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***  NMA_MIARA_CALMODULIN  ***

elNémo ID: 200510174347110137

Job options:

ID        	=	 200510174347110137
JOBID     	=	 NMA_MIARA_CALMODULIN
USERID    	=	 miara1502
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER NMA_MIARA_CALMODULIN

HEADER    TRANSFERASE                             12-MAR-03   1HKX              
TITLE     CRYSTAL STRUCTURE OF CALCIUM/CALMODULIN-DEPENDENT                     
TITLE    2 PROTEIN KINASE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE           
COMPND   3  II ALPHA CHAIN;                                                     
COMPND   4 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;                     
COMPND   5 FRAGMENT: ASSOCIATION DOMAIN, RESIDUES 336-478;                      
COMPND   6 SYNONYM: CAM-KINASE II ALPHA CHAIN, CAM KINASE II ALPHA              
COMPND   7  SUBUNIT, CAMK-II ALPHA SUBUNIT, CAMK2A;                             
COMPND   8 EC: 2.7.1.123;                                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, CALMODULIN-             
KEYWDS   2 BINDING, PHOSPHORYLATION, ATP-BINDING, ALTERNATIVE                   
KEYWDS   3 SPLICING                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HOELZ,A.C.NAIRN,J.KURIYAN                                           
REVDAT   2   24-FEB-09 1HKX    1       VERSN                                    
REVDAT   1   02-JUN-03 1HKX    0                                                
JRNL        AUTH   A.HOELZ,A.C.NAIRN,J.KURIYAN                                  
JRNL        TITL   CRYSTAL STRUCTURE OF A TETRADECAMERIC ASSEMBLY OF            
JRNL        TITL 2 THE ASSOCIATION DOMAIN OF                                    
JRNL        TITL 3 CA2+/CALMODULIN-DEPENDENT KINASE II                          
JRNL        REF    MOL.CELL                      V.  11  1241 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12769848                                                     
JRNL        DOI    10.1016/S1097-2765(03)00171-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 175595.70                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.000000                       
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 135629                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 6774                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.2                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 17306                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.358                        
REMARK   3   BIN FREE R VALUE                    : 0.381                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.7                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 850                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15588                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.9                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.2                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.65                                                
REMARK   3    B22 (A**2) : -5.76                                                
REMARK   3    B33 (A**2) : 7.41                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -5.20                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.46                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.45                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.4                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.7                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.07                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.85  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.41  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.94  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.19  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30536                                              
REMARK   3   BSOL        : 33.0973                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : TBR_XPLOR.PAR                                  
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  5  : DTT.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : DTT.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : TBR_XPLOR.TOP                                  
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HKX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12355.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ALS; ALS                           
REMARK 200  BEAMLINE                       : 5.0.2; 8.2.1                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9187,0.9191,1.2543; 1.2545,      
REMARK 200                                   1.0038,1.0090                      
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; MAD                                       
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: RAVE, CCP4                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       73.97300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.02150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       73.97300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       59.02150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: TETRADECAMERIC                    
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC             
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  THIS KINASE MAY PLAY A ROLE IN NEUROTRANSMISSION.                   
REMARK 400  CATALYES ATP + PROTEIN = ADP + O-PHOSPHOPROTEIN.                    
REMARK 400  AUTOPHOSPHORYLATION OF THR-286 MAY ALLOW THE KINASE                 
REMARK 400  TO SWITCH FROM A CALMODULIN-DEPENDENT TO A CALMODULIN-              
REMARK 400  INDEPENDENT STATE.                                                  
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   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     LEU A   476                                                      
REMARK 465     PRO A   477                                                      
REMARK 465     HIS A   478                                                      
REMARK 465     GLY B   332                                                      
REMARK 465     PRO B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     MET B   335                                                      
REMARK 465     THR B   336                                                      
REMARK 465     THR B   337                                                      
REMARK 465     ILE B   338                                                      
REMARK 465     GLU B   339                                                      
REMARK 465     LEU B   476                                                      
REMARK 465     PRO B   477                                                      
REMARK 465     HIS B   478                                                      
REMARK 465     GLY C   332                                                      
REMARK 465     PRO C   333                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     MET C   335                                                      
REMARK 465     THR C   336                                                      
REMARK 465     LEU C   476                                                      
REMARK 465     PRO C   477                                                      
REMARK 465     HIS C   478                                                      
REMARK 465     GLY D   332                                                      
REMARK 465     PRO D   333                                                      
REMARK 465     HIS D   334                                                      
REMARK 465     MET D   335                                                      
REMARK 465     THR D   336                                                      
REMARK 465     THR D   337                                                      
REMARK 465     LEU D   476                                                      
REMARK 465     PRO D   477                                                      
REMARK 465     HIS D   478                                                      
REMARK 465     LEU E   476                                                      
REMARK 465     PRO E   477                                                      
REMARK 465     HIS E   478                                                      
REMARK 465     GLY F   332                                                      
REMARK 465     PRO F   333                                                      
REMARK 465     HIS F   334                                                      
REMARK 465     MET F   335                                                      
REMARK 465     THR F   336                                                      
REMARK 465     LEU F   476                                                      
REMARK 465     PRO F   477                                                      
REMARK 465     HIS F   478                                                      
REMARK 465     GLY G   332                                                      
REMARK 465     PRO G   333                                                      
REMARK 465     HIS G   334                                                      
REMARK 465     MET G   335                                                      
REMARK 465     THR G   336                                                      
REMARK 465     THR G   337                                                      
REMARK 465     ILE G   338                                                      
REMARK 465     GLU G   339                                                      
REMARK 465     LEU G   476                                                      
REMARK 465     PRO G   477                                                      
REMARK 465     HIS G   478                                                      
REMARK 465     GLY H   332                                                      
REMARK 465     LEU H   476                                                      
REMARK 465     PRO H   477                                                      
REMARK 465     HIS H   478                                                      
REMARK 465     GLY I   332                                                      
REMARK 465     PRO I   333                                                      
REMARK 465     HIS I   334                                                      
REMARK 465     MET I   335                                                      
REMARK 465     THR I   336                                                      
REMARK 465     THR I   337                                                      
REMARK 465     ILE I   338                                                      
REMARK 465     GLU I   339                                                      
REMARK 465     ASP I   340                                                      
REMARK 465     LEU I   476                                                      
REMARK 465     PRO I   477                                                      
REMARK 465     HIS I   478                                                      
REMARK 465     GLY J   332                                                      
REMARK 465     PRO J   333                                                      
REMARK 465     HIS J   334                                                      
REMARK 465     MET J   335                                                      
REMARK 465     THR J   336                                                      
REMARK 465     LEU J   476                                                      
REMARK 465     PRO J   477                                                      
REMARK 465     HIS J   478                                                      
REMARK 465     GLY K   332                                                      
REMARK 465     PRO K   333                                                      
REMARK 465     HIS K   334                                                      
REMARK 465     MET K   335                                                      
REMARK 465     THR K   336                                                      
REMARK 465     THR K   337                                                      
REMARK 465     ILE K   338                                                      
REMARK 465     GLU K   339                                                      
REMARK 465     ASP K   340                                                      
REMARK 465     LEU K   476                                                      
REMARK 465     PRO K   477                                                      
REMARK 465     HIS K   478                                                      
REMARK 465     GLY L   332                                                      
REMARK 465     PRO L   333                                                      
REMARK 465     HIS L   334                                                      
REMARK 465     MET L   335                                                      
REMARK 465     THR L   336                                                      
REMARK 465     THR L   337                                                      
REMARK 465     ILE L   338                                                      
REMARK 465     GLU L   339                                                      
REMARK 465     ASP L   340                                                      
REMARK 465     LEU L   476                                                      
REMARK 465     PRO L   477                                                      
REMARK 465     HIS L   478                                                      
REMARK 465     GLY M   332                                                      
REMARK 465     PRO M   333                                                      
REMARK 465     HIS M   334                                                      
REMARK 465     MET M   335                                                      
REMARK 465     THR M   336                                                      
REMARK 465     LEU M   476                                                      
REMARK 465     PRO M   477                                                      
REMARK 465     HIS M   478                                                      
REMARK 465     GLY N   332                                                      
REMARK 465     PRO N   333                                                      
REMARK 465     HIS N   334                                                      
REMARK 465     MET N   335                                                      
REMARK 465     THR N   336                                                      
REMARK 465     THR N   337                                                      
REMARK 465     ILE N   338                                                      
REMARK 465     GLU N   339                                                      
REMARK 465     LEU N   476                                                      
REMARK 465     PRO N   477                                                      
REMARK 465     HIS N   478                                                      
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     VAL A 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL B 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL C 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL D 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL E 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL F 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL G 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL H 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL I 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL J 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL K 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL L 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL M 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL N 475    CA   C    O    CB   CG1  CG2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 439   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    PRO D 473   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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 339       74.55     53.09                                   
REMARK 500    ASP A 340      -38.85    156.88                                   
REMARK 500    LEU A 402       69.30   -156.34                                   
REMARK 500    LEU A 438     -151.64    -98.87                                   
REMARK 500    ASP A 439     -128.94   -168.02                                   
REMARK 500    ALA A 472      -14.05    -36.32                                   
REMARK 500    GLU B 341      -11.11     64.59                                   
REMARK 500    PHE B 397      -41.92    157.59                                   
REMARK 500    SER B 404       12.62    -66.44                                   
REMARK 500    ARG B 405       -2.95    -57.02                                   
REMARK 500    ASN B 406       44.96    -81.83                                   
REMARK 500    SER B 407       19.34   -161.92                                   
REMARK 500    LYS B 408      106.66   -175.90                                   
REMARK 500    LEU B 438     -131.58    -98.93                                   
REMARK 500    ASP B 439     -150.77     45.88                                   
REMARK 500    PRO B 473      136.04    -22.55                                   
REMARK 500    ILE C 338       35.83    -82.78                                   
REMARK 500    ASP C 340       36.30    -80.88                                   
REMARK 500    LEU C 402       58.89   -142.34                                   
REMARK 500    SER C 404       46.22    -69.73                                   
REMARK 500    LEU C 438     -130.89    -99.73                                   
REMARK 500    ASP C 439     -163.09     52.06                                   
REMARK 500    ALA C 472       30.87    175.00                                   
REMARK 500    PRO C 473      -95.40    -47.89                                   
REMARK 500    ASP D 340        4.34    159.05                                   
REMARK 500    GLU D 400      -71.78    -91.11                                   
REMARK 500    LEU D 402       19.73   -150.20                                   
REMARK 500    SER D 404       46.12    -73.47                                   
REMARK 500    ASN D 406       28.31    -76.41                                   
REMARK 500    SER D 407        4.37   -151.33                                   
REMARK 500    LEU D 438     -138.53    -97.46                                   
REMARK 500    ASP D 439     -148.23     56.15                                   
REMARK 500    ALA D 472      -62.10    177.65                                   
REMARK 500    PRO D 473      155.86    -12.44                                   
REMARK 500    HIS E 334       61.61     69.85                                   
REMARK 500    THR E 337      156.74    165.78                                   
REMARK 500    ASN E 401      -68.23   -101.10                                   
REMARK 500    SER E 404       22.23    -65.45                                   
REMARK 500    ASN E 406       76.16    -65.51                                   
REMARK 500    SER E 407       -0.95   -140.50                                   
REMARK 500    LEU E 438     -116.61   -101.88                                   
REMARK 500    ASP E 439     -168.63     40.40                                   
REMARK 500    ALA E 472      -29.51   -171.88                                   
REMARK 500    ASP F 340       76.55     77.06                                   
REMARK 500    ASN F 401       71.75   -110.90                                   
REMARK 500    LEU F 402      -12.51    177.97                                   
REMARK 500    TRP F 403      -66.06     -5.41                                   
REMARK 500    SER F 407       20.65    -60.78                                   
REMARK 500    LYS F 408      133.47    166.91                                   
REMARK 500    LEU F 438     -123.28   -100.43                                   
REMARK 500    ASP F 439     -172.99     57.00                                   
REMARK 500    ALA F 472      -35.21    177.78                                   
REMARK 500    PRO F 473      174.18    -51.65                                   
REMARK 500    GLU G 341       -9.28     64.51                                   
REMARK 500    PHE G 399      -76.24    -79.89                                   
REMARK 500    GLU G 400      -31.25    -36.93                                   
REMARK 500    LEU G 402       33.09   -167.19                                   
REMARK 500    SER G 404       -8.03    -58.53                                   
REMARK 500    ASN G 406       50.23    -68.47                                   
REMARK 500    SER G 407      -59.60   -146.95                                   
REMARK 500    LEU G 438     -123.00   -101.08                                   
REMARK 500    ASP G 439     -164.90     50.02                                   
REMARK 500    ALA G 472      -55.15   -120.94                                   
REMARK 500    PRO G 473      148.96    -18.05                                   
REMARK 500    MET H 335       73.21    -36.65                                   
REMARK 500    THR H 336      -34.91   -169.55                                   
REMARK 500    ILE H 338      -54.32   -167.88                                   
REMARK 500    LEU H 402       56.93   -151.94                                   
REMARK 500    LEU H 438     -132.92   -100.45                                   
REMARK 500    ASP H 439     -167.43     50.99                                   
REMARK 500    ALA H 472      -77.90   -128.01                                   
REMARK 500    PRO H 473     -142.84      5.77                                   
REMARK 500    ARG I 396        5.41    -63.85                                   
REMARK 500    GLU I 400      -72.75    -57.91                                   
REMARK 500    LEU I 402       65.42   -169.04                                   
REMARK 500    SER I 404       30.92    -98.92                                   
REMARK 500    ARG I 405       48.62    -72.74                                   
REMARK 500    ASN I 406      -53.68   -166.10                                   
REMARK 500    SER I 407        4.96    -61.56                                   
REMARK 500    PRO I 409      108.44    -53.78                                   
REMARK 500    LEU I 438     -135.74    -94.97                                   
REMARK 500    ASP I 439     -156.67   -165.39                                   
REMARK 500    ALA I 472       -4.98    178.69                                   
REMARK 500    PRO I 473     -121.42    -59.64                                   
REMARK 500    ASP J 340     -154.51    -71.18                                   
REMARK 500    GLU J 341      -23.32     67.21                                   
REMARK 500    GLU J 400      -75.97   -113.75                                   
REMARK 500    SER J 407       19.37   -172.98                                   
REMARK 500    LYS J 408      103.81   -171.30                                   
REMARK 500    LEU J 438      -76.84    -90.25                                   
REMARK 500    ASP J 439     -109.33    -60.79                                   
REMARK 500    SER J 449      145.32    176.22                                   
REMARK 500    ARG J 458     -112.34    -99.46                                   
REMARK 500    ALA J 472       32.80    162.43                                   
REMARK 500    PRO J 473     -106.04    -77.70                                   
REMARK 500    ASN K 401       37.16    -73.85                                   
REMARK 500    LEU K 402       72.88   -179.50                                   
REMARK 500    ASN K 416       51.91     39.26                                   
REMARK 500    TYR K 437     -166.40   -126.12                                   
REMARK 500    ASP K 439     -168.54     48.10                                   
REMARK 500    ALA K 472      -46.04    172.58                                   
REMARK 500    PRO K 473       97.33    -25.37                                   
REMARK 500    LEU L 402       20.44   -143.78                                   
REMARK 500    SER L 404       49.89    -70.43                                   
REMARK 500    SER L 407       36.38    -69.48                                   
REMARK 500    LYS L 408      110.09    169.00                                   
REMARK 500    LEU L 438     -116.08   -124.96                                   
REMARK 500    ASP L 439     -169.81     47.03                                   
REMARK 500    ALA L 472      -34.18   -179.75                                   
REMARK 500    PRO L 473      -98.69    -24.48                                   
REMARK 500    ILE M 338      -20.85   -146.68                                   
REMARK 500    GLU M 339      177.93    -58.38                                   
REMARK 500    ASP M 340       77.35     11.59                                   
REMARK 500    THR M 343       13.37    -65.31                                   
REMARK 500    LEU M 402       77.85   -162.72                                   
REMARK 500    SER M 404       39.83    -66.65                                   
REMARK 500    ASN M 406      -83.46    -59.53                                   
REMARK 500    SER M 407       13.68    -68.02                                   
REMARK 500    LEU M 438     -108.87    -94.39                                   
REMARK 500    ASP M 439     -149.53     31.16                                   
REMARK 500    ALA M 472      -68.38   -105.95                                   
REMARK 500    PRO M 473      151.34    -24.43                                   
REMARK 500    GLU N 341       82.07    -42.17                                   
REMARK 500    PHE N 399      -72.64    -80.54                                   
REMARK 500    LYS N 408      123.28    172.66                                   
REMARK 500    LEU N 438     -129.45   -100.10                                   
REMARK 500    ASP N 439     -179.71     72.75                                   
REMARK 500    ALA N 472      -30.75   -158.75                                   
REMARK 500    PRO N 473     -171.54    -50.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL E1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL F1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL G1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL H1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL I1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL J1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL K1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL L1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL M1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL N1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBR A2000                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CDM   RELATED DB: PDB                                   
DBREF  1HKX A  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX A  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX B  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX B  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX C  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX C  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX D  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX D  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX E  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX E  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX F  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX F  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX G  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX G  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX H  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX H  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX I  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX I  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX J  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX J  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX K  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX K  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX L  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX L  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX M  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX M  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX N  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX N  336   478  UNP    P11798   KCCA_MOUSE     336    478             
SEQRES   1 A  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 A  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 A  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 A  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 A  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 A  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 A  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 A  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 A  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 A  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 A  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 A  147  VAL LEU PRO HIS                                              
SEQRES   1 B  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 B  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 B  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 B  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 B  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 B  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 B  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 B  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 B  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 B  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 B  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 B  147  VAL LEU PRO HIS                                              
SEQRES   1 C  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 C  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 C  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 C  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 C  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 C  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 C  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 C  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 C  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 C  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 C  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 C  147  VAL LEU PRO HIS                                              
SEQRES   1 D  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 D  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 D  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 D  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 D  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 D  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 D  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 D  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 D  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 D  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 D  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 D  147  VAL LEU PRO HIS                                              
SEQRES   1 E  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 E  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 E  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 E  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 E  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 E  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 E  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 E  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 E  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 E  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 E  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 E  147  VAL LEU PRO HIS                                              
SEQRES   1 F  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 F  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 F  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 F  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 F  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 F  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 F  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 F  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 F  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 F  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 F  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 F  147  VAL LEU PRO HIS                                              
SEQRES   1 G  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 G  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 G  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 G  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 G  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 G  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 G  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 G  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 G  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 G  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 G  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 G  147  VAL LEU PRO HIS                                              
SEQRES   1 H  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 H  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 H  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 H  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 H  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 H  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 H  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 H  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 H  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 H  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 H  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 H  147  VAL LEU PRO HIS                                              
SEQRES   1 I  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 I  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 I  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 I  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 I  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 I  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 I  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 I  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 I  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 I  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 I  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 I  147  VAL LEU PRO HIS                                              
SEQRES   1 J  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 J  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 J  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 J  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 J  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 J  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 J  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 J  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 J  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 J  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 J  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 J  147  VAL LEU PRO HIS                                              
SEQRES   1 K  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 K  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 K  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 K  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 K  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 K  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 K  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 K  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 K  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 K  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 K  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 K  147  VAL LEU PRO HIS                                              
SEQRES   1 L  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 L  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 L  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 L  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 L  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 L  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 L  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 L  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 L  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 L  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 L  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 L  147  VAL LEU PRO HIS                                              
SEQRES   1 M  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 M  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 M  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 M  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 M  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 M  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 M  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 M  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 M  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 M  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 M  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 M  147  VAL LEU PRO HIS                                              
SEQRES   1 N  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 N  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 N  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 N  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 N  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 N  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 N  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 N  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 N  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 N  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 N  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 N  147  VAL LEU PRO HIS                                              
HET     CL  A1476       1                                                       
HET     CL  B1475       1                                                       
HET     CL  C1475       1                                                       
HET     CL  D1475       1                                                       
HET     CL  E1475       1                                                       
HET     CL  F1475       1                                                       
HET     CL  G1475       1                                                       
HET     CL  H1475       1                                                       
HET     CL  I1475       1                                                       
HET     CL  J1475       1                                                       
HET     CL  K1475       1                                                       
HET     CL  L1475       1                                                       
HET     CL  M1475       1                                                       
HET     CL  N1475       1                                                       
HET    DTT  A1475       8                                                       
HET    TBR  A2000      18                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     TBR HEXATANTALUM DODECABROMIDE                                       
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL  15   CL    14(CL 1-)                                                    
FORMUL  29  DTT    C4 H10 O2 S2                                                 
FORMUL  30  TBR    BR12 TA6 2+                                                  
FORMUL  31  HOH   *62(H2 O1)                                                    
HELIX    1   1 ASP A  340  ASN A  363  1                                  24    
HELIX    2   2 ASP A  365  MET A  372  1                                   8    
HELIX    3   3 GLU A  381  LEU A  385  5                                   5    
HELIX    4   4 LEU A  392  ASN A  401  1                                  10    
HELIX    5   5 TRP A  403  SER A  407  5                                   5    
HELIX    6   6 GLU B  341  ASN B  363  1                                  23    
HELIX    7   7 ASP B  365  MET B  372  1                                   8    
HELIX    8   8 GLU B  381  LEU B  385  5                                   5    
HELIX    9   9 LEU B  392  ASN B  401  1                                  10    
HELIX   10  10 TRP B  403  SER B  407  5                                   5    
HELIX   11  11 GLU C  341  ASN C  363  1                                  23    
HELIX   12  12 ASP C  365  MET C  372  1                                   8    
HELIX   13  13 GLU C  381  LEU C  385  5                                   5    
HELIX   14  14 LEU C  392  ASN C  401  1                                  10    
HELIX   15  15 TRP C  403  SER C  407  5                                   5    
HELIX   16  16 GLU D  341  ASN D  363  1                                  23    
HELIX   17  17 ASP D  365  MET D  372  1                                   8    
HELIX   18  18 GLU D  381  LEU D  385  5                                   5    
HELIX   19  19 LEU D  392  ASN D  401  1                                  10    
HELIX   20  20 TRP D  403  SER D  407  5                                   5    
HELIX   21  21 GLU E  341  ASN E  363  1                                  23    
HELIX   22  22 ASP E  365  MET E  372  1                                   8    
HELIX   23  23 GLU E  381  LEU E  385  5                                   5    
HELIX   24  24 LEU E  392  ASN E  401  1                                  10    
HELIX   25  25 TRP E  403  SER E  407  5                                   5    
HELIX   26  26 GLU F  341  ASN F  363  1                                  23    
HELIX   27  27 ASP F  365  MET F  372  1                                   8    
HELIX   28  28 GLU F  381  LEU F  385  5                                   5    
HELIX   29  29 LEU F  392  ASN F  401  1                                  10    
HELIX   30  30 TRP F  403  SER F  407  5                                   5    
HELIX   31  31 GLU G  341  ASN G  363  1                                  23    
HELIX   32  32 ASP G  365  MET G  372  1                                   8    
HELIX   33  33 GLU G  381  LEU G  385  5                                   5    
HELIX   34  34 LEU G  392  ASN G  401  1                                   7    
HELIX   35  35 TRP G  403  SER G  407  5                                   5    
HELIX   36  36 GLU H  339  ASN H  363  1                                  25    
HELIX   37  37 ASP H  365  MET H  372  1                                   8    
HELIX   38  38 GLU H  381  LEU H  385  5                                   5    
HELIX   39  39 LEU H  392  ASN H  401  1                                  10    
HELIX   40  40 TRP H  403  SER H  407  5                                   6    
HELIX   41  41 ASP I  342  ASN I  363  1                                  22    
HELIX   42  42 ASP I  365  MET I  372  1                                   8    
HELIX   43  43 GLU I  381  LEU I  385  5                                   5    
HELIX   44  44 LEU I  392  ASN I  401  1                                  10    
HELIX   45  45 TRP I  403  SER I  407  5                                   5    
HELIX   46  46 ASP J  342  ASN J  363  1                                  22    
HELIX   47  47 ASP J  365  MET J  372  1                                   8    
HELIX   48  48 GLU J  381  LEU J  385  5                                   5    
HELIX   49  49 LEU J  392  ASN J  401  1                                  10    
HELIX   50  50 TRP J  403  SER J  407  5                                   5    
HELIX   51  51 GLU K  341  ASN K  363  1                                  23    
HELIX   52  52 ASP K  365  MET K  372  1                                   8    
HELIX   53  53 GLU K  381  LEU K  385  5                                   5    
HELIX   54  54 LEU K  392  ASN K  401  1                                  10    
HELIX   55  55 TRP K  403  SER K  407  5                                   5    
HELIX   56  56 GLU L  341  ASN L  363  1                                  23    
HELIX   57  57 ASP L  365  MET L  372  1                                   8    
HELIX   58  58 GLU L  381  LEU L  385  5                                   5    
HELIX   59  59 LEU L  392  ASN L  401  1                                  10    
HELIX   60  60 TRP L  403  SER L  407  5                                   5    
HELIX   61  61 ASP M  340  ASN M  363  1                                  24    
HELIX   62  62 ASP M  365  MET M  372  1                                   8    
HELIX   63  63 GLU M  381  LEU M  385  5                                   5    
HELIX   64  64 LEU M  392  ASN M  401  1                                  10    
HELIX   65  65 TRP M  403  SER M  407  5                                   5    
HELIX   66  66 GLU N  341  ASN N  363  1                                  23    
HELIX   67  67 ASP N  365  MET N  372  1                                   8    
HELIX   68  68 GLU N  381  LEU N  385  5                                   5    
HELIX   69  69 LEU N  392  ASN N  401  1                                  10    
HELIX   70  70 TRP N  403  SER N  407  5                                   5    
SHEET    1  AA 6 VAL A 389  GLU A 390  0                                        
SHEET    2  AA 6 CYS A 373  PHE A 380 -1  O  ALA A 379   N  VAL A 389           
SHEET    3  AA 6 LYS A 461  SER A 470  1  O  ILE A 464   N  ASP A 374           
SHEET    4  AA 6 ARG A 445  ARG A 458 -1  O  GLU A 450   N  SER A 470           
SHEET    5  AA 6 SER A 426  TYR A 437 -1  O  ALA A 427   N  TRP A 455           
SHEET    6  AA 6 VAL A 410  LEU A 421 -1  O  HIS A 411   N  GLN A 436           
SHEET    1  BA 6 VAL B 389  GLU B 390  0                                        
SHEET    2  BA 6 CYS B 373  PHE B 380 -1  O  ALA B 379   N  VAL B 389           
SHEET    3  BA 6 LYS B 461  GLY B 471  1  O  ILE B 464   N  ASP B 374           
SHEET    4  BA 6 ARG B 445  ARG B 458 -1  O  GLU B 450   N  SER B 470           
SHEET    5  BA 6 SER B 426  TYR B 437 -1  O  ALA B 427   N  TRP B 455           
SHEET    6  BA 6 HIS B 411  LEU B 421 -1  O  HIS B 411   N  GLN B 436           
SHEET    1  CA 6 VAL C 389  GLU C 390  0                                        
SHEET    2  CA 6 CYS C 373  PHE C 380 -1  O  ALA C 379   N  VAL C 389           
SHEET    3  CA 6 LYS C 461  SER C 470  1  O  ILE C 464   N  ASP C 374           
SHEET    4  CA 6 ARG C 445  ARG C 458 -1  O  GLU C 450   N  SER C 470           
SHEET    5  CA 6 SER C 426  TYR C 437 -1  O  ALA C 427   N  TRP C 455           
SHEET    6  CA 6 VAL C 410  LEU C 421 -1  O  HIS C 411   N  GLN C 436           
SHEET    1  DA 6 VAL D 389  GLU D 390  0                                        
SHEET    2  DA 6 CYS D 373  PHE D 380 -1  O  ALA D 379   N  VAL D 389           
SHEET    3  DA 6 LYS D 461  SER D 470  1  O  ILE D 464   N  ASP D 374           
SHEET    4  DA 6 ARG D 445  ARG D 458 -1  O  GLU D 450   N  SER D 470           
SHEET    5  DA 6 SER D 426  TYR D 437 -1  O  ALA D 427   N  TRP D 455           
SHEET    6  DA 6 HIS D 411  LEU D 421 -1  O  HIS D 411   N  GLN D 436           
SHEET    1  EA 6 VAL E 389  GLU E 390  0                                        
SHEET    2  EA 6 CYS E 373  PHE E 380 -1  O  ALA E 379   N  VAL E 389           
SHEET    3  EA 6 LYS E 461  SER E 470  1  O  ILE E 464   N  ASP E 374           
SHEET    4  EA 6 ARG E 445  ARG E 458 -1  O  GLU E 450   N  SER E 470           
SHEET    5  EA 6 SER E 426  TYR E 437 -1  O  ALA E 427   N  TRP E 455           
SHEET    6  EA 6 VAL E 410  LEU E 421 -1  O  HIS E 411   N  GLN E 436           
SHEET    1  FA 6 VAL F 389  GLU F 390  0                                        
SHEET    2  FA 6 CYS F 373  PHE F 380 -1  O  ALA F 379   N  VAL F 389           
SHEET    3  FA 6 LYS F 461  SER F 470  1  O  ILE F 464   N  ASP F 374           
SHEET    4  FA 6 ARG F 445  ARG F 458 -1  O  GLU F 450   N  SER F 470           
SHEET    5  FA 6 SER F 426  TYR F 437 -1  O  ALA F 427   N  TRP F 455           
SHEET    6  FA 6 HIS F 411  LEU F 421 -1  O  HIS F 411   N  GLN F 436           
SHEET    1  GA 6 VAL G 389  GLU G 390  0                                        
SHEET    2  GA 6 CYS G 373  PHE G 380 -1  O  ALA G 379   N  VAL G 389           
SHEET    3  GA 6 LYS G 461  GLY G 471  1  O  ILE G 464   N  ASP G 374           
SHEET    4  GA 6 ARG G 445  ARG G 458 -1  O  GLU G 450   N  SER G 470           
SHEET    5  GA 6 SER G 426  TYR G 437 -1  O  ALA G 427   N  TRP G 455           
SHEET    6  GA 6 HIS G 411  LEU G 421 -1  O  HIS G 411   N  GLN G 436           
SHEET    1  HA 6 VAL H 389  GLU H 390  0                                        
SHEET    2  HA 6 CYS H 373  PHE H 380 -1  O  ALA H 379   N  VAL H 389           
SHEET    3  HA 6 LYS H 461  GLY H 471  1  O  ILE H 464   N  ASP H 374           
SHEET    4  HA 6 ARG H 445  ARG H 458 -1  O  GLU H 450   N  SER H 470           
SHEET    5  HA 6 SER H 426  TYR H 437 -1  O  ALA H 427   N  TRP H 455           
SHEET    6  HA 6 HIS H 411  LEU H 421 -1  O  HIS H 411   N  GLN H 436           
SHEET    1  IA 6 VAL I 389  GLU I 390  0                                        
SHEET    2  IA 6 CYS I 373  PHE I 380 -1  O  ALA I 379   N  VAL I 389           
SHEET    3  IA 6 LYS I 461  SER I 470  1  O  ILE I 464   N  ASP I 374           
SHEET    4  IA 6 ARG I 445  ARG I 458 -1  O  GLU I 450   N  SER I 470           
SHEET    5  IA 6 SER I 426  TYR I 437 -1  O  ALA I 427   N  TRP I 455           
SHEET    6  IA 6 HIS I 411  LEU I 421 -1  O  HIS I 411   N  GLN I 436           
SHEET    1  JA 6 VAL J 389  GLU J 390  0                                        
SHEET    2  JA 6 CYS J 373  PHE J 380 -1  O  ALA J 379   N  VAL J 389           
SHEET    3  JA 6 TRP J 462  SER J 470  1  O  ILE J 464   N  ASP J 374           
SHEET    4  JA 6 GLU J 450  ARG J 457 -1  O  GLU J 450   N  SER J 470           
SHEET    5  JA 6 SER J 426  TYR J 437 -1  O  ALA J 427   N  TRP J 455           
SHEET    6  JA 6 HIS J 411  LEU J 421 -1  O  HIS J 411   N  GLN J 436           
SHEET    1  JB 6 VAL J 389  GLU J 390  0                                        
SHEET    2  JB 6 CYS J 373  PHE J 380 -1  O  ALA J 379   N  VAL J 389           
SHEET    3  JB 6 TRP J 462  SER J 470  1  O  ILE J 464   N  ASP J 374           
SHEET    4  JB 6 GLU J 450  ARG J 457 -1  O  GLU J 450   N  SER J 470           
SHEET    5  JB 6 SER J 426  TYR J 437 -1  O  ALA J 427   N  TRP J 455           
SHEET    6  JB 6 ARG J 445  ALA J 447 -1  O  ARG J 445   N  TYR J 437           
SHEET    1  KA 6 VAL K 389  GLU K 390  0                                        
SHEET    2  KA 6 CYS K 373  PHE K 380 -1  O  ALA K 379   N  VAL K 389           
SHEET    3  KA 6 LYS K 461  SER K 470  1  O  ILE K 464   N  ASP K 374           
SHEET    4  KA 6 ARG K 445  ARG K 458 -1  O  GLU K 450   N  SER K 470           
SHEET    5  KA 6 SER K 426  TYR K 437 -1  O  ALA K 427   N  TRP K 455           
SHEET    6  KA 6 HIS K 411  LEU K 421 -1  O  HIS K 411   N  GLN K 436           
SHEET    1  LA 6 VAL L 389  GLU L 390  0                                        
SHEET    2  LA 6 CYS L 373  PHE L 380 -1  O  ALA L 379   N  VAL L 389           
SHEET    3  LA 6 TRP L 462  SER L 470  1  O  ILE L 464   N  ASP L 374           
SHEET    4  LA 6 ARG L 445  ARG L 457 -1  O  GLU L 450   N  SER L 470           
SHEET    5  LA 6 SER L 426  TYR L 437 -1  O  ALA L 427   N  TRP L 455           
SHEET    6  LA 6 HIS L 411  LEU L 421 -1  O  HIS L 411   N  GLN L 436           
SHEET    1  MA 6 VAL M 389  GLU M 390  0                                        
SHEET    2  MA 6 CYS M 373  PHE M 380 -1  O  ALA M 379   N  VAL M 389           
SHEET    3  MA 6 LYS M 461  GLY M 471  1  O  ILE M 464   N  ASP M 374           
SHEET    4  MA 6 ARG M 445  ARG M 458 -1  O  GLU M 450   N  SER M 470           
SHEET    5  MA 6 SER M 426  TYR M 437 -1  O  ALA M 427   N  TRP M 455           
SHEET    6  MA 6 HIS M 411  MET M 422 -1  O  HIS M 411   N  GLN M 436           
SHEET    1  NA 6 VAL N 389  GLU N 390  0                                        
SHEET    2  NA 6 CYS N 373  PHE N 380 -1  O  ALA N 379   N  VAL N 389           
SHEET    3  NA 6 LYS N 461  SER N 470  1  O  ILE N 464   N  ASP N 374           
SHEET    4  NA 6 ARG N 445  ARG N 458 -1  O  GLU N 450   N  SER N 470           
SHEET    5  NA 6 SER N 426  TYR N 437 -1  O  ALA N 427   N  TRP N 455           
SHEET    6  NA 6 HIS N 411  LEU N 421 -1  O  HIS N 411   N  GLN N 436           
SITE     1 AC1  4 ILE A 361  TYR A 369  ARG A 453  PHE A 467                    
SITE     1 AC2  4 ILE B 361  TYR B 369  ARG B 453  PHE B 467                    
SITE     1 AC3  4 ILE C 361  TYR C 369  ARG C 453  PHE C 467                    
SITE     1 AC4  4 ILE D 361  TYR D 369  ARG D 453  PHE D 467                    
SITE     1 AC5  4 ILE E 361  TYR E 369  ARG E 453  PHE E 467                    
SITE     1 AC6  3 ILE F 361  TYR F 369  PHE F 467                               
SITE     1 AC7  4 ILE G 361  TYR G 369  ARG G 453  PHE G 467                    
SITE     1 AC8  5 ILE H 361  TYR H 369  ARG H 453  PHE H 467                    
SITE     2 AC8  5 ARG H 469                                                     
SITE     1 AC9  5 ILE I 361  PHE I 467  ARG I 469  VAL I 475                    
SITE     2 AC9  5 HOH I2002                                                     
SITE     1 BC1  4 ILE J 361  TYR J 369  ARG J 453  PHE J 467                    
SITE     1 BC2  3 TYR K 369  ARG K 453  PHE K 467                               
SITE     1 BC3  3 ILE L 361  ARG L 453  PHE L 467                               
SITE     1 BC4  4 ILE M 361  TYR M 369  ARG M 453  PHE M 467                    
SITE     1 BC5  5 ILE N 361  TYR N 369  ARG N 453  PHE N 467                    
SITE     2 BC5  5 VAL N 475                                                     
SITE     1 BC6  7 GLU A 339  ASP A 342  ARG A 346  ASP A 424                    
SITE     2 BC6  7 TBR A2000  HIS G 456  ARG G 458                               
SITE     1 BC7 11 THR A 343  ARG A 346  LEU A 421  GLY A 423                    
SITE     2 BC7 11 DTT A1475  HIS B 456  HIS G 456  THR H 343                    
SITE     3 BC7 11 ARG H 346  LEU H 421  GLY H 423                               
CRYST1  147.946  118.043  157.820  90.00 110.91  90.00 C 1 2 1      56          
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      0.006759  0.000000  0.002582        0.00000                         
SCALE2      0.000000  0.008471  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006783        0.00000                         
ATOM      1  N   MET A 335       4.803  -8.900  43.071  1.00115.72           N  
ATOM      2  CA  MET A 335       3.416  -9.163  42.598  1.00115.33           C  
ATOM      3  C   MET A 335       3.101  -8.304  41.379  1.00114.69           C  
ATOM      4  O   MET A 335       2.575  -8.790  40.379  1.00114.53           O  
ATOM      5  CB  MET A 335       2.410  -8.844  43.709  1.00115.98           C  
ATOM      6  CG  MET A 335       0.994  -9.337  43.430  1.00116.93           C  
ATOM      7  SD  MET A 335       0.712 -11.074  43.902  1.00117.41           S  
ATOM      8  CE  MET A 335       1.461 -11.953  42.557  1.00117.33           C  
ATOM      9  N   THR A 336       3.433  -7.021  41.473  1.00114.15           N  
ATOM     10  CA  THR A 336       3.177  -6.071  40.395  1.00113.04           C  
ATOM     11  C   THR A 336       4.444  -5.636  39.652  1.00111.92           C  
ATOM     12  O   THR A 336       4.466  -4.572  39.033  1.00111.37           O  
ATOM     13  CB  THR A 336       2.471  -4.804  40.935  1.00113.03           C  
ATOM     14  OG1 THR A 336       3.379  -4.061  41.756  1.00112.66           O  
ATOM     15  CG2 THR A 336       1.254  -5.186  41.768  1.00112.85           C  
ATOM     16  N   THR A 337       5.491  -6.457  39.711  1.00110.56           N  
ATOM     17  CA  THR A 337       6.746  -6.140  39.031  1.00109.42           C  
ATOM     18  C   THR A 337       6.494  -5.895  37.540  1.00108.09           C  
ATOM     19  O   THR A 337       6.646  -4.773  37.054  1.00107.51           O  
ATOM     20  CB  THR A 337       7.792  -7.274  39.231  1.00109.82           C  
ATOM     21  OG1 THR A 337       8.849  -7.131  38.272  1.00109.62           O  
ATOM     22  CG2 THR A 337       7.142  -8.645  39.098  1.00109.85           C  
ATOM     23  N   ILE A 338       6.114  -6.939  36.810  1.00106.71           N  
ATOM     24  CA  ILE A 338       5.803  -6.769  35.396  1.00105.25           C  
ATOM     25  C   ILE A 338       4.579  -5.874  35.464  1.00104.60           C  
ATOM     26  O   ILE A 338       3.965  -5.754  36.523  1.00105.44           O  
ATOM     27  CB  ILE A 338       5.351  -8.086  34.721  1.00104.81           C  
ATOM     28  CG1 ILE A 338       6.252  -9.249  35.135  1.00105.14           C  
ATOM     29  CG2 ILE A 338       5.352  -7.921  33.221  1.00103.89           C  
ATOM     30  CD1 ILE A 338       5.851  -9.903  36.451  1.00104.84           C  
ATOM     31  N   GLU A 339       4.207  -5.244  34.363  1.00103.41           N  
ATOM     32  CA  GLU A 339       3.009  -4.411  34.393  1.00102.76           C  
ATOM     33  C   GLU A 339       3.118  -3.413  35.540  1.00100.20           C  
ATOM     34  O   GLU A 339       2.457  -3.555  36.567  1.00100.40           O  
ATOM     35  CB  GLU A 339       1.769  -5.293  34.604  1.00104.96           C  
ATOM     36  CG  GLU A 339       1.860  -6.670  33.945  1.00107.80           C  
ATOM     37  CD  GLU A 339       0.506  -7.339  33.786  1.00109.21           C  
ATOM     38  OE1 GLU A 339      -0.390  -6.732  33.151  1.00108.47           O  
ATOM     39  OE2 GLU A 339       0.344  -8.473  34.291  1.00110.39           O  
ATOM     40  N   ASP A 340       3.952  -2.405  35.337  1.00 96.94           N  
ATOM     41  CA  ASP A 340       4.232  -1.359  36.313  1.00 94.07           C  
ATOM     42  C   ASP A 340       5.580  -0.891  35.838  1.00 91.99           C  
ATOM     43  O   ASP A 340       5.920   0.291  35.849  1.00 91.31           O  
ATOM     44  CB  ASP A 340       4.387  -1.932  37.717  1.00 94.13           C  
ATOM     45  CG  ASP A 340       5.191  -1.025  38.622  1.00 93.82           C  
ATOM     46  OD1 ASP A 340       4.810   0.150  38.779  1.00 94.37           O  
ATOM     47  OD2 ASP A 340       6.210  -1.480  39.173  1.00 93.58           O  
ATOM     48  N   GLU A 341       6.354  -1.876  35.427  1.00 90.04           N  
ATOM     49  CA  GLU A 341       7.656  -1.625  34.893  1.00 88.46           C  
ATOM     50  C   GLU A 341       7.340  -1.116  33.496  1.00 88.57           C  
ATOM     51  O   GLU A 341       8.149  -0.438  32.868  1.00 88.82           O  
ATOM     52  CB  GLU A 341       8.443  -2.935  34.833  1.00 86.75           C  
ATOM     53  CG  GLU A 341       9.909  -2.769  34.510  1.00 84.57           C  
ATOM     54  CD  GLU A 341      10.127  -2.230  33.118  1.00 83.08           C  
ATOM     55  OE1 GLU A 341       9.522  -2.803  32.190  1.00 82.76           O  
ATOM     56  OE2 GLU A 341      10.893  -1.248  32.949  1.00 80.62           O  
ATOM     57  N   ASP A 342       6.135  -1.401  33.015  1.00 89.32           N  
ATOM     58  CA  ASP A 342       5.821  -0.960  31.672  1.00 88.55           C  
ATOM     59  C   ASP A 342       5.122   0.387  31.692  1.00 87.22           C  
ATOM     60  O   ASP A 342       5.190   1.142  30.730  1.00 86.67           O  
ATOM     61  CB  ASP A 342       4.980  -2.005  30.935  1.00 89.73           C  
ATOM     62  CG  ASP A 342       3.517  -1.921  31.275  1.00 89.54           C  
ATOM     63  OD1 ASP A 342       3.174  -2.071  32.461  1.00 90.98           O  
ATOM     64  OD2 ASP A 342       2.707  -1.704  30.355  1.00 87.38           O  
ATOM     65  N   THR A 343       4.451   0.691  32.794  1.00 85.50           N  
ATOM     66  CA  THR A 343       3.783   1.974  32.921  1.00 83.97           C  
ATOM     67  C   THR A 343       4.899   2.998  32.990  1.00 82.58           C  
ATOM     68  O   THR A 343       4.743   4.148  32.590  1.00 82.17           O  
ATOM     69  CB  THR A 343       2.958   2.059  34.206  1.00 83.96           C  
ATOM     70  OG1 THR A 343       3.831   2.065  35.334  1.00 85.11           O  
ATOM     71  CG2 THR A 343       2.029   0.879  34.307  1.00 83.93           C  
ATOM     72  N   LYS A 344       6.037   2.551  33.502  1.00 81.10           N  
ATOM     73  CA  LYS A 344       7.214   3.386  33.624  1.00 79.67           C  
ATOM     74  C   LYS A 344       7.709   3.738  32.227  1.00 77.19           C  
ATOM     75  O   LYS A 344       8.014   4.893  31.946  1.00 77.58           O  
ATOM     76  CB  LYS A 344       8.305   2.632  34.395  1.00 82.13           C  
ATOM     77  CG  LYS A 344       9.558   3.441  34.719  1.00 84.11           C  
ATOM     78  CD  LYS A 344       9.269   4.538  35.737  1.00 87.28           C  
ATOM     79  CE  LYS A 344      10.532   5.307  36.109  1.00 88.29           C  
ATOM     80  NZ  LYS A 344      11.152   5.968  34.923  1.00 89.14           N  
ATOM     81  N   VAL A 345       7.781   2.745  31.348  1.00 73.96           N  
ATOM     82  CA  VAL A 345       8.252   2.989  29.992  1.00 71.83           C  
ATOM     83  C   VAL A 345       7.193   3.663  29.128  1.00 69.46           C  
ATOM     84  O   VAL A 345       7.515   4.394  28.197  1.00 68.71           O  
ATOM     85  CB  VAL A 345       8.731   1.679  29.295  1.00 72.03           C  
ATOM     86  CG1 VAL A 345       9.882   1.068  30.074  1.00 72.23           C  
ATOM     87  CG2 VAL A 345       7.596   0.698  29.166  1.00 72.98           C  
ATOM     88  N   ARG A 346       5.926   3.416  29.433  1.00 67.85           N  
ATOM     89  CA  ARG A 346       4.840   4.031  28.681  1.00 65.58           C  
ATOM     90  C   ARG A 346       4.846   5.530  28.945  1.00 63.93           C  
ATOM     91  O   ARG A 346       4.614   6.326  28.041  1.00 63.28           O  
ATOM     92  CB  ARG A 346       3.494   3.448  29.097  1.00 66.91           C  
ATOM     93  CG  ARG A 346       3.207   2.079  28.532  1.00 68.33           C  
ATOM     94  CD  ARG A 346       1.891   1.530  29.061  1.00 69.63           C  
ATOM     95  NE  ARG A 346       1.557   0.259  28.429  1.00 72.39           N  
ATOM     96  CZ  ARG A 346       1.212   0.129  27.153  1.00 72.69           C  
ATOM     97  NH1 ARG A 346       1.149   1.192  26.370  1.00 73.22           N  
ATOM     98  NH2 ARG A 346       0.944  -1.067  26.655  1.00 73.28           N  
ATOM     99  N   LYS A 347       5.107   5.907  30.193  1.00 61.10           N  
ATOM    100  CA  LYS A 347       5.165   7.308  30.559  1.00 58.56           C  
ATOM    101  C   LYS A 347       6.372   7.979  29.928  1.00 58.90           C  
ATOM    102  O   LYS A 347       6.298   9.134  29.510  1.00 59.52           O  
ATOM    103  CB  LYS A 347       5.220   7.466  32.072  1.00 55.90           C  
ATOM    104  CG  LYS A 347       3.909   7.150  32.737  1.00 54.20           C  
ATOM    105  CD  LYS A 347       3.884   7.586  34.179  1.00 52.08           C  
ATOM    106  CE  LYS A 347       2.502   7.402  34.753  1.00 50.14           C  
ATOM    107  NZ  LYS A 347       2.433   7.833  36.160  1.00 49.47           N  
ATOM    108  N   GLN A 348       7.489   7.265  29.861  1.00 58.96           N  
ATOM    109  CA  GLN A 348       8.679   7.832  29.251  1.00 59.88           C  
ATOM    110  C   GLN A 348       8.394   8.024  27.771  1.00 59.14           C  
ATOM    111  O   GLN A 348       8.915   8.937  27.140  1.00 59.52           O  
ATOM    112  CB  GLN A 348       9.889   6.913  29.441  1.00 61.35           C  
ATOM    113  CG  GLN A 348      11.164   7.462  28.800  1.00 64.25           C  
ATOM    114  CD  GLN A 348      11.585   8.815  29.373  1.00 66.35           C  
ATOM    115  OE1 GLN A 348      12.211   9.634  28.680  1.00 65.67           O  
ATOM    116  NE2 GLN A 348      11.254   9.051  30.645  1.00 66.43           N  
ATOM    117  N   GLU A 349       7.557   7.146  27.229  1.00 59.20           N  
ATOM    118  CA  GLU A 349       7.153   7.198  25.831  1.00 58.45           C  
ATOM    119  C   GLU A 349       6.438   8.538  25.614  1.00 57.00           C  
ATOM    120  O   GLU A 349       6.749   9.284  24.690  1.00 57.10           O  
ATOM    121  CB  GLU A 349       6.216   6.018  25.551  1.00 61.59           C  
ATOM    122  CG  GLU A 349       5.291   6.162  24.349  1.00 65.62           C  
ATOM    123  CD  GLU A 349       5.928   5.739  23.047  1.00 67.45           C  
ATOM    124  OE1 GLU A 349       6.915   6.379  22.622  1.00 68.29           O  
ATOM    125  OE2 GLU A 349       5.430   4.756  22.452  1.00 69.61           O  
ATOM    126  N   ILE A 350       5.491   8.843  26.491  1.00 54.84           N  
ATOM    127  CA  ILE A 350       4.751  10.091  26.402  1.00 53.91           C  
ATOM    128  C   ILE A 350       5.663  11.304  26.597  1.00 52.93           C  
ATOM    129  O   ILE A 350       5.511  12.312  25.915  1.00 52.52           O  
ATOM    130  CB  ILE A 350       3.581  10.121  27.427  1.00 52.17           C  
ATOM    131  CG1 ILE A 350       2.314   9.537  26.800  1.00 52.39           C  
ATOM    132  CG2 ILE A 350       3.262  11.547  27.824  1.00 52.86           C  
ATOM    133  CD1 ILE A 350       2.500   8.254  26.059  1.00 54.32           C  
ATOM    134  N   ILE A 351       6.609  11.214  27.523  1.00 52.83           N  
ATOM    135  CA  ILE A 351       7.522  12.327  27.753  1.00 52.58           C  
ATOM    136  C   ILE A 351       8.375  12.579  26.520  1.00 53.40           C  
ATOM    137  O   ILE A 351       8.694  13.726  26.206  1.00 53.69           O  
ATOM    138  CB  ILE A 351       8.443  12.079  28.968  1.00 51.93           C  
ATOM    139  CG1 ILE A 351       7.624  12.187  30.254  1.00 52.60           C  
ATOM    140  CG2 ILE A 351       9.588  13.086  28.986  1.00 48.50           C  
ATOM    141  CD1 ILE A 351       8.439  12.057  31.527  1.00 53.74           C  
ATOM    142  N   LYS A 352       8.725  11.515  25.805  1.00 53.61           N  
ATOM    143  CA  LYS A 352       9.547  11.657  24.609  1.00 54.65           C  
ATOM    144  C   LYS A 352       8.819  12.373  23.471  1.00 52.66           C  
ATOM    145  O   LYS A 352       9.389  13.247  22.826  1.00 51.95           O  
ATOM    146  CB  LYS A 352      10.050  10.283  24.141  1.00 56.91           C  
ATOM    147  CG  LYS A 352      10.874  10.333  22.870  1.00 61.40           C  
ATOM    148  CD  LYS A 352      11.805   9.133  22.730  1.00 66.19           C  
ATOM    149  CE  LYS A 352      12.958   9.190  23.757  1.00 69.99           C  
ATOM    150  NZ  LYS A 352      13.911   8.033  23.658  1.00 69.77           N  
ATOM    151  N   VAL A 353       7.563  12.011  23.228  1.00 51.62           N  
ATOM    152  CA  VAL A 353       6.803  12.651  22.163  1.00 50.18           C  
ATOM    153  C   VAL A 353       6.524  14.102  22.508  1.00 48.82           C  
ATOM    154  O   VAL A 353       6.490  14.959  21.627  1.00 48.68           O  
ATOM    155  CB  VAL A 353       5.471  11.914  21.870  1.00 50.12           C  
ATOM    156  CG1 VAL A 353       5.768  10.556  21.267  1.00 48.74           C  
ATOM    157  CG2 VAL A 353       4.644  11.772  23.137  1.00 49.67           C  
ATOM    158  N   THR A 354       6.330  14.380  23.792  1.00 47.87           N  
ATOM    159  CA  THR A 354       6.087  15.747  24.231  1.00 46.69           C  
ATOM    160  C   THR A 354       7.344  16.576  23.972  1.00 46.96           C  
ATOM    161  O   THR A 354       7.268  17.711  23.501  1.00 45.86           O  
ATOM    162  CB  THR A 354       5.731  15.793  25.709  1.00 45.75           C  
ATOM    163  OG1 THR A 354       4.574  14.984  25.935  1.00 46.60           O  
ATOM    164  CG2 THR A 354       5.421  17.223  26.141  1.00 44.66           C  
ATOM    165  N   GLU A 355       8.502  15.994  24.268  1.00 47.87           N  
ATOM    166  CA  GLU A 355       9.781  16.661  24.031  1.00 49.09           C  
ATOM    167  C   GLU A 355       9.961  16.887  22.542  1.00 49.00           C  
ATOM    168  O   GLU A 355      10.427  17.939  22.111  1.00 48.74           O  
ATOM    169  CB  GLU A 355      10.935  15.809  24.548  1.00 49.82           C  
ATOM    170  CG  GLU A 355      11.371  16.146  25.955  1.00 53.65           C  
ATOM    171  CD  GLU A 355      12.074  14.987  26.639  1.00 56.44           C  
ATOM    172  OE1 GLU A 355      12.693  14.162  25.930  1.00 56.56           O  
ATOM    173  OE2 GLU A 355      12.012  14.910  27.888  1.00 58.60           O  
ATOM    174  N   GLN A 356       9.590  15.886  21.755  1.00 49.46           N  
ATOM    175  CA  GLN A 356       9.705  15.985  20.309  1.00 50.61           C  
ATOM    176  C   GLN A 356       8.797  17.094  19.789  1.00 50.28           C  
ATOM    177  O   GLN A 356       9.199  17.893  18.942  1.00 50.10           O  
ATOM    178  CB  GLN A 356       9.335  14.650  19.670  1.00 52.86           C  
ATOM    179  CG  GLN A 356      10.429  13.603  19.770  1.00 56.20           C  
ATOM    180  CD  GLN A 356       9.950  12.224  19.365  1.00 59.63           C  
ATOM    181  OE1 GLN A 356       9.223  12.064  18.378  1.00 63.01           O  
ATOM    182  NE2 GLN A 356      10.358  11.217  20.117  1.00 60.37           N  
ATOM    183  N   LEU A 357       7.576  17.142  20.311  1.00 49.70           N  
ATOM    184  CA  LEU A 357       6.610  18.156  19.920  1.00 48.86           C  
ATOM    185  C   LEU A 357       7.175  19.544  20.218  1.00 50.22           C  
ATOM    186  O   LEU A 357       7.160  20.441  19.370  1.00 49.43           O  
ATOM    187  CB  LEU A 357       5.315  17.969  20.699  1.00 48.31           C  
ATOM    188  CG  LEU A 357       4.234  19.000  20.378  1.00 47.29           C  
ATOM    189  CD1 LEU A 357       3.515  18.610  19.100  1.00 47.56           C  
ATOM    190  CD2 LEU A 357       3.264  19.084  21.542  1.00 46.02           C  
ATOM    191  N   ILE A 358       7.673  19.720  21.435  1.00 50.65           N  
ATOM    192  CA  ILE A 358       8.231  21.000  21.828  1.00 51.85           C  
ATOM    193  C   ILE A 358       9.418  21.393  20.949  1.00 53.87           C  
ATOM    194  O   ILE A 358       9.583  22.570  20.613  1.00 53.62           O  
ATOM    195  CB  ILE A 358       8.650  20.987  23.311  1.00 51.16           C  
ATOM    196  CG1 ILE A 358       7.398  20.894  24.187  1.00 51.25           C  
ATOM    197  CG2 ILE A 358       9.454  22.231  23.639  1.00 48.66           C  
ATOM    198  CD1 ILE A 358       7.679  20.823  25.670  1.00 53.15           C  
ATOM    199  N   GLU A 359      10.239  20.421  20.565  1.00 55.31           N  
ATOM    200  CA  GLU A 359      11.390  20.718  19.716  1.00 58.29           C  
ATOM    201  C   GLU A 359      10.935  21.204  18.349  1.00 58.24           C  
ATOM    202  O   GLU A 359      11.494  22.156  17.801  1.00 56.73           O  
ATOM    203  CB  GLU A 359      12.271  19.485  19.546  1.00 61.87           C  
ATOM    204  CG  GLU A 359      13.052  19.111  20.797  1.00 69.04           C  
ATOM    205  CD  GLU A 359      13.936  17.881  20.591  1.00 72.61           C  
ATOM    206  OE1 GLU A 359      14.755  17.901  19.636  1.00 74.95           O  
ATOM    207  OE2 GLU A 359      13.814  16.906  21.380  1.00 71.92           O  
ATOM    208  N   ALA A 360       9.920  20.541  17.801  1.00 58.05           N  
ATOM    209  CA  ALA A 360       9.388  20.924  16.505  1.00 57.81           C  
ATOM    210  C   ALA A 360       8.872  22.353  16.608  1.00 58.35           C  
ATOM    211  O   ALA A 360       9.158  23.180  15.744  1.00 59.22           O  
ATOM    212  CB  ALA A 360       8.270  19.984  16.101  1.00 57.13           C  
ATOM    213  N   ILE A 361       8.118  22.643  17.668  1.00 58.39           N  
ATOM    214  CA  ILE A 361       7.584  23.983  17.873  1.00 59.44           C  
ATOM    215  C   ILE A 361       8.740  24.964  17.975  1.00 61.42           C  
ATOM    216  O   ILE A 361       8.773  25.990  17.298  1.00 62.23           O  
ATOM    217  CB  ILE A 361       6.778  24.086  19.181  1.00 58.01           C  
ATOM    218  CG1 ILE A 361       5.522  23.224  19.096  1.00 56.60           C  
ATOM    219  CG2 ILE A 361       6.422  25.537  19.453  1.00 56.62           C  
ATOM    220  CD1 ILE A 361       4.782  23.111  20.398  1.00 54.32           C  
ATOM    221  N   SER A 362       9.697  24.628  18.828  1.00 63.29           N  
ATOM    222  CA  SER A 362      10.856  25.475  19.057  1.00 65.08           C  
ATOM    223  C   SER A 362      11.696  25.740  17.810  1.00 65.30           C  
ATOM    224  O   SER A 362      12.351  26.774  17.711  1.00 66.03           O  
ATOM    225  CB  SER A 362      11.723  24.855  20.151  1.00 65.48           C  
ATOM    226  OG  SER A 362      12.712  25.762  20.585  1.00 68.07           O  
ATOM    227  N   ASN A 363      11.685  24.816  16.859  1.00 66.35           N  
ATOM    228  CA  ASN A 363      12.467  25.002  15.641  1.00 67.85           C  
ATOM    229  C   ASN A 363      11.629  25.508  14.480  1.00 68.46           C  
ATOM    230  O   ASN A 363      12.104  25.565  13.350  1.00 69.29           O  
ATOM    231  CB  ASN A 363      13.148  23.697  15.226  1.00 68.60           C  
ATOM    232  CG  ASN A 363      14.144  23.200  16.256  1.00 70.29           C  
ATOM    233  OD1 ASN A 363      14.739  23.987  16.992  1.00 70.94           O  
ATOM    234  ND2 ASN A 363      14.346  21.887  16.299  1.00 71.05           N  
ATOM    235  N   GLY A 364      10.381  25.870  14.757  1.00 69.34           N  
ATOM    236  CA  GLY A 364       9.500  26.362  13.710  1.00 69.66           C  
ATOM    237  C   GLY A 364       9.248  25.346  12.607  1.00 69.72           C  
ATOM    238  O   GLY A 364       8.938  25.712  11.473  1.00 70.28           O  
ATOM    239  N   ASP A 365       9.377  24.065  12.938  1.00 68.68           N  
ATOM    240  CA  ASP A 365       9.168  22.996  11.969  1.00 67.82           C  
ATOM    241  C   ASP A 365       7.699  22.580  11.926  1.00 67.55           C  
ATOM    242  O   ASP A 365       7.304  21.599  12.553  1.00 67.26           O  
ATOM    243  CB  ASP A 365      10.041  21.806  12.346  1.00 68.13           C  
ATOM    244  CG  ASP A 365       9.915  20.661  11.378  1.00 68.20           C  
ATOM    245  OD1 ASP A 365      10.638  19.665  11.559  1.00 69.93           O  
ATOM    246  OD2 ASP A 365       9.099  20.747  10.443  1.00 69.53           O  
ATOM    247  N   PHE A 366       6.900  23.322  11.166  1.00 67.18           N  
ATOM    248  CA  PHE A 366       5.470  23.056  11.058  1.00 68.02           C  
ATOM    249  C   PHE A 366       5.095  21.687  10.483  1.00 68.40           C  
ATOM    250  O   PHE A 366       4.054  21.129  10.832  1.00 67.74           O  
ATOM    251  CB  PHE A 366       4.802  24.152  10.230  1.00 68.39           C  
ATOM    252  CG  PHE A 366       3.301  24.127  10.294  1.00 68.93           C  
ATOM    253  CD1 PHE A 366       2.638  24.377  11.493  1.00 68.84           C  
ATOM    254  CD2 PHE A 366       2.547  23.875   9.152  1.00 69.05           C  
ATOM    255  CE1 PHE A 366       1.243  24.380  11.554  1.00 69.84           C  
ATOM    256  CE2 PHE A 366       1.155  23.876   9.202  1.00 69.99           C  
ATOM    257  CZ  PHE A 366       0.499  24.130  10.408  1.00 69.65           C  
ATOM    258  N   GLU A 367       5.926  21.151   9.597  1.00 69.00           N  
ATOM    259  CA  GLU A 367       5.642  19.848   9.005  1.00 70.63           C  
ATOM    260  C   GLU A 367       5.627  18.761  10.067  1.00 69.63           C  
ATOM    261  O   GLU A 367       4.680  17.982  10.152  1.00 69.43           O  
ATOM    262  CB  GLU A 367       6.676  19.489   7.934  1.00 74.21           C  
ATOM    263  CG  GLU A 367       6.413  20.106   6.560  1.00 78.55           C  
ATOM    264  CD  GLU A 367       6.726  21.598   6.499  1.00 81.90           C  
ATOM    265  OE1 GLU A 367       6.438  22.221   5.452  1.00 82.80           O  
ATOM    266  OE2 GLU A 367       7.266  22.147   7.489  1.00 83.98           O  
ATOM    267  N   SER A 368       6.684  18.703  10.870  1.00 68.06           N  
ATOM    268  CA  SER A 368       6.765  17.714  11.937  1.00 66.19           C  
ATOM    269  C   SER A 368       5.618  17.932  12.917  1.00 65.29           C  
ATOM    270  O   SER A 368       5.024  16.978  13.429  1.00 65.28           O  
ATOM    271  CB  SER A 368       8.090  17.849  12.673  1.00 65.97           C  
ATOM    272  OG  SER A 368       9.165  17.652  11.781  1.00 67.85           O  
ATOM    273  N   TYR A 369       5.311  19.199  13.173  1.00 63.53           N  
ATOM    274  CA  TYR A 369       4.239  19.552  14.088  1.00 62.07           C  
ATOM    275  C   TYR A 369       2.912  18.940  13.647  1.00 62.74           C  
ATOM    276  O   TYR A 369       2.285  18.203  14.409  1.00 62.71           O  
ATOM    277  CB  TYR A 369       4.098  21.070  14.170  1.00 60.39           C  
ATOM    278  CG  TYR A 369       3.102  21.527  15.209  1.00 59.58           C  
ATOM    279  CD1 TYR A 369       3.340  21.319  16.568  1.00 59.54           C  
ATOM    280  CD2 TYR A 369       1.914  22.151  14.839  1.00 57.96           C  
ATOM    281  CE1 TYR A 369       2.421  21.719  17.528  1.00 58.08           C  
ATOM    282  CE2 TYR A 369       0.990  22.553  15.791  1.00 57.19           C  
ATOM    283  CZ  TYR A 369       1.249  22.334  17.131  1.00 57.70           C  
ATOM    284  OH  TYR A 369       0.327  22.728  18.072  1.00 59.09           O  
ATOM    285  N   THR A 370       2.491  19.242  12.418  1.00 62.38           N  
ATOM    286  CA  THR A 370       1.228  18.724  11.899  1.00 63.25           C  
ATOM    287  C   THR A 370       1.207  17.204  11.929  1.00 63.34           C  
ATOM    288  O   THR A 370       0.169  16.585  12.161  1.00 64.55           O  
ATOM    289  CB  THR A 370       0.973  19.178  10.450  1.00 63.77           C  
ATOM    290  OG1 THR A 370       1.966  18.612   9.593  1.00 65.94           O  
ATOM    291  CG2 THR A 370       1.026  20.692  10.343  1.00 63.85           C  
ATOM    292  N   LYS A 371       2.367  16.613  11.690  1.00 62.81           N  
ATOM    293  CA  LYS A 371       2.519  15.170  11.695  1.00 62.19           C  
ATOM    294  C   LYS A 371       2.145  14.638  13.083  1.00 60.67           C  
ATOM    295  O   LYS A 371       1.614  13.536  13.218  1.00 61.00           O  
ATOM    296  CB  LYS A 371       3.977  14.830  11.360  1.00 64.73           C  
ATOM    297  CG  LYS A 371       4.191  13.768  10.286  1.00 68.12           C  
ATOM    298  CD  LYS A 371       4.037  12.354  10.864  1.00 71.47           C  
ATOM    299  CE  LYS A 371       4.509  11.283   9.880  1.00 72.53           C  
ATOM    300  NZ  LYS A 371       4.509   9.920  10.487  1.00 72.77           N  
ATOM    301  N   MET A 372       2.399  15.445  14.109  1.00 58.40           N  
ATOM    302  CA  MET A 372       2.119  15.052  15.485  1.00 56.19           C  
ATOM    303  C   MET A 372       0.758  15.471  16.016  1.00 55.25           C  
ATOM    304  O   MET A 372       0.389  15.112  17.136  1.00 55.35           O  
ATOM    305  CB  MET A 372       3.197  15.608  16.407  1.00 56.77           C  
ATOM    306  CG  MET A 372       4.597  15.141  16.077  1.00 57.59           C  
ATOM    307  SD  MET A 372       5.828  15.828  17.183  1.00 60.33           S  
ATOM    308  CE  MET A 372       6.662  16.925  16.118  1.00 57.47           C  
ATOM    309  N   CYS A 373       0.007  16.226  15.226  1.00 53.59           N  
ATOM    310  CA  CYS A 373      -1.308  16.676  15.669  1.00 53.09           C  
ATOM    311  C   CYS A 373      -2.456  16.031  14.906  1.00 52.74           C  
ATOM    312  O   CYS A 373      -2.364  15.796  13.701  1.00 53.42           O  
ATOM    313  CB  CYS A 373      -1.435  18.191  15.517  1.00 53.65           C  
ATOM    314  SG  CYS A 373      -0.234  19.179  16.400  1.00 54.39           S  
ATOM    315  N   ASP A 374      -3.542  15.752  15.616  1.00 52.09           N  
ATOM    316  CA  ASP A 374      -4.730  15.183  14.996  1.00 51.43           C  
ATOM    317  C   ASP A 374      -5.373  16.332  14.221  1.00 51.84           C  
ATOM    318  O   ASP A 374      -5.398  17.470  14.687  1.00 51.02           O  
ATOM    319  CB  ASP A 374      -5.686  14.670  16.069  1.00 50.73           C  
ATOM    320  CG  ASP A 374      -6.988  14.165  15.493  1.00 52.44           C  
ATOM    321  OD1 ASP A 374      -7.392  13.032  15.842  1.00 52.48           O  
ATOM    322  OD2 ASP A 374      -7.613  14.902  14.700  1.00 51.06           O  
ATOM    323  N   PRO A 375      -5.895  16.057  13.020  1.00 52.47           N  
ATOM    324  CA  PRO A 375      -6.523  17.117  12.216  1.00 51.75           C  
ATOM    325  C   PRO A 375      -7.600  17.908  12.961  1.00 51.67           C  
ATOM    326  O   PRO A 375      -7.756  19.116  12.750  1.00 51.38           O  
ATOM    327  CB  PRO A 375      -7.088  16.352  11.027  1.00 51.24           C  
ATOM    328  CG  PRO A 375      -6.104  15.219  10.878  1.00 51.92           C  
ATOM    329  CD  PRO A 375      -5.912  14.770  12.301  1.00 51.43           C  
ATOM    330  N   GLY A 376      -8.340  17.217  13.826  1.00 50.89           N  
ATOM    331  CA  GLY A 376      -9.395  17.861  14.589  1.00 49.79           C  
ATOM    332  C   GLY A 376      -8.911  18.320  15.951  1.00 49.74           C  
ATOM    333  O   GLY A 376      -9.676  18.377  16.919  1.00 49.93           O  
ATOM    334  N   MET A 377      -7.626  18.651  16.018  1.00 48.67           N  
ATOM    335  CA  MET A 377      -7.008  19.115  17.251  1.00 48.33           C  
ATOM    336  C   MET A 377      -7.675  20.377  17.782  1.00 46.60           C  
ATOM    337  O   MET A 377      -7.984  21.301  17.041  1.00 46.94           O  
ATOM    338  CB  MET A 377      -5.525  19.386  17.021  1.00 49.55           C  
ATOM    339  CG  MET A 377      -4.794  19.872  18.247  1.00 50.89           C  
ATOM    340  SD  MET A 377      -3.330  20.762  17.747  1.00 55.21           S  
ATOM    341  CE  MET A 377      -2.158  20.131  18.863  1.00 55.73           C  
ATOM    342  N   THR A 378      -7.871  20.404  19.088  1.00 44.95           N  
ATOM    343  CA  THR A 378      -8.505  21.519  19.760  1.00 42.44           C  
ATOM    344  C   THR A 378      -7.480  22.212  20.689  1.00 40.70           C  
ATOM    345  O   THR A 378      -6.556  21.566  21.181  1.00 41.24           O  
ATOM    346  CB  THR A 378      -9.733  20.960  20.511  1.00 42.66           C  
ATOM    347  OG1 THR A 378     -10.917  21.408  19.850  1.00 44.22           O  
ATOM    348  CG2 THR A 378      -9.757  21.370  21.953  1.00 43.50           C  
ATOM    349  N   ALA A 379      -7.619  23.518  20.915  1.00 37.74           N  
ATOM    350  CA  ALA A 379      -6.664  24.218  21.777  1.00 36.33           C  
ATOM    351  C   ALA A 379      -7.130  25.484  22.499  1.00 36.84           C  
ATOM    352  O   ALA A 379      -7.962  26.249  22.013  1.00 37.35           O  
ATOM    353  CB  ALA A 379      -5.387  24.545  20.983  1.00 33.45           C  
ATOM    354  N   PHE A 380      -6.556  25.679  23.679  1.00 36.65           N  
ATOM    355  CA  PHE A 380      -6.779  26.847  24.526  1.00 33.74           C  
ATOM    356  C   PHE A 380      -5.375  27.410  24.742  1.00 34.17           C  
ATOM    357  O   PHE A 380      -4.472  26.694  25.163  1.00 32.64           O  
ATOM    358  CB  PHE A 380      -7.349  26.428  25.868  1.00 31.48           C  
ATOM    359  CG  PHE A 380      -8.839  26.417  25.927  1.00 31.07           C  
ATOM    360  CD1 PHE A 380      -9.502  25.448  26.673  1.00 32.34           C  
ATOM    361  CD2 PHE A 380      -9.591  27.391  25.281  1.00 31.18           C  
ATOM    362  CE1 PHE A 380     -10.897  25.448  26.778  1.00 31.81           C  
ATOM    363  CE2 PHE A 380     -10.985  27.402  25.379  1.00 28.41           C  
ATOM    364  CZ  PHE A 380     -11.637  26.431  26.127  1.00 30.14           C  
ATOM    365  N   GLU A 381      -5.177  28.676  24.424  1.00 36.25           N  
ATOM    366  CA  GLU A 381      -3.867  29.290  24.601  1.00 39.03           C  
ATOM    367  C   GLU A 381      -3.990  30.815  24.579  1.00 40.02           C  
ATOM    368  O   GLU A 381      -4.899  31.372  23.966  1.00 39.16           O  
ATOM    369  CB  GLU A 381      -2.898  28.819  23.508  1.00 39.72           C  
ATOM    370  CG  GLU A 381      -3.244  29.306  22.115  1.00 43.22           C  
ATOM    371  CD  GLU A 381      -2.263  28.822  21.076  1.00 46.92           C  
ATOM    372  OE1 GLU A 381      -2.322  29.296  19.936  1.00 51.15           O  
ATOM    373  OE2 GLU A 381      -1.421  27.964  21.385  1.00 52.13           O  
ATOM    374  N   PRO A 382      -3.072  31.509  25.263  1.00 40.41           N  
ATOM    375  CA  PRO A 382      -3.093  32.971  25.318  1.00 39.51           C  
ATOM    376  C   PRO A 382      -3.287  33.645  23.966  1.00 39.16           C  
ATOM    377  O   PRO A 382      -4.019  34.619  23.854  1.00 38.45           O  
ATOM    378  CB  PRO A 382      -1.744  33.306  25.944  1.00 39.56           C  
ATOM    379  CG  PRO A 382      -1.518  32.158  26.866  1.00 40.00           C  
ATOM    380  CD  PRO A 382      -1.923  30.972  26.019  1.00 40.08           C  
ATOM    381  N   GLU A 383      -2.635  33.124  22.938  1.00 40.06           N  
ATOM    382  CA  GLU A 383      -2.737  33.719  21.611  1.00 41.74           C  
ATOM    383  C   GLU A 383      -4.150  33.647  21.021  1.00 41.64           C  
ATOM    384  O   GLU A 383      -4.464  34.374  20.084  1.00 42.55           O  
ATOM    385  CB  GLU A 383      -1.737  33.058  20.647  1.00 43.14           C  
ATOM    386  CG  GLU A 383      -0.282  33.154  21.084  1.00 47.60           C  
ATOM    387  CD  GLU A 383       0.174  31.964  21.910  1.00 51.64           C  
ATOM    388  OE1 GLU A 383      -0.507  31.594  22.894  1.00 53.43           O  
ATOM    389  OE2 GLU A 383       1.227  31.393  21.574  1.00 55.46           O  
ATOM    390  N   ALA A 384      -4.997  32.775  21.568  1.00 40.23           N  
ATOM    391  CA  ALA A 384      -6.362  32.610  21.080  1.00 37.30           C  
ATOM    392  C   ALA A 384      -7.389  33.470  21.826  1.00 37.16           C  
ATOM    393  O   ALA A 384      -8.599  33.314  21.650  1.00 35.21           O  
ATOM    394  CB  ALA A 384      -6.754  31.143  21.144  1.00 37.27           C  
ATOM    395  N   LEU A 385      -6.895  34.360  22.677  1.00 37.56           N  
ATOM    396  CA  LEU A 385      -7.736  35.291  23.424  1.00 37.78           C  
ATOM    397  C   LEU A 385      -8.981  34.734  24.098  1.00 38.54           C  
ATOM    398  O   LEU A 385     -10.063  35.313  23.981  1.00 40.58           O  
ATOM    399  CB  LEU A 385      -8.155  36.427  22.492  1.00 38.18           C  
ATOM    400  CG  LEU A 385      -6.995  37.110  21.762  1.00 39.88           C  
ATOM    401  CD1 LEU A 385      -7.533  38.066  20.720  1.00 38.96           C  
ATOM    402  CD2 LEU A 385      -6.116  37.845  22.776  1.00 37.62           C  
ATOM    403  N   GLY A 386      -8.845  33.625  24.807  1.00 38.96           N  
ATOM    404  CA  GLY A 386      -9.999  33.065  25.482  1.00 38.07           C  
ATOM    405  C   GLY A 386     -10.920  32.226  24.620  1.00 38.19           C  
ATOM    406  O   GLY A 386     -11.946  31.760  25.111  1.00 39.46           O  
ATOM    407  N   ASN A 387     -10.572  32.030  23.352  1.00 37.22           N  
ATOM    408  CA  ASN A 387     -11.390  31.213  22.454  1.00 37.93           C  
ATOM    409  C   ASN A 387     -10.809  29.812  22.266  1.00 39.58           C  
ATOM    410  O   ASN A 387      -9.591  29.623  22.291  1.00 40.99           O  
ATOM    411  CB  ASN A 387     -11.497  31.879  21.077  1.00 36.83           C  
ATOM    412  CG  ASN A 387     -12.181  33.232  21.133  1.00 37.20           C  
ATOM    413  OD1 ASN A 387     -13.376  33.328  21.439  1.00 33.19           O  
ATOM    414  ND2 ASN A 387     -11.423  34.291  20.843  1.00 34.66           N  
ATOM    415  N   LEU A 388     -11.683  28.828  22.084  1.00 40.96           N  
ATOM    416  CA  LEU A 388     -11.246  27.463  21.829  1.00 42.52           C  
ATOM    417  C   LEU A 388     -11.015  27.386  20.324  1.00 43.50           C  
ATOM    418  O   LEU A 388     -11.940  27.585  19.547  1.00 44.28           O  
ATOM    419  CB  LEU A 388     -12.329  26.469  22.230  1.00 42.80           C  
ATOM    420  CG  LEU A 388     -11.824  25.049  22.517  1.00 47.02           C  
ATOM    421  CD1 LEU A 388     -13.005  24.134  22.762  1.00 48.78           C  
ATOM    422  CD2 LEU A 388     -11.006  24.523  21.350  1.00 47.73           C  
ATOM    423  N   VAL A 389      -9.781  27.117  19.915  1.00 45.08           N  
ATOM    424  CA  VAL A 389      -9.438  27.040  18.501  1.00 47.67           C  
ATOM    425  C   VAL A 389      -9.377  25.598  17.969  1.00 50.08           C  
ATOM    426  O   VAL A 389      -9.007  24.679  18.705  1.00 49.26           O  
ATOM    427  CB  VAL A 389      -8.093  27.739  18.262  1.00 46.25           C  
ATOM    428  CG1 VAL A 389      -7.623  27.516  16.852  1.00 49.21           C  
ATOM    429  CG2 VAL A 389      -8.250  29.209  18.498  1.00 48.45           C  
ATOM    430  N   GLU A 390      -9.753  25.405  16.698  1.00 52.92           N  
ATOM    431  CA  GLU A 390      -9.729  24.072  16.062  1.00 54.62           C  
ATOM    432  C   GLU A 390      -8.770  24.000  14.896  1.00 54.28           C  
ATOM    433  O   GLU A 390      -8.523  25.000  14.227  1.00 56.07           O  
ATOM    434  CB  GLU A 390     -11.094  23.675  15.515  1.00 55.99           C  
ATOM    435  CG  GLU A 390     -12.127  23.296  16.534  1.00 62.01           C  
ATOM    436  CD  GLU A 390     -13.296  22.559  15.891  1.00 65.76           C  
ATOM    437  OE1 GLU A 390     -13.090  21.404  15.433  1.00 65.20           O  
ATOM    438  OE2 GLU A 390     -14.411  23.140  15.835  1.00 67.69           O  
ATOM    439  N   GLY A 391      -8.254  22.804  14.641  1.00 53.73           N  
ATOM    440  CA  GLY A 391      -7.337  22.610  13.533  1.00 53.83           C  
ATOM    441  C   GLY A 391      -5.956  23.190  13.748  1.00 54.83           C  
ATOM    442  O   GLY A 391      -5.693  23.836  14.764  1.00 56.41           O  
ATOM    443  N   LEU A 392      -5.067  22.965  12.787  1.00 54.62           N  
ATOM    444  CA  LEU A 392      -3.705  23.466  12.883  1.00 55.59           C  
ATOM    445  C   LEU A 392      -3.552  24.785  12.158  1.00 56.11           C  
ATOM    446  O   LEU A 392      -2.541  25.465  12.280  1.00 56.40           O  
ATOM    447  CB  LEU A 392      -2.730  22.458  12.284  1.00 55.90           C  
ATOM    448  CG  LEU A 392      -2.685  21.097  12.966  1.00 56.19           C  
ATOM    449  CD1 LEU A 392      -3.871  20.273  12.563  1.00 56.53           C  
ATOM    450  CD2 LEU A 392      -1.418  20.400  12.569  1.00 58.07           C  
ATOM    451  N   ASP A 393      -4.574  25.141  11.401  1.00 57.77           N  
ATOM    452  CA  ASP A 393      -4.564  26.361  10.620  1.00 58.72           C  
ATOM    453  C   ASP A 393      -4.190  27.597  11.434  1.00 57.34           C  
ATOM    454  O   ASP A 393      -3.404  28.430  10.985  1.00 57.00           O  
ATOM    455  CB  ASP A 393      -5.936  26.533   9.977  1.00 63.06           C  
ATOM    456  CG  ASP A 393      -5.993  27.709   9.042  1.00 67.77           C  
ATOM    457  OD1 ASP A 393      -5.222  27.709   8.049  1.00 69.15           O  
ATOM    458  OD2 ASP A 393      -6.815  28.623   9.309  1.00 70.13           O  
ATOM    459  N   PHE A 394      -4.744  27.703  12.639  1.00 56.40           N  
ATOM    460  CA  PHE A 394      -4.487  28.841  13.518  1.00 53.25           C  
ATOM    461  C   PHE A 394      -3.047  28.912  14.008  1.00 52.87           C  
ATOM    462  O   PHE A 394      -2.514  29.993  14.259  1.00 53.57           O  
ATOM    463  CB  PHE A 394      -5.438  28.785  14.715  1.00 51.61           C  
ATOM    464  CG  PHE A 394      -5.266  29.921  15.688  1.00 49.68           C  
ATOM    465  CD1 PHE A 394      -4.427  29.785  16.797  1.00 48.85           C  
ATOM    466  CD2 PHE A 394      -5.938  31.123  15.495  1.00 45.96           C  
ATOM    467  CE1 PHE A 394      -4.265  30.835  17.698  1.00 48.53           C  
ATOM    468  CE2 PHE A 394      -5.788  32.173  16.379  1.00 46.29           C  
ATOM    469  CZ  PHE A 394      -4.952  32.038  17.488  1.00 48.57           C  
ATOM    470  N   HIS A 395      -2.413  27.758  14.131  1.00 51.40           N  
ATOM    471  CA  HIS A 395      -1.045  27.702  14.610  1.00 52.44           C  
ATOM    472  C   HIS A 395       0.015  27.968  13.537  1.00 54.48           C  
ATOM    473  O   HIS A 395       1.099  28.471  13.841  1.00 54.68           O  
ATOM    474  CB  HIS A 395      -0.815  26.346  15.268  1.00 49.44           C  
ATOM    475  CG  HIS A 395      -1.845  26.011  16.301  1.00 48.15           C  
ATOM    476  ND1 HIS A 395      -1.874  26.602  17.547  1.00 47.11           N  
ATOM    477  CD2 HIS A 395      -2.919  25.187  16.252  1.00 46.93           C  
ATOM    478  CE1 HIS A 395      -2.921  26.158  18.219  1.00 46.36           C  
ATOM    479  NE2 HIS A 395      -3.571  25.298  17.456  1.00 46.17           N  
ATOM    480  N   ARG A 396      -0.284  27.633  12.287  1.00 56.51           N  
ATOM    481  CA  ARG A 396       0.674  27.856  11.210  1.00 58.33           C  
ATOM    482  C   ARG A 396       1.218  29.285  11.222  1.00 59.03           C  
ATOM    483  O   ARG A 396       2.386  29.517  10.919  1.00 59.80           O  
ATOM    484  CB  ARG A 396       0.029  27.573   9.853  1.00 59.18           C  
ATOM    485  CG  ARG A 396       0.860  28.045   8.670  1.00 60.89           C  
ATOM    486  CD  ARG A 396       0.104  27.859   7.369  1.00 63.57           C  
ATOM    487  NE  ARG A 396       0.327  26.544   6.778  1.00 65.41           N  
ATOM    488  CZ  ARG A 396       1.469  26.173   6.201  1.00 66.74           C  
ATOM    489  NH1 ARG A 396       2.494  27.017   6.138  1.00 66.70           N  
ATOM    490  NH2 ARG A 396       1.586  24.959   5.679  1.00 66.77           N  
ATOM    491  N   PHE A 397       0.374  30.241  11.583  1.00 59.23           N  
ATOM    492  CA  PHE A 397       0.787  31.635  11.607  1.00 59.95           C  
ATOM    493  C   PHE A 397       2.065  31.894  12.400  1.00 61.45           C  
ATOM    494  O   PHE A 397       2.982  32.552  11.913  1.00 60.63           O  
ATOM    495  CB  PHE A 397      -0.331  32.502  12.177  1.00 59.95           C  
ATOM    496  CG  PHE A 397      -0.006  33.958  12.189  1.00 59.92           C  
ATOM    497  CD1 PHE A 397       0.098  34.668  10.994  1.00 60.50           C  
ATOM    498  CD2 PHE A 397       0.219  34.621  13.388  1.00 60.26           C  
ATOM    499  CE1 PHE A 397       0.425  36.024  10.986  1.00 61.14           C  
ATOM    500  CE2 PHE A 397       0.548  35.980  13.398  1.00 62.87           C  
ATOM    501  CZ  PHE A 397       0.652  36.686  12.187  1.00 62.25           C  
ATOM    502  N   TYR A 398       2.113  31.384  13.628  1.00 63.45           N  
ATOM    503  CA  TYR A 398       3.266  31.577  14.496  1.00 65.60           C  
ATOM    504  C   TYR A 398       4.492  30.803  14.046  1.00 66.91           C  
ATOM    505  O   TYR A 398       5.619  31.162  14.374  1.00 66.24           O  
ATOM    506  CB  TYR A 398       2.905  31.203  15.927  1.00 66.03           C  
ATOM    507  CG  TYR A 398       1.741  32.005  16.450  1.00 66.38           C  
ATOM    508  CD1 TYR A 398       0.443  31.492  16.416  1.00 66.77           C  
ATOM    509  CD2 TYR A 398       1.930  33.295  16.942  1.00 65.79           C  
ATOM    510  CE1 TYR A 398      -0.640  32.248  16.861  1.00 67.08           C  
ATOM    511  CE2 TYR A 398       0.858  34.060  17.386  1.00 66.24           C  
ATOM    512  CZ  TYR A 398      -0.423  33.531  17.343  1.00 66.64           C  
ATOM    513  OH  TYR A 398      -1.482  34.288  17.777  1.00 66.58           O  
ATOM    514  N   PHE A 399       4.274  29.732  13.299  1.00 69.25           N  
ATOM    515  CA  PHE A 399       5.390  28.962  12.787  1.00 71.94           C  
ATOM    516  C   PHE A 399       6.050  29.753  11.677  1.00 74.68           C  
ATOM    517  O   PHE A 399       7.237  30.060  11.737  1.00 75.02           O  
ATOM    518  CB  PHE A 399       4.918  27.619  12.234  1.00 69.77           C  
ATOM    519  CG  PHE A 399       4.802  26.562  13.269  1.00 67.97           C  
ATOM    520  CD1 PHE A 399       3.804  26.624  14.231  1.00 67.50           C  
ATOM    521  CD2 PHE A 399       5.713  25.516  13.308  1.00 67.97           C  
ATOM    522  CE1 PHE A 399       3.715  25.655  15.223  1.00 67.35           C  
ATOM    523  CE2 PHE A 399       5.635  24.539  14.295  1.00 67.35           C  
ATOM    524  CZ  PHE A 399       4.633  24.609  15.256  1.00 67.73           C  
ATOM    525  N   GLU A 400       5.260  30.093  10.667  1.00 78.05           N  
ATOM    526  CA  GLU A 400       5.760  30.828   9.523  1.00 81.93           C  
ATOM    527  C   GLU A 400       6.282  32.229   9.863  1.00 83.29           C  
ATOM    528  O   GLU A 400       7.136  32.758   9.156  1.00 83.70           O  
ATOM    529  CB  GLU A 400       4.665  30.918   8.460  1.00 83.56           C  
ATOM    530  CG  GLU A 400       5.184  31.001   7.028  1.00 87.21           C  
ATOM    531  CD  GLU A 400       4.062  31.161   6.008  1.00 89.31           C  
ATOM    532  OE1 GLU A 400       3.112  30.340   6.035  1.00 90.25           O  
ATOM    533  OE2 GLU A 400       4.131  32.105   5.182  1.00 89.12           O  
ATOM    534  N   ASN A 401       5.794  32.829  10.942  1.00 85.11           N  
ATOM    535  CA  ASN A 401       6.251  34.168  11.290  1.00 88.02           C  
ATOM    536  C   ASN A 401       7.162  34.232  12.496  1.00 90.48           C  
ATOM    537  O   ASN A 401       7.078  35.150  13.312  1.00 90.51           O  
ATOM    538  CB  ASN A 401       5.059  35.095  11.487  1.00 87.70           C  
ATOM    539  CG  ASN A 401       4.217  35.207  10.241  1.00 87.83           C  
ATOM    540  OD1 ASN A 401       3.378  34.350   9.966  1.00 88.31           O  
ATOM    541  ND2 ASN A 401       4.455  36.250   9.462  1.00 87.62           N  
ATOM    542  N   LEU A 402       8.044  33.247  12.586  1.00 93.90           N  
ATOM    543  CA  LEU A 402       9.015  33.148  13.664  1.00 97.18           C  
ATOM    544  C   LEU A 402      10.177  32.307  13.152  1.00 99.64           C  
ATOM    545  O   LEU A 402      10.379  31.166  13.577  1.00 99.12           O  
ATOM    546  CB  LEU A 402       8.386  32.498  14.897  1.00 97.36           C  
ATOM    547  CG  LEU A 402       7.373  33.319  15.701  1.00 97.85           C  
ATOM    548  CD1 LEU A 402       6.824  32.474  16.844  1.00 97.56           C  
ATOM    549  CD2 LEU A 402       8.042  34.579  16.236  1.00 97.29           C  
ATOM    550  N   TRP A 403      10.918  32.892  12.212  1.00102.99           N  
ATOM    551  CA  TRP A 403      12.077  32.259  11.588  1.00106.25           C  
ATOM    552  C   TRP A 403      13.372  32.781  12.197  1.00107.48           C  
ATOM    553  O   TRP A 403      14.297  32.013  12.465  1.00107.61           O  
ATOM    554  CB  TRP A 403      12.080  32.536  10.080  1.00108.02           C  
ATOM    555  CG  TRP A 403      11.054  31.760   9.302  1.00110.10           C  
ATOM    556  CD1 TRP A 403      10.571  32.060   8.054  1.00110.57           C  
ATOM    557  CD2 TRP A 403      10.405  30.541   9.701  1.00110.81           C  
ATOM    558  NE1 TRP A 403       9.663  31.105   7.655  1.00111.50           N  
ATOM    559  CE2 TRP A 403       9.542  30.162   8.645  1.00111.67           C  
ATOM    560  CE3 TRP A 403      10.469  29.731  10.846  1.00109.92           C  
ATOM    561  CZ2 TRP A 403       8.748  29.007   8.703  1.00111.38           C  
ATOM    562  CZ3 TRP A 403       9.683  28.588  10.901  1.00109.83           C  
ATOM    563  CH2 TRP A 403       8.833  28.237   9.836  1.00110.46           C  
ATOM    564  N   SER A 404      13.434  34.092  12.405  1.00108.65           N  
ATOM    565  CA  SER A 404      14.612  34.718  12.991  1.00109.75           C  
ATOM    566  C   SER A 404      15.050  33.943  14.239  1.00110.45           C  
ATOM    567  O   SER A 404      16.228  33.944  14.601  1.00110.47           O  
ATOM    568  CB  SER A 404      14.295  36.170  13.356  1.00110.02           C  
ATOM    569  OG  SER A 404      13.753  36.861  12.243  1.00110.41           O  
ATOM    570  N   ARG A 405      14.092  33.282  14.887  1.00110.86           N  
ATOM    571  CA  ARG A 405      14.373  32.495  16.081  1.00111.02           C  
ATOM    572  C   ARG A 405      15.438  31.456  15.764  1.00111.21           C  
ATOM    573  O   ARG A 405      16.143  30.992  16.660  1.00111.42           O  
ATOM    574  CB  ARG A 405      13.120  31.764  16.565  1.00111.41           C  
ATOM    575  CG  ARG A 405      11.921  32.635  16.868  1.00111.54           C  
ATOM    576  CD  ARG A 405      10.711  31.754  17.174  1.00111.80           C  
ATOM    577  NE  ARG A 405      10.446  30.808  16.089  1.00111.28           N  
ATOM    578  CZ  ARG A 405       9.439  29.940  16.069  1.00110.95           C  
ATOM    579  NH1 ARG A 405       8.579  29.881  17.080  1.00110.56           N  
ATOM    580  NH2 ARG A 405       9.287  29.136  15.028  1.00110.29           N  
ATOM    581  N   ASN A 406      15.539  31.076  14.491  1.00111.17           N  
ATOM    582  CA  ASN A 406      16.529  30.085  14.074  1.00111.53           C  
ATOM    583  C   ASN A 406      17.848  30.437  14.741  1.00110.88           C  
ATOM    584  O   ASN A 406      18.430  29.626  15.473  1.00111.09           O  
ATOM    585  CB  ASN A 406      16.693  30.082  12.545  1.00112.25           C  
ATOM    586  CG  ASN A 406      15.804  29.046  11.856  1.00113.24           C  
ATOM    587  OD1 ASN A 406      14.584  29.031  12.040  1.00113.76           O  
ATOM    588  ND2 ASN A 406      16.417  28.179  11.055  1.00112.79           N  
ATOM    589  N   SER A 407      18.301  31.662  14.492  1.00109.69           N  
ATOM    590  CA  SER A 407      19.538  32.157  15.077  1.00107.81           C  
ATOM    591  C   SER A 407      19.310  32.345  16.575  1.00105.61           C  
ATOM    592  O   SER A 407      20.182  32.040  17.387  1.00106.01           O  
ATOM    593  CB  SER A 407      19.936  33.490  14.429  1.00108.77           C  
ATOM    594  OG  SER A 407      18.895  34.450  14.532  1.00109.36           O  
ATOM    595  N   LYS A 408      18.128  32.842  16.931  1.00102.48           N  
ATOM    596  CA  LYS A 408      17.786  33.058  18.330  1.00 99.28           C  
ATOM    597  C   LYS A 408      17.927  31.743  19.099  1.00 95.61           C  
ATOM    598  O   LYS A 408      17.167  30.796  18.880  1.00 95.37           O  
ATOM    599  CB  LYS A 408      16.343  33.576  18.464  1.00101.12           C  
ATOM    600  CG  LYS A 408      15.921  33.865  19.908  1.00103.29           C  
ATOM    601  CD  LYS A 408      14.419  33.667  20.157  1.00104.62           C  
ATOM    602  CE  LYS A 408      13.547  34.750  19.522  1.00105.33           C  
ATOM    603  NZ  LYS A 408      12.101  34.595  19.908  1.00104.99           N  
ATOM    604  N   PRO A 409      18.923  31.658  19.993  1.00 91.84           N  
ATOM    605  CA  PRO A 409      19.119  30.434  20.775  1.00 88.09           C  
ATOM    606  C   PRO A 409      17.930  30.230  21.713  1.00 83.88           C  
ATOM    607  O   PRO A 409      17.489  31.172  22.377  1.00 82.81           O  
ATOM    608  CB  PRO A 409      20.413  30.716  21.536  1.00 89.05           C  
ATOM    609  CG  PRO A 409      21.149  31.653  20.622  1.00 89.82           C  
ATOM    610  CD  PRO A 409      20.055  32.584  20.178  1.00 91.16           C  
ATOM    611  N   VAL A 410      17.406  29.009  21.761  1.00 79.60           N  
ATOM    612  CA  VAL A 410      16.269  28.724  22.627  1.00 75.95           C  
ATOM    613  C   VAL A 410      16.445  27.442  23.418  1.00 72.98           C  
ATOM    614  O   VAL A 410      16.671  26.379  22.845  1.00 72.88           O  
ATOM    615  CB  VAL A 410      14.958  28.574  21.831  1.00 76.45           C  
ATOM    616  CG1 VAL A 410      13.785  28.471  22.793  1.00 75.86           C  
ATOM    617  CG2 VAL A 410      14.774  29.741  20.883  1.00 77.50           C  
ATOM    618  N   HIS A 411      16.351  27.538  24.738  1.00 69.84           N  
ATOM    619  CA  HIS A 411      16.450  26.342  25.561  1.00 65.57           C  
ATOM    620  C   HIS A 411      15.138  26.143  26.302  1.00 63.12           C  
ATOM    621  O   HIS A 411      14.600  27.080  26.900  1.00 63.81           O  
ATOM    622  CB  HIS A 411      17.586  26.433  26.570  1.00 65.03           C  
ATOM    623  CG  HIS A 411      17.767  25.178  27.364  1.00 64.85           C  
ATOM    624  ND1 HIS A 411      18.070  23.969  26.778  1.00 64.69           N  
ATOM    625  CD2 HIS A 411      17.651  24.934  28.691  1.00 64.80           C  
ATOM    626  CE1 HIS A 411      18.132  23.033  27.709  1.00 63.36           C  
ATOM    627  NE2 HIS A 411      17.881  23.592  28.878  1.00 63.33           N  
ATOM    628  N   THR A 412      14.620  24.923  26.253  1.00 58.95           N  
ATOM    629  CA  THR A 412      13.363  24.618  26.909  1.00 55.10           C  
ATOM    630  C   THR A 412      13.537  23.586  28.000  1.00 53.66           C  
ATOM    631  O   THR A 412      14.316  22.657  27.870  1.00 53.64           O  
ATOM    632  CB  THR A 412      12.318  24.110  25.905  1.00 54.57           C  
ATOM    633  OG1 THR A 412      11.949  25.173  25.018  1.00 53.64           O  
ATOM    634  CG2 THR A 412      11.081  23.621  26.625  1.00 54.08           C  
ATOM    635  N   THR A 413      12.800  23.765  29.084  1.00 52.09           N  
ATOM    636  CA  THR A 413      12.860  22.862  30.215  1.00 49.35           C  
ATOM    637  C   THR A 413      11.441  22.469  30.558  1.00 49.04           C  
ATOM    638  O   THR A 413      10.549  23.307  30.596  1.00 49.87           O  
ATOM    639  CB  THR A 413      13.485  23.545  31.454  1.00 48.40           C  
ATOM    640  OG1 THR A 413      14.813  23.987  31.148  1.00 48.21           O  
ATOM    641  CG2 THR A 413      13.526  22.588  32.622  1.00 45.15           C  
ATOM    642  N   ILE A 414      11.237  21.186  30.799  1.00 48.46           N  
ATOM    643  CA  ILE A 414       9.931  20.669  31.157  1.00 47.07           C  
ATOM    644  C   ILE A 414      10.027  20.349  32.634  1.00 46.73           C  
ATOM    645  O   ILE A 414      10.775  19.462  33.027  1.00 48.46           O  
ATOM    646  CB  ILE A 414       9.619  19.381  30.365  1.00 46.61           C  
ATOM    647  CG1 ILE A 414       9.535  19.704  28.878  1.00 45.71           C  
ATOM    648  CG2 ILE A 414       8.327  18.744  30.880  1.00 45.24           C  
ATOM    649  CD1 ILE A 414       9.294  18.492  28.013  1.00 47.29           C  
ATOM    650  N   LEU A 415       9.280  21.065  33.457  1.00 46.60           N  
ATOM    651  CA  LEU A 415       9.340  20.838  34.896  1.00 46.40           C  
ATOM    652  C   LEU A 415       8.142  20.158  35.508  1.00 45.06           C  
ATOM    653  O   LEU A 415       7.017  20.342  35.077  1.00 45.28           O  
ATOM    654  CB  LEU A 415       9.530  22.151  35.650  1.00 46.81           C  
ATOM    655  CG  LEU A 415      10.772  22.987  35.408  1.00 49.06           C  
ATOM    656  CD1 LEU A 415      10.717  24.172  36.348  1.00 50.70           C  
ATOM    657  CD2 LEU A 415      12.027  22.171  35.655  1.00 50.99           C  
ATOM    658  N   ASN A 416       8.416  19.384  36.546  1.00 44.72           N  
ATOM    659  CA  ASN A 416       7.403  18.692  37.311  1.00 43.45           C  
ATOM    660  C   ASN A 416       6.345  17.990  36.450  1.00 43.07           C  
ATOM    661  O   ASN A 416       5.152  18.135  36.687  1.00 42.98           O  
ATOM    662  CB  ASN A 416       6.779  19.713  38.269  1.00 43.07           C  
ATOM    663  CG  ASN A 416       5.940  19.077  39.345  1.00 45.64           C  
ATOM    664  OD1 ASN A 416       6.229  17.971  39.805  1.00 48.11           O  
ATOM    665  ND2 ASN A 416       4.899  19.786  39.780  1.00 47.01           N  
ATOM    666  N   PRO A 417       6.779  17.195  35.454  1.00 42.25           N  
ATOM    667  CA  PRO A 417       5.865  16.474  34.567  1.00 42.21           C  
ATOM    668  C   PRO A 417       4.972  15.494  35.318  1.00 42.56           C  
ATOM    669  O   PRO A 417       5.379  14.912  36.323  1.00 44.11           O  
ATOM    670  CB  PRO A 417       6.812  15.728  33.632  1.00 42.13           C  
ATOM    671  CG  PRO A 417       8.034  16.547  33.644  1.00 41.75           C  
ATOM    672  CD  PRO A 417       8.171  16.918  35.072  1.00 41.49           C  
ATOM    673  N   HIS A 418       3.757  15.317  34.822  1.00 41.17           N  
ATOM    674  CA  HIS A 418       2.820  14.369  35.404  1.00 42.18           C  
ATOM    675  C   HIS A 418       2.033  13.719  34.269  1.00 42.84           C  
ATOM    676  O   HIS A 418       1.351  14.402  33.494  1.00 42.67           O  
ATOM    677  CB  HIS A 418       1.873  15.060  36.373  1.00 41.75           C  
ATOM    678  CG  HIS A 418       2.487  15.362  37.703  1.00 43.44           C  
ATOM    679  ND1 HIS A 418       2.095  14.729  38.861  1.00 42.81           N  
ATOM    680  CD2 HIS A 418       3.444  16.252  38.065  1.00 43.44           C  
ATOM    681  CE1 HIS A 418       2.781  15.218  39.879  1.00 42.24           C  
ATOM    682  NE2 HIS A 418       3.605  16.142  39.423  1.00 42.74           N  
ATOM    683  N   ILE A 419       2.156  12.404  34.148  1.00 41.86           N  
ATOM    684  CA  ILE A 419       1.449  11.697  33.106  1.00 42.90           C  
ATOM    685  C   ILE A 419       0.324  10.886  33.692  1.00 43.22           C  
ATOM    686  O   ILE A 419       0.433  10.359  34.784  1.00 43.07           O  
ATOM    687  CB  ILE A 419       2.369  10.729  32.316  1.00 44.34           C  
ATOM    688  CG1 ILE A 419       3.449  11.504  31.552  1.00 43.00           C  
ATOM    689  CG2 ILE A 419       1.545   9.921  31.330  1.00 42.97           C  
ATOM    690  CD1 ILE A 419       4.560  12.013  32.414  1.00 43.83           C  
ATOM    691  N   HIS A 420      -0.771  10.821  32.951  1.00 44.16           N  
ATOM    692  CA  HIS A 420      -1.937  10.043  33.334  1.00 45.07           C  
ATOM    693  C   HIS A 420      -2.174   9.097  32.169  1.00 46.61           C  
ATOM    694  O   HIS A 420      -2.412   9.539  31.046  1.00 46.19           O  
ATOM    695  CB  HIS A 420      -3.154  10.940  33.502  1.00 44.58           C  
ATOM    696  CG  HIS A 420      -3.088  11.835  34.695  1.00 44.09           C  
ATOM    697  ND1 HIS A 420      -3.359  11.394  35.971  1.00 42.67           N  
ATOM    698  CD2 HIS A 420      -2.808  13.156  34.802  1.00 44.68           C  
ATOM    699  CE1 HIS A 420      -3.255  12.407  36.813  1.00 43.57           C  
ATOM    700  NE2 HIS A 420      -2.923  13.487  36.130  1.00 43.43           N  
ATOM    701  N   LEU A 421      -2.078   7.798  32.420  1.00 48.62           N  
ATOM    702  CA  LEU A 421      -2.299   6.828  31.362  1.00 50.19           C  
ATOM    703  C   LEU A 421      -3.777   6.438  31.400  1.00 52.43           C  
ATOM    704  O   LEU A 421      -4.354   6.261  32.472  1.00 52.39           O  
ATOM    705  CB  LEU A 421      -1.400   5.614  31.572  1.00 48.94           C  
ATOM    706  CG  LEU A 421       0.094   5.939  31.567  1.00 49.70           C  
ATOM    707  CD1 LEU A 421       0.897   4.711  31.973  1.00 49.93           C  
ATOM    708  CD2 LEU A 421       0.509   6.415  30.185  1.00 47.65           C  
ATOM    709  N   MET A 422      -4.392   6.340  30.224  1.00 54.65           N  
ATOM    710  CA  MET A 422      -5.800   5.984  30.112  1.00 57.89           C  
ATOM    711  C   MET A 422      -5.943   5.036  28.931  1.00 60.51           C  
ATOM    712  O   MET A 422      -6.169   5.464  27.810  1.00 63.41           O  
ATOM    713  CB  MET A 422      -6.607   7.249  29.868  1.00 58.09           C  
ATOM    714  CG  MET A 422      -6.204   8.373  30.798  1.00 58.24           C  
ATOM    715  SD  MET A 422      -6.522   9.994  30.140  1.00 59.99           S  
ATOM    716  CE  MET A 422      -5.191  10.247  29.108  1.00 54.09           C  
ATOM    717  N   GLY A 423      -5.822   3.744  29.180  1.00 62.61           N  
ATOM    718  CA  GLY A 423      -5.897   2.793  28.090  1.00 63.57           C  
ATOM    719  C   GLY A 423      -4.537   2.783  27.419  1.00 63.70           C  
ATOM    720  O   GLY A 423      -3.657   3.552  27.786  1.00 61.14           O  
ATOM    721  N   ASP A 424      -4.361   1.921  26.428  1.00 65.94           N  
ATOM    722  CA  ASP A 424      -3.083   1.823  25.739  1.00 66.65           C  
ATOM    723  C   ASP A 424      -2.951   2.825  24.614  1.00 66.36           C  
ATOM    724  O   ASP A 424      -1.863   3.011  24.081  1.00 66.29           O  
ATOM    725  CB  ASP A 424      -2.884   0.409  25.166  1.00 69.83           C  
ATOM    726  CG  ASP A 424      -2.728  -0.648  26.244  1.00 72.52           C  
ATOM    727  OD1 ASP A 424      -1.825  -0.494  27.092  1.00 72.91           O  
ATOM    728  OD2 ASP A 424      -3.508  -1.629  26.240  1.00 75.20           O  
ATOM    729  N   GLU A 425      -4.048   3.480  24.253  1.00 66.35           N  
ATOM    730  CA  GLU A 425      -4.014   4.437  23.150  1.00 65.19           C  
ATOM    731  C   GLU A 425      -4.277   5.874  23.598  1.00 63.01           C  
ATOM    732  O   GLU A 425      -4.375   6.778  22.761  1.00 62.69           O  
ATOM    733  CB  GLU A 425      -5.065   4.042  22.101  1.00 68.72           C  
ATOM    734  CG  GLU A 425      -5.190   2.537  21.860  1.00 72.68           C  
ATOM    735  CD  GLU A 425      -3.910   1.923  21.331  1.00 74.51           C  
ATOM    736  OE1 GLU A 425      -3.470   2.298  20.221  1.00 76.20           O  
ATOM    737  OE2 GLU A 425      -3.343   1.062  22.031  1.00 76.02           O  
ATOM    738  N   SER A 426      -4.375   6.089  24.906  1.00 58.80           N  
ATOM    739  CA  SER A 426      -4.690   7.417  25.421  1.00 56.61           C  
ATOM    740  C   SER A 426      -3.879   7.885  26.632  1.00 54.40           C  
ATOM    741  O   SER A 426      -3.851   7.230  27.673  1.00 54.22           O  
ATOM    742  CB  SER A 426      -6.192   7.471  25.725  1.00 55.60           C  
ATOM    743  OG  SER A 426      -6.482   8.300  26.826  1.00 57.28           O  
ATOM    744  N   ALA A 427      -3.229   9.035  26.489  1.00 50.59           N  
ATOM    745  CA  ALA A 427      -2.422   9.586  27.567  1.00 49.38           C  
ATOM    746  C   ALA A 427      -2.623  11.091  27.747  1.00 48.63           C  
ATOM    747  O   ALA A 427      -3.067  11.804  26.839  1.00 48.24           O  
ATOM    748  CB  ALA A 427      -0.945   9.287  27.330  1.00 50.64           C  
ATOM    749  N   CYS A 428      -2.286  11.568  28.937  1.00 45.79           N  
ATOM    750  CA  CYS A 428      -2.422  12.977  29.275  1.00 42.70           C  
ATOM    751  C   CYS A 428      -1.218  13.458  30.066  1.00 39.88           C  
ATOM    752  O   CYS A 428      -0.902  12.900  31.116  1.00 40.10           O  
ATOM    753  CB  CYS A 428      -3.665  13.182  30.121  1.00 44.86           C  
ATOM    754  SG  CYS A 428      -3.901  14.872  30.570  1.00 51.98           S  
ATOM    755  N   ILE A 429      -0.548  14.492  29.578  1.00 36.01           N  
ATOM    756  CA  ILE A 429       0.609  15.005  30.286  1.00 35.03           C  
ATOM    757  C   ILE A 429       0.477  16.487  30.618  1.00 35.83           C  
ATOM    758  O   ILE A 429       0.052  17.295  29.786  1.00 35.74           O  
ATOM    759  CB  ILE A 429       1.899  14.774  29.474  1.00 35.22           C  
ATOM    760  CG1 ILE A 429       3.115  15.165  30.309  1.00 34.48           C  
ATOM    761  CG2 ILE A 429       1.855  15.570  28.176  1.00 34.90           C  
ATOM    762  CD1 ILE A 429       4.415  14.931  29.619  1.00 34.56           C  
ATOM    763  N   ALA A 430       0.841  16.836  31.846  1.00 35.04           N  
ATOM    764  CA  ALA A 430       0.776  18.222  32.309  1.00 35.42           C  
ATOM    765  C   ALA A 430       2.134  18.615  32.863  1.00 35.31           C  
ATOM    766  O   ALA A 430       2.716  17.883  33.648  1.00 36.77           O  
ATOM    767  CB  ALA A 430      -0.294  18.363  33.401  1.00 34.65           C  
ATOM    768  N   TYR A 431       2.638  19.773  32.472  1.00 34.82           N  
ATOM    769  CA  TYR A 431       3.943  20.204  32.955  1.00 34.75           C  
ATOM    770  C   TYR A 431       4.112  21.718  32.894  1.00 35.76           C  
ATOM    771  O   TYR A 431       3.304  22.421  32.297  1.00 37.44           O  
ATOM    772  CB  TYR A 431       5.027  19.547  32.111  1.00 33.28           C  
ATOM    773  CG  TYR A 431       4.850  19.825  30.641  1.00 34.01           C  
ATOM    774  CD1 TYR A 431       5.427  20.944  30.053  1.00 33.97           C  
ATOM    775  CD2 TYR A 431       4.044  19.000  29.842  1.00 34.87           C  
ATOM    776  CE1 TYR A 431       5.214  21.249  28.712  1.00 35.05           C  
ATOM    777  CE2 TYR A 431       3.821  19.297  28.501  1.00 34.42           C  
ATOM    778  CZ  TYR A 431       4.412  20.427  27.944  1.00 35.92           C  
ATOM    779  OH  TYR A 431       4.207  20.758  26.626  1.00 37.34           O  
ATOM    780  N   ILE A 432       5.163  22.216  33.532  1.00 35.04           N  
ATOM    781  CA  ILE A 432       5.468  23.629  33.503  1.00 33.11           C  
ATOM    782  C   ILE A 432       6.495  23.728  32.406  1.00 32.80           C  
ATOM    783  O   ILE A 432       7.444  22.974  32.388  1.00 32.17           O  
ATOM    784  CB  ILE A 432       6.123  24.114  34.806  1.00 34.45           C  
ATOM    785  CG1 ILE A 432       5.202  23.858  36.001  1.00 33.33           C  
ATOM    786  CG2 ILE A 432       6.474  25.594  34.686  1.00 34.21           C  
ATOM    787  CD1 ILE A 432       3.949  24.647  35.973  1.00 36.44           C  
ATOM    788  N   ARG A 433       6.305  24.653  31.484  1.00 35.26           N  
ATOM    789  CA  ARG A 433       7.239  24.817  30.386  1.00 38.00           C  
ATOM    790  C   ARG A 433       8.028  26.100  30.595  1.00 39.36           C  
ATOM    791  O   ARG A 433       7.470  27.195  30.595  1.00 39.17           O  
ATOM    792  CB  ARG A 433       6.465  24.874  29.069  1.00 39.74           C  
ATOM    793  CG  ARG A 433       7.304  25.117  27.833  1.00 42.74           C  
ATOM    794  CD  ARG A 433       6.388  25.189  26.627  1.00 44.09           C  
ATOM    795  NE  ARG A 433       7.100  25.448  25.381  1.00 45.80           N  
ATOM    796  CZ  ARG A 433       6.491  25.631  24.213  1.00 45.62           C  
ATOM    797  NH1 ARG A 433       5.172  25.573  24.145  1.00 45.30           N  
ATOM    798  NH2 ARG A 433       7.191  25.892  23.121  1.00 45.11           N  
ATOM    799  N   ILE A 434       9.330  25.961  30.779  1.00 41.31           N  
ATOM    800  CA  ILE A 434      10.168  27.126  30.987  1.00 42.94           C  
ATOM    801  C   ILE A 434      11.040  27.343  29.772  1.00 43.59           C  
ATOM    802  O   ILE A 434      11.717  26.429  29.317  1.00 43.24           O  
ATOM    803  CB  ILE A 434      11.046  26.960  32.229  1.00 43.66           C  
ATOM    804  CG1 ILE A 434      10.148  26.836  33.459  1.00 44.01           C  
ATOM    805  CG2 ILE A 434      11.979  28.143  32.367  1.00 42.57           C  
ATOM    806  CD1 ILE A 434      10.881  26.876  34.748  1.00 45.15           C  
ATOM    807  N   THR A 435      11.010  28.559  29.248  1.00 44.14           N  
ATOM    808  CA  THR A 435      11.785  28.895  28.073  1.00 46.06           C  
ATOM    809  C   THR A 435      12.807  29.979  28.367  1.00 47.84           C  
ATOM    810  O   THR A 435      12.480  31.035  28.927  1.00 46.20           O  
ATOM    811  CB  THR A 435      10.861  29.379  26.940  1.00 46.73           C  
ATOM    812  OG1 THR A 435       9.852  28.394  26.708  1.00 48.68           O  
ATOM    813  CG2 THR A 435      11.641  29.609  25.657  1.00 45.13           C  
ATOM    814  N   GLN A 436      14.048  29.693  27.992  1.00 50.32           N  
ATOM    815  CA  GLN A 436      15.143  30.626  28.170  1.00 54.37           C  
ATOM    816  C   GLN A 436      15.491  31.129  26.778  1.00 57.18           C  
ATOM    817  O   GLN A 436      15.865  30.352  25.904  1.00 57.63           O  
ATOM    818  CB  GLN A 436      16.345  29.928  28.812  1.00 52.76           C  
ATOM    819  CG  GLN A 436      16.081  29.501  30.246  1.00 52.46           C  
ATOM    820  CD  GLN A 436      17.203  28.672  30.835  1.00 51.52           C  
ATOM    821  OE1 GLN A 436      17.635  27.689  30.241  1.00 51.70           O  
ATOM    822  NE2 GLN A 436      17.672  29.059  32.012  1.00 50.24           N  
ATOM    823  N   TYR A 437      15.340  32.428  26.573  1.00 60.58           N  
ATOM    824  CA  TYR A 437      15.630  33.034  25.288  1.00 64.82           C  
ATOM    825  C   TYR A 437      16.379  34.355  25.511  1.00 68.04           C  
ATOM    826  O   TYR A 437      16.440  34.844  26.624  1.00 67.59           O  
ATOM    827  CB  TYR A 437      14.321  33.290  24.535  1.00 64.64           C  
ATOM    828  CG  TYR A 437      13.375  34.237  25.246  1.00 64.00           C  
ATOM    829  CD1 TYR A 437      13.336  35.590  24.917  1.00 63.58           C  
ATOM    830  CD2 TYR A 437      12.552  33.790  26.284  1.00 63.69           C  
ATOM    831  CE1 TYR A 437      12.505  36.478  25.601  1.00 64.83           C  
ATOM    832  CE2 TYR A 437      11.718  34.672  26.979  1.00 64.27           C  
ATOM    833  CZ  TYR A 437      11.701  36.010  26.635  1.00 64.83           C  
ATOM    834  OH  TYR A 437      10.891  36.878  27.332  1.00 64.14           O  
ATOM    835  N   LEU A 438      16.925  34.935  24.444  1.00 72.86           N  
ATOM    836  CA  LEU A 438      17.659  36.199  24.544  1.00 77.75           C  
ATOM    837  C   LEU A 438      16.713  37.332  24.125  1.00 80.81           C  
ATOM    838  O   LEU A 438      15.560  37.326  24.434  1.00 81.63           O  
ATOM    839  CB  LEU A 438      18.893  36.123  23.625  1.00 77.72           C  
ATOM    840  CG  LEU A 438      20.017  35.218  24.124  1.00 78.06           C  
ATOM    841  CD1 LEU A 438      21.142  35.118  23.127  1.00 77.72           C  
ATOM    842  CD2 LEU A 438      20.544  35.746  25.460  1.00 79.53           C  
ATOM    843  N   ASP A 439      17.206  38.416  23.600  1.00 83.89           N  
ATOM    844  CA  ASP A 439      16.268  39.381  23.031  1.00 86.31           C  
ATOM    845  C   ASP A 439      17.029  40.384  22.238  1.00 87.43           C  
ATOM    846  O   ASP A 439      17.790  39.989  21.365  1.00 87.31           O  
ATOM    847  CB  ASP A 439      15.247  40.085  23.931  1.00 88.23           C  
ATOM    848  CG  ASP A 439      13.990  40.526  23.089  1.00 90.81           C  
ATOM    849  OD1 ASP A 439      14.121  40.494  21.837  1.00 92.08           O  
ATOM    850  OD2 ASP A 439      12.888  40.857  23.589  1.00 91.88           O  
ATOM    851  N   ALA A 440      16.794  41.661  22.491  1.00 88.34           N  
ATOM    852  CA  ALA A 440      17.508  42.674  21.760  1.00 88.67           C  
ATOM    853  C   ALA A 440      18.568  43.096  22.779  1.00 88.73           C  
ATOM    854  O   ALA A 440      18.264  43.313  23.955  1.00 88.00           O  
ATOM    855  CB  ALA A 440      16.608  43.784  21.414  1.00 89.03           C  
ATOM    856  N   GLY A 441      19.818  43.176  22.338  1.00 88.88           N  
ATOM    857  CA  GLY A 441      20.883  43.535  23.256  1.00 88.67           C  
ATOM    858  C   GLY A 441      21.364  42.218  23.807  1.00 88.32           C  
ATOM    859  O   GLY A 441      22.292  42.162  24.623  1.00 88.05           O  
ATOM    860  N   GLY A 442      20.717  41.151  23.336  1.00 87.89           N  
ATOM    861  CA  GLY A 442      21.045  39.801  23.753  1.00 86.70           C  
ATOM    862  C   GLY A 442      20.763  39.574  25.215  1.00 85.85           C  
ATOM    863  O   GLY A 442      21.488  38.821  25.868  1.00 85.54           O  
ATOM    864  N   ILE A 443      19.715  40.203  25.728  1.00 85.27           N  
ATOM    865  CA  ILE A 443      19.356  40.070  27.147  1.00 85.54           C  
ATOM    866  C   ILE A 443      18.656  38.733  27.458  1.00 84.35           C  
ATOM    867  O   ILE A 443      17.637  38.392  26.862  1.00 84.68           O  
ATOM    868  CB  ILE A 443      18.392  41.195  27.620  1.00 86.90           C  
ATOM    869  CG1 ILE A 443      19.033  42.568  27.385  1.00 87.79           C  
ATOM    870  CG2 ILE A 443      18.080  41.028  29.100  1.00 86.72           C  
ATOM    871  CD1 ILE A 443      18.148  43.747  27.757  1.00 87.68           C  
ATOM    872  N   PRO A 444      19.180  37.998  28.453  1.00 82.40           N  
ATOM    873  CA  PRO A 444      18.573  36.729  28.802  1.00 80.11           C  
ATOM    874  C   PRO A 444      17.331  36.891  29.664  1.00 77.58           C  
ATOM    875  O   PRO A 444      17.366  37.521  30.711  1.00 78.03           O  
ATOM    876  CB  PRO A 444      19.723  36.023  29.525  1.00 80.65           C  
ATOM    877  CG  PRO A 444      20.961  36.688  29.030  1.00 81.52           C  
ATOM    878  CD  PRO A 444      20.534  38.082  29.045  1.00 82.34           C  
ATOM    879  N   ARG A 445      16.231  36.315  29.205  1.00 74.91           N  
ATOM    880  CA  ARG A 445      14.986  36.381  29.965  1.00 71.46           C  
ATOM    881  C   ARG A 445      14.320  35.004  30.026  1.00 66.44           C  
ATOM    882  O   ARG A 445      14.609  34.122  29.216  1.00 64.70           O  
ATOM    883  CB  ARG A 445      14.048  37.428  29.364  1.00 74.04           C  
ATOM    884  CG  ARG A 445      14.562  38.847  29.576  1.00 78.05           C  
ATOM    885  CD  ARG A 445      13.474  39.890  29.358  1.00 82.00           C  
ATOM    886  NE  ARG A 445      13.941  41.246  29.655  1.00 86.11           N  
ATOM    887  CZ  ARG A 445      14.871  41.900  28.958  1.00 87.57           C  
ATOM    888  NH1 ARG A 445      15.450  41.330  27.907  1.00 88.25           N  
ATOM    889  NH2 ARG A 445      15.223  43.132  29.312  1.00 88.30           N  
ATOM    890  N   THR A 446      13.433  34.827  30.996  1.00 61.57           N  
ATOM    891  CA  THR A 446      12.761  33.555  31.184  1.00 56.70           C  
ATOM    892  C   THR A 446      11.251  33.695  31.192  1.00 53.59           C  
ATOM    893  O   THR A 446      10.696  34.593  31.827  1.00 51.67           O  
ATOM    894  CB  THR A 446      13.193  32.898  32.518  1.00 56.18           C  
ATOM    895  OG1 THR A 446      14.611  32.719  32.526  1.00 55.87           O  
ATOM    896  CG2 THR A 446      12.534  31.551  32.685  1.00 55.04           C  
ATOM    897  N   ALA A 447      10.591  32.777  30.493  1.00 50.50           N  
ATOM    898  CA  ALA A 447       9.135  32.768  30.415  1.00 46.70           C  
ATOM    899  C   ALA A 447       8.610  31.447  30.931  1.00 42.89           C  
ATOM    900  O   ALA A 447       9.225  30.417  30.730  1.00 41.96           O  
ATOM    901  CB  ALA A 447       8.683  32.985  28.972  1.00 46.63           C  
ATOM    902  N   GLN A 448       7.468  31.486  31.602  1.00 41.70           N  
ATOM    903  CA  GLN A 448       6.852  30.288  32.153  1.00 39.20           C  
ATOM    904  C   GLN A 448       5.431  30.112  31.644  1.00 39.48           C  
ATOM    905  O   GLN A 448       4.706  31.082  31.410  1.00 40.24           O  
ATOM    906  CB  GLN A 448       6.799  30.354  33.688  1.00 39.56           C  
ATOM    907  CG  GLN A 448       6.240  29.078  34.315  1.00 44.38           C  
ATOM    908  CD  GLN A 448       6.081  29.146  35.832  1.00 46.89           C  
ATOM    909  OE1 GLN A 448       6.883  29.775  36.526  1.00 50.89           O  
ATOM    910  NE2 GLN A 448       5.054  28.471  36.355  1.00 45.29           N  
ATOM    911  N   SER A 449       5.027  28.865  31.468  1.00 39.43           N  
ATOM    912  CA  SER A 449       3.664  28.576  31.056  1.00 38.50           C  
ATOM    913  C   SER A 449       3.307  27.168  31.494  1.00 37.54           C  
ATOM    914  O   SER A 449       4.152  26.279  31.508  1.00 34.99           O  
ATOM    915  CB  SER A 449       3.485  28.739  29.539  1.00 38.05           C  
ATOM    916  OG  SER A 449       4.187  27.759  28.820  1.00 41.56           O  
ATOM    917  N   GLU A 450       2.054  26.990  31.897  1.00 38.13           N  
ATOM    918  CA  GLU A 450       1.562  25.694  32.319  1.00 37.75           C  
ATOM    919  C   GLU A 450       0.938  25.058  31.088  1.00 37.45           C  
ATOM    920  O   GLU A 450       0.132  25.686  30.407  1.00 37.25           O  
ATOM    921  CB  GLU A 450       0.516  25.861  33.415  1.00 40.14           C  
ATOM    922  CG  GLU A 450       1.052  26.509  34.685  1.00 45.58           C  
ATOM    923  CD  GLU A 450       1.279  28.001  34.536  1.00 49.87           C  
ATOM    924  OE1 GLU A 450       0.289  28.711  34.274  1.00 53.03           O  
ATOM    925  OE2 GLU A 450       2.435  28.472  34.678  1.00 51.18           O  
ATOM    926  N   GLU A 451       1.319  23.827  30.781  1.00 35.66           N  
ATOM    927  CA  GLU A 451       0.761  23.177  29.609  1.00 35.22           C  
ATOM    928  C   GLU A 451       0.187  21.795  29.875  1.00 34.69           C  
ATOM    929  O   GLU A 451       0.701  21.025  30.683  1.00 34.58           O  
ATOM    930  CB  GLU A 451       1.810  23.067  28.497  1.00 34.89           C  
ATOM    931  CG  GLU A 451       2.514  24.353  28.161  1.00 36.81           C  
ATOM    932  CD  GLU A 451       3.171  24.324  26.784  1.00 39.73           C  
ATOM    933  OE1 GLU A 451       3.575  23.232  26.339  1.00 40.72           O  
ATOM    934  OE2 GLU A 451       3.299  25.398  26.151  1.00 41.06           O  
ATOM    935  N   THR A 452      -0.902  21.508  29.177  1.00 34.51           N  
ATOM    936  CA  THR A 452      -1.575  20.225  29.241  1.00 34.07           C  
ATOM    937  C   THR A 452      -1.642  19.743  27.796  1.00 35.31           C  
ATOM    938  O   THR A 452      -2.059  20.486  26.912  1.00 34.96           O  
ATOM    939  CB  THR A 452      -2.998  20.365  29.766  1.00 32.86           C  
ATOM    940  OG1 THR A 452      -2.969  20.720  31.150  1.00 33.90           O  
ATOM    941  CG2 THR A 452      -3.744  19.071  29.587  1.00 31.83           C  
ATOM    942  N   ARG A 453      -1.198  18.520  27.549  1.00 36.42           N  
ATOM    943  CA  ARG A 453      -1.243  17.954  26.204  1.00 36.83           C  
ATOM    944  C   ARG A 453      -2.011  16.645  26.303  1.00 37.77           C  
ATOM    945  O   ARG A 453      -1.697  15.811  27.151  1.00 39.25           O  
ATOM    946  CB  ARG A 453       0.168  17.667  25.686  1.00 36.95           C  
ATOM    947  CG  ARG A 453       1.106  18.856  25.651  1.00 37.65           C  
ATOM    948  CD  ARG A 453       0.876  19.702  24.434  1.00 39.95           C  
ATOM    949  NE  ARG A 453       1.828  20.800  24.369  1.00 40.48           N  
ATOM    950  CZ  ARG A 453       1.831  21.732  23.422  1.00 42.16           C  
ATOM    951  NH1 ARG A 453       0.925  21.711  22.445  1.00 41.41           N  
ATOM    952  NH2 ARG A 453       2.749  22.689  23.450  1.00 42.20           N  
ATOM    953  N   VAL A 454      -3.029  16.462  25.468  1.00 38.38           N  
ATOM    954  CA  VAL A 454      -3.778  15.210  25.490  1.00 38.68           C  
ATOM    955  C   VAL A 454      -3.395  14.404  24.257  1.00 40.19           C  
ATOM    956  O   VAL A 454      -3.606  14.845  23.121  1.00 40.50           O  
ATOM    957  CB  VAL A 454      -5.283  15.457  25.517  1.00 38.57           C  
ATOM    958  CG1 VAL A 454      -6.014  14.135  25.536  1.00 38.34           C  
ATOM    959  CG2 VAL A 454      -5.647  16.274  26.765  1.00 38.89           C  
ATOM    960  N   TRP A 455      -2.814  13.226  24.497  1.00 41.70           N  
ATOM    961  CA  TRP A 455      -2.346  12.346  23.427  1.00 42.46           C  
ATOM    962  C   TRP A 455      -3.222  11.154  23.092  1.00 44.21           C  
ATOM    963  O   TRP A 455      -3.763  10.490  23.975  1.00 44.45           O  
ATOM    964  CB  TRP A 455      -0.959  11.807  23.758  1.00 39.62           C  
ATOM    965  CG  TRP A 455       0.102  12.816  23.848  1.00 36.57           C  
ATOM    966  CD1 TRP A 455       0.565  13.422  24.982  1.00 36.55           C  
ATOM    967  CD2 TRP A 455       0.894  13.316  22.767  1.00 35.57           C  
ATOM    968  NE1 TRP A 455       1.607  14.267  24.672  1.00 36.65           N  
ATOM    969  CE2 TRP A 455       1.828  14.223  23.319  1.00 35.38           C  
ATOM    970  CE3 TRP A 455       0.907  13.087  21.384  1.00 33.17           C  
ATOM    971  CZ2 TRP A 455       2.766  14.900  22.536  1.00 35.41           C  
ATOM    972  CZ3 TRP A 455       1.844  13.761  20.603  1.00 33.31           C  
ATOM    973  CH2 TRP A 455       2.761  14.657  21.183  1.00 34.83           C  
ATOM    974  N   HIS A 456      -3.334  10.877  21.800  1.00 48.63           N  
ATOM    975  CA  HIS A 456      -4.103   9.739  21.331  1.00 53.16           C  
ATOM    976  C   HIS A 456      -3.295   8.978  20.292  1.00 56.09           C  
ATOM    977  O   HIS A 456      -2.789   9.565  19.335  1.00 56.17           O  
ATOM    978  CB  HIS A 456      -5.422  10.187  20.729  1.00 54.00           C  
ATOM    979  CG  HIS A 456      -6.354   9.055  20.443  1.00 58.21           C  
ATOM    980  ND1 HIS A 456      -6.712   8.692  19.163  1.00 58.19           N  
ATOM    981  CD2 HIS A 456      -6.979   8.185  21.272  1.00 59.50           C  
ATOM    982  CE1 HIS A 456      -7.519   7.647  19.217  1.00 59.65           C  
ATOM    983  NE2 HIS A 456      -7.697   7.320  20.485  1.00 60.68           N  
ATOM    984  N   ARG A 457      -3.168   7.673  20.502  1.00 60.00           N  
ATOM    985  CA  ARG A 457      -2.426   6.791  19.606  1.00 64.81           C  
ATOM    986  C   ARG A 457      -3.276   6.410  18.391  1.00 67.20           C  
ATOM    987  O   ARG A 457      -4.325   5.772  18.529  1.00 67.36           O  
ATOM    988  CB  ARG A 457      -2.031   5.520  20.362  1.00 67.67           C  
ATOM    989  CG  ARG A 457      -1.081   4.588  19.624  1.00 70.70           C  
ATOM    990  CD  ARG A 457       0.323   5.142  19.642  1.00 72.77           C  
ATOM    991  NE  ARG A 457       1.325   4.118  19.921  1.00 75.70           N  
ATOM    992  CZ  ARG A 457       1.284   3.277  20.955  1.00 77.85           C  
ATOM    993  NH1 ARG A 457       0.282   3.317  21.824  1.00 77.71           N  
ATOM    994  NH2 ARG A 457       2.263   2.403  21.138  1.00 79.54           N  
ATOM    995  N   ARG A 458      -2.830   6.808  17.204  1.00 69.88           N  
ATOM    996  CA  ARG A 458      -3.554   6.482  15.976  1.00 73.08           C  
ATOM    997  C   ARG A 458      -2.632   5.805  14.973  1.00 73.47           C  
ATOM    998  O   ARG A 458      -1.614   6.371  14.573  1.00 73.32           O  
ATOM    999  CB  ARG A 458      -4.150   7.734  15.327  1.00 75.10           C  
ATOM   1000  CG  ARG A 458      -4.686   7.468  13.920  1.00 79.13           C  
ATOM   1001  CD  ARG A 458      -5.035   8.742  13.152  1.00 82.94           C  
ATOM   1002  NE  ARG A 458      -6.371   9.251  13.462  1.00 86.10           N  
ATOM   1003  CZ  ARG A 458      -6.923  10.299  12.859  1.00 88.07           C  
ATOM   1004  NH1 ARG A 458      -6.250  10.951  11.915  1.00 89.52           N  
ATOM   1005  NH2 ARG A 458      -8.148  10.693  13.191  1.00 88.30           N  
ATOM   1006  N   ASP A 459      -2.996   4.590  14.573  1.00 73.86           N  
ATOM   1007  CA  ASP A 459      -2.216   3.827  13.605  1.00 73.73           C  
ATOM   1008  C   ASP A 459      -0.717   3.830  13.901  1.00 72.46           C  
ATOM   1009  O   ASP A 459       0.095   4.063  13.011  1.00 72.19           O  
ATOM   1010  CB  ASP A 459      -2.454   4.371  12.189  1.00 75.26           C  
ATOM   1011  CG  ASP A 459      -3.930   4.418  11.813  1.00 76.75           C  
ATOM   1012  OD1 ASP A 459      -4.620   3.384  11.949  1.00 76.04           O  
ATOM   1013  OD2 ASP A 459      -4.396   5.494  11.373  1.00 78.12           O  
ATOM   1014  N   GLY A 460      -0.349   3.586  15.152  1.00 71.35           N  
ATOM   1015  CA  GLY A 460       1.062   3.548  15.485  1.00 70.05           C  
ATOM   1016  C   GLY A 460       1.692   4.774  16.126  1.00 69.29           C  
ATOM   1017  O   GLY A 460       2.441   4.634  17.098  1.00 69.66           O  
ATOM   1018  N   LYS A 461       1.424   5.968  15.597  1.00 67.49           N  
ATOM   1019  CA  LYS A 461       2.017   7.165  16.185  1.00 66.21           C  
ATOM   1020  C   LYS A 461       1.072   7.991  17.043  1.00 63.77           C  
ATOM   1021  O   LYS A 461      -0.138   8.038  16.804  1.00 62.91           O  
ATOM   1022  CB  LYS A 461       2.642   8.066  15.116  1.00 68.05           C  
ATOM   1023  CG  LYS A 461       1.692   8.601  14.070  1.00 71.03           C  
ATOM   1024  CD  LYS A 461       2.398   9.649  13.206  1.00 73.35           C  
ATOM   1025  CE  LYS A 461       1.727   9.824  11.836  1.00 75.24           C  
ATOM   1026  NZ  LYS A 461       0.294  10.256  11.901  1.00 76.21           N  
ATOM   1027  N   TRP A 462       1.658   8.632  18.054  1.00 60.03           N  
ATOM   1028  CA  TRP A 462       0.929   9.472  18.986  1.00 55.28           C  
ATOM   1029  C   TRP A 462       0.606  10.807  18.366  1.00 54.13           C  
ATOM   1030  O   TRP A 462       1.454  11.412  17.707  1.00 53.78           O  
ATOM   1031  CB  TRP A 462       1.754   9.711  20.242  1.00 52.12           C  
ATOM   1032  CG  TRP A 462       1.853   8.527  21.119  1.00 49.65           C  
ATOM   1033  CD1 TRP A 462       2.905   7.665  21.218  1.00 47.96           C  
ATOM   1034  CD2 TRP A 462       0.866   8.074  22.053  1.00 47.44           C  
ATOM   1035  NE1 TRP A 462       2.637   6.706  22.163  1.00 47.17           N  
ATOM   1036  CE2 TRP A 462       1.393   6.933  22.692  1.00 46.62           C  
ATOM   1037  CE3 TRP A 462      -0.408   8.523  22.412  1.00 44.95           C  
ATOM   1038  CZ2 TRP A 462       0.690   6.234  23.671  1.00 45.01           C  
ATOM   1039  CZ3 TRP A 462      -1.107   7.824  23.386  1.00 46.63           C  
ATOM   1040  CH2 TRP A 462      -0.554   6.692  24.003  1.00 45.97           C  
ATOM   1041  N   GLN A 463      -0.620  11.271  18.582  1.00 52.68           N  
ATOM   1042  CA  GLN A 463      -1.037  12.559  18.050  1.00 51.85           C  
ATOM   1043  C   GLN A 463      -1.731  13.396  19.112  1.00 50.33           C  
ATOM   1044  O   GLN A 463      -2.423  12.870  19.980  1.00 50.11           O  
ATOM   1045  CB  GLN A 463      -1.973  12.368  16.859  1.00 53.72           C  
ATOM   1046  CG  GLN A 463      -1.303  11.750  15.649  1.00 56.63           C  
ATOM   1047  CD  GLN A 463      -2.078  11.990  14.375  1.00 57.97           C  
ATOM   1048  OE1 GLN A 463      -3.235  11.569  14.241  1.00 58.08           O  
ATOM   1049  NE2 GLN A 463      -1.446  12.678  13.426  1.00 58.39           N  
ATOM   1050  N   ILE A 464      -1.531  14.703  19.060  1.00 47.74           N  
ATOM   1051  CA  ILE A 464      -2.187  15.558  20.024  1.00 46.44           C  
ATOM   1052  C   ILE A 464      -3.619  15.787  19.606  1.00 44.84           C  
ATOM   1053  O   ILE A 464      -3.896  16.150  18.465  1.00 44.42           O  
ATOM   1054  CB  ILE A 464      -1.489  16.903  20.163  1.00 48.00           C  
ATOM   1055  CG1 ILE A 464      -0.177  16.700  20.920  1.00 49.67           C  
ATOM   1056  CG2 ILE A 464      -2.387  17.881  20.919  1.00 46.30           C  
ATOM   1057  CD1 ILE A 464       0.485  17.978  21.334  1.00 51.62           C  
ATOM   1058  N   VAL A 465      -4.530  15.576  20.542  1.00 43.13           N  
ATOM   1059  CA  VAL A 465      -5.939  15.734  20.254  1.00 42.92           C  
ATOM   1060  C   VAL A 465      -6.471  17.045  20.867  1.00 42.33           C  
ATOM   1061  O   VAL A 465      -7.465  17.616  20.411  1.00 41.91           O  
ATOM   1062  CB  VAL A 465      -6.708  14.489  20.763  1.00 41.13           C  
ATOM   1063  CG1 VAL A 465      -7.112  14.656  22.200  1.00 42.52           C  
ATOM   1064  CG2 VAL A 465      -7.884  14.237  19.895  1.00 45.80           C  
ATOM   1065  N   HIS A 466      -5.765  17.536  21.878  1.00 41.87           N  
ATOM   1066  CA  HIS A 466      -6.141  18.770  22.558  1.00 40.37           C  
ATOM   1067  C   HIS A 466      -5.010  19.257  23.437  1.00 40.38           C  
ATOM   1068  O   HIS A 466      -4.267  18.451  24.003  1.00 40.65           O  
ATOM   1069  CB  HIS A 466      -7.359  18.545  23.449  1.00 38.98           C  
ATOM   1070  CG  HIS A 466      -7.664  19.697  24.357  1.00 39.47           C  
ATOM   1071  ND1 HIS A 466      -8.041  20.939  23.889  1.00 37.51           N  
ATOM   1072  CD2 HIS A 466      -7.671  19.786  25.709  1.00 40.26           C  
ATOM   1073  CE1 HIS A 466      -8.274  21.742  24.913  1.00 37.99           C  
ATOM   1074  NE2 HIS A 466      -8.056  21.067  26.029  1.00 40.58           N  
ATOM   1075  N   PHE A 467      -4.871  20.572  23.549  1.00 38.30           N  
ATOM   1076  CA  PHE A 467      -3.858  21.113  24.423  1.00 36.66           C  
ATOM   1077  C   PHE A 467      -4.330  22.421  25.021  1.00 37.14           C  
ATOM   1078  O   PHE A 467      -5.136  23.143  24.430  1.00 36.13           O  
ATOM   1079  CB  PHE A 467      -2.508  21.234  23.705  1.00 35.82           C  
ATOM   1080  CG  PHE A 467      -2.351  22.446  22.848  1.00 35.25           C  
ATOM   1081  CD1 PHE A 467      -1.999  23.666  23.405  1.00 35.28           C  
ATOM   1082  CD2 PHE A 467      -2.430  22.344  21.468  1.00 36.28           C  
ATOM   1083  CE1 PHE A 467      -1.716  24.768  22.593  1.00 35.56           C  
ATOM   1084  CE2 PHE A 467      -2.151  23.434  20.649  1.00 36.72           C  
ATOM   1085  CZ  PHE A 467      -1.791  24.650  21.216  1.00 35.45           C  
ATOM   1086  N   HIS A 468      -3.851  22.692  26.229  1.00 36.39           N  
ATOM   1087  CA  HIS A 468      -4.235  23.881  26.964  1.00 34.41           C  
ATOM   1088  C   HIS A 468      -2.987  24.546  27.537  1.00 37.08           C  
ATOM   1089  O   HIS A 468      -2.259  23.938  28.314  1.00 36.56           O  
ATOM   1090  CB  HIS A 468      -5.197  23.454  28.064  1.00 29.69           C  
ATOM   1091  CG  HIS A 468      -5.858  24.586  28.783  1.00 29.16           C  
ATOM   1092  ND1 HIS A 468      -7.003  24.414  29.537  1.00 26.14           N  
ATOM   1093  CD2 HIS A 468      -5.516  25.891  28.906  1.00 27.95           C  
ATOM   1094  CE1 HIS A 468      -7.335  25.564  30.094  1.00 26.50           C  
ATOM   1095  NE2 HIS A 468      -6.450  26.476  29.728  1.00 27.95           N  
ATOM   1096  N   ARG A 469      -2.736  25.792  27.132  1.00 39.28           N  
ATOM   1097  CA  ARG A 469      -1.572  26.539  27.595  1.00 40.60           C  
ATOM   1098  C   ARG A 469      -2.010  27.762  28.411  1.00 42.21           C  
ATOM   1099  O   ARG A 469      -2.881  28.509  27.989  1.00 42.75           O  
ATOM   1100  CB  ARG A 469      -0.733  27.004  26.401  1.00 41.46           C  
ATOM   1101  CG  ARG A 469       0.762  26.988  26.661  1.00 47.46           C  
ATOM   1102  CD  ARG A 469       1.514  28.260  26.206  1.00 49.30           C  
ATOM   1103  NE  ARG A 469       1.239  28.664  24.830  1.00 50.28           N  
ATOM   1104  CZ  ARG A 469       1.067  27.825  23.811  1.00 51.68           C  
ATOM   1105  NH1 ARG A 469       1.136  26.508  24.002  1.00 50.40           N  
ATOM   1106  NH2 ARG A 469       0.828  28.311  22.594  1.00 50.41           N  
ATOM   1107  N   SER A 470      -1.412  27.949  29.587  1.00 44.60           N  
ATOM   1108  CA  SER A 470      -1.690  29.085  30.472  1.00 45.02           C  
ATOM   1109  C   SER A 470      -0.414  29.851  30.764  1.00 49.04           C  
ATOM   1110  O   SER A 470       0.690  29.342  30.586  1.00 47.52           O  
ATOM   1111  CB  SER A 470      -2.262  28.639  31.797  1.00 41.21           C  
ATOM   1112  OG  SER A 470      -3.641  28.518  31.697  1.00 42.61           O  
ATOM   1113  N   GLY A 471      -0.575  31.061  31.280  1.00 54.71           N  
ATOM   1114  CA  GLY A 471       0.572  31.902  31.528  1.00 60.78           C  
ATOM   1115  C   GLY A 471       0.791  32.451  30.132  1.00 66.79           C  
ATOM   1116  O   GLY A 471       1.247  31.722  29.239  1.00 68.14           O  
ATOM   1117  N   ALA A 472       0.458  33.725  29.933  1.00 70.93           N  
ATOM   1118  CA  ALA A 472       0.573  34.386  28.630  1.00 74.89           C  
ATOM   1119  C   ALA A 472       1.750  34.048  27.679  1.00 77.66           C  
ATOM   1120  O   ALA A 472       1.711  34.431  26.503  1.00 77.78           O  
ATOM   1121  CB  ALA A 472       0.472  35.908  28.820  1.00 75.09           C  
ATOM   1122  N   PRO A 473       2.817  33.366  28.159  1.00 80.08           N  
ATOM   1123  CA  PRO A 473       3.872  33.082  27.178  1.00 82.04           C  
ATOM   1124  C   PRO A 473       3.405  32.363  25.910  1.00 83.12           C  
ATOM   1125  O   PRO A 473       2.380  31.676  25.901  1.00 82.52           O  
ATOM   1126  CB  PRO A 473       4.862  32.253  27.984  1.00 81.73           C  
ATOM   1127  CG  PRO A 473       4.855  32.967  29.267  1.00 81.61           C  
ATOM   1128  CD  PRO A 473       3.373  33.245  29.523  1.00 80.72           C  
ATOM   1129  N   SER A 474       4.179  32.534  24.844  1.00 84.69           N  
ATOM   1130  CA  SER A 474       3.878  31.925  23.554  1.00 85.96           C  
ATOM   1131  C   SER A 474       4.241  30.441  23.559  1.00 86.24           C  
ATOM   1132  O   SER A 474       4.942  30.006  24.503  1.00 86.88           O  
ATOM   1133  CB  SER A 474       4.658  32.649  22.444  1.00 86.36           C  
ATOM   1134  OG  SER A 474       4.400  34.046  22.458  1.00 86.91           O  
ATOM   1135  N   VAL A 475       3.824  29.733  22.616  1.00 86.38           N  
TER
END


A second structure was input as follows:


HEADER    TRANSFERASE                             12-MAR-03   1HKX              
TITLE     CRYSTAL STRUCTURE OF CALCIUM/CALMODULIN-DEPENDENT                     
TITLE    2 PROTEIN KINASE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE           
COMPND   3  II ALPHA CHAIN;                                                     
COMPND   4 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;                     
COMPND   5 FRAGMENT: ASSOCIATION DOMAIN, RESIDUES 336-478;                      
COMPND   6 SYNONYM: CAM-KINASE II ALPHA CHAIN, CAM KINASE II ALPHA              
COMPND   7  SUBUNIT, CAMK-II ALPHA SUBUNIT, CAMK2A;                             
COMPND   8 EC: 2.7.1.123;                                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET28A                                     
KEYWDS    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, CALMODULIN-             
KEYWDS   2 BINDING, PHOSPHORYLATION, ATP-BINDING, ALTERNATIVE                   
KEYWDS   3 SPLICING                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.HOELZ,A.C.NAIRN,J.KURIYAN                                           
REVDAT   2   24-FEB-09 1HKX    1       VERSN                                    
REVDAT   1   02-JUN-03 1HKX    0                                                
JRNL        AUTH   A.HOELZ,A.C.NAIRN,J.KURIYAN                                  
JRNL        TITL   CRYSTAL STRUCTURE OF A TETRADECAMERIC ASSEMBLY OF            
JRNL        TITL 2 THE ASSOCIATION DOMAIN OF                                    
JRNL        TITL 3 CA2+/CALMODULIN-DEPENDENT KINASE II                          
JRNL        REF    MOL.CELL                      V.  11  1241 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12769848                                                     
JRNL        DOI    10.1016/S1097-2765(03)00171-0                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.84                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 175595.70                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.000000                       
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 135629                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 6774                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.2                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 17306                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.358                        
REMARK   3   BIN FREE R VALUE                    : 0.381                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.7                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 850                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15588                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.9                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.2                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.65                                                
REMARK   3    B22 (A**2) : -5.76                                                
REMARK   3    B33 (A**2) : 7.41                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -5.20                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.46                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.45                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.4                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.7                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.07                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.85  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.41  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.94  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.19  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30536                                              
REMARK   3   BSOL        : 33.0973                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : TBR_XPLOR.PAR                                  
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  5  : DTT.PAR                                        
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : DTT.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : TBR_XPLOR.TOP                                  
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HKX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12355.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ALS; ALS                           
REMARK 200  BEAMLINE                       : 5.0.2; 8.2.1                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9187,0.9191,1.2543; 1.2545,      
REMARK 200                                   1.0038,1.0090                      
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; MAD                                       
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: RAVE, CCP4                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       73.97300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.02150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       73.97300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       59.02150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: TETRADECAMERIC                    
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC             
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  THIS KINASE MAY PLAY A ROLE IN NEUROTRANSMISSION.                   
REMARK 400  CATALYES ATP + PROTEIN = ADP + O-PHOSPHOPROTEIN.                    
REMARK 400  AUTOPHOSPHORYLATION OF THR-286 MAY ALLOW THE KINASE                 
REMARK 400  TO SWITCH FROM A CALMODULIN-DEPENDENT TO A CALMODULIN-              
REMARK 400  INDEPENDENT STATE.                                                  
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   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     LEU A   476                                                      
REMARK 465     PRO A   477                                                      
REMARK 465     HIS A   478                                                      
REMARK 465     GLY B   332                                                      
REMARK 465     PRO B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     MET B   335                                                      
REMARK 465     THR B   336                                                      
REMARK 465     THR B   337                                                      
REMARK 465     ILE B   338                                                      
REMARK 465     GLU B   339                                                      
REMARK 465     LEU B   476                                                      
REMARK 465     PRO B   477                                                      
REMARK 465     HIS B   478                                                      
REMARK 465     GLY C   332                                                      
REMARK 465     PRO C   333                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     MET C   335                                                      
REMARK 465     THR C   336                                                      
REMARK 465     LEU C   476                                                      
REMARK 465     PRO C   477                                                      
REMARK 465     HIS C   478                                                      
REMARK 465     GLY D   332                                                      
REMARK 465     PRO D   333                                                      
REMARK 465     HIS D   334                                                      
REMARK 465     MET D   335                                                      
REMARK 465     THR D   336                                                      
REMARK 465     THR D   337                                                      
REMARK 465     LEU D   476                                                      
REMARK 465     PRO D   477                                                      
REMARK 465     HIS D   478                                                      
REMARK 465     LEU E   476                                                      
REMARK 465     PRO E   477                                                      
REMARK 465     HIS E   478                                                      
REMARK 465     GLY F   332                                                      
REMARK 465     PRO F   333                                                      
REMARK 465     HIS F   334                                                      
REMARK 465     MET F   335                                                      
REMARK 465     THR F   336                                                      
REMARK 465     LEU F   476                                                      
REMARK 465     PRO F   477                                                      
REMARK 465     HIS F   478                                                      
REMARK 465     GLY G   332                                                      
REMARK 465     PRO G   333                                                      
REMARK 465     HIS G   334                                                      
REMARK 465     MET G   335                                                      
REMARK 465     THR G   336                                                      
REMARK 465     THR G   337                                                      
REMARK 465     ILE G   338                                                      
REMARK 465     GLU G   339                                                      
REMARK 465     LEU G   476                                                      
REMARK 465     PRO G   477                                                      
REMARK 465     HIS G   478                                                      
REMARK 465     GLY H   332                                                      
REMARK 465     LEU H   476                                                      
REMARK 465     PRO H   477                                                      
REMARK 465     HIS H   478                                                      
REMARK 465     GLY I   332                                                      
REMARK 465     PRO I   333                                                      
REMARK 465     HIS I   334                                                      
REMARK 465     MET I   335                                                      
REMARK 465     THR I   336                                                      
REMARK 465     THR I   337                                                      
REMARK 465     ILE I   338                                                      
REMARK 465     GLU I   339                                                      
REMARK 465     ASP I   340                                                      
REMARK 465     LEU I   476                                                      
REMARK 465     PRO I   477                                                      
REMARK 465     HIS I   478                                                      
REMARK 465     GLY J   332                                                      
REMARK 465     PRO J   333                                                      
REMARK 465     HIS J   334                                                      
REMARK 465     MET J   335                                                      
REMARK 465     THR J   336                                                      
REMARK 465     LEU J   476                                                      
REMARK 465     PRO J   477                                                      
REMARK 465     HIS J   478                                                      
REMARK 465     GLY K   332                                                      
REMARK 465     PRO K   333                                                      
REMARK 465     HIS K   334                                                      
REMARK 465     MET K   335                                                      
REMARK 465     THR K   336                                                      
REMARK 465     THR K   337                                                      
REMARK 465     ILE K   338                                                      
REMARK 465     GLU K   339                                                      
REMARK 465     ASP K   340                                                      
REMARK 465     LEU K   476                                                      
REMARK 465     PRO K   477                                                      
REMARK 465     HIS K   478                                                      
REMARK 465     GLY L   332                                                      
REMARK 465     PRO L   333                                                      
REMARK 465     HIS L   334                                                      
REMARK 465     MET L   335                                                      
REMARK 465     THR L   336                                                      
REMARK 465     THR L   337                                                      
REMARK 465     ILE L   338                                                      
REMARK 465     GLU L   339                                                      
REMARK 465     ASP L   340                                                      
REMARK 465     LEU L   476                                                      
REMARK 465     PRO L   477                                                      
REMARK 465     HIS L   478                                                      
REMARK 465     GLY M   332                                                      
REMARK 465     PRO M   333                                                      
REMARK 465     HIS M   334                                                      
REMARK 465     MET M   335                                                      
REMARK 465     THR M   336                                                      
REMARK 465     LEU M   476                                                      
REMARK 465     PRO M   477                                                      
REMARK 465     HIS M   478                                                      
REMARK 465     GLY N   332                                                      
REMARK 465     PRO N   333                                                      
REMARK 465     HIS N   334                                                      
REMARK 465     MET N   335                                                      
REMARK 465     THR N   336                                                      
REMARK 465     THR N   337                                                      
REMARK 465     ILE N   338                                                      
REMARK 465     GLU N   339                                                      
REMARK 465     LEU N   476                                                      
REMARK 465     PRO N   477                                                      
REMARK 465     HIS N   478                                                      
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     VAL A 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL B 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL C 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL D 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL E 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL F 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL G 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL H 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL I 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL J 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL K 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL L 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL M 475    CA   C    O    CB   CG1  CG2                        
REMARK 470     VAL N 475    CA   C    O    CB   CG1  CG2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 439   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    PRO D 473   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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 339       74.55     53.09                                   
REMARK 500    ASP A 340      -38.85    156.88                                   
REMARK 500    LEU A 402       69.30   -156.34                                   
REMARK 500    LEU A 438     -151.64    -98.87                                   
REMARK 500    ASP A 439     -128.94   -168.02                                   
REMARK 500    ALA A 472      -14.05    -36.32                                   
REMARK 500    GLU B 341      -11.11     64.59                                   
REMARK 500    PHE B 397      -41.92    157.59                                   
REMARK 500    SER B 404       12.62    -66.44                                   
REMARK 500    ARG B 405       -2.95    -57.02                                   
REMARK 500    ASN B 406       44.96    -81.83                                   
REMARK 500    SER B 407       19.34   -161.92                                   
REMARK 500    LYS B 408      106.66   -175.90                                   
REMARK 500    LEU B 438     -131.58    -98.93                                   
REMARK 500    ASP B 439     -150.77     45.88                                   
REMARK 500    PRO B 473      136.04    -22.55                                   
REMARK 500    ILE C 338       35.83    -82.78                                   
REMARK 500    ASP C 340       36.30    -80.88                                   
REMARK 500    LEU C 402       58.89   -142.34                                   
REMARK 500    SER C 404       46.22    -69.73                                   
REMARK 500    LEU C 438     -130.89    -99.73                                   
REMARK 500    ASP C 439     -163.09     52.06                                   
REMARK 500    ALA C 472       30.87    175.00                                   
REMARK 500    PRO C 473      -95.40    -47.89                                   
REMARK 500    ASP D 340        4.34    159.05                                   
REMARK 500    GLU D 400      -71.78    -91.11                                   
REMARK 500    LEU D 402       19.73   -150.20                                   
REMARK 500    SER D 404       46.12    -73.47                                   
REMARK 500    ASN D 406       28.31    -76.41                                   
REMARK 500    SER D 407        4.37   -151.33                                   
REMARK 500    LEU D 438     -138.53    -97.46                                   
REMARK 500    ASP D 439     -148.23     56.15                                   
REMARK 500    ALA D 472      -62.10    177.65                                   
REMARK 500    PRO D 473      155.86    -12.44                                   
REMARK 500    HIS E 334       61.61     69.85                                   
REMARK 500    THR E 337      156.74    165.78                                   
REMARK 500    ASN E 401      -68.23   -101.10                                   
REMARK 500    SER E 404       22.23    -65.45                                   
REMARK 500    ASN E 406       76.16    -65.51                                   
REMARK 500    SER E 407       -0.95   -140.50                                   
REMARK 500    LEU E 438     -116.61   -101.88                                   
REMARK 500    ASP E 439     -168.63     40.40                                   
REMARK 500    ALA E 472      -29.51   -171.88                                   
REMARK 500    ASP F 340       76.55     77.06                                   
REMARK 500    ASN F 401       71.75   -110.90                                   
REMARK 500    LEU F 402      -12.51    177.97                                   
REMARK 500    TRP F 403      -66.06     -5.41                                   
REMARK 500    SER F 407       20.65    -60.78                                   
REMARK 500    LYS F 408      133.47    166.91                                   
REMARK 500    LEU F 438     -123.28   -100.43                                   
REMARK 500    ASP F 439     -172.99     57.00                                   
REMARK 500    ALA F 472      -35.21    177.78                                   
REMARK 500    PRO F 473      174.18    -51.65                                   
REMARK 500    GLU G 341       -9.28     64.51                                   
REMARK 500    PHE G 399      -76.24    -79.89                                   
REMARK 500    GLU G 400      -31.25    -36.93                                   
REMARK 500    LEU G 402       33.09   -167.19                                   
REMARK 500    SER G 404       -8.03    -58.53                                   
REMARK 500    ASN G 406       50.23    -68.47                                   
REMARK 500    SER G 407      -59.60   -146.95                                   
REMARK 500    LEU G 438     -123.00   -101.08                                   
REMARK 500    ASP G 439     -164.90     50.02                                   
REMARK 500    ALA G 472      -55.15   -120.94                                   
REMARK 500    PRO G 473      148.96    -18.05                                   
REMARK 500    MET H 335       73.21    -36.65                                   
REMARK 500    THR H 336      -34.91   -169.55                                   
REMARK 500    ILE H 338      -54.32   -167.88                                   
REMARK 500    LEU H 402       56.93   -151.94                                   
REMARK 500    LEU H 438     -132.92   -100.45                                   
REMARK 500    ASP H 439     -167.43     50.99                                   
REMARK 500    ALA H 472      -77.90   -128.01                                   
REMARK 500    PRO H 473     -142.84      5.77                                   
REMARK 500    ARG I 396        5.41    -63.85                                   
REMARK 500    GLU I 400      -72.75    -57.91                                   
REMARK 500    LEU I 402       65.42   -169.04                                   
REMARK 500    SER I 404       30.92    -98.92                                   
REMARK 500    ARG I 405       48.62    -72.74                                   
REMARK 500    ASN I 406      -53.68   -166.10                                   
REMARK 500    SER I 407        4.96    -61.56                                   
REMARK 500    PRO I 409      108.44    -53.78                                   
REMARK 500    LEU I 438     -135.74    -94.97                                   
REMARK 500    ASP I 439     -156.67   -165.39                                   
REMARK 500    ALA I 472       -4.98    178.69                                   
REMARK 500    PRO I 473     -121.42    -59.64                                   
REMARK 500    ASP J 340     -154.51    -71.18                                   
REMARK 500    GLU J 341      -23.32     67.21                                   
REMARK 500    GLU J 400      -75.97   -113.75                                   
REMARK 500    SER J 407       19.37   -172.98                                   
REMARK 500    LYS J 408      103.81   -171.30                                   
REMARK 500    LEU J 438      -76.84    -90.25                                   
REMARK 500    ASP J 439     -109.33    -60.79                                   
REMARK 500    SER J 449      145.32    176.22                                   
REMARK 500    ARG J 458     -112.34    -99.46                                   
REMARK 500    ALA J 472       32.80    162.43                                   
REMARK 500    PRO J 473     -106.04    -77.70                                   
REMARK 500    ASN K 401       37.16    -73.85                                   
REMARK 500    LEU K 402       72.88   -179.50                                   
REMARK 500    ASN K 416       51.91     39.26                                   
REMARK 500    TYR K 437     -166.40   -126.12                                   
REMARK 500    ASP K 439     -168.54     48.10                                   
REMARK 500    ALA K 472      -46.04    172.58                                   
REMARK 500    PRO K 473       97.33    -25.37                                   
REMARK 500    LEU L 402       20.44   -143.78                                   
REMARK 500    SER L 404       49.89    -70.43                                   
REMARK 500    SER L 407       36.38    -69.48                                   
REMARK 500    LYS L 408      110.09    169.00                                   
REMARK 500    LEU L 438     -116.08   -124.96                                   
REMARK 500    ASP L 439     -169.81     47.03                                   
REMARK 500    ALA L 472      -34.18   -179.75                                   
REMARK 500    PRO L 473      -98.69    -24.48                                   
REMARK 500    ILE M 338      -20.85   -146.68                                   
REMARK 500    GLU M 339      177.93    -58.38                                   
REMARK 500    ASP M 340       77.35     11.59                                   
REMARK 500    THR M 343       13.37    -65.31                                   
REMARK 500    LEU M 402       77.85   -162.72                                   
REMARK 500    SER M 404       39.83    -66.65                                   
REMARK 500    ASN M 406      -83.46    -59.53                                   
REMARK 500    SER M 407       13.68    -68.02                                   
REMARK 500    LEU M 438     -108.87    -94.39                                   
REMARK 500    ASP M 439     -149.53     31.16                                   
REMARK 500    ALA M 472      -68.38   -105.95                                   
REMARK 500    PRO M 473      151.34    -24.43                                   
REMARK 500    GLU N 341       82.07    -42.17                                   
REMARK 500    PHE N 399      -72.64    -80.54                                   
REMARK 500    LYS N 408      123.28    172.66                                   
REMARK 500    LEU N 438     -129.45   -100.10                                   
REMARK 500    ASP N 439     -179.71     72.75                                   
REMARK 500    ALA N 472      -30.75   -158.75                                   
REMARK 500    PRO N 473     -171.54    -50.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL E1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL F1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL G1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL H1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL I1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL J1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL K1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL L1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL M1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL N1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBR A2000                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CDM   RELATED DB: PDB                                   
DBREF  1HKX A  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX A  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX B  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX B  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX C  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX C  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX D  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX D  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX E  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX E  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX F  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX F  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX G  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX G  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX H  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX H  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX I  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX I  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX J  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX J  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX K  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX K  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX L  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX L  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX M  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX M  336   478  UNP    P11798   KCCA_MOUSE     336    478             
DBREF  1HKX N  332   335  PDB    1HKX     1HKX           332    335             
DBREF  1HKX N  336   478  UNP    P11798   KCCA_MOUSE     336    478             
SEQRES   1 A  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 A  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 A  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 A  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 A  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 A  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 A  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 A  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 A  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 A  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 A  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 A  147  VAL LEU PRO HIS                                              
SEQRES   1 B  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 B  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 B  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 B  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 B  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 B  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 B  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 B  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 B  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 B  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 B  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 B  147  VAL LEU PRO HIS                                              
SEQRES   1 C  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 C  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 C  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 C  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 C  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 C  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 C  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 C  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 C  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 C  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 C  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 C  147  VAL LEU PRO HIS                                              
SEQRES   1 D  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 D  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 D  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 D  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 D  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 D  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 D  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 D  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 D  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 D  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 D  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 D  147  VAL LEU PRO HIS                                              
SEQRES   1 E  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 E  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 E  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 E  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 E  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 E  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 E  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 E  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 E  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 E  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 E  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 E  147  VAL LEU PRO HIS                                              
SEQRES   1 F  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 F  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 F  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 F  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 F  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 F  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 F  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 F  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 F  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 F  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 F  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 F  147  VAL LEU PRO HIS                                              
SEQRES   1 G  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 G  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 G  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 G  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 G  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 G  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 G  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 G  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 G  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 G  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 G  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 G  147  VAL LEU PRO HIS                                              
SEQRES   1 H  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 H  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 H  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 H  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 H  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 H  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 H  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 H  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 H  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 H  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 H  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 H  147  VAL LEU PRO HIS                                              
SEQRES   1 I  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 I  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 I  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 I  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 I  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 I  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 I  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 I  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 I  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 I  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 I  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 I  147  VAL LEU PRO HIS                                              
SEQRES   1 J  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 J  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 J  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 J  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 J  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 J  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 J  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 J  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 J  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 J  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 J  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 J  147  VAL LEU PRO HIS                                              
SEQRES   1 K  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 K  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 K  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 K  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 K  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 K  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 K  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 K  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 K  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 K  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 K  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 K  147  VAL LEU PRO HIS                                              
SEQRES   1 L  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 L  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 L  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 L  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 L  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 L  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 L  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 L  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 L  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 L  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 L  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 L  147  VAL LEU PRO HIS                                              
SEQRES   1 M  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 M  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 M  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 M  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 M  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 M  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 M  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 M  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 M  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 M  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 M  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 M  147  VAL LEU PRO HIS                                              
SEQRES   1 N  147  GLY PRO HIS MET THR THR ILE GLU ASP GLU ASP THR LYS          
SEQRES   2 N  147  VAL ARG LYS GLN GLU ILE ILE LYS VAL THR GLU GLN LEU          
SEQRES   3 N  147  ILE GLU ALA ILE SER ASN GLY ASP PHE GLU SER TYR THR          
SEQRES   4 N  147  LYS MET CYS ASP PRO GLY MET THR ALA PHE GLU PRO GLU          
SEQRES   5 N  147  ALA LEU GLY ASN LEU VAL GLU GLY LEU ASP PHE HIS ARG          
SEQRES   6 N  147  PHE TYR PHE GLU ASN LEU TRP SER ARG ASN SER LYS PRO          
SEQRES   7 N  147  VAL HIS THR THR ILE LEU ASN PRO HIS ILE HIS LEU MET          
SEQRES   8 N  147  GLY ASP GLU SER ALA CYS ILE ALA TYR ILE ARG ILE THR          
SEQRES   9 N  147  GLN TYR LEU ASP ALA GLY GLY ILE PRO ARG THR ALA GLN          
SEQRES  10 N  147  SER GLU GLU THR ARG VAL TRP HIS ARG ARG ASP GLY LYS          
SEQRES  11 N  147  TRP GLN ILE VAL HIS PHE HIS ARG SER GLY ALA PRO SER          
SEQRES  12 N  147  VAL LEU PRO HIS                                              
HET     CL  A1476       1                                                       
HET     CL  B1475       1                                                       
HET     CL  C1475       1                                                       
HET     CL  D1475       1                                                       
HET     CL  E1475       1                                                       
HET     CL  F1475       1                                                       
HET     CL  G1475       1                                                       
HET     CL  H1475       1                                                       
HET     CL  I1475       1                                                       
HET     CL  J1475       1                                                       
HET     CL  K1475       1                                                       
HET     CL  L1475       1                                                       
HET     CL  M1475       1                                                       
HET     CL  N1475       1                                                       
HET    DTT  A1475       8                                                       
HET    TBR  A2000      18                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     TBR HEXATANTALUM DODECABROMIDE                                       
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL  15   CL    14(CL 1-)                                                    
FORMUL  29  DTT    C4 H10 O2 S2                                                 
FORMUL  30  TBR    BR12 TA6 2+                                                  
FORMUL  31  HOH   *62(H2 O1)                                                    
HELIX    1   1 ASP A  340  ASN A  363  1                                  24    
HELIX    2   2 ASP A  365  MET A  372  1                                   8    
HELIX    3   3 GLU A  381  LEU A  385  5                                   5    
HELIX    4   4 LEU A  392  ASN A  401  1                                  10    
HELIX    5   5 TRP A  403  SER A  407  5                                   5    
HELIX    6   6 GLU B  341  ASN B  363  1                                  23    
HELIX    7   7 ASP B  365  MET B  372  1                                   8    
HELIX    8   8 GLU B  381  LEU B  385  5                                   5    
HELIX    9   9 LEU B  392  ASN B  401  1                                  10    
HELIX   10  10 TRP B  403  SER B  407  5                                   5    
HELIX   11  11 GLU C  341  ASN C  363  1                                  23    
HELIX   12  12 ASP C  365  MET C  372  1                                   8    
HELIX   13  13 GLU C  381  LEU C  385  5                                   5    
HELIX   14  14 LEU C  392  ASN C  401  1                                  10    
HELIX   15  15 TRP C  403  SER C  407  5                                   5    
HELIX   16  16 GLU D  341  ASN D  363  1                                  23    
HELIX   17  17 ASP D  365  MET D  372  1                                   8    
HELIX   18  18 GLU D  381  LEU D  385  5                                   5    
HELIX   19  19 LEU D  392  ASN D  401  1                                  10    
HELIX   20  20 TRP D  403  SER D  407  5                                   5    
HELIX   21  21 GLU E  341  ASN E  363  1                                  23    
HELIX   22  22 ASP E  365  MET E  372  1                                   8    
HELIX   23  23 GLU E  381  LEU E  385  5                                   5    
HELIX   24  24 LEU E  392  ASN E  401  1                                  10    
HELIX   25  25 TRP E  403  SER E  407  5                                   5    
HELIX   26  26 GLU F  341  ASN F  363  1                                  23    
HELIX   27  27 ASP F  365  MET F  372  1                                   8    
HELIX   28  28 GLU F  381  LEU F  385  5                                   5    
HELIX   29  29 LEU F  392  ASN F  401  1                                  10    
HELIX   30  30 TRP F  403  SER F  407  5                                   5    
HELIX   31  31 GLU G  341  ASN G  363  1                                  23    
HELIX   32  32 ASP G  365  MET G  372  1                                   8    
HELIX   33  33 GLU G  381  LEU G  385  5                                   5    
HELIX   34  34 LEU G  392  ASN G  401  1                                   7    
HELIX   35  35 TRP G  403  SER G  407  5                                   5    
HELIX   36  36 GLU H  339  ASN H  363  1                                  25    
HELIX   37  37 ASP H  365  MET H  372  1                                   8    
HELIX   38  38 GLU H  381  LEU H  385  5                                   5    
HELIX   39  39 LEU H  392  ASN H  401  1                                  10    
HELIX   40  40 TRP H  403  SER H  407  5                                   6    
HELIX   41  41 ASP I  342  ASN I  363  1                                  22    
HELIX   42  42 ASP I  365  MET I  372  1                                   8    
HELIX   43  43 GLU I  381  LEU I  385  5                                   5    
HELIX   44  44 LEU I  392  ASN I  401  1                                  10    
HELIX   45  45 TRP I  403  SER I  407  5                                   5    
HELIX   46  46 ASP J  342  ASN J  363  1                                  22    
HELIX   47  47 ASP J  365  MET J  372  1                                   8    
HELIX   48  48 GLU J  381  LEU J  385  5                                   5    
HELIX   49  49 LEU J  392  ASN J  401  1                                  10    
HELIX   50  50 TRP J  403  SER J  407  5                                   5    
HELIX   51  51 GLU K  341  ASN K  363  1                                  23    
HELIX   52  52 ASP K  365  MET K  372  1                                   8    
HELIX   53  53 GLU K  381  LEU K  385  5                                   5    
HELIX   54  54 LEU K  392  ASN K  401  1                                  10    
HELIX   55  55 TRP K  403  SER K  407  5                                   5    
HELIX   56  56 GLU L  341  ASN L  363  1                                  23    
HELIX   57  57 ASP L  365  MET L  372  1                                   8    
HELIX   58  58 GLU L  381  LEU L  385  5                                   5    
HELIX   59  59 LEU L  392  ASN L  401  1                                  10    
HELIX   60  60 TRP L  403  SER L  407  5                                   5    
HELIX   61  61 ASP M  340  ASN M  363  1                                  24    
HELIX   62  62 ASP M  365  MET M  372  1                                   8    
HELIX   63  63 GLU M  381  LEU M  385  5                                   5    
HELIX   64  64 LEU M  392  ASN M  401  1                                  10    
HELIX   65  65 TRP M  403  SER M  407  5                                   5    
HELIX   66  66 GLU N  341  ASN N  363  1                                  23    
HELIX   67  67 ASP N  365  MET N  372  1                                   8    
HELIX   68  68 GLU N  381  LEU N  385  5                                   5    
HELIX   69  69 LEU N  392  ASN N  401  1                                  10    
HELIX   70  70 TRP N  403  SER N  407  5                                   5    
SHEET    1  AA 6 VAL A 389  GLU A 390  0                                        
SHEET    2  AA 6 CYS A 373  PHE A 380 -1  O  ALA A 379   N  VAL A 389           
SHEET    3  AA 6 LYS A 461  SER A 470  1  O  ILE A 464   N  ASP A 374           
SHEET    4  AA 6 ARG A 445  ARG A 458 -1  O  GLU A 450   N  SER A 470           
SHEET    5  AA 6 SER A 426  TYR A 437 -1  O  ALA A 427   N  TRP A 455           
SHEET    6  AA 6 VAL A 410  LEU A 421 -1  O  HIS A 411   N  GLN A 436           
SHEET    1  BA 6 VAL B 389  GLU B 390  0                                        
SHEET    2  BA 6 CYS B 373  PHE B 380 -1  O  ALA B 379   N  VAL B 389           
SHEET    3  BA 6 LYS B 461  GLY B 471  1  O  ILE B 464   N  ASP B 374           
SHEET    4  BA 6 ARG B 445  ARG B 458 -1  O  GLU B 450   N  SER B 470           
SHEET    5  BA 6 SER B 426  TYR B 437 -1  O  ALA B 427   N  TRP B 455           
SHEET    6  BA 6 HIS B 411  LEU B 421 -1  O  HIS B 411   N  GLN B 436           
SHEET    1  CA 6 VAL C 389  GLU C 390  0                                        
SHEET    2  CA 6 CYS C 373  PHE C 380 -1  O  ALA C 379   N  VAL C 389           
SHEET    3  CA 6 LYS C 461  SER C 470  1  O  ILE C 464   N  ASP C 374           
SHEET    4  CA 6 ARG C 445  ARG C 458 -1  O  GLU C 450   N  SER C 470           
SHEET    5  CA 6 SER C 426  TYR C 437 -1  O  ALA C 427   N  TRP C 455           
SHEET    6  CA 6 VAL C 410  LEU C 421 -1  O  HIS C 411   N  GLN C 436           
SHEET    1  DA 6 VAL D 389  GLU D 390  0                                        
SHEET    2  DA 6 CYS D 373  PHE D 380 -1  O  ALA D 379   N  VAL D 389           
SHEET    3  DA 6 LYS D 461  SER D 470  1  O  ILE D 464   N  ASP D 374           
SHEET    4  DA 6 ARG D 445  ARG D 458 -1  O  GLU D 450   N  SER D 470           
SHEET    5  DA 6 SER D 426  TYR D 437 -1  O  ALA D 427   N  TRP D 455           
SHEET    6  DA 6 HIS D 411  LEU D 421 -1  O  HIS D 411   N  GLN D 436           
SHEET    1  EA 6 VAL E 389  GLU E 390  0                                        
SHEET    2  EA 6 CYS E 373  PHE E 380 -1  O  ALA E 379   N  VAL E 389           
SHEET    3  EA 6 LYS E 461  SER E 470  1  O  ILE E 464   N  ASP E 374           
SHEET    4  EA 6 ARG E 445  ARG E 458 -1  O  GLU E 450   N  SER E 470           
SHEET    5  EA 6 SER E 426  TYR E 437 -1  O  ALA E 427   N  TRP E 455           
SHEET    6  EA 6 VAL E 410  LEU E 421 -1  O  HIS E 411   N  GLN E 436           
SHEET    1  FA 6 VAL F 389  GLU F 390  0                                        
SHEET    2  FA 6 CYS F 373  PHE F 380 -1  O  ALA F 379   N  VAL F 389           
SHEET    3  FA 6 LYS F 461  SER F 470  1  O  ILE F 464   N  ASP F 374           
SHEET    4  FA 6 ARG F 445  ARG F 458 -1  O  GLU F 450   N  SER F 470           
SHEET    5  FA 6 SER F 426  TYR F 437 -1  O  ALA F 427   N  TRP F 455           
SHEET    6  FA 6 HIS F 411  LEU F 421 -1  O  HIS F 411   N  GLN F 436           
SHEET    1  GA 6 VAL G 389  GLU G 390  0                                        
SHEET    2  GA 6 CYS G 373  PHE G 380 -1  O  ALA G 379   N  VAL G 389           
SHEET    3  GA 6 LYS G 461  GLY G 471  1  O  ILE G 464   N  ASP G 374           
SHEET    4  GA 6 ARG G 445  ARG G 458 -1  O  GLU G 450   N  SER G 470           
SHEET    5  GA 6 SER G 426  TYR G 437 -1  O  ALA G 427   N  TRP G 455           
SHEET    6  GA 6 HIS G 411  LEU G 421 -1  O  HIS G 411   N  GLN G 436           
SHEET    1  HA 6 VAL H 389  GLU H 390  0                                        
SHEET    2  HA 6 CYS H 373  PHE H 380 -1  O  ALA H 379   N  VAL H 389           
SHEET    3  HA 6 LYS H 461  GLY H 471  1  O  ILE H 464   N  ASP H 374           
SHEET    4  HA 6 ARG H 445  ARG H 458 -1  O  GLU H 450   N  SER H 470           
SHEET    5  HA 6 SER H 426  TYR H 437 -1  O  ALA H 427   N  TRP H 455           
SHEET    6  HA 6 HIS H 411  LEU H 421 -1  O  HIS H 411   N  GLN H 436           
SHEET    1  IA 6 VAL I 389  GLU I 390  0                                        
SHEET    2  IA 6 CYS I 373  PHE I 380 -1  O  ALA I 379   N  VAL I 389           
SHEET    3  IA 6 LYS I 461  SER I 470  1  O  ILE I 464   N  ASP I 374           
SHEET    4  IA 6 ARG I 445  ARG I 458 -1  O  GLU I 450   N  SER I 470           
SHEET    5  IA 6 SER I 426  TYR I 437 -1  O  ALA I 427   N  TRP I 455           
SHEET    6  IA 6 HIS I 411  LEU I 421 -1  O  HIS I 411   N  GLN I 436           
SHEET    1  JA 6 VAL J 389  GLU J 390  0                                        
SHEET    2  JA 6 CYS J 373  PHE J 380 -1  O  ALA J 379   N  VAL J 389           
SHEET    3  JA 6 TRP J 462  SER J 470  1  O  ILE J 464   N  ASP J 374           
SHEET    4  JA 6 GLU J 450  ARG J 457 -1  O  GLU J 450   N  SER J 470           
SHEET    5  JA 6 SER J 426  TYR J 437 -1  O  ALA J 427   N  TRP J 455           
SHEET    6  JA 6 HIS J 411  LEU J 421 -1  O  HIS J 411   N  GLN J 436           
SHEET    1  JB 6 VAL J 389  GLU J 390  0                                        
SHEET    2  JB 6 CYS J 373  PHE J 380 -1  O  ALA J 379   N  VAL J 389           
SHEET    3  JB 6 TRP J 462  SER J 470  1  O  ILE J 464   N  ASP J 374           
SHEET    4  JB 6 GLU J 450  ARG J 457 -1  O  GLU J 450   N  SER J 470           
SHEET    5  JB 6 SER J 426  TYR J 437 -1  O  ALA J 427   N  TRP J 455           
SHEET    6  JB 6 ARG J 445  ALA J 447 -1  O  ARG J 445   N  TYR J 437           
SHEET    1  KA 6 VAL K 389  GLU K 390  0                                        
SHEET    2  KA 6 CYS K 373  PHE K 380 -1  O  ALA K 379   N  VAL K 389           
SHEET    3  KA 6 LYS K 461  SER K 470  1  O  ILE K 464   N  ASP K 374           
SHEET    4  KA 6 ARG K 445  ARG K 458 -1  O  GLU K 450   N  SER K 470           
SHEET    5  KA 6 SER K 426  TYR K 437 -1  O  ALA K 427   N  TRP K 455           
SHEET    6  KA 6 HIS K 411  LEU K 421 -1  O  HIS K 411   N  GLN K 436           
SHEET    1  LA 6 VAL L 389  GLU L 390  0                                        
SHEET    2  LA 6 CYS L 373  PHE L 380 -1  O  ALA L 379   N  VAL L 389           
SHEET    3  LA 6 TRP L 462  SER L 470  1  O  ILE L 464   N  ASP L 374           
SHEET    4  LA 6 ARG L 445  ARG L 457 -1  O  GLU L 450   N  SER L 470           
SHEET    5  LA 6 SER L 426  TYR L 437 -1  O  ALA L 427   N  TRP L 455           
SHEET    6  LA 6 HIS L 411  LEU L 421 -1  O  HIS L 411   N  GLN L 436           
SHEET    1  MA 6 VAL M 389  GLU M 390  0                                        
SHEET    2  MA 6 CYS M 373  PHE M 380 -1  O  ALA M 379   N  VAL M 389           
SHEET    3  MA 6 LYS M 461  GLY M 471  1  O  ILE M 464   N  ASP M 374           
SHEET    4  MA 6 ARG M 445  ARG M 458 -1  O  GLU M 450   N  SER M 470           
SHEET    5  MA 6 SER M 426  TYR M 437 -1  O  ALA M 427   N  TRP M 455           
SHEET    6  MA 6 HIS M 411  MET M 422 -1  O  HIS M 411   N  GLN M 436           
SHEET    1  NA 6 VAL N 389  GLU N 390  0                                        
SHEET    2  NA 6 CYS N 373  PHE N 380 -1  O  ALA N 379   N  VAL N 389           
SHEET    3  NA 6 LYS N 461  SER N 470  1  O  ILE N 464   N  ASP N 374           
SHEET    4  NA 6 ARG N 445  ARG N 458 -1  O  GLU N 450   N  SER N 470           
SHEET    5  NA 6 SER N 426  TYR N 437 -1  O  ALA N 427   N  TRP N 455           
SHEET    6  NA 6 HIS N 411  LEU N 421 -1  O  HIS N 411   N  GLN N 436           
SITE     1 AC1  4 ILE A 361  TYR A 369  ARG A 453  PHE A 467                    
SITE     1 AC2  4 ILE B 361  TYR B 369  ARG B 453  PHE B 467                    
SITE     1 AC3  4 ILE C 361  TYR C 369  ARG C 453  PHE C 467                    
SITE     1 AC4  4 ILE D 361  TYR D 369  ARG D 453  PHE D 467                    
SITE     1 AC5  4 ILE E 361  TYR E 369  ARG E 453  PHE E 467                    
SITE     1 AC6  3 ILE F 361  TYR F 369  PHE F 467                               
SITE     1 AC7  4 ILE G 361  TYR G 369  ARG G 453  PHE G 467                    
SITE     1 AC8  5 ILE H 361  TYR H 369  ARG H 453  PHE H 467                    
SITE     2 AC8  5 ARG H 469                                                     
SITE     1 AC9  5 ILE I 361  PHE I 467  ARG I 469  VAL I 475                    
SITE     2 AC9  5 HOH I2002                                                     
SITE     1 BC1  4 ILE J 361  TYR J 369  ARG J 453  PHE J 467                    
SITE     1 BC2  3 TYR K 369  ARG K 453  PHE K 467                               
SITE     1 BC3  3 ILE L 361  ARG L 453  PHE L 467                               
SITE     1 BC4  4 ILE M 361  TYR M 369  ARG M 453  PHE M 467                    
SITE     1 BC5  5 ILE N 361  TYR N 369  ARG N 453  PHE N 467                    
SITE     2 BC5  5 VAL N 475                                                     
SITE     1 BC6  7 GLU A 339  ASP A 342  ARG A 346  ASP A 424                    
SITE     2 BC6  7 TBR A2000  HIS G 456  ARG G 458                               
SITE     1 BC7 11 THR A 343  ARG A 346  LEU A 421  GLY A 423                    
SITE     2 BC7 11 DTT A1475  HIS B 456  HIS G 456  THR H 343                    
SITE     3 BC7 11 ARG H 346  LEU H 421  GLY H 423                               
CRYST1  147.946  118.043  157.820  90.00 110.91  90.00 C 1 2 1      56          
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      0.006759  0.000000  0.002582        0.00000                         
SCALE2      0.000000  0.008471  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006783        0.00000                         
ATOM      1  N   MET A 335       4.803  -8.900  43.071  1.00115.72           N  
ATOM      2  CA  MET A 335       3.416  -9.163  42.598  1.00115.33           C  
ATOM      3  C   MET A 335       3.101  -8.304  41.379  1.00114.69           C  
ATOM      4  O   MET A 335       2.575  -8.790  40.379  1.00114.53           O  
ATOM      5  CB  MET A 335       2.410  -8.844  43.709  1.00115.98           C  
ATOM      6  CG  MET A 335       0.994  -9.337  43.430  1.00116.93           C  
ATOM      7  SD  MET A 335       0.712 -11.074  43.902  1.00117.41           S  
ATOM      8  CE  MET A 335       1.461 -11.953  42.557  1.00117.33           C  
ATOM      9  N   THR A 336       3.433  -7.021  41.473  1.00114.15           N  
ATOM     10  CA  THR A 336       3.177  -6.071  40.395  1.00113.04           C  
ATOM     11  C   THR A 336       4.444  -5.636  39.652  1.00111.92           C  
ATOM     12  O   THR A 336       4.466  -4.572  39.033  1.00111.37           O  
ATOM     13  CB  THR A 336       2.471  -4.804  40.935  1.00113.03           C  
ATOM     14  OG1 THR A 336       3.379  -4.061  41.756  1.00112.66           O  
ATOM     15  CG2 THR A 336       1.254  -5.186  41.768  1.00112.85           C  
ATOM     16  N   THR A 337       5.491  -6.457  39.711  1.00110.56           N  
ATOM     17  CA  THR A 337       6.746  -6.140  39.031  1.00109.42           C  
ATOM     18  C   THR A 337       6.494  -5.895  37.540  1.00108.09           C  
ATOM     19  O   THR A 337       6.646  -4.773  37.054  1.00107.51           O  
ATOM     20  CB  THR A 337       7.792  -7.274  39.231  1.00109.82           C  
ATOM     21  OG1 THR A 337       8.849  -7.131  38.272  1.00109.62           O  
ATOM     22  CG2 THR A 337       7.142  -8.645  39.098  1.00109.85           C  
ATOM     23  N   ILE A 338       6.114  -6.939  36.810  1.00106.71           N  
ATOM     24  CA  ILE A 338       5.803  -6.769  35.396  1.00105.25           C  
ATOM     25  C   ILE A 338       4.579  -5.874  35.464  1.00104.60           C  
ATOM     26  O   ILE A 338       3.965  -5.754  36.523  1.00105.44           O  
ATOM     27  CB  ILE A 338       5.351  -8.086  34.721  1.00104.81           C  
ATOM     28  CG1 ILE A 338       6.252  -9.249  35.135  1.00105.14           C  
ATOM     29  CG2 ILE A 338       5.352  -7.921  33.221  1.00103.89           C  
ATOM     30  CD1 ILE A 338       5.851  -9.903  36.451  1.00104.84           C  
ATOM     31  N   GLU A 339       4.207  -5.244  34.363  1.00103.41           N  
ATOM     32  CA  GLU A 339       3.009  -4.411  34.393  1.00102.76           C  
ATOM     33  C   GLU A 339       3.118  -3.413  35.540  1.00100.20           C  
ATOM     34  O   GLU A 339       2.457  -3.555  36.567  1.00100.40           O  
ATOM     35  CB  GLU A 339       1.769  -5.293  34.604  1.00104.96           C  
ATOM     36  CG  GLU A 339       1.860  -6.670  33.945  1.00107.80           C  
ATOM     37  CD  GLU A 339       0.506  -7.339  33.786  1.00109.21           C  
ATOM     38  OE1 GLU A 339      -0.390  -6.732  33.151  1.00108.47           O  
ATOM     39  OE2 GLU A 339       0.344  -8.473  34.291  1.00110.39           O  
ATOM     40  N   ASP A 340       3.952  -2.405  35.337  1.00 96.94           N  
ATOM     41  CA  ASP A 340       4.232  -1.359  36.313  1.00 94.07           C  
ATOM     42  C   ASP A 340       5.580  -0.891  35.838  1.00 91.99           C  
ATOM     43  O   ASP A 340       5.920   0.291  35.849  1.00 91.31           O  
ATOM     44  CB  ASP A 340       4.387  -1.932  37.717  1.00 94.13           C  
ATOM     45  CG  ASP A 340       5.191  -1.025  38.622  1.00 93.82           C  
ATOM     46  OD1 ASP A 340       4.810   0.150  38.779  1.00 94.37           O  
ATOM     47  OD2 ASP A 340       6.210  -1.480  39.173  1.00 93.58           O  
ATOM     48  N   GLU A 341       6.354  -1.876  35.427  1.00 90.04           N  
ATOM     49  CA  GLU A 341       7.656  -1.625  34.893  1.00 88.46           C  
ATOM     50  C   GLU A 341       7.340  -1.116  33.496  1.00 88.57           C  
ATOM     51  O   GLU A 341       8.149  -0.438  32.868  1.00 88.82           O  
ATOM     52  CB  GLU A 341       8.443  -2.935  34.833  1.00 86.75           C  
ATOM     53  CG  GLU A 341       9.909  -2.769  34.510  1.00 84.57           C  
ATOM     54  CD  GLU A 341      10.127  -2.230  33.118  1.00 83.08           C  
ATOM     55  OE1 GLU A 341       9.522  -2.803  32.190  1.00 82.76           O  
ATOM     56  OE2 GLU A 341      10.893  -1.248  32.949  1.00 80.62           O  
ATOM     57  N   ASP A 342       6.135  -1.401  33.015  1.00 89.32           N  
ATOM     58  CA  ASP A 342       5.821  -0.960  31.672  1.00 88.55           C  
ATOM     59  C   ASP A 342       5.122   0.387  31.692  1.00 87.22           C  
ATOM     60  O   ASP A 342       5.190   1.142  30.730  1.00 86.67           O  
ATOM     61  CB  ASP A 342       4.980  -2.005  30.935  1.00 89.73           C  
ATOM     62  CG  ASP A 342       3.517  -1.921  31.275  1.00 89.54           C  
ATOM     63  OD1 ASP A 342       3.174  -2.071  32.461  1.00 90.98           O  
ATOM     64  OD2 ASP A 342       2.707  -1.704  30.355  1.00 87.38           O  
ATOM     65  N   THR A 343       4.451   0.691  32.794  1.00 85.50           N  
ATOM     66  CA  THR A 343       3.783   1.974  32.921  1.00 83.97           C  
ATOM     67  C   THR A 343       4.899   2.998  32.990  1.00 82.58           C  
ATOM     68  O   THR A 343       4.743   4.148  32.590  1.00 82.17           O  
ATOM     69  CB  THR A 343       2.958   2.059  34.206  1.00 83.96           C  
ATOM     70  OG1 THR A 343       3.831   2.065  35.334  1.00 85.11           O  
ATOM     71  CG2 THR A 343       2.029   0.879  34.307  1.00 83.93           C  
ATOM     72  N   LYS A 344       6.037   2.551  33.502  1.00 81.10           N  
ATOM     73  CA  LYS A 344       7.214   3.386  33.624  1.00 79.67           C  
ATOM     74  C   LYS A 344       7.709   3.738  32.227  1.00 77.19           C  
ATOM     75  O   LYS A 344       8.014   4.893  31.946  1.00 77.58           O  
ATOM     76  CB  LYS A 344       8.305   2.632  34.395  1.00 82.13           C  
ATOM     77  CG  LYS A 344       9.558   3.441  34.719  1.00 84.11           C  
ATOM     78  CD  LYS A 344       9.269   4.538  35.737  1.00 87.28           C  
ATOM     79  CE  LYS A 344      10.532   5.307  36.109  1.00 88.29           C  
ATOM     80  NZ  LYS A 344      11.152   5.968  34.923  1.00 89.14           N  
ATOM     81  N   VAL A 345       7.781   2.745  31.348  1.00 73.96           N  
ATOM     82  CA  VAL A 345       8.252   2.989  29.992  1.00 71.83           C  
ATOM     83  C   VAL A 345       7.193   3.663  29.128  1.00 69.46           C  
ATOM     84  O   VAL A 345       7.515   4.394  28.197  1.00 68.71           O  
ATOM     85  CB  VAL A 345       8.731   1.679  29.295  1.00 72.03           C  
ATOM     86  CG1 VAL A 345       9.882   1.068  30.074  1.00 72.23           C  
ATOM     87  CG2 VAL A 345       7.596   0.698  29.166  1.00 72.98           C  
ATOM     88  N   ARG A 346       5.926   3.416  29.433  1.00 67.85           N  
ATOM     89  CA  ARG A 346       4.840   4.031  28.681  1.00 65.58           C  
ATOM     90  C   ARG A 346       4.846   5.530  28.945  1.00 63.93           C  
ATOM     91  O   ARG A 346       4.614   6.326  28.041  1.00 63.28           O  
ATOM     92  CB  ARG A 346       3.494   3.448  29.097  1.00 66.91           C  
ATOM     93  CG  ARG A 346       3.207   2.079  28.532  1.00 68.33           C  
ATOM     94  CD  ARG A 346       1.891   1.530  29.061  1.00 69.63           C  
ATOM     95  NE  ARG A 346       1.557   0.259  28.429  1.00 72.39           N  
ATOM     96  CZ  ARG A 346       1.212   0.129  27.153  1.00 72.69           C  
ATOM     97  NH1 ARG A 346       1.149   1.192  26.370  1.00 73.22           N  
ATOM     98  NH2 ARG A 346       0.944  -1.067  26.655  1.00 73.28           N  
ATOM     99  N   LYS A 347       5.107   5.907  30.193  1.00 61.10           N  
ATOM    100  CA  LYS A 347       5.165   7.308  30.559  1.00 58.56           C  
ATOM    101  C   LYS A 347       6.372   7.979  29.928  1.00 58.90           C  
ATOM    102  O   LYS A 347       6.298   9.134  29.510  1.00 59.52           O  
ATOM    103  CB  LYS A 347       5.220   7.466  32.072  1.00 55.90           C  
ATOM    104  CG  LYS A 347       3.909   7.150  32.737  1.00 54.20           C  
ATOM    105  CD  LYS A 347       3.884   7.586  34.179  1.00 52.08           C  
ATOM    106  CE  LYS A 347       2.502   7.402  34.753  1.00 50.14           C  
ATOM    107  NZ  LYS A 347       2.433   7.833  36.160  1.00 49.47           N  
ATOM    108  N   GLN A 348       7.489   7.265  29.861  1.00 58.96           N  
ATOM    109  CA  GLN A 348       8.679   7.832  29.251  1.00 59.88           C  
ATOM    110  C   GLN A 348       8.394   8.024  27.771  1.00 59.14           C  
ATOM    111  O   GLN A 348       8.915   8.937  27.140  1.00 59.52           O  
ATOM    112  CB  GLN A 348       9.889   6.913  29.441  1.00 61.35           C  
ATOM    113  CG  GLN A 348      11.164   7.462  28.800  1.00 64.25           C  
ATOM    114  CD  GLN A 348      11.585   8.815  29.373  1.00 66.35           C  
ATOM    115  OE1 GLN A 348      12.211   9.634  28.680  1.00 65.67           O  
ATOM    116  NE2 GLN A 348      11.254   9.051  30.645  1.00 66.43           N  
ATOM    117  N   GLU A 349       7.557   7.146  27.229  1.00 59.20           N  
ATOM    118  CA  GLU A 349       7.153   7.198  25.831  1.00 58.45           C  
ATOM    119  C   GLU A 349       6.438   8.538  25.614  1.00 57.00           C  
ATOM    120  O   GLU A 349       6.749   9.284  24.690  1.00 57.10           O  
ATOM    121  CB  GLU A 349       6.216   6.018  25.551  1.00 61.59           C  
ATOM    122  CG  GLU A 349       5.291   6.162  24.349  1.00 65.62           C  
ATOM    123  CD  GLU A 349       5.928   5.739  23.047  1.00 67.45           C  
ATOM    124  OE1 GLU A 349       6.915   6.379  22.622  1.00 68.29           O  
ATOM    125  OE2 GLU A 349       5.430   4.756  22.452  1.00 69.61           O  
ATOM    126  N   ILE A 350       5.491   8.843  26.491  1.00 54.84           N  
ATOM    127  CA  ILE A 350       4.751  10.091  26.402  1.00 53.91           C  
ATOM    128  C   ILE A 350       5.663  11.304  26.597  1.00 52.93           C  
ATOM    129  O   ILE A 350       5.511  12.312  25.915  1.00 52.52           O  
ATOM    130  CB  ILE A 350       3.581  10.121  27.427  1.00 52.17           C  
ATOM    131  CG1 ILE A 350       2.314   9.537  26.800  1.00 52.39           C  
ATOM    132  CG2 ILE A 350       3.262  11.547  27.824  1.00 52.86           C  
ATOM    133  CD1 ILE A 350       2.500   8.254  26.059  1.00 54.32           C  
ATOM    134  N   ILE A 351       6.609  11.214  27.523  1.00 52.83           N  
ATOM    135  CA  ILE A 351       7.522  12.327  27.753  1.00 52.58           C  
ATOM    136  C   ILE A 351       8.375  12.579  26.520  1.00 53.40           C  
ATOM    137  O   ILE A 351       8.694  13.726  26.206  1.00 53.69           O  
ATOM    138  CB  ILE A 351       8.443  12.079  28.968  1.00 51.93           C  
ATOM    139  CG1 ILE A 351       7.624  12.187  30.254  1.00 52.60           C  
ATOM    140  CG2 ILE A 351       9.588  13.086  28.986  1.00 48.50           C  
ATOM    141  CD1 ILE A 351       8.439  12.057  31.527  1.00 53.74           C  
ATOM    142  N   LYS A 352       8.725  11.515  25.805  1.00 53.61           N  
ATOM    143  CA  LYS A 352       9.547  11.657  24.609  1.00 54.65           C  
ATOM    144  C   LYS A 352       8.819  12.373  23.471  1.00 52.66           C  
ATOM    145  O   LYS A 352       9.389  13.247  22.826  1.00 51.95           O  
ATOM    146  CB  LYS A 352      10.050  10.283  24.141  1.00 56.91           C  
ATOM    147  CG  LYS A 352      10.874  10.333  22.870  1.00 61.40           C  
ATOM    148  CD  LYS A 352      11.805   9.133  22.730  1.00 66.19           C  
ATOM    149  CE  LYS A 352      12.958   9.190  23.757  1.00 69.99           C  
ATOM    150  NZ  LYS A 352      13.911   8.033  23.658  1.00 69.77           N  
ATOM    151  N   VAL A 353       7.563  12.011  23.228  1.00 51.62           N  
ATOM    152  CA  VAL A 353       6.803  12.651  22.163  1.00 50.18           C  
ATOM    153  C   VAL A 353       6.524  14.102  22.508  1.00 48.82           C  
ATOM    154  O   VAL A 353       6.490  14.959  21.627  1.00 48.68           O  
ATOM    155  CB  VAL A 353       5.471  11.914  21.870  1.00 50.12           C  
ATOM    156  CG1 VAL A 353       5.768  10.556  21.267  1.00 48.74           C  
ATOM    157  CG2 VAL A 353       4.644  11.772  23.137  1.00 49.67           C  
ATOM    158  N   THR A 354       6.330  14.380  23.792  1.00 47.87           N  
ATOM    159  CA  THR A 354       6.087  15.747  24.231  1.00 46.69           C  
ATOM    160  C   THR A 354       7.344  16.576  23.972  1.00 46.96           C  
ATOM    161  O   THR A 354       7.268  17.711  23.501  1.00 45.86           O  
ATOM    162  CB  THR A 354       5.731  15.793  25.709  1.00 45.75           C  
ATOM    163  OG1 THR A 354       4.574  14.984  25.935  1.00 46.60           O  
ATOM    164  CG2 THR A 354       5.421  17.223  26.141  1.00 44.66           C  
ATOM    165  N   GLU A 355       8.502  15.994  24.268  1.00 47.87           N  
ATOM    166  CA  GLU A 355       9.781  16.661  24.031  1.00 49.09           C  
ATOM    167  C   GLU A 355       9.961  16.887  22.542  1.00 49.00           C  
ATOM    168  O   GLU A 355      10.427  17.939  22.111  1.00 48.74           O  
ATOM    169  CB  GLU A 355      10.935  15.809  24.548  1.00 49.82           C  
ATOM    170  CG  GLU A 355      11.371  16.146  25.955  1.00 53.65           C  
ATOM    171  CD  GLU A 355      12.074  14.987  26.639  1.00 56.44           C  
ATOM    172  OE1 GLU A 355      12.693  14.162  25.930  1.00 56.56           O  
ATOM    173  OE2 GLU A 355      12.012  14.910  27.888  1.00 58.60           O  
ATOM    174  N   GLN A 356       9.590  15.886  21.755  1.00 49.46           N  
ATOM    175  CA  GLN A 356       9.705  15.985  20.309  1.00 50.61           C  
ATOM    176  C   GLN A 356       8.797  17.094  19.789  1.00 50.28           C  
ATOM    177  O   GLN A 356       9.199  17.893  18.942  1.00 50.10           O  
ATOM    178  CB  GLN A 356       9.335  14.650  19.670  1.00 52.86           C  
ATOM    179  CG  GLN A 356      10.429  13.603  19.770  1.00 56.20           C  
ATOM    180  CD  GLN A 356       9.950  12.224  19.365  1.00 59.63           C  
ATOM    181  OE1 GLN A 356       9.223  12.064  18.378  1.00 63.01           O  
ATOM    182  NE2 GLN A 356      10.358  11.217  20.117  1.00 60.37           N  
ATOM    183  N   LEU A 357       7.576  17.142  20.311  1.00 49.70           N  
ATOM    184  CA  LEU A 357       6.610  18.156  19.920  1.00 48.86           C  
ATOM    185  C   LEU A 357       7.175  19.544  20.218  1.00 50.22           C  
ATOM    186  O   LEU A 357       7.160  20.441  19.370  1.00 49.43           O  
ATOM    187  CB  LEU A 357       5.315  17.969  20.699  1.00 48.31           C  
ATOM    188  CG  LEU A 357       4.234  19.000  20.378  1.00 47.29           C  
ATOM    189  CD1 LEU A 357       3.515  18.610  19.100  1.00 47.56           C  
ATOM    190  CD2 LEU A 357       3.264  19.084  21.542  1.00 46.02           C  
ATOM    191  N   ILE A 358       7.673  19.720  21.435  1.00 50.65           N  
ATOM    192  CA  ILE A 358       8.231  21.000  21.828  1.00 51.85           C  
ATOM    193  C   ILE A 358       9.418  21.393  20.949  1.00 53.87           C  
ATOM    194  O   ILE A 358       9.583  22.570  20.613  1.00 53.62           O  
ATOM    195  CB  ILE A 358       8.650  20.987  23.311  1.00 51.16           C  
ATOM    196  CG1 ILE A 358       7.398  20.894  24.187  1.00 51.25           C  
ATOM    197  CG2 ILE A 358       9.454  22.231  23.639  1.00 48.66           C  
ATOM    198  CD1 ILE A 358       7.679  20.823  25.670  1.00 53.15           C  
ATOM    199  N   GLU A 359      10.239  20.421  20.565  1.00 55.31           N  
ATOM    200  CA  GLU A 359      11.390  20.718  19.716  1.00 58.29           C  
ATOM    201  C   GLU A 359      10.935  21.204  18.349  1.00 58.24           C  
ATOM    202  O   GLU A 359      11.494  22.156  17.801  1.00 56.73           O  
ATOM    203  CB  GLU A 359      12.271  19.485  19.546  1.00 61.87           C  
ATOM    204  CG  GLU A 359      13.052  19.111  20.797  1.00 69.04           C  
ATOM    205  CD  GLU A 359      13.936  17.881  20.591  1.00 72.61           C  
ATOM    206  OE1 GLU A 359      14.755  17.901  19.636  1.00 74.95           O  
ATOM    207  OE2 GLU A 359      13.814  16.906  21.380  1.00 71.92           O  
ATOM    208  N   ALA A 360       9.920  20.541  17.801  1.00 58.05           N  
ATOM    209  CA  ALA A 360       9.388  20.924  16.505  1.00 57.81           C  
ATOM    210  C   ALA A 360       8.872  22.353  16.608  1.00 58.35           C  
ATOM    211  O   ALA A 360       9.158  23.180  15.744  1.00 59.22           O  
ATOM    212  CB  ALA A 360       8.270  19.984  16.101  1.00 57.13           C  
ATOM    213  N   ILE A 361       8.118  22.643  17.668  1.00 58.39           N  
ATOM    214  CA  ILE A 361       7.584  23.983  17.873  1.00 59.44           C  
ATOM    215  C   ILE A 361       8.740  24.964  17.975  1.00 61.42           C  
ATOM    216  O   ILE A 361       8.773  25.990  17.298  1.00 62.23           O  
ATOM    217  CB  ILE A 361       6.778  24.086  19.181  1.00 58.01           C  
ATOM    218  CG1 ILE A 361       5.522  23.224  19.096  1.00 56.60           C  
ATOM    219  CG2 ILE A 361       6.422  25.537  19.453  1.00 56.62           C  
ATOM    220  CD1 ILE A 361       4.782  23.111  20.398  1.00 54.32           C  
ATOM    221  N   SER A 362       9.697  24.628  18.828  1.00 63.29           N  
ATOM    222  CA  SER A 362      10.856  25.475  19.057  1.00 65.08           C  
ATOM    223  C   SER A 362      11.696  25.740  17.810  1.00 65.30           C  
ATOM    224  O   SER A 362      12.351  26.774  17.711  1.00 66.03           O  
ATOM    225  CB  SER A 362      11.723  24.855  20.151  1.00 65.48           C  
ATOM    226  OG  SER A 362      12.712  25.762  20.585  1.00 68.07           O  
ATOM    227  N   ASN A 363      11.685  24.816  16.859  1.00 66.35           N  
ATOM    228  CA  ASN A 363      12.467  25.002  15.641  1.00 67.85           C  
ATOM    229  C   ASN A 363      11.629  25.508  14.480  1.00 68.46           C  
ATOM    230  O   ASN A 363      12.104  25.565  13.350  1.00 69.29           O  
ATOM    231  CB  ASN A 363      13.148  23.697  15.226  1.00 68.60           C  
ATOM    232  CG  ASN A 363      14.144  23.200  16.256  1.00 70.29           C  
ATOM    233  OD1 ASN A 363      14.739  23.987  16.992  1.00 70.94           O  
ATOM    234  ND2 ASN A 363      14.346  21.887  16.299  1.00 71.05           N  
ATOM    235  N   GLY A 364      10.381  25.870  14.757  1.00 69.34           N  
ATOM    236  CA  GLY A 364       9.500  26.362  13.710  1.00 69.66           C  
ATOM    237  C   GLY A 364       9.248  25.346  12.607  1.00 69.72           C  
ATOM    238  O   GLY A 364       8.938  25.712  11.473  1.00 70.28           O  
ATOM    239  N   ASP A 365       9.377  24.065  12.938  1.00 68.68           N  
ATOM    240  CA  ASP A 365       9.168  22.996  11.969  1.00 67.82           C  
ATOM    241  C   ASP A 365       7.699  22.580  11.926  1.00 67.55           C  
ATOM    242  O   ASP A 365       7.304  21.599  12.553  1.00 67.26           O  
ATOM    243  CB  ASP A 365      10.041  21.806  12.346  1.00 68.13           C  
ATOM    244  CG  ASP A 365       9.915  20.661  11.378  1.00 68.20           C  
ATOM    245  OD1 ASP A 365      10.638  19.665  11.559  1.00 69.93           O  
ATOM    246  OD2 ASP A 365       9.099  20.747  10.443  1.00 69.53           O  
ATOM    247  N   PHE A 366       6.900  23.322  11.166  1.00 67.18           N  
ATOM    248  CA  PHE A 366       5.470  23.056  11.058  1.00 68.02           C  
ATOM    249  C   PHE A 366       5.095  21.687  10.483  1.00 68.40           C  
ATOM    250  O   PHE A 366       4.054  21.129  10.832  1.00 67.74           O  
ATOM    251  CB  PHE A 366       4.802  24.152  10.230  1.00 68.39           C  
ATOM    252  CG  PHE A 366       3.301  24.127  10.294  1.00 68.93           C  
ATOM    253  CD1 PHE A 366       2.638  24.377  11.493  1.00 68.84           C  
ATOM    254  CD2 PHE A 366       2.547  23.875   9.152  1.00 69.05           C  
ATOM    255  CE1 PHE A 366       1.243  24.380  11.554  1.00 69.84           C  
ATOM    256  CE2 PHE A 366       1.155  23.876   9.202  1.00 69.99           C  
ATOM    257  CZ  PHE A 366       0.499  24.130  10.408  1.00 69.65           C  
ATOM    258  N   GLU A 367       5.926  21.151   9.597  1.00 69.00           N  
ATOM    259  CA  GLU A 367       5.642  19.848   9.005  1.00 70.63           C  
ATOM    260  C   GLU A 367       5.627  18.761  10.067  1.00 69.63           C  
ATOM    261  O   GLU A 367       4.680  17.982  10.152  1.00 69.43           O  
ATOM    262  CB  GLU A 367       6.676  19.489   7.934  1.00 74.21           C  
ATOM    263  CG  GLU A 367       6.413  20.106   6.560  1.00 78.55           C  
ATOM    264  CD  GLU A 367       6.726  21.598   6.499  1.00 81.90           C  
ATOM    265  OE1 GLU A 367       6.438  22.221   5.452  1.00 82.80           O  
ATOM    266  OE2 GLU A 367       7.266  22.147   7.489  1.00 83.98           O  
ATOM    267  N   SER A 368       6.684  18.703  10.870  1.00 68.06           N  
ATOM    268  CA  SER A 368       6.765  17.714  11.937  1.00 66.19           C  
ATOM    269  C   SER A 368       5.618  17.932  12.917  1.00 65.29           C  
ATOM    270  O   SER A 368       5.024  16.978  13.429  1.00 65.28           O  
ATOM    271  CB  SER A 368       8.090  17.849  12.673  1.00 65.97           C  
ATOM    272  OG  SER A 368       9.165  17.652  11.781  1.00 67.85           O  
ATOM    273  N   TYR A 369       5.311  19.199  13.173  1.00 63.53           N  
ATOM    274  CA  TYR A 369       4.239  19.552  14.088  1.00 62.07           C  
ATOM    275  C   TYR A 369       2.912  18.940  13.647  1.00 62.74           C  
ATOM    276  O   TYR A 369       2.285  18.203  14.409  1.00 62.71           O  
ATOM    277  CB  TYR A 369       4.098  21.070  14.170  1.00 60.39           C  
ATOM    278  CG  TYR A 369       3.102  21.527  15.209  1.00 59.58           C  
ATOM    279  CD1 TYR A 369       3.340  21.319  16.568  1.00 59.54           C  
ATOM    280  CD2 TYR A 369       1.914  22.151  14.839  1.00 57.96           C  
ATOM    281  CE1 TYR A 369       2.421  21.719  17.528  1.00 58.08           C  
ATOM    282  CE2 TYR A 369       0.990  22.553  15.791  1.00 57.19           C  
ATOM    283  CZ  TYR A 369       1.249  22.334  17.131  1.00 57.70           C  
ATOM    284  OH  TYR A 369       0.327  22.728  18.072  1.00 59.09           O  
ATOM    285  N   THR A 370       2.491  19.242  12.418  1.00 62.38           N  
ATOM    286  CA  THR A 370       1.228  18.724  11.899  1.00 63.25           C  
ATOM    287  C   THR A 370       1.207  17.204  11.929  1.00 63.34           C  
ATOM    288  O   THR A 370       0.169  16.585  12.161  1.00 64.55           O  
ATOM    289  CB  THR A 370       0.973  19.178  10.450  1.00 63.77           C  
ATOM    290  OG1 THR A 370       1.966  18.612   9.593  1.00 65.94           O  
ATOM    291  CG2 THR A 370       1.026  20.692  10.343  1.00 63.85           C  
ATOM    292  N   LYS A 371       2.367  16.613  11.690  1.00 62.81           N  
ATOM    293  CA  LYS A 371       2.519  15.170  11.695  1.00 62.19           C  
ATOM    294  C   LYS A 371       2.145  14.638  13.083  1.00 60.67           C  
ATOM    295  O   LYS A 371       1.614  13.536  13.218  1.00 61.00           O  
ATOM    296  CB  LYS A 371       3.977  14.830  11.360  1.00 64.73           C  
ATOM    297  CG  LYS A 371       4.191  13.768  10.286  1.00 68.12           C  
ATOM    298  CD  LYS A 371       4.037  12.354  10.864  1.00 71.47           C  
ATOM    299  CE  LYS A 371       4.509  11.283   9.880  1.00 72.53           C  
ATOM    300  NZ  LYS A 371       4.509   9.920  10.487  1.00 72.77           N  
ATOM    301  N   MET A 372       2.399  15.445  14.109  1.00 58.40           N  
ATOM    302  CA  MET A 372       2.119  15.052  15.485  1.00 56.19           C  
ATOM    303  C   MET A 372       0.758  15.471  16.016  1.00 55.25           C  
ATOM    304  O   MET A 372       0.389  15.112  17.136  1.00 55.35           O  
ATOM    305  CB  MET A 372       3.197  15.608  16.407  1.00 56.77           C  
ATOM    306  CG  MET A 372       4.597  15.141  16.077  1.00 57.59           C  
ATOM    307  SD  MET A 372       5.828  15.828  17.183  1.00 60.33           S  
ATOM    308  CE  MET A 372       6.662  16.925  16.118  1.00 57.47           C  
ATOM    309  N   CYS A 373       0.007  16.226  15.226  1.00 53.59           N  
ATOM    310  CA  CYS A 373      -1.308  16.676  15.669  1.00 53.09           C  
ATOM    311  C   CYS A 373      -2.456  16.031  14.906  1.00 52.74           C  
ATOM    312  O   CYS A 373      -2.364  15.796  13.701  1.00 53.42           O  
ATOM    313  CB  CYS A 373      -1.435  18.191  15.517  1.00 53.65           C  
ATOM    314  SG  CYS A 373      -0.234  19.179  16.400  1.00 54.39           S  
ATOM    315  N   ASP A 374      -3.542  15.752  15.616  1.00 52.09           N  
ATOM    316  CA  ASP A 374      -4.730  15.183  14.996  1.00 51.43           C  
ATOM    317  C   ASP A 374      -5.373  16.332  14.221  1.00 51.84           C  
ATOM    318  O   ASP A 374      -5.398  17.470  14.687  1.00 51.02           O  
ATOM    319  CB  ASP A 374      -5.686  14.670  16.069  1.00 50.73           C  
ATOM    320  CG  ASP A 374      -6.988  14.165  15.493  1.00 52.44           C  
ATOM    321  OD1 ASP A 374      -7.392  13.032  15.842  1.00 52.48           O  
ATOM    322  OD2 ASP A 374      -7.613  14.902  14.700  1.00 51.06           O  
ATOM    323  N   PRO A 375      -5.895  16.057  13.020  1.00 52.47           N  
ATOM    324  CA  PRO A 375      -6.523  17.117  12.216  1.00 51.75           C  
ATOM    325  C   PRO A 375      -7.600  17.908  12.961  1.00 51.67           C  
ATOM    326  O   PRO A 375      -7.756  19.116  12.750  1.00 51.38           O  
ATOM    327  CB  PRO A 375      -7.088  16.352  11.027  1.00 51.24           C  
ATOM    328  CG  PRO A 375      -6.104  15.219  10.878  1.00 51.92           C  
ATOM    329  CD  PRO A 375      -5.912  14.770  12.301  1.00 51.43           C  
ATOM    330  N   GLY A 376      -8.340  17.217  13.826  1.00 50.89           N  
ATOM    331  CA  GLY A 376      -9.395  17.861  14.589  1.00 49.79           C  
ATOM    332  C   GLY A 376      -8.911  18.320  15.951  1.00 49.74           C  
ATOM    333  O   GLY A 376      -9.676  18.377  16.919  1.00 49.93           O  
ATOM    334  N   MET A 377      -7.626  18.651  16.018  1.00 48.67           N  
ATOM    335  CA  MET A 377      -7.008  19.115  17.251  1.00 48.33           C  
ATOM    336  C   MET A 377      -7.675  20.377  17.782  1.00 46.60           C  
ATOM    337  O   MET A 377      -7.984  21.301  17.041  1.00 46.94           O  
ATOM    338  CB  MET A 377      -5.525  19.386  17.021  1.00 49.55           C  
ATOM    339  CG  MET A 377      -4.794  19.872  18.247  1.00 50.89           C  
ATOM    340  SD  MET A 377      -3.330  20.762  17.747  1.00 55.21           S  
ATOM    341  CE  MET A 377      -2.158  20.131  18.863  1.00 55.73           C  
ATOM    342  N   THR A 378      -7.871  20.404  19.088  1.00 44.95           N  
ATOM    343  CA  THR A 378      -8.505  21.519  19.760  1.00 42.44           C  
ATOM    344  C   THR A 378      -7.480  22.212  20.689  1.00 40.70           C  
ATOM    345  O   THR A 378      -6.556  21.566  21.181  1.00 41.24           O  
ATOM    346  CB  THR A 378      -9.733  20.960  20.511  1.00 42.66           C  
ATOM    347  OG1 THR A 378     -10.917  21.408  19.850  1.00 44.22           O  
ATOM    348  CG2 THR A 378      -9.757  21.370  21.953  1.00 43.50           C  
ATOM    349  N   ALA A 379      -7.619  23.518  20.915  1.00 37.74           N  
ATOM    350  CA  ALA A 379      -6.664  24.218  21.777  1.00 36.33           C  
ATOM    351  C   ALA A 379      -7.130  25.484  22.499  1.00 36.84           C  
ATOM    352  O   ALA A 379      -7.962  26.249  22.013  1.00 37.35           O  
ATOM    353  CB  ALA A 379      -5.387  24.545  20.983  1.00 33.45           C  
ATOM    354  N   PHE A 380      -6.556  25.679  23.679  1.00 36.65           N  
ATOM    355  CA  PHE A 380      -6.779  26.847  24.526  1.00 33.74           C  
ATOM    356  C   PHE A 380      -5.375  27.410  24.742  1.00 34.17           C  
ATOM    357  O   PHE A 380      -4.472  26.694  25.163  1.00 32.64           O  
ATOM    358  CB  PHE A 380      -7.349  26.428  25.868  1.00 31.48           C  
ATOM    359  CG  PHE A 380      -8.839  26.417  25.927  1.00 31.07           C  
ATOM    360  CD1 PHE A 380      -9.502  25.448  26.673  1.00 32.34           C  
ATOM    361  CD2 PHE A 380      -9.591  27.391  25.281  1.00 31.18           C  
ATOM    362  CE1 PHE A 380     -10.897  25.448  26.778  1.00 31.81           C  
ATOM    363  CE2 PHE A 380     -10.985  27.402  25.379  1.00 28.41           C  
ATOM    364  CZ  PHE A 380     -11.637  26.431  26.127  1.00 30.14           C  
ATOM    365  N   GLU A 381      -5.177  28.676  24.424  1.00 36.25           N  
ATOM    366  CA  GLU A 381      -3.867  29.290  24.601  1.00 39.03           C  
ATOM    367  C   GLU A 381      -3.990  30.815  24.579  1.00 40.02           C  
ATOM    368  O   GLU A 381      -4.899  31.372  23.966  1.00 39.16           O  
ATOM    369  CB  GLU A 381      -2.898  28.819  23.508  1.00 39.72           C  
ATOM    370  CG  GLU A 381      -3.244  29.306  22.115  1.00 43.22           C  
ATOM    371  CD  GLU A 381      -2.263  28.822  21.076  1.00 46.92           C  
ATOM    372  OE1 GLU A 381      -2.322  29.296  19.936  1.00 51.15           O  
ATOM    373  OE2 GLU A 381      -1.421  27.964  21.385  1.00 52.13           O  
ATOM    374  N   PRO A 382      -3.072  31.509  25.263  1.00 40.41           N  
ATOM    375  CA  PRO A 382      -3.093  32.971  25.318  1.00 39.51           C  
ATOM    376  C   PRO A 382      -3.287  33.645  23.966  1.00 39.16           C  
ATOM    377  O   PRO A 382      -4.019  34.619  23.854  1.00 38.45           O  
ATOM    378  CB  PRO A 382      -1.744  33.306  25.944  1.00 39.56           C  
ATOM    379  CG  PRO A 382      -1.518  32.158  26.866  1.00 40.00           C  
ATOM    380  CD  PRO A 382      -1.923  30.972  26.019  1.00 40.08           C  
ATOM    381  N   GLU A 383      -2.635  33.124  22.938  1.00 40.06           N  
ATOM    382  CA  GLU A 383      -2.737  33.719  21.611  1.00 41.74           C  
ATOM    383  C   GLU A 383      -4.150  33.647  21.021  1.00 41.64           C  
ATOM    384  O   GLU A 383      -4.464  34.374  20.084  1.00 42.55           O  
ATOM    385  CB  GLU A 383      -1.737  33.058  20.647  1.00 43.14           C  
ATOM    386  CG  GLU A 383      -0.282  33.154  21.084  1.00 47.60           C  
ATOM    387  CD  GLU A 383       0.174  31.964  21.910  1.00 51.64           C  
ATOM    388  OE1 GLU A 383      -0.507  31.594  22.894  1.00 53.43           O  
ATOM    389  OE2 GLU A 383       1.227  31.393  21.574  1.00 55.46           O  
ATOM    390  N   ALA A 384      -4.997  32.775  21.568  1.00 40.23           N  
ATOM    391  CA  ALA A 384      -6.362  32.610  21.080  1.00 37.30           C  
ATOM    392  C   ALA A 384      -7.389  33.470  21.826  1.00 37.16           C  
ATOM    393  O   ALA A 384      -8.599  33.314  21.650  1.00 35.21           O  
ATOM    394  CB  ALA A 384      -6.754  31.143  21.144  1.00 37.27           C  
ATOM    395  N   LEU A 385      -6.895  34.360  22.677  1.00 37.56           N  
ATOM    396  CA  LEU A 385      -7.736  35.291  23.424  1.00 37.78           C  
ATOM    397  C   LEU A 385      -8.981  34.734  24.098  1.00 38.54           C  
ATOM    398  O   LEU A 385     -10.063  35.313  23.981  1.00 40.58           O  
ATOM    399  CB  LEU A 385      -8.155  36.427  22.492  1.00 38.18           C  
ATOM    400  CG  LEU A 385      -6.995  37.110  21.762  1.00 39.88           C  
ATOM    401  CD1 LEU A 385      -7.533  38.066  20.720  1.00 38.96           C  
ATOM    402  CD2 LEU A 385      -6.116  37.845  22.776  1.00 37.62           C  
ATOM    403  N   GLY A 386      -8.845  33.625  24.807  1.00 38.96           N  
ATOM    404  CA  GLY A 386      -9.999  33.065  25.482  1.00 38.07           C  
ATOM    405  C   GLY A 386     -10.920  32.226  24.620  1.00 38.19           C  
ATOM    406  O   GLY A 386     -11.946  31.760  25.111  1.00 39.46           O  
ATOM    407  N   ASN A 387     -10.572  32.030  23.352  1.00 37.22           N  
ATOM    408  CA  ASN A 387     -11.390  31.213  22.454  1.00 37.93           C  
ATOM    409  C   ASN A 387     -10.809  29.812  22.266  1.00 39.58           C  
ATOM    410  O   ASN A 387      -9.591  29.623  22.291  1.00 40.99           O  
ATOM    411  CB  ASN A 387     -11.497  31.879  21.077  1.00 36.83           C  
ATOM    412  CG  ASN A 387     -12.181  33.232  21.133  1.00 37.20           C  
ATOM    413  OD1 ASN A 387     -13.376  33.328  21.439  1.00 33.19           O  
ATOM    414  ND2 ASN A 387     -11.423  34.291  20.843  1.00 34.66           N  
ATOM    415  N   LEU A 388     -11.683  28.828  22.084  1.00 40.96           N  
ATOM    416  CA  LEU A 388     -11.246  27.463  21.829  1.00 42.52           C  
ATOM    417  C   LEU A 388     -11.015  27.386  20.324  1.00 43.50           C  
ATOM    418  O   LEU A 388     -11.940  27.585  19.547  1.00 44.28           O  
ATOM    419  CB  LEU A 388     -12.329  26.469  22.230  1.00 42.80           C  
ATOM    420  CG  LEU A 388     -11.824  25.049  22.517  1.00 47.02           C  
ATOM    421  CD1 LEU A 388     -13.005  24.134  22.762  1.00 48.78           C  
ATOM    422  CD2 LEU A 388     -11.006  24.523  21.350  1.00 47.73           C  
ATOM    423  N   VAL A 389      -9.781  27.117  19.915  1.00 45.08           N  
ATOM    424  CA  VAL A 389      -9.438  27.040  18.501  1.00 47.67           C  
ATOM    425  C   VAL A 389      -9.377  25.598  17.969  1.00 50.08           C  
ATOM    426  O   VAL A 389      -9.007  24.679  18.705  1.00 49.26           O  
ATOM    427  CB  VAL A 389      -8.093  27.739  18.262  1.00 46.25           C  
ATOM    428  CG1 VAL A 389      -7.623  27.516  16.852  1.00 49.21           C  
ATOM    429  CG2 VAL A 389      -8.250  29.209  18.498  1.00 48.45           C  
ATOM    430  N   GLU A 390      -9.753  25.405  16.698  1.00 52.92           N  
ATOM    431  CA  GLU A 390      -9.729  24.072  16.062  1.00 54.62           C  
ATOM    432  C   GLU A 390      -8.770  24.000  14.896  1.00 54.28           C  
ATOM    433  O   GLU A 390      -8.523  25.000  14.227  1.00 56.07           O  
ATOM    434  CB  GLU A 390     -11.094  23.675  15.515  1.00 55.99           C  
ATOM    435  CG  GLU A 390     -12.127  23.296  16.534  1.00 62.01           C  
ATOM    436  CD  GLU A 390     -13.296  22.559  15.891  1.00 65.76           C  
ATOM    437  OE1 GLU A 390     -13.090  21.404  15.433  1.00 65.20           O  
ATOM    438  OE2 GLU A 390     -14.411  23.140  15.835  1.00 67.69           O  
ATOM    439  N   GLY A 391      -8.254  22.804  14.641  1.00 53.73           N  
ATOM    440  CA  GLY A 391      -7.337  22.610  13.533  1.00 53.83           C  
ATOM    441  C   GLY A 391      -5.956  23.190  13.748  1.00 54.83           C  
ATOM    442  O   GLY A 391      -5.693  23.836  14.764  1.00 56.41           O  
ATOM    443  N   LEU A 392      -5.067  22.965  12.787  1.00 54.62           N  
ATOM    444  CA  LEU A 392      -3.705  23.466  12.883  1.00 55.59           C  
ATOM    445  C   LEU A 392      -3.552  24.785  12.158  1.00 56.11           C  
ATOM    446  O   LEU A 392      -2.541  25.465  12.280  1.00 56.40           O  
ATOM    447  CB  LEU A 392      -2.730  22.458  12.284  1.00 55.90           C  
ATOM    448  CG  LEU A 392      -2.685  21.097  12.966  1.00 56.19           C  
ATOM    449  CD1 LEU A 392      -3.871  20.273  12.563  1.00 56.53           C  
ATOM    450  CD2 LEU A 392      -1.418  20.400  12.569  1.00 58.07           C  
ATOM    451  N   ASP A 393      -4.574  25.141  11.401  1.00 57.77           N  
ATOM    452  CA  ASP A 393      -4.564  26.361  10.620  1.00 58.72           C  
ATOM    453  C   ASP A 393      -4.190  27.597  11.434  1.00 57.34           C  
ATOM    454  O   ASP A 393      -3.404  28.430  10.985  1.00 57.00           O  
ATOM    455  CB  ASP A 393      -5.936  26.533   9.977  1.00 63.06           C  
ATOM    456  CG  ASP A 393      -5.993  27.709   9.042  1.00 67.77           C  
ATOM    457  OD1 ASP A 393      -5.222  27.709   8.049  1.00 69.15           O  
ATOM    458  OD2 ASP A 393      -6.815  28.623   9.309  1.00 70.13           O  
ATOM    459  N   PHE A 394      -4.744  27.703  12.639  1.00 56.40           N  
ATOM    460  CA  PHE A 394      -4.487  28.841  13.518  1.00 53.25           C  
ATOM    461  C   PHE A 394      -3.047  28.912  14.008  1.00 52.87           C  
ATOM    462  O   PHE A 394      -2.514  29.993  14.259  1.00 53.57           O  
ATOM    463  CB  PHE A 394      -5.438  28.785  14.715  1.00 51.61           C  
ATOM    464  CG  PHE A 394      -5.266  29.921  15.688  1.00 49.68           C  
ATOM    465  CD1 PHE A 394      -4.427  29.785  16.797  1.00 48.85           C  
ATOM    466  CD2 PHE A 394      -5.938  31.123  15.495  1.00 45.96           C  
ATOM    467  CE1 PHE A 394      -4.265  30.835  17.698  1.00 48.53           C  
ATOM    468  CE2 PHE A 394      -5.788  32.173  16.379  1.00 46.29           C  
ATOM    469  CZ  PHE A 394      -4.952  32.038  17.488  1.00 48.57           C  
ATOM    470  N   HIS A 395      -2.413  27.758  14.131  1.00 51.40           N  
ATOM    471  CA  HIS A 395      -1.045  27.702  14.610  1.00 52.44           C  
ATOM    472  C   HIS A 395       0.015  27.968  13.537  1.00 54.48           C  
ATOM    473  O   HIS A 395       1.099  28.471  13.841  1.00 54.68           O  
ATOM    474  CB  HIS A 395      -0.815  26.346  15.268  1.00 49.44           C  
ATOM    475  CG  HIS A 395      -1.845  26.011  16.301  1.00 48.15           C  
ATOM    476  ND1 HIS A 395      -1.874  26.602  17.547  1.00 47.11           N  
ATOM    477  CD2 HIS A 395      -2.919  25.187  16.252  1.00 46.93           C  
ATOM    478  CE1 HIS A 395      -2.921  26.158  18.219  1.00 46.36           C  
ATOM    479  NE2 HIS A 395      -3.571  25.298  17.456  1.00 46.17           N  
ATOM    480  N   ARG A 396      -0.284  27.633  12.287  1.00 56.51           N  
ATOM    481  CA  ARG A 396       0.674  27.856  11.210  1.00 58.33           C  
ATOM    482  C   ARG A 396       1.218  29.285  11.222  1.00 59.03           C  
ATOM    483  O   ARG A 396       2.386  29.517  10.919  1.00 59.80           O  
ATOM    484  CB  ARG A 396       0.029  27.573   9.853  1.00 59.18           C  
ATOM    485  CG  ARG A 396       0.860  28.045   8.670  1.00 60.89           C  
ATOM    486  CD  ARG A 396       0.104  27.859   7.369  1.00 63.57           C  
ATOM    487  NE  ARG A 396       0.327  26.544   6.778  1.00 65.41           N  
ATOM    488  CZ  ARG A 396       1.469  26.173   6.201  1.00 66.74           C  
ATOM    489  NH1 ARG A 396       2.494  27.017   6.138  1.00 66.70           N  
ATOM    490  NH2 ARG A 396       1.586  24.959   5.679  1.00 66.77           N  
ATOM    491  N   PHE A 397       0.374  30.241  11.583  1.00 59.23           N  
ATOM    492  CA  PHE A 397       0.787  31.635  11.607  1.00 59.95           C  
ATOM    493  C   PHE A 397       2.065  31.894  12.400  1.00 61.45           C  
ATOM    494  O   PHE A 397       2.982  32.552  11.913  1.00 60.63           O  
ATOM    495  CB  PHE A 397      -0.331  32.502  12.177  1.00 59.95           C  
ATOM    496  CG  PHE A 397      -0.006  33.958  12.189  1.00 59.92           C  
ATOM    497  CD1 PHE A 397       0.098  34.668  10.994  1.00 60.50           C  
ATOM    498  CD2 PHE A 397       0.219  34.621  13.388  1.00 60.26           C  
ATOM    499  CE1 PHE A 397       0.425  36.024  10.986  1.00 61.14           C  
ATOM    500  CE2 PHE A 397       0.548  35.980  13.398  1.00 62.87           C  
ATOM    501  CZ  PHE A 397       0.652  36.686  12.187  1.00 62.25           C  
ATOM    502  N   TYR A 398       2.113  31.384  13.628  1.00 63.45           N  
ATOM    503  CA  TYR A 398       3.266  31.577  14.496  1.00 65.60           C  
ATOM    504  C   TYR A 398       4.492  30.803  14.046  1.00 66.91           C  
ATOM    505  O   TYR A 398       5.619  31.162  14.374  1.00 66.24           O  
ATOM    506  CB  TYR A 398       2.905  31.203  15.927  1.00 66.03           C  
ATOM    507  CG  TYR A 398       1.741  32.005  16.450  1.00 66.38           C  
ATOM    508  CD1 TYR A 398       0.443  31.492  16.416  1.00 66.77           C  
ATOM    509  CD2 TYR A 398       1.930  33.295  16.942  1.00 65.79           C  
ATOM    510  CE1 TYR A 398      -0.640  32.248  16.861  1.00 67.08           C  
ATOM    511  CE2 TYR A 398       0.858  34.060  17.386  1.00 66.24           C  
ATOM    512  CZ  TYR A 398      -0.423  33.531  17.343  1.00 66.64           C  
ATOM    513  OH  TYR A 398      -1.482  34.288  17.777  1.00 66.58           O  
ATOM    514  N   PHE A 399       4.274  29.732  13.299  1.00 69.25           N  
ATOM    515  CA  PHE A 399       5.390  28.962  12.787  1.00 71.94           C  
ATOM    516  C   PHE A 399       6.050  29.753  11.677  1.00 74.68           C  
ATOM    517  O   PHE A 399       7.237  30.060  11.737  1.00 75.02           O  
ATOM    518  CB  PHE A 399       4.918  27.619  12.234  1.00 69.77           C  
ATOM    519  CG  PHE A 399       4.802  26.562  13.269  1.00 67.97           C  
ATOM    520  CD1 PHE A 399       3.804  26.624  14.231  1.00 67.50           C  
ATOM    521  CD2 PHE A 399       5.713  25.516  13.308  1.00 67.97           C  
ATOM    522  CE1 PHE A 399       3.715  25.655  15.223  1.00 67.35           C  
ATOM    523  CE2 PHE A 399       5.635  24.539  14.295  1.00 67.35           C  
ATOM    524  CZ  PHE A 399       4.633  24.609  15.256  1.00 67.73           C  
ATOM    525  N   GLU A 400       5.260  30.093  10.667  1.00 78.05           N  
ATOM    526  CA  GLU A 400       5.760  30.828   9.523  1.00 81.93           C  
ATOM    527  C   GLU A 400       6.282  32.229   9.863  1.00 83.29           C  
ATOM    528  O   GLU A 400       7.136  32.758   9.156  1.00 83.70           O  
ATOM    529  CB  GLU A 400       4.665  30.918   8.460  1.00 83.56           C  
ATOM    530  CG  GLU A 400       5.184  31.001   7.028  1.00 87.21           C  
ATOM    531  CD  GLU A 400       4.062  31.161   6.008  1.00 89.31           C  
ATOM    532  OE1 GLU A 400       3.112  30.340   6.035  1.00 90.25           O  
ATOM    533  OE2 GLU A 400       4.131  32.105   5.182  1.00 89.12           O  
ATOM    534  N   ASN A 401       5.794  32.829  10.942  1.00 85.11           N  
ATOM    535  CA  ASN A 401       6.251  34.168  11.290  1.00 88.02           C  
ATOM    536  C   ASN A 401       7.162  34.232  12.496  1.00 90.48           C  
ATOM    537  O   ASN A 401       7.078  35.150  13.312  1.00 90.51           O  
ATOM    538  CB  ASN A 401       5.059  35.095  11.487  1.00 87.70           C  
ATOM    539  CG  ASN A 401       4.217  35.207  10.241  1.00 87.83           C  
ATOM    540  OD1 ASN A 401       3.378  34.350   9.966  1.00 88.31           O  
ATOM    541  ND2 ASN A 401       4.455  36.250   9.462  1.00 87.62           N  
ATOM    542  N   LEU A 402       8.044  33.247  12.586  1.00 93.90           N  
ATOM    543  CA  LEU A 402       9.015  33.148  13.664  1.00 97.18           C  
ATOM    544  C   LEU A 402      10.177  32.307  13.152  1.00 99.64           C  
ATOM    545  O   LEU A 402      10.379  31.166  13.577  1.00 99.12           O  
ATOM    546  CB  LEU A 402       8.386  32.498  14.897  1.00 97.36           C  
ATOM    547  CG  LEU A 402       7.373  33.319  15.701  1.00 97.85           C  
ATOM    548  CD1 LEU A 402       6.824  32.474  16.844  1.00 97.56           C  
ATOM    549  CD2 LEU A 402       8.042  34.579  16.236  1.00 97.29           C  
ATOM    550  N   TRP A 403      10.918  32.892  12.212  1.00102.99           N  
ATOM    551  CA  TRP A 403      12.077  32.259  11.588  1.00106.25           C  
ATOM    552  C   TRP A 403      13.372  32.781  12.197  1.00107.48           C  
ATOM    553  O   TRP A 403      14.297  32.013  12.465  1.00107.61           O  
ATOM    554  CB  TRP A 403      12.080  32.536  10.080  1.00108.02           C  
ATOM    555  CG  TRP A 403      11.054  31.760   9.302  1.00110.10           C  
ATOM    556  CD1 TRP A 403      10.571  32.060   8.054  1.00110.57           C  
ATOM    557  CD2 TRP A 403      10.405  30.541   9.701  1.00110.81           C  
ATOM    558  NE1 TRP A 403       9.663  31.105   7.655  1.00111.50           N  
ATOM    559  CE2 TRP A 403       9.542  30.162   8.645  1.00111.67           C  
ATOM    560  CE3 TRP A 403      10.469  29.731  10.846  1.00109.92           C  
ATOM    561  CZ2 TRP A 403       8.748  29.007   8.703  1.00111.38           C  
ATOM    562  CZ3 TRP A 403       9.683  28.588  10.901  1.00109.83           C  
ATOM    563  CH2 TRP A 403       8.833  28.237   9.836  1.00110.46           C  
ATOM    564  N   SER A 404      13.434  34.092  12.405  1.00108.65           N  
ATOM    565  CA  SER A 404      14.612  34.718  12.991  1.00109.75           C  
ATOM    566  C   SER A 404      15.050  33.943  14.239  1.00110.45           C  
ATOM    567  O   SER A 404      16.228  33.944  14.601  1.00110.47           O  
ATOM    568  CB  SER A 404      14.295  36.170  13.356  1.00110.02           C  
ATOM    569  OG  SER A 404      13.753  36.861  12.243  1.00110.41           O  
ATOM    570  N   ARG A 405      14.092  33.282  14.887  1.00110.86           N  
ATOM    571  CA  ARG A 405      14.373  32.495  16.081  1.00111.02           C  
ATOM    572  C   ARG A 405      15.438  31.456  15.764  1.00111.21           C  
ATOM    573  O   ARG A 405      16.143  30.992  16.660  1.00111.42           O  
ATOM    574  CB  ARG A 405      13.120  31.764  16.565  1.00111.41           C  
ATOM    575  CG  ARG A 405      11.921  32.635  16.868  1.00111.54           C  
ATOM    576  CD  ARG A 405      10.711  31.754  17.174  1.00111.80           C  
ATOM    577  NE  ARG A 405      10.446  30.808  16.089  1.00111.28           N  
ATOM    578  CZ  ARG A 405       9.439  29.940  16.069  1.00110.95           C  
ATOM    579  NH1 ARG A 405       8.579  29.881  17.080  1.00110.56           N  
ATOM    580  NH2 ARG A 405       9.287  29.136  15.028  1.00110.29           N  
ATOM    581  N   ASN A 406      15.539  31.076  14.491  1.00111.17           N  
ATOM    582  CA  ASN A 406      16.529  30.085  14.074  1.00111.53           C  
ATOM    583  C   ASN A 406      17.848  30.437  14.741  1.00110.88           C  
ATOM    584  O   ASN A 406      18.430  29.626  15.473  1.00111.09           O  
ATOM    585  CB  ASN A 406      16.693  30.082  12.545  1.00112.25           C  
ATOM    586  CG  ASN A 406      15.804  29.046  11.856  1.00113.24           C  
ATOM    587  OD1 ASN A 406      14.584  29.031  12.040  1.00113.76           O  
ATOM    588  ND2 ASN A 406      16.417  28.179  11.055  1.00112.79           N  
ATOM    589  N   SER A 407      18.301  31.662  14.492  1.00109.69           N  
ATOM    590  CA  SER A 407      19.538  32.157  15.077  1.00107.81           C  
ATOM    591  C   SER A 407      19.310  32.345  16.575  1.00105.61           C  
ATOM    592  O   SER A 407      20.182  32.040  17.387  1.00106.01           O  
ATOM    593  CB  SER A 407      19.936  33.490  14.429  1.00108.77           C  
ATOM    594  OG  SER A 407      18.895  34.450  14.532  1.00109.36           O  
ATOM    595  N   LYS A 408      18.128  32.842  16.931  1.00102.48           N  
ATOM    596  CA  LYS A 408      17.786  33.058  18.330  1.00 99.28           C  
ATOM    597  C   LYS A 408      17.927  31.743  19.099  1.00 95.61           C  
ATOM    598  O   LYS A 408      17.167  30.796  18.880  1.00 95.37           O  
ATOM    599  CB  LYS A 408      16.343  33.576  18.464  1.00101.12           C  
ATOM    600  CG  LYS A 408      15.921  33.865  19.908  1.00103.29           C  
ATOM    601  CD  LYS A 408      14.419  33.667  20.157  1.00104.62           C  
ATOM    602  CE  LYS A 408      13.547  34.750  19.522  1.00105.33           C  
ATOM    603  NZ  LYS A 408      12.101  34.595  19.908  1.00104.99           N  
ATOM    604  N   PRO A 409      18.923  31.658  19.993  1.00 91.84           N  
ATOM    605  CA  PRO A 409      19.119  30.434  20.775  1.00 88.09           C  
ATOM    606  C   PRO A 409      17.930  30.230  21.713  1.00 83.88           C  
ATOM    607  O   PRO A 409      17.489  31.172  22.377  1.00 82.81           O  
ATOM    608  CB  PRO A 409      20.413  30.716  21.536  1.00 89.05           C  
ATOM    609  CG  PRO A 409      21.149  31.653  20.622  1.00 89.82           C  
ATOM    610  CD  PRO A 409      20.055  32.584  20.178  1.00 91.16           C  
ATOM    611  N   VAL A 410      17.406  29.009  21.761  1.00 79.60           N  
ATOM    612  CA  VAL A 410      16.269  28.724  22.627  1.00 75.95           C  
ATOM    613  C   VAL A 410      16.445  27.442  23.418  1.00 72.98           C  
ATOM    614  O   VAL A 410      16.671  26.379  22.845  1.00 72.88           O  
ATOM    615  CB  VAL A 410      14.958  28.574  21.831  1.00 76.45           C  
ATOM    616  CG1 VAL A 410      13.785  28.471  22.793  1.00 75.86           C  
ATOM    617  CG2 VAL A 410      14.774  29.741  20.883  1.00 77.50           C  
ATOM    618  N   HIS A 411      16.351  27.538  24.738  1.00 69.84           N  
ATOM    619  CA  HIS A 411      16.450  26.342  25.561  1.00 65.57           C  
ATOM    620  C   HIS A 411      15.138  26.143  26.302  1.00 63.12           C  
ATOM    621  O   HIS A 411      14.600  27.080  26.900  1.00 63.81           O  
ATOM    622  CB  HIS A 411      17.586  26.433  26.570  1.00 65.03           C  
ATOM    623  CG  HIS A 411      17.767  25.178  27.364  1.00 64.85           C  
ATOM    624  ND1 HIS A 411      18.070  23.969  26.778  1.00 64.69           N  
ATOM    625  CD2 HIS A 411      17.651  24.934  28.691  1.00 64.80           C  
ATOM    626  CE1 HIS A 411      18.132  23.033  27.709  1.00 63.36           C  
ATOM    627  NE2 HIS A 411      17.881  23.592  28.878  1.00 63.33           N  
ATOM    628  N   THR A 412      14.620  24.923  26.253  1.00 58.95           N  
ATOM    629  CA  THR A 412      13.363  24.618  26.909  1.00 55.10           C  
ATOM    630  C   THR A 412      13.537  23.586  28.000  1.00 53.66           C  
ATOM    631  O   THR A 412      14.316  22.657  27.870  1.00 53.64           O  
ATOM    632  CB  THR A 412      12.318  24.110  25.905  1.00 54.57           C  
ATOM    633  OG1 THR A 412      11.949  25.173  25.018  1.00 53.64           O  
ATOM    634  CG2 THR A 412      11.081  23.621  26.625  1.00 54.08           C  
ATOM    635  N   THR A 413      12.800  23.765  29.084  1.00 52.09           N  
ATOM    636  CA  THR A 413      12.860  22.862  30.215  1.00 49.35           C  
ATOM    637  C   THR A 413      11.441  22.469  30.558  1.00 49.04           C  
ATOM    638  O   THR A 413      10.549  23.307  30.596  1.00 49.87           O  
ATOM    639  CB  THR A 413      13.485  23.545  31.454  1.00 48.40           C  
ATOM    640  OG1 THR A 413      14.813  23.987  31.148  1.00 48.21           O  
ATOM    641  CG2 THR A 413      13.526  22.588  32.622  1.00 45.15           C  
ATOM    642  N   ILE A 414      11.237  21.186  30.799  1.00 48.46           N  
ATOM    643  CA  ILE A 414       9.931  20.669  31.157  1.00 47.07           C  
ATOM    644  C   ILE A 414      10.027  20.349  32.634  1.00 46.73           C  
ATOM    645  O   ILE A 414      10.775  19.462  33.027  1.00 48.46           O  
ATOM    646  CB  ILE A 414       9.619  19.381  30.365  1.00 46.61           C  
ATOM    647  CG1 ILE A 414       9.535  19.704  28.878  1.00 45.71           C  
ATOM    648  CG2 ILE A 414       8.327  18.744  30.880  1.00 45.24           C  
ATOM    649  CD1 ILE A 414       9.294  18.492  28.013  1.00 47.29           C  
ATOM    650  N   LEU A 415       9.280  21.065  33.457  1.00 46.60           N  
ATOM    651  CA  LEU A 415       9.340  20.838  34.896  1.00 46.40           C  
ATOM    652  C   LEU A 415       8.142  20.158  35.508  1.00 45.06           C  
ATOM    653  O   LEU A 415       7.017  20.342  35.077  1.00 45.28           O  
ATOM    654  CB  LEU A 415       9.530  22.151  35.650  1.00 46.81           C  
ATOM    655  CG  LEU A 415      10.772  22.987  35.408  1.00 49.06           C  
ATOM    656  CD1 LEU A 415      10.717  24.172  36.348  1.00 50.70           C  
ATOM    657  CD2 LEU A 415      12.027  22.171  35.655  1.00 50.99           C  
ATOM    658  N   ASN A 416       8.416  19.384  36.546  1.00 44.72           N  
ATOM    659  CA  ASN A 416       7.403  18.692  37.311  1.00 43.45           C  
ATOM    660  C   ASN A 416       6.345  17.990  36.450  1.00 43.07           C  
ATOM    661  O   ASN A 416       5.152  18.135  36.687  1.00 42.98           O  
ATOM    662  CB  ASN A 416       6.779  19.713  38.269  1.00 43.07           C  
ATOM    663  CG  ASN A 416       5.940  19.077  39.345  1.00 45.64           C  
ATOM    664  OD1 ASN A 416       6.229  17.971  39.805  1.00 48.11           O  
ATOM    665  ND2 ASN A 416       4.899  19.786  39.780  1.00 47.01           N  
ATOM    666  N   PRO A 417       6.779  17.195  35.454  1.00 42.25           N  
ATOM    667  CA  PRO A 417       5.865  16.474  34.567  1.00 42.21           C  
ATOM    668  C   PRO A 417       4.972  15.494  35.318  1.00 42.56           C  
ATOM    669  O   PRO A 417       5.379  14.912  36.323  1.00 44.11           O  
ATOM    670  CB  PRO A 417       6.812  15.728  33.632  1.00 42.13           C  
ATOM    671  CG  PRO A 417       8.034  16.547  33.644  1.00 41.75           C  
ATOM    672  CD  PRO A 417       8.171  16.918  35.072  1.00 41.49           C  
ATOM    673  N   HIS A 418       3.757  15.317  34.822  1.00 41.17           N  
ATOM    674  CA  HIS A 418       2.820  14.369  35.404  1.00 42.18           C  
ATOM    675  C   HIS A 418       2.033  13.719  34.269  1.00 42.84           C  
ATOM    676  O   HIS A 418       1.351  14.402  33.494  1.00 42.67           O  
ATOM    677  CB  HIS A 418       1.873  15.060  36.373  1.00 41.75           C  
ATOM    678  CG  HIS A 418       2.487  15.362  37.703  1.00 43.44           C  
ATOM    679  ND1 HIS A 418       2.095  14.729  38.861  1.00 42.81           N  
ATOM    680  CD2 HIS A 418       3.444  16.252  38.065  1.00 43.44           C  
ATOM    681  CE1 HIS A 418       2.781  15.218  39.879  1.00 42.24           C  
ATOM    682  NE2 HIS A 418       3.605  16.142  39.423  1.00 42.74           N  
ATOM    683  N   ILE A 419       2.156  12.404  34.148  1.00 41.86           N  
ATOM    684  CA  ILE A 419       1.449  11.697  33.106  1.00 42.90           C  
ATOM    685  C   ILE A 419       0.324  10.886  33.692  1.00 43.22           C  
ATOM    686  O   ILE A 419       0.433  10.359  34.784  1.00 43.07           O  
ATOM    687  CB  ILE A 419       2.369  10.729  32.316  1.00 44.34           C  
ATOM    688  CG1 ILE A 419       3.449  11.504  31.552  1.00 43.00           C  
ATOM    689  CG2 ILE A 419       1.545   9.921  31.330  1.00 42.97           C  
ATOM    690  CD1 ILE A 419       4.560  12.013  32.414  1.00 43.83           C  
ATOM    691  N   HIS A 420      -0.771  10.821  32.951  1.00 44.16           N  
ATOM    692  CA  HIS A 420      -1.937  10.043  33.334  1.00 45.07           C  
ATOM    693  C   HIS A 420      -2.174   9.097  32.169  1.00 46.61           C  
ATOM    694  O   HIS A 420      -2.412   9.539  31.046  1.00 46.19           O  
ATOM    695  CB  HIS A 420      -3.154  10.940  33.502  1.00 44.58           C  
ATOM    696  CG  HIS A 420      -3.088  11.835  34.695  1.00 44.09           C  
ATOM    697  ND1 HIS A 420      -3.359  11.394  35.971  1.00 42.67           N  
ATOM    698  CD2 HIS A 420      -2.808  13.156  34.802  1.00 44.68           C  
ATOM    699  CE1 HIS A 420      -3.255  12.407  36.813  1.00 43.57           C  
ATOM    700  NE2 HIS A 420      -2.923  13.487  36.130  1.00 43.43           N  
ATOM    701  N   LEU A 421      -2.078   7.798  32.420  1.00 48.62           N  
ATOM    702  CA  LEU A 421      -2.299   6.828  31.362  1.00 50.19           C  
ATOM    703  C   LEU A 421      -3.777   6.438  31.400  1.00 52.43           C  
ATOM    704  O   LEU A 421      -4.354   6.261  32.472  1.00 52.39           O  
ATOM    705  CB  LEU A 421      -1.400   5.614  31.572  1.00 48.94           C  
ATOM    706  CG  LEU A 421       0.094   5.939  31.567  1.00 49.70           C  
ATOM    707  CD1 LEU A 421       0.897   4.711  31.973  1.00 49.93           C  
ATOM    708  CD2 LEU A 421       0.509   6.415  30.185  1.00 47.65           C  
ATOM    709  N   MET A 422      -4.392   6.340  30.224  1.00 54.65           N  
ATOM    710  CA  MET A 422      -5.800   5.984  30.112  1.00 57.89           C  
ATOM    711  C   MET A 422      -5.943   5.036  28.931  1.00 60.51           C  
ATOM    712  O   MET A 422      -6.169   5.464  27.810  1.00 63.41           O  
ATOM    713  CB  MET A 422      -6.607   7.249  29.868  1.00 58.09           C  
ATOM    714  CG  MET A 422      -6.204   8.373  30.798  1.00 58.24           C  
ATOM    715  SD  MET A 422      -6.522   9.994  30.140  1.00 59.99           S  
ATOM    716  CE  MET A 422      -5.191  10.247  29.108  1.00 54.09           C  
ATOM    717  N   GLY A 423      -5.822   3.744  29.180  1.00 62.61           N  
ATOM    718  CA  GLY A 423      -5.897   2.793  28.090  1.00 63.57           C  
ATOM    719  C   GLY A 423      -4.537   2.783  27.419  1.00 63.70           C  
ATOM    720  O   GLY A 423      -3.657   3.552  27.786  1.00 61.14           O  
ATOM    721  N   ASP A 424      -4.361   1.921  26.428  1.00 65.94           N  
ATOM    722  CA  ASP A 424      -3.083   1.823  25.739  1.00 66.65           C  
ATOM    723  C   ASP A 424      -2.951   2.825  24.614  1.00 66.36           C  
ATOM    724  O   ASP A 424      -1.863   3.011  24.081  1.00 66.29           O  
ATOM    725  CB  ASP A 424      -2.884   0.409  25.166  1.00 69.83           C  
ATOM    726  CG  ASP A 424      -2.728  -0.648  26.244  1.00 72.52           C  
ATOM    727  OD1 ASP A 424      -1.825  -0.494  27.092  1.00 72.91           O  
ATOM    728  OD2 ASP A 424      -3.508  -1.629  26.240  1.00 75.20           O  
ATOM    729  N   GLU A 425      -4.048   3.480  24.253  1.00 66.35           N  
ATOM    730  CA  GLU A 425      -4.014   4.437  23.150  1.00 65.19           C  
ATOM    731  C   GLU A 425      -4.277   5.874  23.598  1.00 63.01           C  
ATOM    732  O   GLU A 425      -4.375   6.778  22.761  1.00 62.69           O  
ATOM    733  CB  GLU A 425      -5.065   4.042  22.101  1.00 68.72           C  
ATOM    734  CG  GLU A 425      -5.190   2.537  21.860  1.00 72.68           C  
ATOM    735  CD  GLU A 425      -3.910   1.923  21.331  1.00 74.51           C  
ATOM    736  OE1 GLU A 425      -3.470   2.298  20.221  1.00 76.20           O  
ATOM    737  OE2 GLU A 425      -3.343   1.062  22.031  1.00 76.02           O  
ATOM    738  N   SER A 426      -4.375   6.089  24.906  1.00 58.80           N  
ATOM    739  CA  SER A 426      -4.690   7.417  25.421  1.00 56.61           C  
ATOM    740  C   SER A 426      -3.879   7.885  26.632  1.00 54.40           C  
ATOM    741  O   SER A 426      -3.851   7.230  27.673  1.00 54.22           O  
ATOM    742  CB  SER A 426      -6.192   7.471  25.725  1.00 55.60           C  
ATOM    743  OG  SER A 426      -6.482   8.300  26.826  1.00 57.28           O  
ATOM    744  N   ALA A 427      -3.229   9.035  26.489  1.00 50.59           N  
ATOM    745  CA  ALA A 427      -2.422   9.586  27.567  1.00 49.38           C  
ATOM    746  C   ALA A 427      -2.623  11.091  27.747  1.00 48.63           C  
ATOM    747  O   ALA A 427      -3.067  11.804  26.839  1.00 48.24           O  
ATOM    748  CB  ALA A 427      -0.945   9.287  27.330  1.00 50.64           C  
ATOM    749  N   CYS A 428      -2.286  11.568  28.937  1.00 45.79           N  
ATOM    750  CA  CYS A 428      -2.422  12.977  29.275  1.00 42.70           C  
ATOM    751  C   CYS A 428      -1.218  13.458  30.066  1.00 39.88           C  
ATOM    752  O   CYS A 428      -0.902  12.900  31.116  1.00 40.10           O  
ATOM    753  CB  CYS A 428      -3.665  13.182  30.121  1.00 44.86           C  
ATOM    754  SG  CYS A 428      -3.901  14.872  30.570  1.00 51.98           S  
ATOM    755  N   ILE A 429      -0.548  14.492  29.578  1.00 36.01           N  
ATOM    756  CA  ILE A 429       0.609  15.005  30.286  1.00 35.03           C  
ATOM    757  C   ILE A 429       0.477  16.487  30.618  1.00 35.83           C  
ATOM    758  O   ILE A 429       0.052  17.295  29.786  1.00 35.74           O  
ATOM    759  CB  ILE A 429       1.899  14.774  29.474  1.00 35.22           C  
ATOM    760  CG1 ILE A 429       3.115  15.165  30.309  1.00 34.48           C  
ATOM    761  CG2 ILE A 429       1.855  15.570  28.176  1.00 34.90           C  
ATOM    762  CD1 ILE A 429       4.415  14.931  29.619  1.00 34.56           C  
ATOM    763  N   ALA A 430       0.841  16.836  31.846  1.00 35.04           N  
ATOM    764  CA  ALA A 430       0.776  18.222  32.309  1.00 35.42           C  
ATOM    765  C   ALA A 430       2.134  18.615  32.863  1.00 35.31           C  
ATOM    766  O   ALA A 430       2.716  17.883  33.648  1.00 36.77           O  
ATOM    767  CB  ALA A 430      -0.294  18.363  33.401  1.00 34.65           C  
ATOM    768  N   TYR A 431       2.638  19.773  32.472  1.00 34.82           N  
ATOM    769  CA  TYR A 431       3.943  20.204  32.955  1.00 34.75           C  
ATOM    770  C   TYR A 431       4.112  21.718  32.894  1.00 35.76           C  
ATOM    771  O   TYR A 431       3.304  22.421  32.297  1.00 37.44           O  
ATOM    772  CB  TYR A 431       5.027  19.547  32.111  1.00 33.28           C  
ATOM    773  CG  TYR A 431       4.850  19.825  30.641  1.00 34.01           C  
ATOM    774  CD1 TYR A 431       5.427  20.944  30.053  1.00 33.97           C  
ATOM    775  CD2 TYR A 431       4.044  19.000  29.842  1.00 34.87           C  
ATOM    776  CE1 TYR A 431       5.214  21.249  28.712  1.00 35.05           C  
ATOM    777  CE2 TYR A 431       3.821  19.297  28.501  1.00 34.42           C  
ATOM    778  CZ  TYR A 431       4.412  20.427  27.944  1.00 35.92           C  
ATOM    779  OH  TYR A 431       4.207  20.758  26.626  1.00 37.34           O  
ATOM    780  N   ILE A 432       5.163  22.216  33.532  1.00 35.04           N  
ATOM    781  CA  ILE A 432       5.468  23.629  33.503  1.00 33.11           C  
ATOM    782  C   ILE A 432       6.495  23.728  32.406  1.00 32.80           C  
ATOM    783  O   ILE A 432       7.444  22.974  32.388  1.00 32.17           O  
ATOM    784  CB  ILE A 432       6.123  24.114  34.806  1.00 34.45           C  
ATOM    785  CG1 ILE A 432       5.202  23.858  36.001  1.00 33.33           C  
ATOM    786  CG2 ILE A 432       6.474  25.594  34.686  1.00 34.21           C  
ATOM    787  CD1 ILE A 432       3.949  24.647  35.973  1.00 36.44           C  
ATOM    788  N   ARG A 433       6.305  24.653  31.484  1.00 35.26           N  
ATOM    789  CA  ARG A 433       7.239  24.817  30.386  1.00 38.00           C  
ATOM    790  C   ARG A 433       8.028  26.100  30.595  1.00 39.36           C  
ATOM    791  O   ARG A 433       7.470  27.195  30.595  1.00 39.17           O  
ATOM    792  CB  ARG A 433       6.465  24.874  29.069  1.00 39.74           C  
ATOM    793  CG  ARG A 433       7.304  25.117  27.833  1.00 42.74           C  
ATOM    794  CD  ARG A 433       6.388  25.189  26.627  1.00 44.09           C  
ATOM    795  NE  ARG A 433       7.100  25.448  25.381  1.00 45.80           N  
ATOM    796  CZ  ARG A 433       6.491  25.631  24.213  1.00 45.62           C  
ATOM    797  NH1 ARG A 433       5.172  25.573  24.145  1.00 45.30           N  
ATOM    798  NH2 ARG A 433       7.191  25.892  23.121  1.00 45.11           N  
ATOM    799  N   ILE A 434       9.330  25.961  30.779  1.00 41.31           N  
ATOM    800  CA  ILE A 434      10.168  27.126  30.987  1.00 42.94           C  
ATOM    801  C   ILE A 434      11.040  27.343  29.772  1.00 43.59           C  
ATOM    802  O   ILE A 434      11.717  26.429  29.317  1.00 43.24           O  
ATOM    803  CB  ILE A 434      11.046  26.960  32.229  1.00 43.66           C  
ATOM    804  CG1 ILE A 434      10.148  26.836  33.459  1.00 44.01           C  
ATOM    805  CG2 ILE A 434      11.979  28.143  32.367  1.00 42.57           C  
ATOM    806  CD1 ILE A 434      10.881  26.876  34.748  1.00 45.15           C  
ATOM    807  N   THR A 435      11.010  28.559  29.248  1.00 44.14           N  
ATOM    808  CA  THR A 435      11.785  28.895  28.073  1.00 46.06           C  
ATOM    809  C   THR A 435      12.807  29.979  28.367  1.00 47.84           C  
ATOM    810  O   THR A 435      12.480  31.035  28.927  1.00 46.20           O  
ATOM    811  CB  THR A 435      10.861  29.379  26.940  1.00 46.73           C  
ATOM    812  OG1 THR A 435       9.852  28.394  26.708  1.00 48.68           O  
ATOM    813  CG2 THR A 435      11.641  29.609  25.657  1.00 45.13           C  
ATOM    814  N   GLN A 436      14.048  29.693  27.992  1.00 50.32           N  
ATOM    815  CA  GLN A 436      15.143  30.626  28.170  1.00 54.37           C  
ATOM    816  C   GLN A 436      15.491  31.129  26.778  1.00 57.18           C  
ATOM    817  O   GLN A 436      15.865  30.352  25.904  1.00 57.63           O  
ATOM    818  CB  GLN A 436      16.345  29.928  28.812  1.00 52.76           C  
ATOM    819  CG  GLN A 436      16.081  29.501  30.246  1.00 52.46           C  
ATOM    820  CD  GLN A 436      17.203  28.672  30.835  1.00 51.52           C  
ATOM    821  OE1 GLN A 436      17.635  27.689  30.241  1.00 51.70           O  
ATOM    822  NE2 GLN A 436      17.672  29.059  32.012  1.00 50.24           N  
ATOM    823  N   TYR A 437      15.340  32.428  26.573  1.00 60.58           N  
ATOM    824  CA  TYR A 437      15.630  33.034  25.288  1.00 64.82           C  
ATOM    825  C   TYR A 437      16.379  34.355  25.511  1.00 68.04           C  
ATOM    826  O   TYR A 437      16.440  34.844  26.624  1.00 67.59           O  
ATOM    827  CB  TYR A 437      14.321  33.290  24.535  1.00 64.64           C  
ATOM    828  CG  TYR A 437      13.375  34.237  25.246  1.00 64.00           C  
ATOM    829  CD1 TYR A 437      13.336  35.590  24.917  1.00 63.58           C  
ATOM    830  CD2 TYR A 437      12.552  33.790  26.284  1.00 63.69           C  
ATOM    831  CE1 TYR A 437      12.505  36.478  25.601  1.00 64.83           C  
ATOM    832  CE2 TYR A 437      11.718  34.672  26.979  1.00 64.27           C  
ATOM    833  CZ  TYR A 437      11.701  36.010  26.635  1.00 64.83           C  
ATOM    834  OH  TYR A 437      10.891  36.878  27.332  1.00 64.14           O  
ATOM    835  N   LEU A 438      16.925  34.935  24.444  1.00 72.86           N  
ATOM    836  CA  LEU A 438      17.659  36.199  24.544  1.00 77.75           C  
ATOM    837  C   LEU A 438      16.713  37.332  24.125  1.00 80.81           C  
ATOM    838  O   LEU A 438      15.560  37.326  24.434  1.00 81.63           O  
ATOM    839  CB  LEU A 438      18.893  36.123  23.625  1.00 77.72           C  
ATOM    840  CG  LEU A 438      20.017  35.218  24.124  1.00 78.06           C  
ATOM    841  CD1 LEU A 438      21.142  35.118  23.127  1.00 77.72           C  
ATOM    842  CD2 LEU A 438      20.544  35.746  25.460  1.00 79.53           C  
ATOM    843  N   ASP A 439      17.206  38.416  23.600  1.00 83.89           N  
ATOM    844  CA  ASP A 439      16.268  39.381  23.031  1.00 86.31           C  
ATOM    845  C   ASP A 439      17.029  40.384  22.238  1.00 87.43           C  
ATOM    846  O   ASP A 439      17.790  39.989  21.365  1.00 87.31           O  
ATOM    847  CB  ASP A 439      15.247  40.085  23.931  1.00 88.23           C  
ATOM    848  CG  ASP A 439      13.990  40.526  23.089  1.00 90.81           C  
ATOM    849  OD1 ASP A 439      14.121  40.494  21.837  1.00 92.08           O  
ATOM    850  OD2 ASP A 439      12.888  40.857  23.589  1.00 91.88           O  
ATOM    851  N   ALA A 440      16.794  41.661  22.491  1.00 88.34           N  
ATOM    852  CA  ALA A 440      17.508  42.674  21.760  1.00 88.67           C  
ATOM    853  C   ALA A 440      18.568  43.096  22.779  1.00 88.73           C  
ATOM    854  O   ALA A 440      18.264  43.313  23.955  1.00 88.00           O  
ATOM    855  CB  ALA A 440      16.608  43.784  21.414  1.00 89.03           C  
ATOM    856  N   GLY A 441      19.818  43.176  22.338  1.00 88.88           N  
ATOM    857  CA  GLY A 441      20.883  43.535  23.256  1.00 88.67           C  
ATOM    858  C   GLY A 441      21.364  42.218  23.807  1.00 88.32           C  
ATOM    859  O   GLY A 441      22.292  42.162  24.623  1.00 88.05           O  
ATOM    860  N   GLY A 442      20.717  41.151  23.336  1.00 87.89           N  
ATOM    861  CA  GLY A 442      21.045  39.801  23.753  1.00 86.70           C  
ATOM    862  C   GLY A 442      20.763  39.574  25.215  1.00 85.85           C  
ATOM    863  O   GLY A 442      21.488  38.821  25.868  1.00 85.54           O  
ATOM    864  N   ILE A 443      19.715  40.203  25.728  1.00 85.27           N  
ATOM    865  CA  ILE A 443      19.356  40.070  27.147  1.00 85.54           C  
ATOM    866  C   ILE A 443      18.656  38.733  27.458  1.00 84.35           C  
ATOM    867  O   ILE A 443      17.637  38.392  26.862  1.00 84.68           O  
ATOM    868  CB  ILE A 443      18.392  41.195  27.620  1.00 86.90           C  
ATOM    869  CG1 ILE A 443      19.033  42.568  27.385  1.00 87.79           C  
ATOM    870  CG2 ILE A 443      18.080  41.028  29.100  1.00 86.72           C  
ATOM    871  CD1 ILE A 443      18.148  43.747  27.757  1.00 87.68           C  
ATOM    872  N   PRO A 444      19.180  37.998  28.453  1.00 82.40           N  
ATOM    873  CA  PRO A 444      18.573  36.729  28.802  1.00 80.11           C  
ATOM    874  C   PRO A 444      17.331  36.891  29.664  1.00 77.58           C  
ATOM    875  O   PRO A 444      17.366  37.521  30.711  1.00 78.03           O  
ATOM    876  CB  PRO A 444      19.723  36.023  29.525  1.00 80.65           C  
ATOM    877  CG  PRO A 444      20.961  36.688  29.030  1.00 81.52           C  
ATOM    878  CD  PRO A 444      20.534  38.082  29.045  1.00 82.34           C  
ATOM    879  N   ARG A 445      16.231  36.315  29.205  1.00 74.91           N  
ATOM    880  CA  ARG A 445      14.986  36.381  29.965  1.00 71.46           C  
ATOM    881  C   ARG A 445      14.320  35.004  30.026  1.00 66.44           C  
ATOM    882  O   ARG A 445      14.609  34.122  29.216  1.00 64.70           O  
ATOM    883  CB  ARG A 445      14.048  37.428  29.364  1.00 74.04           C  
ATOM    884  CG  ARG A 445      14.562  38.847  29.576  1.00 78.05           C  
ATOM    885  CD  ARG A 445      13.474  39.890  29.358  1.00 82.00           C  
ATOM    886  NE  ARG A 445      13.941  41.246  29.655  1.00 86.11           N  
ATOM    887  CZ  ARG A 445      14.871  41.900  28.958  1.00 87.57           C  
ATOM    888  NH1 ARG A 445      15.450  41.330  27.907  1.00 88.25           N  
ATOM    889  NH2 ARG A 445      15.223  43.132  29.312  1.00 88.30           N  
ATOM    890  N   THR A 446      13.433  34.827  30.996  1.00 61.57           N  
ATOM    891  CA  THR A 446      12.761  33.555  31.184  1.00 56.70           C  
ATOM    892  C   THR A 446      11.251  33.695  31.192  1.00 53.59           C  
ATOM    893  O   THR A 446      10.696  34.593  31.827  1.00 51.67           O  
ATOM    894  CB  THR A 446      13.193  32.898  32.518  1.00 56.18           C  
ATOM    895  OG1 THR A 446      14.611  32.719  32.526  1.00 55.87           O  
ATOM    896  CG2 THR A 446      12.534  31.551  32.685  1.00 55.04           C  
ATOM    897  N   ALA A 447      10.591  32.777  30.493  1.00 50.50           N  
ATOM    898  CA  ALA A 447       9.135  32.768  30.415  1.00 46.70           C  
ATOM    899  C   ALA A 447       8.610  31.447  30.931  1.00 42.89           C  
ATOM    900  O   ALA A 447       9.225  30.417  30.730  1.00 41.96           O  
ATOM    901  CB  ALA A 447       8.683  32.985  28.972  1.00 46.63           C  
ATOM    902  N   GLN A 448       7.468  31.486  31.602  1.00 41.70           N  
ATOM    903  CA  GLN A 448       6.852  30.288  32.153  1.00 39.20           C  
ATOM    904  C   GLN A 448       5.431  30.112  31.644  1.00 39.48           C  
ATOM    905  O   GLN A 448       4.706  31.082  31.410  1.00 40.24           O  
ATOM    906  CB  GLN A 448       6.799  30.354  33.688  1.00 39.56           C  
ATOM    907  CG  GLN A 448       6.240  29.078  34.315  1.00 44.38           C  
ATOM    908  CD  GLN A 448       6.081  29.146  35.832  1.00 46.89           C  
ATOM    909  OE1 GLN A 448       6.883  29.775  36.526  1.00 50.89           O  
ATOM    910  NE2 GLN A 448       5.054  28.471  36.355  1.00 45.29           N  
ATOM    911  N   SER A 449       5.027  28.865  31.468  1.00 39.43           N  
ATOM    912  CA  SER A 449       3.664  28.576  31.056  1.00 38.50           C  
ATOM    913  C   SER A 449       3.307  27.168  31.494  1.00 37.54           C  
ATOM    914  O   SER A 449       4.152  26.279  31.508  1.00 34.99           O  
ATOM    915  CB  SER A 449       3.485  28.739  29.539  1.00 38.05           C  
ATOM    916  OG  SER A 449       4.187  27.759  28.820  1.00 41.56           O  
ATOM    917  N   GLU A 450       2.054  26.990  31.897  1.00 38.13           N  
ATOM    918  CA  GLU A 450       1.562  25.694  32.319  1.00 37.75           C  
ATOM    919  C   GLU A 450       0.938  25.058  31.088  1.00 37.45           C  
ATOM    920  O   GLU A 450       0.132  25.686  30.407  1.00 37.25           O  
ATOM    921  CB  GLU A 450       0.516  25.861  33.415  1.00 40.14           C  
ATOM    922  CG  GLU A 450       1.052  26.509  34.685  1.00 45.58           C  
ATOM    923  CD  GLU A 450       1.279  28.001  34.536  1.00 49.87           C  
ATOM    924  OE1 GLU A 450       0.289  28.711  34.274  1.00 53.03           O  
ATOM    925  OE2 GLU A 450       2.435  28.472  34.678  1.00 51.18           O  
ATOM    926  N   GLU A 451       1.319  23.827  30.781  1.00 35.66           N  
ATOM    927  CA  GLU A 451       0.761  23.177  29.609  1.00 35.22           C  
ATOM    928  C   GLU A 451       0.187  21.795  29.875  1.00 34.69           C  
ATOM    929  O   GLU A 451       0.701  21.025  30.683  1.00 34.58           O  
ATOM    930  CB  GLU A 451       1.810  23.067  28.497  1.00 34.89           C  
ATOM    931  CG  GLU A 451       2.514  24.353  28.161  1.00 36.81           C  
ATOM    932  CD  GLU A 451       3.171  24.324  26.784  1.00 39.73           C  
ATOM    933  OE1 GLU A 451       3.575  23.232  26.339  1.00 40.72           O  
ATOM    934  OE2 GLU A 451       3.299  25.398  26.151  1.00 41.06           O  
ATOM    935  N   THR A 452      -0.902  21.508  29.177  1.00 34.51           N  
ATOM    936  CA  THR A 452      -1.575  20.225  29.241  1.00 34.07           C  
ATOM    937  C   THR A 452      -1.642  19.743  27.796  1.00 35.31           C  
ATOM    938  O   THR A 452      -2.059  20.486  26.912  1.00 34.96           O  
ATOM    939  CB  THR A 452      -2.998  20.365  29.766  1.00 32.86           C  
ATOM    940  OG1 THR A 452      -2.969  20.720  31.150  1.00 33.90           O  
ATOM    941  CG2 THR A 452      -3.744  19.071  29.587  1.00 31.83           C  
ATOM    942  N   ARG A 453      -1.198  18.520  27.549  1.00 36.42           N  
ATOM    943  CA  ARG A 453      -1.243  17.954  26.204  1.00 36.83           C  
ATOM    944  C   ARG A 453      -2.011  16.645  26.303  1.00 37.77           C  
ATOM    945  O   ARG A 453      -1.697  15.811  27.151  1.00 39.25           O  
ATOM    946  CB  ARG A 453       0.168  17.667  25.686  1.00 36.95           C  
ATOM    947  CG  ARG A 453       1.106  18.856  25.651  1.00 37.65           C  
ATOM    948  CD  ARG A 453       0.876  19.702  24.434  1.00 39.95           C  
ATOM    949  NE  ARG A 453       1.828  20.800  24.369  1.00 40.48           N  
ATOM    950  CZ  ARG A 453       1.831  21.732  23.422  1.00 42.16           C  
ATOM    951  NH1 ARG A 453       0.925  21.711  22.445  1.00 41.41           N  
ATOM    952  NH2 ARG A 453       2.749  22.689  23.450  1.00 42.20           N  
ATOM    953  N   VAL A 454      -3.029  16.462  25.468  1.00 38.38           N  
ATOM    954  CA  VAL A 454      -3.778  15.210  25.490  1.00 38.68           C  
ATOM    955  C   VAL A 454      -3.395  14.404  24.257  1.00 40.19           C  
ATOM    956  O   VAL A 454      -3.606  14.845  23.121  1.00 40.50           O  
ATOM    957  CB  VAL A 454      -5.283  15.457  25.517  1.00 38.57           C  
ATOM    958  CG1 VAL A 454      -6.014  14.135  25.536  1.00 38.34           C  
ATOM    959  CG2 VAL A 454      -5.647  16.274  26.765  1.00 38.89           C  
ATOM    960  N   TRP A 455      -2.814  13.226  24.497  1.00 41.70           N  
ATOM    961  CA  TRP A 455      -2.346  12.346  23.427  1.00 42.46           C  
ATOM    962  C   TRP A 455      -3.222  11.154  23.092  1.00 44.21           C  
ATOM    963  O   TRP A 455      -3.763  10.490  23.975  1.00 44.45           O  
ATOM    964  CB  TRP A 455      -0.959  11.807  23.758  1.00 39.62           C  
ATOM    965  CG  TRP A 455       0.102  12.816  23.848  1.00 36.57           C  
ATOM    966  CD1 TRP A 455       0.565  13.422  24.982  1.00 36.55           C  
ATOM    967  CD2 TRP A 455       0.894  13.316  22.767  1.00 35.57           C  
ATOM    968  NE1 TRP A 455       1.607  14.267  24.672  1.00 36.65           N  
ATOM    969  CE2 TRP A 455       1.828  14.223  23.319  1.00 35.38           C  
ATOM    970  CE3 TRP A 455       0.907  13.087  21.384  1.00 33.17           C  
ATOM    971  CZ2 TRP A 455       2.766  14.900  22.536  1.00 35.41           C  
ATOM    972  CZ3 TRP A 455       1.844  13.761  20.603  1.00 33.31           C  
ATOM    973  CH2 TRP A 455       2.761  14.657  21.183  1.00 34.83           C  
ATOM    974  N   HIS A 456      -3.334  10.877  21.800  1.00 48.63           N  
ATOM    975  CA  HIS A 456      -4.103   9.739  21.331  1.00 53.16           C  
ATOM    976  C   HIS A 456      -3.295   8.978  20.292  1.00 56.09           C  
ATOM    977  O   HIS A 456      -2.789   9.565  19.335  1.00 56.17           O  
ATOM    978  CB  HIS A 456      -5.422  10.187  20.729  1.00 54.00           C  
ATOM    979  CG  HIS A 456      -6.354   9.055  20.443  1.00 58.21           C  
ATOM    980  ND1 HIS A 456      -6.712   8.692  19.163  1.00 58.19           N  
ATOM    981  CD2 HIS A 456      -6.979   8.185  21.272  1.00 59.50           C  
ATOM    982  CE1 HIS A 456      -7.519   7.647  19.217  1.00 59.65           C  
ATOM    983  NE2 HIS A 456      -7.697   7.320  20.485  1.00 60.68           N  
ATOM    984  N   ARG A 457      -3.168   7.673  20.502  1.00 60.00           N  
ATOM    985  CA  ARG A 457      -2.426   6.791  19.606  1.00 64.81           C  
ATOM    986  C   ARG A 457      -3.276   6.410  18.391  1.00 67.20           C  
ATOM    987  O   ARG A 457      -4.325   5.772  18.529  1.00 67.36           O  
ATOM    988  CB  ARG A 457      -2.031   5.520  20.362  1.00 67.67           C  
ATOM    989  CG  ARG A 457      -1.081   4.588  19.624  1.00 70.70           C  
ATOM    990  CD  ARG A 457       0.323   5.142  19.642  1.00 72.77           C  
ATOM    991  NE  ARG A 457       1.325   4.118  19.921  1.00 75.70           N  
ATOM    992  CZ  ARG A 457       1.284   3.277  20.955  1.00 77.85           C  
ATOM    993  NH1 ARG A 457       0.282   3.317  21.824  1.00 77.71           N  
ATOM    994  NH2 ARG A 457       2.263   2.403  21.138  1.00 79.54           N  
ATOM    995  N   ARG A 458      -2.830   6.808  17.204  1.00 69.88           N  
ATOM    996  CA  ARG A 458      -3.554   6.482  15.976  1.00 73.08           C  
ATOM    997  C   ARG A 458      -2.632   5.805  14.973  1.00 73.47           C  
ATOM    998  O   ARG A 458      -1.614   6.371  14.573  1.00 73.32           O  
ATOM    999  CB  ARG A 458      -4.150   7.734  15.327  1.00 75.10           C  
ATOM   1000  CG  ARG A 458      -4.686   7.468  13.920  1.00 79.13           C  
ATOM   1001  CD  ARG A 458      -5.035   8.742  13.152  1.00 82.94           C  
ATOM   1002  NE  ARG A 458      -6.371   9.251  13.462  1.00 86.10           N  
ATOM   1003  CZ  ARG A 458      -6.923  10.299  12.859  1.00 88.07           C  
ATOM   1004  NH1 ARG A 458      -6.250  10.951  11.915  1.00 89.52           N  
ATOM   1005  NH2 ARG A 458      -8.148  10.693  13.191  1.00 88.30           N  
ATOM   1006  N   ASP A 459      -2.996   4.590  14.573  1.00 73.86           N  
ATOM   1007  CA  ASP A 459      -2.216   3.827  13.605  1.00 73.73           C  
ATOM   1008  C   ASP A 459      -0.717   3.830  13.901  1.00 72.46           C  
ATOM   1009  O   ASP A 459       0.095   4.063  13.011  1.00 72.19           O  
ATOM   1010  CB  ASP A 459      -2.454   4.371  12.189  1.00 75.26           C  
ATOM   1011  CG  ASP A 459      -3.930   4.418  11.813  1.00 76.75           C  
ATOM   1012  OD1 ASP A 459      -4.620   3.384  11.949  1.00 76.04           O  
ATOM   1013  OD2 ASP A 459      -4.396   5.494  11.373  1.00 78.12           O  
ATOM   1014  N   GLY A 460      -0.349   3.586  15.152  1.00 71.35           N  
ATOM   1015  CA  GLY A 460       1.062   3.548  15.485  1.00 70.05           C  
ATOM   1016  C   GLY A 460       1.692   4.774  16.126  1.00 69.29           C  
ATOM   1017  O   GLY A 460       2.441   4.634  17.098  1.00 69.66           O  
ATOM   1018  N   LYS A 461       1.424   5.968  15.597  1.00 67.49           N  
ATOM   1019  CA  LYS A 461       2.017   7.165  16.185  1.00 66.21           C  
ATOM   1020  C   LYS A 461       1.072   7.991  17.043  1.00 63.77           C  
ATOM   1021  O   LYS A 461      -0.138   8.038  16.804  1.00 62.91           O  
ATOM   1022  CB  LYS A 461       2.642   8.066  15.116  1.00 68.05           C  
ATOM   1023  CG  LYS A 461       1.692   8.601  14.070  1.00 71.03           C  
ATOM   1024  CD  LYS A 461       2.398   9.649  13.206  1.00 73.35           C  
ATOM   1025  CE  LYS A 461       1.727   9.824  11.836  1.00 75.24           C  
ATOM   1026  NZ  LYS A 461       0.294  10.256  11.901  1.00 76.21           N  
ATOM   1027  N   TRP A 462       1.658   8.632  18.054  1.00 60.03           N  
ATOM   1028  CA  TRP A 462       0.929   9.472  18.986  1.00 55.28           C  
ATOM   1029  C   TRP A 462       0.606  10.807  18.366  1.00 54.13           C  
ATOM   1030  O   TRP A 462       1.454  11.412  17.707  1.00 53.78           O  
ATOM   1031  CB  TRP A 462       1.754   9.711  20.242  1.00 52.12           C  
ATOM   1032  CG  TRP A 462       1.853   8.527  21.119  1.00 49.65           C  
ATOM   1033  CD1 TRP A 462       2.905   7.665  21.218  1.00 47.96           C  
ATOM   1034  CD2 TRP A 462       0.866   8.074  22.053  1.00 47.44           C  
ATOM   1035  NE1 TRP A 462       2.637   6.706  22.163  1.00 47.17           N  
ATOM   1036  CE2 TRP A 462       1.393   6.933  22.692  1.00 46.62           C  
ATOM   1037  CE3 TRP A 462      -0.408   8.523  22.412  1.00 44.95           C  
ATOM   1038  CZ2 TRP A 462       0.690   6.234  23.671  1.00 45.01           C  
ATOM   1039  CZ3 TRP A 462      -1.107   7.824  23.386  1.00 46.63           C  
ATOM   1040  CH2 TRP A 462      -0.554   6.692  24.003  1.00 45.97           C  
ATOM   1041  N   GLN A 463      -0.620  11.271  18.582  1.00 52.68           N  
ATOM   1042  CA  GLN A 463      -1.037  12.559  18.050  1.00 51.85           C  
ATOM   1043  C   GLN A 463      -1.731  13.396  19.112  1.00 50.33           C  
ATOM   1044  O   GLN A 463      -2.423  12.870  19.980  1.00 50.11           O  
ATOM   1045  CB  GLN A 463      -1.973  12.368  16.859  1.00 53.72           C  
ATOM   1046  CG  GLN A 463      -1.303  11.750  15.649  1.00 56.63           C  
ATOM   1047  CD  GLN A 463      -2.078  11.990  14.375  1.00 57.97           C  
ATOM   1048  OE1 GLN A 463      -3.235  11.569  14.241  1.00 58.08           O  
ATOM   1049  NE2 GLN A 463      -1.446  12.678  13.426  1.00 58.39           N  
ATOM   1050  N   ILE A 464      -1.531  14.703  19.060  1.00 47.74           N  
ATOM   1051  CA  ILE A 464      -2.187  15.558  20.024  1.00 46.44           C  
ATOM   1052  C   ILE A 464      -3.619  15.787  19.606  1.00 44.84           C  
ATOM   1053  O   ILE A 464      -3.896  16.150  18.465  1.00 44.42           O  
ATOM   1054  CB  ILE A 464      -1.489  16.903  20.163  1.00 48.00           C  
ATOM   1055  CG1 ILE A 464      -0.177  16.700  20.920  1.00 49.67           C  
ATOM   1056  CG2 ILE A 464      -2.387  17.881  20.919  1.00 46.30           C  
ATOM   1057  CD1 ILE A 464       0.485  17.978  21.334  1.00 51.62           C  
ATOM   1058  N   VAL A 465      -4.530  15.576  20.542  1.00 43.13           N  
ATOM   1059  CA  VAL A 465      -5.939  15.734  20.254  1.00 42.92           C  
ATOM   1060  C   VAL A 465      -6.471  17.045  20.867  1.00 42.33           C  
ATOM   1061  O   VAL A 465      -7.465  17.616  20.411  1.00 41.91           O  
ATOM   1062  CB  VAL A 465      -6.708  14.489  20.763  1.00 41.13           C  
ATOM   1063  CG1 VAL A 465      -7.112  14.656  22.200  1.00 42.52           C  
ATOM   1064  CG2 VAL A 465      -7.884  14.237  19.895  1.00 45.80           C  
ATOM   1065  N   HIS A 466      -5.765  17.536  21.878  1.00 41.87           N  
ATOM   1066  CA  HIS A 466      -6.141  18.770  22.558  1.00 40.37           C  
ATOM   1067  C   HIS A 466      -5.010  19.257  23.437  1.00 40.38           C  
ATOM   1068  O   HIS A 466      -4.267  18.451  24.003  1.00 40.65           O  
ATOM   1069  CB  HIS A 466      -7.359  18.545  23.449  1.00 38.98           C  
ATOM   1070  CG  HIS A 466      -7.664  19.697  24.357  1.00 39.47           C  
ATOM   1071  ND1 HIS A 466      -8.041  20.939  23.889  1.00 37.51           N  
ATOM   1072  CD2 HIS A 466      -7.671  19.786  25.709  1.00 40.26           C  
ATOM   1073  CE1 HIS A 466      -8.274  21.742  24.913  1.00 37.99           C  
ATOM   1074  NE2 HIS A 466      -8.056  21.067  26.029  1.00 40.58           N  
ATOM   1075  N   PHE A 467      -4.871  20.572  23.549  1.00 38.30           N  
ATOM   1076  CA  PHE A 467      -3.858  21.113  24.423  1.00 36.66           C  
ATOM   1077  C   PHE A 467      -4.330  22.421  25.021  1.00 37.14           C  
ATOM   1078  O   PHE A 467      -5.136  23.143  24.430  1.00 36.13           O  
ATOM   1079  CB  PHE A 467      -2.508  21.234  23.705  1.00 35.82           C  
ATOM   1080  CG  PHE A 467      -2.351  22.446  22.848  1.00 35.25           C  
ATOM   1081  CD1 PHE A 467      -1.999  23.666  23.405  1.00 35.28           C  
ATOM   1082  CD2 PHE A 467      -2.430  22.344  21.468  1.00 36.28           C  
ATOM   1083  CE1 PHE A 467      -1.716  24.768  22.593  1.00 35.56           C  
ATOM   1084  CE2 PHE A 467      -2.151  23.434  20.649  1.00 36.72           C  
ATOM   1085  CZ  PHE A 467      -1.791  24.650  21.216  1.00 35.45           C  
ATOM   1086  N   HIS A 468      -3.851  22.692  26.229  1.00 36.39           N  
ATOM   1087  CA  HIS A 468      -4.235  23.881  26.964  1.00 34.41           C  
ATOM   1088  C   HIS A 468      -2.987  24.546  27.537  1.00 37.08           C  
ATOM   1089  O   HIS A 468      -2.259  23.938  28.314  1.00 36.56           O  
ATOM   1090  CB  HIS A 468      -5.197  23.454  28.064  1.00 29.69           C  
ATOM   1091  CG  HIS A 468      -5.858  24.586  28.783  1.00 29.16           C  
ATOM   1092  ND1 HIS A 468      -7.003  24.414  29.537  1.00 26.14           N  
ATOM   1093  CD2 HIS A 468      -5.516  25.891  28.906  1.00 27.95           C  
ATOM   1094  CE1 HIS A 468      -7.335  25.564  30.094  1.00 26.50           C  
ATOM   1095  NE2 HIS A 468      -6.450  26.476  29.728  1.00 27.95           N  
ATOM   1096  N   ARG A 469      -2.736  25.792  27.132  1.00 39.28           N  
ATOM   1097  CA  ARG A 469      -1.572  26.539  27.595  1.00 40.60           C  
ATOM   1098  C   ARG A 469      -2.010  27.762  28.411  1.00 42.21           C  
ATOM   1099  O   ARG A 469      -2.881  28.509  27.989  1.00 42.75           O  
ATOM   1100  CB  ARG A 469      -0.733  27.004  26.401  1.00 41.46           C  
ATOM   1101  CG  ARG A 469       0.762  26.988  26.661  1.00 47.46           C  
ATOM   1102  CD  ARG A 469       1.514  28.260  26.206  1.00 49.30           C  
ATOM   1103  NE  ARG A 469       1.239  28.664  24.830  1.00 50.28           N  
ATOM   1104  CZ  ARG A 469       1.067  27.825  23.811  1.00 51.68           C  
ATOM   1105  NH1 ARG A 469       1.136  26.508  24.002  1.00 50.40           N  
ATOM   1106  NH2 ARG A 469       0.828  28.311  22.594  1.00 50.41           N  
ATOM   1107  N   SER A 470      -1.412  27.949  29.587  1.00 44.60           N  
ATOM   1108  CA  SER A 470      -1.690  29.085  30.472  1.00 45.02           C  
ATOM   1109  C   SER A 470      -0.414  29.851  30.764  1.00 49.04           C  
ATOM   1110  O   SER A 470       0.690  29.342  30.586  1.00 47.52           O  
ATOM   1111  CB  SER A 470      -2.262  28.639  31.797  1.00 41.21           C  
ATOM   1112  OG  SER A 470      -3.641  28.518  31.697  1.00 42.61           O  
ATOM   1113  N   GLY A 471      -0.575  31.061  31.280  1.00 54.71           N  
ATOM   1114  CA  GLY A 471       0.572  31.902  31.528  1.00 60.78           C  
ATOM   1115  C   GLY A 471       0.791  32.451  30.132  1.00 66.79           C  
ATOM   1116  O   GLY A 471       1.247  31.722  29.239  1.00 68.14           O  
ATOM   1117  N   ALA A 472       0.458  33.725  29.933  1.00 70.93           N  
ATOM   1118  CA  ALA A 472       0.573  34.386  28.630  1.00 74.89           C  
ATOM   1119  C   ALA A 472       1.750  34.048  27.679  1.00 77.66           C  
ATOM   1120  O   ALA A 472       1.711  34.431  26.503  1.00 77.78           O  
ATOM   1121  CB  ALA A 472       0.472  35.908  28.820  1.00 75.09           C  
ATOM   1122  N   PRO A 473       2.817  33.366  28.159  1.00 80.08           N  
ATOM   1123  CA  PRO A 473       3.872  33.082  27.178  1.00 82.04           C  
ATOM   1124  C   PRO A 473       3.405  32.363  25.910  1.00 83.12           C  
ATOM   1125  O   PRO A 473       2.380  31.676  25.901  1.00 82.52           O  
ATOM   1126  CB  PRO A 473       4.862  32.253  27.984  1.00 81.73           C  
ATOM   1127  CG  PRO A 473       4.855  32.967  29.267  1.00 81.61           C  
ATOM   1128  CD  PRO A 473       3.373  33.245  29.523  1.00 80.72           C  
ATOM   1129  N   SER A 474       4.179  32.534  24.844  1.00 84.69           N  
ATOM   1130  CA  SER A 474       3.878  31.925  23.554  1.00 85.96           C  
ATOM   1131  C   SER A 474       4.241  30.441  23.559  1.00 86.24           C  
ATOM   1132  O   SER A 474       4.942  30.006  24.503  1.00 86.88           O  
ATOM   1133  CB  SER A 474       4.658  32.649  22.444  1.00 86.36           C  
ATOM   1134  OG  SER A 474       4.400  34.046  22.458  1.00 86.91           O  
ATOM   1135  N   VAL A 475       3.824  29.733  22.616  1.00 86.38           N  
TER
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.