Welcome to PDBbind-CN database

Browse entries in the PDBbind-CN Database

HEADER    TRANSPORT PROTEIN                       07-MAR-08   3CH5              
TITLE     THE CRYSTAL STRUCTURE OF THE RANGDP-NUP153ZNF2 COMPLEX                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GTPASE RAN; RAS-LIKE PROTEIN TC4; ANDROGEN RECEPTOR-        
COMPND   5 ASSOCIATED PROTEIN 24;                                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: FRAGMENT OF NUCLEAR PORE COMPLEX PROTEIN NUP153;           
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: RESIDUES 703-754;                                          
COMPND  11 SYNONYM: NUP153ZNF2; NUCLEOPORIN NUP153;                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAN, ARA24;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3D;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  13 ORGANISM_COMMON: RAT;                                                
SOURCE  14 ORGANISM_TAXID: 10116;                                               
SOURCE  15 GENE: NUP153;                                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODONPLUS;                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1                                  
KEYWDS    RANBP2 TYPE C2-C2 ZINC FINGER, TRANSPORT PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.R.VETTER,N.SCHRADER                                                 
REVDAT   4   13-JUL-11 3CH5    1       VERSN                                    
REVDAT   3   24-FEB-09 3CH5    1       VERSN                                    
REVDAT   2   22-JUL-08 3CH5    1       JRNL                                     
REVDAT   1   01-JUL-08 3CH5    0                                                
JRNL        AUTH   N.SCHRADER,C.KOERNER,K.KOESSMEIER,J.A.BANGERT,               
JRNL        AUTH 2 A.WITTINGHOFER,R.STOLL,I.R.VETTER                            
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE RAN-NUP153ZNF2 COMPLEX: A       
JRNL        TITL 2 GENERAL RAN DOCKING SITE AT THE NUCLEAR PORE COMPLEX         
JRNL        REF    STRUCTURE                     V.  16  1116 2008              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   18611384                                                     
JRNL        DOI    10.1016/J.STR.2008.03.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 18026                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 949                             
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1350                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1820                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 71                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 13.47                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.32000                                             
REMARK   3    B22 (A**2) : 2.92000                                              
REMARK   3    B33 (A**2) : -1.60000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.186         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.166         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.866        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1969 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2686 ; 1.674 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   241 ; 6.993 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    89 ;38.235 ;24.719       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   331 ;18.353 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;13.087 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   289 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1503 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   850 ; 0.226 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1339 ; 0.313 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    94 ; 0.147 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.010 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    39 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.302 ; 0.200       
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):  1214 ; 0.751 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1935 ; 1.234 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   867 ; 1.841 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   751 ; 2.800 ; 4.500       
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  : 2                                          
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     7        A   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2428 -14.2837 -46.4228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0644 T22:  -0.0997                                     
REMARK   3      T33:  -0.0474 T12:   0.0295                                     
REMARK   3      T13:  -0.0522 T23:   0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8087 L22:   2.1541                                     
REMARK   3      L33:   3.5811 L12:  -0.5553                                     
REMARK   3      L13:  -0.2415 L23:   0.0844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1568 S12:  -0.0814 S13:  -0.5499                       
REMARK   3      S21:  -0.0217 S22:  -0.2189 S23:   0.0972                       
REMARK   3      S31:   0.5185 S32:   0.2902 S33:   0.0621                       
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   713        B   749                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.5564 -12.9017 -25.7564              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0480 T22:   0.2076                                     
REMARK   3      T33:   0.0125 T12:  -0.0574                                     
REMARK   3      T13:   0.0925 T23:   0.1540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.6597 L22:   8.1697                                     
REMARK   3      L33:   4.5533 L12:   2.9284                                     
REMARK   3      L13:  -4.6143 L23:  -1.0098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0351 S12:  -0.8811 S13:  -0.4114                       
REMARK   3      S21:   0.3609 S22:  -0.2078 S23:   0.5918                       
REMARK   3      S31:   0.0175 S32:  -0.3419 S33:   0.2429                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3CH5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046770.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2726                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18026                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.310                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: RANGDP                                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M BIS TRIS,    
REMARK 280  PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.67500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       61.52500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.67500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.52500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       37.67500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.52500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.85000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       37.67500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       61.52500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -240.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000     -123.05000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000     -123.05000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     VAL A   137                                                      
REMARK 465     PHE A   138                                                      
REMARK 465     HIS A   139                                                      
REMARK 465     ARG A   140                                                      
REMARK 465     LYS A   141                                                      
REMARK 465     LYS A   142                                                      
REMARK 465     THR A   206                                                      
REMARK 465     THR A   207                                                      
REMARK 465     ALA A   208                                                      
REMARK 465     LEU A   209                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     ASP A   214                                                      
REMARK 465     ASP A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     SER B   703                                                      
REMARK 465     ASP B   704                                                      
REMARK 465     LYS B   705                                                      
REMARK 465     PRO B   706                                                      
REMARK 465     ALA B   707                                                      
REMARK 465     SER B   708                                                      
REMARK 465     THR B   709                                                      
REMARK 465     SER B   710                                                      
REMARK 465     GLY B   711                                                      
REMARK 465     THR B   712                                                      
REMARK 465     GLY B   750                                                      
REMARK 465     THR B   751                                                      
REMARK 465     GLY B   752                                                      
REMARK 465     VAL B   753                                                      
REMARK 465     LYS B   754                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 737   CG    GLU B 737   CD      0.099                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS B 730   N   -  CA  -  C   ANGL. DEV. =  16.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A   8     -153.29   -129.64                                   
REMARK 500    CYS A 112      -64.20    -95.55                                   
REMARK 500    LYS A 123       31.96     74.66                                   
REMARK 500    ALA A 204      -67.84    -90.01                                   
REMARK 500    LYS B 717       31.26     79.24                                   
REMARK 500    PHE B 718       -0.49   -150.95                                   
REMARK 500    LEU B 731       69.62   -112.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    CYS A 112        19.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 717        23.1      L          L   OUTSIDE RANGE           
REMARK 500    CYS B 730        21.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 731        45.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 221  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  24   OG1                                                    
REMARK 620 2 GDP A 220   O1B  95.4                                              
REMARK 620 3 HOH A 265   O    87.9  95.4                                        
REMARK 620 4 HOH A 269   O   172.0  89.6  85.4                                  
REMARK 620 5 HOH A 236   O    90.1  91.2 173.2  96.0                            
REMARK 620 6 HOH A 270   O    79.5 174.5  86.5  95.7  86.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 800  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 727   SG                                                     
REMARK 620 2 CYS B 730   SG  118.1                                              
REMARK 620 3 CYS B 741   SG  108.9 104.9                                        
REMARK 620 4 CYS B 744   SG   97.7 118.4 108.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 221                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 800                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 222                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 220                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2KOC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2EBV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2GQE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2EBQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2EBR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1IBR   RELATED DB: PDB                                   
DBREF  3CH5 A    1   216  UNP    P62826   RAN_HUMAN        1    216             
DBREF  3CH5 B  703   754  UNP    P49791   NU153_RAT      703    754             
SEQRES   1 A  216  MET ALA ALA GLN GLY GLU PRO GLN VAL GLN PHE LYS LEU          
SEQRES   2 A  216  VAL LEU VAL GLY ASP GLY GLY THR GLY LYS THR THR PHE          
SEQRES   3 A  216  VAL LYS ARG HIS LEU THR GLY GLU PHE GLU LYS LYS TYR          
SEQRES   4 A  216  VAL ALA THR LEU GLY VAL GLU VAL HIS PRO LEU VAL PHE          
SEQRES   5 A  216  HIS THR ASN ARG GLY PRO ILE LYS PHE ASN VAL TRP ASP          
SEQRES   6 A  216  THR ALA GLY GLN GLU LYS PHE GLY GLY LEU ARG ASP GLY          
SEQRES   7 A  216  TYR TYR ILE GLN ALA GLN CYS ALA ILE ILE MET PHE ASP          
SEQRES   8 A  216  VAL THR SER ARG VAL THR TYR LYS ASN VAL PRO ASN TRP          
SEQRES   9 A  216  HIS ARG ASP LEU VAL ARG VAL CYS GLU ASN ILE PRO ILE          
SEQRES  10 A  216  VAL LEU CYS GLY ASN LYS VAL ASP ILE LYS ASP ARG LYS          
SEQRES  11 A  216  VAL LYS ALA LYS SER ILE VAL PHE HIS ARG LYS LYS ASN          
SEQRES  12 A  216  LEU GLN TYR TYR ASP ILE SER ALA LYS SER ASN TYR ASN          
SEQRES  13 A  216  PHE GLU LYS PRO PHE LEU TRP LEU ALA ARG LYS LEU ILE          
SEQRES  14 A  216  GLY ASP PRO ASN LEU GLU PHE VAL ALA MET PRO ALA LEU          
SEQRES  15 A  216  ALA PRO PRO GLU VAL VAL MET ASP PRO ALA LEU ALA ALA          
SEQRES  16 A  216  GLN TYR GLU HIS ASP LEU GLU VAL ALA GLN THR THR ALA          
SEQRES  17 A  216  LEU PRO ASP GLU ASP ASP ASP LEU                              
SEQRES   1 B   52  SER ASP LYS PRO ALA SER THR SER GLY THR GLY PHE GLY          
SEQRES   2 B   52  ASP LYS PHE LYS PRO ALA ILE GLY THR TRP ASP CYS ASP          
SEQRES   3 B   52  THR CYS LEU VAL GLN ASN LYS PRO GLU ALA VAL LYS CYS          
SEQRES   4 B   52  VAL ALA CYS GLU THR PRO LYS PRO GLY THR GLY VAL LYS          
HET     MG  A 221       1                                                       
HET    SO4  A 222       5                                                       
HET     ZN  B 800       1                                                       
HET    GDP  A 220      28                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  GDP    C10 H15 N5 O11 P2                                            
FORMUL   7  HOH   *71(H2 O)                                                     
HELIX    1   1 GLY A   22  HIS A   30  1                                   9    
HELIX    2   1 THR A   32  LYS A   37  1                                   6    
HELIX    3   2 GLN A   69  GLY A   73  5                                   5    
HELIX    4   3 ARG A   76  ILE A   81  1                                   6    
HELIX    5   4 SER A   94  ASN A  100  1                                   7    
HELIX    6   5 ASN A  100  GLU A  113  1                                  14    
HELIX    7   7 GLU A  158  GLY A  170  1                                  13    
HELIX    8   8 ALA A  192  GLN A  205  1                                  14    
SHEET    1   A 6 LYS A  38  VAL A  40  0                                        
SHEET    2   A 6 VAL A  45  THR A  54  0                                        
SHEET    3   A 6 GLY A  57  THR A  66 -1  O  PHE A  61   N  LEU A  50           
SHEET    4   A 6 VAL A   9  GLY A  17  1  N  LEU A  13   O  TRP A  64           
SHEET    5   A 6 CYS A  85  ASP A  91  1  O  MET A  89   N  VAL A  16           
SHEET    6   A 6 ILE A 117  ASN A 122  1  O  ASN A 122   N  PHE A  90           
SHEET    7   A 6 GLN A 145  ASP A 148  1  O  GLN A 145   N  LEU A 119           
SHEET    1   B 3 LYS A  38  TYR A  39  0                                        
SHEET    2   B 3 VAL A  45  THR A  54 -1  O  VAL A  47   N  LYS A  38           
SHEET    3   B 3 PHE A 176  ALA A 178 -1  O  VAL A 177   N  HIS A  53           
SHEET    1   C 2 TRP B 725  ASP B 726  0                                        
SHEET    2   C 2 GLN B 733  ASN B 734 -1  O  ASN B 734   N  TRP B 725           
LINK         OG1 THR A  24                MG    MG A 221     1555   1555  2.17  
LINK         SG  CYS B 727                ZN    ZN B 800     1555   1555  2.24  
LINK         SG  CYS B 730                ZN    ZN B 800     1555   1555  2.36  
LINK         SG  CYS B 741                ZN    ZN B 800     1555   1555  2.40  
LINK         SG  CYS B 744                ZN    ZN B 800     1555   1555  2.41  
LINK        MG    MG A 221                 O1B GDP A 220     1555   1555  2.00  
LINK        MG    MG A 221                 O   HOH A 265     1555   1555  2.13  
LINK        MG    MG A 221                 O   HOH A 269     1555   1555  2.21  
LINK        MG    MG A 221                 O   HOH A 236     1555   1555  2.14  
LINK        MG    MG A 221                 O   HOH A 270     1555   1555  1.98  
CISPEP   1 PRO A    7    GLN A    8          0         5.09                     
CISPEP   2 CYS A  112    GLU A  113          0       -23.54                     
CISPEP   3 PHE B  714    GLY B  715          0        -4.32                     
CISPEP   4 ASP B  716    LYS B  717          0        -8.87                     
CISPEP   5 CYS B  730    LEU B  731          0       -24.61                     
SITE     1 AC1  1 THR A  24                                                     
SITE     1 AC2  4 CYS B 727  CYS B 730  CYS B 741  CYS B 744                    
SITE     1 AC3  4 THR A  32  HIS A  53  PRO A 180  ALA A 181                    
SITE     1 AC4 15 ASP A  18  GLY A  19  GLY A  20  THR A  21                    
SITE     2 AC4 15 GLY A  22  LYS A  23  THR A  24  THR A  25                    
SITE     3 AC4 15 ASN A 122  LYS A 123  ASP A 125  ILE A 126                    
SITE     4 AC4 15 SER A 150  ALA A 151  LYS A 152                               
CRYST1   69.700   75.350  123.050  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014347  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013271  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008127        0.00000                         
ATOM      1  N   PRO A   7      -8.487  -9.461 -32.889  1.00 62.04           N  
ATOM      2  CA  PRO A   7      -7.715  -9.321 -31.646  1.00 61.81           C  
ATOM      3  C   PRO A   7      -6.159  -9.336 -31.759  1.00 61.51           C  
ATOM      4  O   PRO A   7      -5.488  -9.044 -30.764  1.00 61.78           O  
ATOM      5  CB  PRO A   7      -8.210 -10.508 -30.805  1.00 61.89           C  
ATOM      6  CG  PRO A   7      -9.627 -10.822 -31.360  1.00 62.06           C  
ATOM      7  CD  PRO A   7      -9.823 -10.033 -32.641  1.00 61.97           C  
ATOM      8  N   GLN A   8      -5.573  -9.630 -32.927  1.00 60.58           N  
ATOM      9  CA  GLN A   8      -6.285  -9.852 -34.200  1.00 59.36           C  
ATOM     10  C   GLN A   8      -5.824 -11.167 -34.861  1.00 57.83           C  
ATOM     11  O   GLN A   8      -5.412 -12.102 -34.156  1.00 57.87           O  
ATOM     12  CB  GLN A   8      -6.137  -8.616 -35.115  1.00 59.45           C  
ATOM     13  CG  GLN A   8      -4.913  -7.733 -34.783  1.00 61.29           C  
ATOM     14  CD  GLN A   8      -5.157  -6.208 -34.928  1.00 63.59           C  
ATOM     15  OE1 GLN A   8      -6.274  -5.754 -35.229  1.00 64.05           O  
ATOM     16  NE2 GLN A   8      -4.097  -5.421 -34.707  1.00 63.18           N  
ATOM     17  N   VAL A   9      -5.923 -11.258 -36.190  1.00 55.57           N  
ATOM     18  CA  VAL A   9      -5.322 -12.379 -36.941  1.00 52.98           C  
ATOM     19  C   VAL A   9      -3.832 -12.078 -37.255  1.00 50.71           C  
ATOM     20  O   VAL A   9      -3.492 -11.430 -38.260  1.00 50.03           O  
ATOM     21  CB  VAL A   9      -6.172 -12.777 -38.196  1.00 53.47           C  
ATOM     22  CG1 VAL A   9      -6.308 -11.614 -39.180  1.00 53.22           C  
ATOM     23  CG2 VAL A   9      -5.636 -14.067 -38.865  1.00 53.73           C  
ATOM     24  N   GLN A  10      -2.973 -12.598 -36.380  1.00 47.56           N  
ATOM     25  CA  GLN A  10      -1.593 -12.158 -36.197  1.00 44.49           C  
ATOM     26  C   GLN A  10      -0.678 -13.378 -36.044  1.00 42.32           C  
ATOM     27  O   GLN A  10      -0.996 -14.304 -35.291  1.00 41.29           O  
ATOM     28  CB  GLN A  10      -1.576 -11.389 -34.887  1.00 45.18           C  
ATOM     29  CG  GLN A  10      -0.439 -10.475 -34.644  1.00 45.63           C  
ATOM     30  CD  GLN A  10      -0.651  -9.691 -33.375  1.00 46.82           C  
ATOM     31  OE1 GLN A  10      -1.475 -10.070 -32.540  1.00 47.62           O  
ATOM     32  NE2 GLN A  10       0.064  -8.579 -33.229  1.00 44.75           N  
ATOM     33  N   PHE A  11       0.459 -13.380 -36.729  1.00 38.83           N  
ATOM     34  CA  PHE A  11       1.346 -14.534 -36.697  1.00 35.96           C  
ATOM     35  C   PHE A  11       2.770 -14.047 -36.562  1.00 34.12           C  
ATOM     36  O   PHE A  11       3.201 -13.179 -37.338  1.00 31.25           O  
ATOM     37  CB  PHE A  11       1.239 -15.350 -37.985  1.00 36.05           C  
ATOM     38  CG  PHE A  11      -0.118 -15.951 -38.218  1.00 37.50           C  
ATOM     39  CD1 PHE A  11      -0.485 -17.116 -37.587  1.00 34.21           C  
ATOM     40  CD2 PHE A  11      -1.030 -15.335 -39.074  1.00 39.67           C  
ATOM     41  CE1 PHE A  11      -1.731 -17.669 -37.799  1.00 38.53           C  
ATOM     42  CE2 PHE A  11      -2.289 -15.876 -39.277  1.00 38.04           C  
ATOM     43  CZ  PHE A  11      -2.638 -17.039 -38.643  1.00 38.32           C  
ATOM     44  N   LYS A  12       3.503 -14.636 -35.618  1.00 31.42           N  
ATOM     45  CA  LYS A  12       4.939 -14.382 -35.514  1.00 30.49           C  
ATOM     46  C   LYS A  12       5.662 -15.101 -36.644  1.00 30.01           C  
ATOM     47  O   LYS A  12       5.529 -16.303 -36.824  1.00 30.81           O  
ATOM     48  CB  LYS A  12       5.505 -14.847 -34.171  1.00 29.72           C  
ATOM     49  CG  LYS A  12       7.029 -14.699 -34.081  1.00 28.05           C  
ATOM     50  CD  LYS A  12       7.506 -15.099 -32.688  1.00 31.32           C  
ATOM     51  CE  LYS A  12       8.986 -15.395 -32.677  1.00 29.58           C  
ATOM     52  NZ  LYS A  12       9.477 -15.209 -31.297  1.00 31.31           N  
ATOM     53  N   LEU A  13       6.413 -14.355 -37.417  1.00 29.84           N  
ATOM     54  CA  LEU A  13       7.224 -14.937 -38.473  1.00 30.16           C  
ATOM     55  C   LEU A  13       8.705 -14.665 -38.190  1.00 30.41           C  
ATOM     56  O   LEU A  13       9.104 -13.525 -38.047  1.00 30.68           O  
ATOM     57  CB  LEU A  13       6.803 -14.345 -39.821  1.00 30.40           C  
ATOM     58  CG  LEU A  13       7.366 -14.920 -41.126  1.00 30.20           C  
ATOM     59  CD1 LEU A  13       6.528 -14.454 -42.321  1.00 31.09           C  
ATOM     60  CD2 LEU A  13       8.783 -14.519 -41.313  1.00 29.66           C  
ATOM     61  N   VAL A  14       9.503 -15.730 -38.082  1.00 31.05           N  
ATOM     62  CA  VAL A  14      10.957 -15.609 -37.901  1.00 30.88           C  
ATOM     63  C   VAL A  14      11.687 -15.619 -39.258  1.00 31.14           C  
ATOM     64  O   VAL A  14      11.503 -16.524 -40.067  1.00 32.66           O  
ATOM     65  CB  VAL A  14      11.543 -16.690 -36.953  1.00 30.54           C  
ATOM     66  CG1 VAL A  14      11.078 -16.453 -35.512  1.00 31.59           C  
ATOM     67  CG2 VAL A  14      11.154 -18.111 -37.375  1.00 30.90           C  
ATOM     68  N   LEU A  15      12.506 -14.605 -39.490  1.00 30.60           N  
ATOM     69  CA  LEU A  15      13.244 -14.444 -40.730  1.00 30.70           C  
ATOM     70  C   LEU A  15      14.698 -14.766 -40.398  1.00 30.49           C  
ATOM     71  O   LEU A  15      15.324 -14.038 -39.627  1.00 31.62           O  
ATOM     72  CB  LEU A  15      13.098 -12.988 -41.185  1.00 30.33           C  
ATOM     73  CG  LEU A  15      13.923 -12.506 -42.373  1.00 33.37           C  
ATOM     74  CD1 LEU A  15      13.700 -13.436 -43.566  1.00 31.86           C  
ATOM     75  CD2 LEU A  15      13.489 -11.077 -42.729  1.00 31.03           C  
ATOM     76  N   VAL A  16      15.220 -15.880 -40.926  1.00 30.38           N  
ATOM     77  CA  VAL A  16      16.543 -16.390 -40.547  1.00 29.61           C  
ATOM     78  C   VAL A  16      17.382 -16.676 -41.805  1.00 29.71           C  
ATOM     79  O   VAL A  16      16.891 -16.581 -42.929  1.00 30.13           O  
ATOM     80  CB  VAL A  16      16.471 -17.656 -39.610  1.00 29.79           C  
ATOM     81  CG1 VAL A  16      15.720 -17.362 -38.320  1.00 29.59           C  
ATOM     82  CG2 VAL A  16      15.872 -18.844 -40.319  1.00 28.13           C  
ATOM     83  N   GLY A  17      18.653 -16.989 -41.630  1.00 28.96           N  
ATOM     84  CA  GLY A  17      19.563 -17.146 -42.776  1.00 29.50           C  
ATOM     85  C   GLY A  17      20.824 -16.356 -42.516  1.00 29.77           C  
ATOM     86  O   GLY A  17      20.825 -15.454 -41.685  1.00 29.86           O  
ATOM     87  N   ASP A  18      21.900 -16.701 -43.211  1.00 30.57           N  
ATOM     88  CA  ASP A  18      23.224 -16.128 -42.952  1.00 31.06           C  
ATOM     89  C   ASP A  18      23.240 -14.598 -42.963  1.00 30.97           C  
ATOM     90  O   ASP A  18      22.418 -13.967 -43.621  1.00 30.78           O  
ATOM     91  CB  ASP A  18      24.223 -16.672 -43.976  1.00 31.71           C  
ATOM     92  CG  ASP A  18      24.604 -18.128 -43.716  1.00 32.76           C  
ATOM     93  OD1 ASP A  18      25.457 -18.654 -44.481  1.00 35.40           O  
ATOM     94  OD2 ASP A  18      24.067 -18.751 -42.759  1.00 31.47           O  
ATOM     95  N   GLY A  19      24.164 -13.991 -42.223  1.00 31.13           N  
ATOM     96  CA  GLY A  19      24.323 -12.539 -42.320  1.00 30.98           C  
ATOM     97  C   GLY A  19      24.706 -12.151 -43.749  1.00 31.58           C  
ATOM     98  O   GLY A  19      25.440 -12.876 -44.424  1.00 30.89           O  
ATOM     99  N   GLY A  20      24.189 -11.013 -44.217  1.00 32.20           N  
ATOM    100  CA  GLY A  20      24.516 -10.510 -45.532  1.00 31.99           C  
ATOM    101  C   GLY A  20      23.674 -11.084 -46.665  1.00 32.86           C  
ATOM    102  O   GLY A  20      23.958 -10.796 -47.826  1.00 33.03           O  
ATOM    103  N   THR A  21      22.615 -11.843 -46.348  1.00 32.62           N  
ATOM    104  CA  THR A  21      21.777 -12.463 -47.393  1.00 32.42           C  
ATOM    105  C   THR A  21      20.658 -11.534 -47.833  1.00 32.11           C  
ATOM    106  O   THR A  21      20.017 -11.762 -48.860  1.00 31.71           O  
ATOM    107  CB  THR A  21      21.175 -13.831 -46.967  1.00 32.97           C  
ATOM    108  OG1 THR A  21      20.383 -13.679 -45.787  1.00 34.47           O  
ATOM    109  CG2 THR A  21      22.267 -14.876 -46.700  1.00 29.41           C  
ATOM    110  N   GLY A  22      20.421 -10.493 -47.044  1.00 31.86           N  
ATOM    111  CA  GLY A  22      19.472  -9.466 -47.397  1.00 32.47           C  
ATOM    112  C   GLY A  22      18.221  -9.442 -46.548  1.00 32.71           C  
ATOM    113  O   GLY A  22      17.209  -8.848 -46.946  1.00 33.28           O  
ATOM    114  N   LYS A  23      18.290 -10.054 -45.370  1.00 32.53           N  
ATOM    115  CA  LYS A  23      17.125 -10.206 -44.512  1.00 32.48           C  
ATOM    116  C   LYS A  23      16.557  -8.859 -44.092  1.00 33.41           C  
ATOM    117  O   LYS A  23      15.376  -8.637 -44.230  1.00 33.97           O  
ATOM    118  CB  LYS A  23      17.459 -11.054 -43.278  1.00 31.57           C  
ATOM    119  CG  LYS A  23      17.897 -12.460 -43.617  1.00 29.92           C  
ATOM    120  CD  LYS A  23      18.075 -13.305 -42.353  1.00 29.27           C  
ATOM    121  CE  LYS A  23      19.163 -12.758 -41.381  1.00 26.52           C  
ATOM    122  NZ  LYS A  23      20.506 -12.717 -42.035  1.00 24.21           N  
ATOM    123  N   THR A  24      17.399  -7.969 -43.572  1.00 34.02           N  
ATOM    124  CA  THR A  24      16.960  -6.649 -43.121  1.00 33.74           C  
ATOM    125  C   THR A  24      16.431  -5.840 -44.306  1.00 34.07           C  
ATOM    126  O   THR A  24      15.358  -5.211 -44.226  1.00 34.15           O  
ATOM    127  CB  THR A  24      18.099  -5.947 -42.408  1.00 33.80           C  
ATOM    128  OG1 THR A  24      18.389  -6.654 -41.194  1.00 32.70           O  
ATOM    129  CG2 THR A  24      17.770  -4.469 -42.084  1.00 34.56           C  
ATOM    130  N   THR A  25      17.153  -5.901 -45.421  1.00 33.13           N  
ATOM    131  CA  THR A  25      16.756  -5.194 -46.638  1.00 33.40           C  
ATOM    132  C   THR A  25      15.360  -5.583 -47.091  1.00 33.27           C  
ATOM    133  O   THR A  25      14.584  -4.737 -47.547  1.00 33.09           O  
ATOM    134  CB  THR A  25      17.753  -5.454 -47.790  1.00 32.36           C  
ATOM    135  OG1 THR A  25      19.037  -5.004 -47.381  1.00 33.48           O  
ATOM    136  CG2 THR A  25      17.392  -4.647 -49.021  1.00 33.61           C  
ATOM    137  N   PHE A  26      15.079  -6.875 -46.982  1.00 33.22           N  
ATOM    138  CA  PHE A  26      13.830  -7.469 -47.404  1.00 34.06           C  
ATOM    139  C   PHE A  26      12.675  -7.059 -46.513  1.00 34.39           C  
ATOM    140  O   PHE A  26      11.608  -6.714 -47.020  1.00 33.97           O  
ATOM    141  CB  PHE A  26      13.964  -8.992 -47.387  1.00 33.96           C  
ATOM    142  CG  PHE A  26      12.688  -9.746 -47.671  1.00 35.16           C  
ATOM    143  CD1 PHE A  26      12.146  -9.785 -48.947  1.00 35.46           C  
ATOM    144  CD2 PHE A  26      12.079 -10.493 -46.668  1.00 36.24           C  
ATOM    145  CE1 PHE A  26      10.968 -10.535 -49.208  1.00 36.87           C  
ATOM    146  CE2 PHE A  26      10.916 -11.233 -46.912  1.00 36.77           C  
ATOM    147  CZ  PHE A  26      10.366 -11.257 -48.184  1.00 36.40           C  
ATOM    148  N   VAL A  27      12.865  -7.129 -45.196  1.00 34.40           N  
ATOM    149  CA  VAL A  27      11.749  -6.828 -44.304  1.00 34.52           C  
ATOM    150  C   VAL A  27      11.413  -5.325 -44.353  1.00 35.10           C  
ATOM    151  O   VAL A  27      10.239  -4.931 -44.201  1.00 35.48           O  
ATOM    152  CB  VAL A  27      12.019  -7.349 -42.860  1.00 35.02           C  
ATOM    153  CG1 VAL A  27      13.063  -6.466 -42.132  1.00 33.54           C  
ATOM    154  CG2 VAL A  27      10.695  -7.405 -42.083  1.00 34.90           C  
ATOM    155  N   LYS A  28      12.424  -4.497 -44.651  1.00 34.76           N  
ATOM    156  CA  LYS A  28      12.228  -3.036 -44.773  1.00 35.22           C  
ATOM    157  C   LYS A  28      11.538  -2.547 -46.056  1.00 34.58           C  
ATOM    158  O   LYS A  28      11.260  -1.356 -46.188  1.00 34.71           O  
ATOM    159  CB  LYS A  28      13.550  -2.304 -44.614  1.00 35.49           C  
ATOM    160  CG  LYS A  28      14.131  -2.450 -43.228  1.00 38.32           C  
ATOM    161  CD  LYS A  28      15.550  -1.920 -43.242  1.00 43.90           C  
ATOM    162  CE  LYS A  28      15.711  -0.701 -42.356  1.00 50.48           C  
ATOM    163  NZ  LYS A  28      15.774  -1.097 -40.906  1.00 53.46           N  
ATOM    164  N   ARG A  29      11.266  -3.442 -47.002  1.00 33.82           N  
ATOM    165  CA  ARG A  29      10.510  -3.066 -48.191  1.00 32.68           C  
ATOM    166  C   ARG A  29       9.082  -2.689 -47.785  1.00 33.06           C  
ATOM    167  O   ARG A  29       8.469  -1.799 -48.383  1.00 34.82           O  
ATOM    168  CB  ARG A  29      10.460  -4.249 -49.186  1.00 32.62           C  
ATOM    169  CG  ARG A  29      11.820  -4.844 -49.577  1.00 31.93           C  
ATOM    170  CD  ARG A  29      12.864  -3.763 -49.881  1.00 32.28           C  
ATOM    171  NE  ARG A  29      12.495  -2.955 -51.030  1.00 34.27           N  
ATOM    172  CZ  ARG A  29      13.248  -1.951 -51.462  1.00 33.92           C  
ATOM    173  NH1 ARG A  29      12.874  -1.255 -52.514  1.00 33.91           N  
ATOM    174  NH2 ARG A  29      14.389  -1.661 -50.837  1.00 32.16           N  
ATOM    175  N   HIS A  30       8.535  -3.357 -46.773  1.00 31.80           N  
ATOM    176  CA  HIS A  30       7.214  -2.987 -46.260  1.00 31.90           C  
ATOM    177  C   HIS A  30       7.308  -1.673 -45.449  1.00 31.86           C  
ATOM    178  O   HIS A  30       7.832  -1.650 -44.320  1.00 32.38           O  
ATOM    179  CB  HIS A  30       6.636  -4.129 -45.446  1.00 31.14           C  
ATOM    180  CG  HIS A  30       5.220  -3.919 -45.038  1.00 32.04           C  
ATOM    181  ND1 HIS A  30       4.183  -4.693 -45.522  1.00 31.57           N  
ATOM    182  CD2 HIS A  30       4.665  -3.032 -44.178  1.00 30.43           C  
ATOM    183  CE1 HIS A  30       3.050  -4.304 -44.964  1.00 32.18           C  
ATOM    184  NE2 HIS A  30       3.313  -3.273 -44.169  1.00 37.53           N  
ATOM    185  N   LEU A  31       6.860  -0.570 -46.047  1.00 30.68           N  
ATOM    186  CA  LEU A  31       7.126   0.759 -45.455  1.00 30.06           C  
ATOM    187  C   LEU A  31       6.429   1.007 -44.106  1.00 30.81           C  
ATOM    188  O   LEU A  31       7.046   1.510 -43.165  1.00 29.36           O  
ATOM    189  CB  LEU A  31       6.796   1.874 -46.432  1.00 30.24           C  
ATOM    190  CG  LEU A  31       7.670   1.984 -47.679  1.00 28.45           C  
ATOM    191  CD1 LEU A  31       7.141   3.167 -48.495  1.00 28.35           C  
ATOM    192  CD2 LEU A  31       9.160   2.176 -47.291  1.00 28.95           C  
ATOM    193  N   THR A  32       5.157   0.631 -43.994  1.00 30.99           N  
ATOM    194  CA  THR A  32       4.466   0.781 -42.704  1.00 32.37           C  
ATOM    195  C   THR A  32       5.060  -0.110 -41.574  1.00 33.34           C  
ATOM    196  O   THR A  32       5.187   0.326 -40.423  1.00 32.65           O  
ATOM    197  CB  THR A  32       2.939   0.584 -42.867  1.00 32.59           C  
ATOM    198  OG1 THR A  32       2.425   1.700 -43.621  1.00 33.58           O  
ATOM    199  CG2 THR A  32       2.255   0.553 -41.520  1.00 29.90           C  
ATOM    200  N   GLY A  33       5.443  -1.331 -41.915  1.00 32.77           N  
ATOM    201  CA  GLY A  33       6.044  -2.237 -40.926  1.00 33.73           C  
ATOM    202  C   GLY A  33       7.362  -1.714 -40.405  1.00 33.96           C  
ATOM    203  O   GLY A  33       7.727  -1.981 -39.260  1.00 34.81           O  
ATOM    204  N   GLU A  34       8.085  -0.987 -41.251  1.00 33.28           N  
ATOM    205  CA  GLU A  34       9.310  -0.295 -40.858  1.00 34.03           C  
ATOM    206  C   GLU A  34       9.027   0.914 -39.957  1.00 33.29           C  
ATOM    207  O   GLU A  34       9.705   1.120 -38.967  1.00 33.56           O  
ATOM    208  CB  GLU A  34      10.128   0.118 -42.094  1.00 33.53           C  
ATOM    209  CG  GLU A  34      11.283   1.096 -41.802  1.00 38.38           C  
ATOM    210  CD  GLU A  34      12.420   0.463 -41.003  1.00 41.63           C  
ATOM    211  OE1 GLU A  34      12.419  -0.785 -40.888  1.00 42.14           O  
ATOM    212  OE2 GLU A  34      13.299   1.203 -40.495  1.00 40.87           O  
ATOM    213  N   PHE A  35       8.042   1.728 -40.314  1.00 33.87           N  
ATOM    214  CA  PHE A  35       7.629   2.854 -39.477  1.00 33.72           C  
ATOM    215  C   PHE A  35       7.153   2.397 -38.063  1.00 33.82           C  
ATOM    216  O   PHE A  35       7.364   3.085 -37.073  1.00 33.43           O  
ATOM    217  CB  PHE A  35       6.534   3.621 -40.212  1.00 33.15           C  
ATOM    218  CG  PHE A  35       5.976   4.802 -39.459  1.00 34.03           C  
ATOM    219  CD1 PHE A  35       6.797   5.839 -39.028  1.00 34.13           C  
ATOM    220  CD2 PHE A  35       4.612   4.876 -39.203  1.00 33.55           C  
ATOM    221  CE1 PHE A  35       6.260   6.941 -38.344  1.00 35.08           C  
ATOM    222  CE2 PHE A  35       4.061   5.940 -38.531  1.00 31.89           C  
ATOM    223  CZ  PHE A  35       4.863   6.990 -38.110  1.00 34.70           C  
ATOM    224  N  AGLU A  36       6.577   1.205 -38.004  0.50 33.56           N  
ATOM    225  N  BGLU A  36       6.500   1.245 -37.986  0.50 34.00           N  
ATOM    226  CA AGLU A  36       5.938   0.709 -36.789  0.50 33.52           C  
ATOM    227  CA BGLU A  36       5.950   0.780 -36.709  0.50 34.39           C  
ATOM    228  C  AGLU A  36       6.742  -0.387 -36.083  0.50 33.45           C  
ATOM    229  C  BGLU A  36       6.725  -0.410 -36.105  0.50 33.91           C  
ATOM    230  O  AGLU A  36       6.239  -1.036 -35.171  0.50 33.28           O  
ATOM    231  O  BGLU A  36       6.188  -1.144 -35.284  0.50 33.65           O  
ATOM    232  CB AGLU A  36       4.560   0.173 -37.144  0.50 33.41           C  
ATOM    233  CB BGLU A  36       4.454   0.460 -36.855  0.50 34.67           C  
ATOM    234  CG AGLU A  36       3.779   1.082 -38.057  0.50 32.65           C  
ATOM    235  CG BGLU A  36       3.533   1.697 -36.927  0.50 36.93           C  
ATOM    236  CD AGLU A  36       2.308   0.908 -37.875  0.50 33.91           C  
ATOM    237  CD BGLU A  36       2.969   2.143 -35.573  0.50 40.31           C  
ATOM    238  OE1AGLU A  36       1.862  -0.264 -37.891  0.50 32.86           O  
ATOM    239  OE1BGLU A  36       3.400   1.634 -34.507  0.50 41.39           O  
ATOM    240  OE2AGLU A  36       1.613   1.937 -37.696  0.50 32.36           O  
ATOM    241  OE2BGLU A  36       2.075   3.021 -35.578  0.50 42.96           O  
ATOM    242  N   LYS A  37       7.985  -0.585 -36.507  1.00 33.37           N  
ATOM    243  CA  LYS A  37       8.837  -1.645 -35.944  1.00 33.60           C  
ATOM    244  C   LYS A  37       9.070  -1.429 -34.442  1.00 33.39           C  
ATOM    245  O   LYS A  37       9.128  -0.294 -33.972  1.00 31.69           O  
ATOM    246  CB  LYS A  37      10.177  -1.719 -36.649  1.00 33.34           C  
ATOM    247  CG  LYS A  37      11.096  -0.534 -36.393  1.00 35.60           C  
ATOM    248  CD  LYS A  37      12.363  -0.724 -37.188  1.00 39.98           C  
ATOM    249  CE  LYS A  37      13.283   0.476 -37.058  1.00 41.93           C  
ATOM    250  NZ  LYS A  37      14.451   0.246 -37.970  1.00 45.05           N  
ATOM    251  N   LYS A  38       9.187  -2.529 -33.706  1.00 33.43           N  
ATOM    252  CA  LYS A  38       9.373  -2.456 -32.264  1.00 34.07           C  
ATOM    253  C   LYS A  38      10.717  -3.073 -31.962  1.00 34.60           C  
ATOM    254  O   LYS A  38      11.030  -4.166 -32.446  1.00 35.01           O  
ATOM    255  CB  LYS A  38       8.244  -3.221 -31.555  1.00 34.78           C  
ATOM    256  CG  LYS A  38       6.853  -2.778 -31.974  1.00 35.56           C  
ATOM    257  CD  LYS A  38       5.781  -3.287 -31.044  1.00 41.47           C  
ATOM    258  CE  LYS A  38       5.755  -2.496 -29.740  1.00 43.80           C  
ATOM    259  NZ  LYS A  38       5.478  -1.053 -29.944  1.00 46.83           N  
ATOM    260  N   TYR A  39      11.532  -2.368 -31.199  1.00 34.48           N  
ATOM    261  CA  TYR A  39      12.851  -2.861 -30.874  1.00 34.80           C  
ATOM    262  C   TYR A  39      12.777  -3.659 -29.572  1.00 34.28           C  
ATOM    263  O   TYR A  39      12.275  -3.171 -28.565  1.00 33.55           O  
ATOM    264  CB  TYR A  39      13.843  -1.698 -30.717  1.00 35.57           C  
ATOM    265  CG  TYR A  39      15.209  -2.152 -30.236  1.00 36.47           C  
ATOM    266  CD1 TYR A  39      15.931  -3.100 -30.958  1.00 37.60           C  
ATOM    267  CD2 TYR A  39      15.765  -1.646 -29.061  1.00 37.87           C  
ATOM    268  CE1 TYR A  39      17.168  -3.530 -30.541  1.00 38.24           C  
ATOM    269  CE2 TYR A  39      17.012  -2.072 -28.626  1.00 38.53           C  
ATOM    270  CZ  TYR A  39      17.705  -3.017 -29.381  1.00 37.71           C  
ATOM    271  OH  TYR A  39      18.941  -3.461 -28.984  1.00 39.05           O  
ATOM    272  N   VAL A  40      13.265  -4.891 -29.611  1.00 34.15           N  
ATOM    273  CA  VAL A  40      13.207  -5.759 -28.450  1.00 34.27           C  
ATOM    274  C   VAL A  40      14.604  -5.825 -27.850  1.00 34.72           C  
ATOM    275  O   VAL A  40      15.428  -6.656 -28.242  1.00 34.05           O  
ATOM    276  CB  VAL A  40      12.664  -7.159 -28.787  1.00 33.59           C  
ATOM    277  CG1 VAL A  40      12.516  -7.975 -27.524  1.00 33.72           C  
ATOM    278  CG2 VAL A  40      11.328  -7.046 -29.482  1.00 33.81           C  
ATOM    279  N   ALA A  41      14.840  -4.939 -26.884  1.00 35.79           N  
ATOM    280  CA  ALA A  41      16.170  -4.730 -26.323  1.00 37.25           C  
ATOM    281  C   ALA A  41      16.815  -6.008 -25.781  1.00 37.99           C  
ATOM    282  O   ALA A  41      17.976  -6.293 -26.071  1.00 38.11           O  
ATOM    283  CB  ALA A  41      16.129  -3.645 -25.239  1.00 37.25           C  
ATOM    284  N   THR A  42      16.053  -6.778 -25.004  1.00 38.53           N  
ATOM    285  CA  THR A  42      16.582  -7.977 -24.344  1.00 38.75           C  
ATOM    286  C   THR A  42      17.004  -9.100 -25.321  1.00 38.38           C  
ATOM    287  O   THR A  42      17.816  -9.950 -24.965  1.00 38.78           O  
ATOM    288  CB  THR A  42      15.580  -8.519 -23.314  1.00 38.72           C  
ATOM    289  OG1 THR A  42      14.285  -8.599 -23.917  1.00 39.51           O  
ATOM    290  CG2 THR A  42      15.502  -7.582 -22.093  1.00 39.29           C  
ATOM    291  N   LEU A  43      16.484  -9.082 -26.546  1.00 37.84           N  
ATOM    292  CA  LEU A  43      16.732 -10.163 -27.522  1.00 37.30           C  
ATOM    293  C   LEU A  43      17.522  -9.762 -28.781  1.00 37.41           C  
ATOM    294  O   LEU A  43      17.862 -10.628 -29.604  1.00 37.55           O  
ATOM    295  CB  LEU A  43      15.406 -10.825 -27.940  1.00 36.66           C  
ATOM    296  CG  LEU A  43      14.588 -11.515 -26.841  1.00 36.96           C  
ATOM    297  CD1 LEU A  43      13.205 -11.888 -27.347  1.00 35.98           C  
ATOM    298  CD2 LEU A  43      15.312 -12.747 -26.270  1.00 35.44           C  
ATOM    299  N   GLY A  44      17.806  -8.467 -28.941  1.00 37.30           N  
ATOM    300  CA  GLY A  44      18.449  -7.968 -30.170  1.00 37.60           C  
ATOM    301  C   GLY A  44      17.604  -8.254 -31.400  1.00 38.03           C  
ATOM    302  O   GLY A  44      18.038  -8.959 -32.327  1.00 39.18           O  
ATOM    303  N   VAL A  45      16.378  -7.736 -31.402  1.00 36.67           N  
ATOM    304  CA  VAL A  45      15.428  -8.023 -32.465  1.00 36.01           C  
ATOM    305  C   VAL A  45      14.665  -6.742 -32.780  1.00 35.03           C  
ATOM    306  O   VAL A  45      14.382  -5.946 -31.892  1.00 34.78           O  
ATOM    307  CB  VAL A  45      14.410  -9.132 -32.038  1.00 36.10           C  
ATOM    308  CG1 VAL A  45      13.332  -9.370 -33.105  1.00 36.97           C  
ATOM    309  CG2 VAL A  45      15.114 -10.434 -31.715  1.00 36.08           C  
ATOM    310  N   GLU A  46      14.330  -6.545 -34.045  1.00 34.68           N  
ATOM    311  CA  GLU A  46      13.312  -5.581 -34.392  1.00 34.38           C  
ATOM    312  C   GLU A  46      12.171  -6.398 -34.944  1.00 33.76           C  
ATOM    313  O   GLU A  46      12.372  -7.195 -35.856  1.00 34.21           O  
ATOM    314  CB  GLU A  46      13.802  -4.596 -35.459  1.00 35.24           C  
ATOM    315  CG  GLU A  46      14.900  -3.626 -35.021  1.00 38.51           C  
ATOM    316  CD  GLU A  46      14.390  -2.273 -34.510  1.00 45.09           C  
ATOM    317  OE1 GLU A  46      13.214  -2.159 -34.105  1.00 46.44           O  
ATOM    318  OE2 GLU A  46      15.193  -1.308 -34.498  1.00 49.42           O  
ATOM    319  N   VAL A  47      10.980  -6.209 -34.384  1.00 32.77           N  
ATOM    320  CA  VAL A  47       9.761  -6.852 -34.872  1.00 31.65           C  
ATOM    321  C   VAL A  47       9.005  -5.911 -35.791  1.00 31.52           C  
ATOM    322  O   VAL A  47       8.601  -4.827 -35.374  1.00 30.24           O  
ATOM    323  CB  VAL A  47       8.807  -7.217 -33.720  1.00 31.38           C  
ATOM    324  CG1 VAL A  47       7.645  -8.053 -34.280  1.00 31.79           C  
ATOM    325  CG2 VAL A  47       9.557  -7.971 -32.619  1.00 29.55           C  
ATOM    326  N   HIS A  48       8.814  -6.334 -37.033  1.00 31.33           N  
ATOM    327  CA  HIS A  48       8.136  -5.503 -38.033  1.00 31.81           C  
ATOM    328  C   HIS A  48       6.727  -6.044 -38.252  1.00 32.14           C  
ATOM    329  O   HIS A  48       6.564  -7.163 -38.743  1.00 32.86           O  
ATOM    330  CB  HIS A  48       8.858  -5.570 -39.377  1.00 31.04           C  
ATOM    331  CG  HIS A  48      10.209  -4.933 -39.402  1.00 32.31           C  
ATOM    332  ND1 HIS A  48      11.272  -5.395 -38.653  1.00 32.31           N  
ATOM    333  CD2 HIS A  48      10.685  -3.899 -40.136  1.00 30.56           C  
ATOM    334  CE1 HIS A  48      12.342  -4.669 -38.915  1.00 29.97           C  
ATOM    335  NE2 HIS A  48      12.018  -3.767 -39.826  1.00 35.11           N  
ATOM    336  N   PRO A  49       5.708  -5.266 -37.883  1.00 33.25           N  
ATOM    337  CA  PRO A  49       4.317  -5.704 -38.049  1.00 33.61           C  
ATOM    338  C   PRO A  49       3.838  -5.477 -39.496  1.00 34.74           C  
ATOM    339  O   PRO A  49       3.531  -4.357 -39.882  1.00 35.02           O  
ATOM    340  CB  PRO A  49       3.550  -4.827 -37.036  1.00 34.40           C  
ATOM    341  CG  PRO A  49       4.399  -3.588 -36.843  1.00 33.27           C  
ATOM    342  CD  PRO A  49       5.822  -3.923 -37.267  1.00 32.45           C  
ATOM    343  N   LEU A  50       3.835  -6.538 -40.303  1.00 34.14           N  
ATOM    344  CA  LEU A  50       3.537  -6.422 -41.722  1.00 33.98           C  
ATOM    345  C   LEU A  50       2.104  -6.831 -41.930  1.00 33.90           C  
ATOM    346  O   LEU A  50       1.769  -8.005 -41.749  1.00 34.30           O  
ATOM    347  CB  LEU A  50       4.419  -7.367 -42.558  1.00 33.10           C  
ATOM    348  CG  LEU A  50       5.936  -7.311 -42.438  1.00 36.23           C  
ATOM    349  CD1 LEU A  50       6.557  -7.776 -43.749  1.00 33.54           C  
ATOM    350  CD2 LEU A  50       6.381  -5.886 -42.078  1.00 30.60           C  
ATOM    351  N   VAL A  51       1.269  -5.873 -42.303  1.00 33.23           N  
ATOM    352  CA  VAL A  51      -0.126  -6.147 -42.568  1.00 33.44           C  
ATOM    353  C   VAL A  51      -0.295  -6.400 -44.061  1.00 33.76           C  
ATOM    354  O   VAL A  51       0.227  -5.642 -44.875  1.00 34.27           O  
ATOM    355  CB  VAL A  51      -1.046  -4.984 -42.075  1.00 32.88           C  
ATOM    356  CG1 VAL A  51      -2.529  -5.297 -42.387  1.00 34.10           C  
ATOM    357  CG2 VAL A  51      -0.904  -4.806 -40.583  1.00 32.28           C  
ATOM    358  N   PHE A  52      -1.034  -7.450 -44.411  1.00 34.07           N  
ATOM    359  CA  PHE A  52      -1.375  -7.768 -45.805  1.00 33.84           C  
ATOM    360  C   PHE A  52      -2.876  -7.879 -45.883  1.00 33.65           C  
ATOM    361  O   PHE A  52      -3.539  -8.123 -44.870  1.00 33.82           O  
ATOM    362  CB  PHE A  52      -0.721  -9.102 -46.255  1.00 33.87           C  
ATOM    363  CG  PHE A  52       0.790  -9.018 -46.394  1.00 34.76           C  
ATOM    364  CD1 PHE A  52       1.624  -9.341 -45.325  1.00 34.82           C  
ATOM    365  CD2 PHE A  52       1.372  -8.590 -47.598  1.00 33.81           C  
ATOM    366  CE1 PHE A  52       3.033  -9.261 -45.444  1.00 33.66           C  
ATOM    367  CE2 PHE A  52       2.760  -8.483 -47.731  1.00 32.98           C  
ATOM    368  CZ  PHE A  52       3.604  -8.830 -46.655  1.00 35.52           C  
ATOM    369  N   HIS A  53      -3.424  -7.708 -47.080  1.00 33.37           N  
ATOM    370  CA  HIS A  53      -4.859  -7.597 -47.242  1.00 33.04           C  
ATOM    371  C   HIS A  53      -5.336  -8.612 -48.237  1.00 32.78           C  
ATOM    372  O   HIS A  53      -5.031  -8.498 -49.420  1.00 32.79           O  
ATOM    373  CB  HIS A  53      -5.210  -6.189 -47.699  1.00 34.12           C  
ATOM    374  CG  HIS A  53      -4.575  -5.131 -46.855  1.00 35.73           C  
ATOM    375  ND1 HIS A  53      -5.107  -4.727 -45.648  1.00 37.32           N  
ATOM    376  CD2 HIS A  53      -3.425  -4.434 -47.016  1.00 37.82           C  
ATOM    377  CE1 HIS A  53      -4.318  -3.811 -45.112  1.00 38.51           C  
ATOM    378  NE2 HIS A  53      -3.296  -3.611 -45.925  1.00 38.09           N  
ATOM    379  N   THR A  54      -6.058  -9.616 -47.732  1.00 31.45           N  
ATOM    380  CA  THR A  54      -6.485 -10.751 -48.522  1.00 29.77           C  
ATOM    381  C   THR A  54      -7.927 -10.535 -48.928  1.00 30.13           C  
ATOM    382  O   THR A  54      -8.593  -9.625 -48.434  1.00 30.66           O  
ATOM    383  CB  THR A  54      -6.366 -12.104 -47.750  1.00 28.93           C  
ATOM    384  OG1 THR A  54      -7.387 -12.183 -46.761  1.00 28.24           O  
ATOM    385  CG2 THR A  54      -5.032 -12.268 -47.056  1.00 26.72           C  
ATOM    386  N   ASN A  55      -8.403 -11.371 -49.840  1.00 29.75           N  
ATOM    387  CA  ASN A  55      -9.804 -11.396 -50.212  1.00 29.75           C  
ATOM    388  C   ASN A  55     -10.733 -11.735 -49.042  1.00 30.45           C  
ATOM    389  O   ASN A  55     -11.936 -11.554 -49.142  1.00 29.48           O  
ATOM    390  CB  ASN A  55     -10.030 -12.368 -51.372  1.00 28.87           C  
ATOM    391  CG  ASN A  55      -9.663 -13.796 -51.027  1.00 28.04           C  
ATOM    392  OD1 ASN A  55     -10.522 -14.686 -51.029  1.00 28.22           O  
ATOM    393  ND2 ASN A  55      -8.397 -14.030 -50.739  1.00 27.39           N  
ATOM    394  N   ARG A  56     -10.165 -12.229 -47.942  1.00 31.74           N  
ATOM    395  CA  ARG A  56     -10.959 -12.534 -46.750  1.00 33.18           C  
ATOM    396  C   ARG A  56     -10.589 -11.629 -45.580  1.00 32.93           C  
ATOM    397  O   ARG A  56     -11.000 -11.864 -44.456  1.00 34.03           O  
ATOM    398  CB  ARG A  56     -10.781 -13.994 -46.338  1.00 33.41           C  
ATOM    399  CG  ARG A  56     -11.238 -14.982 -47.370  1.00 35.85           C  
ATOM    400  CD  ARG A  56     -10.847 -16.378 -46.952  1.00 39.14           C  
ATOM    401  NE  ARG A  56     -11.746 -16.909 -45.923  1.00 41.69           N  
ATOM    402  CZ  ARG A  56     -11.682 -18.144 -45.433  1.00 42.00           C  
ATOM    403  NH1 ARG A  56     -12.551 -18.530 -44.505  1.00 43.76           N  
ATOM    404  NH2 ARG A  56     -10.764 -18.998 -45.875  1.00 42.17           N  
ATOM    405  N   GLY A  57      -9.804 -10.600 -45.839  1.00 32.69           N  
ATOM    406  CA  GLY A  57      -9.491  -9.635 -44.801  1.00 31.55           C  
ATOM    407  C   GLY A  57      -8.024  -9.554 -44.456  1.00 31.39           C  
ATOM    408  O   GLY A  57      -7.173 -10.226 -45.070  1.00 30.18           O  
ATOM    409  N   PRO A  58      -7.707  -8.682 -43.485  1.00 31.69           N  
ATOM    410  CA  PRO A  58      -6.323  -8.421 -43.161  1.00 31.65           C  
ATOM    411  C   PRO A  58      -5.661  -9.603 -42.496  1.00 31.91           C  
ATOM    412  O   PRO A  58      -6.312 -10.336 -41.771  1.00 31.89           O  
ATOM    413  CB  PRO A  58      -6.388  -7.230 -42.189  1.00 31.72           C  
ATOM    414  CG  PRO A  58      -7.764  -7.237 -41.636  1.00 31.95           C  
ATOM    415  CD  PRO A  58      -8.654  -7.886 -42.671  1.00 31.78           C  
ATOM    416  N   ILE A  59      -4.373  -9.768 -42.764  1.00 32.41           N  
ATOM    417  CA  ILE A  59      -3.540 -10.706 -42.045  1.00 33.63           C  
ATOM    418  C   ILE A  59      -2.283  -9.960 -41.592  1.00 32.46           C  
ATOM    419  O   ILE A  59      -1.717  -9.192 -42.357  1.00 32.96           O  
ATOM    420  CB  ILE A  59      -3.181 -11.929 -42.912  1.00 33.32           C  
ATOM    421  CG1 ILE A  59      -2.505 -13.010 -42.068  1.00 36.45           C  
ATOM    422  CG2 ILE A  59      -2.269 -11.550 -44.056  1.00 32.84           C  
ATOM    423  CD1 ILE A  59      -2.476 -14.414 -42.761  1.00 35.55           C  
ATOM    424  N   LYS A  60      -1.837 -10.204 -40.368  1.00 31.57           N  
ATOM    425  CA  LYS A  60      -0.621  -9.542 -39.845  1.00 31.73           C  
ATOM    426  C   LYS A  60       0.479 -10.550 -39.553  1.00 31.40           C  
ATOM    427  O   LYS A  60       0.276 -11.492 -38.781  1.00 30.39           O  
ATOM    428  CB  LYS A  60      -0.961  -8.815 -38.566  1.00 32.05           C  
ATOM    429  CG  LYS A  60       0.067  -7.804 -38.075  1.00 33.58           C  
ATOM    430  CD  LYS A  60      -0.521  -7.157 -36.843  1.00 36.20           C  
ATOM    431  CE  LYS A  60       0.130  -5.856 -36.511  1.00 42.43           C  
ATOM    432  NZ  LYS A  60       0.143  -5.701 -35.027  1.00 45.27           N  
ATOM    433  N   PHE A  61       1.638 -10.349 -40.169  1.00 30.97           N  
ATOM    434  CA  PHE A  61       2.809 -11.153 -39.874  1.00 31.64           C  
ATOM    435  C   PHE A  61       3.721 -10.269 -39.039  1.00 31.42           C  
ATOM    436  O   PHE A  61       4.094  -9.183 -39.485  1.00 31.28           O  
ATOM    437  CB  PHE A  61       3.511 -11.519 -41.175  1.00 31.80           C  
ATOM    438  CG  PHE A  61       2.818 -12.614 -41.962  1.00 34.39           C  
ATOM    439  CD1 PHE A  61       2.831 -13.928 -41.508  1.00 33.30           C  
ATOM    440  CD2 PHE A  61       2.160 -12.323 -43.165  1.00 34.47           C  
ATOM    441  CE1 PHE A  61       2.189 -14.957 -42.221  1.00 34.66           C  
ATOM    442  CE2 PHE A  61       1.523 -13.348 -43.881  1.00 33.70           C  
ATOM    443  CZ  PHE A  61       1.544 -14.656 -43.406  1.00 34.50           C  
ATOM    444  N   ASN A  62       4.039 -10.680 -37.823  1.00 30.85           N  
ATOM    445  CA  ASN A  62       5.020  -9.918 -37.033  1.00 31.03           C  
ATOM    446  C   ASN A  62       6.354 -10.547 -37.308  1.00 31.01           C  
ATOM    447  O   ASN A  62       6.641 -11.631 -36.822  1.00 31.15           O  
ATOM    448  CB  ASN A  62       4.684  -9.933 -35.540  1.00 30.30           C  
ATOM    449  CG  ASN A  62       3.355  -9.246 -35.241  1.00 30.58           C  
ATOM    450  OD1 ASN A  62       2.535  -9.741 -34.473  1.00 32.94           O  
ATOM    451  ND2 ASN A  62       3.122  -8.128 -35.891  1.00 28.54           N  
ATOM    452  N   VAL A  63       7.138  -9.884 -38.143  1.00 31.26           N  
ATOM    453  CA  VAL A  63       8.393 -10.436 -38.627  1.00 31.19           C  
ATOM    454  C   VAL A  63       9.567 -10.088 -37.735  1.00 30.82           C  
ATOM    455  O   VAL A  63       9.858  -8.928 -37.545  1.00 30.68           O  
ATOM    456  CB  VAL A  63       8.703  -9.979 -40.056  1.00 31.31           C  
ATOM    457  CG1 VAL A  63      10.061 -10.532 -40.485  1.00 32.50           C  
ATOM    458  CG2 VAL A  63       7.595 -10.455 -41.023  1.00 31.44           C  
ATOM    459  N   TRP A  64      10.235 -11.110 -37.200  1.00 30.93           N  
ATOM    460  CA  TRP A  64      11.379 -10.914 -36.311  1.00 31.11           C  
ATOM    461  C   TRP A  64      12.679 -10.860 -37.092  1.00 32.41           C  
ATOM    462  O   TRP A  64      13.081 -11.839 -37.699  1.00 34.08           O  
ATOM    463  CB  TRP A  64      11.440 -12.019 -35.264  1.00 29.35           C  
ATOM    464  CG  TRP A  64      10.352 -11.885 -34.203  1.00 26.79           C  
ATOM    465  CD1 TRP A  64       9.023 -11.647 -34.414  1.00 25.42           C  
ATOM    466  CD2 TRP A  64      10.523 -11.981 -32.788  1.00 24.74           C  
ATOM    467  NE1 TRP A  64       8.358 -11.588 -33.212  1.00 24.30           N  
ATOM    468  CE2 TRP A  64       9.257 -11.808 -32.201  1.00 22.71           C  
ATOM    469  CE3 TRP A  64      11.629 -12.223 -31.956  1.00 23.03           C  
ATOM    470  CZ2 TRP A  64       9.069 -11.833 -30.839  1.00 23.96           C  
ATOM    471  CZ3 TRP A  64      11.436 -12.263 -30.606  1.00 26.35           C  
ATOM    472  CH2 TRP A  64      10.169 -12.063 -30.049  1.00 27.04           C  
ATOM    473  N   ASP A  65      13.320  -9.697 -37.092  1.00 32.79           N  
ATOM    474  CA  ASP A  65      14.567  -9.517 -37.822  1.00 33.41           C  
ATOM    475  C   ASP A  65      15.687  -9.364 -36.816  1.00 32.80           C  
ATOM    476  O   ASP A  65      15.549  -8.642 -35.804  1.00 32.76           O  
ATOM    477  CB  ASP A  65      14.483  -8.301 -38.764  1.00 33.32           C  
ATOM    478  CG  ASP A  65      15.723  -8.169 -39.692  1.00 35.83           C  
ATOM    479  OD1 ASP A  65      16.234  -9.196 -40.248  1.00 37.20           O  
ATOM    480  OD2 ASP A  65      16.177  -7.014 -39.850  1.00 34.98           O  
ATOM    481  N   THR A  66      16.794 -10.057 -37.065  1.00 32.26           N  
ATOM    482  CA  THR A  66      17.925  -9.965 -36.157  1.00 32.83           C  
ATOM    483  C   THR A  66      18.567  -8.577 -36.262  1.00 32.66           C  
ATOM    484  O   THR A  66      18.284  -7.818 -37.201  1.00 32.07           O  
ATOM    485  CB  THR A  66      18.982 -11.023 -36.484  1.00 33.31           C  
ATOM    486  OG1 THR A  66      19.678 -10.613 -37.658  1.00 32.66           O  
ATOM    487  CG2 THR A  66      18.339 -12.391 -36.735  1.00 33.54           C  
ATOM    488  N   ALA A  67      19.393  -8.240 -35.277  1.00 32.82           N  
ATOM    489  CA  ALA A  67      20.247  -7.055 -35.309  1.00 33.63           C  
ATOM    490  C   ALA A  67      21.672  -7.492 -35.652  1.00 34.39           C  
ATOM    491  O   ALA A  67      22.645  -6.898 -35.160  1.00 35.32           O  
ATOM    492  CB  ALA A  67      20.240  -6.353 -33.932  1.00 33.71           C  
ATOM    493  N   GLY A  68      21.799  -8.571 -36.428  1.00 34.22           N  
ATOM    494  CA  GLY A  68      23.074  -8.992 -36.979  1.00 34.35           C  
ATOM    495  C   GLY A  68      23.858 -10.029 -36.198  1.00 35.26           C  
ATOM    496  O   GLY A  68      24.965 -10.381 -36.605  1.00 35.15           O  
ATOM    497  N   GLN A  69      23.305 -10.530 -35.091  1.00 35.34           N  
ATOM    498  CA  GLN A  69      24.057 -11.440 -34.234  1.00 36.24           C  
ATOM    499  C   GLN A  69      24.281 -12.818 -34.846  1.00 36.15           C  
ATOM    500  O   GLN A  69      25.188 -13.521 -34.421  1.00 34.98           O  
ATOM    501  CB  GLN A  69      23.488 -11.532 -32.806  1.00 36.85           C  
ATOM    502  CG  GLN A  69      22.091 -12.066 -32.710  1.00 38.89           C  
ATOM    503  CD  GLN A  69      21.013 -11.001 -32.861  1.00 42.16           C  
ATOM    504  OE1 GLN A  69      21.143 -10.048 -33.639  1.00 40.83           O  
ATOM    505  NE2 GLN A  69      19.916 -11.184 -32.132  1.00 42.87           N  
ATOM    506  N   GLU A  70      23.502 -13.178 -35.871  1.00 36.13           N  
ATOM    507  CA  GLU A  70      23.739 -14.432 -36.606  1.00 36.42           C  
ATOM    508  C   GLU A  70      25.116 -14.473 -37.291  1.00 37.27           C  
ATOM    509  O   GLU A  70      25.577 -15.528 -37.717  1.00 37.30           O  
ATOM    510  CB  GLU A  70      22.636 -14.699 -37.630  1.00 35.94           C  
ATOM    511  CG  GLU A  70      22.719 -13.842 -38.887  1.00 36.21           C  
ATOM    512  CD  GLU A  70      22.104 -12.442 -38.723  1.00 35.92           C  
ATOM    513  OE1 GLU A  70      21.850 -12.006 -37.571  1.00 35.17           O  
ATOM    514  OE2 GLU A  70      21.873 -11.779 -39.755  1.00 35.96           O  
ATOM    515  N   LYS A  71      25.757 -13.321 -37.416  1.00 38.06           N  
ATOM    516  CA  LYS A  71      27.112 -13.276 -37.931  1.00 39.57           C  
ATOM    517  C   LYS A  71      28.107 -13.819 -36.906  1.00 39.76           C  
ATOM    518  O   LYS A  71      29.105 -14.428 -37.274  1.00 40.58           O  
ATOM    519  CB  LYS A  71      27.458 -11.858 -38.371  1.00 39.33           C  
ATOM    520  CG  LYS A  71      26.452 -11.372 -39.400  1.00 42.20           C  
ATOM    521  CD  LYS A  71      26.861 -10.112 -40.099  1.00 45.68           C  
ATOM    522  CE  LYS A  71      26.102  -8.925 -39.575  1.00 46.01           C  
ATOM    523  NZ  LYS A  71      25.864  -8.012 -40.726  1.00 46.14           N  
ATOM    524  N   PHE A  72      27.806 -13.646 -35.622  1.00 40.26           N  
ATOM    525  CA  PHE A  72      28.768 -13.935 -34.549  1.00 40.41           C  
ATOM    526  C   PHE A  72      28.432 -15.178 -33.745  1.00 40.00           C  
ATOM    527  O   PHE A  72      29.306 -15.772 -33.145  1.00 39.89           O  
ATOM    528  CB  PHE A  72      28.908 -12.713 -33.631  1.00 41.04           C  
ATOM    529  CG  PHE A  72      29.038 -11.423 -34.388  1.00 43.12           C  
ATOM    530  CD1 PHE A  72      27.973 -10.528 -34.450  1.00 44.96           C  
ATOM    531  CD2 PHE A  72      30.213 -11.122 -35.081  1.00 45.53           C  
ATOM    532  CE1 PHE A  72      28.075  -9.344 -35.184  1.00 46.35           C  
ATOM    533  CE2 PHE A  72      30.327  -9.936 -35.822  1.00 47.02           C  
ATOM    534  CZ  PHE A  72      29.256  -9.047 -35.873  1.00 45.14           C  
ATOM    535  N   GLY A  73      27.172 -15.582 -33.738  1.00 39.72           N  
ATOM    536  CA  GLY A  73      26.774 -16.764 -32.986  1.00 39.70           C  
ATOM    537  C   GLY A  73      25.362 -17.191 -33.314  1.00 39.81           C  
ATOM    538  O   GLY A  73      24.760 -16.689 -34.256  1.00 39.17           O  
ATOM    539  N   GLY A  74      24.836 -18.128 -32.528  1.00 40.27           N  
ATOM    540  CA  GLY A  74      23.453 -18.570 -32.706  1.00 40.39           C  
ATOM    541  C   GLY A  74      22.450 -17.649 -32.034  1.00 40.24           C  
ATOM    542  O   GLY A  74      22.774 -16.941 -31.075  1.00 40.20           O  
ATOM    543  N   LEU A  75      21.224 -17.671 -32.542  1.00 40.24           N  
ATOM    544  CA  LEU A  75      20.137 -16.860 -32.007  1.00 40.16           C  
ATOM    545  C   LEU A  75      19.630 -17.437 -30.697  1.00 40.72           C  
ATOM    546  O   LEU A  75      19.612 -18.660 -30.519  1.00 40.69           O  
ATOM    547  CB  LEU A  75      18.996 -16.803 -33.024  1.00 39.86           C  
ATOM    548  CG  LEU A  75      19.417 -16.402 -34.434  1.00 38.31           C  
ATOM    549  CD1 LEU A  75      18.247 -16.473 -35.382  1.00 38.82           C  
ATOM    550  CD2 LEU A  75      20.005 -15.003 -34.401  1.00 37.94           C  
ATOM    551  N   ARG A  76      19.219 -16.561 -29.779  1.00 41.17           N  
ATOM    552  CA  ARG A  76      18.634 -17.000 -28.505  1.00 42.05           C  
ATOM    553  C   ARG A  76      17.379 -17.852 -28.746  1.00 40.99           C  
ATOM    554  O   ARG A  76      16.732 -17.719 -29.770  1.00 40.20           O  
ATOM    555  CB  ARG A  76      18.260 -15.789 -27.633  1.00 42.44           C  
ATOM    556  CG  ARG A  76      19.432 -15.017 -27.006  1.00 43.70           C  
ATOM    557  CD  ARG A  76      18.919 -13.763 -26.263  1.00 44.20           C  
ATOM    558  NE  ARG A  76      18.994 -13.855 -24.798  1.00 47.39           N  
ATOM    559  CZ  ARG A  76      18.058 -14.372 -23.992  1.00 48.68           C  
ATOM    560  NH1 ARG A  76      16.925 -14.890 -24.470  1.00 50.19           N  
ATOM    561  NH2 ARG A  76      18.269 -14.385 -22.682  1.00 48.98           N  
ATOM    562  N   ASP A  77      17.033 -18.717 -27.798  1.00 40.55           N  
ATOM    563  CA  ASP A  77      15.725 -19.385 -27.819  1.00 39.99           C  
ATOM    564  C   ASP A  77      14.552 -18.392 -27.898  1.00 38.94           C  
ATOM    565  O   ASP A  77      13.605 -18.601 -28.655  1.00 38.75           O  
ATOM    566  CB  ASP A  77      15.563 -20.267 -26.591  1.00 40.86           C  
ATOM    567  CG  ASP A  77      16.405 -21.532 -26.659  1.00 42.67           C  
ATOM    568  OD1 ASP A  77      16.642 -22.037 -27.786  1.00 44.68           O  
ATOM    569  OD2 ASP A  77      16.809 -22.028 -25.578  1.00 45.41           O  
ATOM    570  N   GLY A  78      14.625 -17.310 -27.123  1.00 37.73           N  
ATOM    571  CA  GLY A  78      13.571 -16.300 -27.092  1.00 36.52           C  
ATOM    572  C   GLY A  78      13.211 -15.796 -28.478  1.00 35.96           C  
ATOM    573  O   GLY A  78      12.055 -15.424 -28.738  1.00 35.84           O  
ATOM    574  N   TYR A  79      14.205 -15.795 -29.370  1.00 35.26           N  
ATOM    575  CA  TYR A  79      14.011 -15.423 -30.772  1.00 34.71           C  
ATOM    576  C   TYR A  79      12.983 -16.327 -31.467  1.00 34.54           C  
ATOM    577  O   TYR A  79      12.160 -15.862 -32.241  1.00 34.84           O  
ATOM    578  CB  TYR A  79      15.350 -15.443 -31.534  1.00 34.65           C  
ATOM    579  CG  TYR A  79      15.186 -15.012 -32.961  1.00 33.70           C  
ATOM    580  CD1 TYR A  79      15.258 -13.670 -33.313  1.00 34.10           C  
ATOM    581  CD2 TYR A  79      14.909 -15.937 -33.956  1.00 32.67           C  
ATOM    582  CE1 TYR A  79      15.080 -13.254 -34.636  1.00 32.90           C  
ATOM    583  CE2 TYR A  79      14.715 -15.540 -35.275  1.00 34.46           C  
ATOM    584  CZ  TYR A  79      14.809 -14.201 -35.607  1.00 34.68           C  
ATOM    585  OH  TYR A  79      14.620 -13.822 -36.919  1.00 38.06           O  
ATOM    586  N   TYR A  80      13.039 -17.619 -31.167  1.00 34.47           N  
ATOM    587  CA  TYR A  80      12.163 -18.623 -31.773  1.00 34.38           C  
ATOM    588  C   TYR A  80      10.847 -18.890 -31.029  1.00 33.15           C  
ATOM    589  O   TYR A  80       9.968 -19.547 -31.560  1.00 33.41           O  
ATOM    590  CB  TYR A  80      12.909 -19.950 -31.901  1.00 35.28           C  
ATOM    591  CG  TYR A  80      14.071 -19.933 -32.868  1.00 37.25           C  
ATOM    592  CD1 TYR A  80      15.388 -20.011 -32.410  1.00 37.88           C  
ATOM    593  CD2 TYR A  80      13.855 -19.861 -34.235  1.00 38.17           C  
ATOM    594  CE1 TYR A  80      16.457 -20.015 -33.299  1.00 38.06           C  
ATOM    595  CE2 TYR A  80      14.920 -19.859 -35.130  1.00 39.06           C  
ATOM    596  CZ  TYR A  80      16.211 -19.942 -34.653  1.00 38.69           C  
ATOM    597  OH  TYR A  80      17.252 -19.934 -35.556  1.00 40.07           O  
ATOM    598  N   ILE A  81      10.702 -18.400 -29.810  1.00 31.93           N  
ATOM    599  CA  ILE A  81       9.519 -18.749 -29.027  1.00 30.82           C  
ATOM    600  C   ILE A  81       8.217 -18.242 -29.686  1.00 29.90           C  
ATOM    601  O   ILE A  81       8.119 -17.084 -30.058  1.00 28.72           O  
ATOM    602  CB  ILE A  81       9.692 -18.354 -27.553  1.00 31.08           C  
ATOM    603  CG1 ILE A  81      10.521 -19.448 -26.860  1.00 32.54           C  
ATOM    604  CG2 ILE A  81       8.343 -18.219 -26.843  1.00 31.71           C  
ATOM    605  CD1 ILE A  81      11.292 -19.022 -25.624  1.00 34.50           C  
ATOM    606  N  AGLN A  82       7.278 -19.174 -29.844  0.50 29.74           N  
ATOM    607  N  BGLN A  82       7.233 -19.131 -29.822  0.50 29.42           N  
ATOM    608  CA AGLN A  82       5.947 -18.947 -30.418  0.50 29.88           C  
ATOM    609  CA BGLN A  82       5.912 -18.825 -30.418  0.50 29.14           C  
ATOM    610  C  AGLN A  82       5.964 -18.495 -31.877  0.50 30.03           C  
ATOM    611  C  BGLN A  82       5.940 -18.507 -31.916  0.50 29.65           C  
ATOM    612  O  AGLN A  82       5.013 -17.861 -32.344  0.50 30.11           O  
ATOM    613  O  BGLN A  82       4.964 -17.980 -32.458  0.50 29.69           O  
ATOM    614  CB AGLN A  82       5.095 -18.016 -29.540  0.50 29.89           C  
ATOM    615  CB BGLN A  82       5.148 -17.727 -29.647  0.50 29.08           C  
ATOM    616  CG AGLN A  82       4.874 -18.503 -28.092  0.50 30.07           C  
ATOM    617  CG BGLN A  82       3.718 -17.501 -30.183  0.50 28.90           C  
ATOM    618  CD AGLN A  82       4.010 -19.769 -27.947  0.50 30.50           C  
ATOM    619  CD BGLN A  82       2.867 -16.608 -29.313  0.50 27.74           C  
ATOM    620  OE1AGLN A  82       3.548 -20.360 -28.929  0.50 30.85           O  
ATOM    621  OE1BGLN A  82       2.445 -17.002 -28.225  0.50 25.13           O  
ATOM    622  NE2AGLN A  82       3.804 -20.185 -26.706  0.50 28.75           N  
ATOM    623  NE2BGLN A  82       2.588 -15.406 -29.799  0.50 24.62           N  
ATOM    624  N   ALA A  83       7.037 -18.841 -32.592  1.00 29.80           N  
ATOM    625  CA  ALA A  83       7.117 -18.606 -34.032  1.00 30.39           C  
ATOM    626  C   ALA A  83       6.098 -19.517 -34.677  1.00 30.46           C  
ATOM    627  O   ALA A  83       6.026 -20.692 -34.348  1.00 30.87           O  
ATOM    628  CB  ALA A  83       8.514 -18.919 -34.566  1.00 30.46           C  
ATOM    629  N   GLN A  84       5.298 -18.976 -35.577  1.00 30.90           N  
ATOM    630  CA  GLN A  84       4.255 -19.783 -36.181  1.00 31.44           C  
ATOM    631  C   GLN A  84       4.502 -20.029 -37.652  1.00 31.60           C  
ATOM    632  O   GLN A  84       3.795 -20.815 -38.264  1.00 31.74           O  
ATOM    633  CB  GLN A  84       2.909 -19.129 -35.975  1.00 31.85           C  
ATOM    634  CG  GLN A  84       2.428 -19.201 -34.537  1.00 30.85           C  
ATOM    635  CD  GLN A  84       1.531 -18.039 -34.254  1.00 33.34           C  
ATOM    636  OE1 GLN A  84       1.990 -16.879 -34.145  1.00 31.69           O  
ATOM    637  NE2 GLN A  84       0.235 -18.313 -34.201  1.00 31.52           N  
ATOM    638  N   CYS A  85       5.501 -19.345 -38.206  1.00 30.91           N  
ATOM    639  CA  CYS A  85       5.970 -19.595 -39.553  1.00 30.96           C  
ATOM    640  C   CYS A  85       7.372 -18.994 -39.691  1.00 30.82           C  
ATOM    641  O   CYS A  85       7.847 -18.313 -38.779  1.00 31.34           O  
ATOM    642  CB  CYS A  85       4.999 -19.004 -40.575  1.00 31.15           C  
ATOM    643  SG  CYS A  85       4.691 -17.241 -40.301  1.00 33.40           S  
ATOM    644  N   ALA A  86       8.034 -19.257 -40.815  1.00 29.98           N  
ATOM    645  CA  ALA A  86       9.402 -18.834 -41.007  1.00 29.84           C  
ATOM    646  C   ALA A  86       9.713 -18.626 -42.472  1.00 30.77           C  
ATOM    647  O   ALA A  86       9.118 -19.253 -43.352  1.00 30.60           O  
ATOM    648  CB  ALA A  86      10.374 -19.854 -40.412  1.00 30.20           C  
ATOM    649  N   ILE A  87      10.637 -17.703 -42.717  1.00 30.94           N  
ATOM    650  CA  ILE A  87      11.328 -17.593 -43.980  1.00 30.19           C  
ATOM    651  C   ILE A  87      12.805 -17.799 -43.700  1.00 30.84           C  
ATOM    652  O   ILE A  87      13.367 -17.165 -42.802  1.00 30.45           O  
ATOM    653  CB  ILE A  87      11.152 -16.191 -44.592  1.00 30.41           C  
ATOM    654  CG1 ILE A  87       9.685 -15.952 -44.988  1.00 29.83           C  
ATOM    655  CG2 ILE A  87      12.108 -16.030 -45.798  1.00 28.84           C  
ATOM    656  CD1 ILE A  87       9.336 -14.456 -45.221  1.00 27.89           C  
ATOM    657  N   ILE A  88      13.416 -18.722 -44.439  1.00 31.75           N  
ATOM    658  CA  ILE A  88      14.878 -18.896 -44.467  1.00 31.80           C  
ATOM    659  C   ILE A  88      15.375 -18.220 -45.741  1.00 32.36           C  
ATOM    660  O   ILE A  88      14.884 -18.507 -46.839  1.00 32.18           O  
ATOM    661  CB  ILE A  88      15.294 -20.377 -44.546  1.00 31.23           C  
ATOM    662  CG1 ILE A  88      14.755 -21.171 -43.361  1.00 31.21           C  
ATOM    663  CG2 ILE A  88      16.828 -20.523 -44.588  1.00 31.82           C  
ATOM    664  CD1 ILE A  88      14.764 -22.669 -43.598  1.00 29.37           C  
ATOM    665  N   MET A  89      16.353 -17.335 -45.601  1.00 33.20           N  
ATOM    666  CA  MET A  89      16.877 -16.598 -46.739  1.00 34.67           C  
ATOM    667  C   MET A  89      18.264 -17.088 -47.082  1.00 33.44           C  
ATOM    668  O   MET A  89      18.989 -17.614 -46.226  1.00 33.34           O  
ATOM    669  CB  MET A  89      16.891 -15.096 -46.455  1.00 33.62           C  
ATOM    670  CG  MET A  89      17.071 -14.270 -47.714  1.00 35.94           C  
ATOM    671  SD  MET A  89      16.180 -12.718 -47.709  1.00 41.95           S  
ATOM    672  CE  MET A  89      14.524 -13.334 -47.551  1.00 36.57           C  
ATOM    673  N   PHE A  90      18.611 -16.971 -48.354  1.00 33.15           N  
ATOM    674  CA  PHE A  90      19.994 -17.135 -48.767  1.00 33.08           C  
ATOM    675  C   PHE A  90      20.337 -16.178 -49.886  1.00 33.49           C  
ATOM    676  O   PHE A  90      19.471 -15.448 -50.406  1.00 33.27           O  
ATOM    677  CB  PHE A  90      20.377 -18.601 -49.053  1.00 33.41           C  
ATOM    678  CG  PHE A  90      19.723 -19.201 -50.269  1.00 32.91           C  
ATOM    679  CD1 PHE A  90      20.377 -19.206 -51.490  1.00 33.08           C  
ATOM    680  CD2 PHE A  90      18.468 -19.789 -50.176  1.00 32.00           C  
ATOM    681  CE1 PHE A  90      19.784 -19.770 -52.612  1.00 34.09           C  
ATOM    682  CE2 PHE A  90      17.872 -20.368 -51.278  1.00 32.81           C  
ATOM    683  CZ  PHE A  90      18.534 -20.362 -52.509  1.00 31.98           C  
ATOM    684  N   ASP A  91      21.609 -16.141 -50.225  1.00 33.35           N  
ATOM    685  CA  ASP A  91      22.083 -15.209 -51.220  1.00 33.71           C  
ATOM    686  C   ASP A  91      22.502 -16.042 -52.432  1.00 33.37           C  
ATOM    687  O   ASP A  91      23.387 -16.899 -52.361  1.00 33.45           O  
ATOM    688  CB  ASP A  91      23.229 -14.391 -50.627  1.00 34.00           C  
ATOM    689  CG  ASP A  91      23.873 -13.446 -51.608  1.00 36.00           C  
ATOM    690  OD1 ASP A  91      23.557 -13.464 -52.836  1.00 38.10           O  
ATOM    691  OD2 ASP A  91      24.730 -12.663 -51.126  1.00 39.02           O  
ATOM    692  N   VAL A  92      21.826 -15.769 -53.544  1.00 33.46           N  
ATOM    693  CA  VAL A  92      21.947 -16.519 -54.779  1.00 33.05           C  
ATOM    694  C   VAL A  92      23.349 -16.352 -55.434  1.00 33.33           C  
ATOM    695  O   VAL A  92      23.722 -17.096 -56.342  1.00 33.60           O  
ATOM    696  CB  VAL A  92      20.712 -16.137 -55.651  1.00 33.91           C  
ATOM    697  CG1 VAL A  92      21.056 -15.515 -57.001  1.00 32.45           C  
ATOM    698  CG2 VAL A  92      19.674 -17.261 -55.684  1.00 33.15           C  
ATOM    699  N   THR A  93      24.131 -15.400 -54.913  1.00 33.26           N  
ATOM    700  CA  THR A  93      25.494 -15.096 -55.377  1.00 33.41           C  
ATOM    701  C   THR A  93      26.568 -15.595 -54.411  1.00 33.81           C  
ATOM    702  O   THR A  93      27.761 -15.375 -54.644  1.00 33.83           O  
ATOM    703  CB  THR A  93      25.699 -13.569 -55.587  1.00 33.94           C  
ATOM    704  OG1 THR A  93      25.632 -12.880 -54.325  1.00 35.53           O  
ATOM    705  CG2 THR A  93      24.619 -12.995 -56.537  1.00 32.69           C  
ATOM    706  N   SER A  94      26.146 -16.265 -53.336  1.00 33.19           N  
ATOM    707  CA  SER A  94      27.074 -16.767 -52.339  1.00 33.38           C  
ATOM    708  C   SER A  94      26.680 -18.191 -51.969  1.00 33.46           C  
ATOM    709  O   SER A  94      25.655 -18.418 -51.324  1.00 34.06           O  
ATOM    710  CB  SER A  94      27.110 -15.834 -51.129  1.00 32.97           C  
ATOM    711  OG  SER A  94      27.855 -16.379 -50.061  1.00 34.67           O  
ATOM    712  N   ARG A  95      27.484 -19.148 -52.414  1.00 33.15           N  
ATOM    713  CA  ARG A  95      27.136 -20.553 -52.264  1.00 33.50           C  
ATOM    714  C   ARG A  95      27.095 -21.039 -50.821  1.00 33.10           C  
ATOM    715  O   ARG A  95      26.219 -21.827 -50.469  1.00 33.13           O  
ATOM    716  CB  ARG A  95      28.038 -21.433 -53.118  1.00 33.56           C  
ATOM    717  CG  ARG A  95      27.401 -21.730 -54.455  1.00 35.39           C  
ATOM    718  CD  ARG A  95      28.243 -22.683 -55.277  1.00 40.10           C  
ATOM    719  NE  ARG A  95      29.216 -21.949 -56.081  1.00 42.55           N  
ATOM    720  CZ  ARG A  95      29.018 -21.578 -57.343  1.00 43.95           C  
ATOM    721  NH1 ARG A  95      29.962 -20.909 -58.001  1.00 45.33           N  
ATOM    722  NH2 ARG A  95      27.882 -21.887 -57.955  1.00 44.04           N  
ATOM    723  N   VAL A  96      28.019 -20.552 -49.992  1.00 32.79           N  
ATOM    724  CA  VAL A  96      28.016 -20.884 -48.564  1.00 32.55           C  
ATOM    725  C   VAL A  96      26.662 -20.614 -47.906  1.00 31.74           C  
ATOM    726  O   VAL A  96      26.222 -21.385 -47.064  1.00 32.12           O  
ATOM    727  CB  VAL A  96      29.182 -20.182 -47.772  1.00 32.66           C  
ATOM    728  CG1 VAL A  96      28.962 -18.669 -47.655  1.00 33.42           C  
ATOM    729  CG2 VAL A  96      29.327 -20.795 -46.399  1.00 34.19           C  
ATOM    730  N   THR A  97      25.985 -19.538 -48.300  1.00 30.97           N  
ATOM    731  CA  THR A  97      24.726 -19.204 -47.663  1.00 30.18           C  
ATOM    732  C   THR A  97      23.652 -20.220 -48.000  1.00 30.38           C  
ATOM    733  O   THR A  97      22.787 -20.515 -47.172  1.00 30.55           O  
ATOM    734  CB  THR A  97      24.222 -17.787 -47.989  1.00 29.55           C  
ATOM    735  OG1 THR A  97      23.800 -17.713 -49.354  1.00 28.09           O  
ATOM    736  CG2 THR A  97      25.312 -16.761 -47.712  1.00 28.97           C  
ATOM    737  N   TYR A  98      23.711 -20.746 -49.216  1.00 30.38           N  
ATOM    738  CA  TYR A  98      22.798 -21.787 -49.630  1.00 30.44           C  
ATOM    739  C   TYR A  98      23.127 -23.118 -48.958  1.00 30.32           C  
ATOM    740  O   TYR A  98      22.243 -23.895 -48.634  1.00 30.49           O  
ATOM    741  CB  TYR A  98      22.814 -21.955 -51.141  1.00 31.23           C  
ATOM    742  CG  TYR A  98      21.899 -23.057 -51.589  1.00 32.41           C  
ATOM    743  CD1 TYR A  98      20.521 -22.963 -51.375  1.00 33.98           C  
ATOM    744  CD2 TYR A  98      22.404 -24.211 -52.180  1.00 35.06           C  
ATOM    745  CE1 TYR A  98      19.667 -23.973 -51.769  1.00 34.35           C  
ATOM    746  CE2 TYR A  98      21.559 -25.232 -52.581  1.00 34.89           C  
ATOM    747  CZ  TYR A  98      20.198 -25.099 -52.377  1.00 34.16           C  
ATOM    748  OH  TYR A  98      19.344 -26.090 -52.770  1.00 34.65           O  
ATOM    749  N   LYS A  99      24.403 -23.376 -48.740  1.00 30.25           N  
ATOM    750  CA  LYS A  99      24.803 -24.628 -48.111  1.00 30.23           C  
ATOM    751  C   LYS A  99      24.415 -24.702 -46.640  1.00 29.75           C  
ATOM    752  O   LYS A  99      24.381 -25.775 -46.059  1.00 29.98           O  
ATOM    753  CB  LYS A  99      26.295 -24.854 -48.282  1.00 30.69           C  
ATOM    754  CG  LYS A  99      26.663 -25.403 -49.650  1.00 32.77           C  
ATOM    755  CD  LYS A  99      28.015 -26.108 -49.574  1.00 34.40           C  
ATOM    756  CE  LYS A  99      27.858 -27.582 -48.992  1.00 35.74           C  
ATOM    757  NZ  LYS A  99      29.159 -27.793 -48.061  1.00 34.38           N  
ATOM    758  N   ASN A 100      24.117 -23.555 -46.038  1.00 29.92           N  
ATOM    759  CA  ASN A 100      23.737 -23.514 -44.637  1.00 29.60           C  
ATOM    760  C   ASN A 100      22.233 -23.638 -44.451  1.00 29.54           C  
ATOM    761  O   ASN A 100      21.755 -23.818 -43.334  1.00 29.32           O  
ATOM    762  CB  ASN A 100      24.224 -22.218 -43.996  1.00 30.59           C  
ATOM    763  CG  ASN A 100      25.567 -22.357 -43.338  1.00 31.31           C  
ATOM    764  OD1 ASN A 100      25.909 -23.407 -42.779  1.00 34.63           O  
ATOM    765  ND2 ASN A 100      26.347 -21.278 -43.383  1.00 35.53           N  
ATOM    766  N   VAL A 101      21.489 -23.526 -45.544  1.00 29.08           N  
ATOM    767  CA  VAL A 101      20.038 -23.595 -45.483  1.00 29.04           C  
ATOM    768  C   VAL A 101      19.512 -24.830 -44.712  1.00 29.89           C  
ATOM    769  O   VAL A 101      18.645 -24.668 -43.845  1.00 29.90           O  
ATOM    770  CB  VAL A 101      19.406 -23.428 -46.885  1.00 28.90           C  
ATOM    771  CG1 VAL A 101      18.034 -24.124 -46.978  1.00 28.20           C  
ATOM    772  CG2 VAL A 101      19.328 -21.950 -47.229  1.00 27.68           C  
ATOM    773  N   PRO A 102      20.040 -26.048 -44.998  1.00 29.83           N  
ATOM    774  CA  PRO A 102      19.628 -27.197 -44.201  1.00 30.87           C  
ATOM    775  C   PRO A 102      19.940 -27.063 -42.707  1.00 31.80           C  
ATOM    776  O   PRO A 102      19.275 -27.714 -41.906  1.00 32.74           O  
ATOM    777  CB  PRO A 102      20.495 -28.350 -44.761  1.00 30.66           C  
ATOM    778  CG  PRO A 102      20.806 -27.932 -46.156  1.00 29.94           C  
ATOM    779  CD  PRO A 102      20.991 -26.440 -46.055  1.00 30.15           C  
ATOM    780  N   ASN A 103      20.963 -26.286 -42.337  1.00 32.49           N  
ATOM    781  CA  ASN A 103      21.273 -26.067 -40.911  1.00 33.36           C  
ATOM    782  C   ASN A 103      20.312 -25.036 -40.291  1.00 33.16           C  
ATOM    783  O   ASN A 103      19.951 -25.132 -39.124  1.00 33.65           O  
ATOM    784  CB  ASN A 103      22.736 -25.646 -40.681  1.00 33.11           C  
ATOM    785  CG  ASN A 103      23.742 -26.649 -41.216  1.00 34.36           C  
ATOM    786  OD1 ASN A 103      24.555 -26.309 -42.079  1.00 37.13           O  
ATOM    787  ND2 ASN A 103      23.721 -27.876 -40.694  1.00 34.84           N  
ATOM    788  N   TRP A 104      19.887 -24.054 -41.070  1.00 33.72           N  
ATOM    789  CA  TRP A 104      18.839 -23.153 -40.606  1.00 34.09           C  
ATOM    790  C   TRP A 104      17.534 -23.934 -40.508  1.00 34.47           C  
ATOM    791  O   TRP A 104      16.788 -23.790 -39.547  1.00 34.12           O  
ATOM    792  CB  TRP A 104      18.702 -21.949 -41.530  1.00 34.36           C  
ATOM    793  CG  TRP A 104      19.789 -20.947 -41.329  1.00 34.86           C  
ATOM    794  CD1 TRP A 104      20.848 -20.709 -42.159  1.00 34.88           C  
ATOM    795  CD2 TRP A 104      19.936 -20.059 -40.215  1.00 34.45           C  
ATOM    796  NE1 TRP A 104      21.643 -19.725 -41.630  1.00 35.64           N  
ATOM    797  CE2 TRP A 104      21.107 -19.304 -40.438  1.00 36.15           C  
ATOM    798  CE3 TRP A 104      19.195 -19.835 -39.043  1.00 33.66           C  
ATOM    799  CZ2 TRP A 104      21.553 -18.315 -39.538  1.00 34.70           C  
ATOM    800  CZ3 TRP A 104      19.646 -18.875 -38.142  1.00 34.69           C  
ATOM    801  CH2 TRP A 104      20.810 -18.113 -38.407  1.00 34.31           C  
ATOM    802  N   HIS A 105      17.298 -24.802 -41.487  1.00 35.19           N  
ATOM    803  CA  HIS A 105      16.081 -25.591 -41.539  1.00 36.21           C  
ATOM    804  C   HIS A 105      15.960 -26.538 -40.322  1.00 37.12           C  
ATOM    805  O   HIS A 105      14.907 -26.577 -39.675  1.00 37.18           O  
ATOM    806  CB  HIS A 105      15.971 -26.311 -42.894  1.00 36.33           C  
ATOM    807  CG  HIS A 105      14.746 -27.187 -43.001  1.00 37.70           C  
ATOM    808  ND1 HIS A 105      14.814 -28.546 -43.288  1.00 42.82           N  
ATOM    809  CD2 HIS A 105      13.429 -26.910 -42.817  1.00 37.76           C  
ATOM    810  CE1 HIS A 105      13.584 -29.056 -43.309  1.00 42.22           C  
ATOM    811  NE2 HIS A 105      12.726 -28.080 -43.033  1.00 38.27           N  
ATOM    812  N  AARG A 106      17.024 -27.283 -40.026  0.50 37.40           N  
ATOM    813  N  BARG A 106      17.058 -27.231 -40.005  0.50 37.49           N  
ATOM    814  CA AARG A 106      17.073 -28.157 -38.847  0.50 38.06           C  
ATOM    815  CA BARG A 106      17.156 -28.172 -38.870  0.50 38.22           C  
ATOM    816  C  AARG A 106      16.926 -27.353 -37.555  0.50 38.39           C  
ATOM    817  C  BARG A 106      17.321 -27.517 -37.489  0.50 38.57           C  
ATOM    818  O  AARG A 106      16.174 -27.738 -36.661  0.50 38.46           O  
ATOM    819  O  BARG A 106      17.207 -28.184 -36.462  0.50 38.77           O  
ATOM    820  CB AARG A 106      18.376 -28.967 -38.825  0.50 37.72           C  
ATOM    821  CB BARG A 106      18.294 -29.172 -39.103  0.50 37.91           C  
ATOM    822  CG AARG A 106      18.568 -29.841 -37.576  0.50 38.50           C  
ATOM    823  CG BARG A 106      18.027 -30.212 -40.195  0.50 38.51           C  
ATOM    824  CD AARG A 106      19.866 -30.660 -37.643  0.50 38.31           C  
ATOM    825  CD BARG A 106      19.150 -31.357 -40.131  0.50 38.67           C  
ATOM    826  NE AARG A 106      19.742 -31.810 -38.558  0.50 38.62           N  
ATOM    827  NE BARG A 106      20.265 -31.160 -41.172  0.50 40.09           N  
ATOM    828  CZ AARG A 106      19.923 -33.096 -38.218  0.50 37.76           C  
ATOM    829  CZ BARG A 106      21.561 -30.689 -40.935  0.50 39.59           C  
ATOM    830  NH1AARG A 106      19.776 -34.047 -39.147  0.50 37.68           N  
ATOM    831  NH1BARG A 106      22.427 -30.389 -41.955  0.50 39.64           N  
ATOM    832  NH2AARG A 106      20.259 -33.441 -36.968  0.50 37.72           N  
ATOM    833  NH2BARG A 106      21.963 -30.527 -39.670  0.50 38.40           N  
ATOM    834  N   ASP A 107      17.631 -26.225 -37.478  1.00 39.00           N  
ATOM    835  CA  ASP A 107      17.664 -25.405 -36.263  1.00 39.90           C  
ATOM    836  C   ASP A 107      16.240 -24.965 -35.897  1.00 40.34           C  
ATOM    837  O   ASP A 107      15.861 -24.950 -34.716  1.00 40.54           O  
ATOM    838  CB  ASP A 107      18.550 -24.179 -36.520  1.00 40.57           C  
ATOM    839  CG  ASP A 107      18.773 -23.341 -35.287  1.00 41.57           C  
ATOM    840  OD1 ASP A 107      19.125 -23.918 -34.247  1.00 44.10           O  
ATOM    841  OD2 ASP A 107      18.622 -22.098 -35.364  1.00 44.38           O  
ATOM    842  N   LEU A 108      15.464 -24.640 -36.933  1.00 40.64           N  
ATOM    843  CA  LEU A 108      14.068 -24.218 -36.831  1.00 41.31           C  
ATOM    844  C   LEU A 108      13.179 -25.371 -36.366  1.00 42.07           C  
ATOM    845  O   LEU A 108      12.431 -25.253 -35.388  1.00 41.49           O  
ATOM    846  CB  LEU A 108      13.600 -23.743 -38.214  1.00 40.99           C  
ATOM    847  CG  LEU A 108      13.063 -22.345 -38.447  1.00 40.90           C  
ATOM    848  CD1 LEU A 108      13.557 -21.389 -37.407  1.00 39.53           C  
ATOM    849  CD2 LEU A 108      13.506 -21.901 -39.832  1.00 40.62           C  
ATOM    850  N   VAL A 109      13.277 -26.477 -37.099  1.00 43.53           N  
ATOM    851  CA  VAL A 109      12.622 -27.739 -36.782  1.00 45.14           C  
ATOM    852  C   VAL A 109      12.836 -28.175 -35.320  1.00 46.22           C  
ATOM    853  O   VAL A 109      11.869 -28.425 -34.601  1.00 46.26           O  
ATOM    854  CB  VAL A 109      13.075 -28.838 -37.790  1.00 45.11           C  
ATOM    855  CG1 VAL A 109      12.647 -30.230 -37.345  1.00 45.04           C  
ATOM    856  CG2 VAL A 109      12.536 -28.520 -39.192  1.00 45.62           C  
ATOM    857  N   ARG A 110      14.096 -28.233 -34.884  1.00 47.88           N  
ATOM    858  CA  ARG A 110      14.450 -28.616 -33.510  1.00 49.22           C  
ATOM    859  C   ARG A 110      13.630 -27.850 -32.477  1.00 50.16           C  
ATOM    860  O   ARG A 110      13.256 -28.398 -31.447  1.00 50.30           O  
ATOM    861  CB  ARG A 110      15.949 -28.395 -33.244  1.00 49.33           C  
ATOM    862  CG  ARG A 110      16.885 -29.446 -33.849  1.00 50.18           C  
ATOM    863  CD  ARG A 110      17.424 -30.432 -32.812  1.00 52.24           C  
ATOM    864  NE  ARG A 110      16.363 -31.005 -31.976  1.00 53.12           N  
ATOM    865  CZ  ARG A 110      16.558 -31.847 -30.961  1.00 53.07           C  
ATOM    866  NH1 ARG A 110      15.517 -32.295 -30.272  1.00 52.60           N  
ATOM    867  NH2 ARG A 110      17.786 -32.245 -30.634  1.00 53.46           N  
ATOM    868  N   VAL A 111      13.329 -26.594 -32.778  1.00 51.28           N  
ATOM    869  CA  VAL A 111      12.709 -25.685 -31.820  1.00 52.70           C  
ATOM    870  C   VAL A 111      11.211 -25.393 -32.060  1.00 53.55           C  
ATOM    871  O   VAL A 111      10.557 -24.862 -31.161  1.00 54.04           O  
ATOM    872  CB  VAL A 111      13.500 -24.327 -31.732  1.00 52.75           C  
ATOM    873  CG1 VAL A 111      12.942 -23.424 -30.631  1.00 52.79           C  
ATOM    874  CG2 VAL A 111      14.993 -24.570 -31.497  1.00 52.78           C  
ATOM    875  N   CYS A 112      10.649 -25.743 -33.223  1.00 54.34           N  
ATOM    876  CA  CYS A 112       9.315 -25.196 -33.564  1.00 54.79           C  
ATOM    877  C   CYS A 112       7.989 -25.955 -33.293  1.00 55.23           C  
ATOM    878  O   CYS A 112       7.174 -25.426 -32.529  1.00 55.37           O  
ATOM    879  CB  CYS A 112       9.336 -24.412 -34.865  1.00 55.21           C  
ATOM    880  SG  CYS A 112      10.046 -22.774 -34.544  1.00 55.15           S  
ATOM    881  N   GLU A 113       7.685 -27.112 -33.894  1.00 55.42           N  
ATOM    882  CA  GLU A 113       8.184 -27.643 -35.157  1.00 55.04           C  
ATOM    883  C   GLU A 113       6.937 -27.799 -36.068  1.00 54.09           C  
ATOM    884  O   GLU A 113       5.816 -27.462 -35.651  1.00 54.51           O  
ATOM    885  CB  GLU A 113       8.890 -28.992 -34.901  1.00 55.50           C  
ATOM    886  CG  GLU A 113       8.797 -30.087 -36.001  1.00 57.56           C  
ATOM    887  CD  GLU A 113       9.322 -29.664 -37.396  1.00 60.28           C  
ATOM    888  OE1 GLU A 113       9.611 -28.454 -37.640  1.00 61.57           O  
ATOM    889  OE2 GLU A 113       9.419 -30.561 -38.269  1.00 61.20           O  
ATOM    890  N   ASN A 114       7.139 -28.305 -37.289  1.00 52.41           N  
ATOM    891  CA  ASN A 114       6.149 -28.343 -38.389  1.00 50.34           C  
ATOM    892  C   ASN A 114       5.373 -27.042 -38.613  1.00 48.39           C  
ATOM    893  O   ASN A 114       4.198 -27.051 -38.986  1.00 48.73           O  
ATOM    894  CB  ASN A 114       5.257 -29.611 -38.390  1.00 50.91           C  
ATOM    895  CG  ASN A 114       4.310 -29.701 -37.186  1.00 52.17           C  
ATOM    896  OD1 ASN A 114       3.625 -28.731 -36.832  1.00 53.30           O  
ATOM    897  ND2 ASN A 114       4.247 -30.893 -36.571  1.00 52.67           N  
ATOM    898  N   ILE A 115       6.055 -25.923 -38.385  1.00 45.38           N  
ATOM    899  CA  ILE A 115       5.560 -24.641 -38.855  1.00 42.27           C  
ATOM    900  C   ILE A 115       5.879 -24.577 -40.336  1.00 40.79           C  
ATOM    901  O   ILE A 115       6.873 -25.171 -40.775  1.00 41.12           O  
ATOM    902  CB  ILE A 115       6.175 -23.440 -38.099  1.00 42.09           C  
ATOM    903  CG1 ILE A 115       7.674 -23.295 -38.392  1.00 41.50           C  
ATOM    904  CG2 ILE A 115       5.857 -23.536 -36.609  1.00 41.10           C  
ATOM    905  CD1 ILE A 115       8.313 -22.063 -37.750  1.00 40.97           C  
ATOM    906  N   PRO A 116       5.006 -23.923 -41.120  1.00 38.96           N  
ATOM    907  CA  PRO A 116       5.315 -23.696 -42.528  1.00 37.83           C  
ATOM    908  C   PRO A 116       6.550 -22.809 -42.715  1.00 36.49           C  
ATOM    909  O   PRO A 116       6.720 -21.815 -42.013  1.00 35.47           O  
ATOM    910  CB  PRO A 116       4.054 -23.002 -43.056  1.00 38.11           C  
ATOM    911  CG  PRO A 116       3.394 -22.418 -41.840  1.00 38.75           C  
ATOM    912  CD  PRO A 116       3.677 -23.397 -40.754  1.00 38.60           C  
ATOM    913  N   ILE A 117       7.401 -23.195 -43.657  1.00 35.12           N  
ATOM    914  CA  ILE A 117       8.655 -22.510 -43.913  1.00 34.57           C  
ATOM    915  C   ILE A 117       8.765 -22.244 -45.414  1.00 34.57           C  
ATOM    916  O   ILE A 117       8.540 -23.135 -46.211  1.00 35.77           O  
ATOM    917  CB  ILE A 117       9.863 -23.381 -43.455  1.00 34.14           C  
ATOM    918  CG1 ILE A 117       9.852 -23.580 -41.938  1.00 34.11           C  
ATOM    919  CG2 ILE A 117      11.174 -22.756 -43.885  1.00 34.38           C  
ATOM    920  CD1 ILE A 117      10.743 -24.693 -41.432  1.00 34.05           C  
ATOM    921  N   VAL A 118       9.087 -21.022 -45.792  1.00 34.55           N  
ATOM    922  CA  VAL A 118       9.436 -20.700 -47.165  1.00 34.56           C  
ATOM    923  C   VAL A 118      10.930 -20.414 -47.246  1.00 33.95           C  
ATOM    924  O   VAL A 118      11.477 -19.675 -46.410  1.00 34.64           O  
ATOM    925  CB  VAL A 118       8.737 -19.407 -47.667  1.00 34.39           C  
ATOM    926  CG1 VAL A 118       9.005 -19.200 -49.154  1.00 34.59           C  
ATOM    927  CG2 VAL A 118       7.273 -19.480 -47.480  1.00 36.74           C  
ATOM    928  N   LEU A 119      11.553 -20.957 -48.286  1.00 32.20           N  
ATOM    929  CA  LEU A 119      12.939 -20.730 -48.623  1.00 31.95           C  
ATOM    930  C   LEU A 119      13.030 -19.655 -49.709  1.00 32.45           C  
ATOM    931  O   LEU A 119      12.354 -19.732 -50.729  1.00 32.50           O  
ATOM    932  CB  LEU A 119      13.550 -22.060 -49.119  1.00 31.78           C  
ATOM    933  CG  LEU A 119      15.017 -22.020 -49.530  1.00 31.85           C  
ATOM    934  CD1 LEU A 119      15.856 -21.558 -48.349  1.00 31.03           C  
ATOM    935  CD2 LEU A 119      15.516 -23.381 -50.055  1.00 31.71           C  
ATOM    936  N   CYS A 120      13.844 -18.634 -49.495  1.00 32.88           N  
ATOM    937  CA  CYS A 120      13.958 -17.543 -50.473  1.00 33.22           C  
ATOM    938  C   CYS A 120      15.399 -17.336 -50.897  1.00 33.72           C  
ATOM    939  O   CYS A 120      16.299 -17.159 -50.054  1.00 34.15           O  
ATOM    940  CB  CYS A 120      13.450 -16.220 -49.894  1.00 33.07           C  
ATOM    941  SG  CYS A 120      11.656 -16.017 -49.585  1.00 33.94           S  
ATOM    942  N   GLY A 121      15.622 -17.328 -52.202  1.00 34.07           N  
ATOM    943  CA  GLY A 121      16.952 -17.061 -52.758  1.00 33.44           C  
ATOM    944  C   GLY A 121      16.975 -15.620 -53.156  1.00 33.50           C  
ATOM    945  O   GLY A 121      16.324 -15.231 -54.137  1.00 33.63           O  
ATOM    946  N   ASN A 122      17.696 -14.811 -52.388  1.00 32.99           N  
ATOM    947  CA  ASN A 122      17.731 -13.382 -52.603  1.00 32.64           C  
ATOM    948  C   ASN A 122      18.796 -12.919 -53.599  1.00 33.16           C  
ATOM    949  O   ASN A 122      19.734 -13.662 -53.927  1.00 34.05           O  
ATOM    950  CB  ASN A 122      17.883 -12.657 -51.256  1.00 33.47           C  
ATOM    951  CG  ASN A 122      17.561 -11.172 -51.350  1.00 32.69           C  
ATOM    952  OD1 ASN A 122      16.851 -10.757 -52.249  1.00 34.04           O  
ATOM    953  ND2 ASN A 122      18.100 -10.370 -50.436  1.00 33.34           N  
ATOM    954  N   LYS A 123      18.618 -11.700 -54.103  1.00 32.92           N  
ATOM    955  CA  LYS A 123      19.584 -11.006 -54.971  1.00 32.55           C  
ATOM    956  C   LYS A 123      19.594 -11.564 -56.375  1.00 33.28           C  
ATOM    957  O   LYS A 123      20.636 -11.560 -57.035  1.00 32.58           O  
ATOM    958  CB  LYS A 123      21.014 -10.983 -54.380  1.00 33.01           C  
ATOM    959  CG  LYS A 123      21.082 -10.393 -52.937  1.00 31.47           C  
ATOM    960  CD  LYS A 123      22.509 -10.244 -52.469  1.00 31.79           C  
ATOM    961  CE  LYS A 123      22.566 -10.087 -50.959  1.00 29.62           C  
ATOM    962  NZ  LYS A 123      23.955  -9.859 -50.458  1.00 29.55           N  
ATOM    963  N   VAL A 124      18.439 -12.041 -56.843  1.00 33.49           N  
ATOM    964  CA  VAL A 124      18.389 -12.600 -58.196  1.00 34.29           C  
ATOM    965  C   VAL A 124      18.486 -11.471 -59.238  1.00 34.56           C  
ATOM    966  O   VAL A 124      18.545 -11.730 -60.434  1.00 34.59           O  
ATOM    967  CB  VAL A 124      17.161 -13.531 -58.464  1.00 34.05           C  
ATOM    968  CG1 VAL A 124      17.157 -14.728 -57.531  1.00 33.31           C  
ATOM    969  CG2 VAL A 124      15.840 -12.762 -58.379  1.00 34.61           C  
ATOM    970  N   ASP A 125      18.525 -10.222 -58.782  1.00 35.06           N  
ATOM    971  CA  ASP A 125      18.787  -9.107 -59.690  1.00 35.87           C  
ATOM    972  C   ASP A 125      20.222  -9.135 -60.232  1.00 36.61           C  
ATOM    973  O   ASP A 125      20.485  -8.601 -61.305  1.00 36.47           O  
ATOM    974  CB  ASP A 125      18.512  -7.766 -59.019  1.00 36.13           C  
ATOM    975  CG  ASP A 125      19.251  -7.608 -57.706  1.00 36.11           C  
ATOM    976  OD1 ASP A 125      18.770  -8.114 -56.652  1.00 37.16           O  
ATOM    977  OD2 ASP A 125      20.310  -6.953 -57.722  1.00 36.98           O  
ATOM    978  N   ILE A 126      21.147  -9.741 -59.490  1.00 37.02           N  
ATOM    979  CA  ILE A 126      22.540  -9.805 -59.925  1.00 38.08           C  
ATOM    980  C   ILE A 126      22.678 -10.877 -61.013  1.00 38.47           C  
ATOM    981  O   ILE A 126      22.365 -12.037 -60.785  1.00 38.97           O  
ATOM    982  CB  ILE A 126      23.509 -10.013 -58.723  1.00 38.14           C  
ATOM    983  CG1 ILE A 126      23.435  -8.793 -57.795  1.00 38.36           C  
ATOM    984  CG2 ILE A 126      24.958 -10.237 -59.213  1.00 38.68           C  
ATOM    985  CD1 ILE A 126      23.922  -9.026 -56.392  1.00 40.85           C  
ATOM    986  N   LYS A 127      23.112 -10.465 -62.201  1.00 39.47           N  
ATOM    987  CA  LYS A 127      23.248 -11.361 -63.368  1.00 39.69           C  
ATOM    988  C   LYS A 127      24.247 -12.508 -63.133  1.00 39.31           C  
ATOM    989  O   LYS A 127      24.065 -13.621 -63.652  1.00 39.38           O  
ATOM    990  CB  LYS A 127      23.641 -10.544 -64.604  1.00 40.35           C  
ATOM    991  CG  LYS A 127      23.856 -11.347 -65.894  1.00 43.01           C  
ATOM    992  CD  LYS A 127      24.952 -10.702 -66.770  1.00 45.89           C  
ATOM    993  CE  LYS A 127      25.714 -11.740 -67.601  1.00 46.94           C  
ATOM    994  NZ  LYS A 127      25.116 -11.939 -68.962  1.00 48.63           N  
ATOM    995  N  AASP A 128      25.247 -12.219 -62.305  0.50 38.96           N  
ATOM    996  N  BASP A 128      25.324 -12.234 -62.389  0.50 38.97           N  
ATOM    997  CA AASP A 128      26.316 -13.135 -61.956  0.50 38.46           C  
ATOM    998  CA BASP A 128      26.329 -13.259 -62.069  0.50 38.50           C  
ATOM    999  C  AASP A 128      25.862 -14.140 -60.879  0.50 37.95           C  
ATOM   1000  C  BASP A 128      25.855 -14.135 -60.909  0.50 37.99           C  
ATOM   1001  O  AASP A 128      26.402 -14.159 -59.773  0.50 37.67           O  
ATOM   1002  O  BASP A 128      26.351 -14.049 -59.785  0.50 37.70           O  
ATOM   1003  CB AASP A 128      27.524 -12.314 -61.470  0.50 38.66           C  
ATOM   1004  CB BASP A 128      27.708 -12.640 -61.774  0.50 38.77           C  
ATOM   1005  CG AASP A 128      27.671 -10.973 -62.209  0.50 38.73           C  
ATOM   1006  CG BASP A 128      28.808 -13.696 -61.592  0.50 38.73           C  
ATOM   1007  OD1AASP A 128      27.003  -9.984 -61.816  0.50 37.79           O  
ATOM   1008  OD1BASP A 128      29.698 -13.487 -60.734  0.50 38.68           O  
ATOM   1009  OD2AASP A 128      28.467 -10.909 -63.175  0.50 39.24           O  
ATOM   1010  OD2BASP A 128      28.774 -14.734 -62.295  0.50 38.33           O  
ATOM   1011  N   ARG A 129      24.879 -14.977 -61.218  1.00 37.62           N  
ATOM   1012  CA  ARG A 129      24.224 -15.865 -60.243  1.00 36.79           C  
ATOM   1013  C   ARG A 129      24.965 -17.198 -60.079  1.00 36.67           C  
ATOM   1014  O   ARG A 129      25.293 -17.844 -61.075  1.00 36.54           O  
ATOM   1015  CB  ARG A 129      22.769 -16.097 -60.678  1.00 36.42           C  
ATOM   1016  CG  ARG A 129      22.024 -17.156 -59.916  1.00 35.91           C  
ATOM   1017  CD  ARG A 129      20.563 -17.234 -60.337  1.00 35.76           C  
ATOM   1018  NE  ARG A 129      19.829 -18.038 -59.367  1.00 34.79           N  
ATOM   1019  CZ  ARG A 129      18.507 -18.081 -59.235  1.00 35.09           C  
ATOM   1020  NH1 ARG A 129      17.979 -18.856 -58.305  1.00 34.42           N  
ATOM   1021  NH2 ARG A 129      17.713 -17.365 -60.025  1.00 34.72           N  
ATOM   1022  N   LYS A 130      25.216 -17.607 -58.831  1.00 36.39           N  
ATOM   1023  CA  LYS A 130      26.008 -18.807 -58.559  1.00 36.47           C  
ATOM   1024  C   LYS A 130      25.124 -19.997 -58.256  1.00 35.90           C  
ATOM   1025  O   LYS A 130      25.426 -21.107 -58.658  1.00 35.33           O  
ATOM   1026  CB  LYS A 130      26.992 -18.568 -57.409  1.00 36.65           C  
ATOM   1027  CG  LYS A 130      27.819 -17.291 -57.547  1.00 39.05           C  
ATOM   1028  CD  LYS A 130      28.807 -17.388 -58.706  1.00 41.72           C  
ATOM   1029  CE  LYS A 130      29.697 -16.156 -58.780  1.00 43.96           C  
ATOM   1030  NZ  LYS A 130      30.985 -16.458 -59.485  1.00 45.02           N  
ATOM   1031  N   VAL A 131      24.028 -19.761 -57.541  1.00 35.86           N  
ATOM   1032  CA  VAL A 131      23.141 -20.851 -57.147  1.00 35.69           C  
ATOM   1033  C   VAL A 131      21.909 -20.840 -58.055  1.00 36.54           C  
ATOM   1034  O   VAL A 131      21.011 -20.039 -57.887  1.00 35.98           O  
ATOM   1035  CB  VAL A 131      22.735 -20.775 -55.640  1.00 35.37           C  
ATOM   1036  CG1 VAL A 131      21.942 -21.982 -55.259  1.00 34.96           C  
ATOM   1037  CG2 VAL A 131      23.958 -20.659 -54.716  1.00 33.00           C  
ATOM   1038  N   LYS A 132      21.876 -21.732 -59.031  1.00 37.80           N  
ATOM   1039  CA  LYS A 132      20.768 -21.745 -59.975  1.00 39.35           C  
ATOM   1040  C   LYS A 132      19.717 -22.792 -59.596  1.00 40.21           C  
ATOM   1041  O   LYS A 132      19.981 -23.697 -58.797  1.00 40.35           O  
ATOM   1042  CB  LYS A 132      21.286 -21.961 -61.399  1.00 39.55           C  
ATOM   1043  CG  LYS A 132      22.500 -21.104 -61.732  1.00 40.43           C  
ATOM   1044  CD  LYS A 132      23.169 -21.549 -63.012  1.00 43.01           C  
ATOM   1045  CE  LYS A 132      24.592 -20.994 -63.137  1.00 45.38           C  
ATOM   1046  NZ  LYS A 132      24.588 -19.495 -63.194  1.00 45.26           N  
ATOM   1047  N   ALA A 133      18.531 -22.665 -60.190  1.00 41.04           N  
ATOM   1048  CA  ALA A 133      17.395 -23.561 -59.930  1.00 41.79           C  
ATOM   1049  C   ALA A 133      17.747 -25.064 -59.897  1.00 42.21           C  
ATOM   1050  O   ALA A 133      17.248 -25.802 -59.037  1.00 41.98           O  
ATOM   1051  CB  ALA A 133      16.290 -23.293 -60.933  1.00 41.92           C  
ATOM   1052  N   LYS A 134      18.602 -25.501 -60.822  1.00 42.88           N  
ATOM   1053  CA  LYS A 134      19.089 -26.888 -60.859  1.00 43.69           C  
ATOM   1054  C   LYS A 134      19.421 -27.432 -59.462  1.00 44.01           C  
ATOM   1055  O   LYS A 134      19.104 -28.591 -59.143  1.00 44.27           O  
ATOM   1056  CB  LYS A 134      20.305 -27.013 -61.803  1.00 43.96           C  
ATOM   1057  CG  LYS A 134      21.512 -27.778 -61.231  1.00 44.27           C  
ATOM   1058  CD  LYS A 134      22.595 -28.073 -62.284  1.00 44.64           C  
ATOM   1059  CE  LYS A 134      24.022 -28.164 -61.667  1.00 44.44           C  
ATOM   1060  NZ  LYS A 134      24.164 -29.025 -60.451  1.00 44.03           N  
ATOM   1061  N   SER A 135      20.047 -26.581 -58.643  1.00 44.19           N  
ATOM   1062  CA  SER A 135      20.508 -26.936 -57.299  1.00 44.36           C  
ATOM   1063  C   SER A 135      19.405 -26.870 -56.241  1.00 44.16           C  
ATOM   1064  O   SER A 135      19.460 -27.593 -55.249  1.00 44.39           O  
ATOM   1065  CB  SER A 135      21.668 -26.028 -56.874  1.00 44.60           C  
ATOM   1066  OG  SER A 135      22.699 -26.008 -57.846  1.00 45.02           O  
ATOM   1067  N   ILE A 136      18.415 -26.008 -56.449  1.00 43.48           N  
ATOM   1068  CA  ILE A 136      17.377 -25.785 -55.445  1.00 43.24           C  
ATOM   1069  C   ILE A 136      16.187 -26.736 -55.607  1.00 43.35           C  
ATOM   1070  O   ILE A 136      16.233 -27.690 -56.393  1.00 44.47           O  
ATOM   1071  CB  ILE A 136      16.886 -24.294 -55.446  1.00 42.89           C  
ATOM   1072  CG1 ILE A 136      18.080 -23.334 -55.434  1.00 42.36           C  
ATOM   1073  CG2 ILE A 136      15.986 -24.027 -54.243  1.00 42.05           C  
ATOM   1074  CD1 ILE A 136      17.848 -22.027 -56.174  1.00 40.91           C  
ATOM   1075  N   ASN A 143       6.877 -26.329 -44.509  1.00 52.04           N  
ATOM   1076  CA  ASN A 143       6.599 -26.946 -45.805  1.00 52.35           C  
ATOM   1077  C   ASN A 143       7.403 -26.191 -46.885  1.00 51.40           C  
ATOM   1078  O   ASN A 143       7.066 -25.074 -47.249  1.00 52.55           O  
ATOM   1079  CB  ASN A 143       5.081 -26.948 -46.062  1.00 52.66           C  
ATOM   1080  CG  ASN A 143       4.632 -28.079 -46.970  1.00 53.44           C  
ATOM   1081  OD1 ASN A 143       4.930 -28.087 -48.164  1.00 54.85           O  
ATOM   1082  ND2 ASN A 143       3.883 -29.028 -46.412  1.00 55.22           N  
ATOM   1083  N   LEU A 144       8.474 -26.810 -47.380  1.00 50.23           N  
ATOM   1084  CA  LEU A 144       9.616 -26.072 -47.968  1.00 48.37           C  
ATOM   1085  C   LEU A 144       9.453 -25.543 -49.406  1.00 46.65           C  
ATOM   1086  O   LEU A 144      10.105 -26.022 -50.356  1.00 47.04           O  
ATOM   1087  CB  LEU A 144      10.904 -26.893 -47.827  1.00 48.47           C  
ATOM   1088  CG  LEU A 144      12.224 -26.120 -47.806  1.00 48.12           C  
ATOM   1089  CD1 LEU A 144      12.353 -25.283 -46.563  1.00 46.32           C  
ATOM   1090  CD2 LEU A 144      13.374 -27.144 -47.877  1.00 48.98           C  
ATOM   1091  N   GLN A 145       8.588 -24.544 -49.536  1.00 43.45           N  
ATOM   1092  CA  GLN A 145       8.341 -23.851 -50.782  1.00 40.77           C  
ATOM   1093  C   GLN A 145       9.540 -22.960 -51.104  1.00 38.70           C  
ATOM   1094  O   GLN A 145      10.105 -22.316 -50.211  1.00 37.95           O  
ATOM   1095  CB  GLN A 145       7.071 -22.996 -50.618  1.00 40.97           C  
ATOM   1096  CG  GLN A 145       6.713 -22.080 -51.758  1.00 41.21           C  
ATOM   1097  CD  GLN A 145       6.407 -22.833 -53.018  1.00 41.83           C  
ATOM   1098  OE1 GLN A 145       5.579 -23.740 -53.025  1.00 43.39           O  
ATOM   1099  NE2 GLN A 145       7.094 -22.481 -54.096  1.00 41.83           N  
ATOM   1100  N   TYR A 146       9.926 -22.926 -52.374  1.00 36.08           N  
ATOM   1101  CA  TYR A 146      10.982 -22.018 -52.812  1.00 33.99           C  
ATOM   1102  C   TYR A 146      10.491 -20.831 -53.691  1.00 33.71           C  
ATOM   1103  O   TYR A 146       9.644 -21.029 -54.569  1.00 34.49           O  
ATOM   1104  CB  TYR A 146      12.087 -22.800 -53.538  1.00 32.26           C  
ATOM   1105  CG  TYR A 146      13.137 -21.861 -54.036  1.00 30.46           C  
ATOM   1106  CD1 TYR A 146      14.040 -21.296 -53.148  1.00 30.26           C  
ATOM   1107  CD2 TYR A 146      13.178 -21.463 -55.364  1.00 27.73           C  
ATOM   1108  CE1 TYR A 146      14.987 -20.367 -53.565  1.00 32.37           C  
ATOM   1109  CE2 TYR A 146      14.130 -20.537 -55.801  1.00 30.89           C  
ATOM   1110  CZ  TYR A 146      15.023 -19.990 -54.895  1.00 30.51           C  
ATOM   1111  OH  TYR A 146      15.990 -19.113 -55.278  1.00 29.79           O  
ATOM   1112  N   TYR A 147      11.038 -19.628 -53.470  1.00 32.61           N  
ATOM   1113  CA  TYR A 147      10.918 -18.487 -54.397  1.00 32.23           C  
ATOM   1114  C   TYR A 147      12.245 -17.787 -54.614  1.00 32.47           C  
ATOM   1115  O   TYR A 147      13.007 -17.605 -53.664  1.00 31.93           O  
ATOM   1116  CB  TYR A 147       9.928 -17.412 -53.890  1.00 31.86           C  
ATOM   1117  CG  TYR A 147       8.510 -17.907 -53.798  1.00 32.05           C  
ATOM   1118  CD1 TYR A 147       7.950 -18.192 -52.568  1.00 30.14           C  
ATOM   1119  CD2 TYR A 147       7.737 -18.121 -54.950  1.00 31.74           C  
ATOM   1120  CE1 TYR A 147       6.654 -18.691 -52.465  1.00 31.65           C  
ATOM   1121  CE2 TYR A 147       6.436 -18.630 -54.858  1.00 32.64           C  
ATOM   1122  CZ  TYR A 147       5.909 -18.916 -53.598  1.00 31.82           C  
ATOM   1123  OH  TYR A 147       4.635 -19.411 -53.455  1.00 31.73           O  
ATOM   1124  N   ASP A 148      12.515 -17.401 -55.863  1.00 32.72           N  
ATOM   1125  CA  ASP A 148      13.554 -16.427 -56.189  1.00 33.73           C  
ATOM   1126  C   ASP A 148      13.021 -15.085 -55.729  1.00 34.11           C  
ATOM   1127  O   ASP A 148      11.852 -14.758 -55.990  1.00 34.28           O  
ATOM   1128  CB  ASP A 148      13.749 -16.317 -57.708  1.00 34.44           C  
ATOM   1129  CG  ASP A 148      14.705 -17.364 -58.287  1.00 37.86           C  
ATOM   1130  OD1 ASP A 148      15.426 -18.093 -57.554  1.00 37.96           O  
ATOM   1131  OD2 ASP A 148      14.745 -17.449 -59.535  1.00 43.31           O  
ATOM   1132  N   ILE A 149      13.836 -14.283 -55.057  1.00 33.61           N  
ATOM   1133  CA  ILE A 149      13.386 -12.923 -54.763  1.00 33.08           C  
ATOM   1134  C   ILE A 149      14.474 -11.915 -55.051  1.00 31.94           C  
ATOM   1135  O   ILE A 149      15.629 -12.271 -55.208  1.00 31.98           O  
ATOM   1136  CB  ILE A 149      12.893 -12.737 -53.282  1.00 33.18           C  
ATOM   1137  CG1 ILE A 149      14.043 -12.860 -52.290  1.00 34.82           C  
ATOM   1138  CG2 ILE A 149      11.685 -13.669 -52.959  1.00 34.78           C  
ATOM   1139  CD1 ILE A 149      13.733 -12.280 -50.839  1.00 34.62           C  
ATOM   1140  N   SER A 150      14.105 -10.642 -55.126  1.00 31.01           N  
ATOM   1141  CA  SER A 150      15.094  -9.603 -55.139  1.00 31.14           C  
ATOM   1142  C   SER A 150      14.556  -8.514 -54.260  1.00 31.75           C  
ATOM   1143  O   SER A 150      13.582  -7.827 -54.622  1.00 31.36           O  
ATOM   1144  CB  SER A 150      15.383  -9.108 -56.546  1.00 31.22           C  
ATOM   1145  OG  SER A 150      16.143  -7.909 -56.459  1.00 32.06           O  
ATOM   1146  N   ALA A 151      15.113  -8.431 -53.047  1.00 31.85           N  
ATOM   1147  CA  ALA A 151      14.602  -7.484 -52.057  1.00 32.44           C  
ATOM   1148  C   ALA A 151      14.657  -6.057 -52.596  1.00 33.21           C  
ATOM   1149  O   ALA A 151      13.701  -5.289 -52.437  1.00 34.45           O  
ATOM   1150  CB  ALA A 151      15.399  -7.585 -50.726  1.00 32.77           C  
ATOM   1151  N   LYS A 152      15.772  -5.703 -53.230  1.00 32.44           N  
ATOM   1152  CA  LYS A 152      15.987  -4.342 -53.679  1.00 32.64           C  
ATOM   1153  C   LYS A 152      15.170  -3.918 -54.883  1.00 32.96           C  
ATOM   1154  O   LYS A 152      15.083  -2.731 -55.136  1.00 32.74           O  
ATOM   1155  CB  LYS A 152      17.464  -4.091 -53.971  1.00 33.04           C  
ATOM   1156  CG  LYS A 152      18.246  -3.855 -52.721  1.00 34.03           C  
ATOM   1157  CD  LYS A 152      19.489  -3.115 -53.017  1.00 36.00           C  
ATOM   1158  CE  LYS A 152      20.097  -2.719 -51.730  1.00 39.41           C  
ATOM   1159  NZ  LYS A 152      21.378  -2.063 -52.097  1.00 43.12           N  
ATOM   1160  N   SER A 153      14.598  -4.867 -55.630  1.00 32.66           N  
ATOM   1161  CA  SER A 153      13.619  -4.514 -56.673  1.00 33.13           C  
ATOM   1162  C   SER A 153      12.172  -4.845 -56.288  1.00 33.17           C  
ATOM   1163  O   SER A 153      11.288  -4.627 -57.081  1.00 33.75           O  
ATOM   1164  CB  SER A 153      13.967  -5.180 -58.011  1.00 32.48           C  
ATOM   1165  OG  SER A 153      13.989  -6.575 -57.849  1.00 31.89           O  
ATOM   1166  N   ASN A 154      11.928  -5.344 -55.071  1.00 33.32           N  
ATOM   1167  CA  ASN A 154      10.604  -5.875 -54.669  1.00 33.15           C  
ATOM   1168  C   ASN A 154      10.138  -7.069 -55.514  1.00 33.50           C  
ATOM   1169  O   ASN A 154       8.965  -7.435 -55.463  1.00 33.81           O  
ATOM   1170  CB  ASN A 154       9.503  -4.791 -54.682  1.00 32.92           C  
ATOM   1171  CG  ASN A 154       9.863  -3.596 -53.836  1.00 33.13           C  
ATOM   1172  OD1 ASN A 154      10.424  -3.774 -52.763  1.00 33.02           O  
ATOM   1173  ND2 ASN A 154       9.543  -2.372 -54.303  1.00 25.53           N  
ATOM   1174  N   TYR A 155      11.039  -7.686 -56.263  1.00 33.41           N  
ATOM   1175  CA  TYR A 155      10.651  -8.809 -57.103  1.00 34.33           C  
ATOM   1176  C   TYR A 155      10.223  -9.992 -56.236  1.00 34.34           C  
ATOM   1177  O   TYR A 155      10.962 -10.447 -55.365  1.00 34.67           O  
ATOM   1178  CB  TYR A 155      11.785  -9.212 -58.056  1.00 34.42           C  
ATOM   1179  CG  TYR A 155      11.498 -10.480 -58.847  1.00 34.53           C  
ATOM   1180  CD1 TYR A 155      10.497 -10.524 -59.832  1.00 33.97           C  
ATOM   1181  CD2 TYR A 155      12.218 -11.631 -58.597  1.00 33.83           C  
ATOM   1182  CE1 TYR A 155      10.231 -11.705 -60.553  1.00 33.34           C  
ATOM   1183  CE2 TYR A 155      11.980 -12.807 -59.314  1.00 34.63           C  
ATOM   1184  CZ  TYR A 155      10.994 -12.842 -60.274  1.00 35.03           C  
ATOM   1185  OH  TYR A 155      10.820 -14.029 -60.952  1.00 37.89           O  
ATOM   1186  N   ASN A 156       9.005 -10.458 -56.470  1.00 34.95           N  
ATOM   1187  CA  ASN A 156       8.427 -11.558 -55.702  1.00 35.59           C  
ATOM   1188  C   ASN A 156       8.240 -11.307 -54.210  1.00 35.55           C  
ATOM   1189  O   ASN A 156       7.968 -12.229 -53.456  1.00 35.82           O  
ATOM   1190  CB  ASN A 156       9.182 -12.860 -55.935  1.00 33.95           C  
ATOM   1191  CG  ASN A 156       8.745 -13.552 -57.205  1.00 34.58           C  
ATOM   1192  OD1 ASN A 156       7.736 -13.181 -57.805  1.00 32.50           O  
ATOM   1193  ND2 ASN A 156       9.507 -14.543 -57.630  1.00 26.98           N  
ATOM   1194  N   PHE A 157       8.314 -10.043 -53.811  1.00 36.85           N  
ATOM   1195  CA  PHE A 157       8.114  -9.676 -52.406  1.00 37.27           C  
ATOM   1196  C   PHE A 157       6.875 -10.331 -51.747  1.00 37.48           C  
ATOM   1197  O   PHE A 157       6.987 -10.881 -50.673  1.00 37.59           O  
ATOM   1198  CB  PHE A 157       8.108  -8.148 -52.198  1.00 36.09           C  
ATOM   1199  CG  PHE A 157       7.924  -7.773 -50.753  1.00 36.48           C  
ATOM   1200  CD1 PHE A 157       9.004  -7.826 -49.871  1.00 34.57           C  
ATOM   1201  CD2 PHE A 157       6.645  -7.488 -50.246  1.00 33.60           C  
ATOM   1202  CE1 PHE A 157       8.831  -7.533 -48.523  1.00 34.43           C  
ATOM   1203  CE2 PHE A 157       6.463  -7.212 -48.888  1.00 33.22           C  
ATOM   1204  CZ  PHE A 157       7.547  -7.231 -48.036  1.00 34.83           C  
ATOM   1205  N   GLU A 158       5.722 -10.291 -52.419  1.00 38.40           N  
ATOM   1206  CA  GLU A 158       4.452 -10.812 -51.880  1.00 39.12           C  
ATOM   1207  C   GLU A 158       4.447 -12.336 -51.664  1.00 37.76           C  
ATOM   1208  O   GLU A 158       3.750 -12.823 -50.780  1.00 36.90           O  
ATOM   1209  CB  GLU A 158       3.256 -10.493 -52.820  1.00 40.31           C  
ATOM   1210  CG  GLU A 158       3.442  -9.346 -53.856  1.00 46.49           C  
ATOM   1211  CD  GLU A 158       4.541  -9.617 -54.921  1.00 52.24           C  
ATOM   1212  OE1 GLU A 158       4.553 -10.704 -55.560  1.00 54.28           O  
ATOM   1213  OE2 GLU A 158       5.389  -8.721 -55.127  1.00 54.37           O  
ATOM   1214  N   LYS A 159       5.201 -13.074 -52.482  1.00 35.78           N  
ATOM   1215  CA  LYS A 159       5.021 -14.529 -52.615  1.00 35.32           C  
ATOM   1216  C   LYS A 159       5.216 -15.340 -51.358  1.00 34.62           C  
ATOM   1217  O   LYS A 159       4.374 -16.199 -51.052  1.00 33.43           O  
ATOM   1218  CB  LYS A 159       5.950 -15.102 -53.695  1.00 35.38           C  
ATOM   1219  CG  LYS A 159       5.944 -14.287 -54.947  1.00 37.68           C  
ATOM   1220  CD  LYS A 159       4.860 -14.683 -55.855  1.00 41.08           C  
ATOM   1221  CE  LYS A 159       5.460 -15.572 -56.895  1.00 42.25           C  
ATOM   1222  NZ  LYS A 159       4.877 -15.236 -58.230  1.00 43.08           N  
ATOM   1223  N   PRO A 160       6.349 -15.108 -50.640  1.00 34.19           N  
ATOM   1224  CA  PRO A 160       6.530 -15.878 -49.404  1.00 33.69           C  
ATOM   1225  C   PRO A 160       5.352 -15.678 -48.462  1.00 33.11           C  
ATOM   1226  O   PRO A 160       4.874 -16.642 -47.863  1.00 32.47           O  
ATOM   1227  CB  PRO A 160       7.797 -15.280 -48.775  1.00 33.02           C  
ATOM   1228  CG  PRO A 160       8.440 -14.460 -49.810  1.00 33.00           C  
ATOM   1229  CD  PRO A 160       7.479 -14.205 -50.919  1.00 33.64           C  
ATOM   1230  N   PHE A 161       4.891 -14.436 -48.349  1.00 32.73           N  
ATOM   1231  CA  PHE A 161       3.819 -14.102 -47.427  1.00 32.91           C  
ATOM   1232  C   PHE A 161       2.486 -14.643 -47.885  1.00 32.55           C  
ATOM   1233  O   PHE A 161       1.667 -15.036 -47.063  1.00 32.95           O  
ATOM   1234  CB  PHE A 161       3.711 -12.598 -47.222  1.00 32.73           C  
ATOM   1235  CG  PHE A 161       4.995 -11.950 -46.751  1.00 34.10           C  
ATOM   1236  CD1 PHE A 161       5.812 -11.266 -47.652  1.00 32.60           C  
ATOM   1237  CD2 PHE A 161       5.351 -11.982 -45.417  1.00 31.82           C  
ATOM   1238  CE1 PHE A 161       6.972 -10.637 -47.237  1.00 31.02           C  
ATOM   1239  CE2 PHE A 161       6.510 -11.360 -44.995  1.00 34.85           C  
ATOM   1240  CZ  PHE A 161       7.336 -10.707 -45.916  1.00 33.92           C  
ATOM   1241  N   LEU A 162       2.257 -14.666 -49.197  1.00 32.31           N  
ATOM   1242  CA  LEU A 162       1.018 -15.216 -49.726  1.00 31.00           C  
ATOM   1243  C   LEU A 162       0.989 -16.716 -49.497  1.00 31.21           C  
ATOM   1244  O   LEU A 162      -0.041 -17.286 -49.111  1.00 30.71           O  
ATOM   1245  CB  LEU A 162       0.868 -14.886 -51.204  1.00 30.83           C  
ATOM   1246  CG  LEU A 162      -0.409 -15.400 -51.874  1.00 31.00           C  
ATOM   1247  CD1 LEU A 162      -1.689 -14.939 -51.179  1.00 31.07           C  
ATOM   1248  CD2 LEU A 162      -0.426 -15.042 -53.364  1.00 32.07           C  
ATOM   1249  N   TRP A 163       2.127 -17.364 -49.734  1.00 31.26           N  
ATOM   1250  CA  TRP A 163       2.186 -18.814 -49.606  1.00 30.35           C  
ATOM   1251  C   TRP A 163       1.952 -19.190 -48.143  1.00 30.18           C  
ATOM   1252  O   TRP A 163       1.181 -20.090 -47.840  1.00 29.31           O  
ATOM   1253  CB  TRP A 163       3.523 -19.358 -50.117  1.00 30.95           C  
ATOM   1254  CG  TRP A 163       3.558 -20.857 -50.053  1.00 29.70           C  
ATOM   1255  CD1 TRP A 163       3.157 -21.732 -51.015  1.00 30.78           C  
ATOM   1256  CD2 TRP A 163       3.991 -21.642 -48.942  1.00 30.63           C  
ATOM   1257  NE1 TRP A 163       3.323 -23.031 -50.568  1.00 30.78           N  
ATOM   1258  CE2 TRP A 163       3.830 -22.996 -49.294  1.00 30.39           C  
ATOM   1259  CE3 TRP A 163       4.509 -21.327 -47.676  1.00 31.21           C  
ATOM   1260  CZ2 TRP A 163       4.173 -24.038 -48.429  1.00 32.16           C  
ATOM   1261  CZ3 TRP A 163       4.844 -22.357 -46.821  1.00 31.96           C  
ATOM   1262  CH2 TRP A 163       4.664 -23.701 -47.198  1.00 30.88           C  
ATOM   1263  N   LEU A 164       2.628 -18.481 -47.238  1.00 30.52           N  
ATOM   1264  CA  LEU A 164       2.449 -18.663 -45.793  1.00 30.92           C  
ATOM   1265  C   LEU A 164       1.024 -18.364 -45.352  1.00 31.23           C  
ATOM   1266  O   LEU A 164       0.509 -19.014 -44.473  1.00 31.69           O  
ATOM   1267  CB  LEU A 164       3.400 -17.762 -45.019  1.00 30.56           C  
ATOM   1268  CG  LEU A 164       4.843 -18.225 -45.075  1.00 31.56           C  
ATOM   1269  CD1 LEU A 164       5.712 -17.209 -44.398  1.00 30.27           C  
ATOM   1270  CD2 LEU A 164       5.005 -19.598 -44.444  1.00 29.38           C  
ATOM   1271  N   ALA A 165       0.386 -17.368 -45.950  1.00 31.83           N  
ATOM   1272  CA  ALA A 165      -1.006 -17.078 -45.585  1.00 32.01           C  
ATOM   1273  C   ALA A 165      -1.898 -18.239 -46.000  1.00 32.20           C  
ATOM   1274  O   ALA A 165      -2.710 -18.732 -45.200  1.00 31.43           O  
ATOM   1275  CB  ALA A 165      -1.462 -15.806 -46.221  1.00 32.24           C  
ATOM   1276  N   ARG A 166      -1.736 -18.695 -47.246  1.00 32.44           N  
ATOM   1277  CA  ARG A 166      -2.530 -19.815 -47.768  1.00 32.37           C  
ATOM   1278  C   ARG A 166      -2.337 -21.074 -46.927  1.00 32.38           C  
ATOM   1279  O   ARG A 166      -3.300 -21.788 -46.664  1.00 32.05           O  
ATOM   1280  CB  ARG A 166      -2.184 -20.114 -49.229  1.00 32.47           C  
ATOM   1281  CG  ARG A 166      -2.577 -19.011 -50.183  1.00 34.71           C  
ATOM   1282  CD  ARG A 166      -2.040 -19.261 -51.570  1.00 36.56           C  
ATOM   1283  NE  ARG A 166      -2.756 -18.458 -52.554  1.00 39.34           N  
ATOM   1284  CZ  ARG A 166      -2.580 -18.515 -53.874  1.00 41.55           C  
ATOM   1285  NH1 ARG A 166      -3.315 -17.740 -54.673  1.00 41.18           N  
ATOM   1286  NH2 ARG A 166      -1.680 -19.338 -54.402  1.00 42.10           N  
ATOM   1287  N   LYS A 167      -1.095 -21.333 -46.504  1.00 32.42           N  
ATOM   1288  CA  LYS A 167      -0.801 -22.508 -45.660  1.00 32.73           C  
ATOM   1289  C   LYS A 167      -1.372 -22.325 -44.250  1.00 32.74           C  
ATOM   1290  O   LYS A 167      -1.974 -23.234 -43.725  1.00 32.96           O  
ATOM   1291  CB  LYS A 167       0.706 -22.813 -45.607  1.00 31.79           C  
ATOM   1292  CG  LYS A 167       1.051 -24.308 -45.523  1.00 35.07           C  
ATOM   1293  CD  LYS A 167       0.838 -25.066 -46.841  1.00 33.97           C  
ATOM   1294  CE  LYS A 167       1.643 -26.362 -46.840  1.00 36.01           C  
ATOM   1295  NZ  LYS A 167       0.913 -27.577 -46.345  1.00 36.07           N  
ATOM   1296  N   LEU A 168      -1.216 -21.139 -43.647  1.00 32.95           N  
ATOM   1297  CA  LEU A 168      -1.727 -20.936 -42.276  1.00 32.98           C  
ATOM   1298  C   LEU A 168      -3.254 -20.937 -42.186  1.00 32.94           C  
ATOM   1299  O   LEU A 168      -3.822 -21.542 -41.280  1.00 32.69           O  
ATOM   1300  CB  LEU A 168      -1.172 -19.666 -41.654  1.00 32.66           C  
ATOM   1301  CG  LEU A 168       0.314 -19.614 -41.312  1.00 33.19           C  
ATOM   1302  CD1 LEU A 168       0.707 -18.159 -41.145  1.00 30.68           C  
ATOM   1303  CD2 LEU A 168       0.636 -20.428 -40.061  1.00 32.59           C  
ATOM   1304  N   ILE A 169      -3.905 -20.265 -43.135  1.00 32.56           N  
ATOM   1305  CA  ILE A 169      -5.353 -20.178 -43.172  1.00 32.36           C  
ATOM   1306  C   ILE A 169      -6.004 -21.454 -43.714  1.00 31.73           C  
ATOM   1307  O   ILE A 169      -7.144 -21.727 -43.384  1.00 31.46           O  
ATOM   1308  CB  ILE A 169      -5.836 -18.961 -44.005  1.00 32.38           C  
ATOM   1309  CG1 ILE A 169      -5.160 -17.631 -43.552  1.00 34.19           C  
ATOM   1310  CG2 ILE A 169      -7.369 -18.890 -44.047  1.00 33.67           C  
ATOM   1311  CD1 ILE A 169      -5.191 -17.302 -42.050  1.00 34.44           C  
ATOM   1312  N   GLY A 170      -5.303 -22.213 -44.556  1.00 31.43           N  
ATOM   1313  CA  GLY A 170      -5.871 -23.449 -45.135  1.00 31.97           C  
ATOM   1314  C   GLY A 170      -6.686 -23.203 -46.396  1.00 32.28           C  
ATOM   1315  O   GLY A 170      -7.493 -24.042 -46.806  1.00 32.09           O  
ATOM   1316  N   ASP A 171      -6.446 -22.056 -47.028  1.00 32.28           N  
ATOM   1317  CA  ASP A 171      -7.170 -21.623 -48.224  1.00 33.01           C  
ATOM   1318  C   ASP A 171      -6.148 -21.510 -49.369  1.00 33.14           C  
ATOM   1319  O   ASP A 171      -5.386 -20.555 -49.428  1.00 32.46           O  
ATOM   1320  CB  ASP A 171      -7.883 -20.280 -47.936  1.00 33.18           C  
ATOM   1321  CG  ASP A 171      -8.777 -19.791 -49.084  1.00 34.03           C  
ATOM   1322  OD1 ASP A 171      -8.913 -20.493 -50.109  1.00 31.77           O  
ATOM   1323  OD2 ASP A 171      -9.355 -18.671 -48.948  1.00 34.75           O  
ATOM   1324  N   PRO A 172      -6.100 -22.522 -50.255  1.00 33.53           N  
ATOM   1325  CA  PRO A 172      -5.159 -22.516 -51.383  1.00 33.78           C  
ATOM   1326  C   PRO A 172      -5.406 -21.399 -52.397  1.00 34.00           C  
ATOM   1327  O   PRO A 172      -4.515 -21.103 -53.187  1.00 34.56           O  
ATOM   1328  CB  PRO A 172      -5.390 -23.889 -52.038  1.00 33.55           C  
ATOM   1329  CG  PRO A 172      -6.755 -24.289 -51.598  1.00 33.75           C  
ATOM   1330  CD  PRO A 172      -6.889 -23.767 -50.212  1.00 33.39           C  
ATOM   1331  N   ASN A 173      -6.593 -20.794 -52.373  1.00 34.16           N  
ATOM   1332  CA  ASN A 173      -6.962 -19.744 -53.337  1.00 34.54           C  
ATOM   1333  C   ASN A 173      -7.023 -18.332 -52.779  1.00 34.85           C  
ATOM   1334  O   ASN A 173      -7.523 -17.417 -53.443  1.00 35.54           O  
ATOM   1335  CB  ASN A 173      -8.282 -20.078 -54.021  1.00 35.28           C  
ATOM   1336  CG  ASN A 173      -8.216 -21.372 -54.760  1.00 35.09           C  
ATOM   1337  OD1 ASN A 173      -7.703 -21.433 -55.875  1.00 37.71           O  
ATOM   1338  ND2 ASN A 173      -8.698 -22.430 -54.134  1.00 36.47           N  
ATOM   1339  N   LEU A 174      -6.510 -18.163 -51.564  1.00 33.65           N  
ATOM   1340  CA  LEU A 174      -6.351 -16.856 -50.970  1.00 33.32           C  
ATOM   1341  C   LEU A 174      -5.510 -15.982 -51.905  1.00 33.10           C  
ATOM   1342  O   LEU A 174      -4.537 -16.461 -52.512  1.00 32.51           O  
ATOM   1343  CB  LEU A 174      -5.636 -17.007 -49.635  1.00 32.94           C  
ATOM   1344  CG  LEU A 174      -5.928 -15.955 -48.586  1.00 35.30           C  
ATOM   1345  CD1 LEU A 174      -7.236 -16.296 -47.907  1.00 36.55           C  
ATOM   1346  CD2 LEU A 174      -4.787 -15.930 -47.585  1.00 35.24           C  
ATOM   1347  N   GLU A 175      -5.908 -14.716 -52.029  1.00 32.75           N  
ATOM   1348  CA  GLU A 175      -5.217 -13.721 -52.838  1.00 33.09           C  
ATOM   1349  C   GLU A 175      -5.041 -12.437 -52.032  1.00 32.88           C  
ATOM   1350  O   GLU A 175      -5.879 -12.123 -51.190  1.00 32.66           O  
ATOM   1351  CB  GLU A 175      -6.047 -13.389 -54.084  1.00 33.30           C  
ATOM   1352  CG  GLU A 175      -6.223 -14.535 -55.084  1.00 36.05           C  
ATOM   1353  CD  GLU A 175      -4.920 -14.969 -55.790  1.00 40.51           C  
ATOM   1354  OE1 GLU A 175      -3.832 -14.375 -55.558  1.00 41.42           O  
ATOM   1355  OE2 GLU A 175      -5.003 -15.914 -56.604  1.00 42.83           O  
ATOM   1356  N   PHE A 176      -3.956 -11.699 -52.279  1.00 33.04           N  
ATOM   1357  CA  PHE A 176      -3.859 -10.318 -51.807  1.00 33.27           C  
ATOM   1358  C   PHE A 176      -4.560  -9.404 -52.786  1.00 33.82           C  
ATOM   1359  O   PHE A 176      -4.199  -9.363 -53.957  1.00 35.27           O  
ATOM   1360  CB  PHE A 176      -2.411  -9.868 -51.635  1.00 33.01           C  
ATOM   1361  CG  PHE A 176      -1.672 -10.609 -50.588  1.00 32.28           C  
ATOM   1362  CD1 PHE A 176      -0.280 -10.726 -50.660  1.00 31.25           C  
ATOM   1363  CD2 PHE A 176      -2.351 -11.199 -49.513  1.00 32.30           C  
ATOM   1364  CE1 PHE A 176       0.428 -11.433 -49.686  1.00 34.81           C  
ATOM   1365  CE2 PHE A 176      -1.656 -11.905 -48.511  1.00 33.13           C  
ATOM   1366  CZ  PHE A 176      -0.270 -12.036 -48.593  1.00 32.99           C  
ATOM   1367  N   VAL A 177      -5.574  -8.691 -52.304  1.00 33.75           N  
ATOM   1368  CA  VAL A 177      -6.399  -7.803 -53.129  1.00 33.61           C  
ATOM   1369  C   VAL A 177      -5.838  -6.395 -53.332  1.00 33.35           C  
ATOM   1370  O   VAL A 177      -6.352  -5.633 -54.155  1.00 32.89           O  
ATOM   1371  CB  VAL A 177      -7.860  -7.713 -52.583  1.00 33.38           C  
ATOM   1372  CG1 VAL A 177      -8.473  -9.081 -52.583  1.00 32.91           C  
ATOM   1373  CG2 VAL A 177      -7.902  -7.122 -51.168  1.00 34.20           C  
ATOM   1374  N   ALA A 178      -4.807  -6.051 -52.561  1.00 33.02           N  
ATOM   1375  CA  ALA A 178      -4.187  -4.741 -52.599  1.00 33.00           C  
ATOM   1376  C   ALA A 178      -2.811  -4.952 -52.036  1.00 34.25           C  
ATOM   1377  O   ALA A 178      -2.647  -5.713 -51.055  1.00 34.32           O  
ATOM   1378  CB  ALA A 178      -4.951  -3.761 -51.734  1.00 32.79           C  
ATOM   1379  N  AMET A 179      -1.822  -4.287 -52.622  0.50 34.40           N  
ATOM   1380  N  BMET A 179      -1.797  -4.337 -52.653  0.50 34.86           N  
ATOM   1381  CA AMET A 179      -0.455  -4.435 -52.158  0.50 35.03           C  
ATOM   1382  CA BMET A 179      -0.422  -4.476 -52.160  0.50 36.39           C  
ATOM   1383  C  AMET A 179      -0.116  -3.391 -51.088  0.50 34.80           C  
ATOM   1384  C  BMET A 179      -0.119  -3.417 -51.093  0.50 35.28           C  
ATOM   1385  O  AMET A 179      -0.587  -2.249 -51.151  0.50 35.05           O  
ATOM   1386  O  BMET A 179      -0.613  -2.287 -51.169  0.50 35.67           O  
ATOM   1387  CB AMET A 179       0.519  -4.382 -53.342  0.50 35.87           C  
ATOM   1388  CB BMET A 179       0.611  -4.430 -53.308  0.50 36.36           C  
ATOM   1389  CG AMET A 179       0.134  -5.282 -54.536  0.50 37.90           C  
ATOM   1390  CG BMET A 179       1.976  -5.125 -52.975  0.50 38.27           C  
ATOM   1391  SD AMET A 179      -0.735  -6.847 -54.147  0.50 42.86           S  
ATOM   1392  SD BMET A 179       3.386  -4.859 -54.104  0.50 41.52           S  
ATOM   1393  CE AMET A 179      -1.847  -6.962 -55.551  0.50 38.71           C  
ATOM   1394  CE BMET A 179       3.126  -3.163 -54.651  0.50 40.24           C  
ATOM   1395  N   PRO A 180       0.677  -3.783 -50.078  1.00 35.01           N  
ATOM   1396  CA  PRO A 180       1.157  -2.775 -49.139  1.00 34.73           C  
ATOM   1397  C   PRO A 180       2.091  -1.748 -49.823  1.00 34.35           C  
ATOM   1398  O   PRO A 180       2.679  -2.045 -50.859  1.00 35.29           O  
ATOM   1399  CB  PRO A 180       1.940  -3.584 -48.119  1.00 34.97           C  
ATOM   1400  CG  PRO A 180       2.304  -4.883 -48.830  1.00 36.55           C  
ATOM   1401  CD  PRO A 180       1.165  -5.149 -49.752  1.00 35.41           C  
ATOM   1402  N   ALA A 181       2.226  -0.557 -49.255  1.00 33.49           N  
ATOM   1403  CA  ALA A 181       3.196   0.427 -49.760  1.00 31.94           C  
ATOM   1404  C   ALA A 181       4.591  -0.188 -49.632  1.00 31.80           C  
ATOM   1405  O   ALA A 181       4.964  -0.617 -48.539  1.00 30.98           O  
ATOM   1406  CB  ALA A 181       3.100   1.666 -48.950  1.00 32.18           C  
ATOM   1407  N   LEU A 182       5.335  -0.281 -50.732  1.00 30.45           N  
ATOM   1408  CA  LEU A 182       6.690  -0.877 -50.697  1.00 30.84           C  
ATOM   1409  C   LEU A 182       7.710   0.200 -51.007  1.00 30.33           C  
ATOM   1410  O   LEU A 182       7.419   1.144 -51.752  1.00 29.89           O  
ATOM   1411  CB  LEU A 182       6.838  -1.997 -51.725  1.00 29.77           C  
ATOM   1412  CG  LEU A 182       5.867  -3.137 -51.493  1.00 32.46           C  
ATOM   1413  CD1 LEU A 182       6.168  -4.179 -52.513  1.00 33.93           C  
ATOM   1414  CD2 LEU A 182       6.005  -3.734 -50.059  1.00 32.77           C  
ATOM   1415  N   ALA A 183       8.894   0.062 -50.427  1.00 30.66           N  
ATOM   1416  CA  ALA A 183      10.013   0.977 -50.721  1.00 30.79           C  
ATOM   1417  C   ALA A 183      10.224   1.067 -52.241  1.00 31.08           C  
ATOM   1418  O   ALA A 183      10.263   0.042 -52.907  1.00 30.93           O  
ATOM   1419  CB  ALA A 183      11.240   0.468 -50.049  1.00 30.45           C  
ATOM   1420  N   PRO A 184      10.342   2.292 -52.804  1.00 31.65           N  
ATOM   1421  CA  PRO A 184      10.649   2.362 -54.247  1.00 32.59           C  
ATOM   1422  C   PRO A 184      11.854   1.474 -54.588  1.00 33.97           C  
ATOM   1423  O   PRO A 184      12.822   1.459 -53.820  1.00 34.76           O  
ATOM   1424  CB  PRO A 184      11.016   3.834 -54.443  1.00 32.61           C  
ATOM   1425  CG  PRO A 184      10.122   4.548 -53.425  1.00 33.12           C  
ATOM   1426  CD  PRO A 184      10.202   3.623 -52.196  1.00 30.71           C  
ATOM   1427  N   PRO A 185      11.789   0.709 -55.704  1.00 35.11           N  
ATOM   1428  CA  PRO A 185      12.913  -0.182 -56.085  1.00 35.18           C  
ATOM   1429  C   PRO A 185      14.239   0.578 -56.235  1.00 34.57           C  
ATOM   1430  O   PRO A 185      14.287   1.686 -56.764  1.00 32.80           O  
ATOM   1431  CB  PRO A 185      12.467  -0.777 -57.423  1.00 35.57           C  
ATOM   1432  CG  PRO A 185      10.946  -0.645 -57.423  1.00 36.89           C  
ATOM   1433  CD  PRO A 185      10.663   0.629 -56.669  1.00 35.76           C  
ATOM   1434  N   GLU A 186      15.308  -0.023 -55.736  1.00 34.62           N  
ATOM   1435  CA  GLU A 186      16.616   0.621 -55.771  1.00 35.16           C  
ATOM   1436  C   GLU A 186      17.473   0.009 -56.854  1.00 34.68           C  
ATOM   1437  O   GLU A 186      18.596   0.439 -57.089  1.00 35.11           O  
ATOM   1438  CB  GLU A 186      17.312   0.520 -54.415  1.00 35.01           C  
ATOM   1439  CG  GLU A 186      16.601   1.327 -53.326  1.00 38.44           C  
ATOM   1440  CD  GLU A 186      16.849   0.793 -51.917  1.00 45.71           C  
ATOM   1441  OE1 GLU A 186      18.033   0.517 -51.574  1.00 48.07           O  
ATOM   1442  OE2 GLU A 186      15.859   0.672 -51.153  1.00 47.87           O  
ATOM   1443  N   VAL A 187      16.904  -0.974 -57.529  1.00 34.56           N  
ATOM   1444  CA  VAL A 187      17.611  -1.802 -58.480  1.00 34.55           C  
ATOM   1445  C   VAL A 187      16.527  -2.302 -59.442  1.00 34.33           C  
ATOM   1446  O   VAL A 187      15.389  -2.448 -59.034  1.00 33.83           O  
ATOM   1447  CB  VAL A 187      18.287  -2.940 -57.656  1.00 34.91           C  
ATOM   1448  CG1 VAL A 187      17.875  -4.322 -58.084  1.00 34.70           C  
ATOM   1449  CG2 VAL A 187      19.817  -2.742 -57.533  1.00 33.93           C  
ATOM   1450  N   VAL A 188      16.842  -2.521 -60.710  1.00 34.55           N  
ATOM   1451  CA  VAL A 188      15.842  -3.137 -61.605  1.00 35.54           C  
ATOM   1452  C   VAL A 188      15.923  -4.675 -61.653  1.00 35.94           C  
ATOM   1453  O   VAL A 188      17.005  -5.269 -61.561  1.00 36.20           O  
ATOM   1454  CB  VAL A 188      15.891  -2.616 -63.049  1.00 35.13           C  
ATOM   1455  CG1 VAL A 188      15.620  -1.122 -63.093  1.00 35.92           C  
ATOM   1456  CG2 VAL A 188      17.204  -2.973 -63.693  1.00 35.08           C  
ATOM   1457  N   MET A 189      14.762  -5.307 -61.798  1.00 36.29           N  
ATOM   1458  CA  MET A 189      14.691  -6.733 -62.148  1.00 36.63           C  
ATOM   1459  C   MET A 189      14.241  -6.851 -63.611  1.00 36.60           C  
ATOM   1460  O   MET A 189      13.118  -6.462 -63.962  1.00 36.46           O  
ATOM   1461  CB  MET A 189      13.730  -7.475 -61.206  1.00 36.95           C  
ATOM   1462  CG  MET A 189      13.687  -8.987 -61.437  1.00 38.36           C  
ATOM   1463  SD  MET A 189      15.264  -9.798 -61.099  1.00 39.35           S  
ATOM   1464  CE  MET A 189      15.039 -11.383 -61.952  1.00 37.08           C  
ATOM   1465  N   ASP A 190      15.140  -7.332 -64.467  1.00 36.99           N  
ATOM   1466  CA  ASP A 190      14.839  -7.546 -65.884  1.00 37.46           C  
ATOM   1467  C   ASP A 190      13.733  -8.622 -66.000  1.00 37.40           C  
ATOM   1468  O   ASP A 190      13.933  -9.756 -65.554  1.00 36.97           O  
ATOM   1469  CB  ASP A 190      16.119  -7.983 -66.616  1.00 37.71           C  
ATOM   1470  CG  ASP A 190      15.936  -8.090 -68.126  1.00 39.13           C  
ATOM   1471  OD1 ASP A 190      14.796  -8.185 -68.606  1.00 40.93           O  
ATOM   1472  OD2 ASP A 190      16.949  -8.096 -68.857  1.00 42.07           O  
ATOM   1473  N   PRO A 191      12.561  -8.265 -66.584  1.00 37.61           N  
ATOM   1474  CA  PRO A 191      11.436  -9.212 -66.639  1.00 37.43           C  
ATOM   1475  C   PRO A 191      11.736 -10.427 -67.525  1.00 36.43           C  
ATOM   1476  O   PRO A 191      11.224 -11.508 -67.256  1.00 36.79           O  
ATOM   1477  CB  PRO A 191      10.274  -8.377 -67.232  1.00 37.67           C  
ATOM   1478  CG  PRO A 191      10.700  -6.968 -67.087  1.00 38.08           C  
ATOM   1479  CD  PRO A 191      12.201  -6.990 -67.235  1.00 37.92           C  
ATOM   1480  N   ALA A 192      12.562 -10.248 -68.554  1.00 35.44           N  
ATOM   1481  CA  ALA A 192      13.035 -11.360 -69.368  1.00 34.31           C  
ATOM   1482  C   ALA A 192      13.972 -12.321 -68.605  1.00 33.83           C  
ATOM   1483  O   ALA A 192      13.965 -13.524 -68.863  1.00 33.75           O  
ATOM   1484  CB  ALA A 192      13.704 -10.851 -70.618  1.00 34.48           C  
ATOM   1485  N   LEU A 193      14.799 -11.794 -67.705  1.00 32.89           N  
ATOM   1486  CA  LEU A 193      15.593 -12.634 -66.823  1.00 32.87           C  
ATOM   1487  C   LEU A 193      14.652 -13.383 -65.854  1.00 32.47           C  
ATOM   1488  O   LEU A 193      14.828 -14.578 -65.601  1.00 32.24           O  
ATOM   1489  CB  LEU A 193      16.546 -11.773 -65.988  1.00 33.16           C  
ATOM   1490  CG  LEU A 193      18.029 -12.118 -65.802  1.00 34.15           C  
ATOM   1491  CD1 LEU A 193      18.402 -11.853 -64.357  1.00 34.36           C  
ATOM   1492  CD2 LEU A 193      18.418 -13.546 -66.233  1.00 35.13           C  
ATOM   1493  N   ALA A 194      13.664 -12.671 -65.315  1.00 31.83           N  
ATOM   1494  CA  ALA A 194      12.700 -13.275 -64.408  1.00 32.16           C  
ATOM   1495  C   ALA A 194      11.972 -14.442 -65.093  1.00 32.94           C  
ATOM   1496  O   ALA A 194      11.722 -15.461 -64.449  1.00 32.75           O  
ATOM   1497  CB  ALA A 194      11.727 -12.265 -63.888  1.00 31.24           C  
ATOM   1498  N   ALA A 195      11.669 -14.302 -66.392  1.00 32.22           N  
ATOM   1499  CA  ALA A 195      11.014 -15.362 -67.142  1.00 32.43           C  
ATOM   1500  C   ALA A 195      11.965 -16.541 -67.413  1.00 32.70           C  
ATOM   1501  O   ALA A 195      11.530 -17.697 -67.426  1.00 32.25           O  
ATOM   1502  CB  ALA A 195      10.424 -14.826 -68.452  1.00 32.16           C  
ATOM   1503  N  AGLN A 196      13.245 -16.247 -67.637  0.50 32.64           N  
ATOM   1504  N  BGLN A 196      13.242 -16.228 -67.651  0.50 32.83           N  
ATOM   1505  CA AGLN A 196      14.229 -17.296 -67.818  0.50 32.96           C  
ATOM   1506  CA BGLN A 196      14.287 -17.228 -67.808  0.50 33.36           C  
ATOM   1507  C  AGLN A 196      14.395 -18.098 -66.518  0.50 33.21           C  
ATOM   1508  C  BGLN A 196      14.395 -18.074 -66.530  0.50 33.42           C  
ATOM   1509  O  AGLN A 196      14.414 -19.327 -66.550  0.50 33.33           O  
ATOM   1510  O  BGLN A 196      14.373 -19.302 -66.590  0.50 33.52           O  
ATOM   1511  CB AGLN A 196      15.565 -16.727 -68.308  0.50 32.99           C  
ATOM   1512  CB BGLN A 196      15.629 -16.555 -68.148  0.50 33.43           C  
ATOM   1513  CG AGLN A 196      16.609 -17.789 -68.634  0.50 32.48           C  
ATOM   1514  CG BGLN A 196      16.861 -17.430 -67.909  0.50 33.37           C  
ATOM   1515  CD AGLN A 196      16.107 -18.847 -69.611  0.50 31.97           C  
ATOM   1516  CD BGLN A 196      18.168 -16.783 -68.352  0.50 34.04           C  
ATOM   1517  OE1AGLN A 196      15.818 -18.554 -70.776  0.50 31.96           O  
ATOM   1518  OE1BGLN A 196      19.103 -16.647 -67.559  0.50 34.41           O  
ATOM   1519  NE2AGLN A 196      16.015 -20.087 -69.140  0.50 31.08           N  
ATOM   1520  NE2BGLN A 196      18.249 -16.407 -69.629  0.50 35.37           N  
ATOM   1521  N   TYR A 197      14.491 -17.399 -65.390  1.00 33.46           N  
ATOM   1522  CA  TYR A 197      14.565 -18.042 -64.071  1.00 34.37           C  
ATOM   1523  C   TYR A 197      13.333 -18.864 -63.688  1.00 35.14           C  
ATOM   1524  O   TYR A 197      13.473 -19.898 -63.030  1.00 34.49           O  
ATOM   1525  CB  TYR A 197      14.790 -17.003 -62.968  1.00 34.72           C  
ATOM   1526  CG  TYR A 197      16.159 -16.377 -62.938  1.00 35.20           C  
ATOM   1527  CD1 TYR A 197      16.393 -15.218 -62.202  1.00 35.50           C  
ATOM   1528  CD2 TYR A 197      17.221 -16.938 -63.650  1.00 34.97           C  
ATOM   1529  CE1 TYR A 197      17.661 -14.646 -62.163  1.00 36.39           C  
ATOM   1530  CE2 TYR A 197      18.471 -16.367 -63.634  1.00 35.74           C  
ATOM   1531  CZ  TYR A 197      18.684 -15.227 -62.882  1.00 35.95           C  
ATOM   1532  OH  TYR A 197      19.941 -14.673 -62.872  1.00 38.54           O  
ATOM   1533  N  AGLU A 198      12.150 -18.365 -64.068  0.50 35.41           N  
ATOM   1534  N  BGLU A 198      12.136 -18.411 -64.064  0.50 35.57           N  
ATOM   1535  CA AGLU A 198      10.878 -19.062 -63.882  0.50 36.06           C  
ATOM   1536  CA BGLU A 198      10.930 -19.186 -63.776  0.50 36.30           C  
ATOM   1537  C  AGLU A 198      10.893 -20.391 -64.632  0.50 36.35           C  
ATOM   1538  C  BGLU A 198      10.889 -20.446 -64.635  0.50 36.53           C  
ATOM   1539  O  AGLU A 198      10.430 -21.411 -64.121  0.50 36.50           O  
ATOM   1540  O  BGLU A 198      10.365 -21.476 -64.208  0.50 36.68           O  
ATOM   1541  CB AGLU A 198       9.702 -18.184 -64.354  0.50 36.07           C  
ATOM   1542  CB BGLU A 198       9.650 -18.364 -63.965  0.50 36.64           C  
ATOM   1543  CG AGLU A 198       9.034 -17.358 -63.224  0.50 36.06           C  
ATOM   1544  CG BGLU A 198       9.526 -17.117 -63.065  0.50 37.63           C  
ATOM   1545  CD AGLU A 198       8.439 -16.005 -63.667  0.50 36.70           C  
ATOM   1546  CD BGLU A 198       9.290 -17.417 -61.584  0.50 39.60           C  
ATOM   1547  OE1AGLU A 198       7.993 -15.870 -64.837  0.50 37.55           O  
ATOM   1548  OE1BGLU A 198      10.179 -17.994 -60.922  0.50 40.25           O  
ATOM   1549  OE2AGLU A 198       8.408 -15.072 -62.816  0.50 36.73           O  
ATOM   1550  OE2BGLU A 198       8.218 -17.032 -61.064  0.50 42.08           O  
ATOM   1551  N   HIS A 199      11.444 -20.359 -65.842  1.00 36.64           N  
ATOM   1552  CA  HIS A 199      11.541 -21.513 -66.718  1.00 37.28           C  
ATOM   1553  C   HIS A 199      12.556 -22.542 -66.190  1.00 38.16           C  
ATOM   1554  O   HIS A 199      12.335 -23.749 -66.308  1.00 38.33           O  
ATOM   1555  CB  HIS A 199      11.923 -21.072 -68.132  1.00 36.79           C  
ATOM   1556  CG  HIS A 199      12.239 -22.211 -69.048  1.00 37.88           C  
ATOM   1557  ND1 HIS A 199      13.516 -22.713 -69.193  1.00 38.13           N  
ATOM   1558  CD2 HIS A 199      11.444 -22.969 -69.840  1.00 38.19           C  
ATOM   1559  CE1 HIS A 199      13.496 -23.717 -70.052  1.00 39.99           C  
ATOM   1560  NE2 HIS A 199      12.251 -23.895 -70.456  1.00 39.80           N  
ATOM   1561  N   ASP A 200      13.670 -22.062 -65.636  1.00 39.13           N  
ATOM   1562  CA  ASP A 200      14.697 -22.931 -65.049  1.00 40.33           C  
ATOM   1563  C   ASP A 200      14.116 -23.719 -63.882  1.00 40.87           C  
ATOM   1564  O   ASP A 200      14.342 -24.922 -63.781  1.00 40.93           O  
ATOM   1565  CB  ASP A 200      15.917 -22.127 -64.592  1.00 40.28           C  
ATOM   1566  CG  ASP A 200      16.665 -21.476 -65.746  1.00 41.26           C  
ATOM   1567  OD1 ASP A 200      16.399 -21.828 -66.920  1.00 40.27           O  
ATOM   1568  OD2 ASP A 200      17.527 -20.603 -65.471  1.00 43.09           O  
ATOM   1569  N   LEU A 201      13.352 -23.040 -63.029  1.00 41.86           N  
ATOM   1570  CA  LEU A 201      12.668 -23.678 -61.907  1.00 43.32           C  
ATOM   1571  C   LEU A 201      11.677 -24.724 -62.373  1.00 44.56           C  
ATOM   1572  O   LEU A 201      11.690 -25.851 -61.871  1.00 45.60           O  
ATOM   1573  CB  LEU A 201      11.961 -22.651 -61.028  1.00 43.33           C  
ATOM   1574  CG  LEU A 201      12.818 -22.006 -59.938  1.00 43.95           C  
ATOM   1575  CD1 LEU A 201      12.091 -20.814 -59.377  1.00 44.06           C  
ATOM   1576  CD2 LEU A 201      13.185 -22.993 -58.814  1.00 43.61           C  
ATOM   1577  N   GLU A 202      10.841 -24.372 -63.347  1.00 45.51           N  
ATOM   1578  CA  GLU A 202       9.934 -25.339 -63.956  1.00 46.65           C  
ATOM   1579  C   GLU A 202      10.678 -26.535 -64.596  1.00 46.90           C  
ATOM   1580  O   GLU A 202      10.146 -27.646 -64.629  1.00 47.55           O  
ATOM   1581  CB  GLU A 202       8.997 -24.645 -64.955  1.00 46.87           C  
ATOM   1582  CG  GLU A 202       7.917 -25.558 -65.565  1.00 48.48           C  
ATOM   1583  CD  GLU A 202       6.659 -24.801 -65.984  1.00 50.22           C  
ATOM   1584  OE1 GLU A 202       6.405 -23.703 -65.424  1.00 50.87           O  
ATOM   1585  OE2 GLU A 202       5.924 -25.313 -66.867  1.00 50.67           O  
ATOM   1586  N   VAL A 203      11.901 -26.312 -65.087  1.00 47.19           N  
ATOM   1587  CA  VAL A 203      12.727 -27.387 -65.690  1.00 47.18           C  
ATOM   1588  C   VAL A 203      13.664 -28.066 -64.664  1.00 47.48           C  
ATOM   1589  O   VAL A 203      14.448 -28.950 -65.014  1.00 48.03           O  
ATOM   1590  CB  VAL A 203      13.508 -26.868 -66.928  1.00 46.92           C  
ATOM   1591  CG1 VAL A 203      14.497 -27.917 -67.460  1.00 47.28           C  
ATOM   1592  CG2 VAL A 203      12.535 -26.460 -68.019  1.00 46.82           C  
ATOM   1593  N   ALA A 204      13.588 -27.633 -63.406  1.00 47.99           N  
ATOM   1594  CA  ALA A 204      14.183 -28.356 -62.283  1.00 48.23           C  
ATOM   1595  C   ALA A 204      13.121 -29.319 -61.760  1.00 48.73           C  
ATOM   1596  O   ALA A 204      13.257 -30.542 -61.912  1.00 48.96           O  
ATOM   1597  CB  ALA A 204      14.636 -27.399 -61.195  1.00 47.83           C  
ATOM   1598  N   GLN A 205      12.056 -28.761 -61.176  1.00 49.08           N  
ATOM   1599  CA  GLN A 205      10.853 -29.515 -60.805  1.00 49.57           C  
ATOM   1600  C   GLN A 205      10.311 -30.318 -61.986  1.00 49.47           C  
ATOM   1601  O   GLN A 205       9.941 -31.480 -61.844  1.00 49.68           O  
ATOM   1602  CB  GLN A 205       9.763 -28.565 -60.318  1.00 49.67           C  
ATOM   1603  CG  GLN A 205      10.133 -27.776 -59.082  1.00 51.12           C  
ATOM   1604  CD  GLN A 205       9.581 -26.347 -59.103  1.00 53.91           C  
ATOM   1605  OE1 GLN A 205       8.604 -26.043 -59.803  1.00 54.98           O  
ATOM   1606  NE2 GLN A 205      10.216 -25.460 -58.334  1.00 53.88           N  
TER    1607      GLN A 205                                                      
ATOM   1608  N   GLY B 713     -14.768 -15.502 -44.515  1.00 46.38           N  
ATOM   1609  CA  GLY B 713     -14.146 -14.384 -43.668  1.00 46.70           C  
ATOM   1610  C   GLY B 713     -13.604 -14.871 -42.332  1.00 46.87           C  
ATOM   1611  O   GLY B 713     -14.350 -14.981 -41.356  1.00 47.00           O  
ATOM   1612  N   PHE B 714     -12.305 -15.161 -42.292  1.00 46.88           N  
ATOM   1613  CA  PHE B 714     -11.608 -15.531 -41.053  1.00 47.16           C  
ATOM   1614  C   PHE B 714     -11.334 -14.275 -40.195  1.00 47.52           C  
ATOM   1615  O   PHE B 714     -11.623 -13.158 -40.641  1.00 47.85           O  
ATOM   1616  CB  PHE B 714     -10.290 -16.251 -41.382  1.00 46.84           C  
ATOM   1617  CG  PHE B 714      -9.254 -15.366 -42.033  1.00 46.31           C  
ATOM   1618  CD1 PHE B 714      -9.101 -15.357 -43.412  1.00 45.94           C  
ATOM   1619  CD2 PHE B 714      -8.434 -14.545 -41.269  1.00 45.60           C  
ATOM   1620  CE1 PHE B 714      -8.147 -14.546 -44.019  1.00 45.66           C  
ATOM   1621  CE2 PHE B 714      -7.485 -13.731 -41.872  1.00 45.82           C  
ATOM   1622  CZ  PHE B 714      -7.341 -13.734 -43.249  1.00 45.52           C  
ATOM   1623  N   GLY B 715     -10.784 -14.427 -38.983  1.00 47.56           N  
ATOM   1624  CA  GLY B 715     -10.492 -15.718 -38.346  1.00 47.66           C  
ATOM   1625  C   GLY B 715     -11.630 -16.149 -37.437  1.00 47.55           C  
ATOM   1626  O   GLY B 715     -12.120 -15.350 -36.636  1.00 47.73           O  
ATOM   1627  N   ASP B 716     -12.043 -17.410 -37.552  1.00 47.09           N  
ATOM   1628  CA  ASP B 716     -13.266 -17.864 -36.889  1.00 46.71           C  
ATOM   1629  C   ASP B 716     -13.213 -17.905 -35.338  1.00 46.32           C  
ATOM   1630  O   ASP B 716     -13.984 -17.148 -34.728  1.00 46.63           O  
ATOM   1631  CB  ASP B 716     -13.843 -19.146 -37.530  1.00 46.71           C  
ATOM   1632  CG  ASP B 716     -15.348 -19.311 -37.289  1.00 46.94           C  
ATOM   1633  OD1 ASP B 716     -15.914 -18.641 -36.394  1.00 47.11           O  
ATOM   1634  OD2 ASP B 716     -15.973 -20.122 -38.007  1.00 46.02           O  
ATOM   1635  N   LYS B 717     -12.394 -18.730 -34.654  1.00 45.33           N  
ATOM   1636  CA  LYS B 717     -11.522 -19.864 -35.102  1.00 44.38           C  
ATOM   1637  C   LYS B 717     -10.173 -19.507 -35.738  1.00 43.23           C  
ATOM   1638  O   LYS B 717      -9.651 -20.206 -36.613  1.00 43.30           O  
ATOM   1639  CB  LYS B 717     -12.265 -21.021 -35.807  1.00 44.72           C  
ATOM   1640  CG  LYS B 717     -11.546 -22.375 -35.703  1.00 44.78           C  
ATOM   1641  CD  LYS B 717     -12.443 -23.540 -36.153  1.00 45.06           C  
ATOM   1642  CE  LYS B 717     -11.686 -24.872 -36.205  1.00 45.92           C  
ATOM   1643  NZ  LYS B 717     -10.632 -24.991 -35.129  1.00 47.00           N  
ATOM   1644  N   PHE B 718      -9.645 -18.391 -35.262  1.00 41.41           N  
ATOM   1645  CA  PHE B 718      -8.228 -18.114 -35.223  1.00 39.61           C  
ATOM   1646  C   PHE B 718      -8.021 -17.193 -34.036  1.00 38.09           C  
ATOM   1647  O   PHE B 718      -6.902 -16.781 -33.749  1.00 38.07           O  
ATOM   1648  CB  PHE B 718      -7.740 -17.466 -36.518  1.00 39.84           C  
ATOM   1649  CG  PHE B 718      -7.000 -18.407 -37.417  1.00 39.78           C  
ATOM   1650  CD1 PHE B 718      -5.651 -18.687 -37.185  1.00 39.14           C  
ATOM   1651  CD2 PHE B 718      -7.649 -19.027 -38.486  1.00 40.04           C  
ATOM   1652  CE1 PHE B 718      -4.958 -19.562 -38.010  1.00 39.00           C  
ATOM   1653  CE2 PHE B 718      -6.968 -19.906 -39.316  1.00 40.09           C  
ATOM   1654  CZ  PHE B 718      -5.615 -20.168 -39.081  1.00 39.86           C  
ATOM   1655  N   LYS B 719      -9.117 -16.862 -33.352  1.00 36.51           N  
ATOM   1656  CA  LYS B 719      -9.049 -15.968 -32.195  1.00 35.35           C  
ATOM   1657  C   LYS B 719      -8.337 -16.662 -31.045  1.00 34.20           C  
ATOM   1658  O   LYS B 719      -8.389 -17.886 -30.955  1.00 33.69           O  
ATOM   1659  CB  LYS B 719     -10.429 -15.419 -31.780  1.00 35.47           C  
ATOM   1660  CG  LYS B 719     -11.465 -16.420 -31.345  1.00 35.18           C  
ATOM   1661  CD  LYS B 719     -12.626 -15.709 -30.673  1.00 36.05           C  
ATOM   1662  CE  LYS B 719     -13.955 -16.266 -31.160  1.00 36.38           C  
ATOM   1663  NZ  LYS B 719     -15.113 -15.976 -30.251  1.00 37.29           N  
ATOM   1664  N   PRO B 720      -7.633 -15.892 -30.188  1.00 33.39           N  
ATOM   1665  CA  PRO B 720      -6.889 -16.554 -29.127  1.00 32.70           C  
ATOM   1666  C   PRO B 720      -7.789 -16.950 -27.958  1.00 31.82           C  
ATOM   1667  O   PRO B 720      -8.940 -16.509 -27.863  1.00 30.74           O  
ATOM   1668  CB  PRO B 720      -5.861 -15.501 -28.686  1.00 33.23           C  
ATOM   1669  CG  PRO B 720      -6.158 -14.243 -29.480  1.00 33.87           C  
ATOM   1670  CD  PRO B 720      -7.491 -14.427 -30.125  1.00 33.58           C  
ATOM   1671  N   ALA B 721      -7.249 -17.804 -27.096  1.00 31.13           N  
ATOM   1672  CA  ALA B 721      -7.909 -18.193 -25.872  1.00 30.36           C  
ATOM   1673  C   ALA B 721      -8.336 -16.907 -25.160  1.00 29.84           C  
ATOM   1674  O   ALA B 721      -7.721 -15.843 -25.333  1.00 28.80           O  
ATOM   1675  CB  ALA B 721      -6.951 -18.976 -25.013  1.00 30.68           C  
ATOM   1676  N   ILE B 722      -9.401 -17.008 -24.385  1.00 29.22           N  
ATOM   1677  CA  ILE B 722      -9.848 -15.901 -23.566  1.00 29.27           C  
ATOM   1678  C   ILE B 722      -8.718 -15.422 -22.632  1.00 29.18           C  
ATOM   1679  O   ILE B 722      -7.919 -16.231 -22.122  1.00 29.60           O  
ATOM   1680  CB  ILE B 722     -11.159 -16.275 -22.830  1.00 28.18           C  
ATOM   1681  CG1 ILE B 722     -12.325 -16.376 -23.834  1.00 28.28           C  
ATOM   1682  CG2 ILE B 722     -11.474 -15.322 -21.686  1.00 28.86           C  
ATOM   1683  CD1 ILE B 722     -12.734 -15.090 -24.531  1.00 26.84           C  
ATOM   1684  N   GLY B 723      -8.629 -14.083 -22.481  1.00 29.17           N  
ATOM   1685  CA  GLY B 723      -7.657 -13.475 -21.593  1.00 29.25           C  
ATOM   1686  C   GLY B 723      -6.227 -13.482 -22.095  1.00 30.03           C  
ATOM   1687  O   GLY B 723      -5.340 -13.035 -21.371  1.00 30.20           O  
ATOM   1688  N   THR B 724      -5.992 -14.006 -23.305  1.00 30.08           N  
ATOM   1689  CA  THR B 724      -4.692 -13.851 -23.988  1.00 30.73           C  
ATOM   1690  C   THR B 724      -4.367 -12.374 -24.142  1.00 31.04           C  
ATOM   1691  O   THR B 724      -5.221 -11.582 -24.558  1.00 30.79           O  
ATOM   1692  CB  THR B 724      -4.690 -14.473 -25.386  1.00 30.15           C  
ATOM   1693  OG1 THR B 724      -4.969 -15.867 -25.288  1.00 32.17           O  
ATOM   1694  CG2 THR B 724      -3.320 -14.317 -26.064  1.00 32.24           C  
ATOM   1695  N   TRP B 725      -3.131 -12.010 -23.808  1.00 31.28           N  
ATOM   1696  CA  TRP B 725      -2.691 -10.623 -23.876  1.00 32.00           C  
ATOM   1697  C   TRP B 725      -1.426 -10.504 -24.739  1.00 32.22           C  
ATOM   1698  O   TRP B 725      -0.558 -11.375 -24.711  1.00 32.03           O  
ATOM   1699  CB  TRP B 725      -2.501 -10.045 -22.459  1.00 31.88           C  
ATOM   1700  CG  TRP B 725      -1.472 -10.783 -21.607  1.00 32.16           C  
ATOM   1701  CD1 TRP B 725      -1.685 -11.882 -20.815  1.00 31.60           C  
ATOM   1702  CD2 TRP B 725      -0.073 -10.471 -21.493  1.00 32.31           C  
ATOM   1703  NE1 TRP B 725      -0.507 -12.270 -20.212  1.00 31.95           N  
ATOM   1704  CE2 TRP B 725       0.495 -11.415 -20.605  1.00 33.07           C  
ATOM   1705  CE3 TRP B 725       0.755  -9.479 -22.056  1.00 32.53           C  
ATOM   1706  CZ2 TRP B 725       1.859 -11.401 -20.263  1.00 32.62           C  
ATOM   1707  CZ3 TRP B 725       2.114  -9.459 -21.709  1.00 32.01           C  
ATOM   1708  CH2 TRP B 725       2.648 -10.416 -20.816  1.00 32.05           C  
ATOM   1709  N   ASP B 726      -1.344  -9.445 -25.536  1.00 32.95           N  
ATOM   1710  CA  ASP B 726      -0.202  -9.253 -26.426  1.00 33.72           C  
ATOM   1711  C   ASP B 726       0.866  -8.424 -25.753  1.00 33.03           C  
ATOM   1712  O   ASP B 726       0.575  -7.353 -25.240  1.00 33.48           O  
ATOM   1713  CB  ASP B 726      -0.630  -8.565 -27.735  1.00 34.31           C  
ATOM   1714  CG  ASP B 726      -1.718  -9.339 -28.478  1.00 37.76           C  
ATOM   1715  OD1 ASP B 726      -1.766 -10.589 -28.365  1.00 41.67           O  
ATOM   1716  OD2 ASP B 726      -2.544  -8.700 -29.178  1.00 41.38           O  
ATOM   1717  N   CYS B 727       2.098  -8.920 -25.765  1.00 32.60           N  
ATOM   1718  CA  CYS B 727       3.263  -8.171 -25.253  1.00 32.32           C  
ATOM   1719  C   CYS B 727       3.461  -6.848 -26.011  1.00 32.47           C  
ATOM   1720  O   CYS B 727       3.517  -6.837 -27.235  1.00 31.66           O  
ATOM   1721  CB  CYS B 727       4.526  -9.023 -25.359  1.00 32.21           C  
ATOM   1722  SG  CYS B 727       6.114  -8.227 -24.813  1.00 31.28           S  
ATOM   1723  N   ASP B 728       3.552  -5.736 -25.280  1.00 32.67           N  
ATOM   1724  CA  ASP B 728       3.769  -4.427 -25.913  1.00 33.75           C  
ATOM   1725  C   ASP B 728       5.200  -4.260 -26.397  1.00 33.32           C  
ATOM   1726  O   ASP B 728       5.515  -3.269 -27.032  1.00 33.28           O  
ATOM   1727  CB  ASP B 728       3.426  -3.277 -24.963  1.00 34.13           C  
ATOM   1728  CG  ASP B 728       2.006  -3.356 -24.453  1.00 37.88           C  
ATOM   1729  OD1 ASP B 728       1.104  -3.666 -25.273  1.00 41.01           O  
ATOM   1730  OD2 ASP B 728       1.788  -3.121 -23.230  1.00 42.11           O  
ATOM   1731  N   THR B 729       6.069  -5.207 -26.069  1.00 33.34           N  
ATOM   1732  CA  THR B 729       7.440  -5.122 -26.524  1.00 33.78           C  
ATOM   1733  C   THR B 729       7.655  -5.895 -27.820  1.00 33.94           C  
ATOM   1734  O   THR B 729       8.349  -5.397 -28.684  1.00 34.19           O  
ATOM   1735  CB  THR B 729       8.464  -5.579 -25.450  1.00 34.14           C  
ATOM   1736  OG1 THR B 729       8.325  -4.787 -24.266  1.00 34.55           O  
ATOM   1737  CG2 THR B 729       9.888  -5.443 -25.965  1.00 32.32           C  
ATOM   1738  N   CYS B 730       7.041  -7.075 -27.972  1.00 34.46           N  
ATOM   1739  CA  CYS B 730       7.531  -8.024 -28.979  1.00 35.24           C  
ATOM   1740  C   CYS B 730       6.688  -8.764 -30.076  1.00 34.70           C  
ATOM   1741  O   CYS B 730       7.263  -9.489 -30.842  1.00 36.15           O  
ATOM   1742  CB  CYS B 730       8.499  -9.016 -28.312  1.00 34.04           C  
ATOM   1743  SG  CYS B 730       7.689 -10.459 -27.665  1.00 36.45           S  
ATOM   1744  N   LEU B 731       5.398  -8.742 -30.246  1.00 35.62           N  
ATOM   1745  CA  LEU B 731       4.286  -8.507 -29.449  1.00 34.36           C  
ATOM   1746  C   LEU B 731       3.760  -9.957 -29.504  1.00 34.27           C  
ATOM   1747  O   LEU B 731       2.794 -10.275 -30.212  1.00 33.16           O  
ATOM   1748  CB  LEU B 731       3.371  -7.661 -30.334  1.00 35.63           C  
ATOM   1749  CG  LEU B 731       3.869  -6.380 -31.008  1.00 33.84           C  
ATOM   1750  CD1 LEU B 731       4.293  -6.562 -32.451  1.00 37.08           C  
ATOM   1751  CD2 LEU B 731       2.716  -5.401 -30.945  1.00 34.81           C  
ATOM   1752  N   VAL B 732       4.485 -10.860 -28.854  1.00 33.79           N  
ATOM   1753  CA  VAL B 732       4.052 -12.217 -28.683  1.00 34.69           C  
ATOM   1754  C   VAL B 732       2.746 -12.239 -27.863  1.00 35.79           C  
ATOM   1755  O   VAL B 732       2.485 -11.349 -27.029  1.00 35.79           O  
ATOM   1756  CB  VAL B 732       5.199 -13.069 -28.045  1.00 34.60           C  
ATOM   1757  CG1 VAL B 732       4.666 -14.277 -27.307  1.00 33.95           C  
ATOM   1758  CG2 VAL B 732       6.216 -13.474 -29.129  1.00 32.68           C  
ATOM   1759  N   GLN B 733       1.922 -13.246 -28.143  1.00 36.64           N  
ATOM   1760  CA  GLN B 733       0.656 -13.457 -27.456  1.00 37.37           C  
ATOM   1761  C   GLN B 733       0.860 -14.386 -26.261  1.00 37.62           C  
ATOM   1762  O   GLN B 733       1.382 -15.493 -26.387  1.00 37.31           O  
ATOM   1763  CB  GLN B 733      -0.361 -14.036 -28.434  1.00 37.70           C  
ATOM   1764  CG  GLN B 733      -0.555 -13.175 -29.675  1.00 40.15           C  
ATOM   1765  CD  GLN B 733      -1.521 -13.800 -30.666  1.00 44.21           C  
ATOM   1766  OE1 GLN B 733      -1.118 -14.591 -31.529  1.00 44.53           O  
ATOM   1767  NE2 GLN B 733      -2.803 -13.441 -30.552  1.00 43.29           N  
ATOM   1768  N   ASN B 734       0.456 -13.916 -25.094  1.00 37.23           N  
ATOM   1769  CA  ASN B 734       0.787 -14.602 -23.878  1.00 37.91           C  
ATOM   1770  C   ASN B 734      -0.438 -15.148 -23.180  1.00 37.76           C  
ATOM   1771  O   ASN B 734      -1.515 -14.562 -23.274  1.00 37.92           O  
ATOM   1772  CB  ASN B 734       1.575 -13.664 -22.978  1.00 37.66           C  
ATOM   1773  CG  ASN B 734       3.018 -13.573 -23.390  1.00 38.80           C  
ATOM   1774  OD1 ASN B 734       3.424 -12.633 -24.080  1.00 40.04           O  
ATOM   1775  ND2 ASN B 734       3.802 -14.575 -23.008  1.00 39.34           N  
ATOM   1776  N   LYS B 735      -0.267 -16.282 -22.503  1.00 38.68           N  
ATOM   1777  CA  LYS B 735      -1.367 -16.969 -21.813  1.00 38.65           C  
ATOM   1778  C   LYS B 735      -1.882 -16.054 -20.707  1.00 38.78           C  
ATOM   1779  O   LYS B 735      -1.099 -15.232 -20.199  1.00 38.39           O  
ATOM   1780  CB  LYS B 735      -0.863 -18.275 -21.199  1.00 39.32           C  
ATOM   1781  CG  LYS B 735      -0.345 -19.329 -22.184  1.00 38.82           C  
ATOM   1782  CD  LYS B 735      -0.268 -20.714 -21.418  1.00 40.31           C  
ATOM   1783  CE  LYS B 735       0.223 -21.844 -22.357  1.00 41.91           C  
ATOM   1784  NZ  LYS B 735       1.447 -21.460 -23.178  1.00 43.01           N  
ATOM   1785  N   PRO B 736      -3.193 -16.170 -20.333  1.00 38.97           N  
ATOM   1786  CA  PRO B 736      -3.676 -15.231 -19.312  1.00 39.17           C  
ATOM   1787  C   PRO B 736      -2.911 -15.290 -17.984  1.00 39.78           C  
ATOM   1788  O   PRO B 736      -2.781 -14.258 -17.304  1.00 40.21           O  
ATOM   1789  CB  PRO B 736      -5.162 -15.585 -19.141  1.00 39.60           C  
ATOM   1790  CG  PRO B 736      -5.388 -16.862 -19.868  1.00 39.76           C  
ATOM   1791  CD  PRO B 736      -4.264 -17.061 -20.852  1.00 38.52           C  
ATOM   1792  N   GLU B 737      -2.387 -16.472 -17.639  1.00 40.52           N  
ATOM   1793  CA  GLU B 737      -1.588 -16.672 -16.406  1.00 41.11           C  
ATOM   1794  C   GLU B 737      -0.149 -16.102 -16.479  1.00 40.45           C  
ATOM   1795  O   GLU B 737       0.532 -16.003 -15.459  1.00 41.23           O  
ATOM   1796  CB  GLU B 737      -1.515 -18.173 -16.043  1.00 41.33           C  
ATOM   1797  CG  GLU B 737      -2.712 -19.043 -16.506  1.00 44.45           C  
ATOM   1798  CD  GLU B 737      -2.367 -19.958 -17.790  1.00 47.20           C  
ATOM   1799  OE1 GLU B 737      -1.387 -20.788 -17.793  1.00 49.84           O  
ATOM   1800  OE2 GLU B 737      -3.084 -19.821 -18.818  1.00 50.48           O  
ATOM   1801  N   ALA B 738       0.330 -15.762 -17.684  1.00 40.10           N  
ATOM   1802  CA  ALA B 738       1.695 -15.247 -17.842  1.00 39.12           C  
ATOM   1803  C   ALA B 738       1.865 -13.872 -17.138  1.00 38.67           C  
ATOM   1804  O   ALA B 738       1.068 -12.951 -17.421  1.00 38.03           O  
ATOM   1805  CB  ALA B 738       2.088 -15.204 -19.321  1.00 39.12           C  
ATOM   1806  N   VAL B 739       2.878 -13.748 -16.306  1.00 38.41           N  
ATOM   1807  CA  VAL B 739       3.141 -12.479 -15.612  1.00 38.01           C  
ATOM   1808  C   VAL B 739       4.183 -11.702 -16.431  1.00 37.99           C  
ATOM   1809  O   VAL B 739       4.164 -10.454 -16.359  1.00 37.93           O  
ATOM   1810  CB  VAL B 739       3.597 -12.713 -14.133  1.00 38.27           C  
ATOM   1811  CG1 VAL B 739       4.461 -11.555 -13.660  1.00 38.61           C  
ATOM   1812  CG2 VAL B 739       2.393 -12.929 -13.224  1.00 37.52           C  
ATOM   1813  N   LYS B 740       5.091 -12.478 -17.090  1.00 37.28           N  
ATOM   1814  CA  LYS B 740       6.107 -11.938 -17.985  1.00 37.18           C  
ATOM   1815  C   LYS B 740       5.804 -12.440 -19.383  1.00 36.07           C  
ATOM   1816  O   LYS B 740       5.160 -13.476 -19.564  1.00 36.01           O  
ATOM   1817  CB  LYS B 740       7.492 -12.446 -17.589  1.00 36.88           C  
ATOM   1818  CG  LYS B 740       8.091 -11.763 -16.300  1.00 37.74           C  
ATOM   1819  CD  LYS B 740       9.513 -12.273 -16.026  1.00 37.59           C  
ATOM   1820  CE  LYS B 740       9.457 -13.728 -15.480  1.00 38.99           C  
ATOM   1821  NZ  LYS B 740      10.787 -14.111 -14.904  1.00 39.43           N  
ATOM   1822  N   CYS B 741       6.281 -11.717 -20.387  1.00 35.70           N  
ATOM   1823  CA  CYS B 741       6.211 -12.228 -21.740  1.00 35.18           C  
ATOM   1824  C   CYS B 741       7.119 -13.453 -21.879  1.00 35.29           C  
ATOM   1825  O   CYS B 741       8.284 -13.447 -21.443  1.00 35.29           O  
ATOM   1826  CB  CYS B 741       6.560 -11.166 -22.760  1.00 35.33           C  
ATOM   1827  SG  CYS B 741       6.717 -11.923 -24.326  1.00 34.49           S  
ATOM   1828  N   VAL B 742       6.560 -14.511 -22.462  1.00 35.27           N  
ATOM   1829  CA  VAL B 742       7.237 -15.800 -22.594  1.00 34.94           C  
ATOM   1830  C   VAL B 742       8.481 -15.692 -23.488  1.00 34.84           C  
ATOM   1831  O   VAL B 742       9.466 -16.402 -23.280  1.00 34.69           O  
ATOM   1832  CB  VAL B 742       6.258 -16.923 -23.090  1.00 35.29           C  
ATOM   1833  CG1 VAL B 742       5.880 -16.740 -24.573  1.00 34.20           C  
ATOM   1834  CG2 VAL B 742       6.834 -18.315 -22.831  1.00 35.09           C  
ATOM   1835  N   ALA B 743       8.452 -14.795 -24.466  1.00 34.35           N  
ATOM   1836  CA  ALA B 743       9.591 -14.651 -25.351  1.00 34.06           C  
ATOM   1837  C   ALA B 743      10.642 -13.679 -24.805  1.00 34.20           C  
ATOM   1838  O   ALA B 743      11.823 -14.033 -24.734  1.00 34.44           O  
ATOM   1839  CB  ALA B 743       9.144 -14.247 -26.785  1.00 33.54           C  
ATOM   1840  N   CYS B 744      10.225 -12.457 -24.448  1.00 34.04           N  
ATOM   1841  CA  CYS B 744      11.167 -11.363 -24.164  1.00 33.98           C  
ATOM   1842  C   CYS B 744      11.288 -11.016 -22.682  1.00 34.53           C  
ATOM   1843  O   CYS B 744      12.073 -10.140 -22.314  1.00 34.91           O  
ATOM   1844  CB  CYS B 744      10.791 -10.096 -24.949  1.00 33.90           C  
ATOM   1845  SG  CYS B 744       9.442  -9.139 -24.203  1.00 32.40           S  
ATOM   1846  N   GLU B 745      10.489 -11.686 -21.851  1.00 34.98           N  
ATOM   1847  CA  GLU B 745      10.508 -11.520 -20.404  1.00 35.61           C  
ATOM   1848  C   GLU B 745      10.027 -10.156 -19.881  1.00 35.65           C  
ATOM   1849  O   GLU B 745      10.155  -9.878 -18.687  1.00 35.49           O  
ATOM   1850  CB  GLU B 745      11.891 -11.891 -19.836  1.00 36.21           C  
ATOM   1851  CG  GLU B 745      12.366 -13.319 -20.151  1.00 38.01           C  
ATOM   1852  CD  GLU B 745      11.586 -14.382 -19.403  1.00 41.22           C  
ATOM   1853  OE1 GLU B 745      12.083 -14.846 -18.347  1.00 42.13           O  
ATOM   1854  OE2 GLU B 745      10.475 -14.747 -19.862  1.00 41.80           O  
ATOM   1855  N   THR B 746       9.452  -9.319 -20.750  1.00 35.38           N  
ATOM   1856  CA  THR B 746       8.850  -8.060 -20.300  1.00 35.98           C  
ATOM   1857  C   THR B 746       7.605  -8.333 -19.470  1.00 36.57           C  
ATOM   1858  O   THR B 746       6.740  -9.087 -19.908  1.00 36.12           O  
ATOM   1859  CB  THR B 746       8.459  -7.140 -21.465  1.00 35.91           C  
ATOM   1860  OG1 THR B 746       9.613  -6.868 -22.255  1.00 36.16           O  
ATOM   1861  CG2 THR B 746       7.889  -5.813 -20.954  1.00 36.26           C  
ATOM   1862  N   PRO B 747       7.517  -7.725 -18.268  1.00 37.64           N  
ATOM   1863  CA  PRO B 747       6.368  -7.950 -17.399  1.00 38.60           C  
ATOM   1864  C   PRO B 747       5.090  -7.383 -17.990  1.00 39.65           C  
ATOM   1865  O   PRO B 747       5.120  -6.331 -18.641  1.00 39.69           O  
ATOM   1866  CB  PRO B 747       6.739  -7.203 -16.101  1.00 38.67           C  
ATOM   1867  CG  PRO B 747       7.767  -6.209 -16.494  1.00 38.48           C  
ATOM   1868  CD  PRO B 747       8.503  -6.807 -17.660  1.00 37.88           C  
ATOM   1869  N   LYS B 748       3.995  -8.113 -17.781  1.00 40.73           N  
ATOM   1870  CA  LYS B 748       2.634  -7.695 -18.136  1.00 41.87           C  
ATOM   1871  C   LYS B 748       2.279  -6.353 -17.487  1.00 42.18           C  
ATOM   1872  O   LYS B 748       2.467  -6.178 -16.277  1.00 42.43           O  
ATOM   1873  CB  LYS B 748       1.631  -8.783 -17.708  1.00 41.73           C  
ATOM   1874  CG  LYS B 748       0.150  -8.412 -17.805  1.00 42.48           C  
ATOM   1875  CD  LYS B 748      -0.732  -9.610 -17.412  1.00 42.45           C  
ATOM   1876  CE  LYS B 748      -2.218  -9.246 -17.263  1.00 43.38           C  
ATOM   1877  NZ  LYS B 748      -2.685  -9.098 -15.828  1.00 42.97           N  
ATOM   1878  N   PRO B 749       1.776  -5.400 -18.294  1.00 42.53           N  
ATOM   1879  CA  PRO B 749       1.313  -4.114 -17.764  1.00 42.74           C  
ATOM   1880  C   PRO B 749      -0.022  -4.244 -17.024  1.00 42.71           C  
ATOM   1881  O   PRO B 749      -0.031  -4.393 -15.796  1.00 42.65           O  
ATOM   1882  CB  PRO B 749       1.149  -3.261 -19.026  1.00 42.82           C  
ATOM   1883  CG  PRO B 749       0.859  -4.244 -20.104  1.00 42.68           C  
ATOM   1884  CD  PRO B 749       1.633  -5.479 -19.761  1.00 42.50           C  
TER    1885      PRO B 749                                                      
HETATM 1886  PB  GDP A 220      21.235  -9.308 -43.655  1.00 28.74           P  
HETATM 1887  O1B GDP A 220      20.237  -8.548 -42.781  1.00 27.47           O  
HETATM 1888  O2B GDP A 220      22.566  -9.366 -42.934  1.00 29.41           O  
HETATM 1889  O3B GDP A 220      20.812 -10.719 -43.946  1.00 24.62           O  
HETATM 1890  O3A GDP A 220      21.443  -8.557 -45.063  1.00 29.20           O  
HETATM 1891  PA  GDP A 220      21.340  -6.951 -45.236  1.00 27.52           P  
HETATM 1892  O1A GDP A 220      19.890  -6.627 -45.428  1.00 29.66           O  
HETATM 1893  O2A GDP A 220      21.960  -6.141 -44.164  1.00 27.70           O  
HETATM 1894  O5' GDP A 220      22.064  -6.749 -46.657  1.00 31.00           O  
HETATM 1895  C5' GDP A 220      23.345  -7.303 -46.974  1.00 32.60           C  
HETATM 1896  C4' GDP A 220      23.860  -6.638 -48.256  1.00 33.23           C  
HETATM 1897  O4' GDP A 220      23.144  -7.143 -49.392  1.00 33.30           O  
HETATM 1898  C3' GDP A 220      23.613  -5.148 -48.254  1.00 35.59           C  
HETATM 1899  O3' GDP A 220      24.751  -4.531 -48.840  1.00 40.52           O  
HETATM 1900  C2' GDP A 220      22.437  -4.931 -49.177  1.00 35.14           C  
HETATM 1901  O2' GDP A 220      22.550  -3.690 -49.862  1.00 35.67           O  
HETATM 1902  C1' GDP A 220      22.568  -6.070 -50.138  1.00 32.53           C  
HETATM 1903  N9  GDP A 220      21.281  -6.556 -50.675  1.00 33.25           N  
HETATM 1904  C8  GDP A 220      20.217  -6.942 -49.960  1.00 30.94           C  
HETATM 1905  N7  GDP A 220      19.246  -7.376 -50.761  1.00 30.57           N  
HETATM 1906  C5  GDP A 220      19.677  -7.261 -52.018  1.00 30.82           C  
HETATM 1907  C6  GDP A 220      19.105  -7.527 -53.346  1.00 31.45           C  
HETATM 1908  O6  GDP A 220      17.949  -7.974 -53.448  1.00 31.75           O  
HETATM 1909  N1  GDP A 220      19.881  -7.291 -54.420  1.00 32.53           N  
HETATM 1910  C2  GDP A 220      21.135  -6.795 -54.325  1.00 31.92           C  
HETATM 1911  N2  GDP A 220      21.820  -6.588 -55.470  1.00 31.94           N  
HETATM 1912  N3  GDP A 220      21.726  -6.504 -53.129  1.00 32.58           N  
HETATM 1913  C4  GDP A 220      21.035  -6.728 -51.970  1.00 31.52           C  
HETATM 1914 MG    MG A 221      20.205  -7.805 -40.922  1.00 22.72          MG  
HETATM 1915  S   SO4 A 222      -0.116  -0.568 -46.082  0.50 26.98           S  
HETATM 1916  O1  SO4 A 222       0.817  -0.340 -44.999  0.50 26.04           O  
HETATM 1917  O2  SO4 A 222      -1.238   0.356 -45.958  0.50 25.92           O  
HETATM 1918  O3  SO4 A 222       0.562  -0.289 -47.326  0.50 25.45           O  
HETATM 1919  O4  SO4 A 222      -0.573  -1.973 -46.041  0.50 25.47           O  
HETATM 1920 ZN    ZN B 800       7.485  -9.910 -25.377  1.00 44.77          ZN  
HETATM 1921  O   HOH A 223       3.671  -0.451 -46.106  1.00 23.40           O  
HETATM 1922  O   HOH A 224      15.261  -2.202 -48.037  1.00 26.32           O  
HETATM 1923  O   HOH A 225       9.184  -3.426 -42.479  1.00 24.77           O  
HETATM 1924  O   HOH A 226      16.705 -11.687 -39.527  1.00 30.89           O  
HETATM 1925  O   HOH A 227       3.860  -0.067 -53.217  1.00 31.18           O  
HETATM 1926  O   HOH A 228      24.632  -7.627 -43.108  1.00 30.29           O  
HETATM 1927  O   HOH A 229      10.254 -18.052 -57.956  1.00 39.57           O  
HETATM 1928  O   HOH A 230      12.192   0.788 -45.293  1.00 39.65           O  
HETATM 1929  O   HOH A 231      21.536 -18.743 -45.373  1.00 32.29           O  
HETATM 1930  O   HOH A 232      11.373  -8.867 -52.943  1.00 32.93           O  
HETATM 1931  O   HOH A 233      19.564  -2.041 -61.522  1.00 36.85           O  
HETATM 1932  O   HOH A 234      12.467   3.445 -57.939  1.00 33.09           O  
HETATM 1933  O   HOH A 235      -2.512 -12.063 -54.574  1.00 37.03           O  
HETATM 1934  O   HOH A 236      21.372  -6.117 -41.527  1.00 30.16           O  
HETATM 1935  O   HOH A 237       7.098  -9.308 -58.190  1.00 41.05           O  
HETATM 1936  O   HOH A 238       1.717  -2.612 -41.156  1.00 36.05           O  
HETATM 1937  O   HOH A 239      13.868   2.725 -51.563  1.00 33.96           O  
HETATM 1938  O   HOH A 240      15.242  -4.749 -38.899  1.00 28.64           O  
HETATM 1939  O   HOH A 241       7.813  -2.075 -56.445  1.00 41.57           O  
HETATM 1940  O   HOH A 242      -2.585  -2.380 -54.746  1.00 40.27           O  
HETATM 1941  O   HOH A 243      -1.582  -7.206 -49.337  1.00 43.15           O  
HETATM 1942  O   HOH A 244      21.450  -5.399 -59.626  1.00 41.92           O  
HETATM 1943  O   HOH A 245      -0.406  -0.318 -52.549  0.50 28.96           O  
HETATM 1944  O   HOH A 246      15.245   4.270 -55.781  1.00 42.85           O  
HETATM 1945  O   HOH A 247       8.646 -11.848 -66.613  1.00 36.45           O  
HETATM 1946  O   HOH A 248       6.976 -22.602 -32.512  1.00 41.30           O  
HETATM 1947  O   HOH A 249      26.087 -15.602 -40.783  1.00 41.14           O  
HETATM 1948  O   HOH A 250      -8.701  -6.834 -47.557  1.00 42.52           O  
HETATM 1949  O   HOH A 251      17.008  -5.109 -36.747  1.00 40.15           O  
HETATM 1950  O   HOH A 252       1.977 -14.615 -32.169  1.00 40.79           O  
HETATM 1951  O   HOH A 253      24.418 -18.035 -37.680  1.00 44.68           O  
HETATM 1952  O   HOH A 254       7.007   1.550 -54.477  1.00 35.46           O  
HETATM 1953  O   HOH A 255       9.619  -2.674 -28.128  1.00 47.18           O  
HETATM 1954  O   HOH A 256      14.095   0.209 -47.256  1.00 44.70           O  
HETATM 1955  O   HOH A 257      10.384   4.595 -41.181  1.00 41.70           O  
HETATM 1956  O   HOH A 258      20.198  -2.762 -48.068  1.00 51.56           O  
HETATM 1957  O   HOH A 259       8.604   2.231 -34.673  1.00 43.59           O  
HETATM 1958  O   HOH A 260      17.979  -7.861 -63.340  1.00 48.74           O  
HETATM 1959  O   HOH A 261      12.255  -3.902 -61.817  1.00 47.47           O  
HETATM 1960  O   HOH A 262      13.166 -14.584 -71.230  1.00 40.99           O  
HETATM 1961  O   HOH A 263      28.034 -12.671 -58.076  1.00 48.93           O  
HETATM 1962  O   HOH A 264      28.183 -14.687 -47.591  1.00 48.28           O  
HETATM 1963  O   HOH A 265      19.003  -9.360 -40.105  1.00 35.87           O  
HETATM 1964  O   HOH A 266      12.165 -16.772 -60.540  1.00 41.41           O  
HETATM 1965  O   HOH A 267      -7.035  -5.685 -45.176  1.00 35.04           O  
HETATM 1966  O   HOH A 268      18.090 -20.489 -61.646  1.00 43.74           O  
HETATM 1967  O   HOH A 269      21.918  -9.094 -40.394  1.00 31.17           O  
HETATM 1968  O   HOH A 270      20.064  -6.930 -39.152  1.00 31.81           O  
HETATM 1969  O   HOH A 271      25.021  -7.593 -51.960  1.00 40.51           O  
HETATM 1970  O   HOH A 272       8.534   3.703 -43.452  1.00 37.85           O  
HETATM 1971  O   HOH A 273       6.467  -6.770 -55.596  1.00 35.76           O  
HETATM 1972  O   HOH A 274       7.235 -22.059 -29.851  1.00 53.66           O  
HETATM 1973  O   HOH A 275       0.450  -2.043 -43.326  1.00 50.77           O  
HETATM 1974  O   HOH A 276       9.850  -6.428 -59.829  1.00 49.88           O  
HETATM 1975  O   HOH A 277     -10.640 -17.879 -51.756  1.00 53.05           O  
HETATM 1976  O   HOH A 278      -2.294 -16.132 -33.993  1.00 48.19           O  
HETATM 1977  O   HOH A 279      -0.484   1.758 -39.227  1.00 44.11           O  
HETATM 1978  O   HOH A 280      19.808 -13.842 -30.353  1.00 38.86           O  
HETATM 1979  O   HOH A 281      26.780  -8.007 -46.278  1.00 59.74           O  
HETATM 1980  O   HOH A 282      17.253  -1.765 -38.135  1.00 55.83           O  
HETATM 1981  O   HOH A 283      21.337  -3.344 -41.075  1.00 41.35           O  
HETATM 1982  O   HOH A 284      13.368  -5.611 -24.202  1.00 44.64           O  
HETATM 1983  O   HOH A 285      21.976  -9.694 -29.016  1.00 50.67           O  
HETATM 1984  O   HOH A 286      29.840 -18.402 -53.888  1.00 49.93           O  
HETATM 1985  O   HOH A 287      30.368 -19.280 -51.530  1.00 55.75           O  
HETATM 1986  O   HOH A 288       9.201 -24.926 -54.076  1.00 48.17           O  
HETATM 1987  O   HOH A 289       9.488 -20.713 -57.386  1.00 56.20           O  
HETATM 1988  O   HOH B 801     -10.134 -12.236 -24.473  1.00 43.49           O  
HETATM 1989  O   HOH B 802       5.833 -11.126 -32.334  1.00 29.37           O  
HETATM 1990  O   HOH B 803       3.030 -12.277 -32.479  1.00 35.22           O  
HETATM 1991  O   HOH B 804       2.369 -16.957 -22.402  1.00 45.68           O  
CONECT  128 1914                                                                
CONECT 1722 1920                                                                
CONECT 1743 1920                                                                
CONECT 1827 1920                                                                
CONECT 1845 1920                                                                
CONECT 1886 1887 1888 1889 1890                                                 
CONECT 1887 1886 1914                                                           
CONECT 1888 1886                                                                
CONECT 1889 1886                                                                
CONECT 1890 1886 1891                                                           
CONECT 1891 1890 1892 1893 1894                                                 
CONECT 1892 1891                                                                
CONECT 1893 1891                                                                
CONECT 1894 1891 1895                                                           
CONECT 1895 1894 1896                                                           
CONECT 1896 1895 1897 1898                                                      
CONECT 1897 1896 1902                                                           
CONECT 1898 1896 1899 1900                                                      
CONECT 1899 1898                                                                
CONECT 1900 1898 1901 1902                                                      
CONECT 1901 1900                                                                
CONECT 1902 1897 1900 1903                                                      
CONECT 1903 1902 1904 1913                                                      
CONECT 1904 1903 1905                                                           
CONECT 1905 1904 1906                                                           
CONECT 1906 1905 1907 1913                                                      
CONECT 1907 1906 1908 1909                                                      
CONECT 1908 1907                                                                
CONECT 1909 1907 1910                                                           
CONECT 1910 1909 1911 1912                                                      
CONECT 1911 1910                                                                
CONECT 1912 1910 1913                                                           
CONECT 1913 1903 1906 1912                                                      
CONECT 1914  128 1887 1934 1963                                                 
CONECT 1914 1967 1968                                                           
CONECT 1915 1916 1917 1918 1919                                                 
CONECT 1916 1915                                                                
CONECT 1917 1915                                                                
CONECT 1918 1915                                                                
CONECT 1919 1915                                                                
CONECT 1920 1722 1743 1827 1845                                                 
CONECT 1934 1914                                                                
CONECT 1963 1914                                                                
CONECT 1967 1914                                                                
CONECT 1968 1914                                                                
MASTER      487    0    4    8   12    0    7    6 1926    2   45   21          
END

Display Options: Goto PDB code: 3D presentation of molecule is powered by 3Dmol, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button: left to rotate,middle to shift,right to zoom

Related entries of code: 3ch5

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
3gj6	RCSB PDB PDBbind	34aa, >3GJ6_2\|Chain... at 100%
3gj7	RCSB PDB PDBbind	98aa, >3GJ7_2\|Chains... *
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	3ch5
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	RanGDP
Ligand Name	Nup153-ZnF2
EC.Number	E.C.-.-.-.-
Resolution	2.1(Å)
Affinity (Kd/Ki/IC50)	Kd=120uM
Release Year	2008
Protein/NA Sequence	Check fasta file
Primary Reference	(2008) Structure Vol. 16: pp. 1116-1125

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): P49791 P62826
Entrez Gene ID	NCBI Entrez Gene ID: 5901
ASD	Information of known allosteric effects of PDB entries

This site has been visited

times since Nov 2007.

Technical Support（技术支持）: yingsaisi@foxmail.com