  82      -0.866  22.193   7.099  1.00 16.18           C  
ATOM   2739  C   ILE C  82       0.258  23.155   7.406  1.00 14.93           C  
ATOM   2740  O   ILE C  82       0.408  23.611   8.539  1.00 15.48           O  
ATOM   2741  CB  ILE C  82      -2.195  22.975   7.036  1.00 16.92           C  
ATOM   2742  CG1 ILE C  82      -3.369  22.043   6.800  1.00 17.15           C  
ATOM   2743  CG2 ILE C  82      -2.168  23.984   5.886  1.00 17.38           C  
ATOM   2744  CD1 ILE C  82      -4.776  22.692   6.826  1.00 17.05           C  
ATOM   2745  N  AASN C  83       1.057  23.444   6.394  0.60 14.96           N  
ATOM   2746  N  BASN C  83       1.070  23.449   6.404  0.40 16.28           N  
ATOM   2747  CA AASN C  83       2.162  24.384   6.529  0.60 15.25           C  
ATOM   2748  CA BASN C  83       2.077  24.486   6.576  0.40 17.44           C  
ATOM   2749  C  AASN C  83       2.230  25.202   5.262  0.60 13.99           C  
ATOM   2750  C  BASN C  83       2.460  25.142   5.260  0.40 15.03           C  
ATOM   2751  O  AASN C  83       1.817  24.742   4.237  0.60 15.82           O  
ATOM   2752  O  BASN C  83       2.633  24.487   4.211  0.40 11.53           O  
ATOM   2753  CB AASN C  83       3.449  23.624   6.781  0.60 15.44           C  
ATOM   2754  CB BASN C  83       3.303  23.968   7.332  0.40 19.54           C  
ATOM   2755  CG AASN C  83       3.483  23.001   8.179  0.60 14.54           C  
ATOM   2756  CG BASN C  83       3.994  22.857   6.614  0.40 28.11           C  
ATOM   2757  OD1AASN C  83       3.725  23.696   9.158  0.60 16.86           O  
ATOM   2758  OD1BASN C  83       3.961  21.706   7.053  0.40 38.17           O  
ATOM   2759  ND2AASN C  83       3.224  21.707   8.278  0.60 17.37           N  
ATOM   2760  ND2BASN C  83       4.636  23.185   5.501  0.40 32.72           N  
ATOM   2761  N   GLY C  84       2.657  26.445   5.335  1.00 14.61           N  
ATOM   2762  CA  GLY C  84       2.910  27.182   4.114  1.00 16.46           C  
ATOM   2763  C   GLY C  84       3.180  28.652   4.247  1.00 14.77           C  
ATOM   2764  O   GLY C  84       3.303  29.163   5.352  1.00 15.68           O  
ATOM   2765  N   ILE C  85       3.260  29.281   3.080  1.00 15.57           N  
ATOM   2766  CA  ILE C  85       3.666  30.647   2.923  1.00 14.15           C  
ATOM   2767  C   ILE C  85       2.864  31.270   1.820  1.00 14.92           C  
ATOM   2768  O   ILE C  85       2.238  30.579   1.007  1.00 15.41           O  
ATOM   2769  CB  ILE C  85       5.205  30.746   2.618  1.00 15.04           C  
ATOM   2770  CG1 ILE C  85       5.615  30.024   1.325  1.00 15.55           C  
ATOM   2771  CG2 ILE C  85       6.030  30.243   3.810  1.00 16.40           C  
ATOM   2772  CD1 ILE C  85       7.105  30.224   0.900  1.00 16.19           C  
ATOM   2773  N   GLY C  86       2.910  32.572   1.751  1.00 14.86           N  
ATOM   2774  CA  GLY C  86       2.191  33.319   0.738  1.00 14.91           C  
ATOM   2775  C   GLY C  86       2.047  34.761   1.108  1.00 14.61           C  
ATOM   2776  O   GLY C  86       2.754  35.238   1.992  1.00 16.45           O  
ATOM   2777  N   ALA C  87       1.207  35.492   0.379  1.00 12.95           N  
ATOM   2778  CA  ALA C  87       0.981  36.919   0.637  1.00 14.05           C  
ATOM   2779  C   ALA C  87      -0.491  37.187   0.683  1.00 13.82           C  
ATOM   2780  O   ALA C  87      -1.265  36.563  -0.028  1.00 15.10           O  
ATOM   2781  CB  ALA C  87       1.633  37.805  -0.435  1.00 17.24           C  
ATOM   2782  N   ILE C  88      -0.856  38.135   1.537  1.00 13.55           N  
ATOM   2783  CA  ILE C  88      -2.249  38.439   1.856  1.00 12.56           C  
ATOM   2784  C   ILE C  88      -2.489  39.937   1.914  1.00 12.94           C  
ATOM   2785  O   ILE C  88      -1.570  40.722   2.130  1.00 13.10           O  
ATOM   2786  CB  ILE C  88      -2.677  37.739   3.183  1.00 12.73           C  
ATOM   2787  CG1 ILE C  88      -1.808  38.247   4.332  1.00 14.06           C  
ATOM   2788  CG2 ILE C  88      -2.629  36.211   3.029  1.00 13.51           C  
ATOM   2789  CD1 ILE C  88      -2.232  37.706   5.711  1.00 14.82           C  
ATOM   2790  N   GLY C  89      -3.746  40.327   1.702  1.00 12.61           N  
ATOM   2791  CA  GLY C  89      -4.198  41.700   1.828  1.00 13.57           C  
ATOM   2792  C   GLY C  89      -5.166  41.967   2.974  1.00 13.54           C  
ATOM   2793  O   GLY C  89      -5.583  43.105   3.177  1.00 14.10           O  
ATOM   2794  N  AGLU C  90      -5.518  40.936   3.740  0.70 13.49           N  
ATOM   2795  N  BGLU C  90      -5.504  40.924   3.727  0.30 13.00           N  
ATOM   2796  CA AGLU C  90      -6.389  41.041   4.884  0.70 13.91           C  
ATOM   2797  CA BGLU C  90      -6.350  41.039   4.888  0.30 12.26           C  
ATOM   2798  C  AGLU C  90      -6.087  39.843   5.791  0.70 13.13           C  
ATOM   2799  C  BGLU C  90      -6.056  39.843   5.794  0.30 12.56           C  
ATOM   2800  O  AGLU C  90      -5.793  38.774   5.280  0.70 13.55           O  
ATOM   2801  O  BGLU C  90      -5.713  38.774   5.299  0.30 12.69           O  
ATOM   2802  CB AGLU C  90      -7.871  41.034   4.494  0.70 14.75           C  
ATOM   2803  CB BGLU C  90      -7.828  41.099   4.493  0.30 12.75           C  
ATOM   2804  CG AGLU C  90      -8.810  41.327   5.667  0.70 17.72           C  
ATOM   2805  CG BGLU C  90      -8.734  41.617   5.610  0.30 12.15           C  
ATOM   2806  CD AGLU C  90     -10.279  41.142   5.332  0.70 19.90           C  
ATOM   2807  CD BGLU C  90     -10.035  42.223   5.121  0.30 12.25           C  
ATOM   2808  OE1AGLU C  90     -10.830  42.001   4.612  0.70 24.91           O  
ATOM   2809  OE1BGLU C  90     -11.076  41.967   5.761  0.30 14.07           O  
ATOM   2810  OE2AGLU C  90     -10.885  40.141   5.768  0.70 26.07           O  
ATOM   2811  OE2BGLU C  90     -10.033  42.954   4.113  0.30 12.50           O  
ATOM   2812  N   LEU C  91      -6.135  40.052   7.106  1.00 13.32           N  
ATOM   2813  CA  LEU C  91      -5.854  39.018   8.093  1.00 12.04           C  
ATOM   2814  C   LEU C  91      -6.725  39.240   9.297  1.00 14.60           C  
ATOM   2815  O   LEU C  91      -6.811  40.367   9.768  1.00 14.43           O  
ATOM   2816  CB  LEU C  91      -4.415  39.138   8.600  1.00 12.63           C  
ATOM   2817  CG  LEU C  91      -3.934  38.199   9.697  1.00 12.93           C  
ATOM   2818  CD1 LEU C  91      -3.928  36.781   9.204  1.00 14.65           C  
ATOM   2819  CD2 LEU C  91      -2.542  38.653  10.203  1.00 14.07           C  
ATOM   2820  N   THR C  92      -7.285  38.159   9.823  1.00 13.45           N  
ATOM   2821  CA  THR C  92      -8.010  38.227  11.078  1.00 13.18           C  
ATOM   2822  C   THR C  92      -7.428  37.220  12.055  1.00 13.74           C  
ATOM   2823  O   THR C  92      -7.367  36.050  11.749  1.00 13.44           O  
ATOM   2824  CB  THR C  92      -9.501  37.981  10.916  1.00 13.14           C  
ATOM   2825  OG1 THR C  92     -10.041  38.932   9.983  1.00 14.87           O  
ATOM   2826  CG2 THR C  92     -10.226  38.160  12.242  1.00 14.34           C  
ATOM   2827  N   LEU C  93      -6.979  37.705  13.217  1.00 13.15           N  
ATOM   2828  CA  LEU C  93      -6.436  36.889  14.257  1.00 12.39           C  
ATOM   2829  C   LEU C  93      -7.339  36.940  15.476  1.00 13.12           C  
ATOM   2830  O   LEU C  93      -7.957  37.959  15.704  1.00 14.84           O  
ATOM   2831  CB  LEU C  93      -5.053  37.425  14.679  1.00 12.90           C  
ATOM   2832  CG  LEU C  93      -3.961  37.448  13.606  1.00 14.57           C  
ATOM   2833  CD1 LEU C  93      -2.698  38.073  14.161  1.00 15.05           C  
ATOM   2834  CD2 LEU C  93      -3.688  36.042  13.084  1.00 14.36           C  
ATOM   2835  N   ARG C  94      -7.368  35.862  16.248  1.00 13.25           N  
ATOM   2836  CA  ARG C  94      -8.129  35.827  17.477  1.00 13.05           C  
ATOM   2837  C   ARG C  94      -7.212  35.711  18.668  1.00 14.02           C  
ATOM   2838  O   ARG C  94      -6.321  34.879  18.662  1.00 14.97           O  
ATOM   2839  CB  ARG C  94      -9.107  34.659  17.476  1.00 14.13           C  
ATOM   2840  CG  ARG C  94      -9.863  34.480  18.805  1.00 14.27           C  
ATOM   2841  CD  ARG C  94     -10.969  33.488  18.694  1.00 14.88           C  
ATOM   2842  NE  ARG C  94     -12.052  34.060  17.936  1.00 14.59           N  
ATOM   2843  CZ  ARG C  94     -13.115  33.421  17.485  1.00 16.72           C  
ATOM   2844  NH1 ARG C  94     -13.263  32.138  17.685  1.00 19.97           N  
ATOM   2845  NH2 ARG C  94     -14.002  34.099  16.803  1.00 16.35           N  
ATOM   2846  N   PHE C  95      -7.461  36.523  19.695  1.00 13.62           N  
ATOM   2847  CA  PHE C  95      -6.722  36.445  20.943  1.00 14.58           C  
ATOM   2848  C   PHE C  95      -7.727  36.114  22.043  1.00 15.42           C  
ATOM   2849  O   PHE C  95      -8.599  36.907  22.382  1.00 16.66           O  
ATOM   2850  CB  PHE C  95      -5.944  37.726  21.274  1.00 16.51           C  
ATOM   2851  CG  PHE C  95      -4.991  37.519  22.394  1.00 14.40           C  
ATOM   2852  CD1 PHE C  95      -3.750  36.967  22.136  1.00 16.62           C  
ATOM   2853  CD2 PHE C  95      -5.362  37.776  23.697  1.00 18.90           C  
ATOM   2854  CE1 PHE C  95      -2.875  36.716  23.192  1.00 16.96           C  
ATOM   2855  CE2 PHE C  95      -4.488  37.527  24.751  1.00 18.75           C  
ATOM   2856  CZ  PHE C  95      -3.270  36.986  24.482  1.00 17.41           C  
ATOM   2857  N   PHE C  96      -7.531  34.949  22.638  1.00 15.85           N  
ATOM   2858  CA  PHE C  96      -8.444  34.393  23.659  1.00 15.04           C  
ATOM   2859  C   PHE C  96      -7.859  34.577  25.038  1.00 15.26           C  
ATOM   2860  O   PHE C  96      -6.714  34.247  25.278  1.00 17.56           O  
ATOM   2861  CB  PHE C  96      -8.685  32.909  23.377  1.00 16.01           C  
ATOM   2862  CG  PHE C  96      -9.480  32.185  24.433  1.00 17.41           C  
ATOM   2863  CD1 PHE C  96     -10.807  32.435  24.598  1.00 19.09           C  
ATOM   2864  CD2 PHE C  96      -8.908  31.205  25.214  1.00 17.24           C  
ATOM   2865  CE1 PHE C  96     -11.557  31.741  25.521  1.00 23.21           C  
ATOM   2866  CE2 PHE C  96      -9.657  30.510  26.128  1.00 16.54           C  
ATOM   2867  CZ  PHE C  96     -10.973  30.778  26.287  1.00 19.73           C  
ATOM   2868  N   ASN C  97      -8.675  35.104  25.946  1.00 14.85           N  
ATOM   2869  CA  ASN C  97      -8.289  35.319  27.335  1.00 16.95           C  
ATOM   2870  C   ASN C  97      -8.876  34.195  28.176  1.00 17.48           C  
ATOM   2871  O   ASN C  97     -10.079  34.181  28.442  1.00 18.02           O  
ATOM   2872  CB  ASN C  97      -8.826  36.652  27.817  1.00 18.95           C  
ATOM   2873  CG  ASN C  97      -8.380  36.992  29.230  1.00 24.49           C  
ATOM   2874  OD1 ASN C  97      -8.116  36.102  30.053  1.00 28.71           O  
ATOM   2875  ND2 ASN C  97      -8.328  38.298  29.539  1.00 23.75           N  
ATOM   2876  N   PRO C  98      -8.050  33.226  28.596  1.00 17.48           N  
ATOM   2877  CA  PRO C  98      -8.597  32.114  29.373  1.00 19.24           C  
ATOM   2878  C   PRO C  98      -9.187  32.490  30.724  1.00 20.35           C  
ATOM   2879  O   PRO C  98     -10.019  31.739  31.230  1.00 24.12           O  
ATOM   2880  CB  PRO C  98      -7.396  31.182  29.597  1.00 20.03           C  
ATOM   2881  CG  PRO C  98      -6.245  31.834  29.065  1.00 22.29           C  
ATOM   2882  CD  PRO C  98      -6.601  33.101  28.376  1.00 19.56           C  
ATOM   2883  N   LYS C  99      -8.783  33.612  31.300  1.00 19.09           N  
ATOM   2884  CA  LYS C  99      -9.297  33.999  32.618  1.00 22.86           C  
ATOM   2885  C   LYS C  99     -10.755  34.415  32.521  1.00 23.69           C  
ATOM   2886  O   LYS C  99     -11.598  33.939  33.278  1.00 26.68           O  
ATOM   2887  CB  LYS C  99      -8.466  35.128  33.231  1.00 23.97           C  
ATOM   2888  N   THR C 100     -11.052  35.304  31.591  1.00 20.94           N  
ATOM   2889  CA  THR C 100     -12.399  35.859  31.482  1.00 18.25           C  
ATOM   2890  C   THR C 100     -13.255  35.200  30.397  1.00 17.42           C  
ATOM   2891  O   THR C 100     -14.470  35.444  30.334  1.00 18.45           O  
ATOM   2892  CB  THR C 100     -12.309  37.336  31.153  1.00 18.09           C  
ATOM   2893  OG1 THR C 100     -11.706  37.477  29.868  1.00 16.38           O  
ATOM   2894  CG2 THR C 100     -11.484  38.089  32.198  1.00 18.01           C  
ATOM   2895  N   LYS C 101     -12.615  34.429  29.512  1.00 16.37           N  
ATOM   2896  CA  LYS C 101     -13.238  33.832  28.340  1.00 17.34           C  
ATOM   2897  C   LYS C 101     -13.606  34.853  27.280  1.00 15.45           C  
ATOM   2898  O   LYS C 101     -14.263  34.507  26.321  1.00 16.88           O  
ATOM   2899  CB  LYS C 101     -14.471  32.969  28.675  1.00 20.55           C  
ATOM   2900  CG  LYS C 101     -14.274  31.989  29.830  1.00 24.42           C  
ATOM   2901  CD  LYS C 101     -13.177  30.983  29.569  1.00 26.45           C  
ATOM   2902  CE  LYS C 101     -13.023  30.047  30.780  1.00 30.54           C  
ATOM   2903  NZ  LYS C 101     -12.603  30.789  32.040  1.00 36.43           N  
ATOM   2904  N   ALA C 102     -13.142  36.096  27.413  1.00 15.17           N  
ATOM   2905  CA  ALA C 102     -13.260  37.076  26.355  1.00 13.47           C  
ATOM   2906  C   ALA C 102     -12.348  36.707  25.214  1.00 15.29           C  
ATOM   2907  O   ALA C 102     -11.288  36.099  25.410  1.00 17.97           O  
ATOM   2908  CB  ALA C 102     -12.828  38.446  26.883  1.00 12.72           C  
ATOM   2909  N   TYR C 103     -12.736  37.092  24.010  1.00 13.79           N  
ATOM   2910  CA  TYR C 103     -11.913  36.848  22.846  1.00 14.39           C  
ATOM   2911  C   TYR C 103     -11.975  38.062  21.954  1.00 14.81           C  
ATOM   2912  O   TYR C 103     -12.998  38.727  21.848  1.00 15.63           O  
ATOM   2913  CB  TYR C 103     -12.310  35.561  22.130  1.00 15.75           C  
ATOM   2914  CG  TYR C 103     -13.705  35.502  21.584  1.00 15.21           C  
ATOM   2915  CD1 TYR C 103     -14.762  35.065  22.353  1.00 15.26           C  
ATOM   2916  CD2 TYR C 103     -13.973  35.889  20.272  1.00 16.63           C  
ATOM   2917  CE1 TYR C 103     -16.034  35.012  21.827  1.00 16.82           C  
ATOM   2918  CE2 TYR C 103     -15.241  35.811  19.731  1.00 17.48           C  
ATOM   2919  CZ  TYR C 103     -16.268  35.375  20.522  1.00 17.06           C  
ATOM   2920  OH  TYR C 103     -17.548  35.301  20.026  1.00 20.07           O  
ATOM   2921  N   ASP C 104     -10.842  38.363  21.337  1.00 13.35           N  
ATOM   2922  CA  ASP C 104     -10.664  39.593  20.551  1.00 15.86           C  
ATOM   2923  C   ASP C 104     -10.294  39.164  19.147  1.00 15.97           C  
ATOM   2924  O   ASP C 104      -9.308  38.455  18.973  1.00 16.18           O  
ATOM   2925  CB  ASP C 104      -9.518  40.413  21.195  1.00 16.73           C  
ATOM   2926  CG  ASP C 104      -9.432  41.819  20.733  1.00 24.89           C  
ATOM   2927  OD1 ASP C 104     -10.321  42.285  20.017  1.00 16.81           O  
ATOM   2928  OD2 ASP C 104      -8.502  42.547  21.192  1.00 25.52           O  
ATOM   2929  N   ASP C 105     -11.045  39.605  18.142  1.00 13.68           N  
ATOM   2930  CA  ASP C 105     -10.777  39.255  16.745  1.00 14.93           C  
ATOM   2931  C   ASP C 105     -10.317  40.527  16.061  1.00 14.41           C  
ATOM   2932  O   ASP C 105     -11.115  41.455  15.869  1.00 14.48           O  
ATOM   2933  CB  ASP C 105     -12.018  38.710  16.051  1.00 15.84           C  
ATOM   2934  CG  ASP C 105     -12.470  37.371  16.592  1.00 16.45           C  
ATOM   2935  OD1 ASP C 105     -11.739  36.764  17.389  1.00 14.87           O  
ATOM   2936  OD2 ASP C 105     -13.561  36.911  16.174  1.00 16.98           O  
ATOM   2937  N   LYS C 106      -9.042  40.584  15.672  1.00 13.26           N  
ATOM   2938  CA  LYS C 106      -8.514  41.780  15.037  1.00 14.84           C  
ATOM   2939  C   LYS C 106      -8.260  41.518  13.561  1.00 13.24           C  
ATOM   2940  O   LYS C 106      -7.588  40.560  13.199  1.00 13.80           O  
ATOM   2941  CB  LYS C 106      -7.228  42.247  15.716  1.00 15.31           C  
ATOM   2942  CG  LYS C 106      -6.750  43.593  15.169  1.00 14.74           C  
ATOM   2943  CD  LYS C 106      -5.743  44.264  16.075  1.00 15.70           C  
ATOM   2944  CE  LYS C 106      -5.406  45.602  15.506  1.00 16.77           C  
ATOM   2945  NZ  LYS C 106      -4.397  46.394  16.367  1.00 20.34           N  
ATOM   2946  N   THR C 107      -8.769  42.430  12.735  1.00 12.15           N  
ATOM   2947  CA  THR C 107      -8.638  42.419  11.281  1.00 13.28           C  
ATOM   2948  C   THR C 107      -7.712  43.534  10.819  1.00 14.18           C  
ATOM   2949  O   THR C 107      -7.931  44.712  11.110  1.00 14.59           O  
ATOM   2950  CB  THR C 107      -9.988  42.524  10.602  1.00 14.63           C  
ATOM   2951  OG1 THR C 107     -10.786  41.399  10.981  1.00 14.79           O  
ATOM   2952  CG2 THR C 107      -9.830  42.546   9.067  1.00 13.48           C  
ATOM   2953  N   PHE C 108      -6.652  43.120  10.126  1.00 13.58           N  
ATOM   2954  CA  PHE C 108      -5.654  43.978   9.528  1.00 14.72           C  
ATOM   2955  C   PHE C 108      -5.963  44.065   8.028  1.00 14.59           C  
ATOM   2956  O   PHE C 108      -6.239  43.039   7.418  1.00 14.36           O  
ATOM   2957  CB  PHE C 108      -4.266  43.387   9.770  1.00 15.00           C  
ATOM   2958  CG  PHE C 108      -3.901  43.250  11.221  1.00 13.92           C  
ATOM   2959  CD1 PHE C 108      -4.207  42.117  11.913  1.00 13.67           C  
ATOM   2960  CD2 PHE C 108      -3.248  44.277  11.873  1.00 15.29           C  
ATOM   2961  CE1 PHE C 108      -3.858  41.987  13.247  1.00 15.80           C  
ATOM   2962  CE2 PHE C 108      -2.899  44.160  13.215  1.00 16.83           C  
ATOM   2963  CZ  PHE C 108      -3.230  43.010  13.894  1.00 15.19           C  
ATOM   2964  N   ARG C 109      -5.922  45.279   7.470  1.00 13.62           N  
ATOM   2965  CA  ARG C 109      -6.297  45.551   6.092  1.00 12.99           C  
ATOM   2966  C   ARG C 109      -5.120  46.277   5.479  1.00 13.75           C  
ATOM   2967  O   ARG C 109      -5.048  47.518   5.451  1.00 16.03           O  
ATOM   2968  CB  ARG C 109      -7.598  46.375   6.065  1.00 13.84           C  
ATOM   2969  CG  ARG C 109      -8.772  45.571   6.642  1.00 15.97           C  
ATOM   2970  CD  ARG C 109     -10.083  46.275   6.468  1.00 15.87           C  
ATOM   2971  NE  ARG C 109     -10.165  47.436   7.330  1.00 15.92           N  
ATOM   2972  CZ  ARG C 109     -11.187  48.283   7.330  1.00 15.43           C  
ATOM   2973  NH1 ARG C 109     -12.208  48.119   6.504  1.00 19.58           N  
ATOM   2974  NH2 ARG C 109     -11.185  49.307   8.159  1.00 14.23           N  
ATOM   2975  N   GLU C 110      -4.164  45.480   5.010  1.00 14.30           N  
ATOM   2976  CA  GLU C 110      -2.895  45.963   4.498  1.00 14.92           C  
ATOM   2977  C   GLU C 110      -2.189  44.788   3.869  1.00 13.71           C  
ATOM   2978  O   GLU C 110      -2.619  43.647   4.025  1.00 14.02           O  
ATOM   2979  CB  GLU C 110      -2.057  46.490   5.656  1.00 14.82           C  
ATOM   2980  CG  GLU C 110      -1.727  45.406   6.686  1.00 13.98           C  
ATOM   2981  CD  GLU C 110      -1.105  45.992   7.926  1.00 19.24           C  
ATOM   2982  OE1 GLU C 110      -1.856  46.478   8.796  1.00 18.69           O  
ATOM   2983  OE2 GLU C 110       0.138  45.987   8.007  1.00 15.96           O  
ATOM   2984  N   GLN C 111      -1.131  45.040   3.111  1.00 14.31           N  
ATOM   2985  CA  GLN C 111      -0.399  43.952   2.490  1.00 13.57           C  
ATOM   2986  C   GLN C 111       0.547  43.330   3.484  1.00 11.95           C  
ATOM   2987  O   GLN C 111       1.258  44.043   4.190  1.00 13.67           O  
ATOM   2988  CB  GLN C 111       0.389  44.490   1.288  1.00 13.28           C  
ATOM   2989  CG  GLN C 111       1.052  43.454   0.401  1.00 14.89           C  
ATOM   2990  CD  GLN C 111       0.061  42.518  -0.290  1.00 14.91           C  
ATOM   2991  OE1 GLN C 111      -1.134  42.836  -0.405  1.00 16.30           O  
ATOM   2992  NE2 GLN C 111       0.554  41.386  -0.774  1.00 15.00           N  
HETATM 2993  N   MSE C 112       0.573  42.005   3.548  1.00 12.45           N  
HETATM 2994  CA  MSE C 112       1.405  41.258   4.473  1.00 14.01           C  
HETATM 2995  C   MSE C 112       1.940  40.012   3.801  1.00 13.67           C  
HETATM 2996  O   MSE C 112       1.318  39.477   2.896  1.00 14.34           O  
HETATM 2997  CB  MSE C 112       0.607  40.856   5.720  1.00 14.25           C  
HETATM 2998  CG  MSE C 112       0.168  42.001   6.580  1.00 13.67           C  
HETATM 2999 SE   MSE C 112      -1.267  41.618   7.808  0.75 12.21          SE  
HETATM 3000  CE  MSE C 112      -2.720  41.548   6.486  1.00 16.11           C  
ATOM   3001  N   GLU C 113       3.106  39.578   4.241  1.00 13.75           N  
ATOM   3002  CA  GLU C 113       3.655  38.310   3.833  1.00 13.09           C  
ATOM   3003  C   GLU C 113       3.440  37.270   4.930  1.00 13.12           C  
ATOM   3004  O   GLU C 113       3.731  37.522   6.090  1.00 14.57           O  
ATOM   3005  CB  GLU C 113       5.152  38.420   3.550  1.00 15.98           C  
ATOM   3006  CG  GLU C 113       5.457  39.190   2.289  1.00 17.30           C  
ATOM   3007  CD  GLU C 113       5.089  38.483   0.991  1.00 20.42           C  
ATOM   3008  OE1 GLU C 113       4.725  37.284   1.015  1.00 20.16           O  
ATOM   3009  OE2 GLU C 113       5.113  39.163  -0.082  1.00 21.02           O  
ATOM   3010  N   ILE C 114       2.914  36.095   4.594  1.00 13.62           N  
ATOM   3011  CA  ILE C 114       2.822  35.018   5.530  1.00 13.14           C  
ATOM   3012  C   ILE C 114       4.188  34.368   5.663  1.00 14.17           C  
ATOM   3013  O   ILE C 114       4.620  33.699   4.738  1.00 14.25           O  
ATOM   3014  CB  ILE C 114       1.822  33.953   5.058  1.00 14.45           C  
ATOM   3015  CG1 ILE C 114       0.427  34.545   4.858  1.00 14.71           C  
ATOM   3016  CG2 ILE C 114       1.794  32.813   6.086  1.00 15.26           C  
ATOM   3017  CD1 ILE C 114      -0.542  33.520   4.169  1.00 15.68           C  
ATOM   3018  N   SER C 115       4.869  34.585   6.786  1.00 13.95           N  
ATOM   3019  CA  SER C 115       6.178  33.954   6.943  1.00 12.72           C  
ATOM   3020  C   SER C 115       6.048  32.514   7.362  1.00 13.05           C  
ATOM   3021  O   SER C 115       6.917  31.711   7.049  1.00 14.20           O  
ATOM   3022  CB  SER C 115       7.050  34.718   7.910  1.00 15.03           C  
ATOM   3023  OG  SER C 115       6.527  34.762   9.223  1.00 15.01           O  
ATOM   3024  N   ASN C 116       4.952  32.168   8.024  1.00 14.68           N  
ATOM   3025  CA  ASN C 116       4.670  30.798   8.337  1.00 13.78           C  
ATOM   3026  C   ASN C 116       3.210  30.669   8.703  1.00 14.52           C  
ATOM   3027  O   ASN C 116       2.708  31.435   9.460  1.00 15.23           O  
ATOM   3028  CB  ASN C 116       5.536  30.356   9.534  1.00 15.14           C  
ATOM   3029  CG  ASN C 116       5.209  29.006  10.027  1.00 20.15           C  
ATOM   3030  OD1 ASN C 116       4.239  28.824  10.753  1.00 23.32           O  
ATOM   3031  ND2 ASN C 116       5.990  28.030   9.626  1.00 28.86           N  
ATOM   3032  N   LEU C 117       2.546  29.675   8.122  1.00 16.29           N  
ATOM   3033  CA  LEU C 117       1.220  29.237   8.584  1.00 15.55           C  
ATOM   3034  C   LEU C 117       1.460  27.807   9.036  1.00 16.99           C  
ATOM   3035  O   LEU C 117       2.038  27.017   8.291  1.00 19.03           O  
ATOM   3036  CB  LEU C 117       0.207  29.313   7.483  1.00 16.43           C  
ATOM   3037  CG  LEU C 117      -1.241  28.913   7.822  1.00 18.84           C  
ATOM   3038  CD1 LEU C 117      -2.180  29.638   6.883  1.00 19.18           C  
ATOM   3039  CD2 LEU C 117      -1.423  27.385   7.726  1.00 24.21           C  
ATOM   3040  N  ATHR C 118       1.124  27.512  10.306  0.34 15.50           N  
ATOM   3041  N  BTHR C 118       1.101  27.512  10.284  0.33 18.99           N  
ATOM   3042  N  CTHR C 118       0.972  27.469  10.200  0.33 15.40           N  
ATOM   3043  CA ATHR C 118       1.318  26.193  10.978  0.34 14.84           C  
ATOM   3044  CA BTHR C 118       1.221  26.176  10.871  0.33 19.85           C  
ATOM   3045  CA CTHR C 118       1.134  26.111  10.593  0.33 14.02           C  
ATOM   3046  C  ATHR C 118      -0.020  25.709  11.550  0.34 14.90           C  
ATOM   3047  C  BTHR C 118      -0.131  25.764  11.377  0.33 17.85           C  
ATOM   3048  C  CTHR C 118       0.002  25.691  11.500  0.33 14.50           C  
ATOM   3049  O  ATHR C 118      -0.649  26.427  12.323  0.34 13.78           O  
ATOM   3050  O  BTHR C 118      -0.875  26.583  11.902  0.33 16.60           O  
ATOM   3051  O  CTHR C 118      -0.434  26.404  12.404  0.33 13.89           O  
ATOM   3052  CB ATHR C 118       2.328  26.260  12.182  0.34 15.26           C  
ATOM   3053  CB BTHR C 118       2.123  26.142  12.105  0.33 20.95           C  
ATOM   3054  CB CTHR C 118       2.494  25.872  11.195  0.33 11.68           C  
ATOM   3055  OG1ATHR C 118       3.587  26.822  11.775  0.34 12.98           O  
ATOM   3056  OG1BTHR C 118       1.799  27.235  12.963  0.33 27.44           O  
ATOM   3057  OG1CTHR C 118       2.644  24.473  11.385  0.33 12.45           O  
ATOM   3058  CG2ATHR C 118       2.587  24.844  12.803  0.34 10.78           C  
ATOM   3059  CG2BTHR C 118       3.571  26.223  11.723  0.33 24.02           C  
ATOM   3060  CG2CTHR C 118       2.650  26.586  12.529  0.33 10.05           C  
ATOM   3061  N   GLY C 119      -0.471  24.496  11.212  1.00 15.19           N  
ATOM   3062  CA  GLY C 119      -1.668  24.013  11.793  1.00 18.41           C  
ATOM   3063  C   GLY C 119      -1.873  22.559  11.618  1.00 15.50           C  
ATOM   3064  O   GLY C 119      -1.032  21.857  11.067  1.00 15.67           O  
ATOM   3065  N   ASN C 120      -3.015  22.139  12.124  1.00 13.64           N  
ATOM   3066  CA  ASN C 120      -3.349  20.726  12.111  1.00 13.79           C  
ATOM   3067  C   ASN C 120      -4.794  20.508  11.740  1.00 14.47           C  
ATOM   3068  O   ASN C 120      -5.625  21.437  11.774  1.00 14.29           O  
ATOM   3069  CB  ASN C 120      -2.941  20.094  13.452  1.00 15.01           C  
ATOM   3070  CG  ASN C 120      -3.569  20.741  14.643  1.00 16.25           C  
ATOM   3071  OD1 ASN C 120      -4.792  20.842  14.707  1.00 16.58           O  
ATOM   3072  ND2 ASN C 120      -2.747  21.155  15.637  1.00 16.37           N  
ATOM   3073  N   ILE C 121      -5.064  19.269  11.346  1.00 15.81           N  
ATOM   3074  CA  ILE C 121      -6.360  18.800  10.890  1.00 14.51           C  
ATOM   3075  C   ILE C 121      -6.773  17.663  11.804  1.00 14.83           C  
ATOM   3076  O   ILE C 121      -5.952  16.795  12.134  1.00 15.57           O  
ATOM   3077  CB  ILE C 121      -6.280  18.286   9.447  1.00 15.56           C  
ATOM   3078  CG1 ILE C 121      -5.654  19.304   8.494  1.00 15.93           C  
ATOM   3079  CG2 ILE C 121      -7.677  17.849   8.921  1.00 15.36           C  
ATOM   3080  CD1 ILE C 121      -5.149  18.735   7.208  1.00 16.00           C  
ATOM   3081  N   SER C 122      -8.039  17.660  12.191  1.00 15.40           N  
ATOM   3082  CA  SER C 122      -8.627  16.627  13.021  1.00 16.22           C  
ATOM   3083  C   SER C 122     -10.122  16.651  12.726  1.00 16.65           C  
ATOM   3084  O   SER C 122     -10.533  17.250  11.726  1.00 15.68           O  
ATOM   3085  CB  SER C 122      -8.293  16.894  14.478  1.00 17.30           C  
ATOM   3086  OG  SER C 122      -8.726  18.176  14.906  1.00 16.91           O  
ATOM   3087  N   SER C 123     -10.931  15.990  13.539  1.00 16.24           N  
ATOM   3088  CA  SER C 123     -12.347  16.075  13.322  1.00 14.54           C  
ATOM   3089  C   SER C 123     -13.099  16.127  14.621  1.00 15.48           C  
ATOM   3090  O   SER C 123     -12.591  15.743  15.676  1.00 17.64           O  
ATOM   3091  CB  SER C 123     -12.830  14.874  12.507  1.00 17.74           C  
ATOM   3092  OG  SER C 123     -12.616  13.677  13.217  1.00 21.57           O  
HETATM 3093  N   MSE C 124     -14.314  16.637  14.505  1.00 16.11           N  
HETATM 3094  CA  MSE C 124     -15.310  16.545  15.579  1.00 19.07           C  
HETATM 3095  C   MSE C 124     -16.611  16.124  14.933  1.00 18.29           C  
HETATM 3096  O   MSE C 124     -17.086  16.802  14.021  1.00 18.32           O  
HETATM 3097  CB  MSE C 124     -15.486  17.869  16.281  1.00 20.31           C  
HETATM 3098  CG  MSE C 124     -14.230  18.281  16.989  1.00 17.03           C  
HETATM 3099 SE   MSE C 124     -14.477  19.828  18.190  0.75 18.46          SE  
HETATM 3100  CE  MSE C 124     -15.385  19.006  19.510  1.00 20.17           C  
ATOM   3101  N   ASN C 125     -17.157  15.002  15.386  1.00 20.99           N  
ATOM   3102  CA  ASN C 125     -18.413  14.458  14.834  1.00 21.87           C  
ATOM   3103  C   ASN C 125     -18.304  14.289  13.335  1.00 20.33           C  
ATOM   3104  O   ASN C 125     -19.209  14.653  12.595  1.00 19.62           O  
ATOM   3105  CB  ASN C 125     -19.594  15.369  15.191  1.00 25.63           C  
ATOM   3106  CG  ASN C 125     -19.684  15.631  16.681  1.00 33.83           C  
ATOM   3107  OD1 ASN C 125     -19.706  16.787  17.118  1.00 46.52           O  
ATOM   3108  ND2 ASN C 125     -19.675  14.555  17.476  1.00 35.06           N  
ATOM   3109  N   GLU C 126     -17.151  13.776  12.902  1.00 17.07           N  
ATOM   3110  CA  GLU C 126     -16.801  13.589  11.483  1.00 16.23           C  
ATOM   3111  C   GLU C 126     -16.597  14.867  10.665  1.00 17.87           C  
ATOM   3112  O   GLU C 126     -16.282  14.795   9.477  1.00 19.00           O  
ATOM   3113  CB  GLU C 126     -17.814  12.684  10.741  1.00 15.95           C  
ATOM   3114  CG  GLU C 126     -17.997  11.321  11.300  1.00 17.92           C  
ATOM   3115  CD  GLU C 126     -18.973  10.551  10.464  1.00 17.33           C  
ATOM   3116  OE1 GLU C 126     -18.680  10.233   9.280  1.00 15.93           O  
ATOM   3117  OE2 GLU C 126     -20.071  10.264  10.964  1.00 18.01           O  
ATOM   3118  N   GLN C 127     -16.710  16.042  11.278  1.00 15.72           N  
ATOM   3119  CA  GLN C 127     -16.551  17.267  10.552  1.00 16.37           C  
ATOM   3120  C   GLN C 127     -15.105  17.731  10.656  1.00 15.91           C  
ATOM   3121  O   GLN C 127     -14.526  17.692  11.745  1.00 16.31           O  
ATOM   3122  CB  GLN C 127     -17.525  18.306  11.094  1.00 18.93           C  
ATOM   3123  CG  GLN C 127     -18.964  17.798  11.056  1.00 23.09           C  
ATOM   3124  CD  GLN C 127     -19.968  18.852  11.399  1.00 25.19           C  
ATOM   3125  OE1 GLN C 127     -19.751  19.650  12.308  1.00 27.97           O  
ATOM   3126  NE2 GLN C 127     -21.097  18.853  10.687  1.00 29.83           N  
ATOM   3127  N  AVAL C 128     -14.535  18.135   9.525  0.60 14.64           N  
ATOM   3128  N  BVAL C 128     -14.523  18.148   9.540  0.40 16.01           N  
ATOM   3129  CA AVAL C 128     -13.184  18.720   9.465  0.60 15.37           C  
ATOM   3130  CA BVAL C 128     -13.127  18.574   9.548  0.40 16.89           C  
ATOM   3131  C  AVAL C 128     -13.033  19.775  10.558  0.60 14.95           C  
ATOM   3132  C  BVAL C 128     -12.939  19.814  10.435  0.40 16.26           C  
ATOM   3133  O  AVAL C 128     -13.945  20.583  10.777  0.60 14.73           O  
ATOM   3134  O  BVAL C 128     -13.699  20.795  10.357  0.40 15.73           O  
ATOM   3135  CB AVAL C 128     -12.887  19.364   8.083  0.60 14.22           C  
ATOM   3136  CB BVAL C 128     -12.567  18.808   8.129  0.40 17.19           C  
ATOM   3137  CG1AVAL C 128     -11.580  20.214   8.116  0.60 18.07           C  
ATOM   3138  CG1BVAL C 128     -13.087  20.104   7.527  0.40 16.48           C  
ATOM   3139  CG2AVAL C 128     -12.841  18.283   6.974  0.60 16.04           C  
ATOM   3140  CG2BVAL C 128     -11.053  18.798   8.179  0.40 18.86           C  
ATOM   3141  N   TYR C 129     -11.911  19.733  11.274  1.00 15.87           N  
ATOM   3142  CA  TYR C 129     -11.589  20.730  12.273  1.00 15.54           C  
ATOM   3143  C   TYR C 129     -10.176  21.170  11.995  1.00 15.62           C  
ATOM   3144  O   TYR C 129      -9.249  20.363  12.109  1.00 15.24           O  
ATOM   3145  CB  TYR C 129     -11.695  20.137  13.686  1.00 16.84           C  
ATOM   3146  CG  TYR C 129     -11.629  21.160  14.776  1.00 18.89           C  
ATOM   3147  CD1 TYR C 129     -10.413  21.689  15.185  1.00 20.51           C  
ATOM   3148  CD2 TYR C 129     -12.779  21.597  15.402  1.00 20.43           C  
ATOM   3149  CE1 TYR C 129     -10.338  22.634  16.198  1.00 19.00           C  
ATOM   3150  CE2 TYR C 129     -12.734  22.549  16.420  1.00 23.17           C  
ATOM   3151  CZ  TYR C 129     -11.511  23.070  16.817  1.00 21.13           C  
ATOM   3152  OH  TYR C 129     -11.440  24.019  17.821  1.00 23.54           O  
ATOM   3153  N  ALEU C 130     -10.023  22.445  11.646  0.60 14.89           N  
ATOM   3154  N  BLEU C 130      -9.992  22.433  11.608  0.40 14.62           N  
ATOM   3155  CA ALEU C 130      -8.713  23.039  11.449  0.60 15.66           C  
ATOM   3156  CA BLEU C 130      -8.654  22.981  11.331  0.40 14.82           C  
ATOM   3157  C  ALEU C 130      -8.352  23.882  12.652  0.60 15.05           C  
ATOM   3158  C  BLEU C 130      -8.249  23.995  12.411  0.40 14.98           C  
ATOM   3159  O  ALEU C 130      -9.194  24.585  13.238  0.60 15.19           O  
ATOM   3160  O  BLEU C 130      -8.955  24.974  12.632  0.40 15.25           O  
ATOM   3161  CB ALEU C 130      -8.675  23.898  10.196  0.60 16.04           C  
ATOM   3162  CB BLEU C 130      -8.591  23.616   9.933  0.40 13.98           C  
ATOM   3163  CG ALEU C 130      -9.059  23.199   8.908  0.60 14.40           C  
ATOM   3164  CG BLEU C 130      -8.299  22.692   8.748  0.40 14.30           C  
ATOM   3165  CD1ALEU C 130      -8.777  24.163   7.753  0.60 17.96           C  
ATOM   3166  CD1BLEU C 130      -9.372  21.619   8.576  0.40 15.53           C  
ATOM   3167  CD2ALEU C 130      -8.316  21.895   8.694  0.60 16.82           C  
ATOM   3168  CD2BLEU C 130      -8.156  23.519   7.462  0.40 15.17           C  
ATOM   3169  N   HIS C 131      -7.095  23.766  13.047  1.00 14.02           N  
ATOM   3170  CA  HIS C 131      -6.523  24.632  14.069  1.00 14.84           C  
ATOM   3171  C   HIS C 131      -5.263  25.208  13.443  1.00 14.56           C  
ATOM   3172  O   HIS C 131      -4.266  24.507  13.284  1.00 13.66           O  
ATOM   3173  CB  HIS C 131      -6.223  23.843  15.340  1.00 15.57           C  
ATOM   3174  CG  HIS C 131      -5.799  24.688  16.490  1.00 17.48           C  
ATOM   3175  ND1 HIS C 131      -5.190  24.152  17.602  1.00 17.43           N  
ATOM   3176  CD2 HIS C 131      -5.852  26.026  16.692  1.00 16.81           C  
ATOM   3177  CE1 HIS C 131      -4.910  25.125  18.456  1.00 22.09           C  
ATOM   3178  NE2 HIS C 131      -5.336  26.268  17.945  1.00 19.50           N  
ATOM   3179  N   LEU C 132      -5.321  26.492  13.085  1.00 13.66           N  
ATOM   3180  CA  LEU C 132      -4.272  27.140  12.311  1.00 12.90           C  
ATOM   3181  C   LEU C 132      -3.760  28.383  13.032  1.00 12.70           C  
ATOM   3182  O   LEU C 132      -4.550  29.215  13.490  1.00 13.48           O  
ATOM   3183  CB  LEU C 132      -4.796  27.579  10.959  1.00 14.97           C  
ATOM   3184  CG  LEU C 132      -5.553  26.523  10.129  1.00 13.72           C  
ATOM   3185  CD1 LEU C 132      -5.992  27.184   8.830  1.00 18.88           C  
ATOM   3186  CD2 LEU C 132      -4.714  25.300   9.858  1.00 18.72           C  
ATOM   3187  N   HIS C 133      -2.451  28.479  13.136  1.00 13.40           N  
ATOM   3188  CA  HIS C 133      -1.802  29.691  13.637  1.00 13.88           C  
ATOM   3189  C   HIS C 133      -0.958  30.264  12.505  1.00 14.35           C  
ATOM   3190  O   HIS C 133      -0.682  29.599  11.487  1.00 14.08           O  
ATOM   3191  CB  HIS C 133      -0.948  29.426  14.865  1.00 13.96           C  
ATOM   3192  CG  HIS C 133      -1.738  29.186  16.125  1.00 14.05           C  
ATOM   3193  ND1 HIS C 133      -1.135  29.220  17.364  1.00 15.14           N  
ATOM   3194  CD2 HIS C 133      -3.039  28.895  16.350  1.00 15.03           C  
ATOM   3195  CE1 HIS C 133      -2.038  28.977  18.300  1.00 15.85           C  
ATOM   3196  NE2 HIS C 133      -3.207  28.792  17.718  1.00 14.83           N  
ATOM   3197  N   ILE C 134      -0.529  31.499  12.690  1.00 13.60           N  
ATOM   3198  CA  ILE C 134       0.139  32.193  11.620  1.00 13.88           C  
ATOM   3199  C   ILE C 134       1.074  33.252  12.145  1.00 14.73           C  
ATOM   3200  O   ILE C 134       0.865  33.823  13.219  1.00 13.76           O  
ATOM   3201  CB  ILE C 134      -0.904  32.814  10.627  1.00 13.47           C  
ATOM   3202  CG1 ILE C 134      -0.308  33.175   9.252  1.00 13.93           C  
ATOM   3203  CG2 ILE C 134      -1.608  34.043  11.269  1.00 14.16           C  
ATOM   3204  CD1 ILE C 134      -1.406  33.609   8.242  1.00 14.38           C  
ATOM   3205  N   THR C 135       2.127  33.480  11.369  1.00 13.47           N  
ATOM   3206  CA  THR C 135       3.056  34.574  11.590  1.00 13.28           C  
ATOM   3207  C   THR C 135       3.110  35.331  10.279  1.00 13.77           C  
ATOM   3208  O   THR C 135       3.275  34.722   9.214  1.00 13.03           O  
ATOM   3209  CB  THR C 135       4.456  34.085  11.911  1.00 12.62           C  
ATOM   3210  OG1 THR C 135       4.394  33.115  12.986  1.00 14.87           O  
ATOM   3211  CG2 THR C 135       5.358  35.218  12.302  1.00 14.38           C  
ATOM   3212  N   VAL C 136       2.971  36.648  10.319  1.00 12.84           N  
ATOM   3213  CA  VAL C 136       3.051  37.462   9.118  1.00 13.86           C  
ATOM   3214  C   VAL C 136       4.001  38.628   9.320  1.00 12.99           C  
ATOM   3215  O   VAL C 136       4.279  39.043  10.461  1.00 14.28           O  
ATOM   3216  CB  VAL C 136       1.670  38.036   8.684  1.00 15.22           C  
ATOM   3217  CG1 VAL C 136       0.646  36.908   8.471  1.00 14.06           C  
ATOM   3218  CG2 VAL C 136       1.148  39.071   9.700  1.00 15.97           C  
ATOM   3219  N   GLY C 137       4.524  39.132   8.208  1.00 12.63           N  
ATOM   3220  CA  GLY C 137       5.295  40.361   8.200  1.00 11.60           C  
ATOM   3221  C   GLY C 137       4.553  41.486   7.526  1.00 13.52           C  
ATOM   3222  O   GLY C 137       3.914  41.282   6.492  1.00 14.24           O  
ATOM   3223  N   ARG C 138       4.611  42.662   8.125  1.00 12.76           N  
ATOM   3224  CA  ARG C 138       4.001  43.842   7.549  1.00 13.23           C  
ATOM   3225  C   ARG C 138       4.982  44.502   6.596  1.00 13.65           C  
ATOM   3226  O   ARG C 138       6.123  44.030   6.404  1.00 13.43           O  
ATOM   3227  CB  ARG C 138       3.650  44.781   8.700  1.00 13.39           C  
ATOM   3228  CG  ARG C 138       2.751  44.126   9.755  1.00 14.74           C  
ATOM   3229  CD  ARG C 138       2.437  45.033  10.900  1.00 14.69           C  
ATOM   3230  NE  ARG C 138       1.218  45.802  10.660  1.00 14.29           N  
ATOM   3231  CZ  ARG C 138       0.508  46.382  11.622  1.00 15.28           C  
ATOM   3232  NH1 ARG C 138       0.928  46.428  12.863  1.00 16.23           N  
ATOM   3233  NH2 ARG C 138      -0.624  46.994  11.323  1.00 16.08           N  
ATOM   3234  N   SER C 139       4.606  45.650   6.015  1.00 14.49           N  
ATOM   3235  CA  SER C 139       5.464  46.344   5.066  1.00 14.63           C  
ATOM   3236  C   SER C 139       6.719  46.904   5.678  1.00 15.41           C  
ATOM   3237  O   SER C 139       7.692  47.154   4.959  1.00 17.26           O  
ATOM   3238  CB  SER C 139       4.673  47.462   4.375  1.00 17.25           C  
ATOM   3239  OG  SER C 139       4.335  48.469   5.312  1.00 16.39           O  
ATOM   3240  N   ASP C 140       6.731  47.065   6.995  1.00 14.63           N  
ATOM   3241  CA  ASP C 140       7.933  47.494   7.709  1.00 13.98           C  
ATOM   3242  C   ASP C 140       8.721  46.303   8.298  1.00 13.36           C  
ATOM   3243  O   ASP C 140       9.620  46.505   9.099  1.00 15.11           O  
ATOM   3244  CB  ASP C 140       7.583  48.501   8.806  1.00 15.71           C  
ATOM   3245  CG  ASP C 140       6.807  47.911   9.957  1.00 19.38           C  
ATOM   3246  OD1 ASP C 140       6.380  46.740   9.895  1.00 15.38           O  
ATOM   3247  OD2 ASP C 140       6.593  48.628  10.967  1.00 20.59           O  
ATOM   3248  N   TYR C 141       8.334  45.103   7.900  1.00 12.88           N  
ATOM   3249  CA  TYR C 141       8.944  43.840   8.336  1.00 12.38           C  
ATOM   3250  C   TYR C 141       8.662  43.459   9.765  1.00 13.59           C  
ATOM   3251  O   TYR C 141       9.062  42.373  10.185  1.00 13.90           O  
ATOM   3252  CB  TYR C 141      10.453  43.813   8.023  1.00 13.36           C  
ATOM   3253  CG  TYR C 141      10.730  44.127   6.570  1.00 14.40           C  
ATOM   3254  CD1 TYR C 141      10.525  43.154   5.610  1.00 15.37           C  
ATOM   3255  CD2 TYR C 141      11.093  45.384   6.166  1.00 16.51           C  
ATOM   3256  CE1 TYR C 141      10.761  43.406   4.251  1.00 15.58           C  
ATOM   3257  CE2 TYR C 141      11.325  45.652   4.819  1.00 14.85           C  
ATOM   3258  CZ  TYR C 141      11.154  44.651   3.887  1.00 15.89           C  
ATOM   3259  OH  TYR C 141      11.408  44.939   2.573  1.00 18.48           O  
ATOM   3260  N   SER C 142       7.917  44.275  10.521  1.00 13.60           N  
ATOM   3261  CA  SER C 142       7.510  43.849  11.837  1.00 13.90           C  
ATOM   3262  C   SER C 142       6.564  42.664  11.721  1.00 13.90           C  
ATOM   3263  O   SER C 142       5.832  42.551  10.758  1.00 14.31           O  
ATOM   3264  CB  SER C 142       6.839  44.978  12.630  1.00 14.74           C  
ATOM   3265  OG  SER C 142       5.630  45.409  12.029  1.00 15.68           O  
ATOM   3266  N   ALA C 143       6.651  41.761  12.693  1.00 13.74           N  
ATOM   3267  CA  ALA C 143       5.852  40.551  12.668  1.00 12.77           C  
ATOM   3268  C   ALA C 143       4.621  40.607  13.574  1.00 14.13           C  
ATOM   3269  O   ALA C 143       4.708  41.122  14.706  1.00 14.93           O  
ATOM   3270  CB  ALA C 143       6.713  39.329  12.998  1.00 15.86           C  
ATOM   3271  N   LEU C 144       3.523  40.016  13.093  1.00 12.90           N  
ATOM   3272  CA  LEU C 144       2.326  39.794  13.856  1.00 13.38           C  
ATOM   3273  C   LEU C 144       2.139  38.287  13.927  1.00 14.34           C  
ATOM   3274  O   LEU C 144       2.554  37.570  13.001  1.00 15.04           O  
ATOM   3275  CB  LEU C 144       1.122  40.408  13.171  1.00 14.89           C  
ATOM   3276  CG  LEU C 144       1.160  41.915  12.890  1.00 14.83           C  
ATOM   3277  CD1 LEU C 144      -0.024  42.258  11.998  1.00 18.14           C  
ATOM   3278  CD2 LEU C 144       1.140  42.714  14.176  1.00 17.12           C  
ATOM   3279  N   ALA C 145       1.509  37.799  14.990  1.00 13.17           N  
ATOM   3280  CA  ALA C 145       1.370  36.361  15.164  1.00 13.19           C  
ATOM   3281  C   ALA C 145       0.175  36.024  16.010  1.00 12.74           C  
ATOM   3282  O   ALA C 145      -0.169  36.772  16.911  1.00 14.19           O  
ATOM   3283  CB  ALA C 145       2.637  35.767  15.805  1.00 14.77           C  
ATOM   3284  N   GLY C 146      -0.446  34.880  15.709  1.00 13.51           N  
ATOM   3285  CA  GLY C 146      -1.521  34.398  16.526  1.00 14.44           C  
ATOM   3286  C   GLY C 146      -2.352  33.305  15.901  1.00 13.35           C  
ATOM   3287  O   GLY C 146      -1.951  32.676  14.937  1.00 15.20           O  
ATOM   3288  N   HIS C 147      -3.526  33.100  16.488  1.00 13.66           N  
ATOM   3289  CA  HIS C 147      -4.521  32.155  15.996  1.00 13.32           C  
ATOM   3290  C   HIS C 147      -5.231  32.763  14.798  1.00 13.98           C  
ATOM   3291  O   HIS C 147      -5.862  33.826  14.900  1.00 13.60           O  
ATOM   3292  CB  HIS C 147      -5.490  31.842  17.150  1.00 14.45           C  
ATOM   3293  CG  HIS C 147      -6.682  31.023  16.793  1.00 15.10           C  
ATOM   3294  ND1 HIS C 147      -6.697  30.057  15.807  1.00 24.94           N  
ATOM   3295  CD2 HIS C 147      -7.903  30.980  17.370  1.00 20.19           C  
ATOM   3296  CE1 HIS C 147      -7.890  29.475  15.790  1.00 19.09           C  
ATOM   3297  NE2 HIS C 147      -8.646  30.046  16.694  1.00 23.70           N  
ATOM   3298  N   LEU C 148      -5.151  32.054  13.670  1.00 14.14           N  
ATOM   3299  CA  LEU C 148      -5.692  32.506  12.425  1.00 14.75           C  
ATOM   3300  C   LEU C 148      -7.169  32.183  12.299  1.00 14.47           C  
ATOM   3301  O   LEU C 148      -7.566  31.032  12.351  1.00 14.92           O  
ATOM   3302  CB  LEU C 148      -4.937  31.824  11.281  1.00 13.29           C  
ATOM   3303  CG  LEU C 148      -5.455  32.054   9.863  1.00 11.62           C  
ATOM   3304  CD1 LEU C 148      -5.312  33.532   9.481  1.00 15.22           C  
ATOM   3305  CD2 LEU C 148      -4.751  31.133   8.862  1.00 14.19           C  
ATOM   3306  N   LEU C 149      -7.972  33.213  12.038  1.00 13.00           N  
ATOM   3307  CA  LEU C 149      -9.367  33.002  11.683  1.00 13.34           C  
ATOM   3308  C   LEU C 149      -9.648  33.104  10.179  1.00 13.96           C  
ATOM   3309  O   LEU C 149     -10.482  32.353   9.626  1.00 15.70           O  
ATOM   3310  CB  LEU C 149     -10.272  34.033  12.364  1.00 14.60           C  
ATOM   3311  CG  LEU C 149     -10.347  34.038  13.892  1.00 15.00           C  
ATOM   3312  CD1 LEU C 149     -11.457  34.972  14.339  1.00 16.22           C  
ATOM   3313  CD2 LEU C 149     -10.570  32.628  14.468  1.00 16.89           C  
ATOM   3314  N  ASER C 150      -9.010  34.064   9.523  0.50 14.24           N  
ATOM   3315  N  BSER C 150      -8.991  34.060   9.527  0.50 13.13           N  
ATOM   3316  CA ASER C 150      -9.178  34.240   8.092  0.50 14.39           C  
ATOM   3317  CA BSER C 150      -9.254  34.379   8.135  0.50 12.47           C  
ATOM   3318  C  ASER C 150      -8.031  35.068   7.533  0.50 13.44           C  
ATOM   3319  C  BSER C 150      -8.072  35.144   7.526  0.50 12.97           C  
ATOM   3320  O  ASER C 150      -7.366  35.802   8.277  0.50 13.79           O  
ATOM   3321  O  BSER C 150      -7.403  35.906   8.240  0.50 13.16           O  
ATOM   3322  CB ASER C 150     -10.521  34.917   7.780  0.50 16.03           C  
ATOM   3323  CB BSER C 150     -10.523  35.242   8.066  0.50 11.60           C  
ATOM   3324  OG ASER C 150     -10.602  36.200   8.359  0.50 16.84           O  
ATOM   3325  OG BSER C 150     -10.800  35.699   6.752  0.50 16.36           O  
ATOM   3326  N   ALA C 151      -7.823  34.957   6.224  1.00 13.79           N  
ATOM   3327  CA  ALA C 151      -6.848  35.771   5.527  1.00 16.28           C  
ATOM   3328  C   ALA C 151      -7.174  35.720   4.051  1.00 15.06           C  
ATOM   3329  O   ALA C 151      -7.482  34.648   3.522  1.00 16.69           O  
ATOM   3330  CB  ALA C 151      -5.445  35.297   5.763  1.00 14.94           C  
ATOM   3331  N   ILE C 152      -7.106  36.869   3.382  1.00 14.94           N  
ATOM   3332  CA  ILE C 152      -7.433  36.958   1.969  1.00 12.90           C  
ATOM   3333  C   ILE C 152      -6.134  37.057   1.160  1.00 13.98           C  
ATOM   3334  O   ILE C 152      -5.356  38.002   1.345  1.00 13.35           O  
ATOM   3335  CB  ILE C 152      -8.339  38.127   1.643  1.00 12.65           C  
ATOM   3336  CG1 ILE C 152      -9.624  38.087   2.485  1.00 16.27           C  
ATOM   3337  CG2 ILE C 152      -8.666  38.088   0.145  1.00 14.22           C  
ATOM   3338  CD1 ILE C 152     -10.520  39.285   2.318  1.00 18.07           C  
ATOM   3339  N   GLN C 153      -5.899  36.067   0.312  1.00 13.43           N  
ATOM   3340  CA  GLN C 153      -4.685  36.018  -0.475  1.00 12.80           C  
ATOM   3341  C   GLN C 153      -4.594  37.220  -1.435  1.00 13.60           C  
ATOM   3342  O   GLN C 153      -5.583  37.654  -2.020  1.00 14.24           O  
ATOM   3343  CB  GLN C 153      -4.657  34.731  -1.257  1.00 12.71           C  
ATOM   3344  CG  GLN C 153      -3.338  34.474  -1.979  1.00 14.56           C  
ATOM   3345  CD  GLN C 153      -3.233  33.057  -2.457  1.00 15.51           C  
ATOM   3346  OE1 GLN C 153      -3.459  32.140  -1.671  1.00 15.70           O  
ATOM   3347  NE2 GLN C 153      -2.845  32.866  -3.728  1.00 15.88           N  
ATOM   3348  N   ASN C 154      -3.386  37.753  -1.562  1.00 12.99           N  
ATOM   3349  CA  ASN C 154      -3.092  38.811  -2.518  1.00 14.10           C  
ATOM   3350  C   ASN C 154      -1.660  38.579  -2.979  1.00 14.29           C  
ATOM   3351  O   ASN C 154      -0.716  39.222  -2.533  1.00 15.50           O  
ATOM   3352  CB  ASN C 154      -3.284  40.192  -1.920  1.00 13.29           C  
ATOM   3353  CG  ASN C 154      -3.311  41.272  -2.971  1.00 16.66           C  
ATOM   3354  OD1 ASN C 154      -3.876  41.076  -4.053  1.00 17.84           O  
ATOM   3355  ND2 ASN C 154      -2.749  42.441  -2.649  1.00 16.77           N  
ATOM   3356  N   GLY C 155      -1.520  37.610  -3.863  1.00 13.04           N  
ATOM   3357  CA  GLY C 155      -0.225  37.149  -4.339  1.00 14.16           C  
ATOM   3358  C   GLY C 155      -0.318  35.645  -4.455  1.00 15.12           C  
ATOM   3359  O   GLY C 155      -1.333  35.095  -4.947  1.00 16.22           O  
ATOM   3360  N   ALA C 156       0.725  34.965  -3.980  1.00 15.93           N  
ATOM   3361  CA  ALA C 156       0.781  33.502  -3.963  1.00 14.01           C  
ATOM   3362  C   ALA C 156       0.261  32.904  -2.654  1.00 14.84           C  
ATOM   3363  O   ALA C 156       0.146  33.592  -1.651  1.00 15.64           O  
ATOM   3364  CB  ALA C 156       2.220  33.060  -4.187  1.00 18.70           C  
ATOM   3365  N   GLY C 157      -0.012  31.594  -2.668  1.00 14.42           N  
ATOM   3366  CA  GLY C 157      -0.469  30.861  -1.502  1.00 14.75           C  
ATOM   3367  C   GLY C 157      -0.082  29.408  -1.702  1.00 15.52           C  
ATOM   3368  O   GLY C 157      -0.743  28.702  -2.479  1.00 16.73           O  
ATOM   3369  N   GLU C 158       0.993  28.995  -1.043  1.00 15.57           N  
ATOM   3370  CA  GLU C 158       1.671  27.745  -1.297  1.00 14.26           C  
ATOM   3371  C   GLU C 158       1.723  26.940  -0.011  1.00 13.71           C  
ATOM   3372  O   GLU C 158       2.451  27.273   0.924  1.00 14.29           O  
ATOM   3373  CB  GLU C 158       3.076  28.049  -1.837  1.00 14.27           C  
ATOM   3374  CG  GLU C 158       3.032  28.864  -3.128  1.00 14.93           C  
ATOM   3375  CD  GLU C 158       4.362  29.326  -3.620  1.00 15.29           C  
ATOM   3376  OE1 GLU C 158       5.407  28.917  -3.086  1.00 15.74           O  
ATOM   3377  OE2 GLU C 158       4.366  30.176  -4.551  1.00 15.13           O  
ATOM   3378  N   PHE C 159       0.900  25.893   0.057  1.00 15.21           N  
ATOM   3379  CA  PHE C 159       0.718  25.132   1.264  1.00 16.08           C  
ATOM   3380  C   PHE C 159       0.950  23.661   1.029  1.00 17.77           C  
ATOM   3381  O   PHE C 159       0.688  23.153  -0.064  1.00 20.47           O  
ATOM   3382  CB  PHE C 159      -0.677  25.373   1.827  1.00 16.48           C  
ATOM   3383  CG  PHE C 159      -0.940  26.824   2.095  1.00 17.40           C  
ATOM   3384  CD1 PHE C 159      -0.520  27.404   3.263  1.00 18.96           C  
ATOM   3385  CD2 PHE C 159      -1.517  27.628   1.130  1.00 18.18           C  
ATOM   3386  CE1 PHE C 159      -0.666  28.759   3.473  1.00 18.80           C  
ATOM   3387  CE2 PHE C 159      -1.688  28.977   1.341  1.00 18.36           C  
ATOM   3388  CZ  PHE C 159      -1.274  29.533   2.534  1.00 19.91           C  
ATOM   3389  N   VAL C 160       1.501  22.988   2.033  1.00 14.83           N  
ATOM   3390  CA  VAL C 160       1.663  21.552   2.031  1.00 17.11           C  
ATOM   3391  C   VAL C 160       0.666  21.002   3.039  1.00 15.56           C  
ATOM   3392  O   VAL C 160       0.672  21.372   4.228  1.00 15.72           O  
ATOM   3393  CB  VAL C 160       3.061  21.111   2.458  1.00 17.94           C  
ATOM   3394  CG1 VAL C 160       3.135  19.595   2.445  1.00 17.94           C  
ATOM   3395  CG2 VAL C 160       4.114  21.672   1.535  1.00 18.13           C  
ATOM   3396  N   VAL C 161      -0.212  20.127   2.573  1.00 17.73           N  
ATOM   3397  CA  VAL C 161      -1.176  19.448   3.420  1.00 18.10           C  
ATOM   3398  C   VAL C 161      -0.769  17.987   3.470  1.00 20.08           C  
ATOM   3399  O   VAL C 161      -0.792  17.312   2.434  1.00 18.84           O  
ATOM   3400  CB  VAL C 161      -2.580  19.564   2.870  1.00 18.73           C  
ATOM   3401  CG1 VAL C 161      -3.566  18.762   3.737  1.00 19.77           C  
ATOM   3402  CG2 VAL C 161      -3.009  21.050   2.759  1.00 17.96           C  
ATOM   3403  N   GLU C 162      -0.349  17.526   4.639  1.00 17.21           N  
ATOM   3404  CA  GLU C 162       0.001  16.124   4.842  1.00 18.90           C  
ATOM   3405  C   GLU C 162      -1.225  15.442   5.378  1.00 18.00           C  
ATOM   3406  O   GLU C 162      -1.821  15.885   6.336  1.00 17.66           O  
ATOM   3407  CB  GLU C 162       1.149  15.917   5.814  1.00 20.01           C  
ATOM   3408  CG  GLU C 162       1.499  14.439   5.946  1.00 24.30           C  
ATOM   3409  CD  GLU C 162       2.699  14.150   6.819  1.00 26.96           C  
ATOM   3410  OE1 GLU C 162       3.503  15.068   7.081  1.00 36.85           O  
ATOM   3411  OE2 GLU C 162       2.840  12.966   7.227  1.00 33.75           O  
ATOM   3412  N   ASP C 163      -1.581  14.324   4.746  1.00 17.02           N  
ATOM   3413  CA  ASP C 163      -2.715  13.504   5.135  1.00 18.11           C  
ATOM   3414  C   ASP C 163      -2.205  12.308   5.937  1.00 16.39           C  
ATOM   3415  O   ASP C 163      -1.511  11.465   5.386  1.00 18.73           O  
ATOM   3416  CB  ASP C 163      -3.403  13.043   3.850  1.00 18.93           C  
ATOM   3417  CG  ASP C 163      -4.622  12.190   4.080  1.00 19.30           C  
ATOM   3418  OD1 ASP C 163      -5.033  11.947   5.237  1.00 18.18           O  
ATOM   3419  OD2 ASP C 163      -5.185  11.738   3.043  1.00 19.84           O  
ATOM   3420  N   TYR C 164      -2.599  12.229   7.199  1.00 16.66           N  
ATOM   3421  CA  TYR C 164      -2.216  11.106   8.058  1.00 17.21           C  
ATOM   3422  C   TYR C 164      -3.065   9.863   7.871  1.00 18.61           C  
ATOM   3423  O   TYR C 164      -2.691   8.821   8.387  1.00 18.62           O  
ATOM   3424  CB  TYR C 164      -2.299  11.476   9.539  1.00 15.70           C  
ATOM   3425  CG  TYR C 164      -1.449  12.618  10.028  1.00 15.85           C  
ATOM   3426  CD1 TYR C 164      -0.285  13.019   9.382  1.00 16.15           C  
ATOM   3427  CD2 TYR C 164      -1.785  13.266  11.193  1.00 18.06           C  
ATOM   3428  CE1 TYR C 164       0.472  14.067   9.870  1.00 15.27           C  
ATOM   3429  CE2 TYR C 164      -1.043  14.281  11.688  1.00 17.59           C  
ATOM   3430  CZ  TYR C 164       0.074  14.692  11.028  1.00 16.96           C  
ATOM   3431  OH  TYR C 164       0.812  15.737  11.559  1.00 17.50           O  
ATOM   3432  N   SER C 165      -4.210   9.958   7.193  1.00 17.86           N  
ATOM   3433  CA  SER C 165      -5.069   8.795   6.954  1.00 17.47           C  
ATOM   3434  C   SER C 165      -5.507   8.086   8.224  1.00 19.06           C  
ATOM   3435  O   SER C 165      -5.676   6.865   8.217  1.00 22.57           O  
ATOM   3436  CB  SER C 165      -4.355   7.804   6.029  1.00 17.89           C  
ATOM   3437  OG  SER C 165      -4.144   8.365   4.758  1.00 24.45           O  
ATOM   3438  N  AGLU C 166      -5.573   8.839   9.298  0.60 21.06           N  
ATOM   3439  N  BGLU C 166      -5.843   8.839   9.270  0.40 17.27           N  
ATOM   3440  CA AGLU C 166      -5.807   8.342  10.618  0.60 23.95           C  
ATOM   3441  CA BGLU C 166      -6.367   8.283  10.545  0.40 19.17           C  
ATOM   3442  C  AGLU C 166      -6.715   9.342  11.243  0.60 24.28           C  
ATOM   3443  C  BGLU C 166      -7.343   9.227  11.278  0.40 15.95           C  
ATOM   3444  O  AGLU C 166      -6.497  10.540  11.210  0.60 26.00           O  
ATOM   3445  O  BGLU C 166      -7.138  10.446  11.282  0.40 10.45           O  
ATOM   3446  CB AGLU C 166      -4.528   8.263  11.446  0.60 24.96           C  
ATOM   3447  CB BGLU C 166      -5.221   7.910  11.501  0.40 20.14           C  
ATOM   3448  CG AGLU C 166      -3.621   7.119  11.102  0.60 27.14           C  
ATOM   3449  CG BGLU C 166      -4.468   6.652  11.110  0.40 25.72           C  
ATOM   3450  CD AGLU C 166      -4.196   5.756  11.442  0.60 30.70           C  
ATOM   3451  CD BGLU C 166      -3.503   6.156  12.180  0.40 22.90           C  
ATOM   3452  OE1AGLU C 166      -5.175   5.675  12.219  0.60 30.88           O  
ATOM   3453  OE1BGLU C 166      -3.846   6.188  13.383  0.40 29.73           O  
ATOM   3454  OE2AGLU C 166      -3.647   4.765  10.926  0.60 35.02           O  
ATOM   3455  OE2BGLU C 166      -2.401   5.709  11.800  0.40 30.67           O  
ATOM   3456  N  AARG C 167      -7.785   8.810  11.831  0.40 23.45           N  
ATOM   3457  N  BARG C 167      -8.394   8.682  11.907  0.60 16.75           N  
ATOM   3458  CA AARG C 167      -8.811   9.607  12.495  0.40 23.19           C  
ATOM   3459  CA BARG C 167      -9.272   9.507  12.717  0.60 18.28           C  
ATOM   3460  C  AARG C 167      -8.254  10.147  13.794  0.40 22.71           C  
ATOM   3461  C  BARG C 167      -8.493  10.092  13.894  0.60 20.00           C  
ATOM   3462  O  AARG C 167      -7.561   9.434  14.525  0.40 22.33           O  
ATOM   3463  O  BARG C 167      -7.833   9.341  14.613  0.60 20.43           O  
ATOM   3464  CB AARG C 167     -10.061   8.754  12.767  0.40 24.51           C  
ATOM   3465  CB BARG C 167     -10.432   8.632  13.221  0.60 18.63           C  
ATOM   3466  CG AARG C 167     -11.248   9.464  13.458  0.40 25.64           C  
ATOM   3467  CG BARG C 167     -11.543   9.333  13.994  0.60 20.88           C  
ATOM   3468  CD AARG C 167     -12.307   8.419  13.867  0.40 25.50           C  
ATOM   3469  CD BARG C 167     -12.330  10.292  13.099  0.60 18.79           C  
ATOM   3470  NE AARG C 167     -13.314   8.830  14.844  0.40 29.34           N  
ATOM   3471  NE BARG C 167     -13.040   9.668  11.977  0.60 24.43           N  
ATOM   3472  CZ AARG C 167     -13.077   9.142  16.121  0.40 26.54           C  
ATOM   3473  CZ BARG C 167     -13.589  10.337  10.955  0.60 19.07           C  
ATOM   3474  NH1AARG C 167     -14.096   9.478  16.899  0.40 26.13           N  
ATOM   3475  NH1BARG C 167     -14.236   9.664   9.989  0.60 11.90           N  
ATOM   3476  NH2AARG C 167     -11.852   9.126  16.636  0.40 34.01           N  
ATOM   3477  NH2BARG C 167     -13.504  11.679  10.883  0.60 17.16           N  
ATOM   3478  N   ILE C 168      -8.522  11.422  14.058  1.00 20.26           N  
ATOM   3479  CA  ILE C 168      -8.067  12.087  15.304  1.00 18.78           C  
ATOM   3480  C   ILE C 168      -9.192  13.019  15.702  1.00 19.31           C  
ATOM   3481  O   ILE C 168      -9.566  13.908  14.915  1.00 18.46           O  
ATOM   3482  CB  ILE C 168      -6.787  12.931  15.196  1.00 20.99           C  
ATOM   3483  CG1 ILE C 168      -5.594  12.071  14.785  1.00 24.52           C  
ATOM   3484  CG2 ILE C 168      -6.491  13.620  16.536  1.00 23.27           C  
ATOM   3485  CD1 ILE C 168      -4.325  12.855  14.639  1.00 21.88           C  
ATOM   3486  N   SER C 169      -9.720  12.836  16.906  1.00 21.10           N  
ATOM   3487  CA  SER C 169     -10.854  13.618  17.386  1.00 21.91           C  
ATOM   3488  C   SER C 169     -10.490  14.561  18.523  1.00 21.01           C  
ATOM   3489  O   SER C 169      -9.403  14.505  19.087  1.00 21.82           O  
ATOM   3490  CB  SER C 169     -11.973  12.673  17.807  1.00 23.55           C  
ATOM   3491  OG  SER C 169     -13.183  13.385  18.011  1.00 31.65           O  
ATOM   3492  N   ARG C 170     -11.400  15.494  18.794  1.00 20.86           N  
ATOM   3493  CA  ARG C 170     -11.275  16.440  19.895  1.00 18.80           C  
ATOM   3494  C   ARG C 170     -12.508  16.349  20.727  1.00 22.04           C  
ATOM   3495  O   ARG C 170     -13.551  15.901  20.239  1.00 22.51           O  
ATOM   3496  CB  ARG C 170     -11.157  17.864  19.375  1.00 18.59           C  
ATOM   3497  CG  ARG C 170      -9.910  18.112  18.604  1.00 19.88           C  
ATOM   3498  CD  ARG C 170      -9.907  19.464  18.022  1.00 18.83           C  
ATOM   3499  NE  ARG C 170      -8.671  19.721  17.310  1.00 17.55           N  
ATOM   3500  CZ  ARG C 170      -7.576  20.261  17.830  1.00 21.25           C  
ATOM   3501  NH1 ARG C 170      -7.514  20.629  19.104  1.00 22.91           N  
ATOM   3502  NH2 ARG C 170      -6.532  20.423  17.055  1.00 20.77           N  
ATOM   3503  N   THR C 171     -12.399  16.797  21.970  1.00 20.65           N  
ATOM   3504  CA  THR C 171     -13.540  16.869  22.894  1.00 22.16           C  
ATOM   3505  C   THR C 171     -13.540  18.253  23.494  1.00 22.20           C  
ATOM   3506  O   THR C 171     -12.509  18.752  23.907  1.00 20.74           O  
ATOM   3507  CB  THR C 171     -13.423  15.818  24.003  1.00 24.96           C  
ATOM   3508  OG1 THR C 171     -13.496  14.514  23.424  1.00 26.37           O  
ATOM   3509  CG2 THR C 171     -14.520  15.971  25.068  1.00 24.19           C  
ATOM   3510  N   TYR C 172     -14.705  18.887  23.534  1.00 21.09           N  
ATOM   3511  CA  TYR C 172     -14.835  20.176  24.143  1.00 21.78           C  
ATOM   3512  C   TYR C 172     -14.586  20.057  25.645  1.00 23.97           C  
ATOM   3513  O   TYR C 172     -15.131  19.171  26.301  1.00 26.05           O  
ATOM   3514  CB  TYR C 172     -16.221  20.738  23.840  1.00 24.62           C  
ATOM   3515  CG  TYR C 172     -16.506  22.057  24.489  1.00 23.94           C  
ATOM   3516  CD1 TYR C 172     -15.948  23.221  23.998  1.00 24.43           C  
ATOM   3517  CD2 TYR C 172     -17.371  22.141  25.584  1.00 27.47           C  
ATOM   3518  CE1 TYR C 172     -16.208  24.437  24.581  1.00 25.95           C  
ATOM   3519  CE2 TYR C 172     -17.645  23.366  26.165  1.00 27.68           C  
ATOM   3520  CZ  TYR C 172     -17.059  24.496  25.660  1.00 28.29           C  
ATOM   3521  OH  TYR C 172     -17.309  25.726  26.209  1.00 32.03           O  
ATOM   3522  N   ASN C 173     -13.735  20.936  26.166  1.00 22.91           N  
ATOM   3523  CA  ASN C 173     -13.464  21.034  27.587  1.00 22.26           C  
ATOM   3524  C   ASN C 173     -14.228  22.246  28.080  1.00 23.60           C  
ATOM   3525  O   ASN C 173     -13.837  23.364  27.785  1.00 24.92           O  
ATOM   3526  CB  ASN C 173     -11.965  21.177  27.838  1.00 24.47           C  
ATOM   3527  CG  ASN C 173     -11.621  21.222  29.320  1.00 24.66           C  
ATOM   3528  OD1 ASN C 173     -12.353  21.787  30.119  1.00 28.50           O  
ATOM   3529  ND2 ASN C 173     -10.488  20.630  29.681  1.00 27.75           N  
ATOM   3530  N   PRO C 174     -15.328  22.029  28.830  1.00 25.86           N  
ATOM   3531  CA  PRO C 174     -16.144  23.161  29.266  1.00 26.40           C  
ATOM   3532  C   PRO C 174     -15.452  24.102  30.272  1.00 27.45           C  
ATOM   3533  O   PRO C 174     -15.780  25.291  30.304  1.00 30.09           O  
ATOM   3534  CB  PRO C 174     -17.394  22.491  29.861  1.00 26.91           C  
ATOM   3535  CG  PRO C 174     -16.947  21.150  30.273  1.00 24.56           C  
ATOM   3536  CD  PRO C 174     -15.850  20.748  29.336  1.00 26.63           C  
ATOM   3537  N  AASP C 175     -14.501  23.581  31.042  0.70 27.55           N  
ATOM   3538  N  BASP C 175     -14.521  23.593  31.074  0.30 26.85           N  
ATOM   3539  CA AASP C 175     -13.727  24.394  31.985  0.70 28.36           C  
ATOM   3540  CA BASP C 175     -13.761  24.458  31.974  0.30 26.64           C  
ATOM   3541  C  AASP C 175     -12.853  25.405  31.256  0.70 26.81           C  
ATOM   3542  C  BASP C 175     -12.958  25.465  31.168  0.30 25.62           C  
ATOM   3543  O  AASP C 175     -12.695  26.548  31.709  0.70 26.17           O  
ATOM   3544  O  BASP C 175     -12.988  26.667  31.454  0.30 25.01           O  
ATOM   3545  CB AASP C 175     -12.839  23.515  32.879  0.70 30.07           C  
ATOM   3546  CB BASP C 175     -12.805  23.659  32.862  0.30 27.04           C  
ATOM   3547  CG AASP C 175     -13.644  22.549  33.761  0.70 36.26           C  
ATOM   3548  CG BASP C 175     -12.049  24.542  33.853  0.30 28.70           C  
ATOM   3549  OD1AASP C 175     -14.724  22.940  34.273  0.70 37.07           O  
ATOM   3550  OD1BASP C 175     -12.667  25.450  34.456  0.30 26.46           O  
ATOM   3551  OD2AASP C 175     -13.182  21.394  33.934  0.70 42.39           O  
ATOM   3552  OD2BASP C 175     -10.833  24.321  34.031  0.30 30.09           O  
ATOM   3553  N   LEU C 176     -12.274  24.974  30.136  1.00 24.26           N  
ATOM   3554  CA  LEU C 176     -11.429  25.828  29.313  1.00 23.03           C  
ATOM   3555  C   LEU C 176     -12.178  26.601  28.238  1.00 20.27           C  
ATOM   3556  O   LEU C 176     -11.760  27.690  27.860  1.00 21.97           O  
ATOM   3557  CB  LEU C 176     -10.337  24.988  28.649  1.00 23.14           C  
ATOM   3558  CG  LEU C 176      -9.371  24.266  29.586  1.00 22.76           C  
ATOM   3559  CD1 LEU C 176      -8.265  23.561  28.766  1.00 25.50           C  
ATOM   3560  CD2 LEU C 176      -8.758  25.195  30.661  1.00 20.21           C  
ATOM   3561  N   GLY C 177     -13.273  26.051  27.758  1.00 21.33           N  
ATOM   3562  CA  GLY C 177     -13.959  26.606  26.595  1.00 23.63           C  
ATOM   3563  C   GLY C 177     -13.198  26.340  25.303  1.00 23.59           C  
ATOM   3564  O   GLY C 177     -13.322  27.108  24.348  1.00 24.99           O  
ATOM   3565  N   LEU C 178     -12.442  25.235  25.278  1.00 21.76           N  
ATOM   3566  CA  LEU C 178     -11.621  24.846  24.132  1.00 19.95           C  
ATOM   3567  C   LEU C 178     -11.832  23.397  23.742  1.00 19.08           C  
ATOM   3568  O   LEU C 178     -12.128  22.563  24.570  1.00 20.28           O  
ATOM   3569  CB  LEU C 178     -10.136  25.073  24.439  1.00 21.16           C  
ATOM   3570  CG  LEU C 178      -9.706  26.494  24.821  1.00 23.56           C  
ATOM   3571  CD1 LEU C 178      -8.224  26.506  25.209  1.00 23.13           C  
ATOM   3572  CD2 LEU C 178     -10.002  27.471  23.683  1.00 21.98           C  
ATOM   3573  N   ASN C 179     -11.619  23.116  22.458  1.00 19.69           N  
ATOM   3574  CA  ASN C 179     -11.702  21.768  21.917  1.00 18.44           C  
ATOM   3575  C   ASN C 179     -10.318  21.165  21.900  1.00 19.47           C  
ATOM   3576  O   ASN C 179      -9.457  21.609  21.151  1.00 21.65           O  
ATOM   3577  CB  ASN C 179     -12.221  21.839  20.489  1.00 17.24           C  
ATOM   3578  CG  ASN C 179     -13.570  22.418  20.435  1.00 18.15           C  
ATOM   3579  OD1 ASN C 179     -14.479  21.936  21.114  1.00 19.69           O  
ATOM   3580  ND2 ASN C 179     -13.723  23.468  19.664  1.00 19.80           N  
ATOM   3581  N   ILE C 180     -10.109  20.171  22.740  1.00 19.40           N  
ATOM   3582  CA  ILE C 180      -8.800  19.635  23.022  1.00 19.98           C  
ATOM   3583  C   ILE C 180      -8.702  18.241  22.422  1.00 20.50           C  
ATOM   3584  O   ILE C 180      -9.668  17.471  22.419  1.00 19.64           O  
ATOM   3585  CB  ILE C 180      -8.574  19.578  24.575  1.00 22.07           C  
ATOM   3586  CG1 ILE C 180      -8.628  20.978  25.206  1.00 23.25           C  
ATOM   3587  CG2 ILE C 180      -7.267  18.835  24.922  1.00 22.69           C  
ATOM   3588  CD1 ILE C 180      -7.585  21.913  24.707  1.00 20.29           C  
ATOM   3589  N   TYR C 181      -7.530  17.901  21.895  1.00 19.05           N  
ATOM   3590  CA  TYR C 181      -7.324  16.567  21.377  1.00 19.36           C  
ATOM   3591  C   TYR C 181      -7.771  15.480  22.355  1.00 22.28           C  
ATOM   3592  O   TYR C 181      -7.543  15.591  23.549  1.00 21.45           O  
ATOM   3593  CB  TYR C 181      -5.857  16.340  21.086  1.00 20.93           C  
ATOM   3594  CG  TYR C 181      -5.275  16.835  19.782  1.00 18.32           C  
ATOM   3595  CD1 TYR C 181      -5.942  16.699  18.583  1.00 20.12           C  
ATOM   3596  CD2 TYR C 181      -3.956  17.257  19.739  1.00 17.75           C  
ATOM   3597  CE1 TYR C 181      -5.354  17.079  17.385  1.00 20.00           C  
ATOM   3598  CE2 TYR C 181      -3.347  17.610  18.547  1.00 18.48           C  
ATOM   3599  CZ  TYR C 181      -4.055  17.516  17.373  1.00 19.22           C  
ATOM   3600  OH  TYR C 181      -3.489  17.831  16.150  1.00 18.36           O  
ATOM   3601  N   ASP C 182      -8.396  14.435  21.826  1.00 20.52           N  
ATOM   3602  CA  ASP C 182      -8.892  13.323  22.633  1.00 21.67           C  
ATOM   3603  C   ASP C 182      -8.579  12.066  21.852  1.00 21.96           C  
ATOM   3604  O   ASP C 182      -9.337  11.639  20.973  1.00 25.40           O  
ATOM   3605  CB  ASP C 182     -10.386  13.478  22.872  1.00 21.71           C  
ATOM   3606  CG  ASP C 182     -10.934  12.434  23.830  1.00 28.10           C  
ATOM   3607  OD1 ASP C 182     -10.199  11.480  24.161  1.00 26.90           O  
ATOM   3608  OD2 ASP C 182     -12.096  12.582  24.248  1.00 28.54           O  
ATOM   3609  N   PHE C 183      -7.440  11.484  22.147  1.00 25.93           N  
ATOM   3610  CA  PHE C 183      -6.945  10.386  21.323  1.00 28.75           C  
ATOM   3611  C   PHE C 183      -7.641   9.053  21.585  1.00 32.87           C  
ATOM   3612  O   PHE C 183      -7.581   8.143  20.746  1.00 32.12           O  
ATOM   3613  CB  PHE C 183      -5.442  10.237  21.519  1.00 27.84           C  
ATOM   3614  CG  PHE C 183      -4.646  11.464  21.130  1.00 22.88           C  
ATOM   3615  CD1 PHE C 183      -4.775  12.026  19.869  1.00 24.10           C  
ATOM   3616  CD2 PHE C 183      -3.719  12.011  21.992  1.00 25.90           C  
ATOM   3617  CE1 PHE C 183      -4.027  13.132  19.511  1.00 21.95           C  
ATOM   3618  CE2 PHE C 183      -2.973  13.109  21.628  1.00 23.42           C  
ATOM   3619  CZ  PHE C 183      -3.111  13.664  20.391  1.00 22.77           C  
ATOM   3620  N   GLU C 184      -8.292   8.943  22.734  1.00 37.52           N  
ATOM   3621  CA  GLU C 184      -8.993   7.720  23.102  1.00 42.74           C  
ATOM   3622  C   GLU C 184     -10.448   7.674  22.633  1.00 44.83           C  
ATOM   3623  O   GLU C 184     -11.068   6.615  22.750  1.00 46.57           O  
ATOM   3624  CB  GLU C 184      -8.918   7.514  24.626  1.00 43.19           C  
ATOM   3625  CG  GLU C 184      -7.490   7.522  25.202  1.00 46.80           C  
ATOM   3626  CD  GLU C 184      -6.544   6.555  24.496  1.00 47.31           C  
ATOM   3627  N   ARG C 185     -11.000   8.771  22.100  1.00 45.94           N  
ATOM   3628  CA  ARG C 185     -12.387   8.728  21.598  1.00 47.30           C  
ATOM   3629  C   ARG C 185     -12.413   8.319  20.122  1.00 50.04           C  
ATOM   3630  O   ARG C 185     -11.388   8.347  19.435  1.00 50.66           O  
ATOM   3631  CB  ARG C 185     -13.143  10.044  21.846  1.00 47.73           C  
ATOM   3632  CG  ARG C 185     -12.969  11.164  20.841  1.00 46.93           C  
ATOM   3633  CD  ARG C 185     -13.901  12.328  21.185  1.00 46.49           C  
ATOM   3634  NE  ARG C 185     -15.288  12.083  20.785  1.00 46.40           N  
ATOM   3635  CZ  ARG C 185     -16.335  12.854  21.109  1.00 46.90           C  
ATOM   3636  NH1 ARG C 185     -16.208  13.933  21.886  1.00 46.36           N  
ATOM   3637  NH2 ARG C 185     -17.549  12.530  20.668  1.00 47.82           N  
ATOM   3638  OXT ARG C 185     -13.464   7.940  19.598  1.00 51.41           O  
TER    3639      ARG C 185                                                      
HETATM 3640 NI    NI A 201       7.496  35.046  -1.157  0.40 23.35          NI  
HETATM 3641  S   SO4 A 202      15.024  49.074  11.749  1.00 28.21           S  
HETATM 3642  O1  SO4 A 202      16.312  48.451  11.661  1.00 23.78           O  
HETATM 3643  O2  SO4 A 202      14.820  49.876  12.967  1.00 32.30           O  
HETATM 3644  O3  SO4 A 202      13.961  48.052  11.686  1.00 34.81           O  
HETATM 3645  O4  SO4 A 202      14.890  49.985  10.579  1.00 26.82           O  
HETATM 3646  S   SO4 A 203       7.044  11.791   5.742  1.00 68.29           S  
HETATM 3647  O1  SO4 A 203       8.033  12.122   4.720  1.00 74.70           O  
HETATM 3648  O2  SO4 A 203       7.646  10.907   6.734  1.00 75.59           O  
HETATM 3649  O3  SO4 A 203       5.905  11.118   5.125  1.00 74.93           O  
HETATM 3650  O4  SO4 A 203       6.594  13.028   6.395  1.00 75.56           O  
HETATM 3651  S   SO4 A 204      11.827  24.164 -15.566  1.00 36.57           S  
HETATM 3652  O1  SO4 A 204      11.391  25.405 -16.265  1.00 36.68           O  
HETATM 3653  O2  SO4 A 204      13.218  24.354 -15.081  1.00 40.25           O  
HETATM 3654  O3  SO4 A 204      11.819  23.032 -16.492  1.00 38.96           O  
HETATM 3655  O4  SO4 A 204      10.855  23.776 -14.543  1.00 32.33           O  
HETATM 3656  OH2 1PE A 205      15.889  38.502  -6.936  1.00 51.75           O  
HETATM 3657  C12 1PE A 205      16.191  39.307  -8.073  1.00 49.53           C  
HETATM 3658  C22 1PE A 205      14.938  39.462  -8.932  1.00 47.68           C  
HETATM 3659  OH3 1PE A 205      14.394  40.755  -8.701  1.00 44.73           O  
HETATM 3660  C13 1PE A 205      12.289  41.872  -8.796  1.00 33.70           C  
HETATM 3661  C23 1PE A 205      13.398  41.222  -9.599  1.00 37.03           C  
HETATM 3662  OH4 1PE A 205      11.352  40.870  -8.505  1.00 28.34           O  
HETATM 3663  C14 1PE A 205       9.857  40.489  -6.563  1.00 25.80           C  
HETATM 3664  C24 1PE A 205      10.081  41.202  -7.897  1.00 23.49           C  
HETATM 3665  OH5 1PE A 205       9.253  39.199  -6.504  1.00 38.13           O  
HETATM 3666  C15 1PE A 205      11.088  37.739  -5.767  1.00 34.96           C  
HETATM 3667  C25 1PE A 205       9.688  38.276  -5.483  1.00 31.48           C  
HETATM 3668  OH6 1PE A 205      11.177  36.467  -6.397  1.00 43.91           O  
HETATM 3669  C16 1PE A 205      13.470  35.733  -5.576  1.00 52.58           C  
HETATM 3670  C26 1PE A 205      11.971  35.481  -5.721  1.00 47.34           C  
HETATM 3671  OH7 1PE A 205      14.002  34.939  -4.492  1.00 59.20           O  
HETATM 3672  OH5 1PE A 206      33.227  27.860  13.379  1.00 49.12           O  
HETATM 3673  C15 1PE A 206      34.449  29.935  12.791  1.00 46.39           C  
HETATM 3674  C25 1PE A 206      33.114  29.241  13.020  1.00 38.56           C  
HETATM 3675  OH6 1PE A 206      34.246  31.351  12.709  1.00 33.55           O  
HETATM 3676  C16 1PE A 206      34.741  31.681  15.183  1.00 48.40           C  
HETATM 3677  C26 1PE A 206      33.998  32.108  13.921  1.00 41.97           C  
HETATM 3678  OH7 1PE A 206      34.379  32.616  16.211  1.00 53.08           O  
HETATM 3679 FE    FE B 207      19.215  28.148  18.996  0.40 15.35          FE  
HETATM 3680 NI    NI B 208      -6.541  23.789  34.699  0.40 34.35          NI  
HETATM 3681  S   SO4 B 209       8.122  44.290  27.371  1.00 63.56           S  
HETATM 3682  O1  SO4 B 209       8.459  44.136  25.953  1.00 67.14           O  
HETATM 3683  O2  SO4 B 209       8.120  43.011  28.063  1.00 66.58           O  
HETATM 3684  O3  SO4 B 209       6.805  44.904  27.512  1.00 67.57           O  
HETATM 3685  O4  SO4 B 209       9.149  45.125  27.989  1.00 71.43           O  
HETATM 3686  S   SO4 B 210      28.257  10.630  21.362  1.00 53.00           S  
HETATM 3687  O1  SO4 B 210      28.115  12.029  21.780  1.00 44.16           O  
HETATM 3688  O2  SO4 B 210      28.548   9.732  22.491  1.00 56.70           O  
HETATM 3689  O3  SO4 B 210      29.339  10.448  20.400  1.00 51.33           O  
HETATM 3690  O4  SO4 B 210      26.971  10.293  20.747  1.00 54.82           O  
HETATM 3691  S   SO4 B 211       5.729   3.417  20.475  1.00 86.58           S  
HETATM 3692  O1  SO4 B 211       6.456   3.922  19.315  1.00 86.69           O  
HETATM 3693  O2  SO4 B 211       6.662   3.260  21.593  1.00 89.96           O  
HETATM 3694  O3  SO4 B 211       5.160   2.123  20.112  1.00 90.10           O  
HETATM 3695  O4  SO4 B 211       4.639   4.314  20.864  1.00 83.99           O  
HETATM 3696  OH5 1PE B 212       4.164  47.011  25.496  1.00 58.09           O  
HETATM 3697  C15 1PE B 212       3.491  45.187  24.086  1.00 49.82           C  
HETATM 3698  C25 1PE B 212       4.669  45.938  24.691  1.00 52.31           C  
HETATM 3699  OH6 1PE B 212       2.759  44.590  25.150  1.00 46.99           O  
HETATM 3700  C16 1PE B 212       0.964  43.171  25.870  1.00 45.05           C  
HETATM 3701  C26 1PE B 212       1.731  43.725  24.688  1.00 46.43           C  
HETATM 3702  OH7 1PE B 212       1.873  42.815  26.908  1.00 49.36           O  
HETATM 3703  S   SO4 C 213     -16.134  12.070  16.961  1.00 76.96           S  
HETATM 3704  O1  SO4 C 213     -16.426  13.449  17.324  1.00 69.94           O  
HETATM 3705  O2  SO4 C 213     -16.068  11.236  18.153  1.00 77.20           O  
HETATM 3706  O3  SO4 C 213     -14.848  12.046  16.260  1.00 78.49           O  
HETATM 3707  O4  SO4 C 213     -17.183  11.502  16.111  1.00 79.14           O  
HETATM 3708  S   SO4 C 214      -2.092  48.272  14.653  1.00 34.86           S  
HETATM 3709  O1  SO4 C 214      -2.688  48.053  13.454  1.00 16.42           O  
HETATM 3710  O2  SO4 C 214      -1.249  47.090  15.019  1.00 36.87           O  
HETATM 3711  O3  SO4 C 214      -3.242  48.457  15.564  1.00 35.80           O  
HETATM 3712  O4  SO4 C 214      -1.256  49.481  14.653  1.00 38.75           O  
HETATM 3713  OH2 1PE C 215     -13.101  29.714  14.884  1.00 56.99           O  
HETATM 3714  C12 1PE C 215     -14.368  29.593  15.550  1.00 55.22           C  
HETATM 3715  C22 1PE C 215     -15.346  30.752  15.322  1.00 49.33           C  
HETATM 3716  OH3 1PE C 215     -16.322  30.605  16.365  1.00 51.27           O  
HETATM 3717  C13 1PE C 215     -17.130  31.289  18.549  1.00 41.86           C  
HETATM 3718  C23 1PE C 215     -16.787  31.721  17.126  1.00 44.23           C  
HETATM 3719  OH4 1PE C 215     -16.341  31.993  19.517  1.00 36.86           O  
HETATM 3720  C14 1PE C 215     -14.575  31.831  21.151  1.00 28.37           C  
HETATM 3721  C24 1PE C 215     -15.388  31.136  20.109  1.00 22.22           C  
HETATM 3722  OH5 1PE C 215     -13.871  30.761  21.729  1.00 38.71           O  
HETATM 3723  C15 1PE C 215     -11.722  30.783  20.728  1.00 39.07           C  
HETATM 3724  C25 1PE C 215     -12.508  30.955  22.000  1.00 41.86           C  
HETATM 3725  OH6 1PE C 215     -11.165  29.491  20.553  1.00 45.99           O  
HETATM 3726  C16 1PE C 215     -11.863  28.876  18.301  1.00 42.55           C  
HETATM 3727  C26 1PE C 215     -10.733  29.346  19.198  1.00 37.48           C  
HETATM 3728  OH7 1PE C 215     -11.583  27.539  17.869  1.00 49.59           O  
HETATM 3729  OH5 1PE C 216      -6.528  11.728  -3.149  1.00 61.25           O  
HETATM 3730  C15 1PE C 216      -7.399  12.297  -5.254  1.00 62.60           C  
HETATM 3731  C25 1PE C 216      -6.799  11.181  -4.430  1.00 61.78           C  
HETATM 3732  OH6 1PE C 216      -6.352  13.216  -5.602  1.00 61.99           O  
HETATM 3733  C16 1PE C 216      -4.859  13.959  -7.406  1.00 66.52           C  
HETATM 3734  C26 1PE C 216      -6.032  13.083  -6.995  1.00 65.94           C  
HETATM 3735  OH7 1PE C 216      -4.014  13.261  -8.326  1.00 69.81           O  
HETATM 3736  O   HOH A 217       7.392  41.432   5.414  1.00 13.82           O  
HETATM 3737  O   HOH A 218      10.077  26.709  -4.841  1.00 15.96           O  
HETATM 3738  O   HOH A 219      19.493  42.181  16.994  1.00 16.25           O  
HETATM 3739  O   HOH A 220      20.345  46.165  11.285  1.00 17.16           O  
HETATM 3740  O   HOH A 221       9.004  31.860   8.901  1.00 17.20           O  
HETATM 3741  O   HOH A 222       8.517  40.284   3.136  1.00 17.24           O  
HETATM 3742  O   HOH A 223       4.391  23.977  -1.194  1.00 17.52           O  
HETATM 3743  O   HOH A 224      16.203  21.868  12.201  1.00 17.61           O  
HETATM 3744  O   HOH A 225      13.099  33.013  -1.210  1.00 17.66           O  
HETATM 3745  O   HOH A 226      21.502  43.688  18.072  1.00 27.34           O  
HETATM 3746  O   HOH A 227      24.557  22.535  14.356  1.00 17.94           O  
HETATM 3747  O   HOH A 228      13.712  15.264  -6.537  1.00 27.45           O  
HETATM 3748  O   HOH A 229       6.515  22.077  -0.684  1.00 18.61           O  
HETATM 3749  O   HOH A 230      12.016  45.325  15.927  1.00 18.80           O  
HETATM 3750  O   HOH A 231       8.322  48.085   2.516  1.00 18.84           O  
HETATM 3751  O   HOH A 232      25.065  24.158  12.094  1.00 18.99           O  
HETATM 3752  O   HOH A 233      23.975  28.301  -4.976  1.00 27.81           O  
HETATM 3753  O   HOH A 234       6.766  18.902   2.923  1.00 28.08           O  
HETATM 3754  O   HOH A 235       7.304  22.368  -3.481  1.00 20.01           O  
HETATM 3755  O   HOH A 236      31.259  25.897  10.128  1.00 28.29           O  
HETATM 3756  O   HOH A 237       7.892  47.622  -1.584  1.00 20.02           O  
HETATM 3757  O   HOH A 238       5.616  32.501  -5.536  1.00 20.45           O  
HETATM 3758  O   HOH A 239      27.590  24.828  11.351  1.00 20.50           O  
HETATM 3759  O   HOH A 240       4.954  21.094 -13.161  1.00 28.60           O  
HETATM 3760  O   HOH A 241      10.421  43.174  22.279  1.00 20.99           O  
HETATM 3761  O   HOH A 242       8.693  43.486  15.538  1.00 21.16           O  
HETATM 3762  O   HOH A 243      -0.686  27.602  -9.108  1.00 21.26           O  
HETATM 3763  O   HOH A 244      19.004  45.645   1.028  1.00 22.06           O  
HETATM 3764  O   HOH A 245      28.685  26.706  13.116  1.00 22.24           O  
HETATM 3765  O   HOH A 246      12.004  19.181 -12.902  1.00 28.96           O  
HETATM 3766  O   HOH A 247       7.596  41.541 -10.445  1.00 22.47           O  
HETATM 3767  O   HOH A 248      11.451  20.146   5.402  1.00 22.56           O  
HETATM 3768  O   HOH A 249       0.279  40.019  -6.270  1.00 22.59           O  
HETATM 3769  O   HOH A 250       1.700  47.684   0.432  1.00 29.26           O  
HETATM 3770  O   HOH A 251       6.232  49.565   1.676  1.00 29.34           O  
HETATM 3771  O   HOH A 252      20.934  34.751  -1.613  1.00 22.80           O  
HETATM 3772  O   HOH A 253      17.227  45.453  -4.843  1.00 23.38           O  
HETATM 3773  O   HOH A 254       9.714  40.915 -12.120  1.00 29.39           O  
HETATM 3774  O   HOH A 255      22.495  34.344  18.289  1.00 23.46           O  
HETATM 3775  O   HOH A 256       7.272  23.414   1.825  1.00 29.43           O  
HETATM 3776  O   HOH A 257      27.250  51.160   6.697  1.00 29.44           O  
HETATM 3777  O   HOH A 258      28.526  32.449   1.539  1.00 23.76           O  
HETATM 3778  O   HOH A 259      21.811  39.233   3.703  1.00 24.16           O  
HETATM 3779  O   HOH A 260       5.327  34.951  -4.713  1.00 24.23           O  
HETATM 3780  O   HOH A 261      23.227  24.412  17.827  1.00 29.64           O  
HETATM 3781  O   HOH A 262      -0.913  24.392 -12.294  1.00 24.53           O  
HETATM 3782  O   HOH A 263      25.446  44.412   3.563  1.00 24.53           O  
HETATM 3783  O   HOH A 264       1.554  31.695 -13.534  1.00 29.68           O  
HETATM 3784  O   HOH A 265       1.714  25.943 -18.138  1.00 29.80           O  
HETATM 3785  O   HOH A 266      28.960  35.421  10.053  1.00 29.84           O  
HETATM 3786  O   HOH A 267       7.836  35.437  -7.532  1.00 24.55           O  
HETATM 3787  O   HOH A 268      25.875  41.261  12.771  1.00 24.59           O  
HETATM 3788  O   HOH A 269      20.498  28.990  16.808  1.00 24.75           O  
HETATM 3789  O   HOH A 270      14.727  21.902  -8.580  1.00 24.79           O  
HETATM 3790  O   HOH A 271       9.672  27.465 -15.504  1.00 24.82           O  
HETATM 3791  O   HOH A 272      23.322  29.300  16.784  1.00 25.00           O  
HETATM 3792  O   HOH A 273      26.476  39.517  14.659  1.00 25.03           O  
HETATM 3793  O   HOH A 274      23.889  42.686  16.967  1.00 25.15           O  
HETATM 3794  O   HOH A 275      29.803  32.740  14.923  1.00 25.33           O  
HETATM 3795  O   HOH A 276      26.075  42.204   9.151  1.00 25.36           O  
HETATM 3796  O   HOH A 277      24.697  34.723  -1.637  1.00 26.03           O  
HETATM 3797  O   HOH A 278      25.689  22.270  -5.992  1.00 30.73           O  
HETATM 3798  O   HOH A 279      17.910  13.656  -3.537  1.00 30.76           O  
HETATM 3799  O   HOH A 280      29.336  22.898  10.953  1.00 26.15           O  
HETATM 3800  O   HOH A 281      10.831  20.318 -10.609  1.00 26.39           O  
HETATM 3801  O   HOH A 282      28.555  22.279   8.225  1.00 26.40           O  
HETATM 3802  O   HOH A 283       8.633  37.568  -9.307  1.00 26.53           O  
HETATM 3803  O   HOH A 284       0.816  41.902  -8.161  1.00 26.60           O  
HETATM 3804  O   HOH A 285      19.174  40.211  24.566  1.00 31.08           O  
HETATM 3805  O   HOH A 286      16.585  12.071   0.934  1.00 31.24           O  
HETATM 3806  O   HOH A 287      11.620  32.979  -4.171  1.00 26.78           O  
HETATM 3807  O   HOH A 288       8.622  33.004  -5.347  1.00 26.81           O  
HETATM 3808  O   HOH A 289      23.403  31.281  18.432  1.00 31.43           O  
HETATM 3809  O   HOH A 290       8.330  25.432   9.482  1.00 31.47           O  
HETATM 3810  O   HOH A 291      20.165  45.577  -1.386  1.00 26.87           O  
HETATM 3811  O   HOH A 292      12.943  43.023  25.231  1.00 31.52           O  
HETATM 3812  O   HOH A 293       7.022  21.624   9.219  1.00 31.75           O  
HETATM 3813  O   HOH A 294      14.720  49.224  15.456  1.00 32.09           O  
HETATM 3814  O   HOH A 295      20.244  33.035  21.262  1.00 32.33           O  
HETATM 3815  O   HOH A 296      21.139  30.855  22.764  1.00 32.33           O  
HETATM 3816  O   HOH A 297      17.810  35.639  -3.204  1.00 32.82           O  
HETATM 3817  O   HOH A 298      11.617  46.606  18.964  1.00 33.01           O  
HETATM 3818  O   HOH A 299       7.035  45.575 -13.079  1.00 33.12           O  
HETATM 3819  O   HOH A 300      14.348  20.261 -13.082  1.00 33.19           O  
HETATM 3820  O   HOH A 301      15.994  11.683  -1.648  1.00 33.20           O  
HETATM 3821  O   HOH A 302      25.995  46.533  11.930  1.00 33.24           O  
HETATM 3822  O   HOH A 303      27.009  47.304   9.710  1.00 33.33           O  
HETATM 3823  O   HOH A 304      12.361  47.138   9.683  1.00 33.58           O  
HETATM 3824  O   HOH A 305      15.049  12.104  -5.607  1.00 33.58           O  
HETATM 3825  O   HOH A 306      23.211  27.012  18.308  1.00 33.70           O  
HETATM 3826  O   HOH A 307      18.241  45.941  16.788  1.00 33.93           O  
HETATM 3827  O   HOH A 308      15.797  21.193 -10.830  1.00 34.62           O  
HETATM 3828  O   HOH A 309       6.726  38.177  -3.155  1.00 34.65           O  
HETATM 3829  O   HOH A 310      17.496  44.786  19.070  1.00 34.68           O  
HETATM 3830  O   HOH A 311      13.862  51.712   7.035  1.00 34.70           O  
HETATM 3831  O   HOH A 312      18.805  42.628  -2.775  1.00 34.75           O  
HETATM 3832  O   HOH A 313       0.179  47.693  -1.959  1.00 35.01           O  
HETATM 3833  O   HOH A 314      30.145  37.453  15.809  1.00 35.09           O  
HETATM 3834  O   HOH A 315      25.614  32.459  17.411  1.00 35.42           O  
HETATM 3835  O   HOH A 316      10.133  49.823   3.712  1.00 35.56           O  
HETATM 3836  O   HOH A 317      24.154  10.614   4.711  1.00 35.64           O  
HETATM 3837  O   HOH A 318      16.163  47.436  16.862  1.00 35.67           O  
HETATM 3838  O   HOH A 319      19.966  24.414 -10.403  1.00 35.76           O  
HETATM 3839  O   HOH A 320       5.989  43.280 -12.372  1.00 35.80           O  
HETATM 3840  O   HOH A 321       0.752  29.178 -12.944  1.00 35.93           O  
HETATM 3841  O   HOH A 322      27.611  45.483   4.759  1.00 36.04           O  
HETATM 3842  O   HOH A 323      28.368  15.914   4.893  1.00 36.32           O  
HETATM 3843  O   HOH A 324       4.084  19.033 -11.544  1.00 36.58           O  
HETATM 3844  O   HOH A 325      23.516  26.500  -6.808  1.00 36.59           O  
HETATM 3845  O   HOH A 326      24.760  45.048  15.253  1.00 36.89           O  
HETATM 3846  O   HOH A 327       9.974  30.033 -16.596  1.00 37.14           O  
HETATM 3847  O   HOH A 328      16.288  29.516  -6.228  1.00 37.17           O  
HETATM 3848  O   HOH A 329      11.783  11.231  -2.111  1.00 37.21           O  
HETATM 3849  O   HOH A 330      12.151  16.717 -14.060  1.00 37.21           O  
HETATM 3850  O   HOH A 331      26.549  43.692  13.366  1.00 37.43           O  
HETATM 3851  O   HOH A 332      16.828  44.629  -7.531  1.00 37.69           O  
HETATM 3852  O   HOH A 333      14.584  13.315  -8.028  1.00 37.85           O  
HETATM 3853  O   HOH A 334       5.894  47.903 -13.396  1.00 38.15           O  
HETATM 3854  O   HOH A 335       9.534  24.560 -18.121  1.00 38.21           O  
HETATM 3855  O   HOH A 336      28.779  49.496   4.650  1.00 38.23           O  
HETATM 3856  O   HOH A 337       9.557  50.104   6.231  1.00 38.32           O  
HETATM 3857  O   HOH A 338      28.033  49.721   9.211  1.00 38.33           O  
HETATM 3858  O   HOH A 339       9.126  13.053   0.143  1.00 38.42           O  
HETATM 3859  O   HOH A 340      20.734  46.784  16.396  1.00 38.52           O  
HETATM 3860  O   HOH A 341      -0.191  29.860 -16.927  1.00 38.70           O  
HETATM 3861  O   HOH A 342      17.070  30.941  -4.208  1.00 39.36           O  
HETATM 3862  O   HOH A 343      22.158  42.548   0.843  1.00 39.57           O  
HETATM 3863  O   HOH A 344      17.581  19.704  -9.119  1.00 39.69           O  
HETATM 3864  O   HOH A 345       3.692  50.729 -11.691  1.00 40.20           O  
HETATM 3865  O   HOH A 346      15.197  28.738 -10.823  1.00 40.43           O  
HETATM 3866  O   HOH A 347      25.999  24.928  -6.857  1.00 41.45           O  
HETATM 3867  O   HOH A 348      12.710  10.523   6.547  1.00 41.66           O  
HETATM 3868  O   HOH A 349      -2.751  22.310 -12.551  1.00 41.78           O  
HETATM 3869  O   HOH A 350      19.802  40.098  -2.023  1.00 42.21           O  
HETATM 3870  O   HOH A 351       0.587  32.907 -15.957  1.00 42.65           O  
HETATM 3871  O   HOH A 352      31.301  25.958  12.968  1.00 42.81           O  
HETATM 3872  O   HOH A 353       0.723  51.480  -3.013  1.00 43.03           O  
HETATM 3873  O   HOH A 354      18.445  33.131  -4.844  1.00 43.22           O  
HETATM 3874  O   HOH A 355      21.694  40.415  23.963  1.00 43.27           O  
HETATM 3875  O   HOH A 356      27.323  34.734  -0.700  1.00 43.43           O  
HETATM 3876  O   HOH A 357      26.767  48.218  13.952  1.00 43.62           O  
HETATM 3877  O   HOH A 358      32.820  28.587   7.769  1.00 43.83           O  
HETATM 3878  O   HOH A 359      19.000  28.094  -8.652  1.00 43.89           O  
HETATM 3879  O   HOH A 360       8.281  13.997 -11.757  1.00 44.16           O  
HETATM 3880  O   HOH A 361      28.656  18.110   2.244  1.00 44.40           O  
HETATM 3881  O   HOH A 362      14.118  46.498  17.909  1.00 44.46           O  
HETATM 3882  O   HOH A 363      31.108  28.339   3.515  1.00 44.61           O  
HETATM 3883  O   HOH A 364       6.764  23.430   7.258  1.00 44.77           O  
HETATM 3884  O   HOH A 365      26.035  20.543  -8.035  1.00 44.78           O  
HETATM 3885  O   HOH A 366      -0.929  32.717 -12.124  1.00 44.82           O  
HETATM 3886  O   HOH A 367      14.087   9.820  -1.273  1.00 44.86           O  
HETATM 3887  O   HOH A 368      21.284  40.216  -0.305  1.00 44.96           O  
HETATM 3888  O   HOH A 369      28.854  18.370  -0.501  1.00 45.02           O  
HETATM 3889  O   HOH A 370      23.072  41.618  22.211  1.00 45.27           O  
HETATM 3890  O   HOH A 371      22.498  30.520  -5.924  1.00 45.67           O  
HETATM 3891  O   HOH A 372      18.500  44.703  22.915  1.00 46.50           O  
HETATM 3892  O   HOH A 373      14.866  31.364  -5.930  1.00 46.86           O  
HETATM 3893  O   HOH A 374       3.203  47.529 -13.798  1.00 47.30           O  
HETATM 3894  O   HOH A 375      25.053  38.308   1.572  1.00 47.35           O  
HETATM 3895  O   HOH A 376      23.754  37.560  -0.804  1.00 47.37           O  
HETATM 3896  O   HOH A 377      33.187  27.436   5.211  1.00 47.45           O  
HETATM 3897  O   HOH A 378      12.471  45.852  25.035  1.00 47.52           O  
HETATM 3898  O   HOH A 379       1.149  17.795 -11.623  1.00 47.63           O  
HETATM 3899  O   HOH A 380      14.770  47.579  21.523  1.00 47.65           O  
HETATM 3900  O   HOH A 381      26.262  14.301  -4.084  1.00 48.05           O  
HETATM 3901  O   HOH A 382      22.150  44.088  20.828  1.00 48.11           O  
HETATM 3902  O   HOH A 383      17.485  46.909  20.853  1.00 48.24           O  
HETATM 3903  O   HOH A 384      29.510  21.905   0.511  1.00 48.78           O  
HETATM 3904  O   HOH A 385       3.612  42.935 -13.428  1.00 48.83           O  
HETATM 3905  O   HOH A 386      20.572  19.579  -9.956  1.00 49.20           O  
HETATM 3906  O   HOH A 387      27.783  41.106   3.218  1.00 49.37           O  
HETATM 3907  O   HOH A 388      20.994  32.669  -3.850  1.00 49.71           O  
HETATM 3908  O   HOH A 389      27.275  36.961   1.382  1.00 49.74           O  
HETATM 3909  O   HOH A 390      32.808  31.692   4.493  1.00 49.94           O  
HETATM 3910  O   HOH A 391      28.558  15.425  -0.900  1.00 50.03           O  
HETATM 3911  O   HOH A 392      17.848  39.572  27.272  1.00 50.23           O  
HETATM 3912  O   HOH A 393      15.524  32.224  -7.994  1.00 51.10           O  
HETATM 3913  O   HOH A 394      29.853  49.572   6.919  1.00 51.19           O  
HETATM 3914  O   HOH A 395      17.653   9.934  -2.947  1.00 51.77           O  
HETATM 3915  O   HOH A 396      27.505  21.915  -3.701  1.00 52.02           O  
HETATM 3916  O   HOH A 397      21.087  25.957  -8.594  1.00 52.03           O  
HETATM 3917  O   HOH A 398      11.495  48.611  12.702  1.00 52.13           O  
HETATM 3918  O   HOH A 399      27.832  40.093  16.780  1.00 52.47           O  
HETATM 3919  O   HOH A 400      11.570   8.599   4.457  1.00 52.54           O  
HETATM 3920  O   HOH A 401      19.413  38.068  -3.743  1.00 52.69           O  
HETATM 3921  O   HOH A 402      24.060  10.227   1.921  1.00 53.12           O  
HETATM 3922  O   HOH A 403      25.800  10.304   9.582  1.00 53.78           O  
HETATM 3923  O   HOH A 404      21.695  37.090  -2.828  1.00 54.08           O  
HETATM 3924  O   HOH A 405      33.907  28.248  10.122  1.00 54.11           O  
HETATM 3925  O   HOH A 406      10.966  45.714  22.501  1.00 54.77           O  
HETATM 3926  O   HOH A 407       0.678  41.344 -18.438  1.00 57.78           O  
HETATM 3927  O   HOH A 408      27.206  24.686  -9.604  1.00 58.40           O  
HETATM 3928  O   HOH A 409      16.239  18.111 -14.073  1.00 58.90           O  
HETATM 3929  O  AHOH A 410       7.356  35.940  -2.610  0.70 25.82           O  
HETATM 3930  O  BHOH A 410       6.824  36.749  -1.155  0.30 21.59           O  
HETATM 3931  O   HOH B 411       0.228  39.215  25.878  1.00 15.33           O  
HETATM 3932  O   HOH B 412      15.587  36.706  19.774  1.00 15.94           O  
HETATM 3933  O   HOH B 413      -3.460  20.156  24.052  1.00 16.47           O  
HETATM 3934  O   HOH B 414      18.705  18.669  18.695  1.00 17.09           O  
HETATM 3935  O   HOH B 415       0.176  20.702  15.754  1.00 17.17           O  
HETATM 3936  O   HOH B 416       5.819  43.493  21.494  1.00 17.42           O  
HETATM 3937  O   HOH B 417      20.878  10.528  18.476  1.00 18.55           O  
HETATM 3938  O   HOH B 418      19.383   9.204  22.658  1.00 27.29           O  
HETATM 3939  O   HOH B 419       9.703   4.681  28.860  1.00 27.32           O  
HETATM 3940  O   HOH B 420       8.312  43.589  20.501  1.00 18.88           O  
HETATM 3941  O   HOH B 421      -6.108  33.105  20.983  1.00 19.12           O  
HETATM 3942  O   HOH B 422      -5.042  27.009  23.190  1.00 19.27           O  
HETATM 3943  O   HOH B 423      -7.291  23.356  20.641  1.00 27.50           O  
HETATM 3944  O   HOH B 424       5.025  33.585  35.483  1.00 27.51           O  
HETATM 3945  O   HOH B 425       6.417   7.205  15.581  1.00 27.63           O  
HETATM 3946  O   HOH B 426      30.036  32.267  19.235  1.00 27.64           O  
HETATM 3947  O   HOH B 427      -5.517  19.878  22.161  1.00 19.37           O  
HETATM 3948  O   HOH B 428      -3.961  19.723  26.720  1.00 19.45           O  
HETATM 3949  O   HOH B 429       8.704   5.807  15.965  1.00 28.23           O  
HETATM 3950  O   HOH B 430      17.623  16.347  14.139  1.00 19.62           O  
HETATM 3951  O   HOH B 431      21.653   8.577  21.168  1.00 28.40           O  
HETATM 3952  O   HOH B 432      12.790  24.128  30.460  1.00 28.44           O  
HETATM 3953  O   HOH B 433      -4.937  17.271  27.242  1.00 28.50           O  
HETATM 3954  O   HOH B 434      17.670  19.525  11.802  1.00 19.77           O  
HETATM 3955  O   HOH B 435       7.265  42.585  18.214  1.00 19.81           O  
HETATM 3956  O   HOH B 436       9.938   6.156  19.192  1.00 28.71           O  
HETATM 3957  O   HOH B 437      -2.036  34.017  31.257  1.00 28.75           O  
HETATM 3958  O   HOH B 438      28.430  31.769  17.118  1.00 28.77           O  
HETATM 3959  O   HOH B 439      -6.823  20.537  29.628  1.00 28.92           O  
HETATM 3960  O   HOH B 440      21.264   5.419  23.811  1.00 20.29           O  
HETATM 3961  O   HOH B 441      18.076  11.413  21.624  1.00 20.40           O  
HETATM 3962  O   HOH B 442      -6.349  41.178  22.563  1.00 20.60           O  
HETATM 3963  O   HOH B 443      15.637  17.597  12.429  1.00 20.92           O  
HETATM 3964  O   HOH B 444      -5.871  27.364  30.766  1.00 21.07           O  
HETATM 3965  O   HOH B 445       9.363  29.536  15.535  1.00 21.37           O  
HETATM 3966  O   HOH B 446      12.386   4.597  16.314  1.00 29.36           O  
HETATM 3967  O   HOH B 447      19.221  24.011  22.843  1.00 29.36           O  
HETATM 3968  O   HOH B 448      16.044  24.965  22.876  1.00 21.46           O  
HETATM 3969  O   HOH B 449       7.620  17.503  13.419  1.00 21.77           O  
HETATM 3970  O   HOH B 450      -5.933  29.562  23.443  1.00 21.84           O  
HETATM 3971  O   HOH B 451      -4.649  32.490  24.476  1.00 21.88           O  
HETATM 3972  O   HOH B 452       6.028  21.005  33.831  1.00 29.48           O  
HETATM 3973  O   HOH B 453      12.181  16.403  31.121  1.00 29.51           O  
HETATM 3974  O   HOH B 454      14.763   7.155  17.380  1.00 21.95           O  
HETATM 3975  O   HOH B 455       5.607  40.029  30.224  1.00 21.96           O  
HETATM 3976  O   HOH B 456       8.898  46.006  19.380  1.00 21.99           O  
HETATM 3977  O   HOH B 457       3.469  45.062  16.265  1.00 22.12           O  
HETATM 3978  O   HOH B 458      -3.734  27.714  20.805  1.00 22.27           O  
HETATM 3979  O   HOH B 459       7.190  45.644  17.321  1.00 22.30           O  
HETATM 3980  O   HOH B 460      -5.366  21.736  27.731  1.00 22.36           O  
HETATM 3981  O   HOH B 461      -8.245  31.795  20.127  1.00 22.88           O  
HETATM 3982  O   HOH B 462       4.781  46.427  18.204  1.00 23.44           O  
HETATM 3983  O   HOH B 463      15.705  21.168  25.998  1.00 30.21           O  
HETATM 3984  O   HOH B 464      14.710  34.813  32.315  1.00 30.32           O  
HETATM 3985  O   HOH B 465      -0.225  30.431  32.900  1.00 30.33           O  
HETATM 3986  O   HOH B 466      17.475  18.909  25.626  1.00 23.58           O  
HETATM 3987  O   HOH B 467       7.740  31.614  37.125  1.00 23.70           O  
HETATM 3988  O   HOH B 468      28.449  20.833  25.411  1.00 30.64           O  
HETATM 3989  O   HOH B 469      -2.052  38.451  29.516  1.00 30.65           O  
HETATM 3990  O   HOH B 470      -4.776  44.450  21.227  1.00 30.66           O  
HETATM 3991  O   HOH B 471      18.768  14.777  28.074  1.00 23.70           O  
HETATM 3992  O   HOH B 472      -5.935  29.421  26.245  1.00 23.87           O  
HETATM 3993  O   HOH B 473      24.797  10.430  21.458  1.00 24.26           O  
HETATM 3994  O   HOH B 474      11.403  16.367   9.968  1.00 24.32           O  
HETATM 3995  O   HOH B 475      31.317  17.595  22.544  1.00 30.91           O  
HETATM 3996  O   HOH B 476      -4.466  18.998  30.606  1.00 24.49           O  
HETATM 3997  O   HOH B 477      22.812   7.522  12.228  1.00 30.95           O  
HETATM 3998  O   HOH B 478       9.219  30.282  31.191  1.00 24.53           O  
HETATM 3999  O   HOH B 479      -2.668  15.888  27.351  1.00 25.30           O  
HETATM 4000  O   HOH B 480      -5.170  15.962  24.804  1.00 25.33           O  
HETATM 4001  O   HOH B 481      19.507   7.135  25.076  1.00 25.33           O  
HETATM 4002  O   HOH B 482      11.149   6.420  12.203  1.00 31.31           O  
HETATM 4003  O   HOH B 483      27.751  20.504  11.349  1.00 25.34           O  
HETATM 4004  O   HOH B 484      -1.214  40.558  27.885  1.00 25.74           O  
HETATM 4005  O   HOH B 485      24.612  24.986  21.645  1.00 25.85           O  
HETATM 4006  O   HOH B 486      13.290  38.472  32.586  1.00 26.02           O  
HETATM 4007  O   HOH B 487      -1.000  27.664  32.941  1.00 26.04           O  
HETATM 4008  O   HOH B 488      16.681  34.335  20.917  1.00 26.43           O  
HETATM 4009  O   HOH B 489       0.927  44.881  17.079  1.00 26.50           O  
HETATM 4010  O   HOH B 490      -1.292   8.928  25.607  1.00 31.92           O  
HETATM 4011  O   HOH B 491      10.762  23.289  33.436  1.00 26.68           O  
HETATM 4012  O   HOH B 492      26.232  11.879  14.444  1.00 26.82           O  
HETATM 4013  O   HOH B 493      -7.029  25.777  21.717  1.00 26.85           O  
HETATM 4014  O   HOH B 494      28.308  14.414  21.910  1.00 26.88           O  
HETATM 4015  O   HOH B 495      -5.770  40.378  27.353  1.00 32.18           O  
HETATM 4016  O   HOH B 496      -5.273  32.168  32.872  1.00 27.14           O  
HETATM 4017  O   HOH B 497       4.172  45.780  20.909  1.00 27.23           O  
HETATM 4018  O   HOH B 498      21.830  24.084  20.511  1.00 32.48           O  
HETATM 4019  O   HOH B 499       1.853  30.683  33.835  1.00 32.77           O  
HETATM 4020  O   HOH B 500      -6.906  22.409  32.215  1.00 33.34           O  
HETATM 4021  O   HOH B 501      24.687  10.717  12.518  1.00 33.51           O  
HETATM 4022  O   HOH B 502      31.477  21.046  16.518  1.00 34.07           O  
HETATM 4023  O   HOH B 503       2.236  21.046  13.976  1.00 34.25           O  
HETATM 4024  O   HOH B 504      14.865   4.504  17.819  1.00 34.43           O  
HETATM 4025  O   HOH B 505      -4.660  38.042  28.406  1.00 34.45           O  
HETATM 4026  O   HOH B 506      -0.844   5.550  19.608  1.00 34.74           O  
HETATM 4027  O   HOH B 507      10.459  10.482  30.371  1.00 34.99           O  
HETATM 4028  O   HOH B 508      11.063   9.771   9.923  1.00 35.14           O  
HETATM 4029  O   HOH B 509      28.558  29.073  25.374  1.00 35.20           O  
HETATM 4030  O   HOH B 510      13.568  19.818  12.660  1.00 35.43           O  
HETATM 4031  O   HOH B 511      24.844   7.500  21.076  1.00 35.55           O  
HETATM 4032  O   HOH B 512       0.725  39.613  32.848  1.00 35.79           O  
HETATM 4033  O   HOH B 513       7.385  24.666  12.153  1.00 36.10           O  
HETATM 4034  O   HOH B 514       9.124   5.049  13.365  1.00 36.54           O  
HETATM 4035  O   HOH B 515      -2.725  44.362  24.429  1.00 36.83           O  
HETATM 4036  O   HOH B 516      -3.477  42.031  27.597  1.00 36.94           O  
HETATM 4037  O   HOH B 517      11.056  20.569  10.959  1.00 37.05           O  
HETATM 4038  O   HOH B 518       1.100   9.658  27.917  1.00 37.22           O  
HETATM 4039  O   HOH B 519      20.043  29.797  19.324  1.00 37.49           O  
HETATM 4040  O   HOH B 520      16.434  16.062  28.540  1.00 37.77           O  
HETATM 4041  O   HOH B 521      13.584  21.951  11.566  1.00 38.02           O  
HETATM 4042  O   HOH B 522       9.653   6.916  30.848  1.00 38.60           O  
HETATM 4043  O   HOH B 523       4.140  40.618  33.101  1.00 38.61           O  
HETATM 4044  O   HOH B 524      -7.068  41.608  29.691  1.00 38.79           O  
HETATM 4045  O   HOH B 525       0.509  28.123  35.074  1.00 38.90           O  
HETATM 4046  O   HOH B 526      10.967  26.607  33.620  1.00 39.42           O  
HETATM 4047  O   HOH B 527      27.857   6.715  25.285  1.00 39.56           O  
HETATM 4048  O   HOH B 528      21.102  27.796  19.749  1.00 39.64           O  
HETATM 4049  O   HOH B 529      30.737  19.620  14.332  1.00 39.77           O  
HETATM 4050  O   HOH B 530       9.294  22.707  10.387  1.00 39.80           O  
HETATM 4051  O   HOH B 531       7.751  41.695  29.991  1.00 40.00           O  
HETATM 4052  O   HOH B 532       1.444  24.785  24.725  1.00 40.09           O  
HETATM 4053  O   HOH B 533      22.025  16.262  25.685  1.00 40.69           O  
HETATM 4054  O   HOH B 534       0.270  34.839  32.105  1.00 40.95           O  
HETATM 4055  O   HOH B 535       0.576  47.316  22.538  1.00 41.31           O  
HETATM 4056  O   HOH B 536      -2.189  19.824  34.332  1.00 41.41           O  
HETATM 4057  O   HOH B 537      10.649  30.919  34.647  1.00 41.48           O  
HETATM 4058  O   HOH B 538       4.837  49.149  17.826  1.00 42.29           O  
HETATM 4059  O   HOH B 539       5.120  24.949  14.521  1.00 42.63           O  
HETATM 4060  O   HOH B 540      34.576  19.834  21.974  1.00 42.92           O  
HETATM 4061  O   HOH B 541      20.201  36.715  31.364  1.00 43.27           O  
HETATM 4062  O   HOH B 542      29.981  15.329  23.662  1.00 43.48           O  
HETATM 4063  O   HOH B 543      31.779  23.376  14.269  1.00 43.56           O  
HETATM 4064  O   HOH B 544      22.998  38.864  25.593  1.00 44.39           O  
HETATM 4065  O   HOH B 545      -4.127  29.198  34.281  1.00 44.45           O  
HETATM 4066  O   HOH B 546      29.803  27.277  26.612  1.00 44.46           O  
HETATM 4067  O   HOH B 547      24.771  15.277  27.125  1.00 44.47           O  
HETATM 4068  O   HOH B 548      19.420  26.003  25.618  1.00 44.49           O  
HETATM 4069  O   HOH B 549      10.800  18.905   8.928  1.00 44.57           O  
HETATM 4070  O   HOH B 550      25.183  40.033  19.696  1.00 45.43           O  
HETATM 4071  O   HOH B 551       9.450  40.552  31.253  1.00 45.73           O  
HETATM 4072  O   HOH B 552       3.124   8.364  28.769  1.00 46.19           O  
HETATM 4073  O   HOH B 553       3.322   9.607   9.794  1.00 46.65           O  
HETATM 4074  O   HOH B 554      11.706  12.194  32.146  1.00 47.18           O  
HETATM 4075  O   HOH B 555      29.849  15.448   8.010  1.00 47.32           O  
HETATM 4076  O   HOH B 556      32.207  13.600  24.517  1.00 47.38           O  
HETATM 4077  O   HOH B 557       8.921   3.238  16.926  1.00 47.49           O  
HETATM 4078  O   HOH B 558      -1.472  32.528  33.319  1.00 47.53           O  
HETATM 4079  O   HOH B 559      -3.288   7.082  21.620  1.00 48.03           O  
HETATM 4080  O   HOH B 560      13.667  20.807  30.154  1.00 48.25           O  
HETATM 4081  O   HOH B 561      -4.644  36.161  34.447  1.00 48.35           O  
HETATM 4082  O   HOH B 562       9.408   3.651  24.091  1.00 48.66           O  
HETATM 4083  O   HOH B 563       6.274  40.353  34.874  1.00 49.40           O  
HETATM 4084  O   HOH B 564      14.520  26.067  32.334  1.00 49.50           O  
HETATM 4085  O   HOH B 565       2.875  11.745  30.603  1.00 49.58           O  
HETATM 4086  O   HOH B 566      11.693   8.244  30.359  1.00 49.90           O  
HETATM 4087  O   HOH B 567       8.013  46.179  23.889  1.00 50.29           O  
HETATM 4088  O   HOH B 568      16.395  32.315  32.697  1.00 50.77           O  
HETATM 4089  O   HOH B 569      15.933  21.542  28.657  1.00 50.93           O  
HETATM 4090  O   HOH B 570      25.696  25.969  24.028  1.00 51.11           O  
HETATM 4091  O   HOH B 571      27.609   7.132  22.122  1.00 51.43           O  
HETATM 4092  O   HOH B 572      10.447  16.114  37.531  1.00 51.64           O  
HETATM 4093  O   HOH B 573       1.903   3.788  20.531  1.00 51.75           O  
HETATM 4094  O   HOH B 574      28.829  17.333  10.517  1.00 51.85           O  
HETATM 4095  O   HOH B 575       2.977  34.318  34.091  1.00 52.29           O  
HETATM 4096  O   HOH B 576      12.531   8.136   8.349  1.00 52.53           O  
HETATM 4097  O   HOH B 577      -4.468  34.366  31.703  1.00 53.64           O  
HETATM 4098  O   HOH B 578       4.197   9.505  30.746  1.00 54.56           O  
HETATM 4099  O   HOH B 579      -0.655  46.050  24.871  1.00 54.70           O  
HETATM 4100  O   HOH B 580      21.191  11.865  33.234  1.00 54.74           O  
HETATM 4101  O   HOH B 581      14.114  18.231  31.202  1.00 55.40           O  
HETATM 4102  O   HOH B 582       1.448   3.401  13.504  1.00 55.59           O  
HETATM 4103  O   HOH B 583      32.209  33.689  18.852  1.00 55.93           O  
HETATM 4104  O   HOH B 584       2.813  42.616  29.411  1.00 57.26           O  
HETATM 4105  O   HOH B 585      14.081  43.716  28.995  1.00 57.84           O  
HETATM 4106  O   HOH B 586       7.867  47.741  21.153  1.00 58.53           O  
HETATM 4107  O   HOH B 587      34.228  21.145  17.269  1.00 60.48           O  
HETATM 4108  O   HOH B 588      20.794  28.296  32.305  1.00 60.69           O  
HETATM 4109  O   HOH B 589      18.720  29.064  33.439  1.00 66.50           O  
HETATM 4110  O   HOH C 590       1.728  46.092   5.886  1.00 13.83           O  
HETATM 4111  O   HOH C 591      -1.673  36.869  19.267  1.00 14.16           O  
HETATM 4112  O   HOH C 592      -0.109  30.266  -5.353  1.00 15.07           O  
HETATM 4113  O   HOH C 593      -4.435  47.229   8.994  1.00 15.46           O  
HETATM 4114  O   HOH C 594      -7.285  20.330  14.085  1.00 15.88           O  
HETATM 4115  O   HOH C 595       4.798  25.791   0.845  1.00 16.19           O  
HETATM 4116  O   HOH C 596       2.420  29.820  -6.409  1.00 16.49           O  
HETATM 4117  O   HOH C 597       3.714  46.147  13.781  1.00 16.86           O  
HETATM 4118  O   HOH C 598       8.683  39.516  -2.264  1.00 27.25           O  
HETATM 4119  O   HOH C 599      -3.649  35.072  18.669  1.00 17.44           O  
HETATM 4120  O   HOH C 600      -2.253  31.229  -6.827  1.00 17.51           O  
HETATM 4121  O   HOH C 601      -0.824  18.156  15.914  1.00 17.99           O  
HETATM 4122  O   HOH C 602       2.926  16.423  10.165  1.00 27.42           O  
HETATM 4123  O   HOH C 603       5.559  43.406  15.729  1.00 18.85           O  
HETATM 4124  O   HOH C 604      -1.802  33.905  -7.424  1.00 18.90           O  
HETATM 4125  O   HOH C 605      -9.500  38.383   7.191  1.00 18.91           O  
HETATM 4126  O   HOH C 606      -0.801  17.352  13.166  1.00 19.20           O  
HETATM 4127  O   HOH C 607       3.105  30.593  12.384  1.00 19.23           O  
HETATM 4128  O   HOH C 608      -3.549  16.571  13.612  1.00 19.54           O  
HETATM 4129  O   HOH C 609      -2.520  40.170  -6.232  1.00 19.80           O  
HETATM 4130  O   HOH C 610       3.450  41.255  -0.917  1.00 19.88           O  
HETATM 4131  O   HOH C 611       3.280  36.071  -3.118  1.00 20.53           O  
HETATM 4132  O   HOH C 612     -12.133  41.467  13.261  1.00 20.54           O  
HETATM 4133  O   HOH C 613      -7.254  27.938  28.375  1.00 20.57           O  
HETATM 4134  O   HOH C 614      -0.382  47.761   2.595  1.00 20.90           O  
HETATM 4135  O   HOH C 615     -12.849  33.529  -0.753  1.00 20.95           O  
HETATM 4136  O   HOH C 616      -6.148   9.180   3.087  1.00 28.71           O  
HETATM 4137  O   HOH C 617     -14.875  15.840  -3.346  1.00 21.24           O  
HETATM 4138  O   HOH C 618       2.168  19.976   6.144  1.00 21.35           O  
HETATM 4139  O   HOH C 619       4.773  35.304  -0.898  1.00 21.36           O  
HETATM 4140  O   HOH C 620      -4.336  27.976  -7.804  1.00 21.41           O  
HETATM 4141  O   HOH C 621       9.793  45.674  14.313  1.00 21.46           O  
HETATM 4142  O   HOH C 622     -14.877  12.687  14.054  1.00 29.09           O  
HETATM 4143  O   HOH C 623       0.422  19.878  12.349  1.00 29.14           O  
HETATM 4144  O   HOH C 624       6.172  48.436  13.656  1.00 29.20           O  
HETATM 4145  O   HOH C 625     -11.433  15.577   9.106  1.00 21.50           O  
HETATM 4146  O   HOH C 626       4.143  38.707  -2.772  1.00 21.58           O  
HETATM 4147  O   HOH C 627     -10.320  12.628  12.148  1.00 21.66           O  
HETATM 4148  O   HOH C 628     -16.323  16.056   3.238  1.00 21.67           O  
HETATM 4149  O   HOH C 629      -9.236  38.648  24.510  1.00 21.69           O  
HETATM 4150  O   HOH C 630      -2.094  25.925 -10.659  1.00 29.39           O  
HETATM 4151  O   HOH C 631     -12.357  31.867   7.642  1.00 21.90           O  
HETATM 4152  O   HOH C 632       7.949  47.514  15.313  1.00 22.92           O  
HETATM 4153  O   HOH C 633      10.218  46.590  11.836  1.00 22.97           O  
HETATM 4154  O   HOH C 634       1.199  48.527   4.768  1.00 23.03           O  
HETATM 4155  O   HOH C 635     -14.805  25.832   3.459  1.00 29.62           O  
HETATM 4156  O   HOH C 636       1.767  40.015  -3.825  1.00 23.12           O  
HETATM 4157  O   HOH C 637      -3.602  11.029   0.821  1.00 29.65           O  
HETATM 4158  O   HOH C 638      -8.836  24.714  18.463  1.00 29.67           O  
HETATM 4159  O   HOH C 639     -14.181  33.040   4.480  1.00 23.17           O  
HETATM 4160  O   HOH C 640      -2.601  29.703  -9.087  1.00 23.28           O  
HETATM 4161  O   HOH C 641      -3.085  44.808  -0.237  1.00 23.62           O  
HETATM 4162  O   HOH C 642     -11.110  26.513  10.289  1.00 30.16           O  
HETATM 4163  O   HOH C 643     -13.376  13.712   8.811  1.00 30.16           O  
HETATM 4164  O   HOH C 644      -6.838  39.980  -2.739  1.00 23.63           O  
HETATM 4165  O   HOH C 645      -4.634  45.306   1.695  1.00 24.03           O  
HETATM 4166  O   HOH C 646     -11.136  25.369  20.690  1.00 24.09           O  
HETATM 4167  O   HOH C 647      11.102  48.742   8.303  1.00 30.55           O  
HETATM 4168  O   HOH C 648      -7.801  29.281  21.413  1.00 30.56           O  
HETATM 4169  O   HOH C 649     -16.043  21.181   9.133  1.00 24.15           O  
HETATM 4170  O   HOH C 650     -16.383  10.794   8.131  1.00 24.29           O  
HETATM 4171  O   HOH C 651     -12.218  23.969  10.747  1.00 24.46           O  
HETATM 4172  O   HOH C 652      -9.174  10.487  18.450  1.00 30.69           O  
HETATM 4173  O   HOH C 653      -7.480  11.027   5.794  1.00 24.80           O  
HETATM 4174  O   HOH C 654     -12.900  43.661   6.747  1.00 25.02           O  
HETATM 4175  O   HOH C 655      -5.550  48.783  16.943  1.00 30.88           O  
HETATM 4176  O   HOH C 656       7.405  40.381  -0.565  1.00 25.28           O  
HETATM 4177  O   HOH C 657      -3.022  34.016  -9.774  1.00 30.94           O  
HETATM 4178  O   HOH C 658      -3.265  44.910  -4.327  1.00 26.07           O  
HETATM 4179  O   HOH C 659      -5.807  20.990  -9.314  1.00 30.97           O  
HETATM 4180  O   HOH C 660      -5.444  32.605  -8.961  1.00 26.29           O  
HETATM 4181  O   HOH C 661     -12.121  30.927  11.169  1.00 26.43           O  
HETATM 4182  O   HOH C 662     -17.174  17.553  22.630  1.00 31.30           O  
HETATM 4183  O   HOH C 663       5.408  24.728   3.271  1.00 26.52           O  
HETATM 4184  O   HOH C 664      -7.940  44.520   3.239  1.00 26.68           O  
HETATM 4185  O   HOH C 665      -9.753  28.726  29.125  1.00 27.06           O  
HETATM 4186  O   HOH C 666     -16.093  35.301  32.537  1.00 31.48           O  
HETATM 4187  O   HOH C 667     -10.620  10.217   2.586  1.00 27.19           O  
HETATM 4188  O   HOH C 668       6.511  50.412   5.876  1.00 31.86           O  
HETATM 4189  O   HOH C 669      -6.837  12.409   0.905  1.00 31.91           O  
HETATM 4190  O   HOH C 670     -13.169  45.708   5.041  1.00 31.98           O  
HETATM 4191  O   HOH C 671      -1.885  44.928  16.450  1.00 32.05           O  
HETATM 4192  O   HOH C 672      -1.803  12.813  -0.331  1.00 32.16           O  
HETATM 4193  O   HOH C 673     -15.836  15.294  18.880  1.00 32.19           O  
HETATM 4194  O   HOH C 674      -4.277  50.633  19.195  1.00 32.25           O  
HETATM 4195  O   HOH C 675     -11.163  17.731  26.387  1.00 32.50           O  
HETATM 4196  O   HOH C 676      -8.791  34.064  -8.110  1.00 32.67           O  
HETATM 4197  O   HOH C 677      -2.027  15.281  -8.395  1.00 32.95           O  
HETATM 4198  O   HOH C 678     -17.196  22.358  20.581  1.00 33.19           O  
HETATM 4199  O   HOH C 679      -6.679  41.800  -0.803  1.00 33.22           O  
HETATM 4200  O   HOH C 680      -9.395  26.441  15.601  1.00 33.27           O  
HETATM 4201  O   HOH C 681       5.614  25.260   9.956  1.00 33.57           O  
HETATM 4202  O   HOH C 682       1.143  10.862   6.508  1.00 33.67           O  
HETATM 4203  O   HOH C 683      -1.660  47.562  19.155  1.00 33.86           O  
HETATM 4204  O   HOH C 684      -5.622  28.577  18.853  1.00 34.92           O  
HETATM 4205  O   HOH C 685      -8.442   9.077   4.384  1.00 35.02           O  
HETATM 4206  O   HOH C 686      -2.225  46.378  -2.209  1.00 35.26           O  
HETATM 4207  O   HOH C 687     -13.036  40.199   9.437  1.00 35.37           O  
HETATM 4208  O   HOH C 688      -1.741   9.147   4.388  1.00 35.39           O  
HETATM 4209  O   HOH C 689      -1.913  32.965   0.659  1.00 35.54           O  
HETATM 4210  O   HOH C 690      10.789  50.430  10.316  1.00 35.56           O  
HETATM 4211  O   HOH C 691     -15.002  23.099   7.540  1.00 35.56           O  
HETATM 4212  O   HOH C 692      -9.532  40.521  -2.632  1.00 35.61           O  
HETATM 4213  O   HOH C 693      -1.863  48.234  21.761  1.00 35.78           O  
HETATM 4214  O   HOH C 694      -6.990   6.658  14.339  1.00 35.81           O  
HETATM 4215  O   HOH C 695     -13.217  28.360  10.039  1.00 36.11           O  
HETATM 4216  O   HOH C 696      -7.754  28.070  32.476  1.00 36.14           O  
HETATM 4217  O   HOH C 697      -2.132  49.843  17.673  1.00 36.23           O  
HETATM 4218  O   HOH C 698     -13.323  26.836  21.538  1.00 36.28           O  
HETATM 4219  O   HOH C 699     -13.087  37.861   9.266  1.00 37.36           O  
HETATM 4220  O   HOH C 700       3.701  48.574   7.936  1.00 38.15           O  
HETATM 4221  O   HOH C 701       4.758  27.165   7.520  1.00 38.78           O  
HETATM 4222  O   HOH C 702      -9.573  15.719  25.812  1.00 39.37           O  
HETATM 4223  O   HOH C 703     -16.176  31.524   5.179  1.00 39.47           O  
HETATM 4224  O   HOH C 704     -13.507  36.909   2.364  1.00 39.47           O  
HETATM 4225  O   HOH C 705     -13.567  29.247   7.467  1.00 39.87           O  
HETATM 4226  O   HOH C 706      -8.332  21.790  -7.942  1.00 39.88           O  
HETATM 4227  O   HOH C 707     -14.172  37.359  13.434  1.00 39.91           O  
HETATM 4228  O   HOH C 708     -14.690  33.882   1.798  1.00 39.95           O  
HETATM 4229  O   HOH C 709      -7.681  30.870  33.415  1.00 40.23           O  
HETATM 4230  O   HOH C 710       2.933  50.441   3.870  1.00 41.04           O  
HETATM 4231  O   HOH C 711     -12.471  15.644   5.535  1.00 41.09           O  
HETATM 4232  O   HOH C 712      -1.783   9.084   1.670  1.00 41.99           O  
HETATM 4233  O   HOH C 713      -8.671  42.373   0.704  1.00 42.51           O  
HETATM 4234  O   HOH C 714       4.655  18.458  11.023  1.00 42.56           O  
HETATM 4235  O   HOH C 715     -10.612  32.085  -8.036  1.00 42.59           O  
HETATM 4236  O   HOH C 716      -3.035  44.674  -6.724  1.00 42.82           O  
HETATM 4237  O   HOH C 717     -18.052  19.559  14.426  1.00 42.90           O  
HETATM 4238  O   HOH C 718     -11.134  13.175  -3.030  1.00 42.98           O  
HETATM 4239  O   HOH C 719      -5.546  36.330  30.461  1.00 43.00           O  
HETATM 4240  O   HOH C 720     -15.402  20.407  13.364  1.00 43.37           O  
HETATM 4241  O   HOH C 721     -20.784  10.446  13.513  1.00 43.97           O  
HETATM 4242  O   HOH C 722       3.370  20.468  11.410  1.00 44.06           O  
HETATM 4243  O   HOH C 723      -7.353   8.990  17.515  1.00 44.14           O  
HETATM 4244  O   HOH C 724     -11.501  38.759  -2.357  1.00 44.42           O  
HETATM 4245  O   HOH C 725      -3.800  45.617  18.911  1.00 44.65           O  
HETATM 4246  O   HOH C 726     -15.563  10.010  13.289  1.00 44.88           O  
HETATM 4247  O   HOH C 727       1.380   9.995  -5.506  1.00 46.04           O  
HETATM 4248  O   HOH C 728      -3.429  49.301   3.998  1.00 46.34           O  
HETATM 4249  O   HOH C 729      -7.251  26.893  -9.739  1.00 46.88           O  
HETATM 4250  O   HOH C 730      -5.667  43.014  -5.050  1.00 47.00           O  
HETATM 4251  O   HOH C 731      -5.477  44.073  -1.435  1.00 47.28           O  
HETATM 4252  O   HOH C 732     -18.683  25.551  28.481  1.00 47.44           O  
HETATM 4253  O   HOH C 733      -8.741  18.840  28.564  1.00 47.47           O  
HETATM 4254  O   HOH C 734     -13.862  35.693   6.424  1.00 47.78           O  
HETATM 4255  O   HOH C 735       5.122  12.909   0.083  1.00 48.12           O  
HETATM 4256  O   HOH C 736     -13.219  41.517   3.303  1.00 48.46           O  
HETATM 4257  O   HOH C 737      -7.776  39.065  32.272  1.00 49.16           O  
HETATM 4258  O   HOH C 738     -12.419  36.491  -0.978  1.00 49.18           O  
HETATM 4259  O   HOH C 739     -17.932  36.286  17.592  1.00 49.22           O  
HETATM 4260  O   HOH C 740     -12.597  37.463   4.885  1.00 49.26           O  
HETATM 4261  O   HOH C 741      -5.387   9.319  -0.743  1.00 49.37           O  
HETATM 4262  O   HOH C 742       4.600  19.074   5.289  1.00 49.42           O  
HETATM 4263  O   HOH C 743       0.993  50.181  13.594  1.00 49.53           O  
HETATM 4264  O   HOH C 744      -5.932  12.541  24.438  1.00 49.59           O  
HETATM 4265  O   HOH C 745       9.159  49.417  12.044  1.00 50.15           O  
HETATM 4266  O   HOH C 746       6.533  22.069   4.529  1.00 50.19           O  
HETATM 4267  O   HOH C 747     -13.329  36.127  11.217  1.00 50.36           O  
HETATM 4268  O   HOH C 748     -17.437  18.016  26.528  1.00 50.73           O  
HETATM 4269  O   HOH C 749      -2.369  49.002   1.747  1.00 51.21           O  
HETATM 4270  O   HOH C 750     -12.137  35.300  -5.523  1.00 51.37           O  
HETATM 4271  O   HOH C 751     -17.912  16.320  19.829  1.00 51.68           O  
HETATM 4272  O   HOH C 752      -5.429   7.000  19.778  1.00 52.48           O  
HETATM 4273  O   HOH C 753       7.269  51.299  10.835  1.00 52.81           O  
HETATM 4274  O   HOH C 754     -13.840  31.899  -3.014  1.00 52.99           O  
HETATM 4275  O   HOH C 755      -9.809  29.023  31.716  1.00 53.53           O  
HETATM 4276  O   HOH C 756     -15.881  28.169  29.534  1.00 54.51           O  
HETATM 4277  O   HOH C 757     -12.696  17.256  28.500  1.00 54.68           O  
HETATM 4278  O   HOH C 758       0.567  47.220  17.134  1.00 54.75           O  
HETATM 4279  O   HOH C 759     -11.527  44.844   3.192  1.00 54.80           O  
HETATM 4280  O   HOH C 760     -13.957  33.710   9.263  1.00 55.21           O  
HETATM 4281  O   HOH C 761     -18.262  22.177  10.796  1.00 55.46           O  
HETATM 4282  O   HOH C 762      -1.760  18.761 -10.578  1.00 55.98           O  
HETATM 4283  O   HOH C 763      -5.319  47.934   2.133  1.00 56.15           O  
HETATM 4284  O   HOH C 764     -11.362  31.416  -5.463  1.00 56.90           O  
HETATM 4285  O   HOH C 765     -12.366  25.258  13.713  1.00 56.97           O  
HETATM 4286  O   HOH C 766       4.438   9.920   0.911  1.00 57.33           O  
HETATM 4287  O   HOH C 767     -15.586  27.238   5.692  1.00 58.98           O  
HETATM 4288  O   HOH C 768      -9.078  42.388  -4.616  1.00 60.40           O  
HETATM 4289  O   HOH C 769     -18.425  32.109   2.659  1.00 69.90           O  
CONECT    3    9   10                                                           
CONECT    9    3   11                                                           
CONECT   10    3   12                                                           
CONECT   11    9   13   17                                                      
CONECT   12   10   14   18                                                      
CONECT   13   11   15   25                                                      
CONECT   14   12   16   25                                                      
CONECT   15   13                                                                
CONECT   16   14                                                                
CONECT   17   11   19                                                           
CONECT   18   12   20                                                           
CONECT   19   17   21                                                           
CONECT   20   18   22                                                           
CONECT   21   19   23                                                           
CONECT   22   20   24                                                           
CONECT   23   21                                                                
CONECT   24   22                                                                
CONECT   25   13   14                                                           
CONECT  597  604                                                                
CONECT  604  597  605                                                           
CONECT  605  604  606  608                                                      
CONECT  606  605  607  612                                                      
CONECT  607  606                                                                
CONECT  608  605  609                                                           
CONECT  609  608  610                                                           
CONECT  610  609  611                                                           
CONECT  611  610                                                                
CONECT  612  606                                                                
CONECT  700  704                                                                
CONECT  704  700  705                                                           
CONECT  705  704  706  708                                                      
CONECT  706  705  707  712                                                      
CONECT  707  706                                                                
CONECT  708  705  709                                                           
CONECT  709  708  710                                                           
CONECT  710  709  711                                                           
CONECT  711  710                                                                
CONECT  712  706                                                                
CONECT  764 3640                                                                
CONECT  782 3640                                                                
CONECT  887 3640                                                                
CONECT 1221 1227 1228                                                           
CONECT 1227 1221 1229                                                           
CONECT 1228 1221 1230                                                           
CONECT 1229 1227 1231 1235                                                      
CONECT 1230 1228 1232 1236                                                      
CONECT 1231 1229 1233 1243                                                      
CONECT 1232 1230 1234 1243                                                      
CONECT 1233 1231                                                                
CONECT 1234 1232                                                                
CONECT 1235 1229 1237                                                           
CONECT 1236 1230 1238                                                           
CONECT 1237 1235 1239                                                           
CONECT 1238 1236 1240                                                           
CONECT 1239 1237 1241                                                           
CONECT 1240 1238 1242                                                           
CONECT 1241 1239                                                                
CONECT 1242 1240                                                                
CONECT 1243 1231 1232                                                           
CONECT 1392 3680                                                                
CONECT 1754 1761                                                                
CONECT 1761 1754 1762                                                           
CONECT 1762 1761 1763 1765                                                      
CONECT 1763 1762 1764 1769                                                      
CONECT 1764 1763                                                                
CONECT 1765 1762 1766                                                           
CONECT 1766 1765 1767                                                           
CONECT 1767 1766 1768                                                           
CONECT 1768 1767                                                                
CONECT 1769 1763                                                                
CONECT 1850 1854                                                                
CONECT 1854 1850 1855                                                           
CONECT 1855 1854 1856 1858                                                      
CONECT 1856 1855 1857 1862                                                      
CONECT 1857 1856                                                                
CONECT 1858 1855 1859                                                           
CONECT 1859 1858 1860                                                           
CONECT 1860 1859 1861                                                           
CONECT 1861 1860                                                                
CONECT 1862 1856                                                                
CONECT 1932 3679                                                                
CONECT 1950 3679                                                                
CONECT 2054 3679                                                                
CONECT 2394 2400 2401                                                           
CONECT 2400 2394 2402                                                           
CONECT 2401 2394 2403                                                           
CONECT 2402 2400 2404 2408                                                      
CONECT 2403 2401 2405 2409                                                      
CONECT 2404 2402 2406 2416                                                      
CONECT 2405 2403 2407 2416                                                      
CONECT 2406 2404                                                                
CONECT 2407 2405                                                                
CONECT 2408 2402 2410                                                           
CONECT 2409 2403 2411                                                           
CONECT 2410 2408 2412                                                           
CONECT 2411 2409 2413                                                           
CONECT 2412 2410 2414                                                           
CONECT 2413 2411 2415                                                           
CONECT 2414 2412                                                                
CONECT 2415 2413                                                                
CONECT 2416 2404 2405                                                           
CONECT 2986 2993                                                                
CONECT 2993 2986 2994                                                           
CONECT 2994 2993 2995 2997                                                      
CONECT 2995 2994 2996 3001                                                      
CONECT 2996 2995                                                                
CONECT 2997 2994 2998                                                           
CONECT 2998 2997 2999                                                           
CONECT 2999 2998 3000                                                           
CONECT 3000 2999                                                                
CONECT 3001 2995                                                                
CONECT 3089 3093                                                                
CONECT 3093 3089 3094                                                           
CONECT 3094 3093 3095 3097                                                      
CONECT 3095 3094 3096 3101                                                      
CONECT 3096 3095                                                                
CONECT 3097 3094 3098                                                           
CONECT 3098 3097 3099                                                           
CONECT 3099 3098 3100                                                           
CONECT 3100 3099                                                                
CONECT 3101 3095                                                                
CONECT 3640  764  782  887 3929                                                 
CONECT 3640 3930                                                                
CONECT 3641 3642 3643 3644 3645                                                 
CONECT 3642 3641                                                                
CONECT 3643 3641                                                                
CONECT 3644 3641                                                                
CONECT 3645 3641                                                                
CONECT 3646 3647 3648 3649 3650                                                 
CONECT 3647 3646                                                                
CONECT 3648 3646                                                                
CONECT 3649 3646                                                                
CONECT 3650 3646                                                                
CONECT 3651 3652 3653 3654 3655                                                 
CONECT 3652 3651                                                                
CONECT 3653 3651                                                                
CONECT 3654 3651                                                                
CONECT 3655 3651                                                                
CONECT 3656 3657                                                                
CONECT 3657 3656 3658                                                           
CONECT 3658 3657 3659                                                           
CONECT 3659 3658 3661                                                           
CONECT 3660 3661 3662                                                           
CONECT 3661 3659 3660                                                           
CONECT 3662 3660 3664                                                           
CONECT 3663 3664 3665                                                           
CONECT 3664 3662 3663                                                           
CONECT 3665 3663 3667                                                           
CONECT 3666 3667 3668                                                           
CONECT 3667 3665 3666                                                           
CONECT 3668 3666 3670                                                           
CONECT 3669 3670 3671                                                           
CONECT 3670 3668 3669                                                           
CONECT 3671 3669                                                                
CONECT 3672 3674                                                                
CONECT 3673 3674 3675                                                           
CONECT 3674 3672 3673                                                           
CONECT 3675 3673 3677                                                           
CONECT 3676 3677 3678                                                           
CONECT 3677 3675 3676                                                           
CONECT 3678 3676                                                                
CONECT 3679 1932 1950 2054 4039                                                 
CONECT 3679 4048                                                                
CONECT 3680 1392                                                                
CONECT 3681 3682 3683 3684 3685                                                 
CONECT 3682 3681                                                                
CONECT 3683 3681                                                                
CONECT 3684 3681                                                                
CONECT 3685 3681                                                                
CONECT 3686 3687 3688 3689 3690                                                 
CONECT 3687 3686                                                                
CONECT 3688 3686                                                                
CONECT 3689 3686                                                                
CONECT 3690 3686                                                                
CONECT 3691 3692 3693 3694 3695                                                 
CONECT 3692 3691                                                                
CONECT 3693 3691                                                                
CONECT 3694 3691                                                                
CONECT 3695 3691                                                                
CONECT 3696 3698                                                                
CONECT 3697 3698 3699                                                           
CONECT 3698 3696 3697                                                           
CONECT 3699 3697 3701                                                           
CONECT 3700 3701 3702                                                           
CONECT 3701 3699 3700                                                           
CONECT 3702 3700                                                                
CONECT 3703 3704 3705 3706 3707                                                 
CONECT 3704 3703                                                                
CONECT 3705 3703                                                                
CONECT 3706 3703                                                                
CONECT 3707 3703                                                                
CONECT 3708 3709 3710 3711 3712                                                 
CONECT 3709 3708                                                                
CONECT 3710 3708                                                                
CONECT 3711 3708                                                                
CONECT 3712 3708                                                                
CONECT 3713 3714                                                                
CONECT 3714 3713 3715                                                           
CONECT 3715 3714 3716                                                           
CONECT 3716 3715 3718                                                           
CONECT 3717 3718 3719                                                           
CONECT 3718 3716 3717                                                           
CONECT 3719 3717 3721                                                           
CONECT 3720 3721 3722                                                           
CONECT 3721 3719 3720                                                           
CONECT 3722 3720 3724                                                           
CONECT 3723 3724 3725                                                           
CONECT 3724 3722 3723                                                           
CONECT 3725 3723 3727                                                           
CONECT 3726 3727 3728                                                           
CONECT 3727 3725 3726                                                           
CONECT 3728 3726                                                                
CONECT 3729 3731                                                                
CONECT 3730 3731 3732                                                           
CONECT 3731 3729 3730                                                           
CONECT 3732 3730 3734                                                           
CONECT 3733 3734 3735                                                           
CONECT 3734 3732 3733                                                           
CONECT 3735 3733                                                                
CONECT 3929 3640                                                                
CONECT 3930 3640                                                                
CONECT 4039 3679                                                                
CONECT 4048 3679                                                                
MASTER      486    0   25    3   42    0   31    6 3991    3  223   36          
END