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***  PEPTIDE RECOGNITION 20-MAY-98 1BE9  ***

elNémo ID: 2102200935209848

Job options:

ID        	=	 2102200935209848
JOBID     	=	 PEPTIDE RECOGNITION 20-MAY-98 1BE9
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    PEPTIDE RECOGNITION                     20-MAY-98   1BE9              
TITLE     THE THIRD PDZ DOMAIN FROM THE SYNAPTIC PROTEIN PSD-95 IN COMPLEX WITH 
TITLE    2 A C-TERMINAL PEPTIDE DERIVED FROM CRIPT.                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PSD-95;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: THE THIRD PDZ DOMAIN OF PSD-95;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CRIPT;                                                     
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: C-TERMINAL PEPTIDE                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1;                                
SOURCE   9 MOL_ID: 2                                                            
KEYWDS    PEPTIDE RECOGNITION, PROTEIN LOCALIZATION                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.DOYLE,A.LEE,J.LEWIS,E.KIM,M.SHENG,R.MACKINNON                     
REVDAT   5   07-MAR-18 1BE9    1       REMARK                                   
REVDAT   4   22-SEP-10 1BE9    1       REMARK                                   
REVDAT   3   24-FEB-09 1BE9    1       VERSN                                    
REVDAT   2   01-APR-03 1BE9    1       JRNL                                     
REVDAT   1   21-OCT-98 1BE9    0                                                
JRNL        AUTH   D.A.DOYLE,A.LEE,J.LEWIS,E.KIM,M.SHENG,R.MACKINNON            
JRNL        TITL   CRYSTAL STRUCTURES OF A COMPLEXED AND PEPTIDE-FREE MEMBRANE  
JRNL        TITL 2 PROTEIN-BINDING DOMAIN: MOLECULAR BASIS OF PEPTIDE           
JRNL        TITL 3 RECOGNITION BY PDZ.                                          
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  85  1067 1996              
JRNL        PUBL   CELL PRESS                                                   
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   8674113                                                      
JRNL        DOI    10.1016/S0092-8674(00)81307-0                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.L.DANIELS,A.R.COHEN,J.M.ANDERSON,A.T.BRUNGER               
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE HCASK PDZ DOMAIN REVEALS THE        
REMARK   1  TITL 2 STRUCTURAL BASIS OF CLASS II PDZ DOMAIN TARGET RECOGNITION   
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   5   317 1998              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.NIETHAMMER,J.G.VALTSCHANOFF,T.M.KAPOOR,D.W.ALLISON,        
REMARK   1  AUTH 2 T.M.WEINBERG,A.M.CRAIG,M.SHENG                               
REMARK   1  TITL   CRIPT, A NOVEL POSTSYNAPTIC PROTEIN THAT BINDS TO THE THIRD  
REMARK   1  TITL 2 PDZ DOMAIN OF PSD-95/SAP90                                   
REMARK   1  REF    NEURON                        V.  20   693 1998              
REMARK   1  REFN                   ISSN 0896-6273                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.CABRAL,C.PETOSA,M.J.SUTCLIFFE,S.RAZA,O.BYRON,F.POY,        
REMARK   1  AUTH 2 S.M.MARFATIA,A.H.CHISHTI,R.C.LIDDINGTON                      
REMARK   1  TITL   CRYSTAL STRUCTURE OF A PDZ DOMAIN                            
REMARK   1  REF    NATURE                        V. 382   649 1996              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 899                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171651.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : SIEMENS                            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : COLLIMATOR                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11108                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200  ANALYSIS                                                            
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE PEPTIDE-FREE PDZ3 MODEL WAS USED IN A RIGID BODY         
REMARK 200  REFINEMENT, FOLLOWED BY CYCLES OF LEAST-SQUARES REFINEMENT AND      
REMARK 200  MODEL BUILDING.                                                     
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M SODIUM CITRATE, 0.1 M HEPES, PH    
REMARK 280  7.5                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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       44.67000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.67000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.67000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.67000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.67000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.67000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       44.67000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       44.67000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       44.67000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       44.67000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       44.67000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       44.67000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       44.67000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       44.67000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       44.67000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       44.67000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       44.67000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       44.67000            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       67.00500            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       22.33500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       22.33500            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       67.00500            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       67.00500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       67.00500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       22.33500            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       22.33500            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       67.00500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       22.33500            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       67.00500            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       22.33500            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       67.00500            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       22.33500            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       22.33500            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       22.33500            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       67.00500            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       22.33500            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       67.00500            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       67.00500            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       67.00500            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       22.33500            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       22.33500            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       67.00500            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       67.00500            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       22.33500            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       22.33500            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       22.33500            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       22.33500            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       67.00500            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       22.33500            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       67.00500            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       22.33500            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       67.00500            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       67.00500            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       67.00500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 760 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 6510 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   297                                                      
REMARK 465     SER A   298                                                      
REMARK 465     PRO A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE A 301    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 332    CG   OD1  OD2                                       
REMARK 470     LYS B   5    CG   CD   CE   NZ                                   
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    GLU A 334      -59.02      7.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: PEP                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: RESIDUES INVOLVED IN THE BINDING OF THE FOUR C     
REMARK 800  -TERMINAL RESIDUES OF CRIPT.                                        
DBREF  1BE9 A  298   414  UNP    P31016   DLG4_RAT       295    420             
DBREF  1BE9 B    5     9  PDB    1BE9     1BE9             5      9             
SEQADV 1BE9     A       UNP  P31016    VAL   297 DELETION                       
SEQADV 1BE9     A       UNP  P31016    ALA   298 DELETION                       
SEQADV 1BE9     A       UNP  P31016    LYS   299 DELETION                       
SEQADV 1BE9 GLU A  300  UNP  P31016    ASP   300 CONFLICT                       
SEQADV 1BE9 PHE A  301  UNP  P31016    LEU   301 CONFLICT                       
SEQADV 1BE9 ILE A  328  UNP  P31016    VAL   328 CONFLICT                       
SEQADV 1BE9     A       UNP  P31016    LYS   403 DELETION                       
SEQADV 1BE9     A       UNP  P31016    ILE   404 DELETION                       
SEQADV 1BE9     A       UNP  P31016    HIS   405 DELETION                       
SEQADV 1BE9     A       UNP  P31016    ASP   406 DELETION                       
SEQADV 1BE9     A       UNP  P31016    LEU   407 DELETION                       
SEQADV 1BE9     A       UNP  P31016    ARG   408 DELETION                       
SEQADV 1BE9 ASN A  403  UNP  P31016    GLU   409 CONFLICT                       
SEQADV 1BE9 SER A  404  UNP  P31016    GLN   410 CONFLICT                       
SEQADV 1BE9 ARG A  405  UNP  P31016    LEU   411 CONFLICT                       
SEQADV 1BE9 VAL A  406  UNP  P31016    MET   412 CONFLICT                       
SEQADV 1BE9 GLY A  410  UNP  P31016    LEU   416 CONFLICT                       
SEQADV 1BE9 ARG A  411  UNP  P31016    GLY   417 CONFLICT                       
SEQADV 1BE9 ILE A  412  UNP  P31016    SER   418 CONFLICT                       
SEQADV 1BE9 VAL A  413  UNP  P31016    GLY   419 CONFLICT                       
SEQRES   1 A  119  GLY SER PRO GLU PHE LEU GLY GLU GLU ASP ILE PRO ARG          
SEQRES   2 A  119  GLU PRO ARG ARG ILE VAL ILE HIS ARG GLY SER THR GLY          
SEQRES   3 A  119  LEU GLY PHE ASN ILE ILE GLY GLY GLU ASP GLY GLU GLY          
SEQRES   4 A  119  ILE PHE ILE SER PHE ILE LEU ALA GLY GLY PRO ALA ASP          
SEQRES   5 A  119  LEU SER GLY GLU LEU ARG LYS GLY ASP GLN ILE LEU SER          
SEQRES   6 A  119  VAL ASN GLY VAL ASP LEU ARG ASN ALA SER HIS GLU GLN          
SEQRES   7 A  119  ALA ALA ILE ALA LEU LYS ASN ALA GLY GLN THR VAL THR          
SEQRES   8 A  119  ILE ILE ALA GLN TYR LYS PRO GLU GLU TYR SER ARG PHE          
SEQRES   9 A  119  GLU ALA ASN SER ARG VAL ASN SER SER GLY ARG ILE VAL          
SEQRES  10 A  119  THR ASN                                                      
SEQRES   1 B    5  LYS GLN THR SER VAL                                          
FORMUL   3  HOH   *146(H2 O)                                                    
HELIX    1   1 LEU A  302  GLU A  304  5                                   3    
HELIX    2   2 PRO A  346  SER A  350  1                                   5    
HELIX    3   3 HIS A  372  LYS A  380  1                                   9    
HELIX    4   4 PRO A  394  ARG A  399  1                                   6    
SHEET    1   A 3 ARG A 312  HIS A 317  0                                        
SHEET    2   A 3 THR A 385  TYR A 392 -1  N  ALA A 390   O  ARG A 312           
SHEET    3   A 3 ASP A 357  VAL A 362 -1  N  SER A 361   O  ILE A 389           
SHEET    1   B 2 SER A 404  VAL A 406  0                                        
SHEET    2   B 2 ILE A 412  THR A 414 -1  N  VAL A 413   O  ARG A 405           
SHEET    1   C 2 PHE A 325  GLY A 329  0                                        
SHEET    2   C 2 ILE A 336  ILE A 341 -1  N  PHE A 340   O  ASN A 326           
SITE     1 PEP  9 GLY A 322  LEU A 323  GLY A 324  PHE A 325                    
SITE     2 PEP  9 ASN A 326  ILE A 327  SER A 339  HIS A 372                    
SITE     3 PEP  9 LEU A 379                                                     
CRYST1   89.340   89.340   89.340  90.00  90.00  90.00 P 41 3 2     24          
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      0.011193  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011193  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011193        0.00000                         
ATOM      1  N   PHE A 301      60.491  64.723  43.937  1.00 46.74           N  
ATOM      2  CA  PHE A 301      59.665  65.467  44.936  1.00 47.04           C  
ATOM      3  C   PHE A 301      58.206  65.030  44.972  1.00 47.68           C  
ATOM      4  O   PHE A 301      57.855  64.059  45.638  1.00 48.40           O  
ATOM      5  CB  PHE A 301      59.738  66.973  44.672  1.00 47.19           C  
ATOM      6  N   LEU A 302      57.353  65.771  44.273  1.00 47.77           N  
ATOM      7  CA  LEU A 302      55.930  65.460  44.229  1.00 48.13           C  
ATOM      8  C   LEU A 302      55.710  63.975  43.957  1.00 48.63           C  
ATOM      9  O   LEU A 302      54.909  63.324  44.631  1.00 47.21           O  
ATOM     10  CB  LEU A 302      55.241  66.279  43.132  1.00 49.52           C  
ATOM     11  CG  LEU A 302      55.502  67.789  43.077  1.00 49.38           C  
ATOM     12  CD1 LEU A 302      54.858  68.380  41.824  1.00 50.42           C  
ATOM     13  CD2 LEU A 302      54.940  68.446  44.321  1.00 48.37           C  
ATOM     14  N   GLY A 303      56.440  63.455  42.969  1.00 49.39           N  
ATOM     15  CA  GLY A 303      56.331  62.061  42.559  1.00 49.20           C  
ATOM     16  C   GLY A 303      56.369  60.996  43.638  1.00 48.54           C  
ATOM     17  O   GLY A 303      56.195  59.806  43.359  1.00 47.23           O  
ATOM     18  N   GLU A 304      56.593  61.415  44.874  1.00 48.36           N  
ATOM     19  CA  GLU A 304      56.648  60.478  45.980  1.00 48.84           C  
ATOM     20  C   GLU A 304      55.431  60.652  46.881  1.00 46.67           C  
ATOM     21  O   GLU A 304      55.248  59.915  47.850  1.00 48.06           O  
ATOM     22  CB  GLU A 304      57.956  60.686  46.741  1.00 54.47           C  
ATOM     23  CG  GLU A 304      59.160  60.631  45.800  1.00 59.72           C  
ATOM     24  CD  GLU A 304      60.461  61.060  46.443  1.00 63.78           C  
ATOM     25  OE1 GLU A 304      60.424  61.766  47.476  1.00 65.46           O  
ATOM     26  OE2 GLU A 304      61.527  60.688  45.905  1.00 65.83           O  
ATOM     27  N   GLU A 305      54.594  61.628  46.540  1.00 40.78           N  
ATOM     28  CA  GLU A 305      53.376  61.897  47.293  1.00 36.71           C  
ATOM     29  C   GLU A 305      52.269  61.054  46.686  1.00 32.98           C  
ATOM     30  O   GLU A 305      52.228  60.858  45.471  1.00 30.51           O  
ATOM     31  CB  GLU A 305      53.003  63.375  47.193  1.00 38.76           C  
ATOM     32  CG  GLU A 305      54.152  64.325  47.471  1.00 40.45           C  
ATOM     33  CD  GLU A 305      53.715  65.772  47.470  1.00 40.61           C  
ATOM     34  OE1 GLU A 305      52.703  66.088  46.808  1.00 39.25           O  
ATOM     35  OE2 GLU A 305      54.386  66.591  48.133  1.00 44.78           O  
ATOM     36  N   ASP A 306      51.368  60.562  47.525  1.00 28.60           N  
ATOM     37  CA  ASP A 306      50.281  59.726  47.039  1.00 30.37           C  
ATOM     38  C   ASP A 306      49.301  60.508  46.176  1.00 28.08           C  
ATOM     39  O   ASP A 306      48.973  61.653  46.478  1.00 26.38           O  
ATOM     40  CB  ASP A 306      49.538  59.092  48.217  1.00 34.12           C  
ATOM     41  CG  ASP A 306      50.437  58.203  49.064  1.00 39.04           C  
ATOM     42  OD1 ASP A 306      51.441  57.671  48.530  1.00 36.45           O  
ATOM     43  OD2 ASP A 306      50.138  58.040  50.269  1.00 41.96           O  
ATOM     44  N   ILE A 307      48.847  59.886  45.093  1.00 25.30           N  
ATOM     45  CA  ILE A 307      47.884  60.523  44.205  1.00 21.89           C  
ATOM     46  C   ILE A 307      46.501  60.413  44.863  1.00 20.31           C  
ATOM     47  O   ILE A 307      46.085  59.332  45.267  1.00 17.92           O  
ATOM     48  CB  ILE A 307      47.872  59.829  42.817  1.00 21.13           C  
ATOM     49  CG1 ILE A 307      49.250  59.977  42.157  1.00 21.72           C  
ATOM     50  CG2 ILE A 307      46.796  60.448  41.924  1.00 18.43           C  
ATOM     51  CD1 ILE A 307      49.413  59.214  40.854  1.00 23.93           C  
ATOM     52  N   PRO A 308      45.783  61.542  45.002  1.00 18.93           N  
ATOM     53  CA  PRO A 308      44.453  61.495  45.625  1.00 18.88           C  
ATOM     54  C   PRO A 308      43.543  60.460  44.966  1.00 17.94           C  
ATOM     55  O   PRO A 308      43.438  60.403  43.741  1.00 13.21           O  
ATOM     56  CB  PRO A 308      43.934  62.923  45.465  1.00 18.25           C  
ATOM     57  CG  PRO A 308      45.185  63.758  45.363  1.00 16.52           C  
ATOM     58  CD  PRO A 308      46.162  62.911  44.610  1.00 15.24           C  
ATOM     59  N   ARG A 309      42.886  59.643  45.785  1.00 16.37           N  
ATOM     60  CA  ARG A 309      42.015  58.605  45.252  1.00 15.10           C  
ATOM     61  C   ARG A 309      40.523  58.894  45.404  1.00 15.59           C  
ATOM     62  O   ARG A 309      39.683  58.084  45.006  1.00 15.12           O  
ATOM     63  CB  ARG A 309      42.380  57.253  45.881  1.00 16.26           C  
ATOM     64  CG  ARG A 309      43.570  56.588  45.190  1.00 17.86           C  
ATOM     65  CD  ARG A 309      44.106  55.425  45.990  1.00 16.83           C  
ATOM     66  NE  ARG A 309      45.320  54.873  45.394  1.00 17.91           N  
ATOM     67  CZ  ARG A 309      45.346  53.855  44.538  1.00 20.17           C  
ATOM     68  NH1 ARG A 309      44.219  53.270  44.159  1.00 20.06           N  
ATOM     69  NH2 ARG A 309      46.500  53.407  44.064  1.00 21.33           N  
ATOM     70  N   GLU A 310      40.190  60.052  45.968  1.00 16.80           N  
ATOM     71  CA  GLU A 310      38.781  60.422  46.120  1.00 18.33           C  
ATOM     72  C   GLU A 310      38.282  61.093  44.827  1.00 16.50           C  
ATOM     73  O   GLU A 310      39.079  61.588  44.030  1.00 14.19           O  
ATOM     74  CB  GLU A 310      38.593  61.349  47.327  1.00 19.63           C  
ATOM     75  CG  GLU A 310      38.634  62.855  47.055  1.00 30.81           C  
ATOM     76  CD  GLU A 310      38.303  63.671  48.316  1.00 39.26           C  
ATOM     77  OE1 GLU A 310      38.866  63.368  49.401  1.00 45.57           O  
ATOM     78  OE2 GLU A 310      37.474  64.616  48.250  1.00 42.33           O  
ATOM     79  N   PRO A 311      36.953  61.087  44.599  1.00 15.93           N  
ATOM     80  CA  PRO A 311      36.424  61.714  43.380  1.00 13.50           C  
ATOM     81  C   PRO A 311      36.711  63.203  43.347  1.00 13.49           C  
ATOM     82  O   PRO A 311      36.789  63.853  44.393  1.00 16.15           O  
ATOM     83  CB  PRO A 311      34.920  61.432  43.424  1.00 14.51           C  
ATOM     84  CG  PRO A 311      34.695  60.524  44.560  1.00 15.67           C  
ATOM     85  CD  PRO A 311      35.905  60.500  45.439  1.00 14.21           C  
ATOM     86  N   ARG A 312      36.888  63.725  42.133  1.00 11.90           N  
ATOM     87  CA  ARG A 312      37.164  65.134  41.906  1.00 13.21           C  
ATOM     88  C   ARG A 312      36.256  65.675  40.808  1.00 13.50           C  
ATOM     89  O   ARG A 312      35.872  64.944  39.899  1.00 12.93           O  
ATOM     90  CB  ARG A 312      38.612  65.347  41.446  1.00 12.92           C  
ATOM     91  CG  ARG A 312      39.688  64.936  42.433  1.00 15.05           C  
ATOM     92  CD  ARG A 312      40.598  63.857  41.859  1.00 10.73           C  
ATOM     93  NE  ARG A 312      41.010  64.126  40.487  1.00 10.18           N  
ATOM     94  CZ  ARG A 312      41.123  63.187  39.556  1.00 12.03           C  
ATOM     95  NH1 ARG A 312      40.844  61.926  39.855  1.00 11.50           N  
ATOM     96  NH2 ARG A 312      41.511  63.503  38.329  1.00 10.70           N  
ATOM     97  N   ARG A 313      35.906  66.955  40.891  1.00 13.84           N  
ATOM     98  CA  ARG A 313      35.106  67.556  39.831  1.00 15.73           C  
ATOM     99  C   ARG A 313      36.075  68.363  38.976  1.00 12.83           C  
ATOM    100  O   ARG A 313      36.901  69.103  39.495  1.00 14.36           O  
ATOM    101  CB  ARG A 313      34.028  68.479  40.380  1.00 17.02           C  
ATOM    102  CG  ARG A 313      33.237  69.167  39.271  1.00 19.80           C  
ATOM    103  CD  ARG A 313      32.370  70.290  39.806  1.00 21.89           C  
ATOM    104  NE  ARG A 313      31.368  69.799  40.747  1.00 22.79           N  
ATOM    105  CZ  ARG A 313      31.498  69.834  42.071  1.00 22.23           C  
ATOM    106  NH1 ARG A 313      32.593  70.338  42.627  1.00 19.04           N  
ATOM    107  NH2 ARG A 313      30.523  69.369  42.841  1.00 22.82           N  
ATOM    108  N   ILE A 314      35.991  68.192  37.665  1.00 15.57           N  
ATOM    109  CA  ILE A 314      36.863  68.917  36.750  1.00 16.15           C  
ATOM    110  C   ILE A 314      35.982  69.601  35.717  1.00 15.41           C  
ATOM    111  O   ILE A 314      35.194  68.950  35.033  1.00 17.90           O  
ATOM    112  CB  ILE A 314      37.848  67.967  36.015  1.00 15.89           C  
ATOM    113  CG1 ILE A 314      38.748  67.255  37.028  1.00 15.48           C  
ATOM    114  CG2 ILE A 314      38.691  68.759  35.021  1.00 13.51           C  
ATOM    115  CD1 ILE A 314      38.258  65.861  37.431  1.00 16.31           C  
ATOM    116  N   VAL A 315      36.098  70.918  35.624  1.00 16.89           N  
ATOM    117  CA  VAL A 315      35.310  71.661  34.656  1.00 18.70           C  
ATOM    118  C   VAL A 315      36.225  72.114  33.536  1.00 17.83           C  
ATOM    119  O   VAL A 315      37.137  72.914  33.734  1.00 18.32           O  
ATOM    120  CB  VAL A 315      34.629  72.879  35.293  1.00 20.18           C  
ATOM    121  CG1 VAL A 315      33.876  73.676  34.229  1.00 22.50           C  
ATOM    122  CG2 VAL A 315      33.672  72.414  36.380  1.00 14.77           C  
ATOM    123  N   ILE A 316      35.974  71.581  32.352  1.00 19.96           N  
ATOM    124  CA  ILE A 316      36.777  71.904  31.194  1.00 19.29           C  
ATOM    125  C   ILE A 316      35.996  72.772  30.221  1.00 18.88           C  
ATOM    126  O   ILE A 316      34.867  72.454  29.852  1.00 17.02           O  
ATOM    127  CB  ILE A 316      37.230  70.618  30.484  1.00 20.46           C  
ATOM    128  CG1 ILE A 316      38.185  69.844  31.399  1.00 18.40           C  
ATOM    129  CG2 ILE A 316      37.874  70.954  29.144  1.00 19.54           C  
ATOM    130  CD1 ILE A 316      38.967  68.766  30.696  1.00 18.49           C  
ATOM    131  N   HIS A 317      36.602  73.886  29.830  1.00 18.87           N  
ATOM    132  CA  HIS A 317      35.985  74.788  28.874  1.00 23.24           C  
ATOM    133  C   HIS A 317      36.733  74.548  27.570  1.00 21.52           C  
ATOM    134  O   HIS A 317      37.865  74.996  27.407  1.00 26.66           O  
ATOM    135  CB  HIS A 317      36.145  76.234  29.347  1.00 25.70           C  
ATOM    136  CG  HIS A 317      35.611  76.466  30.725  1.00 27.94           C  
ATOM    137  ND1 HIS A 317      34.264  76.471  31.006  1.00 26.80           N  
ATOM    138  CD2 HIS A 317      36.248  76.657  31.905  1.00 28.12           C  
ATOM    139  CE1 HIS A 317      34.090  76.652  32.306  1.00 29.48           C  
ATOM    140  NE2 HIS A 317      35.277  76.768  32.871  1.00 30.52           N  
ATOM    141  N   ARG A 318      36.107  73.826  26.647  1.00 20.49           N  
ATOM    142  CA  ARG A 318      36.759  73.500  25.382  1.00 19.81           C  
ATOM    143  C   ARG A 318      36.070  74.076  24.158  1.00 18.16           C  
ATOM    144  O   ARG A 318      36.464  73.791  23.026  1.00 19.50           O  
ATOM    145  CB  ARG A 318      36.864  71.980  25.234  1.00 16.72           C  
ATOM    146  CG  ARG A 318      35.588  71.242  25.601  1.00 14.85           C  
ATOM    147  CD  ARG A 318      34.648  71.160  24.410  1.00 13.51           C  
ATOM    148  NE  ARG A 318      33.597  70.169  24.611  1.00 15.66           N  
ATOM    149  CZ  ARG A 318      33.608  68.944  24.091  1.00 17.94           C  
ATOM    150  NH1 ARG A 318      34.622  68.544  23.334  1.00 18.48           N  
ATOM    151  NH2 ARG A 318      32.608  68.108  24.346  1.00 18.05           N  
ATOM    152  N   GLY A 319      35.044  74.886  24.379  1.00 17.11           N  
ATOM    153  CA  GLY A 319      34.343  75.466  23.251  1.00 19.37           C  
ATOM    154  C   GLY A 319      33.942  74.392  22.261  1.00 19.56           C  
ATOM    155  O   GLY A 319      33.214  73.465  22.613  1.00 19.45           O  
ATOM    156  N   SER A 320      34.420  74.501  21.027  1.00 20.48           N  
ATOM    157  CA  SER A 320      34.067  73.521  20.007  1.00 22.84           C  
ATOM    158  C   SER A 320      35.264  72.720  19.540  1.00 20.94           C  
ATOM    159  O   SER A 320      35.435  72.455  18.350  1.00 21.21           O  
ATOM    160  CB  SER A 320      33.402  74.207  18.812  1.00 22.02           C  
ATOM    161  OG  SER A 320      31.999  74.246  18.986  1.00 21.22           O  
ATOM    162  N   THR A 321      36.094  72.325  20.494  1.00 22.15           N  
ATOM    163  CA  THR A 321      37.271  71.539  20.183  1.00 18.92           C  
ATOM    164  C   THR A 321      37.227  70.252  21.000  1.00 16.89           C  
ATOM    165  O   THR A 321      36.437  70.127  21.937  1.00 15.13           O  
ATOM    166  CB  THR A 321      38.562  72.342  20.486  1.00 24.16           C  
ATOM    167  OG1 THR A 321      38.596  72.714  21.873  1.00 23.85           O  
ATOM    168  CG2 THR A 321      38.604  73.611  19.629  1.00 21.26           C  
ATOM    169  N   GLY A 322      38.052  69.284  20.625  1.00 16.33           N  
ATOM    170  CA  GLY A 322      38.077  68.031  21.349  1.00 15.88           C  
ATOM    171  C   GLY A 322      38.557  68.252  22.771  1.00 16.25           C  
ATOM    172  O   GLY A 322      39.191  69.261  23.067  1.00 16.85           O  
ATOM    173  N   LEU A 323      38.250  67.309  23.655  1.00 16.16           N  
ATOM    174  CA  LEU A 323      38.665  67.403  25.048  1.00 14.78           C  
ATOM    175  C   LEU A 323      40.160  67.124  25.149  1.00 13.20           C  
ATOM    176  O   LEU A 323      40.832  67.593  26.069  1.00 14.11           O  
ATOM    177  CB  LEU A 323      37.874  66.409  25.899  1.00 12.62           C  
ATOM    178  CG  LEU A 323      36.451  66.895  26.183  1.00 14.27           C  
ATOM    179  CD1 LEU A 323      35.521  65.729  26.412  1.00 10.09           C  
ATOM    180  CD2 LEU A 323      36.473  67.807  27.391  1.00 15.83           C  
ATOM    181  N   GLY A 324      40.681  66.359  24.196  1.00 10.17           N  
ATOM    182  CA  GLY A 324      42.097  66.074  24.204  1.00  8.68           C  
ATOM    183  C   GLY A 324      42.540  64.898  25.045  1.00 10.96           C  
ATOM    184  O   GLY A 324      43.581  64.961  25.711  1.00 12.00           O  
ATOM    185  N   PHE A 325      41.738  63.838  25.060  1.00 12.66           N  
ATOM    186  CA  PHE A 325      42.118  62.620  25.768  1.00 12.59           C  
ATOM    187  C   PHE A 325      41.445  61.386  25.188  1.00 12.59           C  
ATOM    188  O   PHE A 325      40.454  61.480  24.460  1.00 11.46           O  
ATOM    189  CB  PHE A 325      41.900  62.733  27.289  1.00 11.85           C  
ATOM    190  CG  PHE A 325      40.463  62.819  27.720  1.00 13.45           C  
ATOM    191  CD1 PHE A 325      39.692  61.671  27.862  1.00 12.91           C  
ATOM    192  CD2 PHE A 325      39.914  64.042  28.094  1.00 14.38           C  
ATOM    193  CE1 PHE A 325      38.389  61.737  28.376  1.00 12.50           C  
ATOM    194  CE2 PHE A 325      38.615  64.119  28.608  1.00 14.20           C  
ATOM    195  CZ  PHE A 325      37.855  62.960  28.752  1.00 11.37           C  
ATOM    196  N   ASN A 326      42.039  60.236  25.484  1.00 15.98           N  
ATOM    197  CA  ASN A 326      41.581  58.931  25.006  1.00 18.26           C  
ATOM    198  C   ASN A 326      40.897  58.159  26.133  1.00 14.20           C  
ATOM    199  O   ASN A 326      41.284  58.273  27.294  1.00 11.07           O  
ATOM    200  CB  ASN A 326      42.783  58.099  24.532  1.00 20.99           C  
ATOM    201  CG  ASN A 326      43.110  58.296  23.064  1.00 23.08           C  
ATOM    202  OD1 ASN A 326      42.847  59.347  22.482  1.00 20.96           O  
ATOM    203  ND2 ASN A 326      43.699  57.273  22.460  1.00 28.01           N  
ATOM    204  N   ILE A 327      39.889  57.372  25.783  1.00 13.72           N  
ATOM    205  CA  ILE A 327      39.198  56.557  26.771  1.00 14.13           C  
ATOM    206  C   ILE A 327      39.232  55.100  26.330  1.00 12.55           C  
ATOM    207  O   ILE A 327      39.238  54.807  25.137  1.00 13.43           O  
ATOM    208  CB  ILE A 327      37.703  56.973  26.954  1.00 16.22           C  
ATOM    209  CG1 ILE A 327      36.951  56.879  25.621  1.00 14.36           C  
ATOM    210  CG2 ILE A 327      37.616  58.378  27.532  1.00 16.00           C  
ATOM    211  CD1 ILE A 327      35.449  56.733  25.784  1.00 11.90           C  
ATOM    212  N   ILE A 328      39.289  54.203  27.308  1.00 12.94           N  
ATOM    213  CA  ILE A 328      39.273  52.761  27.077  1.00 14.88           C  
ATOM    214  C   ILE A 328      38.246  52.197  28.065  1.00 16.30           C  
ATOM    215  O   ILE A 328      37.899  52.854  29.048  1.00 12.07           O  
ATOM    216  CB  ILE A 328      40.643  52.100  27.358  1.00 15.57           C  
ATOM    217  CG1 ILE A 328      41.048  52.333  28.811  1.00 18.59           C  
ATOM    218  CG2 ILE A 328      41.689  52.671  26.453  1.00 16.98           C  
ATOM    219  CD1 ILE A 328      42.482  51.993  29.097  1.00 27.69           C  
ATOM    220  N   GLY A 329      37.769  50.985  27.803  1.00 18.81           N  
ATOM    221  CA  GLY A 329      36.783  50.366  28.669  1.00 20.74           C  
ATOM    222  C   GLY A 329      35.371  50.490  28.120  1.00 19.78           C  
ATOM    223  O   GLY A 329      35.171  50.885  26.970  1.00 19.50           O  
ATOM    224  N   GLY A 330      34.384  50.171  28.947  1.00 24.57           N  
ATOM    225  CA  GLY A 330      33.008  50.253  28.503  1.00 29.06           C  
ATOM    226  C   GLY A 330      32.507  48.914  28.009  1.00 34.01           C  
ATOM    227  O   GLY A 330      31.429  48.823  27.416  1.00 37.98           O  
ATOM    228  N   GLU A 331      33.297  47.873  28.231  1.00 38.49           N  
ATOM    229  CA  GLU A 331      32.897  46.532  27.828  1.00 44.72           C  
ATOM    230  C   GLU A 331      32.596  45.694  29.065  1.00 44.82           C  
ATOM    231  O   GLU A 331      33.464  45.454  29.905  1.00 47.68           O  
ATOM    232  CB  GLU A 331      33.993  45.870  26.989  1.00 46.07           C  
ATOM    233  CG  GLU A 331      33.994  46.358  25.559  1.00 53.49           C  
ATOM    234  CD  GLU A 331      35.146  45.830  24.740  1.00 61.07           C  
ATOM    235  OE1 GLU A 331      35.843  44.892  25.203  1.00 65.76           O  
ATOM    236  OE2 GLU A 331      35.357  46.356  23.616  1.00 64.90           O  
ATOM    237  N   ASP A 332      31.342  45.293  29.202  1.00 46.50           N  
ATOM    238  CA  ASP A 332      30.945  44.453  30.318  1.00 48.45           C  
ATOM    239  C   ASP A 332      31.215  45.014  31.711  1.00 48.79           C  
ATOM    240  O   ASP A 332      31.824  44.332  32.539  1.00 51.57           O  
ATOM    241  CB  ASP A 332      31.631  43.102  30.191  1.00 48.50           C  
ATOM    242  N   GLY A 333      30.788  46.243  31.977  1.00 48.90           N  
ATOM    243  CA  GLY A 333      30.996  46.798  33.307  1.00 48.17           C  
ATOM    244  C   GLY A 333      32.223  47.674  33.474  1.00 47.11           C  
ATOM    245  O   GLY A 333      32.091  48.872  33.718  1.00 50.84           O  
ATOM    246  N   GLU A 334      33.404  47.076  33.353  1.00 45.31           N  
ATOM    247  CA  GLU A 334      34.694  47.770  33.473  1.00 43.63           C  
ATOM    248  C   GLU A 334      34.710  49.245  33.917  1.00 39.13           C  
ATOM    249  O   GLU A 334      35.335  49.599  34.922  1.00 40.54           O  
ATOM    250  CB  GLU A 334      35.466  47.660  32.150  1.00 47.36           C  
ATOM    251  CG  GLU A 334      35.988  46.272  31.857  1.00 57.08           C  
ATOM    252  CD  GLU A 334      36.680  45.647  33.052  1.00 65.38           C  
ATOM    253  OE1 GLU A 334      37.294  46.399  33.855  1.00 68.10           O  
ATOM    254  OE2 GLU A 334      36.613  44.398  33.198  1.00 71.28           O  
ATOM    255  N   GLY A 335      34.042  50.112  33.164  1.00 31.77           N  
ATOM    256  CA  GLY A 335      34.038  51.524  33.501  1.00 22.95           C  
ATOM    257  C   GLY A 335      34.790  52.248  32.399  1.00 19.05           C  
ATOM    258  O   GLY A 335      35.392  51.591  31.546  1.00 15.92           O  
ATOM    259  N   ILE A 336      34.763  53.580  32.406  1.00 15.28           N  
ATOM    260  CA  ILE A 336      35.446  54.372  31.379  1.00 14.99           C  
ATOM    261  C   ILE A 336      36.695  55.027  31.966  1.00 11.80           C  
ATOM    262  O   ILE A 336      36.610  55.815  32.907  1.00 12.20           O  
ATOM    263  CB  ILE A 336      34.503  55.471  30.797  1.00 15.26           C  
ATOM    264  CG1 ILE A 336      33.250  54.827  30.175  1.00 14.11           C  
ATOM    265  CG2 ILE A 336      35.251  56.312  29.762  1.00 13.09           C  
ATOM    266  CD1 ILE A 336      33.536  53.764  29.130  1.00 12.36           C  
ATOM    267  N   PHE A 337      37.858  54.695  31.411  1.00 12.24           N  
ATOM    268  CA  PHE A 337      39.117  55.245  31.915  1.00 12.77           C  
ATOM    269  C   PHE A 337      39.887  56.073  30.896  1.00 11.75           C  
ATOM    270  O   PHE A 337      39.801  55.832  29.689  1.00 11.63           O  
ATOM    271  CB  PHE A 337      40.036  54.120  32.408  1.00  9.54           C  
ATOM    272  CG  PHE A 337      39.397  53.212  33.413  1.00 13.93           C  
ATOM    273  CD1 PHE A 337      38.422  52.298  33.026  1.00 14.14           C  
ATOM    274  CD2 PHE A 337      39.761  53.279  34.757  1.00 16.95           C  
ATOM    275  CE1 PHE A 337      37.811  51.465  33.963  1.00 14.24           C  
ATOM    276  CE2 PHE A 337      39.159  52.453  35.699  1.00 14.83           C  
ATOM    277  CZ  PHE A 337      38.180  51.544  35.300  1.00 16.41           C  
ATOM    278  N   ILE A 338      40.637  57.051  31.399  1.00  8.82           N  
ATOM    279  CA  ILE A 338      41.461  57.885  30.544  1.00 12.07           C  
ATOM    280  C   ILE A 338      42.756  57.108  30.310  1.00 12.41           C  
ATOM    281  O   ILE A 338      43.428  56.705  31.259  1.00 14.05           O  
ATOM    282  CB  ILE A 338      41.788  59.227  31.208  1.00 13.80           C  
ATOM    283  CG1 ILE A 338      40.499  60.040  31.390  1.00 16.31           C  
ATOM    284  CG2 ILE A 338      42.811  59.982  30.356  1.00 13.32           C  
ATOM    285  CD1 ILE A 338      40.707  61.452  31.927  1.00 13.29           C  
ATOM    286  N   SER A 339      43.098  56.885  29.049  1.00  9.36           N  
ATOM    287  CA  SER A 339      44.297  56.135  28.727  1.00 10.88           C  
ATOM    288  C   SER A 339      45.401  57.022  28.200  1.00 13.10           C  
ATOM    289  O   SER A 339      46.554  56.597  28.104  1.00 14.09           O  
ATOM    290  CB  SER A 339      43.986  55.085  27.664  1.00 13.04           C  
ATOM    291  OG  SER A 339      43.514  55.706  26.481  1.00 12.83           O  
ATOM    292  N   PHE A 340      45.049  58.254  27.860  1.00 12.55           N  
ATOM    293  CA  PHE A 340      46.020  59.170  27.275  1.00 11.75           C  
ATOM    294  C   PHE A 340      45.534  60.613  27.340  1.00  8.95           C  
ATOM    295  O   PHE A 340      44.357  60.895  27.120  1.00  9.69           O  
ATOM    296  CB  PHE A 340      46.253  58.734  25.811  1.00 13.24           C  
ATOM    297  CG  PHE A 340      47.120  59.665  25.001  1.00 10.45           C  
ATOM    298  CD1 PHE A 340      46.596  60.838  24.456  1.00 12.05           C  
ATOM    299  CD2 PHE A 340      48.442  59.324  24.717  1.00 14.86           C  
ATOM    300  CE1 PHE A 340      47.377  61.655  23.642  1.00 11.97           C  
ATOM    301  CE2 PHE A 340      49.238  60.140  23.899  1.00 14.05           C  
ATOM    302  CZ  PHE A 340      48.701  61.304  23.361  1.00 10.29           C  
ATOM    303  N   ILE A 341      46.450  61.518  27.661  1.00  8.14           N  
ATOM    304  CA  ILE A 341      46.120  62.930  27.712  1.00  9.23           C  
ATOM    305  C   ILE A 341      47.000  63.606  26.669  1.00  8.59           C  
ATOM    306  O   ILE A 341      48.223  63.500  26.703  1.00 10.00           O  
ATOM    307  CB  ILE A 341      46.378  63.527  29.109  1.00  8.49           C  
ATOM    308  CG1 ILE A 341      45.722  62.634  30.177  1.00 12.43           C  
ATOM    309  CG2 ILE A 341      45.917  64.989  29.142  1.00 11.02           C  
ATOM    310  CD1 ILE A 341      44.646  63.284  31.039  1.00 14.65           C  
ATOM    311  N   LEU A 342      46.361  64.279  25.721  1.00 10.31           N  
ATOM    312  CA  LEU A 342      47.065  64.950  24.641  1.00  8.74           C  
ATOM    313  C   LEU A 342      47.755  66.223  25.099  1.00 10.56           C  
ATOM    314  O   LEU A 342      47.147  67.070  25.747  1.00 11.56           O  
ATOM    315  CB  LEU A 342      46.079  65.278  23.521  1.00 10.69           C  
ATOM    316  CG  LEU A 342      46.607  66.136  22.376  1.00 15.55           C  
ATOM    317  CD1 LEU A 342      47.560  65.304  21.517  1.00 15.24           C  
ATOM    318  CD2 LEU A 342      45.444  66.647  21.553  1.00 13.96           C  
ATOM    319  N   ALA A 343      49.030  66.357  24.754  1.00 13.86           N  
ATOM    320  CA  ALA A 343      49.792  67.547  25.118  1.00 15.26           C  
ATOM    321  C   ALA A 343      49.189  68.779  24.447  1.00 15.26           C  
ATOM    322  O   ALA A 343      49.004  68.806  23.226  1.00 14.40           O  
ATOM    323  CB  ALA A 343      51.248  67.386  24.690  1.00 14.86           C  
ATOM    324  N   GLY A 344      48.875  69.790  25.249  1.00 13.89           N  
ATOM    325  CA  GLY A 344      48.321  71.013  24.702  1.00 12.93           C  
ATOM    326  C   GLY A 344      46.813  71.047  24.604  1.00 14.71           C  
ATOM    327  O   GLY A 344      46.239  72.102  24.342  1.00 14.71           O  
ATOM    328  N   GLY A 345      46.164  69.907  24.807  1.00 12.42           N  
ATOM    329  CA  GLY A 345      44.717  69.869  24.729  1.00 14.06           C  
ATOM    330  C   GLY A 345      44.034  70.461  25.956  1.00 13.40           C  
ATOM    331  O   GLY A 345      44.691  70.726  26.960  1.00 12.78           O  
ATOM    332  N   PRO A 346      42.716  70.716  25.888  1.00 13.39           N  
ATOM    333  CA  PRO A 346      41.964  71.279  27.015  1.00 13.69           C  
ATOM    334  C   PRO A 346      42.119  70.466  28.299  1.00 13.67           C  
ATOM    335  O   PRO A 346      42.243  71.033  29.381  1.00 16.01           O  
ATOM    336  CB  PRO A 346      40.517  71.286  26.519  1.00 15.27           C  
ATOM    337  CG  PRO A 346      40.633  71.318  25.033  1.00 16.21           C  
ATOM    338  CD  PRO A 346      41.863  70.527  24.700  1.00 14.40           C  
ATOM    339  N   ALA A 347      42.106  69.142  28.186  1.00 13.11           N  
ATOM    340  CA  ALA A 347      42.251  68.286  29.368  1.00 15.75           C  
ATOM    341  C   ALA A 347      43.632  68.467  30.011  1.00 15.54           C  
ATOM    342  O   ALA A 347      43.767  68.472  31.233  1.00 17.98           O  
ATOM    343  CB  ALA A 347      42.028  66.815  28.992  1.00 13.50           C  
ATOM    344  N   ASP A 348      44.657  68.604  29.179  1.00 16.82           N  
ATOM    345  CA  ASP A 348      46.016  68.817  29.667  1.00 17.75           C  
ATOM    346  C   ASP A 348      46.096  70.184  30.375  1.00 19.21           C  
ATOM    347  O   ASP A 348      46.566  70.284  31.512  1.00 17.79           O  
ATOM    348  CB  ASP A 348      46.991  68.772  28.484  1.00 14.89           C  
ATOM    349  CG  ASP A 348      48.430  69.029  28.892  1.00 16.16           C  
ATOM    350  OD1 ASP A 348      48.811  68.732  30.045  1.00 14.85           O  
ATOM    351  OD2 ASP A 348      49.188  69.530  28.046  1.00 17.67           O  
ATOM    352  N   LEU A 349      45.612  71.224  29.699  1.00 17.94           N  
ATOM    353  CA  LEU A 349      45.625  72.583  30.232  1.00 21.74           C  
ATOM    354  C   LEU A 349      44.802  72.742  31.514  1.00 23.67           C  
ATOM    355  O   LEU A 349      44.913  73.749  32.210  1.00 26.00           O  
ATOM    356  CB  LEU A 349      45.129  73.566  29.164  1.00 23.96           C  
ATOM    357  CG  LEU A 349      45.874  73.570  27.821  1.00 27.19           C  
ATOM    358  CD1 LEU A 349      45.481  74.803  27.029  1.00 30.00           C  
ATOM    359  CD2 LEU A 349      47.374  73.548  28.042  1.00 26.65           C  
ATOM    360  N   SER A 350      43.966  71.756  31.819  1.00 25.14           N  
ATOM    361  CA  SER A 350      43.166  71.787  33.038  1.00 25.11           C  
ATOM    362  C   SER A 350      44.067  71.324  34.183  1.00 25.71           C  
ATOM    363  O   SER A 350      43.875  71.704  35.345  1.00 25.29           O  
ATOM    364  CB  SER A 350      41.966  70.843  32.916  1.00 24.46           C  
ATOM    365  OG  SER A 350      42.257  69.562  33.461  1.00 24.35           O  
ATOM    366  N   GLY A 351      45.055  70.501  33.830  1.00 24.86           N  
ATOM    367  CA  GLY A 351      45.997  69.965  34.795  1.00 19.53           C  
ATOM    368  C   GLY A 351      45.334  69.177  35.905  1.00 18.94           C  
ATOM    369  O   GLY A 351      45.957  68.915  36.930  1.00 19.72           O  
ATOM    370  N   GLU A 352      44.079  68.783  35.708  1.00 17.06           N  
ATOM    371  CA  GLU A 352      43.350  68.045  36.734  1.00 17.95           C  
ATOM    372  C   GLU A 352      42.970  66.612  36.379  1.00 18.97           C  
ATOM    373  O   GLU A 352      42.312  65.932  37.166  1.00 17.08           O  
ATOM    374  CB  GLU A 352      42.074  68.788  37.110  1.00 19.10           C  
ATOM    375  CG  GLU A 352      42.292  70.131  37.747  1.00 25.17           C  
ATOM    376  CD  GLU A 352      41.013  70.939  37.793  1.00 31.33           C  
ATOM    377  OE1 GLU A 352      40.708  71.627  36.797  1.00 33.99           O  
ATOM    378  OE2 GLU A 352      40.307  70.885  38.822  1.00 37.15           O  
ATOM    379  N   LEU A 353      43.363  66.160  35.195  1.00 19.39           N  
ATOM    380  CA  LEU A 353      43.054  64.801  34.760  1.00 17.30           C  
ATOM    381  C   LEU A 353      44.342  64.072  34.430  1.00 16.86           C  
ATOM    382  O   LEU A 353      45.352  64.699  34.118  1.00 18.17           O  
ATOM    383  CB  LEU A 353      42.167  64.823  33.516  1.00 18.00           C  
ATOM    384  CG  LEU A 353      40.744  65.370  33.647  1.00 15.10           C  
ATOM    385  CD1 LEU A 353      40.182  65.636  32.254  1.00 17.34           C  
ATOM    386  CD2 LEU A 353      39.867  64.371  34.388  1.00 16.66           C  
ATOM    387  N   ARG A 354      44.304  62.747  34.492  1.00 15.49           N  
ATOM    388  CA  ARG A 354      45.478  61.945  34.183  1.00 15.04           C  
ATOM    389  C   ARG A 354      45.100  60.528  33.771  1.00 15.46           C  
ATOM    390  O   ARG A 354      43.981  60.063  34.012  1.00 12.34           O  
ATOM    391  CB  ARG A 354      46.413  61.890  35.389  1.00 16.16           C  
ATOM    392  CG  ARG A 354      46.006  60.876  36.439  1.00 17.70           C  
ATOM    393  CD  ARG A 354      47.168  60.533  37.351  1.00 27.69           C  
ATOM    394  NE  ARG A 354      47.596  61.668  38.166  1.00 31.67           N  
ATOM    395  CZ  ARG A 354      48.864  62.048  38.309  1.00 37.68           C  
ATOM    396  NH1 ARG A 354      49.837  61.385  37.686  1.00 36.80           N  
ATOM    397  NH2 ARG A 354      49.164  63.092  39.074  1.00 35.54           N  
ATOM    398  N   LYS A 355      46.045  59.849  33.135  1.00 15.40           N  
ATOM    399  CA  LYS A 355      45.839  58.476  32.712  1.00 15.69           C  
ATOM    400  C   LYS A 355      45.558  57.666  33.978  1.00 14.46           C  
ATOM    401  O   LYS A 355      46.214  57.869  35.004  1.00 13.40           O  
ATOM    402  CB  LYS A 355      47.098  57.960  32.019  1.00 14.55           C  
ATOM    403  CG  LYS A 355      47.059  56.491  31.690  1.00 17.13           C  
ATOM    404  CD  LYS A 355      48.244  56.106  30.831  1.00 17.26           C  
ATOM    405  CE  LYS A 355      49.376  55.559  31.683  1.00 21.10           C  
ATOM    406  NZ  LYS A 355      50.278  54.668  30.889  1.00 26.31           N  
ATOM    407  N   GLY A 356      44.585  56.761  33.910  1.00 12.02           N  
ATOM    408  CA  GLY A 356      44.248  55.956  35.077  1.00 13.41           C  
ATOM    409  C   GLY A 356      42.997  56.463  35.775  1.00 11.90           C  
ATOM    410  O   GLY A 356      42.415  55.771  36.611  1.00 10.50           O  
ATOM    411  N   ASP A 357      42.590  57.683  35.427  1.00 11.22           N  
ATOM    412  CA  ASP A 357      41.395  58.307  35.979  1.00  8.99           C  
ATOM    413  C   ASP A 357      40.169  57.661  35.349  1.00 12.51           C  
ATOM    414  O   ASP A 357      40.137  57.426  34.138  1.00 11.87           O  
ATOM    415  CB  ASP A 357      41.355  59.794  35.628  1.00 10.59           C  
ATOM    416  CG  ASP A 357      41.975  60.675  36.686  1.00  9.14           C  
ATOM    417  OD1 ASP A 357      42.145  60.229  37.837  1.00  8.93           O  
ATOM    418  OD2 ASP A 357      42.293  61.836  36.356  1.00 14.55           O  
ATOM    419  N   GLN A 358      39.164  57.367  36.163  1.00 14.16           N  
ATOM    420  CA  GLN A 358      37.932  56.804  35.639  1.00 13.07           C  
ATOM    421  C   GLN A 358      36.962  57.970  35.551  1.00 12.07           C  
ATOM    422  O   GLN A 358      36.907  58.801  36.459  1.00 10.43           O  
ATOM    423  CB  GLN A 358      37.350  55.736  36.567  1.00 14.39           C  
ATOM    424  CG  GLN A 358      36.089  55.091  35.978  1.00 19.65           C  
ATOM    425  CD  GLN A 358      35.327  54.210  36.961  1.00 19.32           C  
ATOM    426  OE1 GLN A 358      35.750  54.001  38.099  1.00 13.89           O  
ATOM    427  NE2 GLN A 358      34.191  53.689  36.514  1.00 16.98           N  
ATOM    428  N   ILE A 359      36.216  58.050  34.453  1.00 12.70           N  
ATOM    429  CA  ILE A 359      35.240  59.123  34.296  1.00 13.71           C  
ATOM    430  C   ILE A 359      33.939  58.617  34.895  1.00 11.02           C  
ATOM    431  O   ILE A 359      33.262  57.781  34.297  1.00 13.53           O  
ATOM    432  CB  ILE A 359      34.968  59.473  32.815  1.00 17.06           C  
ATOM    433  CG1 ILE A 359      36.286  59.629  32.034  1.00 15.88           C  
ATOM    434  CG2 ILE A 359      34.107  60.734  32.750  1.00 15.26           C  
ATOM    435  CD1 ILE A 359      37.108  60.844  32.415  1.00 19.25           C  
ATOM    436  N   LEU A 360      33.597  59.116  36.077  1.00 12.57           N  
ATOM    437  CA  LEU A 360      32.382  58.689  36.753  1.00 13.57           C  
ATOM    438  C   LEU A 360      31.139  59.288  36.108  1.00 14.87           C  
ATOM    439  O   LEU A 360      30.075  58.664  36.077  1.00 15.90           O  
ATOM    440  CB  LEU A 360      32.452  59.069  38.230  1.00 14.94           C  
ATOM    441  CG  LEU A 360      33.629  58.457  39.001  1.00 12.51           C  
ATOM    442  CD1 LEU A 360      33.340  58.524  40.491  1.00 14.64           C  
ATOM    443  CD2 LEU A 360      33.856  57.015  38.564  1.00 14.94           C  
ATOM    444  N   SER A 361      31.280  60.496  35.577  1.00 16.97           N  
ATOM    445  CA  SER A 361      30.157  61.152  34.922  1.00 16.86           C  
ATOM    446  C   SER A 361      30.601  62.371  34.126  1.00 16.92           C  
ATOM    447  O   SER A 361      31.684  62.915  34.343  1.00 14.15           O  
ATOM    448  CB  SER A 361      29.114  61.576  35.958  1.00 14.21           C  
ATOM    449  OG  SER A 361      29.564  62.699  36.691  1.00 19.61           O  
ATOM    450  N   VAL A 362      29.751  62.773  33.190  1.00 15.74           N  
ATOM    451  CA  VAL A 362      29.993  63.942  32.365  1.00 18.66           C  
ATOM    452  C   VAL A 362      28.711  64.774  32.415  1.00 18.84           C  
ATOM    453  O   VAL A 362      27.640  64.315  32.015  1.00 18.08           O  
ATOM    454  CB  VAL A 362      30.329  63.557  30.889  1.00 19.71           C  
ATOM    455  CG1 VAL A 362      29.174  62.815  30.245  1.00 24.01           C  
ATOM    456  CG2 VAL A 362      30.651  64.808  30.095  1.00 22.47           C  
ATOM    457  N   ASN A 363      28.817  65.988  32.942  1.00 18.33           N  
ATOM    458  CA  ASN A 363      27.661  66.867  33.045  1.00 19.63           C  
ATOM    459  C   ASN A 363      26.484  66.159  33.721  1.00 21.40           C  
ATOM    460  O   ASN A 363      25.359  66.179  33.218  1.00 21.79           O  
ATOM    461  CB  ASN A 363      27.246  67.352  31.651  1.00 20.86           C  
ATOM    462  CG  ASN A 363      28.251  68.313  31.042  1.00 21.20           C  
ATOM    463  OD1 ASN A 363      29.212  68.716  31.693  1.00 22.32           O  
ATOM    464  ND2 ASN A 363      28.032  68.683  29.785  1.00 20.10           N  
ATOM    465  N   GLY A 364      26.749  65.523  34.859  1.00 21.91           N  
ATOM    466  CA  GLY A 364      25.691  64.840  35.583  1.00 20.55           C  
ATOM    467  C   GLY A 364      25.321  63.459  35.074  1.00 21.12           C  
ATOM    468  O   GLY A 364      24.694  62.684  35.797  1.00 21.54           O  
ATOM    469  N   VAL A 365      25.695  63.136  33.840  1.00 19.93           N  
ATOM    470  CA  VAL A 365      25.379  61.823  33.293  1.00 19.08           C  
ATOM    471  C   VAL A 365      26.346  60.751  33.801  1.00 20.44           C  
ATOM    472  O   VAL A 365      27.547  60.783  33.522  1.00 18.40           O  
ATOM    473  CB  VAL A 365      25.408  61.837  31.758  1.00 17.84           C  
ATOM    474  CG1 VAL A 365      24.892  60.511  31.217  1.00 15.43           C  
ATOM    475  CG2 VAL A 365      24.560  62.983  31.248  1.00 21.64           C  
ATOM    476  N   ASP A 366      25.800  59.807  34.556  1.00 18.04           N  
ATOM    477  CA  ASP A 366      26.561  58.703  35.128  1.00 19.44           C  
ATOM    478  C   ASP A 366      27.154  57.841  34.015  1.00 20.23           C  
ATOM    479  O   ASP A 366      26.429  57.317  33.166  1.00 20.94           O  
ATOM    480  CB  ASP A 366      25.632  57.864  36.010  1.00 20.05           C  
ATOM    481  CG  ASP A 366      26.366  56.808  36.809  1.00 20.79           C  
ATOM    482  OD1 ASP A 366      27.610  56.745  36.731  1.00 16.73           O  
ATOM    483  OD2 ASP A 366      25.684  56.037  37.521  1.00 25.68           O  
ATOM    484  N   LEU A 367      28.475  57.697  34.015  1.00 18.10           N  
ATOM    485  CA  LEU A 367      29.138  56.895  32.996  1.00 15.06           C  
ATOM    486  C   LEU A 367      29.786  55.646  33.579  1.00 15.66           C  
ATOM    487  O   LEU A 367      30.475  54.917  32.873  1.00 16.78           O  
ATOM    488  CB  LEU A 367      30.209  57.727  32.293  1.00 17.69           C  
ATOM    489  CG  LEU A 367      29.740  58.906  31.440  1.00 18.58           C  
ATOM    490  CD1 LEU A 367      30.935  59.515  30.724  1.00 17.30           C  
ATOM    491  CD2 LEU A 367      28.692  58.434  30.443  1.00 16.88           C  
ATOM    492  N   ARG A 368      29.568  55.391  34.864  1.00 18.04           N  
ATOM    493  CA  ARG A 368      30.177  54.231  35.509  1.00 19.28           C  
ATOM    494  C   ARG A 368      29.911  52.921  34.788  1.00 19.39           C  
ATOM    495  O   ARG A 368      30.795  52.068  34.686  1.00 20.04           O  
ATOM    496  CB  ARG A 368      29.716  54.139  36.959  1.00 17.34           C  
ATOM    497  CG  ARG A 368      30.452  55.110  37.862  1.00 16.27           C  
ATOM    498  CD  ARG A 368      29.880  55.110  39.266  1.00 20.42           C  
ATOM    499  NE  ARG A 368      28.437  55.319  39.261  1.00 18.88           N  
ATOM    500  CZ  ARG A 368      27.592  54.698  40.074  1.00 16.32           C  
ATOM    501  NH1 ARG A 368      28.049  53.826  40.962  1.00 18.04           N  
ATOM    502  NH2 ARG A 368      26.294  54.948  39.996  1.00 15.98           N  
ATOM    503  N   ASN A 369      28.701  52.768  34.267  1.00 20.09           N  
ATOM    504  CA  ASN A 369      28.342  51.546  33.558  1.00 21.99           C  
ATOM    505  C   ASN A 369      27.994  51.792  32.095  1.00 21.05           C  
ATOM    506  O   ASN A 369      27.173  51.090  31.510  1.00 23.68           O  
ATOM    507  CB  ASN A 369      27.178  50.870  34.276  1.00 24.40           C  
ATOM    508  CG  ASN A 369      27.498  50.581  35.726  1.00 26.56           C  
ATOM    509  OD1 ASN A 369      27.953  49.485  36.065  1.00 31.85           O  
ATOM    510  ND2 ASN A 369      27.277  51.568  36.592  1.00 23.39           N  
ATOM    511  N   ALA A 370      28.633  52.794  31.507  1.00 20.28           N  
ATOM    512  CA  ALA A 370      28.394  53.135  30.113  1.00 18.65           C  
ATOM    513  C   ALA A 370      29.131  52.171  29.190  1.00 17.03           C  
ATOM    514  O   ALA A 370      30.094  51.534  29.598  1.00 16.36           O  
ATOM    515  CB  ALA A 370      28.864  54.553  29.852  1.00 14.10           C  
ATOM    516  N   SER A 371      28.663  52.050  27.951  1.00 16.37           N  
ATOM    517  CA  SER A 371      29.336  51.204  26.977  1.00 15.12           C  
ATOM    518  C   SER A 371      30.365  52.139  26.347  1.00 15.55           C  
ATOM    519  O   SER A 371      30.282  53.357  26.512  1.00 16.15           O  
ATOM    520  CB  SER A 371      28.359  50.703  25.917  1.00 16.99           C  
ATOM    521  OG  SER A 371      27.573  51.767  25.420  1.00 22.49           O  
ATOM    522  N   HIS A 372      31.331  51.587  25.628  1.00 16.60           N  
ATOM    523  CA  HIS A 372      32.359  52.420  25.025  1.00 16.83           C  
ATOM    524  C   HIS A 372      31.848  53.546  24.135  1.00 19.05           C  
ATOM    525  O   HIS A 372      32.117  54.723  24.401  1.00 17.13           O  
ATOM    526  CB  HIS A 372      33.343  51.570  24.220  1.00 18.31           C  
ATOM    527  CG  HIS A 372      34.565  52.327  23.804  1.00 16.27           C  
ATOM    528  ND1 HIS A 372      35.725  52.347  24.552  1.00 15.35           N  
ATOM    529  CD2 HIS A 372      34.806  53.116  22.725  1.00 16.64           C  
ATOM    530  CE1 HIS A 372      36.615  53.116  23.962  1.00 17.77           C  
ATOM    531  NE2 HIS A 372      36.086  53.596  22.849  1.00 16.13           N  
ATOM    532  N   GLU A 373      31.117  53.198  23.079  1.00 17.98           N  
ATOM    533  CA  GLU A 373      30.622  54.215  22.159  1.00 21.43           C  
ATOM    534  C   GLU A 373      29.713  55.247  22.798  1.00 18.53           C  
ATOM    535  O   GLU A 373      29.877  56.441  22.547  1.00 22.40           O  
ATOM    536  CB  GLU A 373      29.912  53.581  20.957  1.00 24.74           C  
ATOM    537  CG  GLU A 373      30.035  54.421  19.682  1.00 31.92           C  
ATOM    538  CD  GLU A 373      28.982  54.095  18.626  1.00 37.31           C  
ATOM    539  OE1 GLU A 373      28.454  52.959  18.638  1.00 43.29           O  
ATOM    540  OE2 GLU A 373      28.684  54.976  17.780  1.00 34.25           O  
ATOM    541  N   GLN A 374      28.760  54.806  23.618  1.00 16.93           N  
ATOM    542  CA  GLN A 374      27.838  55.741  24.278  1.00 16.67           C  
ATOM    543  C   GLN A 374      28.632  56.732  25.145  1.00 14.57           C  
ATOM    544  O   GLN A 374      28.309  57.915  25.189  1.00 15.06           O  
ATOM    545  CB  GLN A 374      26.815  54.991  25.154  1.00 18.40           C  
ATOM    546  CG  GLN A 374      25.390  54.787  24.596  1.00 15.08           C  
ATOM    547  CD  GLN A 374      25.045  55.619  23.368  1.00 19.83           C  
ATOM    548  OE1 GLN A 374      24.640  56.781  23.478  1.00 19.49           O  
ATOM    549  NE2 GLN A 374      25.180  55.017  22.193  1.00 19.93           N  
ATOM    550  N   ALA A 375      29.660  56.244  25.839  1.00 14.19           N  
ATOM    551  CA  ALA A 375      30.503  57.106  26.674  1.00 14.92           C  
ATOM    552  C   ALA A 375      31.199  58.139  25.794  1.00 12.85           C  
ATOM    553  O   ALA A 375      31.282  59.318  26.142  1.00 14.07           O  
ATOM    554  CB  ALA A 375      31.550  56.277  27.413  1.00 13.41           C  
ATOM    555  N   ALA A 376      31.710  57.678  24.654  1.00 17.76           N  
ATOM    556  CA  ALA A 376      32.385  58.557  23.710  1.00 16.53           C  
ATOM    557  C   ALA A 376      31.382  59.601  23.228  1.00 18.32           C  
ATOM    558  O   ALA A 376      31.664  60.802  23.236  1.00 17.47           O  
ATOM    559  CB  ALA A 376      32.918  57.749  22.535  1.00 15.46           C  
ATOM    560  N   ILE A 377      30.205  59.135  22.819  1.00 17.97           N  
ATOM    561  CA  ILE A 377      29.158  60.025  22.344  1.00 17.69           C  
ATOM    562  C   ILE A 377      28.826  61.051  23.422  1.00 17.01           C  
ATOM    563  O   ILE A 377      28.673  62.234  23.130  1.00 17.92           O  
ATOM    564  CB  ILE A 377      27.870  59.234  21.965  1.00 20.00           C  
ATOM    565  CG1 ILE A 377      28.088  58.488  20.642  1.00 22.35           C  
ATOM    566  CG2 ILE A 377      26.679  60.186  21.827  1.00 18.02           C  
ATOM    567  CD1 ILE A 377      27.091  57.374  20.398  1.00 22.52           C  
ATOM    568  N   ALA A 378      28.724  60.601  24.669  1.00 14.50           N  
ATOM    569  CA  ALA A 378      28.404  61.503  25.769  1.00 13.34           C  
ATOM    570  C   ALA A 378      29.441  62.616  25.903  1.00 16.03           C  
ATOM    571  O   ALA A 378      29.091  63.783  26.063  1.00 16.68           O  
ATOM    572  CB  ALA A 378      28.299  60.722  27.082  1.00 12.33           C  
ATOM    573  N   LEU A 379      30.718  62.253  25.833  1.00 17.75           N  
ATOM    574  CA  LEU A 379      31.804  63.228  25.952  1.00 18.33           C  
ATOM    575  C   LEU A 379      31.880  64.184  24.764  1.00 16.28           C  
ATOM    576  O   LEU A 379      31.990  65.396  24.933  1.00 14.91           O  
ATOM    577  CB  LEU A 379      33.145  62.501  26.101  1.00 16.79           C  
ATOM    578  CG  LEU A 379      33.335  61.774  27.436  1.00 17.42           C  
ATOM    579  CD1 LEU A 379      34.425  60.716  27.290  1.00 19.45           C  
ATOM    580  CD2 LEU A 379      33.691  62.774  28.529  1.00 14.08           C  
ATOM    581  N   LYS A 380      31.829  63.626  23.563  1.00 17.24           N  
ATOM    582  CA  LYS A 380      31.907  64.421  22.343  1.00 19.43           C  
ATOM    583  C   LYS A 380      30.741  65.401  22.221  1.00 21.25           C  
ATOM    584  O   LYS A 380      30.887  66.505  21.689  1.00 19.79           O  
ATOM    585  CB  LYS A 380      31.917  63.496  21.121  1.00 18.95           C  
ATOM    586  CG  LYS A 380      33.221  62.751  20.907  1.00 17.09           C  
ATOM    587  CD  LYS A 380      33.174  61.897  19.652  1.00 17.79           C  
ATOM    588  CE  LYS A 380      34.537  61.302  19.345  1.00 21.67           C  
ATOM    589  NZ  LYS A 380      34.492  60.372  18.187  1.00 23.84           N  
ATOM    590  N   ASN A 381      29.581  64.994  22.720  1.00 20.25           N  
ATOM    591  CA  ASN A 381      28.397  65.829  22.627  1.00 22.95           C  
ATOM    592  C   ASN A 381      28.077  66.483  23.960  1.00 22.49           C  
ATOM    593  O   ASN A 381      26.969  66.967  24.173  1.00 24.63           O  
ATOM    594  CB  ASN A 381      27.207  64.981  22.155  1.00 28.19           C  
ATOM    595  CG  ASN A 381      27.466  64.285  20.814  1.00 33.23           C  
ATOM    596  OD1 ASN A 381      27.329  64.891  19.753  1.00 40.51           O  
ATOM    597  ND2 ASN A 381      27.834  63.010  20.864  1.00 33.48           N  
ATOM    598  N   ALA A 382      29.059  66.513  24.850  1.00 19.98           N  
ATOM    599  CA  ALA A 382      28.873  67.083  26.176  1.00 21.10           C  
ATOM    600  C   ALA A 382      28.582  68.583  26.192  1.00 22.39           C  
ATOM    601  O   ALA A 382      27.982  69.088  27.142  1.00 25.99           O  
ATOM    602  CB  ALA A 382      30.097  66.781  27.042  1.00 22.90           C  
ATOM    603  N   GLY A 383      29.000  69.296  25.153  1.00 19.21           N  
ATOM    604  CA  GLY A 383      28.766  70.727  25.121  1.00 19.10           C  
ATOM    605  C   GLY A 383      30.082  71.455  25.295  1.00 21.97           C  
ATOM    606  O   GLY A 383      31.118  70.812  25.463  1.00 21.85           O  
ATOM    607  N   GLN A 384      30.049  72.786  25.278  1.00 21.68           N  
ATOM    608  CA  GLN A 384      31.270  73.584  25.403  1.00 21.58           C  
ATOM    609  C   GLN A 384      31.916  73.513  26.777  1.00 20.60           C  
ATOM    610  O   GLN A 384      33.140  73.472  26.887  1.00 21.19           O  
ATOM    611  CB  GLN A 384      30.989  75.039  25.029  1.00 21.93           C  
ATOM    612  CG  GLN A 384      30.412  75.190  23.628  1.00 25.25           C  
ATOM    613  CD  GLN A 384      29.853  76.575  23.368  1.00 26.41           C  
ATOM    614  OE1 GLN A 384      28.768  76.923  23.836  1.00 26.02           O  
ATOM    615  NE2 GLN A 384      30.593  77.373  22.615  1.00 27.20           N  
ATOM    616  N   THR A 385      31.101  73.514  27.824  1.00 22.30           N  
ATOM    617  CA  THR A 385      31.628  73.418  29.181  1.00 22.46           C  
ATOM    618  C   THR A 385      31.336  72.005  29.659  1.00 20.94           C  
ATOM    619  O   THR A 385      30.177  71.616  29.807  1.00 21.29           O  
ATOM    620  CB  THR A 385      30.959  74.429  30.135  1.00 24.76           C  
ATOM    621  OG1 THR A 385      31.321  75.763  29.751  1.00 27.18           O  
ATOM    622  CG2 THR A 385      31.424  74.186  31.568  1.00 26.88           C  
ATOM    623  N   VAL A 386      32.392  71.237  29.889  1.00 18.51           N  
ATOM    624  CA  VAL A 386      32.252  69.855  30.316  1.00 18.08           C  
ATOM    625  C   VAL A 386      32.640  69.682  31.774  1.00 16.81           C  
ATOM    626  O   VAL A 386      33.759  69.996  32.170  1.00 16.97           O  
ATOM    627  CB  VAL A 386      33.125  68.941  29.439  1.00 19.40           C  
ATOM    628  CG1 VAL A 386      32.750  67.473  29.652  1.00 17.33           C  
ATOM    629  CG2 VAL A 386      32.957  69.339  27.976  1.00 15.70           C  
ATOM    630  N   THR A 387      31.701  69.192  32.573  1.00 18.64           N  
ATOM    631  CA  THR A 387      31.946  68.973  33.990  1.00 17.76           C  
ATOM    632  C   THR A 387      32.086  67.487  34.208  1.00 15.44           C  
ATOM    633  O   THR A 387      31.113  66.738  34.118  1.00 16.90           O  
ATOM    634  CB  THR A 387      30.794  69.483  34.854  1.00 20.50           C  
ATOM    635  OG1 THR A 387      30.735  70.910  34.765  1.00 21.95           O  
ATOM    636  CG2 THR A 387      31.014  69.087  36.309  1.00 20.44           C  
ATOM    637  N   ILE A 388      33.311  67.066  34.491  1.00 15.85           N  
ATOM    638  CA  ILE A 388      33.594  65.662  34.701  1.00 16.22           C  
ATOM    639  C   ILE A 388      33.855  65.364  36.172  1.00 14.15           C  
ATOM    640  O   ILE A 388      34.473  66.163  36.878  1.00 13.01           O  
ATOM    641  CB  ILE A 388      34.847  65.231  33.889  1.00 16.29           C  
ATOM    642  CG1 ILE A 388      34.550  65.288  32.385  1.00 16.12           C  
ATOM    643  CG2 ILE A 388      35.281  63.824  34.295  1.00 17.93           C  
ATOM    644  CD1 ILE A 388      35.784  65.341  31.510  1.00 18.45           C  
ATOM    645  N   ILE A 389      33.344  64.230  36.637  1.00 15.09           N  
ATOM    646  CA  ILE A 389      33.616  63.785  37.996  1.00 13.34           C  
ATOM    647  C   ILE A 389      34.522  62.613  37.686  1.00 13.24           C  
ATOM    648  O   ILE A 389      34.099  61.648  37.045  1.00 12.58           O  
ATOM    649  CB  ILE A 389      32.389  63.243  38.729  1.00 14.96           C  
ATOM    650  CG1 ILE A 389      31.347  64.349  38.933  1.00 18.00           C  
ATOM    651  CG2 ILE A 389      32.834  62.666  40.072  1.00 13.70           C  
ATOM    652  CD1 ILE A 389      31.915  65.692  39.354  1.00 17.52           C  
ATOM    653  N   ALA A 390      35.775  62.714  38.112  1.00 14.18           N  
ATOM    654  CA  ALA A 390      36.755  61.676  37.842  1.00 12.59           C  
ATOM    655  C   ALA A 390      37.304  61.079  39.129  1.00 12.43           C  
ATOM    656  O   ALA A 390      37.283  61.715  40.189  1.00 11.61           O  
ATOM    657  CB  ALA A 390      37.893  62.259  36.999  1.00 11.49           C  
ATOM    658  N   GLN A 391      37.786  59.847  39.030  1.00  9.27           N  
ATOM    659  CA  GLN A 391      38.361  59.164  40.178  1.00 11.96           C  
ATOM    660  C   GLN A 391      39.505  58.260  39.748  1.00  9.52           C  
ATOM    661  O   GLN A 391      39.338  57.383  38.903  1.00 10.34           O  
ATOM    662  CB  GLN A 391      37.303  58.341  40.911  1.00 12.97           C  
ATOM    663  CG  GLN A 391      37.816  57.745  42.210  1.00 13.55           C  
ATOM    664  CD  GLN A 391      36.707  57.194  43.062  1.00 16.50           C  
ATOM    665  OE1 GLN A 391      35.661  56.800  42.552  1.00 17.42           O  
ATOM    666  NE2 GLN A 391      36.925  57.163  44.368  1.00 12.40           N  
ATOM    667  N   TYR A 392      40.668  58.489  40.345  1.00 12.70           N  
ATOM    668  CA  TYR A 392      41.872  57.723  40.049  1.00 12.30           C  
ATOM    669  C   TYR A 392      41.745  56.255  40.482  1.00 13.62           C  
ATOM    670  O   TYR A 392      41.582  55.962  41.666  1.00 13.47           O  
ATOM    671  CB  TYR A 392      43.064  58.387  40.752  1.00 11.65           C  
ATOM    672  CG  TYR A 392      44.427  57.917  40.292  1.00 11.87           C  
ATOM    673  CD1 TYR A 392      44.780  57.941  38.939  1.00  7.90           C  
ATOM    674  CD2 TYR A 392      45.367  57.450  41.212  1.00 10.28           C  
ATOM    675  CE1 TYR A 392      46.038  57.511  38.511  1.00  9.85           C  
ATOM    676  CE2 TYR A 392      46.628  57.017  40.797  1.00 15.33           C  
ATOM    677  CZ  TYR A 392      46.959  57.049  39.445  1.00 12.50           C  
ATOM    678  OH  TYR A 392      48.202  56.625  39.037  1.00  9.23           O  
ATOM    679  N   LYS A 393      41.817  55.345  39.509  1.00 15.18           N  
ATOM    680  CA  LYS A 393      41.723  53.896  39.750  1.00 15.95           C  
ATOM    681  C   LYS A 393      42.830  53.213  38.938  1.00 15.07           C  
ATOM    682  O   LYS A 393      42.564  52.501  37.964  1.00 12.39           O  
ATOM    683  CB  LYS A 393      40.357  53.379  39.299  1.00 18.44           C  
ATOM    684  CG  LYS A 393      39.186  54.074  39.970  1.00 20.96           C  
ATOM    685  CD  LYS A 393      38.581  53.209  41.055  1.00 28.78           C  
ATOM    686  CE  LYS A 393      38.109  54.048  42.226  1.00 34.26           C  
ATOM    687  NZ  LYS A 393      37.500  53.212  43.298  1.00 37.08           N  
ATOM    688  N   PRO A 394      44.092  53.400  39.362  1.00 14.37           N  
ATOM    689  CA  PRO A 394      45.264  52.832  38.686  1.00 13.05           C  
ATOM    690  C   PRO A 394      45.283  51.316  38.565  1.00 13.77           C  
ATOM    691  O   PRO A 394      45.724  50.777  37.546  1.00 13.41           O  
ATOM    692  CB  PRO A 394      46.445  53.364  39.495  1.00 12.39           C  
ATOM    693  CG  PRO A 394      45.873  53.682  40.839  1.00 11.98           C  
ATOM    694  CD  PRO A 394      44.464  54.137  40.581  1.00 13.50           C  
ATOM    695  N   GLU A 395      44.818  50.623  39.597  1.00 12.42           N  
ATOM    696  CA  GLU A 395      44.800  49.174  39.578  1.00 13.21           C  
ATOM    697  C   GLU A 395      43.873  48.709  38.491  1.00 12.93           C  
ATOM    698  O   GLU A 395      44.194  47.815  37.692  1.00 13.95           O  
ATOM    699  CB  GLU A 395      44.341  48.639  40.935  1.00 12.18           C  
ATOM    700  CG  GLU A 395      45.362  48.850  42.054  1.00 16.36           C  
ATOM    701  CD  GLU A 395      45.350  50.265  42.624  1.00 15.74           C  
ATOM    702  OE1 GLU A 395      44.290  50.930  42.577  1.00 16.33           O  
ATOM    703  OE2 GLU A 395      46.405  50.714  43.121  1.00 17.62           O  
ATOM    704  N   GLU A 396      42.695  49.315  38.443  1.00 13.51           N  
ATOM    705  CA  GLU A 396      41.717  48.951  37.425  1.00 16.35           C  
ATOM    706  C   GLU A 396      42.264  49.318  36.042  1.00 14.55           C  
ATOM    707  O   GLU A 396      42.176  48.537  35.110  1.00 13.58           O  
ATOM    708  CB  GLU A 396      40.396  49.676  37.681  1.00 20.90           C  
ATOM    709  CG  GLU A 396      39.407  48.889  38.552  1.00 30.27           C  
ATOM    710  CD  GLU A 396      39.554  49.243  40.007  1.00 33.53           C  
ATOM    711  OE1 GLU A 396      40.703  49.524  40.413  1.00 37.46           O  
ATOM    712  OE2 GLU A 396      38.538  49.251  40.748  1.00 39.13           O  
ATOM    713  N   TYR A 397      42.841  50.513  35.933  1.00 13.32           N  
ATOM    714  CA  TYR A 397      43.361  50.932  34.651  1.00 12.63           C  
ATOM    715  C   TYR A 397      44.507  50.044  34.138  1.00 14.22           C  
ATOM    716  O   TYR A 397      44.574  49.645  32.953  1.00 13.62           O  
ATOM    717  CB  TYR A 397      43.854  52.403  34.723  1.00 13.10           C  
ATOM    718  CG  TYR A 397      44.565  52.773  33.454  1.00 12.19           C  
ATOM    719  CD1 TYR A 397      43.839  53.191  32.354  1.00 11.51           C  
ATOM    720  CD2 TYR A 397      45.938  52.565  33.320  1.00 11.14           C  
ATOM    721  CE1 TYR A 397      44.444  53.385  31.133  1.00 10.42           C  
ATOM    722  CE2 TYR A 397      46.567  52.754  32.090  1.00  9.41           C  
ATOM    723  CZ  TYR A 397      45.808  53.159  30.991  1.00 11.58           C  
ATOM    724  OH  TYR A 397      46.400  53.247  29.744  1.00 10.45           O  
ATOM    725  N   SER A 398      45.423  49.715  35.036  1.00 15.84           N  
ATOM    726  CA  SER A 398      46.576  48.939  34.679  1.00 18.02           C  
ATOM    727  C   SER A 398      46.240  47.677  33.915  1.00 18.51           C  
ATOM    728  O   SER A 398      47.086  47.162  33.202  1.00 16.85           O  
ATOM    729  CB  SER A 398      47.380  48.607  35.924  1.00 19.34           C  
ATOM    730  OG  SER A 398      46.807  47.534  36.639  1.00 21.21           O  
ATOM    731  N   ARG A 399      45.003  47.201  34.049  1.00 18.46           N  
ATOM    732  CA  ARG A 399      44.558  45.976  33.373  1.00 18.28           C  
ATOM    733  C   ARG A 399      44.520  46.109  31.847  1.00 17.10           C  
ATOM    734  O   ARG A 399      44.643  45.126  31.119  1.00 15.58           O  
ATOM    735  CB  ARG A 399      43.172  45.596  33.911  1.00 24.35           C  
ATOM    736  CG  ARG A 399      42.457  44.460  33.181  1.00 39.21           C  
ATOM    737  CD  ARG A 399      41.042  44.257  33.744  1.00 44.65           C  
ATOM    738  NE  ARG A 399      40.935  44.645  35.154  1.00 49.22           N  
ATOM    739  CZ  ARG A 399      40.008  44.187  35.991  1.00 50.38           C  
ATOM    740  NH1 ARG A 399      39.099  43.318  35.566  1.00 51.81           N  
ATOM    741  NH2 ARG A 399      39.989  44.600  37.252  1.00 50.24           N  
ATOM    742  N   PHE A 400      44.358  47.342  31.377  1.00 16.09           N  
ATOM    743  CA  PHE A 400      44.266  47.640  29.947  1.00 15.06           C  
ATOM    744  C   PHE A 400      45.596  47.740  29.199  1.00 13.24           C  
ATOM    745  O   PHE A 400      45.744  47.221  28.096  1.00 12.67           O  
ATOM    746  CB  PHE A 400      43.527  48.963  29.751  1.00 13.28           C  
ATOM    747  CG  PHE A 400      42.110  48.949  30.233  1.00 17.73           C  
ATOM    748  CD1 PHE A 400      41.092  48.460  29.421  1.00 17.23           C  
ATOM    749  CD2 PHE A 400      41.781  49.488  31.473  1.00 16.45           C  
ATOM    750  CE1 PHE A 400      39.767  48.508  29.843  1.00 21.49           C  
ATOM    751  CE2 PHE A 400      40.466  49.539  31.898  1.00 18.77           C  
ATOM    752  CZ  PHE A 400      39.456  49.053  31.081  1.00 19.72           C  
ATOM    753  N   GLU A 401      46.549  48.440  29.797  1.00 11.24           N  
ATOM    754  CA  GLU A 401      47.847  48.649  29.176  1.00 13.81           C  
ATOM    755  C   GLU A 401      48.835  47.534  29.492  1.00 14.14           C  
ATOM    756  O   GLU A 401      49.021  47.140  30.646  1.00 13.96           O  
ATOM    757  CB  GLU A 401      48.411  50.007  29.612  1.00 11.46           C  
ATOM    758  CG  GLU A 401      49.391  50.622  28.636  1.00 10.71           C  
ATOM    759  CD  GLU A 401      49.806  52.035  29.011  1.00 11.25           C  
ATOM    760  OE1 GLU A 401      49.061  52.722  29.740  1.00 10.46           O  
ATOM    761  OE2 GLU A 401      50.890  52.464  28.570  1.00 16.29           O  
ATOM    762  N   ALA A 402      49.473  47.030  28.445  1.00 14.30           N  
ATOM    763  CA  ALA A 402      50.436  45.955  28.589  1.00 14.68           C  
ATOM    764  C   ALA A 402      51.599  46.333  29.504  1.00 16.15           C  
ATOM    765  O   ALA A 402      52.029  47.483  29.526  1.00 14.59           O  
ATOM    766  CB  ALA A 402      50.960  45.564  27.217  1.00 14.76           C  
ATOM    767  N   ASN A 403      52.089  45.357  30.267  1.00 16.25           N  
ATOM    768  CA  ASN A 403      53.231  45.553  31.156  1.00 18.84           C  
ATOM    769  C   ASN A 403      53.118  46.731  32.125  1.00 18.20           C  
ATOM    770  O   ASN A 403      54.130  47.334  32.497  1.00 15.97           O  
ATOM    771  CB  ASN A 403      54.503  45.709  30.312  1.00 23.43           C  
ATOM    772  CG  ASN A 403      54.790  44.482  29.453  1.00 26.76           C  
ATOM    773  OD1 ASN A 403      54.641  43.343  29.903  1.00 28.55           O  
ATOM    774  ND2 ASN A 403      55.203  44.711  28.211  1.00 30.74           N  
ATOM    775  N   SER A 404      51.900  47.054  32.545  1.00 16.63           N  
ATOM    776  CA  SER A 404      51.719  48.170  33.461  1.00 19.01           C  
ATOM    777  C   SER A 404      51.293  47.726  34.859  1.00 18.92           C  
ATOM    778  O   SER A 404      50.565  46.742  35.030  1.00 22.13           O  
ATOM    779  CB  SER A 404      50.711  49.166  32.886  1.00 19.38           C  
ATOM    780  OG  SER A 404      49.418  48.601  32.842  1.00 31.43           O  
ATOM    781  N   ARG A 405      51.762  48.463  35.860  1.00 15.77           N  
ATOM    782  CA  ARG A 405      51.465  48.155  37.249  1.00 14.83           C  
ATOM    783  C   ARG A 405      51.402  49.459  38.029  1.00 12.60           C  
ATOM    784  O   ARG A 405      51.604  50.534  37.472  1.00 15.26           O  
ATOM    785  CB  ARG A 405      52.559  47.248  37.820  1.00 15.18           C  
ATOM    786  CG  ARG A 405      53.949  47.815  37.616  1.00 10.83           C  
ATOM    787  CD  ARG A 405      55.055  46.835  37.957  1.00 16.55           C  
ATOM    788  NE  ARG A 405      56.343  47.457  37.674  1.00 18.96           N  
ATOM    789  CZ  ARG A 405      56.996  48.256  38.511  1.00 14.77           C  
ATOM    790  NH1 ARG A 405      56.492  48.537  39.705  1.00 14.50           N  
ATOM    791  NH2 ARG A 405      58.135  48.814  38.126  1.00 15.63           N  
ATOM    792  N   VAL A 406      51.131  49.354  39.322  1.00 13.51           N  
ATOM    793  CA  VAL A 406      51.014  50.518  40.183  1.00 15.62           C  
ATOM    794  C   VAL A 406      52.106  50.487  41.236  1.00 17.09           C  
ATOM    795  O   VAL A 406      52.354  49.440  41.823  1.00 20.71           O  
ATOM    796  CB  VAL A 406      49.639  50.525  40.899  1.00 14.78           C  
ATOM    797  CG1 VAL A 406      49.448  51.817  41.661  1.00 15.04           C  
ATOM    798  CG2 VAL A 406      48.516  50.340  39.880  1.00 17.63           C  
ATOM    799  N   ASN A 407      52.765  51.617  41.477  1.00 20.32           N  
ATOM    800  CA  ASN A 407      53.804  51.643  42.503  1.00 21.46           C  
ATOM    801  C   ASN A 407      53.224  52.096  43.844  1.00 20.01           C  
ATOM    802  O   ASN A 407      52.033  52.398  43.939  1.00 13.53           O  
ATOM    803  CB  ASN A 407      54.996  52.518  42.070  1.00 23.37           C  
ATOM    804  CG  ASN A 407      54.689  54.001  42.088  1.00 22.24           C  
ATOM    805  OD1 ASN A 407      53.676  54.432  42.627  1.00 25.61           O  
ATOM    806  ND2 ASN A 407      55.580  54.793  41.496  1.00 16.39           N  
ATOM    807  N   SER A 408      54.063  52.125  44.875  1.00 21.75           N  
ATOM    808  CA  SER A 408      53.624  52.489  46.219  1.00 27.37           C  
ATOM    809  C   SER A 408      52.931  53.841  46.376  1.00 29.33           C  
ATOM    810  O   SER A 408      52.173  54.039  47.328  1.00 31.93           O  
ATOM    811  CB  SER A 408      54.800  52.395  47.201  1.00 28.13           C  
ATOM    812  OG  SER A 408      55.904  53.172  46.769  1.00 35.98           O  
ATOM    813  N   SER A 409      53.177  54.771  45.459  1.00 28.27           N  
ATOM    814  CA  SER A 409      52.541  56.084  45.545  1.00 25.64           C  
ATOM    815  C   SER A 409      51.273  56.127  44.695  1.00 24.67           C  
ATOM    816  O   SER A 409      50.566  57.140  44.657  1.00 24.19           O  
ATOM    817  CB  SER A 409      53.512  57.171  45.085  1.00 26.42           C  
ATOM    818  OG  SER A 409      53.744  57.081  43.696  1.00 29.84           O  
ATOM    819  N   GLY A 410      50.989  55.017  44.020  1.00 21.88           N  
ATOM    820  CA  GLY A 410      49.810  54.940  43.176  1.00 19.30           C  
ATOM    821  C   GLY A 410      50.087  55.237  41.714  1.00 19.61           C  
ATOM    822  O   GLY A 410      49.179  55.184  40.882  1.00 17.46           O  
ATOM    823  N   ARG A 411      51.341  55.546  41.393  1.00 17.97           N  
ATOM    824  CA  ARG A 411      51.712  55.857  40.022  1.00 20.09           C  
ATOM    825  C   ARG A 411      51.668  54.628  39.122  1.00 19.61           C  
ATOM    826  O   ARG A 411      52.110  53.540  39.503  1.00 17.97           O  
ATOM    827  CB  ARG A 411      53.120  56.468  39.960  1.00 22.60           C  
ATOM    828  CG  ARG A 411      53.364  57.627  40.912  1.00 29.92           C  
ATOM    829  CD  ARG A 411      53.040  58.952  40.262  1.00 33.36           C  
ATOM    830  NE  ARG A 411      53.375  60.106  41.099  1.00 37.26           N  
ATOM    831  CZ  ARG A 411      53.087  60.221  42.393  1.00 38.56           C  
ATOM    832  NH1 ARG A 411      52.453  59.250  43.034  1.00 40.34           N  
ATOM    833  NH2 ARG A 411      53.412  61.326  43.047  1.00 42.33           N  
ATOM    834  N   ILE A 412      51.124  54.818  37.924  1.00 16.85           N  
ATOM    835  CA  ILE A 412      51.036  53.761  36.933  1.00 16.71           C  
ATOM    836  C   ILE A 412      52.389  53.673  36.226  1.00 18.41           C  
ATOM    837  O   ILE A 412      52.810  54.607  35.535  1.00 16.39           O  
ATOM    838  CB  ILE A 412      49.948  54.063  35.887  1.00 16.26           C  
ATOM    839  CG1 ILE A 412      48.571  54.016  36.548  1.00 15.09           C  
ATOM    840  CG2 ILE A 412      50.042  53.068  34.737  1.00 16.38           C  
ATOM    841  CD1 ILE A 412      47.473  54.635  35.714  1.00 16.07           C  
ATOM    842  N   VAL A 413      53.064  52.545  36.411  1.00 19.60           N  
ATOM    843  CA  VAL A 413      54.370  52.309  35.812  1.00 18.33           C  
ATOM    844  C   VAL A 413      54.252  51.248  34.734  1.00 17.29           C  
ATOM    845  O   VAL A 413      53.584  50.229  34.912  1.00 17.18           O  
ATOM    846  CB  VAL A 413      55.377  51.809  36.864  1.00 17.65           C  
ATOM    847  CG1 VAL A 413      56.701  51.455  36.200  1.00 23.12           C  
ATOM    848  CG2 VAL A 413      55.576  52.871  37.933  1.00 21.24           C  
ATOM    849  N   THR A 414      54.904  51.486  33.610  1.00 17.15           N  
ATOM    850  CA  THR A 414      54.872  50.526  32.520  1.00 19.72           C  
ATOM    851  C   THR A 414      56.292  50.030  32.275  1.00 21.06           C  
ATOM    852  O   THR A 414      57.213  50.832  32.147  1.00 23.01           O  
ATOM    853  CB  THR A 414      54.323  51.172  31.236  1.00 19.18           C  
ATOM    854  OG1 THR A 414      52.959  51.561  31.446  1.00 21.54           O  
ATOM    855  CG2 THR A 414      54.396  50.200  30.071  1.00 15.41           C  
ATOM    856  N   ASN A 415      56.467  48.712  32.213  1.00 24.05           N  
ATOM    857  CA  ASN A 415      57.787  48.123  31.992  1.00 27.29           C  
ATOM    858  C   ASN A 415      58.042  47.731  30.533  1.00 29.84           C  
ATOM    859  O   ASN A 415      57.129  47.888  29.696  1.00 31.51           O  
ATOM    860  CB  ASN A 415      57.971  46.901  32.901  1.00 25.14           C  
ATOM    861  CG  ASN A 415      57.629  47.199  34.356  1.00 25.46           C  
ATOM    862  OD1 ASN A 415      58.384  47.873  35.057  1.00 20.10           O  
ATOM    863  ND2 ASN A 415      56.485  46.698  34.813  1.00 23.46           N  
ATOM    864  OXT ASN A 415      59.164  47.265  30.240  1.00 35.37           O  
TER     865      ASN A 415                                                      
ATOM    866  N   LYS B   5      38.594  48.532  22.835  1.00 35.61           N  
ATOM    867  CA  LYS B   5      38.349  49.741  21.993  1.00 31.70           C  
ATOM    868  C   LYS B   5      38.933  50.992  22.639  1.00 28.85           C  
ATOM    869  O   LYS B   5      38.998  51.097  23.865  1.00 29.08           O  
ATOM    870  CB  LYS B   5      36.844  49.921  21.762  1.00 33.53           C  
ATOM    871  N   GLN B   6      39.365  51.933  21.805  1.00 25.12           N  
ATOM    872  CA  GLN B   6      39.933  53.191  22.280  1.00 22.72           C  
ATOM    873  C   GLN B   6      39.426  54.317  21.402  1.00 20.89           C  
ATOM    874  O   GLN B   6      39.508  54.241  20.177  1.00 21.39           O  
ATOM    875  CB  GLN B   6      41.456  53.157  22.212  1.00 21.86           C  
ATOM    876  CG  GLN B   6      42.089  52.350  23.300  1.00 24.26           C  
ATOM    877  CD  GLN B   6      43.279  53.041  23.936  1.00 23.46           C  
ATOM    878  OE1 GLN B   6      43.393  54.275  23.936  1.00 21.71           O  
ATOM    879  NE2 GLN B   6      44.173  52.244  24.496  1.00 26.30           N  
ATOM    880  N   THR B   7      38.912  55.367  22.027  1.00 17.70           N  
ATOM    881  CA  THR B   7      38.385  56.499  21.280  1.00 17.88           C  
ATOM    882  C   THR B   7      38.963  57.817  21.778  1.00 17.05           C  
ATOM    883  O   THR B   7      39.067  58.046  22.980  1.00 16.06           O  
ATOM    884  CB  THR B   7      36.838  56.555  21.379  1.00 14.05           C  
ATOM    885  OG1 THR B   7      36.287  55.316  20.918  1.00 17.31           O  
ATOM    886  CG2 THR B   7      36.281  57.685  20.537  1.00 13.72           C  
ATOM    887  N   SER B   8      39.359  58.674  20.843  1.00 14.96           N  
ATOM    888  CA  SER B   8      39.893  59.974  21.204  1.00 16.48           C  
ATOM    889  C   SER B   8      38.709  60.944  21.277  1.00 17.61           C  
ATOM    890  O   SER B   8      37.853  60.975  20.385  1.00 19.05           O  
ATOM    891  CB  SER B   8      40.923  60.435  20.164  1.00 16.65           C  
ATOM    892  OG  SER B   8      40.503  60.133  18.848  1.00 27.09           O  
ATOM    893  N   VAL B   9      38.653  61.724  22.349  1.00 16.11           N  
ATOM    894  CA  VAL B   9      37.565  62.674  22.546  1.00 15.65           C  
ATOM    895  C   VAL B   9      38.087  64.077  22.850  1.00 14.44           C  
ATOM    896  O   VAL B   9      37.261  65.006  22.965  1.00 16.00           O  
ATOM    897  CB  VAL B   9      36.649  62.225  23.712  1.00 11.15           C  
ATOM    898  CG1 VAL B   9      36.103  60.826  23.446  1.00 14.96           C  
ATOM    899  CG2 VAL B   9      37.427  62.238  25.011  1.00  9.83           C  
ATOM    900  OXT VAL B   9      39.315  64.234  22.983  1.00 15.84           O  
TER     901      VAL B   9                                                      
HETATM  902  O   HOH A   1      40.961  60.530  42.380  1.00 12.71           O  
HETATM  903  O   HOH A   2      33.163  55.055  34.097  1.00 11.94           O  
HETATM  904  O   HOH A   3      51.632  51.071  26.251  1.00 10.16           O  
HETATM  905  O   HOH A   4      48.497  53.463  46.269  1.00 24.55           O  
HETATM  906  O   HOH A   5      48.767  61.167  32.469  1.00 23.73           O  
HETATM  907  O   HOH A   6      41.840  47.699  43.394  1.00 43.65           O  
HETATM  908  O   HOH A   7      29.082  71.922  32.482  1.00 26.97           O  
HETATM  909  O   HOH A   8      44.545  67.468  26.440  1.00  8.75           O  
HETATM  910  O   HOH A   9      29.340  61.123  39.156  1.00 28.81           O  
HETATM  911  O   HOH A  10      45.699  67.217  32.866  1.00 14.57           O  
HETATM  912  O   HOH A  11      22.990  59.874  35.246  1.00 20.07           O  
HETATM  913  O   HOH A  12      54.278  47.671  41.165  1.00 13.24           O  
HETATM  914  O   HOH A  13      39.918  55.785  43.733  1.00 12.30           O  
HETATM  915  O   HOH A  14      29.423  65.286  35.866  1.00 12.97           O  
HETATM  916  O   HOH A  15      51.704  60.792  50.669  1.00 28.13           O  
HETATM  917  O   HOH A  16      50.242  46.605  40.472  1.00 23.27           O  
HETATM  918  O   HOH A  17      56.297  53.967  33.476  1.00 57.50           O  
HETATM  919  O   HOH A  18      41.314  66.804  39.821  1.00 21.18           O  
HETATM  920  O   HOH A  19      53.550  44.559  34.846  1.00 29.16           O  
HETATM  921  O   HOH A  20      43.740  62.291  41.672  1.00 13.93           O  
HETATM  922  O   HOH A  21      41.084  73.460  29.823  1.00 29.18           O  
HETATM  923  O   HOH A  22      48.992  58.241  35.444  1.00 23.69           O  
HETATM  924  O   HOH A  23      41.273  53.696  45.004  1.00 12.23           O  
HETATM  925  O   HOH A  24      26.569  64.812  27.527  1.00 34.41           O  
HETATM  926  O   HOH A  25      37.846  72.885  37.540  1.00 33.75           O  
HETATM  927  O   HOH A  26      51.068  42.858  29.530  1.00 21.20           O  
HETATM  928  O   HOH A  27      45.561  62.118  20.676  1.00 20.99           O  
HETATM  929  O   HOH A  28      47.450  56.763  45.024  1.00 28.99           O  
HETATM  930  O   HOH A  29      43.655  73.699  23.793  1.00 21.20           O  
HETATM  931  O   HOH A  30      51.568  47.786  44.719  1.00 47.06           O  
HETATM  932  O   HOH A  31      29.766  72.418  44.396  1.00 63.73           O  
HETATM  933  O   HOH A  32      49.099  45.307  32.755  1.00 21.59           O  
HETATM  934  O   HOH A  33      29.919  69.029  22.319  1.00 17.10           O  
HETATM  935  O   HOH A  34      50.132  57.535  37.472  1.00 25.35           O  
HETATM  936  O   HOH A  35      48.697  74.105  24.449  1.00 32.13           O  
HETATM  937  O   HOH A  36      44.996  64.300  38.499  1.00 28.83           O  
HETATM  938  O   HOH A  37      34.100  76.770  26.519  1.00 21.52           O  
HETATM  939  O   HOH A  38      47.986  64.609  33.734  1.00 30.49           O  
HETATM  940  O   HOH A  39      47.579  62.610  48.685  1.00 64.69           O  
HETATM  941  O   HOH A  40      40.689  74.727  27.571  1.00 40.09           O  
HETATM  942  O   HOH A  41      26.047  52.911  20.516  1.00 35.56           O  
HETATM  943  O   HOH A  42      55.459  52.578  28.020  1.00 24.57           O  
HETATM  944  O   HOH A  43      39.475  68.874  40.071  1.00 22.21           O  
HETATM  945  O   HOH A  44      50.784  71.923  28.012  1.00 33.03           O  
HETATM  946  O   HOH A  45      49.811  51.435  45.445  1.00 20.03           O  
HETATM  947  O   HOH A  46      57.035  43.490  32.844  1.00 38.53           O  
HETATM  948  O   HOH A  47      44.418  61.775  39.092  1.00 15.62           O  
HETATM  949  O   HOH A  48      37.968  67.671  16.713  1.00 31.42           O  
HETATM  950  O   HOH A  49      32.489  58.411  18.716  1.00 30.59           O  
HETATM  951  O   HOH A  50      35.075  50.364  37.935  1.00 52.25           O  
HETATM  952  O   HOH A  51      48.014  55.098  48.775  1.00 58.59           O  
HETATM  953  O   HOH A  52      39.832  73.005  33.975  1.00 66.84           O  
HETATM  954  O   HOH A  53      52.622  54.743  32.424  1.00 41.84           O  
HETATM  955  O   HOH A  54      30.606  48.329  24.100  1.00 68.85           O  
HETATM  956  O   HOH A  55      34.710  66.032  22.294  1.00 17.87           O  
HETATM  957  O   HOH A  58      28.027  69.138  19.994  1.00 34.80           O  
HETATM  958  O   HOH A  59      52.823  53.890  29.423  1.00 21.35           O  
HETATM  959  O   HOH A  60      55.104  43.796  25.792  1.00 21.63           O  
HETATM  960  O   HOH A  61      40.328  51.000  44.206  1.00 48.95           O  
HETATM  961  O   HOH A  62      49.496  62.978  30.726  1.00 23.26           O  
HETATM  962  O   HOH A  63      45.975  42.703  32.082  1.00 35.54           O  
HETATM  963  O   HOH A  64      58.094  52.870  40.571  1.00 32.05           O  
HETATM  964  O   HOH A  65      37.702  77.552  21.354  1.00 26.84           O  
HETATM  965  O   HOH A  66      34.488  72.529  41.815  1.00 37.04           O  
HETATM  966  O   HOH A  67      28.310  66.894  37.793  1.00 24.22           O  
HETATM  967  O   HOH A  68      43.552  61.819  22.758  1.00 19.72           O  
HETATM  968  O   HOH A  69      46.001  68.724  39.742  1.00 59.28           O  
HETATM  969  O   HOH A  70      28.682  74.528  27.690  1.00 34.97           O  
HETATM  970  O   HOH A  71      56.839  42.387  26.794  1.00 29.02           O  
HETATM  971  O   HOH A  72      39.083  74.920  30.856  1.00 70.57           O  
HETATM  972  O   HOH A  73      31.423  71.122  21.985  1.00 21.38           O  
HETATM  973  O   HOH A  74      25.376  53.846  35.971  1.00 19.87           O  
HETATM  974  O   HOH A  75      26.372  54.191  33.703  1.00 34.48           O  
HETATM  975  O   HOH A  76      26.873  50.878  19.425  1.00 44.93           O  
HETATM  976  O   HOH A  77      25.677  58.874  25.270  1.00 16.96           O  
HETATM  977  O   HOH A  78      50.841  72.982  25.585  1.00 36.52           O  
HETATM  978  O   HOH A  79      56.650  49.867  43.659  1.00 39.75           O  
HETATM  979  O   HOH A  80      28.216  71.924  28.090  1.00 49.55           O  
HETATM  980  O   HOH A  81      58.906  50.256  40.887  1.00 49.05           O  
HETATM  981  O   HOH A  82      49.779  44.840  36.664  1.00 31.14           O  
HETATM  982  O   HOH A  83      42.286  50.967  41.198  1.00 45.96           O  
HETATM  983  O   HOH A  84      43.674  65.074  42.496  1.00 29.23           O  
HETATM  984  O   HOH A  86      24.605  59.337  28.171  1.00 26.56           O  
HETATM  985  O   HOH A  87      36.834  68.826  42.903  1.00 51.44           O  
HETATM  986  O   HOH A  88      29.495  77.471  26.804  1.00 61.03           O  
HETATM  987  O   HOH A  90      47.571  46.656  39.917  1.00 38.45           O  
HETATM  988  O   HOH A  91      35.796  76.124  19.575  1.00 29.43           O  
HETATM  989  O   HOH A  92      35.534  47.335  29.325  1.00 42.25           O  
HETATM  990  O   HOH A  93      26.238  57.980  40.114  1.00 47.21           O  
HETATM  991  O   HOH A  94      35.881  63.688  46.787  1.00 40.37           O  
HETATM  992  O   HOH A  95      50.447  62.569  43.550  1.00 65.32           O  
HETATM  993  O   HOH A  96      43.484  44.061  27.782  1.00 34.29           O  
HETATM  994  O   HOH A  97      52.928  62.437  39.621  1.00 66.97           O  
HETATM  995  O   HOH A  98      54.664  41.473  32.751  1.00 52.16           O  
HETATM  996  O   HOH A  99      47.251  66.003  36.470  1.00 46.22           O  
HETATM  997  O   HOH A 100      25.925  73.504  26.403  1.00 59.53           O  
HETATM  998  O   HOH A 102      62.401  58.016  44.879  1.00 41.48           O  
HETATM  999  O   HOH A 103      30.512  50.469  21.988  1.00 27.81           O  
HETATM 1000  O   HOH A 104      37.358  48.365  36.186  1.00 26.28           O  
HETATM 1001  O   HOH A 105      43.390  44.915  37.531  1.00 52.30           O  
HETATM 1002  O   HOH A 106      52.874  72.826  29.215  1.00 44.97           O  
HETATM 1003  O   HOH A 107      24.817  69.411  25.237  1.00 49.85           O  
HETATM 1004  O   HOH A 108      26.035  61.622  37.886  1.00 48.56           O  
HETATM 1005  O   HOH A 109      31.395  50.649  32.076  1.00 38.81           O  
HETATM 1006  O   HOH A 110      39.688  47.049  34.306  1.00 43.55           O  
HETATM 1007  O   HOH A 111      22.678  55.542  34.246  1.00 29.33           O  
HETATM 1008  O   HOH A 112      32.517  51.103  37.465  1.00 31.87           O  
HETATM 1009  O   HOH A 113      49.962  55.529  47.252  1.00 30.40           O  
HETATM 1010  O   HOH A 114      39.705  42.179  39.639  1.00 63.69           O  
HETATM 1011  O   HOH A 115      34.589  42.251  29.628  1.00 52.71           O  
HETATM 1012  O   HOH A 116      27.657  74.083  24.629  1.00 32.64           O  
HETATM 1013  O   HOH A 117      24.069  57.333  32.358  1.00 18.75           O  
HETATM 1014  O   HOH A 119      24.485  63.250  22.488  1.00 59.39           O  
HETATM 1015  O   HOH A 120      52.575  58.557  35.458  1.00 52.23           O  
HETATM 1016  O   HOH A 122      48.635  49.654  43.846  1.00 25.00           O  
HETATM 1017  O   HOH A 123      28.509  58.783  38.811  1.00 31.00           O  
HETATM 1018  O   HOH A 124      29.103  42.005  30.145  1.00 53.26           O  
HETATM 1019  O   HOH A 125      48.211  69.807  21.082  1.00 59.51           O  
HETATM 1020  O   HOH A 126      35.070  73.557  39.020  1.00 51.60           O  
HETATM 1021  O   HOH A 127      56.751  56.241  44.454  1.00 54.58           O  
HETATM 1022  O   HOH A 128      45.642  72.003  40.094  1.00 29.86           O  
HETATM 1023  O   HOH A 129      26.878  68.512  35.889  1.00 26.09           O  
HETATM 1024  O   HOH A 130      46.154  60.015  49.122  1.00 52.18           O  
HETATM 1025  O   HOH A 131      43.404  59.562  48.846  1.00 30.83           O  
HETATM 1026  O   HOH A 132      43.834  66.596  40.110  1.00 30.96           O  
HETATM 1027  O   HOH A 133      53.536  60.826  37.538  1.00 45.05           O  
HETATM 1028  O   HOH A 134      56.552  55.990  39.272  1.00 44.69           O  
HETATM 1029  O   HOH A 135      35.504  76.641  35.538  1.00 48.35           O  
HETATM 1030  O   HOH A 136      40.976  73.882  22.433  1.00 39.53           O  
HETATM 1031  O   HOH A 137      24.085  59.835  39.148  1.00 37.80           O  
HETATM 1032  O   HOH A 138      44.707  75.204  34.681  1.00 43.98           O  
HETATM 1033  O   HOH A 140      50.508  56.090  52.391  1.00 48.13           O  
HETATM 1034  O   HOH A 141      21.629  62.350  34.167  1.00 70.55           O  
HETATM 1035  O   HOH A 142      40.259  67.994  18.625  1.00 65.65           O  
HETATM 1036  O   HOH A 143      40.255  70.436  18.966  1.00 48.88           O  
HETATM 1037  O   HOH A 144      29.306  61.658  18.353  1.00 68.72           O  
HETATM 1038  O   HOH A 146      27.088  64.919  39.110  1.00 40.27           O  
HETATM 1039  O   HOH B  56      41.900  63.663  21.567  1.00 16.70           O  
HETATM 1040  O   HOH B  57      37.314  60.044  17.990  1.00 20.64           O  
HETATM 1041  O   HOH B  85      40.629  54.188  17.399  1.00 23.73           O  
HETATM 1042  O   HOH B  89      33.515  54.764  19.863  1.00 36.51           O  
HETATM 1043  O   HOH B 101      38.169  51.254  19.159  1.00 53.29           O  
HETATM 1044  O   HOH B 118      38.095  49.467  25.570  1.00 44.76           O  
HETATM 1045  O   HOH B 121      41.515  47.569  20.703  1.00 52.80           O  
HETATM 1046  O   HOH B 139      36.648  54.593  18.449  1.00 38.91           O  
HETATM 1047  O   HOH B 145      39.705  46.113  23.703  1.00 51.08           O  
MASTER      351    0    0    4    7    0    3    6 1045    2    0   11          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.